|
Name |
Accession |
Description |
Interval |
E-value |
| Hamartin |
pfam04388 |
Hamartin protein; This family includes the hamartin protein which is thought to function as a ... |
7-714 |
0e+00 |
|
Hamartin protein; This family includes the hamartin protein which is thought to function as a tumour suppressor. The hamartin protein interacts with the tuberin protein pfam03542. Tuberous sclerosis complex (TSC) is an autosomal dominant disorder and is characterized by the presence of hamartomas in many organs, such as brain, skin, heart, lung, and kidney. It is caused by mutation either TSC1 or TSC2 tumour suppressor gene. TSC1 encodes a protein, hamartin, containing two coiled-coil regions, which have been shown to mediate binding to tuberin. The TSC2 gene codes for tuberin pfam03542. These two proteins function within the same pathway(s) regulating cell cycle, cell growth, adhesion, and vesicular trafficking.
Pssm-ID: 461287 [Multi-domain] Cd Length: 730 Bit Score: 966.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 7 IGELLSMLDSSTLGVRDDVTTIFKESLNSERGPMLVNTLVDYYLETNSQPVLHILTTLQEPHDKHLLDKMNEYVGKAATR 86
Cdd:pfam04388 1 VGELFNLLESNDLGELEEIKKVFHEHLNSTKGSWLVNGLVDYYLSTGSQRALEILVSVREPHDKHLFDKLNECLKKAATR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 87 LSILSLLGHVVRLQPSWKHKLSQAPLLPSLLKCLKMDTDVVVLTTGVLVLITMLPMIPQSGKQHLLDFFDIFGRLSSWCL 166
Cdd:pfam04388 81 LQALTLLGHVVRRQPTWLHKIANHPLLKSLLKCLKTETDIVVLMTGLLVLITLLPMIPQLVKQYLPDIFEIFGRLASWNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 167 KKPGHVTEVYLVHLHASVYALFHRLYGMYPCNFVSFLRSHYSMKENVETFEEVVKPMMEHVRIHPELVTGSKDHELDPRR 246
Cdd:pfam04388 161 KNPGHVPEVYLVHLQASLYSLFHRLYGMYPCNFVSYLRSHYSMKENLETFEETIKPMLEHVRIHPELVTGTKDHELDPTR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 247 WKTLETHDVVIECAKISLDPTEASYEDGDAVShqlsacfphrSADVTTSSYVDTQNSYGGATSTPSSTSRLMLFSTPGQL 326
Cdd:pfam04388 241 WKKMEPHDVVIECAKFSLDPKEASCEEGYSSS----------AADPTASPYTDQQSSYGSSTSTPSSTPRLQLSSSSGTS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 327 PQSLSSLSTRPLPEPLqaSLWSPSAVCGMTTPPTSPGNVPA-------DLSHPYSKAFGTTTGGKGTPSG---TPATSPP 396
Cdd:pfam04388 311 PPYLSPPSIRLKTDSF--PLWSPSSVCGMTTPPTSPGMVPTtpselspSSSHLSSRGSSPPEAAGEATPEttpAKDSPYL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 397 PAPPCPQDDCAHG--PASQASATPPRKEERADSSRPYLPRQQDV-PSDRGLEDLPGSKGSVTLRNLPDFLGDLA-SEEDS 472
Cdd:pfam04388 389 KQPPPLSDSHVHRalPASSQPSSPPRKDGRSQSSFPPLSKQAPTnPNSRGLLEPPGDKSSVTLSELPDFIKDLAlSSEDS 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 473 IEKDKEEAAISKELSEITTAEADPVAPRGGFDSPFYR--DSLSGSQRK--------THSAASGTQGFSVNPE-----PLH 537
Cdd:pfam04388 469 VEGAEEEAAISQELSEITTEKNETDCSRGGLDMPFSRtmESLAGSQRSrnriasycSSTSQSDSHGPATTPEskpsaLAE 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 538 SSLDKHGPDTPKQAFTPIDPPSGSADASPAGDRDRQTSLETSILTPSPCKIPPQRGVSFGSGQLPPYDHLFEVALPKTAC 617
Cdd:pfam04388 549 DGLRRTKSCSFKQSFTPIEQPIESSDDCPTDEQDGENGLETSILTPSPCKIPSRQKVSTQSGQPLPYEHLFDLALPKTAS 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 618 HFVSKKTEELLKKAKGNPEEDCVPSTSPMEVLDRLLEQGAGAHSKELSRLSLPSKSVDWTHFG-----DEIRTLRDQLLL 692
Cdd:pfam04388 629 LFVGRKTAELLKKAKGNSEEDCVSSTSPLEVLDRYIQQGIDAHSKELKRLPLPSKSADWTHFGgsapsDELTTLRDQLLL 708
|
730 740
....*....|....*....|..
