|
Name |
Accession |
Description |
Interval |
E-value |
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
48-282 |
2.22e-60 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 191.40 E-value: 2.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 48 KKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 127
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 128 KVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSL 207
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 669033277 208 MASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELDNALNDIT 282
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
7-152 |
4.89e-26 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 99.69 E-value: 4.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 7 KMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAEadva 86
Cdd:pfam12718 1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE---- 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 669033277 87 SLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAK 152
Cdd:pfam12718 77 NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-264 |
3.74e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 1 MDAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATD 80
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 81 AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDR 160
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 161 KYEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLMASEEEYSTKEDKYEEEIKLLEEKLKEAETRAE 240
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250 260
....*....|....*....|....
gi 669033277 241 FAERSVAKLEKTIDDLEDEVYAQK 264
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLL 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
5-264 |
6.77e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 6.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 5 KKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAEAD 84
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 85 VASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEE 164
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 165 VARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLMASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAER 244
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260
....*....|....*....|
gi 669033277 245 SVAKLEKTIDDLEDEVYAQK 264
Cdd:COG1196 464 LLAELLEEAALLEAALAELL 483
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
21-278 |
4.36e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 21 RAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAEADVASLNRRIQLVEEELD 100
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 101 RAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSE 180
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 181 ERAEVAESRARQLEEELRTMDQALKSLMASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEV 260
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250
....*....|....*...
gi 669033277 261 YAQKMKYKAISEELDNAL 278
Cdd:COG1196 466 AELLEEAALLEAALAELL 483
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
30-274 |
9.85e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 9.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 30 KQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATA 109
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 110 LQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESR 189
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 190 ARQLEEELRTMDQALKSLMASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKA 269
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
....*
gi 669033277 270 ISEEL 274
Cdd:TIGR02168 920 LREKL 924
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
29-284 |
4.70e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 4.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 29 KKQAED--RCKQLEEEQQALQ-----KKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDR 101
Cdd:COG1196 206 ERQAEKaeRYRELKEELKELEaelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 102 AQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEE 181
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 182 RAEVAESRARQLEEELRTMDQALKSLMASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVY 261
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
250 260
....*....|....*....|...
gi 669033277 262 AQKMKYKAISEELDNALNDITSL 284
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAEL 468
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
18-213 |
2.03e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 18 AIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAEADVASLNRRIQLVEE 97
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 98 ELDRAQERLATALQKLEEAEKA-----------ADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVA 166
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 669033277 167 RKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLMASEEE 213
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
22-258 |
4.85e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 22 AEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDR 101
Cdd:PRK02224 344 AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 102 AQERLATALQKLEEAEKAADESERGMKV--------------IENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEvAR 167
Cdd:PRK02224 424 LREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVEERLER-AE 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 168 KLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLMASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVA 247
Cdd:PRK02224 503 DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA 582
|
250
....*....|.
gi 669033277 248 KLEKTIDDLED 258
Cdd:PRK02224 583 ELKERIESLER 593
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-260 |
5.97e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 1 MDAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATD 80
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 81 AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEmqlkeakhiaedsdR 160
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR--------------S 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 161 KYEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSlmASEEEYSTKEDKYEEEIKLLEEKLKEAETRAE 240
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALE 464
|
250 260
....*....|....*....|
gi 669033277 241 FAERSVAKLEKTIDDLEDEV 260
Cdd:TIGR02168 465 ELREELEEAEQALDAAEREL 484
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-275 |
9.55e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 9.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 4 IKKKMQMLKLDKENAID----RAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEK--- 76
Cdd:TIGR02168 198 LERQLKSLERQAEKAERykelKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLevs 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 77 ------------------KATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDE 138
Cdd:TIGR02168 278 eleeeieelqkelyalanEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 139 EKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLMASEEEysTKE 218
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AEL 435
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 669033277 219 DKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELD 275
Cdd:TIGR02168 436 KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
38-221 |
4.12e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 38 QLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLE--QAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEE 115
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 116 AEKAADESERGMKVIENRAMKDEEKMELQEMQLKEA--------KH---------IAEDSDRKYEEVARKLVILEGELER 178
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAelsarytpNHpdvialraqIAALRAQLQQEAQRILASLEAELEA 324
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 669033277 179 SEERAEVAESRARQLEEELRTMDQALKSLMASEEEYSTKEDKY 221
Cdd:COG3206 325 LQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELY 367
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-260 |
1.09e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 2 DAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDA 81
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 82 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRK 161
Cdd:TIGR02168 858 AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 162 YEEVARKL-VILEGELERSEERAEVAESRARQLEEELRTMDQALKSL----MASEEEYSTKEDKYEEEIKLLeeklkeae 236
Cdd:TIGR02168 938 IDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnLAAIEEYEELKERYDFLTAQK-------- 1009
|
250 260
....*....|....*....|....
