|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
162-475 |
2.14e-152 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 439.36 E-value: 2.14e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 162 EEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRqNLEPLFEQYINNLRRQLDSIVGERGRLDSELRN 241
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPS-RLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 242 MQDLVEDLKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDAELSQMQTHISDTSVVLS 321
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 322 MDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQ 401
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 120660432 402 CASLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEECR 475
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
17-159 |
2.03e-25 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 102.43 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 17 GFSANSARLPGVSRSGFSSISVSRSRGSGGLGGACGGAGFGSRSLYGLGGSKRISI---GGGSCAISG---GYGSRAGGS 90
Cdd:pfam16208 1 GFSSCSAVVPSRSRRSYSSVSSSRRGGGGGGGGGGGGGGFGSRSLYNLGGSKSISIsvaGGGSRPGSGfgfGGGGGGGFG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 120660432 91 YGFGGAGSGFGFGGG-------AGIGFGLGGGAGLAGGFGGPGFPVCPPGGIQEVTVNQSLLTPLNLQIDPAIQRV 159
Cdd:pfam16208 81 GGFGGGGGGGFGGGGgfgggfgGGGYGGGGFGGGGFGGRGGFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
162-457 |
1.36e-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: 67.77 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 162 EEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRQNLEplFEQYINNLRRQLDSIVGERGRLDSELRN 241
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE--LSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 242 MQDLVEDLKNKYEDEINKRTAAENEFVTLKKdvdaaymNKVELQAKADTLTDEINFLRALYD---AELSQMQTHISDTSV 318
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREALDelrAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 319 VLSMDNNR-------NLDLDSIIAEVKAQYEEIAQ----------RSRAEAESWYQtKYEELQVTAGRHGDDLRNTKQEI 381
Cdd:TIGR02168 825 RLESLERRiaaterrLEDLEEQIEELSEDIESLAAeieeleelieELESELEALLN-ERASLEEALALLRSELEELSEEL 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 382 AEINRMIQRLRSEIDHVKKQCASLQAAIADAEQR-----------GEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQE 450
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRidnlqerlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
....*..
gi 120660432 451 LMNVKLA 457
Cdd:TIGR02168 984 LGPVNLA 990
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
303-443 |
9.09e-08 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 54.20 E-value: 9.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 303 DAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEiAQRSRAEAESWYQTKYEELQVTAGRHGD---DLRNTKQ 379
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQ 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 120660432 380 EIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQRGemalKDAKNKLEG----LEDALQKAKQDLAR 443
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADlgrrLNVALAQRVQELNR 194
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
152-473 |
1.18e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.91 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 152 IDP-AIQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQ------GTKTVRQNLEPLFEQYINNLRR- 223
Cdd:PRK01156 402 IDPdAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcGTTLGEEKSNHIINHYNEKKSRl 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 224 --QLDSIVGERGRLDSELRNMQDLVEDLKNKyedEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRAL 301
Cdd:PRK01156 482 eeKIREIEIEVKDIDEKIVDLKKRKEYLESE---EINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSL 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 302 YDAELSQMQTHISDTSVVLSmdnnrNLDLDSIIA---EVKAQYEEIAQRSRaEAESWYQTKYEELQVTAGRHGDD---LR 375
Cdd:PRK01156 559 KLEDLDSKRTSWLNALAVIS-----LIDIETNRSrsnEIKKQLNDLESRLQ-EIEIGFPDDKSYIDKSIREIENEannLN 632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 376 NTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQRGEMALkDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVK 455
Cdd:PRK01156 633 NKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRIN-DIEDNLKKSRKALDDAKANRARLESTIEILRTRI 711
|
330
....*....|....*...
gi 120660432 456 LALDVEIATYRKLLEGEE 473
Cdd:PRK01156 712 NELSDRINDINETLESMK 729
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
145-434 |
1.89e-07 |
|
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: 54.29 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 145 LTPLNLQIDPAIQRVRAEEREqIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQgTKTVRQNLEpLFEQYINNLRRQ 224
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAE-LQELEEKLEELRLEVSELEEEIEELQKELYALANE-ISRLEQQKQ-ILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 225 LDSIVGERGRLDSELRNMQDLVEDLKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLR---AL 301
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLElqiAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 302 YDAELSQMQTHISDTSVVLSMDNNRNLDLDSII--AEVKAQYEEIAQRSRAEaeswyqtkyEELQVTAGRHGDDLRNTKQ 379
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLeeAELKELQAELEELEEEL---------EELQEELERLEEALEELRE 468
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 120660432 380 EIAEINRMIQRLRSEIDHVKKQCASLQAAIADAE--QRGEMALKDAKNKLEGLEDAL 434
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQARLDSLERLQENLEgfSEGVKALLKNQSGLSGILGVL 525
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
221-470 |
3.21e-07 |
|
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: 53.53 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 221 LRRQLDSIVGERGRLDSELRNMQDLVEDLKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRA 300
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 301 L---YDAELSQMQTHISdtSVVLSMDNNRNLDLDSIIAEVKAQYEEI-AQRSRAEAeswyqtKYEELQVTAGRHGDDLRN 376
Cdd:TIGR02169 759 ElkeLEARIEELEEDLH--KLEEALNDLEARLSHSRIPEIQAELSKLeEEVSRIEA------RLREIEQKLNRLTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 377 TKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQRgemaLKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKL 456
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE----LEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
250
....*....|....
