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Conserved domains on  [gi|296179395|ref|NP_065780|]
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protein BCAP isoform a [Homo sapiens]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 340-609 5.48e-07

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 52.76  E-value: 5.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   340 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLlhknnqitKTKN 419
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL--------EEDL 746

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   420 KNVEKMRGQMESHLKELERVCDSLtaaERRLHECQESLQCCKGKCADQEhtIRELQGQILKQWEEYSVL-AWVDGNHNLL 498
Cdd:TIGR02169  747 SSLEQEIENVKSELKELEARIEEL---EEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIeARLREIEQKL 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   499 TKLSLEEEncLIQLKCENLQQKLEQMDAENKELEKKLANqeecLKHSNLKFKEKSAEYTALARQLEAALEEgrqkVAEEI 578
Cdd:TIGR02169  822 NRLTLEKE--YLEKEIQELQEQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGD----LKKER 891

                          250       260       270
                   ....*....|....*....|....*....|.
gi 296179395   579 EKMSSRESALQIKILDLETELRKKNEEQNQL 609
Cdd:TIGR02169  892 DELEAQLRELERKIEELEAQIEKKRKRLSEL 922
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 135-443 1.22e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 1.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   135 ENLTDNESENTNLKKKVFEKEAHIQELSCLFQSEKANTLKANRFSQSVKVVHERLQIQIHKREAENDKLKEYVKSLETKI 214
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   215 AKWNLQsrmnkneaivmKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIE 294
Cdd:TIGR02168  764 EELEER-----------LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   295 KTELEVQIETMKKQIINLLEDLKKME---DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSE 371
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296179395   372 LQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSL 443
Cdd:TIGR02168  913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 340-609 5.48e-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: 5.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   340 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLlhknnqitKTKN 419
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL--------EEDL 746

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   420 KNVEKMRGQMESHLKELERVCDSLtaaERRLHECQESLQCCKGKCADQEhtIRELQGQILKQWEEYSVL-AWVDGNHNLL 498
Cdd:TIGR02169  747 SSLEQEIENVKSELKELEARIEEL---EEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIeARLREIEQKL 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   499 TKLSLEEEncLIQLKCENLQQKLEQMDAENKELEKKLANqeecLKHSNLKFKEKSAEYTALARQLEAALEEgrqkVAEEI 578
Cdd:TIGR02169  822 NRLTLEKE--YLEKEIQELQEQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGD----LKKER 891

                          250       260       270
                   ....*....|....*....|....*....|.
gi 296179395   579 EKMSSRESALQIKILDLETELRKKNEEQNQL 609
Cdd:TIGR02169  892 DELEAQLRELERKIEELEAQIEKKRKRLSEL 922
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 135-443 1.22e-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: 48.51  E-value: 1.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   135 ENLTDNESENTNLKKKVFEKEAHIQELSCLFQSEKANTLKANRFSQSVKVVHERLQIQIHKREAENDKLKEYVKSLETKI 214
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   215 AKWNLQsrmnkneaivmKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIE 294
Cdd:TIGR02168  764 EELEER-----------LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   295 KTELEVQIETMKKQIINLLEDLKKME---DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSE 371
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296179395   372 LQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSL 443
Cdd:TIGR02168  913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 296-608 5.79e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 5.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 296 TELEVQIETMKKQiinlledLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEV 375
Cdd:COG1196  196 GELERQLEPLERQ-------AEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 376 EKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKN----------KNVEKMRGQMESHLKELERVCDSLTA 445
Cdd:COG1196  269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReleerleeleEELAELEEELEELEEELEELEEELEE 348

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 446 AERRLHECQESLQCCKGKCADQEHTIRELQGQILKQWEEYSVLAwvdgnHNLLTKLSLEEEnclIQLKCENLQQKLEQMD 525
Cdd:COG1196  349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL-----RAAAELAAQLEE---LEEAEEALLERLERLE 420

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 526 AENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEE 605
Cdd:COG1196  421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500


                 ...
gi 296179395 606 QNQ 608
Cdd:COG1196  501 ADY 503
PRK11637 PRK11637
AmiB activator; Provisional
 418-604 6.89e-05

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 45.45  E-value: 6.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 418 KNKNVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQILKQweEYSVLAWVD----- 492
Cdd:PRK11637  59 KEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQ--ERLLAAQLDaafrq 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 493 GNHN-LLTKLSLEEE-------------NCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLkhSNLKFKEKSAEYTA 558
Cdd:PRK11637 137 GEHTgLQLILSGEESqrgerilayfgylNQARQETIAELKQTREELAAQKAELEEKQSQQKTLL--YEQQAQQQKLEQAR 214