gi 669033277 237 traEFAERSVAKLEKTIDDLEDEV 260
Cdd:TIGR02168 1010 ---EDLTEAKETLEEAIEEIDREA 1030
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-260 |
1.52e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 2 DAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQL-EEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATD 80
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 81 AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDR 160
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 161 KYEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLMASEEEYSTKEDKYEEEIKLLEEKLKEAETRAE 240
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486
|
250 260
....*....|....*....|
gi 669033277 241 FAERSVAKLEKTIDDLEDEV 260
Cdd:TIGR02169 487 KLQRELAEAEAQARASEERV 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-270 |
2.58e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 2 DAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQaekkatda 81
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA-------- 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 82 eadvasLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRK 161
Cdd:TIGR02168 801 ------LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 162 YEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLMASEEEYSTKEDKYEEEIKLLEEK-LKEAETRAE 240
Cdd:TIGR02168 875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLE 954
|
250 260 270
....*....|....*....|....*....|
gi 669033277 241 FAERSVAKLEKTIDDLEDEVYAQKMKYKAI 270
Cdd:TIGR02168 955 EAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
30-277 |
3.06e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 30 KQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATA 109
Cdd:TIGR02169 663 RGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 110 LQKLEEAEKAADESERGMKviENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESR 189
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELK--ELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 190 ARQLEEELRTMDQALKSLMASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKA 269
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
....*...
gi 669033277 270 ISEELDNA 277
Cdd:TIGR02169 901 LERKIEEL 908
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
7-220 |
4.01e-06 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 48.29 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 7 KMQMLKLDKENAIDRAEQ-AEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESvkeAQEKLEQAEKKATDAEA-- 83
Cdd:NF012221 1541 SQQADAVSKHAKQDDAAQnALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTDQN---ALETNGQAQRDAILEESra 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 84 ---DVASLNRRIQLVEEE-------------------LDRAQERLATALQKLEEA-EKAADESERGMKVIENRAMKDEEK 140
Cdd:NF012221 1618 vtkELTTLAQGLDALDSQatyagesgdqwrnpfagglLDRVQEQLDDAKKISGKQlADAKQRHVDNQQKVKDAVAKSEAG 1697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 141 MELQEMQLKEAKHIAED----SDRKYEEVARKlvilEGELERSEERAEVAESRARQLEEElRTMDQALKSLMASEEEYST 216
Cdd:NF012221 1698 VAQGEQNQANAEQDIDDakadAEKRKDDALAK----QNEAQQAESDANAAANDAQSRGEQ-DASAAENKANQAQADAKGA 1772
|
....
gi 669033277 217 KEDK 220
Cdd:NF012221 1773 KQDE 1776
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2-198 |
8.91e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 2 DAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDR---CKQLEEEQ------QALQKKLKGTEDEVEKYSES---VKEAQE 69
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERreaLQRLAEYSwdeidvASAEREIAELEAELERLDASsddLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 70 KLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERgmkvienramkdeekmelqemQLK 149
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR---------------------ALL 751
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 669033277 150 EAKHIAEDSDRKYEEVARKLvilegelersEERAEVAESRARQLEEELR 198
Cdd:COG4913 752 EERFAAALGDAVERELRENL----------EERIDALRARLNRAEEELE 790
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
12-199 |
1.82e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 12 KLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAEAD-VASLNR 90
Cdd:COG4913 266 AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLER 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 91 RIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHiaeDSDRKYEEVARKLV 170
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA---EAEAALRDLRRELR 422
|
170 180
....*....|....*....|....*....