gi 564340089 693 LHNQLLYERFKRQQHALRNRRL 714
Cdd:pfam04388 709 LHNQLLYERYKREQHAERNRRL 730
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
700-970 |
2.43e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 700 ERFKRQQHALRNrrlLRKVIRAAALEEHNAAMkDQLKLQEKDIQMWKVSLQKEQARY-SQLQQQRDTMvTQLHSQIRQLQ 778
Cdd:TIGR02168 213 ERYKELKAELRE---LELALLVLRLEELREEL-EELQEELKEAEEELEELTAELQELeEKLEELRLEV-SELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 779 HdreEFYNQSQELQT----------KLEDCRSMIAELRVELKKANSKVCHTELLLSQVSQKLS----NSESVQQQMEFLN 844
Cdd:TIGR02168 288 K---ELYALANEISRleqqkqilreRLANLERQLEELEAQLEELESKLDELAEELAELEEKLEelkeELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 845 RQLLVLGEVNELY---LEQLQSKHPDTTKEVEmmktAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKD-HLLLE 920
Cdd:TIGR02168 365 AELEELESRLEELeeqLETLRSKVAQLELQIA----SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQA 440
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 564340089 921 QKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRL-EKDGRL 970
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELaQLQARL 491
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
761-964 |
2.76e-09 |
|
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: 58.78 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 761 QQRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRSMIAELRVELKKANSKVCHTELLLSQVSQKLSNSESvqqqm 840
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 841 eflNRQllvlgevnelyLEQLQskhpdttKEVEMMKTAyRKELEKnrsHLLQQNQRLDASQRRVLELESLLAKKDHLLLE 920
Cdd:COG1579 88 ---NKE-----------YEALQ-------KEIESLKRR-ISDLED---EILELMERIEELEEELAELEAELAELEAELEE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 564340089 921 QKKYLEdvksQASGQLLAAESRYEAQR-KITRVLELEILDLYGRL 964
Cdd:COG1579 143 KKAELD----EELAELEAELEELEAEReELAAKIPPELLALYERI 183
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
703-983 |
5.18e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 5.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 703 KRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQQQRDtmvtQLHSQIRQLQHDRE 782
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA----RLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 783 EFYNQSQELQTKLEDCRSMIAELRVELKKANSKVCHTELLLSQVSQKLSNSESVQQQMEflnRQLLvlgEVNELYLEQLQ 862
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE---EELE---ELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 863 SKhpdttkevemmkTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESR 942
Cdd:COG1196 394 AA------------AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 564340089 943 YEAQRKITRVLELEILDLYGRLEKDGRLQKLEEDRAEAAEA 983
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
700-956 |
7.59e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 7.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 700 ERFKRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQQQRDtmvtQLHSQIRQLQH 779
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE----ELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 780 DREEFYNQSQELQTKLEDCRSMIAELRVELKKanskvchtelLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLE 859
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEE----------LEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 860 QLQskhpDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAA 939
Cdd:COG1196 359 ELA----EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250
....*....|....*..
gi 564340089 940 ESRYEAQRKITRVLELE 956
Cdd:COG1196 435 EEEEEEEEALEEAAEEE 451
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
710-957 |
6.45e-08 |
|
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: 56.95 E-value: 6.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 710 RNRRLLRKVIRaaaLEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQQQRDTMVTQLHSQIRQL-QHDR--EEFYN 786
Cdd:TIGR04523 212 KNKSLESQISE---LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELeQNNKkiKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 787 QSQELQTKLEDCRS-----MIAELRVELKKANSKVCHTELLLSQVSQKLS--------------NSES----VQQQMEFL 843
Cdd:TIGR04523 289 QLNQLKSEISDLNNqkeqdWNKELKSELKNQEKKLEEIQNQISQNNKIISqlneqisqlkkeltNSESenseKQRELEEK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 844 NRQLLVLGEVNELYLEQLQSkhpdttkeVEMMKTAYRKELEKNRshllQQNQRLDaSQRRVLELESLLAKKDHLLL---- 919
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKN--------LESQINDLESKIQNQE----KLNQQKD-EQIKKLQQEKELLEKEIERLketi 435
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 564340089 920 -EQKKYLEDVKSQASGQLLAAES---RYEAQRKITRVLELEI 957
Cdd:TIGR04523 436 iKNNSEIKDLTNQDSVKELIIKNldnTRESLETQLKVLSRSI 477
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
708-966 |
1.43e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.91 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 708 ALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQQQrdtmVTQLHSQIRQLQHDREEFYNQ 787
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE----LEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 788 SQELQTKLEDCRSMIAELRVE---LKKANSKVCHT-ELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQlqs 863
Cdd:COG4372 103 LESLQEEAEELQEELEELQKErqdLEQQRKQLEAQiAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA--- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 864 khpDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLA-KKDHLLLEQKKYLEDVKSQASGQLLAAESR 942
Cdd:COG4372 180 ---EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDsLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260
....*....|....*....|....
gi 564340089 943 YEAQRKITRVLELEILDLYGRLEK 966
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEI 280
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
747-966 |
1.56e-07 |
|
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: 55.16 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 747 VSLQKEQARYSQLQQQRDtmvtQLHSQIRQLQHDREEFYNQSQELQTKLEDCRSMIAELRVELKKANSKVCHTELLLSQV 826
Cdd:COG4942 13 LAAAAQADAAAEAEAELE----QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 827 SQKLSNSE-SVQQQMEFLNRQLLVL---GEVNELYLEQLQSKHPDTTKEVEMMK--TAYRKE----LEKNRSHLLQQNQR 896
Cdd:COG4942 89 EKEIAELRaELEAQKEELAELLRALyrlGRQPPLALLLSPEDFLDAVRRLQYLKylAPARREqaeeLRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 897 LDASQRrvlELESLLAKkdhlLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEK 966
Cdd:COG4942 169 LEAERA---ELEALLAE----LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
737-966 |
2.56e-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: 55.06 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 737 LQEKDIQMWKVSLQKEQA-RYSQLQQQRDTM--------VTQLHSQIRQL-------QHDREEFYNQSQELQTKLEDCRS 800
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAeRYKELKAELRELelallvlrLEELREELEELqeelkeaEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 801 MIAELRVELKKANSKVchtELLLSQVSQKLSNSESVQQQMEFLNRQLLVLgevnELYLEQLQSKHPDTTKEVEMMKTAYr 880
Cdd:TIGR02168 275 EVSELEEEIEELQKEL---YALANEISRLEQQKQILRERLANLERQLEEL----EAQLEELESKLDELAEELAELEEKL- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 881 KELEKNrshLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQ---ASGQLLAAESRYEA-QRKITRVLElE 956
Cdd:TIGR02168 347 EELKEE---LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiasLNNEIERLEARLERlEDRRERLQQ-E 422
|
250
....*....|
gi 564340089 957 ILDLYGRLEK 966
Cdd:TIGR02168 423 IEELLKKLEE 432
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
734-982 |
4.61e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 734 QLKLQEKDIQMWKVSLQKEQARYSQLQQQrdtmvtqlhsqIRQLQHDREEFYNQSQELQTKLEDCRSMIAELRVELKKAN 813
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAE-----------LEELEAELEELEAELAELEAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 814 SKVchtELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELyLEQLQSKHPDTTKEVEMMKTAYRKELEKNRSHLLQQ 893
Cdd:COG1196 288 AEE---YELLAELARLEQDIARLEERRRELEERLEELEEELAE-LEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 894 NQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEKDGRLQKL 973
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
....*....