gi 120660432 457 ALDVEIATYRKLLE 470
Cdd:TIGR02169 907 ELEAQIEKKRKRLS 920
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
151-451 |
5.33e-07 |
|
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: 52.76 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 151 QIDPAIQRVRaEEREQIKTLNNKFASFIDKVRflEQQNKVLDTKWTLLQEQGTKTVRQNLE-PLFEQYINNLRRQLDSIV 229
Cdd:TIGR02169 167 EFDRKKEKAL-EELEEVEENIERLDLIIDEKR--QQLERLRREREKAERYQALLKEKREYEgYELLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 230 GERGRLDSELRNMQDLVEDLKNKYE------DEINKRTAA--ENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFL--- 298
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEeieqllEELNKKIKDlgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAeer 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 299 RALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQR----------------SRAEAESWYQTKYEE 362
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEleevdkefaetrdelkDYREKLEKLKREINE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 363 LQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQrgemalkdaknKLEGLEDALQKAKQDLA 442
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW-----------KLEQLAADLSKYEQELY 472
|
....*....
gi 120660432 443 RLLKEYQEL 451
Cdd:TIGR02169 473 DLKEEYDRV 481
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
179-447 |
1.07e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 51.55 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 179 DKVRFLEQQNKVLDTKWTLLQEQgTKTvrqnleplFEQYINNLRRQLDSIVgergrldSELRNMQDLVEDLKNKYEDEIN 258
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQ-IKT--------YNKNIEEQRKKNGENI-------ARKQNKYDELVEEAKTIKAEIE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 259 KRTAAENEFVTLKKDVDAAY----MNKVELQAKADTLTDEINFLRAlYDAELSQMQThISDTsvvlsmdnnrnldlDSII 334
Cdd:PHA02562 238 ELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYEK-GGVCPTCTQQ-ISEG--------------PDRI 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 335 AEVKAQYEEIAQRSRAEaeswyQTKYEELQVTAgrhgDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIadaeQ 414
Cdd:PHA02562 302 TKIKDKLKELQHSLEKL-----DTAIDELEEIM----DEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAI----E 368
|
250 260 270
....*....|....*....|....*....|...
gi 120660432 415 RGEMALKDAKNKLEGLEDALQKAKQDLARLLKE 447
Cdd:PHA02562 369 ELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
279-479 |
1.31e-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: 51.60 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 279 MNKVELQAKADT----LTDEINFL-RALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIaQRSRAEAE 353
Cdd:TIGR02168 202 LKSLERQAEKAErykeLKAELRELeLALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL-RLEVSELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 354 SwyqtKYEELQvtagrhgDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQRGEMA---LKDAKNKLEGL 430
Cdd:TIGR02168 281 E----EIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELaeeLAELEEKLEEL 349
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 120660432 431 EDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRK---LLEGEECRLNGE 479
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaQLELQIASLNNE 401
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
191-451 |
1.47e-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: 51.21 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 191 LDTKWTLLQEQGTKTVRqnleplFEQYINNLRR-QLDSIVGERGRLDSELRNMQDLVEDLKNKYEDEINKRTAAENEFVT 269
Cdd:TIGR02168 198 LERQLKSLERQAEKAER------YKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 270 LKKDVDAAYMNKVELQAKADTLTDEINFL---RALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQ 346
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKELYALANEISRLeqqKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 347 RSRA------EAESWYQ---TKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQR-G 416
Cdd:TIGR02168 352 ELESleaeleELEAELEeleSRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKlE 431
|
250 260 270
....*....|....*....|....*....|....*
gi 120660432 417 EMALKDAKNKLEGLEDALQKAKQDLARLLKEYQEL 451
Cdd:TIGR02168 432 EAELKELQAELEELEEELEELQEELERLEEALEEL 466
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
144-401 |
2.47e-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: 50.45 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 144 LLTPLNLQIDPAIQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRQnleplfeqyINNLRR 223
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE---------IEELER 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 224 QLDSIVGERGRLDSELRNMQDLVEDLKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLralyD 303
Cdd:TIGR02169 344 EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL----S 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 304 AELSQMQTHISdtsvvlsmdnnrnlDLDSIIAEVKAQYEEIAQRSRAEaeswyQTKYEELQVTAGRHGDDLRNTKQEIAE 383
Cdd:TIGR02169 420 EELADLNAAIA--------------GIEAKINELEEEKEDKALEIKKQ-----EWKLEQLAADLSKYEQELYDLKEEYDR 480
|
250
....*....|....*...