gi 669033277 171 ILEGELERSEERAEVAESRARQLEEELRT 199
Cdd:COG4913 423 ELEAEIASLERRKSNIPARLLALRDALAE 451
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
6-142 |
2.44e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 6 KKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTE-DEVEKYSESVKEAQEKLEQAEKKATDAEAD 84
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEAL 367
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 669033277 85 VASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKME 142
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE 425
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
9-284 |
2.66e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.71 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 9 QMLKLDKENAIDRAEQAEADKKQAE--DRCKQLEEEQQALQKKLKGTED-------------EVEKYSESVKEAQEKLEQ 73
Cdd:COG3096 286 RALELRRELFGARRQLAEEQYRLVEmaRELEELSARESDLEQDYQAASDhlnlvqtalrqqeKIERYQEDLEELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 74 AEKKATDAEADVASLNRRIQLVEEELDRAQERLA-----------------TALQKLEEAEKAADESERGMKVIENRAMK 136
Cdd:COG3096 366 QEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAdyqqaldvqqtraiqyqQAVQALEKARALCGLPDLTPENAEDYLAA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 137 DEEKMELQEMQLKEAKH---IAEDSDRKYEEVARKLVILEGELERSEeraevAESRARQLEEELRTMDQALKSLMASEEE 213
Cdd:COG3096 446 FRAKEQQATEEVLELEQklsVADAARRQFEKAYELVCKIAGEVERSQ-----AWQTARELLRRYRSQQALAQRLQQLRAQ 520
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 669033277 214 YSTKEDKYEEEIKLLEEKLK------EAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELDNALNDITSL 284
Cdd:COG3096 521 LAELEQRLRQQQNAERLLEEfcqrigQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKEL 597
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
65-284 |
3.34e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 65 KEAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQ 144
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 145 EMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLMASEEEYSTKEDKYEEE 224
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 225 IKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELDNALNDITSL 284
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1-218 |
4.85e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 1 MDAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEqqalqkkLKGTEDEVEKYSESVKEAQEKLEQAEKKATD 80
Cdd:TIGR02169 289 QLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE-------IDKLLAEIEELEREIEEERKRRDKLTEEYAE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 81 AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDR 160
Cdd:TIGR02169 362 LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEE 441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 669033277 161 KYEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLmasEEEYSTKE 218
Cdd:TIGR02169 442 EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL---QRELAEAE 496
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
12-129 |
7.12e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 7.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 12 KLDKENAIDRAEQAEADK--KQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKatdaEADVASLN 89
Cdd:COG2433 396 EAEREKEHEERELTEEEEeiRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRK----DREISRLD 471
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 669033277 90 RRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKV 129
Cdd:COG2433 472 REIERLERELEEERERIEELKRKLERLKELWKLEHSGELV 511
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
65-284 |
8.15e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 8.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 65 KEAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQE-----------RLATALQKLEEAEKAADESERGMKVIENR 133
Cdd:COG1196 175 EEAERKLEATEENLERLEDILGELERQLEPLERQAEKAERyrelkeelkelEAELLLLKLRELEAELEELEAELEELEAE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 134 AMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLMASEEE 213
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 669033277 214 YSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELDNALNDITSL 284
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
15-284 |
8.56e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 8.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 15 KENAIDRAEQA-EADKKQAEDRCkQLEEEQQALQKKLKGTEDEVEKYSES-------VKEAQEKLEQAEKKATDAEADVA 86
Cdd:PRK04863 315 ELAELNEAESDlEQDYQAASDHL-NLVQTALRQQEKIERYQADLEELEERleeqnevVEEADEQQEENEARAEAAEEEVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 87 SLNRRIQLVEEELDRAQERLAT---ALQKLEEAEK---AADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDR 160
Cdd:PRK04863 394 ELKSQLADYQQALDVQQTRAIQyqqAVQALERAKQlcgLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 161 KYEEVARKLVILEGELERSEeraevAESRARQLEEELRTMDQALKSLMASEEEYSTKEDKYEEEIKLLEEKLK------E 234
Cdd:PRK04863 474 QFEQAYQLVRKIAGEVSRSE-----AWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEfckrlgK 548
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 669033277 235 AETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELDNALNDITSL 284
Cdd:PRK04863 549 NLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRL 598
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
6-269 |
8.63e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 8.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 6 KKMQMLKLDKENA--IDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKySESVKEAQEKLEQAEKKATDAEA 83
Cdd:PTZ00121 1230 KKAEEAKKDAEEAkkAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK-AEEKKKADEAKKAEEKKKADEAK 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 84 DVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYE 163
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 164 EV-----ARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLMASEEEYSTKEDKYEEEIKLLEEKLKEAETR 238
Cdd:PTZ00121 1389 EKkkadeAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
|
250 260 270
....*....|....*....|....*....|.