gi 564340089 974 EEDRAEAAE 982
Cdd:COG1196 444 LEEAAEEEA 452
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
739-948 |
5.19e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 739 EKDIQMWKVSLQKEQARYSQLQQQRDTM---VTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRSMIAELRVELKKANSK 815
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALqaeLEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 816 VCHTELLLSQVSQkLSNSESVQqqmEFLNRQllvlgevneLYLEQLQSKHPDTTKEVEmmktAYRKELEKNRSHLLQQNQ 895
Cdd:COG3883 95 LYRSGGSVSYLDV-LLGSESFS---DFLDRL---------SALSKIADADADLLEELK----ADKAELEAKKAELEAKLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564340089 896 RLDASQRrvlELESLLAKKDHLLLEQKKYLEDVKSQASgQLLAAESRYEAQRK 948
Cdd:COG3883 158 ELEALKA---ELEAAKAELEAQQAEQEALLAQLSAEEA-AAEAQLAELEAELA 206
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
749-956 |
1.65e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.83 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 749 LQKEQARYSQLQQQRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRSMIAELRVELKKANSKVCHTELLLSQVSQ 828
Cdd:COG4372 8 VGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 829 KLSNSESVQQQMEflnrqllvlgevNElyLEQLQSKHPDTTKEVEMMKTAyRKELEKNRSHLLQQNQRLDAS----QRRV 904
Cdd:COG4372 88 QLQAAQAELAQAQ------------EE--LESLQEEAEELQEELEELQKE-RQDLEQQRKQLEAQIAELQSEiaerEEEL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564340089 905 LELESLLAKKDHLLLEQKKYLEDVKSQASGQLLaAESRYEAQRKITRVLELE 956
Cdd:COG4372 153 KELEEQLESLQEELAALEQELQALSEAEAEQAL-DELLKEANRNAEKEEELA 203
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
742-967 |
1.84e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 742 IQMWKVSLQKEQARYSQLQQqrdtmvtqlhsQIRQLQHDREEFYNQSQELQTKLEDCRSMIAELRVELKKANSKVCHTEL 821
Cdd:COG4372 26 IAALSEQLRKALFELDKLQE-----------ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 822 LLSQVSQKLsnsESVQQQMEFLNRQLLVL-GEVNELY--LEQLQSKHPDTTKEVEmMKTAYRKELEKNRSHLLQQNQRLD 898
Cdd:COG4372 95 ELAQAQEEL---ESLQEEAEELQEELEELqKERQDLEqqRKQLEAQIAELQSEIA-EREEELKELEEQLESLQEELAALE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564340089 899 ASQRRvLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEKD 967
Cdd:COG4372 171 QELQA-LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAL 238
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
711-862 |
1.98e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 711 NRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVS--LQKEQARYSQLQQQRDTMVTQL---HSQIRQLQHDREEFY 785
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYtpnHPDVIALRAQIAALR 304
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564340089 786 NQ-SQELQTKLEDCRSMIAELRVELKKANSKvchtellLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQ 862
Cdd:COG3206 305 AQlQQEAQRILASLEAELEALQAREASLQAQ-------LAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
720-971 |
2.31e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 720 RAAALEEHNAAMKDQLKLQEKDIQMWKvSLQKEQARYSQLQQQRDTMVTQLHSQIRQLQHDRE---EFYNQSQELQTKLE 796
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKREraeELRERAAELEAEAE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 797 DCRSMIAELRVELKKANSKV--CHTELL--------LSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQSKHp 866
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVaeLNSKLAelkeriesLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR- 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 867 DTTKEVEmmktayrKELEKNRSHLLQQN-QRLDASQRRVLE-LESLLAKKDHLL---------LEQKKYLEDVKSQASGQ 935
Cdd:PRK02224 634 ERKRELE-------AEFDEARIEEAREDkERAEEYLEQVEEkLDELREERDDLQaeigaveneLEELEELRERREALENR 706
|
250 260 270
....*....|....*....|....*....|....*.