gi 120660432 384 INRMIQRLRSEIDHVKKQ 401
Cdd:TIGR02169 481 VEKELSKLQRELAEAEAQ 498
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
215-490 |
3.25e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 215 EQYIN-NLRRQLDSIVGERGRLDSELRNMQDLVEDLKNKYEDeinkrTAAENEFVTLKKDVDAAYMNKVELQAKADTLTD 293
Cdd:COG3206 159 EAYLEqNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 294 EINFLRALYDAELSQMQTHISDTSVVLSmdnnrnldlDSIIAEVKAQYEEIaqrsraeaeswyQTKYEELQVTAGRHGDD 373
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQ---------SPVIQQLRAQLAEL------------EAELAELSARYTPNHPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 374 LRNTKQEIAEINRMIQRLRSEIDhvkkqcASLQAAIADAEQRgemalkdaKNKLEGLEDALQKAKQDLARLLKEYQELMN 453
Cdd:COG3206 293 VIALRAQIAALRAQLQQEAQRIL------ASLEAELEALQAR--------EASLQAQLAQLEARLAELPELEAELRRLER 358
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 120660432 454 vklalDVEIA--TYRKLLEG-EECRLNgEGVGQVNVSVVQ 490
Cdd:COG3206 359 -----EVEVAreLYESLLQRlEEARLA-EALTVGNVRVID 392
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
165-473 |
5.24e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 5.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 165 EQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQgtktvRQNLEPLFEQyINNLRRQLDSIVGERGRLDSELRNMQD 244
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKE-----VKELEELKEE-IEELEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 245 LVEDLKNKYEdEINKRTAAENEfvtLKKDVDaAYMNKVELQAKADTLTDEINFLRALYDAELSQMQTHISDtsvvLSMDN 324
Cdd:PRK03918 267 RIEELKKEIE-ELEEKVKELKE---LKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE----LEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 325 NRNLDLDSIIAEVKAQYEEIAQRSRAeaeswyqtkYEELQVTAGRhgddLRNTKQEIA-----EINRMIQRLRSEIDHVK 399
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHEL---------YEEAKAKKEE----LERLKKRLTgltpeKLEKELEELEKAKEEIE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 400 KQCASLQAAIADAEQRGE------MALKDAKNKL---------EGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIAT 464
Cdd:PRK03918 405 EEISKITARIGELKKEIKelkkaiEELKKAKGKCpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
....*....
gi 120660432 465 YRKLLEGEE 473
Cdd:PRK03918 485 LEKVLKKES 493
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
199-444 |
6.15e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.40 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 199 QEQGTKTVRQNLE-----PLFEQYINNLRRQLDSIVGERGRLDSELRNMQDLVEDLKNKYEDEINKRTAAENEFVTLKKD 273
Cdd:pfam01576 474 QELLQEETRQKLNlstrlRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 274 VDAAYMNKVELQAKADTLtdeinflralyDAELSQMQTHISDTSVVLsmDNNRNL---------DLDSIIAEVK---AQY 341
Cdd:pfam01576 554 LEALTQQLEEKAAAYDKL-----------EKTKNRLQQELDDLLVDL--DHQRQLvsnlekkqkKFDQMLAEEKaisARY 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 342 EEiaQRSRAEAESwyqTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQ----RLRSEIDHVKKQCASLQAAIADAEQrge 417
Cdd:pfam01576 621 AE--ERDRAEAEA---REKETRALSLARALEEALEAKEELERTNKQLRaemeDLVSSKDDVGKNVHELERSKRALEQ--- 692
|
250 260
....*....|....*....|....*..