gi 669033277 239 AEFAERSVAKLEKTIDDLEDEVYAQKMKYKA 269
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1499
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
14-213 |
1.55e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 14 DKENAIDRAEQA-EADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKySESVKEAQEKLEQAEKKATDAEADVASLNRRI 92
Cdd:PTZ00121 1575 DKNMALRKAEEAkKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK-AEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 93 QLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVIL 172
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 669033277 173 EGELERSEERAEVAEsrARQLEEELRTMDQALKSLMASEEE 213
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEE--AKKDEEEKKKIAHLKKEEEKKAEE 1772
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
11-212 |
1.90e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 11 LKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQK------KLKGTEDEVEKY---SESVKEAQEKLEQAEKKATDA 81
Cdd:PRK11281 61 VQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQaqaeleALKDDNDEETREtlsTLSLRQLESRLAQTLDQLQNA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 82 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESErgmkvIENRAMKDEEKMELQ-EMQLKEAKHiaeDSDR 160
Cdd:PRK11281 141 QNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGK-----VGGKALRPSQRVLLQaEQALLNAQN---DLQR 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 669033277 161 KYEEVARKLVILeGELERSEERAEVAesrarQLEEELRTMDQAL--KSLMASEE 212
Cdd:PRK11281 213 KSLEGNTQLQDL-LQKQRDYLTARIQ-----RLEHQLQLLQEAInsKRLTLSEK 260
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
67-269 |
2.21e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 67 AQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLAtALQKLEEaekaADESERGMKVIENRAmkdeekmelqeM 146
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAE----YSWDEIDVASAEREI-----------A 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 147 QLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLMASEEEYSTKEDKYEEEIK 226
Cdd:COG4913 672 ELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 669033277 227 LLEEKLKEAETR----AEFAERSVAKLEKTIDDLEDEVYAQKMKYKA 269
Cdd:COG4913 752 EERFAAALGDAVerelRENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-260 |
2.95e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 5 KKKMQMLKLDKENAIDRAEQ---AEADKKQAEDRCKQLEEEQQAlqKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDA 81
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADElkkAAAAKKKADEAKKKAEEKKKA--DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE 1467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 82 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRK 161
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 162 YEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLMASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEF 241
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
250
....*....|....*....
gi 669033277 242 AERSVAKLEKTIDDLEDEV 260
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEK 1646
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-273 |
3.00e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 5 KKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKL---KGTEDEVEKYSESVKEAQEKLEQAEKKATDA 81
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKeeaKKKADAAKKKAEEKKKADEAKKKAEEDKKKA 1407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 82 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM---KVIENRAMKDEEKMELQEMQLK--------E 150
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAeeaKKAEEAKKKAEEAKKADEAKKKaeeakkadE 1487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 151 AKHIAEDSDRKYEEVARKLVILEG--ELERSEERAEVAESRA---RQLEEELRTMDQALKS--LMASEEEYSTKEDKYEE 223
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKadEAKKAEEAKKADEAKKaeeAKKADEAKKAEEKKKAdeLKKAEELKKAEEKKKAE 1567
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 669033277 224 EIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEE 273
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-189 |
3.06e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 2 DAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDA 81
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 82 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRK 161
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
170 180
....*....|....*....|....*...