gi 564340089 936 LLAAESRYEaqrkitRVLELEilDLYGRLEKDGRLQ 971
Cdd:PRK02224 707 VEALEALYD------EAEELE--SMYGDLRAELRQR 734
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
714-954 |
3.65e-06 |
|
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: 51.26 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 714 LLRKVIRAAALEEH-NAAMKDQLKL-QEKDIQMWKvsLQKEQARYSQLQQQRDTMVTQLHSQIRQLQHDREEFYNQ---- 787
Cdd:pfam05483 305 LQRSMSTQKALEEDlQIATKTICQLtEEKEAQMEE--LNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQlkii 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 788 SQELQTK---LEDCRSMIAELRVELKKANSKVCHTELLLSQVSQklsnSESVQQQMEFLNRQLLVLGEVNELYLEQLQSK 864
Cdd:pfam05483 383 TMELQKKsseLEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQ----FEKIAEELKGKEQELIFLLQAREKEIHDLEIQ 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 865 HPDTT-------KEVEMMKTayrkELEKNRshlLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDV---KSQASG 934
Cdd:pfam05483 459 LTAIKtseehylKEVEDLKT----ELEKEK---LKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIincKKQEER 531
|
250 260
....*....|....*....|
gi 564340089 935 QLLAAESRYEAQRKITRVLE 954
Cdd:pfam05483 532 MLKQIENLEEKEMNLRDELE 551
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
743-958 |
8.57e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 8.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 743 QMWKVSLQKEQARYSQLQQQRDTM-VTQLHSQIRQLQHDREEfYNQSQELQTKLEDCRSMIAELRVELKKANSKVCHTEL 821
Cdd:COG4717 45 AMLLERLEKEADELFKPQGRKPELnLKELKELEEELKEAEEK-EEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 822 LLSQVSQklsnsesvQQQMEFLNRQLLVLGEVnelyLEQLQSKHpDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQ 901
Cdd:COG4717 124 LLQLLPL--------YQELEALEAELAELPER----LEELEERL-EELRELEEELEELEAELAELQEELEELLEQLSLAT 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564340089 902 RRVL-----ELESLLAKKDHLLLEQKKyLEDVKSQASGQLLAAESRYEAQRKITRVLELEIL 958
Cdd:COG4717 191 EEELqdlaeELEELQQRLAELEEELEE-AQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
704-899 |
9.94e-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: 50.06 E-value: 9.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 704 RQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQQQRDTM---VTQLHSQIRQLQHD 780
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLrseLEELSEELRELESK 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 781 REEFYNQSQELQTKLEDCRSMIAELRVEL----KKANSKVCHT-ELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNE 855
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRIdnlqERLSEEYSLTlEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNL 989
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 564340089 856 LYLEQLQSKhpdttKEVEMMKTAYRKELEKNRSHLLQQNQRLDA 899
Cdd:TIGR02168 990 AAIEEYEEL-----KERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
703-957 |
1.06e-05 |
|
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: 49.97 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 703 KRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQQQrdtmvtqlhsqiRQLQHDRE 782
Cdd:TIGR00618 189 KKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQK------------REAQEEQL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 783 EFYNQSQELQTKLEDCRSMIAELRvELKKANSKVCHTELL------LSQVSQKLSNS-----------ESVQQQMEFLNR 845
Cdd:TIGR00618 257 KKQQLLKQLRARIEELRAQEAVLE-ETQERINRARKAAPLaahikaVTQIEQQAQRIhtelqskmrsrAKLLMKRAAHVK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 846 QLLVLGEVNELyLEQLQSKHPDTTKEVEmMKTAYRKELEKN---RSHLLQQNQRLDASQRRvleLESLLAKKDHLLLEQK 922
Cdd:TIGR00618 336 QQSSIEEQRRL-LQTLHSQEIHIRDAHE-VATSIREISCQQhtlTQHIHTLQQQKTTLTQK---LQSLCKELDILQREQA 410
|
250 260 270
....*....|....*....|....*....|....*..
gi 564340089 923 KYLEDVKSQAS--GQLLAAESRYEAQRKITRVLELEI 957
Cdd:TIGR00618 411 TIDTRTSAFRDlqGQLAHAKKQQELQQRYAELCAAAI 447
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
723-966 |
1.16e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 723 ALEEHNAAMKD---QLKLQEKDIQMwkvsLQKEQARYSQLQqqrdtmvTQLHSQIRQLQHDREEFYNQSQELQTKLEDCR 799
Cdd:TIGR02169 703 RLDELSQELSDasrKIGEIEKEIEQ----LEQEEEKLKERL-------EELEEDLSSLEQEIENVKSELKELEARIEELE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 800 SMIAELRVELKK-----ANSKVCHTELLLSQVSQKLSNSESVQQQME-FLNRQLLVLG----EVNEL--YLEQLQSKHPD 867
Cdd:TIGR02169 772 EDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIEARLREIEqKLNRLTLEKEylekEIQELqeQRIDLKEQIKS 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 868 TTKEVEMMKTAYRK-------------ELEKNRSHLLQQNQRLDAS----QRRVLELESLLAKKDHLLLEQKKYLEDVKS 930
Cdd:TIGR02169 852 IEKEIENLNGKKEEleeeleeleaalrDLESRLGDLKKERDELEAQlrelERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
250 260 270
....*....|....*....|....*....|....*...
gi 564340089 931 QAS--GQLLAAESRYEAQRKITRVLELEILDLYGRLEK 966
Cdd:TIGR02169 932 ELSeiEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRA 969
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
767-966 |
1.30e-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: 49.67 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 767 VTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRSM-------IAELRVELKKANSKVchtELLLSQVSQKLSNSESVQQQ 839
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKEleelsrqISALRKDLARLEAEV---EQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 840 MEFLNRQL------LVLGEVNELYLEQLQSKHPDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRV--------- 904
Cdd:TIGR02168 763 IEELEERLeeaeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIaaterrled 842
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564340089 905 ---------LELESLLAKKDHL------LLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEK 966
Cdd:TIGR02168 843 leeqieelsEDIESLAAEIEELeelieeLESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
725-929 |
2.83e-05 |
|
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: 48.43 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 725 EEHNAAMKDQLKLQEKDIQMWKvsLQKEQARYSQLQ------QQRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDC 798
Cdd:TIGR00618 660 VREHALSIRVLPKELLASRQLA--LQKMQSEKEQLTywkemlAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 799 RSMIAELRVELKK-ANSKVCHTELLLSQVS-------QKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQSKHPDTTK 870
Cdd:TIGR00618 738 EDALNQSLKELMHqARTVLKARTEAHFNNNeevtaalQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDED 817
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564340089 871 EVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVK 929
Cdd:TIGR00618 818 ILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSD 876
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
681-960 |