gi 120660432 418 mALKDAKNKLEGLEDALQKAKQDLARL 444
Cdd:pfam01576 693 -QVEEMKTQLEELEDELQATEDAKLRL 718
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
218-437 |
2.10e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 218 INNLRRQLDSIVGERGRLDSELRNMQDLVEDLKNKYEDEINKRTAAENEFVTLKKDVDaaymnkvELQAKADTLTDEI-N 296
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEERREELgE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 297 FLRALYDAELSqmqthISDTSVVLSMDN-----NRNLDLDSIIAEVKAQYEEI--AQRSRAEAESWYQTKYEELQVTAGR 369
Cdd:COG3883 91 RARALYRSGGS-----VSYLDVLLGSESfsdflDRLSALSKIADADADLLEELkaDKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 120660432 370 HGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQRGEMALKDAKNKLEGLEDALQKA 437
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
373-454 |
5.24e-05 |
|
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: 45.53 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 373 DLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQR---GEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQ 449
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
....*
gi 120660432 450 ELMNV 454
Cdd:COG4942 108 ELLRA 112
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
372-451 |
6.47e-05 |
|
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: 45.53 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 372 DDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQRgemaLKDAKNKLEGLEDALQKAKQDLARLLKEYQEL 451
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAEL 95
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
231-451 |
6.64e-05 |
|
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: 45.53 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 231 ERGRLDSELRNMQDLVEDLKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRalydAELSQMQ 310
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR----AELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 311 THISDTSVVLSMDNNRNldldsiIAEVKAQYEEIAQRSRAEAesWYQTKYEELQvtagRHGDDLRNTKQEIAEINRMIQR 390
Cdd:COG4942 104 EELAELLRALYRLGRQP------PLALLLSPEDFLDAVRRLQ--YLKYLAPARR----EQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 120660432 391 LRSEIDHVKKQCASLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQEL 451
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
329-467 |
9.54e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 9.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 329 DLDSIIAEVKAQYEEIAQRsRAEAEswyqTKYEELQVT-AGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQA 407
Cdd:COG4913 299 ELRAELARLEAELERLEAR-LDALR----EELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 408 AIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRK 467
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
372-478 |
1.19e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 372 DDLRNTKQEIAEINRMIQRLRSEIDHVKKQC----------------ASLQAAIADAEQRGEmALKDAKNKLEGLEDALQ 435
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidvASAEREIAELEAELE-RLDASSDDLAALEEQLE 695
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 120660432 436 KAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLNG 478
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
329-470 |
1.43e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 329 DLDSIIAEVKAQYEEI-AQRSRAEAE-SWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVK--KQCAS 404
Cdd:COG1579 14 ELDSELDRLEHRLKELpAELAELEDElAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEA 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 120660432 405 LQAAIADAEQR---GEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELmnvKLALDVEIATYRKLLE 470
Cdd:COG1579 94 LQKEIESLKRRisdLEDEILELMERIEELEEELAELEAELAELEAELEEK---KAELDEELAELEAELE 159
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
263-467 |
1.89e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 263 AENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYD---AELSQMQTHISDTsvvlsmdnnrNLDLDSIIAEVKA 339
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNelqAELEALQAEIDKL----------QAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 340 QYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNtkqeIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQRGEmA 419
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDVLLGSESFSDFLDR----LSALSKIADADADLLEELKADKAELEAKKAELEAKLA-E 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 120660432 420 LKDAKNKLEGLEDALQKAKQD----LARLLKEYQELMNVKLALDVEIATYRK 467
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEqealLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
222-453 |
2.13e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 222 RRQLDSIVGERGRLDSELRNMQDLVEDLKNKYEDEINKRTAAENEFVTLKKDVDAAymnkvELQAKADTLTDEInflral 301
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELEAEL------ 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 302 ydaelsqmqthisdtsvvlsmdnnRNLDLDS-IIAEVKAQYEEiAQRSRAEAESwyqtKYEELQVTAGRHgddlrntKQE 380