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 296179395 559 LARQ-----LEAALEEGRQKVAEeiekMSSRESALQIKILDLETELRKKNE 604
Cdd:PRK11637 215 NERKktltgLESSLQKDQQQLSE----LRANESRLRDSIARAEREAKARAE 261
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
196-396 2.25e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.24  E-value: 2.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 196 REAENDKLKEYVKSLETKIAKwnLQSRMNKNEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKL- 274
Cdd:COG3206  166 LELRREEARKALEFLEEQLPE--LRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLa 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 275 --------SETISASNAWKSHYEKIVIEKTELEVQIETMKK-------QIINLLEDLKKMEDHGKnscEEILRKVHSIEY 339
Cdd:COG3206  244 alraqlgsGPDALPELLQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQ---QEAQRILASLEA 320

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 296179395 340 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEA 396
Cdd:COG3206  321 ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 33-601 6.32e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.18  E-value: 6.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395    33 ESHLSCLKQDILNEKTELEATLKEAElvtHSVELLLPLFKDTIEKInfenanLSALNLKISEQKEILIKELDTFKSVKLA 112
Cdd:pfam15921  230 DTEISYLKGRIFPVEDQLEALKSESQ---NKIELLLQQHQDRIEQL------ISEHEVEITGLTEKASSARSQANSIQSQ 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   113 LEHLlrkrdyKQTGDNLSSMLLENLTDNESENTNLKKKVFEK----EAHIQELS---CLFQSE--KANTlKANRFSQSVK 183
Cdd:pfam15921  301 LEII------QEQARNQNSMYMRQLSDLESTVSQLRSELREAkrmyEDKIEELEkqlVLANSEltEART-ERDQFSQESG 373

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   184 VVHERLQ---IQIHKREAENDKLKEYVKSLetkiakWNlqsrMNKNEAIVMKEASRQ---KTVALKKASKVYKQRLDHFT 257
Cdd:pfam15921  374 NLDDQLQkllADLHKREKELSLEKEQNKRL------WD----RDTGNSITIDHLRRElddRNMEVQRLEALLKAMKSECQ 443

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   258 GAIEKLTSQIRDQEAKLSETISasnawkshyekiviekteLEVQIETMKKQIINLLEDL--KKME-DHGKNSCEEILRKV 334
Cdd:pfam15921  444 GQMERQMAAIQGKNESLEKVSS------------------LTAQLESTKEMLRKVVEELtaKKMTlESSERTVSDLTASL 505

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   335 HSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEkkqkTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQI 414
Cdd:pfam15921  506 QEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQ----TECEALKLQMAEKDKVIEILRQQIENMTQLVGQH 581

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   415 TKTKNK-NVEK-------------------MRGQMESHLKELE-RVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRE 473
Cdd:pfam15921  582 GRTAGAmQVEKaqlekeindrrlelqefkiLKDKKDAKIRELEaRVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNE 661

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   474 LQ---GQILKQWEEYSVLawvdgNHNLLTKLS-LEEENCLIQLKCENLQQKLEQMDAENKELE----------------- 532
Cdd:pfam15921  662 VKtsrNELNSLSEDYEVL-----KRNFRNKSEeMETTTNKLKMQLKSAQSELEQTRNTLKSMEgsdghamkvamgmqkqi 736

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   533 -----------KKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEgRQKVAEEIEKMSSRESALQIKILDLETELRK 601
Cdd:pfam15921  737 takrgqidalqSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE-KNKMAGELEVLRSQERRLKEKVANMEVALDK 815
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 307-420 9.47e-04

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 39.99  E-value: 9.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395  307 KQIINLLEDLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMY 386
Cdd:pfam11559  34 ARIINVIYELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNE 113

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 296179395  387 KTQVQKLQEAAEIVKSRCENLLHKNN-QITKTKNK 420
Cdd:pfam11559 114 KEELQRLKNALQQIKTQFAHEVKKRDrEIEKLKER 148
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
12-578 7.00e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 7.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395  12 EELFCHLKTISEKEDLPRCTSE--SHLSCLKQDILNEKTELEATLKEAELVTHSVELLLPLFKDTIEKINFENANLSALN 89
Cdd:PRK03918 200 KELEEVLREINEISSELPELREelEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395  90 LKISEQKEILIKELDTFKSVKLALEHLLRKRDYKQTGDNLSSML------LENLTDNESENTNLKKKVFEKEAHIQELSC 163
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIngieerIKELEEKEERLEELKKKLKELEKRLEELEE 359

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 164 ---LFQSEKANTLKANRFSQSVKVVH-ERLQIQIHKREAENDKLKEYVKSLETKIAKWNLQSRMNKNEAIVMKEASRQKT 239
Cdd:PRK03918 360 rheLYEEAKAKKEELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCP 439