5.26e-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: 47.74 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 681 DEIRTLRDQLLLLHNQLLYERFKRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDiqmwkvsLQKEQArysQLQ 760
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE-------AEAEIE---ELE 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 761 QQRDTMVTQLHSQIRQLQHDREEFYNQS---QELQTKLEDCRSMIAELRVELKKANSKVCHTELLLSQVSQKLsnsESVQ 837
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNeeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI---EELE 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 838 QQMEFLNRQL---LVLGEVNELYLEQLQSKHPDTTKEVEMM---KTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLL 911
Cdd:TIGR02168 866 ELIEELESELealLNERASLEEALALLRSELEELSEELRELeskRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 564340089 912 AKKDHLLLE--QKKYLEDVKSQAsgqllaaesryEAQRKITRvLELEILDL 960
Cdd:TIGR02168 946 SEEYSLTLEeaEALENKIEDDEE-----------EARRRLKR-LENKIKEL 984
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
700-903 |
6.66e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.36 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 700 ERFKRQQHALRNRRLLRKVIRAAALEEHN--AAMKDQLKLQEKDIQMWKVSLQ-KEQARYSQLQQQRDTMVTQLHSQIRQ 776
Cdd:PRK10929 65 ERAKQYQQVIDNFPKLSAELRQQLNNERDepRSVPPNMSTDALEQEILQVSSQlLEKSRQAQQEQDRAREISDSLSQLPQ 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 777 LQHD-REEFYNQSQELQ------TKLEDCRSMIAELRVELKKAnsKVchTELLLSQVS----QKLS--NSESVQQQMEFL 843
Cdd:PRK10929 145 QQTEaRRQLNEIERRLQtlgtpnTPLAQAQLTALQAESAALKA--LV--DELELAQLSannrQELArlRSELAKKRSQQL 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564340089 844 NRQLLVLGevNELYlEQLQSKHPDTTKEVEMMK-------TAYRKELEKNR--SHLL-QQNQRLD--ASQRR 903
Cdd:PRK10929 221 DAYLQALR--NQLN-SQRQREAERALESTELLAeqsgdlpKSIVAQFKINRelSQALnQQAQRMDliASQQR 289
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
719-957 |
8.68e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.07 E-value: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 719 IRAAALEEHNAaMKDQLKLQEKDI-QMWKV----SLQKEQARYSQLQQQRDTMVTQLHSQIRQLQHDREEFYNQS----- 788
Cdd:pfam13868 23 ERDAQIAEKKR-IKAEEKEEERRLdEMMEEererALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKlqere 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 789 --QELQTKLEDCRSMIAELRVELKKANSKvchtELLLSQVsQKLSNSESVQQQMEFLNRQLLvlgevneLYLEQLQSKhp 866
Cdd:pfam13868 102 qmDEIVERIQEEDQAEAEEKLEKQRQLRE----EIDEFNE-EQAEWKELEKEEEREEDERIL-------EYLKEKAER-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 867 DTTKEVEMMKTAYRKELEKNRshLLQQNQRLDASQRrvlELESLLAKkdhLLLEQ------KKYLEDVKSQASGQLLAAE 940
Cdd:pfam13868 168 EEEREAEREEIEEEKEREIAR--LRAQQEKAQDEKA---ERDELRAK---LYQEEqerkerQKEREEAEKKARQRQELQQ 239
|
250
....*....|....*..
gi 564340089 941 SRYEAQRKITRVLELEI 957
Cdd:pfam13868 240 AREEQIELKERRLAEEA 256
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
699-952 |
1.79e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 699 YERF-KRQQHALRNRRLL-----RKViraAALEEhnaamkdQLKLQEKDIQMWKVSLQKEQARYSQLQQQRDT------- 765
Cdd:COG4913 587 GTRHeKDDRRRIRSRYVLgfdnrAKL---AALEA-------ELAELEEELAEAEERLEALEAELDALQERREAlqrlaey 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 766 -----MVTQLHSQIRQLQHDREEF---YNQSQELQTKLEDCRSMIAELRVELKKANSKVCHTELLLSQVSQKLSNSESVQ 837
Cdd:COG4913 657 swdeiDVASAEREIAELEAELERLdasSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 838 QQMEFLNRQLLVLgEVNELYLEQLQSKHPDTtkevemMKTAYRKELEKNRSHLLQQNQRL------------------DA 899
Cdd:COG4913 737 EAAEDLARLELRA-LLEERFAAALGDAVERE------LRENLEERIDALRARLNRAEEELeramrafnrewpaetadlDA 809
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 900 SQRRVLELESLLAK-KDHLLLEQKKYLEDVKSQASGQLLA------AESRYEAQRKITRV 952
Cdd:COG4913 810 DLESLPEYLALLDRlEEDGLPEYEERFKELLNENSIEFVAdllsklRRAIREIKERIDPL 869
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
709-957 |
2.02e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 709 LRNRRLLRKVIRAAALEEHN-----------AAMKDQLKLQ-EKDIQMWKVSLQ---KEQAR---------YSQLQQQR- 763
Cdd:COG3206 90 LKSRPVLERVVDKLNLDEDPlgeeasreaaiERLRKNLTVEpVKGSNVIEISYTspdPELAAavanalaeaYLEQNLELr 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 764 -----------DTMVTQLHSQIRQLQHDREEF---------YNQSQELQTKLEDCRSMIAELRVELKKANSKVCHTELLL 823
Cdd:COG3206 170 reearkaleflEEQLPELRKELEEAEAALEEFrqknglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 824 SQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELyLEQLQSKHPDttkevemMKTAyRKELEKNRSHLLQQNQRLDASQRR 903
Cdd:COG3206 250 GSGPDALPELLQSPVIQQLRAQLAELEAELAEL-SARYTPNHPD-------VIAL-RAQIAALRAQLQQEAQRILASLEA 320
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564340089 904 vlELESLLAKKDHLLLEQKKYLEDVKS--QASGQLLAAESRYEAQRKI-----TRVLELEI 957
Cdd:COG3206 321 --ELEALQAREASLQAQLAQLEARLAElpELEAELRRLEREVEVARELyesllQRLEEARL 379
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
700-954 |
2.67e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 700 ERFKRQQHALRNR-RLLRKVIRAAALEEHNAAMK----------DQLKLQEKDIQMWKVSLQKEQARYSQLQQQRDTMVT 768
Cdd:COG4717 105 EELEAELEELREElEKLEKLLQLLPLYQELEALEaelaelperlEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 769 QL----HSQIRQLQHDREEFYNQSQELQTKLEDCRSMIAELRVELKKANSKVCHTEL----------------LLSQVSQ 828
Cdd:COG4717 185 QLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALeerlkearlllliaaaLLALLGL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 829 KLSNSESVQQQMEFLnrqLLVLGEVNELYLEQLQSKHPDTTKEVEMMKTAYRKELEK----------------NRSHLLQ 892
Cdd:COG4717 265 GGSLLSLILTIAGVL---FLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEeeleellaalglppdlSPEELLE 341
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564340089 893 QNQRLDASQRRVLELESLL--AKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLE 954
Cdd:COG4717 342 LLDRIEELQELLREAEELEeeLQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELE 405
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
720-982 |
3.79e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 720 RAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQQQRDTmvtqLHSQIRQLQHDREEFYNQSQELQTKLEDCR 799
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE----LRERFGDAPVDLGNAEDFLEELREERDELR 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 800 SMIAELRVELKKANSKVCHTELLLS-----QVSQKLSNSESV------QQQMEFLnrqllvlgevnELYLEQLQSKHPDT 868
Cdd:PRK02224 426 EREAELEATLRTARERVEEAEALLEagkcpECGQPVEGSPHVetieedRERVEEL-----------EAELEDLEEEVEEV 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 869 TKEVEMMKTAyrKELEKNRSHLLQqnqRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAA---ESRYEA 945
Cdd:PRK02224 495 EERLERAEDL--VEAEDRIERLEE---RREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAaeaEEEAEE 569
|
250 260 270
....*....|....*....|....*....|....*..