Cdd:COG4913 678 ------------------------ERLDASSdDLAALEEQLEE-LEAELEELEE----ELDELKGEIGRL-------EKE 721
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 120660432 381 IAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMN 453
Cdd:COG4913 722 LEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMR 794
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
334-464 |
3.16e-04 |
|
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: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 334 IAEVKAQYEEIAQRSRAEAEswyqtKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAE 413
Cdd:COG1196 262 LAELEAELEELRLELEELEL-----ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 120660432 414 QR---GEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIAT 464
Cdd:COG1196 337 EEleeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
156-455 |
4.83e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.17 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 156 IQRVRAEEREQIKTLNNKFASfidkvrfLEQQNKVLDTKWTLLQE-----------QGTKTVRQNLEPLFEQYINNLRRQ 224
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVE-------LEELKKILAEDEKLLDEkkqfekiaeelKGKEQELIFLLQAREKEIHDLEIQ 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 225 LDSIVGERGRLDSElrnmqdlVEDLKNKYEDEINKRTAaenefvtLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDA 304
Cdd:pfam05483 459 LTAIKTSEEHYLKE-------VEDLKTELEKEKLKNIE-------LTAHCDKLLLENKELTQEASDMTLELKKHQEDIIN 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 305 ELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLR--NTKQEIA 382
Cdd:pfam05483 525 CKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKcnNLKKQIE 604
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 120660432 383 EINRMIQRLRSEIDHVKKQcaslqaaiADAEQRGEMALKDAKNKLEgLEdaLQKAKQDLARLLKEYQELMNVK 455
Cdd:pfam05483 605 NKNKNIEELHQENKALKKK--------GSAENKQLNAYEIKVNKLE-LE--LASAKQKFEEIIDNYQKEIEDK 666
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
165-450 |
5.95e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 165 EQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQgTKTVRQNLEPLfEQYINNLRRQLDSIVGERGRLDSELRNMQD 244
Cdd:TIGR04523 75 NKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSE-IKNDKEQKNKL-EVELNKLEKQKKENKKNIDKFLTEIKKKEK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 245 LVEDLKNKYEDEINKRTAAENEFVTLKKDvdaaymnKVELQAKADTLTDEINFLRALydaeLSQMQTHISdtsvvlsmdn 324
Cdd:TIGR04523 153 ELEKLNNKYNDLKKQKEELENELNLLEKE-------KLNIQKNIDKIKNKLLKLELL----LSNLKKKIQ---------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 325 nRNLDLDSIIAEVKAQYEEIaqrsraeaeswyQTKYEELQvtagrhgDDLRNTKQEIAEINRMIQRLRSEIDHVKKQcas 404
Cdd:TIGR04523 212 -KNKSLESQISELKKQNNQL------------KDNIEKKQ-------QEINEKTTEISNTQTQLNQLKDEQNKIKKQ--- 268
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 120660432 405 LQAAIADAEQrgemalkdAKNKLEGLEDALQKAKQDLARLLKEYQE 450
Cdd:TIGR04523 269 LSEKQKELEQ--------NNKKIKELEKQLNQLKSEISDLNNQKEQ 306
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
336-473 |
7.64e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 336 EVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQR 415
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 120660432 416 gemaLKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEE 473
Cdd:COG1196 297 ----LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
218-474 |
8.11e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 8.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 218 INNLRRQLDSIVGERGRLDSELRNMQDLVEDLKNKYEDEINKRTaaenEFVTLKKDVDAAYMNKVELQAKADTLTDEINF 297
Cdd:PRK02224 208 LNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE----ELETLEAEIEDLRETIAETEREREELAEEVRD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 298 LRALYDaELSQMQTHISDTSVVLSMDNN----RNLDLDSIIAEVKAQYEEI---AQRSRAEAESW------YQTKYEELQ 364
Cdd:PRK02224 284 LRERLE-ELEEERDDLLAEAGLDDADAEaveaRREELEDRDEELRDRLEECrvaAQAHNEEAESLredaddLEERAEELR 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 365 VTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDhvkkqcaSLQAAIADAeqrgEMALKDAKNKLEGLEDALQKAKQDLARL 444
Cdd:PRK02224 363 EEAAELESELEEAREAVEDRREEIEELEEEIE-------ELRERFGDA----PVDLGNAEDFLEELREERDELREREAEL 431
|
250 260 270
....*....|....*....|....*....|
gi 120660432 445 LKEYQELMNVklaldveIATYRKLLEGEEC 474
Cdd:PRK02224 432 EATLRTARER-------VEEAEALLEAGKC 454
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
329-476 |
9.13e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 9.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 329 DLDSIIAEVKAQYEEIAQRSRA----EAESWYQTKYEELQVTAGRHGD---DLRNTKQEIAEINRMIQRLRSEIDHVKKQ 401
Cdd:COG4913 628 EAEERLEALEAELDALQERREAlqrlAEYSWDEIDVASAEREIAELEAeleRLDASSDDLAALEEQLEELEAELEELEEE 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 402 CASLQAAIADAEQRgemaLKDAKNKLEGLEDALQKA-----KQDLARLLKEYQELM------NVKLALDVEIATYRKLLE 470
Cdd:COG4913 708 LDELKGEIGRLEKE----LEQAEEELDELQDRLEAAedlarLELRALLEERFAAALgdaverELRENLEERIDALRARLN 783
|
....*.