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 240 VALKKASKVYKQRLdhftgaIEKLTSQIRDQEAKLSETISASNAWKSHYEKI--VIEKTELEVQIETMKKQIINLLEDLK 317
Cdd:PRK03918 440 VCGRELTEEHRKEL------LEEYTAELKRIEKELKEIEEKERKLRKELRELekVLKKESELIKLKELAEQLKELEEKLK 513

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 318 KMEdhgknsCEEILRKvhSIEYEnetlnlentKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEmyktqvqKLQEaa 397
Cdd:PRK03918 514 KYN------LEELEKK--AEEYE---------KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK-------KLDE-- 567

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 398 eiVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDS---LTAAERRLHECQESLQCCKGKCADQEHTIREL 474
Cdd:PRK03918 568 --LEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAekeLEREEKELKKLEEELDKAFEELAETEKRLEEL 645

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 475 QGQILKQWEEYSVLAWvDGNHNLLTKLSLEEENCLIQLkcENLQQKLEQMDAENKELEKKLANQEECLKHSNL------- 547
Cdd:PRK03918 646 RKELEELEKKYSEEEY-EELREEYLELSRELAGLRAEL--EELEKRREEIKKTLEKLKEELEEREKAKKELEKlekaler 722

                        570       580       590
                 ....*....|....*....|....*....|...
gi 296179395 548 --KFKEKSAEYTALARqlEAALEEgRQKVAEEI 578
Cdd:PRK03918 723 veELREKVKKYKALLK--ERALSK-VGEIASEI 752
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 340-609 5.48e-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: 5.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   340 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLlhknnqitKTKN 419
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL--------EEDL 746

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   420 KNVEKMRGQMESHLKELERVCDSLtaaERRLHECQESLQCCKGKCADQEhtIRELQGQILKQWEEYSVL-AWVDGNHNLL 498
Cdd:TIGR02169  747 SSLEQEIENVKSELKELEARIEEL---EEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIeARLREIEQKL 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   499 TKLSLEEEncLIQLKCENLQQKLEQMDAENKELEKKLANqeecLKHSNLKFKEKSAEYTALARQLEAALEEgrqkVAEEI 578
Cdd:TIGR02169  822 NRLTLEKE--YLEKEIQELQEQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGD----LKKER 891

                          250       260       270
                   ....*....|....*....|....*....|.
gi 296179395   579 EKMSSRESALQIKILDLETELRKKNEEQNQL 609
Cdd:TIGR02169  892 DELEAQLRELERKIEELEAQIEKKRKRLSEL 922
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 135-443 1.22e-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: 48.51  E-value: 1.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   135 ENLTDNESENTNLKKKVFEKEAHIQELSCLFQSEKANTLKANRFSQSVKVVHERLQIQIHKREAENDKLKEYVKSLETKI 214
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   215 AKWNLQsrmnkneaivmKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIE 294
Cdd:TIGR02168  764 EELEER-----------LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   295 KTELEVQIETMKKQIINLLEDLKKME---DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSE 371
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296179395   372 LQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSL 443
Cdd:TIGR02168  913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 296-608 5.79e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 5.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 296 TELEVQIETMKKQiinlledLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEV 375
Cdd:COG1196  196 GELERQLEPLERQ-------AEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 376 EKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKN----------KNVEKMRGQMESHLKELERVCDSLTA 445
Cdd:COG1196  269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReleerleeleEELAELEEELEELEEELEELEEELEE 348

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 446 AERRLHECQESLQCCKGKCADQEHTIRELQGQILKQWEEYSVLAwvdgnHNLLTKLSLEEEnclIQLKCENLQQKLEQMD 525
Cdd:COG1196  349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL-----RAAAELAAQLEE---LEEAEEALLERLERLE 420

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 526 AENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEE 605
Cdd:COG1196  421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500


                 ...
gi 296179395 606 QNQ 608
Cdd:COG1196  501 ADY 503
PRK11637 PRK11637
AmiB activator; Provisional
 418-604 6.89e-05

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 45.45  E-value: 6.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 418 KNKNVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQILKQweEYSVLAWVD----- 492
Cdd:PRK11637  59 KEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQ--ERLLAAQLDaafrq 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 493 GNHN-LLTKLSLEEE-------------NCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLkhSNLKFKEKSAEYTA 558
Cdd:PRK11637 137 GEHTgLQLILSGEESqrgerilayfgylNQARQETIAELKQTREELAAQKAELEEKQSQQKTLL--YEQQAQQQKLEQAR 214

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 296179395 559 LARQ-----LEAALEEGRQKVAEeiekMSSRESALQIKILDLETELRKKNE 604
Cdd:PRK11637 215 NERKktltgLESSLQKDQQQLSE----LRANESRLRDSIARAEREAKARAE 261
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 396-605 1.28e-04