gi 669033277 162 YEEVARKLVILEGELERSEERAEVAESR 189
Cdd:COG1196 493 LLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1-213 |
3.30e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 1 MDAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATD 80
Cdd:TIGR02169 704 LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 81 AEADVAslNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDR 160
Cdd:TIGR02169 784 LEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 669033277 161 KYEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLMASEEE 213
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEK 914
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
2-125 |
3.46e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.57 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 2 DAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDR-------------CKQLEEEQQALQKKLKGTEDEVEKYSESVKE-- 66
Cdd:COG1566 65 DRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQlarleaelgaeaeIAAAEAQLAAAQAQLDLAQRELERYQALYKKga 144
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 67 -AQEKLEQAEKKATDAEADVASLNRRIQLVEEELdRAQERLATALQKLEEAEKAADESER 125
Cdd:COG1566 145 vSQQELDEARAALDAAQAQLEAAQAQLAQAQAGL-REEEELAAAQAQVAQAEAALAQAEL 203
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1-240 |
4.04e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 1 MDAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATD 80
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 81 AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDR 160
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 161 KYEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLMASEEEYSTKEDKYEEEIKLLEEKLKEAETRAE 240
Cdd:COG4372 207 KLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
24-247 |
5.23e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 24 QAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRA- 102
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 103 -----QERLATALQKLEEAEKAADESERgMKVIENRAMKDEEKMElqemQLKEAKHIAEDSDRKYEEVARKLVILEGELE 177
Cdd:COG3883 93 ralyrSGGSVSYLDVLLGSESFSDFLDR-LSALSKIADADADLLE----ELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 178 RSEERAEVAESRARQLEEELRTMDQALKSLMASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVA 247
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
55-198 |
6.54e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.83 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 55 DEVEKYSESVKEAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLAT--ALQK---------LEEAEKAADES 123
Cdd:COG0497 254 ERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLALlrRLARkygvtveelLAYAEELRAEL 333
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 669033277 124 ERgmkvIENramkDEEKMELQEMQLKEAKhiaedsdRKYEEVARKLvilegelerSEERAEVAESRARQLEEELR 198
Cdd:COG0497 334 AE----LEN----SDERLEELEAELAEAE-------AELLEAAEKL---------SAARKKAAKKLEKAVTAELA 384
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
48-276 |
7.31e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 48 KKLKGTEDEVEKYSESVK------EAQEKLEQAEKKATDAEADVASLN-----RRIQLVEEELDRAQERLATALQKLEEA 116
Cdd:COG4913 235 DDLERAHEALEDAREQIEllepirELAERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 117 EKAADESERgmkvienramkdeekmelQEMQLKEAkhIAEDSDRKYEEVARKLVILEGELERSEERAEVAESRARQLEEE 196
Cdd:COG4913 315 EARLDALRE------------------ELDELEAQ--IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 197 LRTMDQALKSLMAseeeystkedkyeeeiklleeklkEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELDN 276
Cdd:COG4913 375 LPASAEEFAALRA------------------------EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
12-255 |
8.73e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 8.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 12 KLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTE----DEVEKYSESVKEAQEKLEQAEKKATDAE----A 83
Cdd:PTZ00121 1439 KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEakkaDEAKKKAEEAKKKADEAKKAAEAKKKADeakkA 1518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 84 DVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYE 163
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVM 1598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 164 EVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKslmaSEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAE 243
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK----KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
250
....*....|..
gi 669033277 244 RSVAKLEKTIDD 255
Cdd:PTZ00121 1675 KKAEEAKKAEED 1686
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
54-156 |
1.13e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 54 EDEVEKYSESVKEAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLA-TALQKLEEAEKAADESERGMKVIEN 132
Cdd:PRK00409 519 NELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEkEAQQAIKEAKKEADEIIKELRQLQK 598
|
90 100
....*....|....*....|....*.
gi 669033277 133 RAMKDEEKMELQEMQ--LKEAKHIAE 156
Cdd:PRK00409 599 GGYASVKAHELIEARkrLNKANEKKE 624
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-251 |
1.58e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 2 DAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDA 81
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA 1586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 82 -EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHI--AEDS 158
Cdd:PTZ00121 1587 kKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikAAEE 1666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 159 DRKYEEVARKlvilEGELERSEERAEVAESRARQLEEELRTMDQALKSlmasEEEYSTKEDKYEEEIKLLEEKLKEAETR 238
Cdd:PTZ00121 1667 AKKAEEDKKK----AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK----EAEEKKKAEELKKAEEENKIKAEEAKKE 1738
|
250
....*....|...
gi 669033277 239 AEFAERSVAKLEK 251
Cdd:PTZ00121 1739 AEEDKKKAEEAKK 1751
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
27-128 |
2.03e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 39.68 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 27 ADKKQAEDRCKQLEEEQQALQK-KLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAEADVAslnrRIQLVEEELDRAQER 105
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKeQDEASFERLAELRDELAELEEELEALKARWEAEKELIE----EIQELKEELEQRYGK 486
|
90 100
....*....|....*....|...