gi 120660432 471 GEECRL 476
Cdd:COG4913 784 RAEEEL 789
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
334-467 |
9.41e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 334 IAEVKAQYEEIAQRsRAEAESWYQTKYEELQVTAGRHgdDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAE 413
Cdd:COG4717 390 ALEQAEEYQELKEE-LEELEEQLEELLGELEELLEAL--DEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 120660432 414 QRGEmalkdaknkLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRK 467
Cdd:COG4717 467 EDGE---------LAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
205-451 |
1.04e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 205 TVRQNLEPLFEqyINNLRRQLDSIVGERGRLDSELRNMQDLVEDLKNKYEDEINKRTAAENEFVTLKKDVDaaymnkvEL 284
Cdd:COG1579 1 AMPEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE-------EV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 285 QAKADTLTDEINFLRalydaelsqmqthisdtsvvlsmdNNRnlDLDSIIAEVkaqyeEIAQRSRAEAEswyqtkyeelq 364
Cdd:COG1579 72 EARIKKYEEQLGNVR------------------------NNK--EYEALQKEI-----ESLKRRISDLE----------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 365 vtagrhgddlrntkQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDL-AR 443
Cdd:COG1579 110 --------------DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIpPE 175
|
....*...
gi 120660432 444 LLKEYQEL 451
Cdd:COG1579 176 LLALYERI 183
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
156-446 |
1.34e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.96 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 156 IQRVRAEEREQIKTLNNK---FASFIDKVRFLEQQNKVLD----------TKWTLLQEQGTKTVRQNLEPLFEQYINNLR 222
Cdd:TIGR01612 598 INKLKLELKEKIKNISDKneyIKKAIDLKKIIENNNAYIDelakispyqvPEHLKNKDKIYSTIKSELSKIYEDDIDALY 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 223 RQLDSIVGErgrldSELRNMQD--LVEDLKNKYEDEINKRTAAENEfvTLKKDVDAAYMNKVELQAKA--------DTLT 292
Cdd:TIGR01612 678 NELSSIVKE-----NAIDNTEDkaKLDDLKSKIDKEYDKIQNMETA--TVELHLSNIENKKNELLDIIveikkhihGEIN 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 293 DEINFLRALYDAELSQMQTHISDTSvvlsmdnNRNLDLD---SIIAEVKAQYEE---IAQRSRAEAESWYQTKYEELQVT 366
Cdd:TIGR01612 751 KDLNKILEDFKNKEKELSNKINDYA-------KEKDELNkykSKISEIKNHYNDqinIDNIKDEDAKQNYDKSKEYIKTI 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 367 AGRHGD------DLRNTKQEI-AEINRMI-------QRLRSEIDHVKKQCASLQAAIADAEQRG-EMALKDAKNKLEGLE 431
Cdd:TIGR01612 824 SIKEDEifkiinEMKFMKDDFlNKVDKFInfennckEKIDSEHEQFAELTNKIKAEISDDKLNDyEKKFNDSKSLINEIN 903
|
330
....*....|....*
gi 120660432 432 DALQKAKQDLARLLK 446
Cdd:TIGR01612 904 KSIEEEYQNINTLKK 918
|
|
| DUF1351 |
pfam07083 |
Protein of unknown function (DUF1351); This family consists of several bacterial and phage ... |
327-462 |
1.52e-03 |
|
Protein of unknown function (DUF1351); This family consists of several bacterial and phage proteins of around 230 residues in length. The function of this family is unknown.
Pssm-ID: 429283 [Multi-domain] Cd Length: 210 Bit Score: 40.05 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 327 NLDLDSIIAEVKAQYEEIAQRSRAEAEswyqtKYEELQVTAgrhgDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCAslq 406
Cdd:pfam07083 1 ELSVTQKPAAISFNFEELETYVDGIVA-----KYEGLVVTE----DTVKEAKKERAELNKIAKALDDKRKEVKKQYS--- 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 120660432 407 AAIADAEQRG---EMALKDAKNKL----EGLEDALQKAKQDLARLLK-EYQELMNVKLAlDVEI 462
Cdd:pfam07083 69 EPYDEFEAKIkelVAKIKEAIDPIdeqiKAFEEKEKDAKRQLVKALIsELAEEYGVPLE-EIEI 131
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
162-436 |
1.64e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.58 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 162 EEREQIKTLNNKFASFIDKVRFLE-------------QQNKVLDTkWTLLQEQGTKTVRQNLEPLFEQYiNNLRRQLDSI 228
Cdd:TIGR01612 693 EDKAKLDDLKSKIDKEYDKIQNMEtatvelhlsnienKKNELLDI-IVEIKKHIHGEINKDLNKILEDF-KNKEKELSNK 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 229 VGERGRLDSELRNMQDLVEDLKNKYEDEINKRTAAENEfvtLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDAELSQ 308
Cdd:TIGR01612 771 INDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDED---AKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNK 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 309 MQTHIsdtsvvlSMDNNRNLDLDSiiaeVKAQYEEIAQRSRAEAESWYQTKYEelqvtagrhgDDLRNTKQEIAEINRMI 388