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: 44.75  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 396 AAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQ 475
Cdd:COG4942   17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 476 GQILKQWEEYS---VLAWVDGNHNLLTKL-----SLEEENCLIQLKC--ENLQQKLEQMDAENKELEKKLANQEECLKHS 545
Cdd:COG4942   97 AELEAQKEELAellRALYRLGRQPPLALLlspedFLDAVRRLQYLKYlaPARREQAEELRADLAELAALRAELEAERAEL 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296179395 546 NLKFKEKSAEYTALA------RQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEE 605
Cdd:COG4942  177 EALLAELEEERAALEalkaerQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 260-534 1.87e-04

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: 44.66  E-value: 1.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   260 IEKLTSQIRDQEAKLSETISASNawkshyekiviEKTELEVQIETMKKQIINLLEDLKKMEDHGKNSCEEILRKVHSIEY 339
Cdd:TIGR02168  255 LEELTAELQELEEKLEELRLEVS-----------ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   340 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTkn 419
Cdd:TIGR02168  324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE-- 401

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   420 knVEKMRGQMESHLKELERVCDSLTAAERRLHECQesLQCCKGKCADQEHTIRELQGQ-ILKQWEEYSVLAWVDGNHNLL 498
Cdd:TIGR02168  402 --IERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEElERLEEALEELREELEEAEQAL 477

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 296179395   499 TKLSLEEENCLIQLK-CENLQQKLEQMDAENKELEKK 534
Cdd:TIGR02168  478 DAAERELAQLQARLDsLERLQENLEGFSEGVKALLKN 514
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
196-396 2.25e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.24  E-value: 2.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 196 REAENDKLKEYVKSLETKIAKwnLQSRMNKNEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKL- 274
Cdd:COG3206  166 LELRREEARKALEFLEEQLPE--LRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLa 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 275 --------SETISASNAWKSHYEKIVIEKTELEVQIETMKK-------QIINLLEDLKKMEDHGKnscEEILRKVHSIEY 339
Cdd:COG3206  244 alraqlgsGPDALPELLQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQ---QEAQRILASLEA 320

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 296179395 340 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEA 396
Cdd:COG3206  321 ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 232-438 2.64e-04

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: 43.60  E-value: 2.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 232 KEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIIN 311
Cdd:COG4942   22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 312 LLEDLK-------KMEDHGK-------NSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEK 377
Cdd:COG4942  102 QKEELAellralyRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296179395 378 KQKTLiemyKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELER 438
Cdd:COG4942  182 ELEEE----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
PTZ00121 PTZ00121
MAEBL; Provisional
 139-606 5.01e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 5.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395  139 DNESENTNLKKKVFEKEAHIQELSCLFQSEKAntlkanRFSQSVKVVHERLQIQIHKREAENDKLKEYVKSLETKiaKWN 218
Cdd:PTZ00121 1246 EEERNNEEIRKFEEARMAHFARRQAAIKAEEA------RKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA--KKA 1317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395  219 LQSRMNKNEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKiVIEKTEL 298
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE-KKKADEA 1396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395  299 EVQIETMKKQIINL--LEDLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVE 376
Cdd:PTZ00121 1397 KKKAEEDKKKADELkkAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAK 1476

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395  377 KKQKTliemyKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKN-KNVEKMRGQMESHLKELERVCDSLTAAERR-----L 450
Cdd:PTZ00121 1477 KKAEE-----AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEaKKAEEAKKADEAKKAEEAKKADEAKKAEEKkkadeL 1551

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395  451 HECQESLQCCKGKCADQEHTIRELQGQILKQWEEysvlawvdgnhnlLTKLSLEEENCLIQLKCENLQQKLEQM-DAENK 529
Cdd:PTZ00121 1552 KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE-------------AKKAEEARIEEVMKLYEEEKKMKAEEAkKAEEA 1618

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296179395  530 ELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKmsSRESALQIKILDLETELRKKNEEQ 606
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK--AEEDKKKAEEAKKAEEDEKKAAEA 1693
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 33-601 6.32e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.18  E-value: 6.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395    33 ESHLSCLKQDILNEKTELEATLKEAElvtHSVELLLPLFKDTIEKInfenanLSALNLKISEQKEILIKELDTFKSVKLA 112
Cdd:pfam15921  230 DTEISYLKGRIFPVEDQLEALKSESQ---NKIELLLQQHQDRIEQL------ISEHEVEITGLTEKASSARSQANSIQSQ 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   113 LEHLlrkrdyKQTGDNLSSMLLENLTDNESENTNLKKKVFEK----EAHIQELS---CLFQSE--KANTlKANRFSQSVK 183
Cdd:pfam15921  301 LEII------QEQARNQNSMYMRQLSDLESTVSQLRSELREAkrmyEDKIEELEkqlVLANSEltEART-ERDQFSQESG 373