gi 669033277 106 LATALQKLEEAEKAADESERGMK 128
Cdd:COG0542 487 IPELEKELAELEEELAELAPLLR 509
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
12-259 |
2.13e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 39.25 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 12 KLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAEADVASLNRR 91
Cdd:COG3064 20 QAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 92 IQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVI 171
Cdd:COG3064 100 AAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 172 LEGELERSEERAEVAESRARQLEEELRTMDQALKSLMASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEK 251
Cdd:COG3064 180 AALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGV 259
|
....*...
gi 669033277 252 TIDDLEDE 259
Cdd:COG3064 260 LGAALAAA 267
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
25-213 |
3.10e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.73 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 25 AEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQE 104
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 105 RLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAE 184
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180
....*....|....*....|....*....
gi 669033277 185 VAESRARQLEEELRTMDQALKSLMASEEE 213
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELA 217
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-245 |
3.73e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 2 DAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDA 81
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 82 EADvaslnrriQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRK 161
Cdd:PTZ00121 1367 EAA--------EKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK 1438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 162 YEEVARKlvilEGELERSEERAEVAESRARQLEEELRTMDQALKSLMASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEF 241
Cdd:PTZ00121 1439 KAEEAKK----ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE 1514
|
....
gi 669033277 242 AERS 245
Cdd:PTZ00121 1515 AKKA 1518
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
30-274 |
3.91e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 38.90 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 30 KQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQE--------KLEQAEKKATDAEADVASLNRRIQLVEEELDR 101
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREyegyellkEKEALERQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 102 AQERLATALQKLEEAEKAADE----------------------SERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSD 159
Cdd:TIGR02169 263 LEKRLEEIEQLLEELNKKIKDlgeeeqlrvkekigeleaeiasLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 160 RKYEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLMASEEEYSTKEDKYEEEIKLLEEKLKEAETRA 239
Cdd:TIGR02169 343 REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL 422
|
250 260 270
....*....|....*....|....*....|....*
gi 669033277 240 EFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEEL 274
Cdd:TIGR02169 423 ADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-177 |
5.05e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 38.50 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 1 MDAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATD 80
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 81 AEADVASLNRRIQLVEEELDRAQERLATALQKL-EEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSD 159
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAI 992
|
170
....*....|....*...
gi 669033277 160 RKYEEVARKLVILEGELE 177
Cdd:TIGR02168 993 EEYEELKERYDFLTAQKE 1010
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
37-263 |
5.11e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 37.96 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 37 KQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEA 116
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 117 EKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESRARQLEEE 196
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 669033277 197 LRTMDQALKSLMASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQ 263
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
5-118 |
5.87e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 37.88 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 5 KKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVK-EAQEKLEQAEKKATDAEA 83
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLeEAEKEAQQAIKEAKKEAD 587
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 669033277 84 DVASLNRRIQ------LVEEELDRAQERLATALQKLEEAEK 118
Cdd:PRK00409 588 EIIKELRQLQkggyasVKAHELIEARKRLNKANEKKEKKKK 628
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
74-284 |
6.37e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 37.82 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 74 AEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKh 153
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 154 iaEDSDRKYEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLMASEEEYSTKEDKYEEEIKLLEEKLK 233
Cdd:COG4942 97 --AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 669033277 234 EAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELDNALNDITSL 284
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1-201 |
6.43e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 37.82 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 1 MDAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATD 80
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 81 AE-----------ADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLK 149
Cdd:COG4942 116 LGrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 669033277 150 EAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESRARQLEEELRTMD 201
Cdd:COG4942 196 ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-277 |
6.48e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.20 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 5 KKKMQMLKLDKENAIDRAEQAEaDKKQAEDRCKQLEEEQQALQKKLKGtedevEKYSESVKEAQEKLEQAEKKATDAEAD 84
Cdd:PTZ00121 1278 RKADELKKAEEKKKADEAKKAE-EKKKADEAKKKAEEAKKADEAKKKA-----EEAKKKADAAKKKAEEAKKAAEAAKAE 1351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 85 VASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESErgmKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEE 164
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK---KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE 1428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 165 VARKlvilEGELERSEERAEVAESRARQLEEELRTMDQALKSLMASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAeR 244
Cdd:PTZ00121 1429 EKKK----ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA-K 1503
|
250 260 270
....*....|....*....|....*....|...