Cdd:TIGR01612 848 VDKFI-------NFENNCKEKIDS----EHEQFAELTNKIKAEISDDKLNDYE----------KKFNDSKSLINEINKSI 906
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 120660432 389 QRLRSEIDHVKKQCASLQAAIADAEqrgemALKDAKNKLEGLEDALQK 436
Cdd:TIGR01612 907 EEEYQNINTLKKVDEYIKICENTKE-----SIEKFHNKQNILKEILNK 949
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
128-475 |
1.98e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 128 PVCPP--GGIQEVTVNQSLLTPLNLQIDpaiqrvraEEREQIKTLNNKFASFIDKVRFLEQQnkvldtkWTLLQEQGTKT 205
Cdd:TIGR00618 525 PLTRRmqRGEQTYAQLETSEEDVYHQLT--------SERKQRASLKEQMQEIQQSFSILTQC-------DNRSKEDIPNL 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 206 vrQNLEPLFEQYINNLRRQLDSIVGERGRLDSELR---NMQDLVEDLKNKYEDEINKRTAAENEFVTLKKDvdaaymnKV 282
Cdd:TIGR00618 590 --QNITVRLQDLTEKLSEAEDMLACEQHALLRKLQpeqDLQDVRLHLQQCSQELALKLTALHALQLTLTQE-------RV 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 283 ELQAKADTLTDEINFLRALydAELSQMQTHISDTSVVLSMDNNRNLDLDSI---IAEVKAQYEEIAQRSRA--------- 350
Cdd:TIGR00618 661 REHALSIRVLPKELLASRQ--LALQKMQSEKEQLTYWKEMLAQCQTLLRELethIEEYDREFNEIENASSSlgsdlaare 738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 351 EAESWYQTKYEELQVTAGRHG--DDLRNTKQEIAEINRM--IQRLRSEIDHVKKQCASLQAAIADAEQRGEMALKDAKNK 426
Cdd:TIGR00618 739 DALNQSLKELMHQARTVLKARteAHFNNNEEVTAALQTGaeLSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDI 818
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 120660432 427 LEGLEDALQKAKQDLARLLKEyqelmnvKLALDVEIAtyRKLLEGEECR 475
Cdd:TIGR00618 819 LNLQCETLVQEEEQFLSRLEE-------KSATLGEIT--HQLLKYEECS 858
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
372-485 |
2.89e-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: 40.82 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 372 DDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQ-------RGEMALKDA---KNKLEGLEDALQKAKQDL 441
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRkigeiekEIEQLEQEEeklKERLEELEEDLSSLEQEI 753
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 120660432 442 ARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLNGEGVGQVN 485
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQ 797
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
233-450 |
3.20e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 39.66 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 233 GRLDSELRNMQDLVEDLKNKYEDE--INKRTAAENEFVTLKKDVDaaymnkvELQAKADTLTDEIN-FLRAL--YDAELS 307
Cdd:cd22656 87 GTIDSYYAEILELIDDLADATDDEelEEAKKTIKALLDDLLKEAK-------KYQDKAAKVVDKLTdFENQTekDQTALE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 308 QMQTHISDtsvVLSMDNNRNL--DLDSIIAEVKAQYEEIAQRSRA---EAESWYQTKYEELQV------TAGRHGDDLRN 376
Cdd:cd22656 160 TLEKALKD---LLTDEGGAIArkEIKDLQKELEKLNEEYAAKLKAkidELKALIADDEAKLAAalrliaDLTAADTDLDN 236
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 120660432 377 TKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQrgemALKDAKNKLEGLEDALQKAKqDLARLLKEYQE 450
Cdd:cd22656 237 LLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDIS----KIPAAILAKLELEKAIEKWN-ELAEKADKFRQ 305
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
153-456 |
6.50e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 153 DPAIQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRQNLEplFEQYINNLRRQLDSIVGER 232
Cdd:PRK02224 323 DEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVED--RREEIEELEEEIEELRERF 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 233 GRLDSELRNMQDLVEDLKNKYEDEINKRTAAENEFVTLKKDVDAAYM-----------NKVELQAKADTLTDEINFLRAL 301
Cdd:PRK02224 401 GDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgQPVEGSPHVETIEEDRERVEEL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 302 yDAELSQMQTHISDTSVVL--------------SMDNNRNlDLDSIIAEVKAQYEE---IAQRSRAEAESwYQTKYEELQ 364
Cdd:PRK02224 481 -EAELEDLEEEVEEVEERLeraedlveaedrieRLEERRE-DLEELIAERRETIEEkreRAEELRERAAE-LEAEAEEKR 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 365 VTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKqCASLQAAIADAEQR-----------GEM---------ALKDAK 424
Cdd:PRK02224 558 EAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEierlrekrealAELnderrerlaEKRERK 636
|
330 340 350
....*....|....*....|....*....|....