gi 564340089 946 QRKITRVLELEILDLYGRLEKDGRLQKLEEDRAEAAE 982
Cdd:PRK02224 570 AREEVAELNSKLAELKERIESLERIRTLLAAIADAED 606
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
699-891 |
3.85e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 699 YERFKRQQHALRNRRllrkviraAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARySQLQqqrdtmvtQLHSQIRQLQ 778
Cdd:COG4717 90 YAELQEELEELEEEL--------EELEAELEELREELEKLEKLLQLLPLYQELEALE-AELA--------ELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 779 HDREEFynqsQELQTKLEDCRSMIAELRVELKKANSKVchTELLLSQVSQKLSNSESVQQQMEFLNRQLlvlgEVNELYL 858
Cdd:COG4717 153 ERLEEL----RELEEELEELEAELAELQEELEELLEQL--SLATEEELQDLAEELEELQQRLAELEEEL----EEAQEEL 222
|
170 180 190
....*....|....*....|....*....|...
gi 564340089 859 EQLQSKHPDTtkEVEMMKTAYRKELEKNRSHLL 891
Cdd:COG4717 223 EELEEELEQL--ENELEAAALEERLKEARLLLL 253
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
729-920 |
3.95e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 729 AAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQQQrdtmVTQLHSQIRQLQhdreefynQSQELQTKLedcrsmiaeLRVE 808
Cdd:PRK11637 71 ASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQ----IDELNASIAKLE--------QQQAAQERL---------LAAQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 809 LKKANSKVCHT--ELLLS-QVSQKlsnSESVQQQMEFLNrqllvlgEVNELYLEQLQSkhpdTTKEVemmkTAYRKELEK 885
Cdd:PRK11637 130 LDAAFRQGEHTglQLILSgEESQR---GERILAYFGYLN-------QARQETIAELKQ----TREEL----AAQKAELEE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564340089 886 NRSH---LL----QQNQRLD----ASQRRVLELESLLAKKDHLLLE 920
Cdd:PRK11637 192 KQSQqktLLyeqqAQQQKLEqarnERKKTLTGLESSLQKDQQQLSE 237
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
722-863 |
4.53e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 41.47 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 722 AALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQQQRDTMVtQLHSQ-IRQLQHDREEFynqsQELQTKledcrs 800
Cdd:pfam07926 4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYEREL-VLHAEdIKALQALREEL----NELKAE------ 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564340089 801 mIAELRVELKKANSkvchtELLLSQVS---QKlsnsESVQQQMEFLNRQLLVLGEVNELYLEQLQS 863
Cdd:pfam07926 73 -IAELKAEAESAKA-----ELEESEESweeQK----KELEKELSELEKRIEDLNEQNKLLHDQLES 128
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
679-956 |
4.61e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 679 FGDEIRTLRDQLLLLHNQLLY------------ERFKRQQHALRNRRL-LRKVI-------------------RAAALEE 726
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDllaeaglddadaEAVEARREELEDRDEeLRDRLeecrvaaqahneeaeslreDADDLEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 727 HNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQQQRDTmvtqLHSQIRQLQHDREEFYNQSQELQTKLEDCRSMIAELR 806
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE----LRERFGDAPVDLGNAEDFLEELREERDELREREAELE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 807 VELKKANSKVCHTELLLS-----QVSQKLSNSESV------QQQMEFLnrqllvlgevnELYLEQLQSKHPDTTKEVEMM 875
Cdd:PRK02224 433 ATLRTARERVEEAEALLEagkcpECGQPVEGSPHVetieedRERVEEL-----------EAELEDLEEEVEEVEERLERA 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 876 KTAyrKELEKNRSHLLqqnQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAA-ESRYEAQRKITRVLE 954
Cdd:PRK02224 502 EDL--VEAEDRIERLE---ERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAaEAEEEAEEAREEVAE 576
|
..
gi 564340089 955 LE 956
Cdd:PRK02224 577 LN 578
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
786-967 |
4.89e-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: 43.98 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 786 NQSQELQTKLEDCRSMIAELRVELKKANSKVCHTELLLSQVSQKLSNSE----SVQQQMEFLNRQLlvlgEVNELYLEQL 861
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALArrirALEQELAALEAEL----AELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 862 QSKHPDTTKEV-EMMKTAYRKELEKNRSHLLQQNQRLDASqrRVLELESLLAKKDHLLLEQ----KKYLEDVKSQASGQ- 935
Cdd:COG4942 96 RAELEAQKEELaELLRALYRLGRQPPLALLLSPEDFLDAV--RRLQYLKYLAPARREQAEElradLAELAALRAELEAEr 173
|
170 180 190
....*....|....*....|....*....|....