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   184 VVHERLQ---IQIHKREAENDKLKEYVKSLetkiakWNlqsrMNKNEAIVMKEASRQ---KTVALKKASKVYKQRLDHFT 257
Cdd:pfam15921  374 NLDDQLQkllADLHKREKELSLEKEQNKRL------WD----RDTGNSITIDHLRRElddRNMEVQRLEALLKAMKSECQ 443

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   258 GAIEKLTSQIRDQEAKLSETISasnawkshyekiviekteLEVQIETMKKQIINLLEDL--KKME-DHGKNSCEEILRKV 334
Cdd:pfam15921  444 GQMERQMAAIQGKNESLEKVSS------------------LTAQLESTKEMLRKVVEELtaKKMTlESSERTVSDLTASL 505

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   335 HSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEkkqkTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQI 414
Cdd:pfam15921  506 QEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQ----TECEALKLQMAEKDKVIEILRQQIENMTQLVGQH 581

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   415 TKTKNK-NVEK-------------------MRGQMESHLKELE-RVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRE 473
Cdd:pfam15921  582 GRTAGAmQVEKaqlekeindrrlelqefkiLKDKKDAKIRELEaRVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNE 661

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   474 LQ---GQILKQWEEYSVLawvdgNHNLLTKLS-LEEENCLIQLKCENLQQKLEQMDAENKELE----------------- 532
Cdd:pfam15921  662 VKtsrNELNSLSEDYEVL-----KRNFRNKSEeMETTTNKLKMQLKSAQSELEQTRNTLKSMEgsdghamkvamgmqkqi 736

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   533 -----------KKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEgRQKVAEEIEKMSSRESALQIKILDLETELRK 601
Cdd:pfam15921  737 takrgqidalqSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE-KNKMAGELEVLRSQERRLKEKVANMEVALDK 815
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 391-609 6.67e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 6.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 391 QKLQEAAEIVKSRcENLLHKNNQITK--TKNKNVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQE 468
Cdd:COG1196  216 RELKEELKELEAE-LLLLKLRELEAEleELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 469 HTIRELQGQILKQWEEYsvlawvdgNHNLLTKLSLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLK 548
Cdd:COG1196  295 AELARLEQDIARLEERR--------RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296179395 549 FKEKSAEYTALARQLEAALEEGRQKVAEEIEKmSSRESALQIKILDLETELRKKNEEQNQL 609
Cdd:COG1196  367 LLEAEAELAEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLERLERLEEELEEL 426
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
258-609 9.16e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 9.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 258 GAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGKNSCEEI------- 330
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIeeleekv 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 331 --LRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKqktlIEMYKTQVQKLQEAAEIVKSRCENLL 408
Cdd:PRK03918 283 keLKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE----LEEKEERLEELKKKLKELEKRLEELE 358

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 409 HKNNQITKTKNKNVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQILKQWEEYSVL 488
Cdd:PRK03918 359 ERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC 438

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 489 ----AWVDGNH--NLLTKLSLEEENclIQLKCENLQQKLEQMDAENKELEKKLANQEECLKhsnlkFKEKSAEYTALARQ 562
Cdd:PRK03918 439 pvcgRELTEEHrkELLEEYTAELKR--IEKELKEIEEKERKLRKELRELEKVLKKESELIK-----LKELAEQLKELEEK 511

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 296179395 563 LEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQL 609
Cdd:PRK03918 512 LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL 558
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 307-420 9.47e-04

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 39.99  E-value: 9.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395  307 KQIINLLEDLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMY 386
Cdd:pfam11559  34 ARIINVIYELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNE 113

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 296179395  387 KTQVQKLQEAAEIVKSRCENLLHKNN-QITKTKNK 420
Cdd:pfam11559 114 KEELQRLKNALQQIKTQFAHEVKKRDrEIEKLKER 148
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 427-609 1.08e-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: 42.35  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   427 GQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQILKQWEEYSVLAwvdgnhNLLTKL----- 501
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA------NEISRLeqqkq 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   502 -------SLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEaALEEGRQKV 574
Cdd:TIGR02168  306 ilrerlaNLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE-ELEEQLETL 384

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 296179395   575 AEEIEKMSSRESALQIKILDLETELRKKNEEQNQL 609
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
187-604 1.49e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 187 ERLQIQIHKREAENdkLKEYVKSLETKIAKwnlqsrmnkneaivmkeaSRQKTVALKKASKVYKQRLDHFTGAIEKLTSQ 266
Cdd:PRK02224 333 CRVAAQAHNEEAES--LREDADDLEERAEE------------------LREEAAELESELEEAREAVEDRREEIEELEEE 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 267 IRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKME---DHGK-NSCEEILRK---VHSIEY 339
Cdd:PRK02224 393 IEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEallEAGKcPECGQPVEGsphVETIEE 472