gi 120660432 425 NKLEGL--EDALQKAKQDLARlLKEYQELMNVKL 456
Cdd:PRK02224 637 RELEAEfdEARIEEAREDKER-AEEYLEQVEEKL 669
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
381-476 |
6.73e-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: 39.67 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 381 IAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQRGEmALKDAKNKLEGLeDALQKAKQDLA--RLLKEYQELMNVKLAL 458
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLE-RLRREREKAERY-QALLKEKREYEgyELLKEKEALERQKEAI 242
|
90
....*....|....*...
gi 120660432 459 DVEIATYRKLLEGEECRL 476
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEI 260
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
334-445 |
6.95e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 39.09 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 334 IAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQ-EIAEINRMIQRLRSEIDHVKKQCASLQAAIADA 412
Cdd:COG2268 246 LAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREiELQEKEAEREEAELEADVRKPAEAEKQAAEAEA 325
|
90 100 110
....*....|....*....|....*....|....*.
gi 120660432 413 EQRGEMALKDAKNKLEGLE---DALQKAKQDLARLL 445
Cdd:COG2268 326 EAEAEAIRAKGLAEAEGKRalaEAWNKLGDAAILLM 361
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
372-476 |
8.54e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 38.46 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 372 DDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQEL 451
Cdd:smart00787 158 EDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQEL 237
|
90 100 110
....*....|....*....|....*....|..
gi 120660432 452 -------MNVKLALDVEIATYRKLLegEECRL 476
Cdd:smart00787 238 eskiedlTNKKSELNTEIAEAEKKL--EQCRG 267
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
335-450 |
8.61e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.99 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 335 AEVKAQYEEIAQRSRAEAE-----SWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAI 409
Cdd:PRK12704 58 ALLEAKEEIHKLRNEFEKElrerrNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELI 137
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 120660432 410 ADAEQRGE----MALKDAKNKLegLEDALQKAKQDLARLLKEYQE 450
Cdd:PRK12704 138 EEQLQELErisgLTAEEAKEIL--LEKVEEEARHEAAVLIKEIEE 180
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
232-470 |
9.21e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.05 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 232 RGRLDSELRNMQDLVEDLKN-----KYEDEINKRTAAENEFVTLKKDVDAAYM-----------NKVELQAKADTLTDEI 295
Cdd:pfam12128 220 RQQVEHWIRDIQAIAGIMKIrpeftKLQQEFNTLESAELRLSHLHFGYKSDETliasrqeerqeTSAELNQLLRTLDDQW 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 296 NFLRALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESwyqtKYEELQVTAGRHGDDLR 375
Cdd:pfam12128 300 KEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELEN----LEERLKALTGKHQDVTA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 376 NTKQEIAEI----NRMIQRLRSEIDHVKKQCASLQAAIADAEQRGEMALKD--------AKNKLEGLEDALQKAKQDLAR 443
Cdd:pfam12128 376 KYNRRRSKIkeqnNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREqleagkleFNEEEYRLKSRLGELKLRLNQ 455
|
250 260
....*....|....*....|....*..
gi 120660432 444 LLKEYQELMNVKlALDVEIATYRKLLE 470
Cdd:pfam12128 456 ATATPELLLQLE-NFDERIERAREEQE 481
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
211-481 |
9.34e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.11 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 211 EPLFEQYINNLRRQLDSIVGERGRLDSELRNMQDLvEDLKNKYEDEINK---RTAAENEFVTLKKDV---------DAAY 278
Cdd:PRK01156 213 HSITLKEIERLSIEYNNAMDDYNNLKSALNELSSL-EDMKNRYESEIKTaesDLSMELEKNNYYKELeerhmkiinDPVY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 279 MNKVELQAKADTLTDEINFLRAL--YDAELSQMQTHISDTSVVLSMDNN------RNLDLDSIIAEVKaQYEEIAQRSRA 350
Cdd:PRK01156 292 KNRNYINDYFKYKNDIENKKQILsnIDAEINKYHAIIKKLSVLQKDYNDyikkksRYDDLNNQILELE-GYEMDYNSYLK 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 351 EAESwYQTKYEELQVTAGRHGDDLRNT--KQEI--AEINRMIQRLRSEIDHVKKQCASLQAAIaDAEQRGEMALKDAKNK 426
Cdd:PRK01156 371 SIES-LKKKIEEYSKNIERMSAFISEIlkIQEIdpDAIKKELNEINVKLQDISSKVSSLNQRI-RALRENLDELSRNMEM 448
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660432 427 LEG---------------LEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEgeecRLNGEGV 481
Cdd:PRK01156 449 LNGqsvcpvcgttlgeekSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKE----YLESEEI 514
|
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