gi 564340089 936 --LLAAESRYEAQRKITRVLELEILDLYGRLEKD 967
Cdd:COG4942 174 aeLEALLAELEEERAALEALKAERQKLLARLEKE 207
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
752-930 |
5.06e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.91 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 752 EQARYSQLQQQR---------------DTMVTQLHS-----QIRQLQHD-------REEFYNQSQ-ELQTKLEDCRSMIA 803
Cdd:pfam05622 242 EELRCAQLQQAElsqadallspssdpgDNLAAEIMPaeireKLIRLQHEnkmlrlgQEGSYRERLtELQQLLEDANRRKN 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 804 ELRVELKKANSKVchTELllsqvsqklsnsesvQQQMEFLNRQLLVLGEVNE--LYLEQLQSKHPDTTKEVEmmktayrK 881
Cdd:pfam05622 322 ELETQNRLANQRI--LEL---------------QQQVEELQKALQEQGSKAEdsSLLKQKLEEHLEKLHEAQ-------S 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 564340089 882 ELEKNRSHLLQQNQRLDAS-QRRVLELESLLAKKDH--LLLEQ--KKYLEDVKS 930
Cdd:pfam05622 378 ELQKKKEQIEELEPKQDSNlAQKIDELQEALRKKDEdmKAMEEryKKYVEKAKS 431
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
721-816 |
6.91e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 41.03 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 721 AAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSqlQQQRDTMVTQLHSQIRQLQHDREEFynqSQELQTKLEDcrs 800
Cdd:smart00935 20 QKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQEFQRKQQKL---QQDLQKRQQE--- 91
|
90
....*....|....*.
gi 564340089 801 MIAELRVELKKANSKV 816
Cdd:smart00935 92 ELQKILDKINKAIKEV 107
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
306-593 |
9.76e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.62 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 306 GATSTPSSTSRlmlfSTPGQLPQSLSSLSTRP--LPEPLQASLWSPSAVCGMTT-PPTSPGNVPADLSHPYSKAFGTTTG 382
Cdd:PHA03307 104 GSPTPPGPSSP----DPPPPTPPPASPPPSPApdLSEMLRPVGSPGPPPAASPPaAGASPAAVASDAASSRQAALPLSSP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 383 gkgtpsgtpatspppappcpqDDCAHGPASQASATPPRKEERADSSRPYLPRQQDVPSDRGLEDLPGSKGSVTLRNLPDf 462
Cdd:PHA03307 180 ---------------------EETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSS- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 463 lgDLASEEDSIEKDKEEaaiskelseitTAEADPVAPRGGFDSPFYRDSLSGSQRKTH---SAASGTQGFSVNPEPLHSS 539
Cdd:PHA03307 238 --DSSSSESSGCGWGPE-----------NECPLPRPAPITLPTRIWEASGWNGPSSRPgpaSSSSSPRERSPSPSPSSPG 304
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 564340089 540 LDKHGPDTPKQAFTPIDPPSGSADASPAGDRDRQTSLETSiltPSPCKIP-PQRG 593
Cdd:PHA03307 305 SGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPG---PSPSRSPsPSRP 356
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
708-813 |
1.05e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 708 ALRNRRLLRKVIRA--AALEEHNA------AMKDQLKLQEKDIQMWKVSLQKEQARYSQLQQQRDTMVTQLHSQIRQLQH 779
Cdd:COG4942 134 AVRRLQYLKYLAPArrEQAEELRAdlaelaALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213
|
90 100 110
....*....|....*....|....*....|....
gi 564340089 780 DREEFYNQSQELQTKLEDCRSMIAELRVELKKAN 813
Cdd:COG4942 214 ELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
704-960 |
1.43e-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: 43.12 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 704 RQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQQQRDTMVTQLHSQIRQLQHDREE 783
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 784 FYNQSQELQTKledcRSMIAELRVELKKANSKVCHTELLLSQVSQklsNSESVQQQMEFLNRQLLVLGEV---NELYLEQ 860
Cdd:TIGR02168 791 IEQLKEELKAL----REALDELRAELTLLNEEAANLRERLESLER---RIAATERRLEDLEEQIEELSEDiesLAAEIEE 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 861 LQSKHPDTTKEVEmmktAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVksqasgQLLAAE 940
Cdd:TIGR02168 864 LEELIEELESELE----ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL------ELRLEG 933
|
250 260
....*....|....*....|
gi 564340089 941 SRYEAQRKITRVLELEILDL 960
Cdd:TIGR02168 934 LEVRIDNLQERLSEEYSLTL 953
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
720-847 |
1.53e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 720 RAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQQ-----------QRDTMVTQLHSQ----IRQLQHDREEF 784
Cdd:COG3883 66 EIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVllgsesfsdflDRLSALSKIADAdadlLEELKADKAEL 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564340089 785 YNQSQELQTKLEDCRSMIAELRVELKKANSKVCHTELLLSQVSQKLsnsESVQQQMEFLNRQL 847
Cdd:COG3883 146 EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE---AAAEAQLAELEAEL 205
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
701-949 |
1.58e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 701 RFKRQQHALRNRRLLRKVIRAAALEEHNaamkdQLKLQEKDIQMWKVSLQKEQARYSQLQQQRDtmvtqlhSQIRQLQHD 780
Cdd:pfam17380 384 QMERQQKNERVRQELEAARKVKILEEER-----QRKIQQQKVEMEQIRAEQEEARQREVRRLEE-------ERAREMERV 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 781 REEfynqSQELQTKLEDCRSMIAELRvelkkanskvchtelllsQVSQKLSNSESVQQQMEFLNRQLLvlgevnELYLEQ 860
Cdd:pfam17380 452 RLE----EQERQQQVERLRQQEEERK------------------RKKLELEKEKRDRKRAEEQRRKIL------EKELEE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 861 LQSKHPDTTKEVEMMKtayrKELEKNRSHLLQQNQRLDASQRRVLELEsllakkdhllLEQKKYLEDVKSQAS---GQLL 937
Cdd:pfam17380 504 RKQAMIEEERKRKLLE----KEMEERQKAIYEEERRREAEEERRKQQE----------MEERRRIQEQMRKATeerSRLE 569
|
250
....*....|..