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 340 ENEtlnlENTKLKTTLAALKDEVVSVE---NELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLlhknnqitk 416
Cdd:PRK02224 473 DRE----RVEELEAELEDLEEEVEEVEerlERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERA--------- 539

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 417 tknknvEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQgqilkqweeysvlawvdgnhN 496
Cdd:PRK02224 540 ------EELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE--------------------R 593

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 497 LLTKLSLEEEnclIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYtalARQLEAALEEGRQKVAE 576
Cdd:PRK02224 594 IRTLLAAIAD---AEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEE---AREDKERAEEYLEQVEE 667

                        410       420
                 ....*....|....*....|....*...
gi 296179395 577 EIEKMSSRESALQIKILDLETELRKKNE 604
Cdd:PRK02224 668 KLDELREERDDLQAEIGAVENELEELEE 695
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 193-609 1.59e-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: 41.75  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   193 IHKREAENDKLKEYVKSLETKIAKWNLQSRMNKNEaiVMKEASRQKtvALKKASKVYKQRLDHFTG----AIEKLTSQIR 268
Cdd:pfam12128  236 IMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSD--ETLIASRQE--ERQETSAELNQLLRTLDDqwkeKRDELNGELS 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   269 DQEAKLS---ETISASNAWKSHYEKIVIEKTELEV-QIETMKKQIINLLEDLKKMEDHGKNSCEEILRKVHSIEYENETl 344
Cdd:pfam12128  312 AADAAVAkdrSELEALEDQHGAFLDADIETAAADQeQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNR- 390

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   345 nlENTKLKTTLAALKDEVVSVENELSElqEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKT------- 417
Cdd:pfam12128  391 --DIAGIKDKLAKIREARDRQLAVAED--DLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATpelllql 466

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   418 --KNKNVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQILKQ-------------- 481
Cdd:pfam12128  467 enFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQagtllhflrkeapd 546

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   482 WEEY--SVLAwvdgnHNLLTKLSLEEENCLIQLKCEN----LQQKLEQMD-----AENKELEKKLANQEECLKHSNLKFK 550
Cdd:pfam12128  547 WEQSigKVIS-----PELLHRTDLDPEVWDGSVGGELnlygVKLDLKRIDvpewaASEEELRERLDKAEEALQSAREKQA 621

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296179395   551 EKSAEYTALARQLEAA-LEEGRQKVA-----EEIEKMSSRESALQIKILD-LETELRKKNEEQNQL 609
Cdd:pfam12128  622 AAEEQLVQANGELEKAsREETFARTAlknarLDLRRLFDEKQSEKDKKNKaLAERKDSANERLNSL 687
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
445-609 1.84e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395  445 AAERRLHECQESLQCCKGKCADQEHTIRELQGQILKQWEEYSVLawvdgnHNLLTKLSLEEEncliqlkcENLQQKLEQM 524
Cdd:COG4913   285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL------EAQIRGNGGDRL--------EQLEREIERL 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395  525 DAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSRESALQikilDLETELRKKNE 604
Cdd:COG4913   351 ERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR----DLRRELRELEA 426


                  ....*
gi 296179395  605 EQNQL 609
Cdd:COG4913   427 EIASL 431
PTZ00121 PTZ00121
MAEBL; Provisional
 195-608 2.04e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395  195 KREAENDKLKEYVKSLETKIAKWNLQSRMNKNEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKL 274
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAA 1414

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395  275 SETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGKNS-----CEEILRKVHSIEYENETLN-LEN 348
Cdd:PTZ00121 1415 AAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAeeakkADEAKKKAEEAKKADEAKKkAEE 1494

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395  349 TKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSrceNLLHKNNQITKTKN-KNVEKMRG 427
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA---DELKKAEELKKAEEkKKAEEAKK 1571

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395  428 QMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRE--LQGQILKQWEEysvlawVDGNHNLLTKLSLEE 505
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakIKAEELKKAEE------EKKKVEQLKKKEAEE 1645

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395  506 ENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNlkfKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSRE 585
Cdd:PTZ00121 1646 KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED---EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELK 1722