gi 669033277 245 SVAKLEKTIDDLEDEVYAQKMKYKAISEELDNA 277
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
14-204 |
6.94e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 37.75 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 14 DKENAIDRAEQAEADKKQAEDRCK-QLEEEQQAlqkKLKGTEDE-----------VEKYSESVKEAQEKLEQAEKKATDA 81
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRfQLEELEAA---ALQPGEEEeleeerrrlsnAEKLREALQEALEALSGGEGGALDL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 82 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAekaADESERGMKVIENramkDEEKMELQEMQLKEAKHIAedsdRK 161
Cdd:COG0497 246 LGQALRALERLAEYDPSLAELAERLESALIELEEA---ASELRRYLDSLEF----DPERLEEVEERLALLRRLA----RK 314
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 669033277 162 Y----EEVARKLVILEGELER---SEERAEVAESRARQLEEELRTMDQAL 204
Cdd:COG0497 315 YgvtvEELLAYAEELRAELAElenSDERLEELEAELAEAEAELLEAAEKL 364
|
|
| Ax_dynein_light |
pfam10211 |
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ... |
22-101 |
7.24e-03 |
|
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organizms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.
Pssm-ID: 463000 [Multi-domain] Cd Length: 187 Bit Score: 36.78 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 22 AEQAEADKKQAEDRCKQLEEEQQALQKKLKgteDEVEKYSESVKEAQEKLEQAEKKATDaeaDVASLNRRIQLVEEELDR 101
Cdd:pfam10211 114 ALQAEQGKAELEKKIADLEEEKEELEKQVA---ELKAKCEAIEKREEERRQAEEKKHAE---EIAFLKKTNQQLKAQLER 187
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3-270 |
7.30e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 37.57 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 3 AIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAE 82
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 83 ADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAkhiaedSDRKY 162
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL------SEAEA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 163 EEVARKLVILEGELERSEERAEVAESRARQLEEELRTMDQALKSLMASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFA 242
Cdd:COG4372 182 EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE 261
|
250 260
....*....|....*....|....*...
gi 669033277 243 ERSVAKLEKTIDDLEDEVYAQKMKYKAI 270
Cdd:COG4372 262 ELELAILVEKDTEEEELEIAALELEALE 289
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
32-259 |
8.62e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 37.44 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 32 AEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQ 111
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 112 KLEEAEKAADESERGMKVIENRamkDEEKMELqemqlkeakhiaedSDRKYEEVARKLVILEGELERSEERAEvaesrar 191
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQ---PPLALLL--------------SPEDFLDAVRRLQYLKYLAPARREQAE------- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 669033277 192 QLEEELRTMDQALKSLMASEEEYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDE 259
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
9-212 |
8.87e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 37.41 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 9 QMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAEADVASL 88
Cdd:pfam17380 396 QELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRK 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 89 NRRIQLVEEELDRAQERLATALQK-LEEAEKAADESERGMKVIEnRAMKDEEKMELQEmqlkEAKHIAEDSDRKYEEVAR 167
Cdd:pfam17380 476 KLELEKEKRDRKRAEEQRRKILEKeLEERKQAMIEEERKRKLLE-KEMEERQKAIYEE----ERRREAEEERRKQQEMEE 550
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 669033277 168 KLVILEGELERSEERaevaeSRARQLEEELRTMDQALKSLMASEE 212
Cdd:pfam17380 551 RRRIQEQMRKATEER-----SRLEAMEREREMMRQIVESEKARAE 590
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
47-220 |
9.47e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 37.29 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 47 QKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAEADVASLN--------RRIQLVEEELDRAQERLATALQKLEEAEK 118
Cdd:pfam05262 162 KNILSGNVSDVDTDSISDKKVVEALREDNEKGVNFRRDMTDLKeresqedaKRAQQLKEELDKKQIDADKAQQKADFAQD 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 119 AADESERGMKVIENRAMKDEEKMELQEMqlKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVA---ESRARQLEE 195
Cdd:pfam05262 242 NADKQRDEVRQKQQEAKNLPKPADTSSP--KEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDlkqESKASEKEA 319
|
170 180
....*....|....*....|....*
gi 669033277 196 ELRTMDQALKSLMASEEEYSTKEDK 220
Cdd:pfam05262 320 EDKELEAQKKREPVAEDLQKTKPQV 344
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
11-133 |
9.94e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 37.59 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033277 11 LKLDKENAIDRAEQAEADKKQAE-DRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKkatDAEADVASLN 89
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE---EFAALRAEAA 390
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 669033277 90 RRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENR 133
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| |