                         410       420
                  ....*....|....*....|...
gi 296179395  586 SALQIKILDLEtELRKKNEEQNQ 608
Cdd:PTZ00121 1723 KAEEENKIKAE-EAKKEAEEDKK 1744
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 166-452 2.53e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 166 QSEKAntLKANRFSQSVKVV-HERLQIQIHKREAENDKLKEYVKSLETKIAKWNLQSRMNKNEaivmKEASRQKTVALKK 244
Cdd:COG1196  208 QAEKA--ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE----LEELRLELEELEL 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 245 ASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGK 324
Cdd:COG1196  282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 325 NSCEEILRKVHSIEYENETLNlentKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRC 404
Cdd:COG1196  362 EAEEALLEAEAELAEAEEELE----ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 296179395 405 ENLLHKNNQITKTKNKNVEKMRgQMESHLKELERVCDSLTAAERRLHE 452
Cdd:COG1196  438 EEEEEALEEAAEEEAELEEEEE-ALLELLAELLEEAALLEAALAELLE 484
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 297-588 2.61e-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: 2.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   297 ELEVQIETMKKQIINLLEDLKKME---DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQ 373
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIEnrlDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   374 EVEKKQKTLIEMYKTQVQKLQEAAEIVKSRcenLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSLTA----AERR 449
Cdd:TIGR02169  758 SELKELEARIEELEEDLHKLEEALNDLEAR---LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLekeyLEKE 834

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   450 LHECQESLQCCKGKCADQEHTIRELQGQILKQWEEYSVLAwvdgnhnlLTKLSLEEENCLIQLKCENLQQKLEQMDAENK 529
Cdd:TIGR02169  835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE--------AALRDLESRLGDLKKERDELEAQLRELERKIE 906

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296179395   530 ELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQ-----KVAEEIEKMSSRESAL 588
Cdd:TIGR02169  907 ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEelsleDVQAELQRVEEEIRAL 970
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 252-571 3.10e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 3.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 252 RLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEdhgknscEEIL 331
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE-------QDIA 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 332 RKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKN 411
Cdd:COG1196  306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 412 NQITKTKNKNVEKmrgqmESHLKELERvcdSLTAAERRLhecqeslqcckgkcADQEHTIRELQGQILKQweeysvlawv 491
Cdd:COG1196  386 EELLEALRAAAEL-----AAQLEELEE---AEEALLERL--------------ERLEEELEELEEALAEL---------- 433

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 492 dgnhnLLTKLSLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGR 571
Cdd:COG1196  434 -----EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
PRK12704 PRK12704
phosphodiesterase; Provisional
 506-591 4.48e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 4.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 506 ENCLIQlKCENLQQKLEQMDAENKELEKklanQEECLKHSNLKFKEKSAEYTALARQLEAALE--------EGRQKVAEE 577
Cdd:PRK12704  88 EKRLLQ-KEENLDRKLELLEKREEELEK----KEKELEQKQQELEKKEEELEELIEEQLQELErisgltaeEAKEILLEK 162

                         90
                 ....*....|....
gi 296179395 578 IEKMSSRESALQIK 591
Cdd:PRK12704 163 VEEEARHEAAVLIK 176
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
355-605 5.04e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 5.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395  355 LAALKDEVVSVENELSELQEVEKKQKTLIEmyktQVQKLQEAAEIVKSRCENLLhknnqitktKNKNVEKMRGQMESHLK 434
Cdd:COG4913   612 LAALEAELAELEEELAEAEERLEALEAELD----ALQERREALQRLAEYSWDEI---------DVASAEREIAELEAELE 678

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395  435 ELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQIlKQWEE-----YSVLAWVDGNHNLLTKLSLEEEncL 509
Cdd:COG4913   679 RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL-EQAEEeldelQDRLEAAEDLARLELRALLEER--F 755

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395  510 IQLKCENLQQKL-EQMDAENKELEKKLANQEE----CLKHSNLKFKEKSA----------EYTALARQLEA-ALEEGRQK 573
Cdd:COG4913   756 AAALGDAVERELrENLEERIDALRARLNRAEEelerAMRAFNREWPAETAdldadleslpEYLALLDRLEEdGLPEYEER 835

                         250       260       270
                  ....*....|....*....|....*....|..
gi 296179395  574 VAEEIEKMSSREsalqikILDLETELRKKNEE 605
Cdd:COG4913   836 FKELLNENSIEF------VADLLSKLRRAIRE 861
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 418-609 5.21e-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: 40.04  E-value: 5.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   418 KNKNVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQILKQWEEYSVLAwvdgnhNL 497
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE------ER 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   498 LTKLSLEEENCLIQLkcENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAA------LEEGR 571
Cdd:TIGR02168  770 LEEAEEELAEAEAEI--EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATerrledLEEQI 847

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 296179395   572 QKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQL 609
Cdd:TIGR02168  848 EELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
12-578 7.00e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 7.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395  12 EELFCHLKTISEKEDLPRCTSE--SHLSCLKQDILNEKTELEATLKEAELVTHSVELLLPLFKDTIEKINFENANLSALN 89
Cdd:PRK03918 200 KELEEVLREINEISSELPELREelEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395  90 LKISEQKEILIKELDTFKSVKLALEHLLRKRDYKQTGDNLSSML------LENLTDNESENTNLKKKVFEKEAHIQELSC 163
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIngieerIKELEEKEERLEELKKKLKELEKRLEELEE 359

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 164 ---LFQSEKANTLKANRFSQSVKVVH-ERLQIQIHKREAENDKLKEYVKSLETKIAKWNLQSRMNKNEAIVMKEASRQKT 239
Cdd:PRK03918 360 rheLYEEAKAKKEELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCP 439

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 240 VALKKASKVYKQRLdhftgaIEKLTSQIRDQEAKLSETISASNAWKSHYEKI--VIEKTELEVQIETMKKQIINLLEDLK 317
Cdd:PRK03918 440 VCGRELTEEHRKEL------LEEYTAELKRIEKELKEIEEKERKLRKELRELekVLKKESELIKLKELAEQLKELEEKLK 513

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 318 KMEdhgknsCEEILRKvhSIEYEnetlnlentKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEmyktqvqKLQEaa 397
Cdd:PRK03918 514 KYN------LEELEKK--AEEYE---------KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK-------KLDE-- 567

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 398 eiVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDS---LTAAERRLHECQESLQCCKGKCADQEHTIREL 474
Cdd:PRK03918 568 --LEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAekeLEREEKELKKLEEELDKAFEELAETEKRLEEL 645

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395 475 QGQILKQWEEYSVLAWvDGNHNLLTKLSLEEENCLIQLkcENLQQKLEQMDAENKELEKKLANQEECLKHSNL------- 547
Cdd:PRK03918 646 RKELEELEKKYSEEEY-EELREEYLELSRELAGLRAEL--EELEKRREEIKKTLEKLKEELEEREKAKKELEKlekaler 722

                        570       580       590
                 ....*....|....*....|....*....|...
gi 296179395 548 --KFKEKSAEYTALARqlEAALEEgRQKVAEEI 578
Cdd:PRK03918 723 veELREKVKKYKALLK--ERALSK-VGEIASEI 752
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 192-547 7.70e-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: 39.65  E-value: 7.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   192 QIHKREAENDKLKEYVKSLETKIAKWNLQSRMNKNEAIVMKEASRQKTvalkkaskvYKQRLDHFTGAIEKLTSQIRDQE 271
Cdd:TIGR01612  646 QVPEHLKNKDKIYSTIKSELSKIYEDDIDALYNELSSIVKENAIDNTE---------DKAKLDDLKSKIDKEYDKIQNME 716

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   272 aklSETIsasnawKSHYEKIVIEKTELEVQIETMKKQIINLL-EDLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTK 350
Cdd:TIGR01612  717 ---TATV------ELHLSNIENKKNELLDIIVEIKKHIHGEInKDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSK 787

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   351 LKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQME 430
Cdd:TIGR01612  788 ISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSEHE 867

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   431 SHLKELERVCDSLTaaerrlhecQESLQCCKGKCADQEHTIRELQGQILKQWEEYSVLAWVDGNHNLltklsleeencli 510
Cdd:TIGR01612  868 QFAELTNKIKAEIS---------DDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIKI------------- 925

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 296179395   511 qlkCENLQQKLEQMDAENKELEKKLANQEECLKHSNL 547
Cdd:TIGR01612  926 ---CENTKESIEKFHNKQNILKEILNKNIDTIKESNL 959
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 367-609 9.37e-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: 39.28  E-value: 9.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   367 NELSELQEVEKKQKTLIEMYKTQVQKLQeaaeivKSRCENLLHKNNQITKTKNKNVEKMRgQMESHLKELERVCDSLTAA 446
Cdd:TIGR02169  177 EELEEVEENIERLDLIIDEKRQQLERLR------REREKAERYQALLKEKREYEGYELLK-EKEALERQKEAIERQLASL 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   447 ERRLHECQESLQCCKGKCADQEHTIRELQGQILKQWEEYSVlawvdgnhNLLTKL-SLEEENCLIQLKCENLQQKLEQMD 525
Cdd:TIGR02169  250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL--------RVKEKIgELEAEIASLERSIAEKERELEDAE 321

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179395   526 AENKELEKKLANQEECLKhsnlKFKEKSAEYTALARQLEAALEEGRQKVAE---EIEKMSSRESALQIKILDLETELRKK 602
Cdd:TIGR02169  322 ERLAKLEAEIDKLLAEIE----ELEREIEEERKRRDKLTEEYAELKEELEDlraELEEVDKEFAETRDELKDYREKLEKL 397


                   ....*..
gi 296179395   603 NEEQNQL 609
Cdd:TIGR02169  398 KREINEL 404
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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