gi 564340089 938 AAESRYEAQRKI 949
Cdd:pfam17380 570 AMEREREMMRQI 581
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
731-950 |
2.28e-03 |
|
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: 42.41 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 731 MKDQLK-LQEKDIQMWKVSLQKEQARYSQLQQQRDTMVT-----------QLHSQIRQLQHDREEFYNQSQELQTKLEDC 798
Cdd:pfam15921 243 VEDQLEaLKSESQNKIELLLQQHQDRIEQLISEHEVEITgltekassarsQANSIQSQLEIIQEQARNQNSMYMRQLSDL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 799 RSMIAELRVELKKAN----SKVCHTELLL----SQVSQKLSNSESVQQQMEFLNRQLLVLgevnelyLEQLQSKHPDTTK 870
Cdd:pfam15921 323 ESTVSQLRSELREAKrmyeDKIEELEKQLvlanSELTEARTERDQFSQESGNLDDQLQKL-------LADLHKREKELSL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 871 EVEMMKTAYRKELeKNRSHLLQQNQRLDASQRRVLELESLLakkdhllleqKKYLEDVKSQASGQLLAAESRYEAQRKIT 950
Cdd:pfam15921 396 EKEQNKRLWDRDT-GNSITIDHLRRELDDRNMEVQRLEALL----------KAMKSECQGQMERQMAAIQGKNESLEKVS 464
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
724-931 |
2.78e-03 |
|
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: 41.93 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 724 LEEHNAAMKDQLK-------LQEKDIQMWKVSLQKEQARYSQLQQQRDTMVTQLhsqirqlqhdrEEFYNQSQELQTKLE 796
Cdd:TIGR04523 445 LTNQDSVKELIIKnldntreSLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL-----------KKLNEEKKELEEKVK 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 797 DCRSMIAELRVELKKANSKVchtelllSQVSQKLSNSESVQQQMEF-LNRQLL---VLG---EVNELYLEQ-----LQSK 864
Cdd:TIGR04523 514 DLTKKISSLKEKIEKLESEK-------KEKESKISDLEDELNKDDFeLKKENLekeIDEknkEIEELKQTQkslkkKQEE 586
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564340089 865 HPDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQ 931
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
831-942 |
3.09e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 39.20 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 831 SNSESVQQQMEFLNRQLLVLGEVNE-LYLEQLQSKhpdttKEVEMMK------TAYRKELEKNRSHLLQQ----NQRLDA 899
Cdd:pfam10473 17 RKADSLKDKVENLERELEMSEENQElAILEAENSK-----AEVETLKaeieemAQNLRDLELDLVTLRSEkenlTKELQK 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 564340089 900 SQRRVLELESLLAKKDHLL--LEQKKYLEDVKSQASGQLLAAESR 942
Cdd:pfam10473 92 KQERVSELESLNSSLENLLeeKEQEKVQMKEESKTAVEMLQTQLK 136
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
706-972 |
3.52e-03 |
|
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: 41.70 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 706 QHALRNRR-----LLRKviraaALEEHNAAMKDQLK-LQEKDIQ-MWKVSLQKEQARYSQL-----QQQRDTMVTQLHSQ 773
Cdd:pfam01576 318 QQELRSKReqevtELKK-----ALEEETRSHEAQLQeMRQKHTQaLEELTEQLEQAKRNKAnlekaKQALESENAELQAE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 774 IRQLQ-------HDREEFYNQSQELQTKLEDCRSMIAELRVELKKANSKVCHTELLLSQVSQKLSNSesvQQQMEFLNRQ 846
Cdd:pfam01576 393 LRTLQqakqdseHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKL---SKDVSSLESQ 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 847 llvLGEVNELYLEQLQSKHPDTTKevemmktayRKELEKNRSHLLQQNQRLDASQRRV-LELESLLAKkdhlLLEQKKYL 925
Cdd:pfam01576 470 ---LQDTQELLQEETRQKLNLSTR---------LRQLEDERNSLQEQLEEEEEAKRNVeRQLSTLQAQ----LSDMKKKL 533
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 564340089 926 EDVksqaSGQLLAAEsryEAQRKITRVLELEILDL------YGRLEK-DGRLQK 972
Cdd:pfam01576 534 EED----AGTLEALE---EGKKRLQRELEALTQQLeekaaaYDKLEKtKNRLQQ 580
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
700-914 |
3.69e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 700 ERFKRQQHALRNRRLLRKVIRA--AALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQQQRDTMVTQLHSQIRQL 777
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKqlAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 778 Q--------------HDREEFYNQSQELQTKLEDCRSMIAELRVELKKANSKvchTELLLSQVSQKLSNSESVQQQMEFl 843
Cdd:COG4942 114 YrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL---RAELEAERAELEALLAELEEERAA- 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564340089 844 nrqllvlgevnelyLEQLQSKHPDTTKEVEMMKTAYRKELEKnrshLLQQNQRLDASQRRVLELESLLAKK 914
Cdd:COG4942 190 --------------LEALKAERQKLLARLEKELAELAAELAE----LQQEAEELEALIARLEAEAAAAAER 242
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
731-956 |
3.80e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.48 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 731 MKDQLKLQEkdiQMWKVSLQKEQ----ARYSQLQQQRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRSM----I 802
Cdd:COG5185 346 EQGQESLTE---NLEAIKEEIENivgeVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAadrqI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 803 AELRVELKKANSKVchtelllsQVSQKLSN---SESVQQQMEFLNRQLLVLGEVNELYLEQLQSKHPDTTKEVEMMKT-- 877
Cdd:COG5185 423 EELQRQIEQATSSN--------EEVSKLLNeliSELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESrv 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 878 -AYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELE 956
Cdd:COG5185 495 sTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELT 574
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
710-920 |
4.20e-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: 41.36 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 710 RNRRLLRKVIRAAALEEHNA-AMKDQLKLQEKDIQMWKVSLQKEQARYSQLQQQRDTmvtQLHSQIRQLQHDREEFYNQS 788
Cdd:pfam12128 330 QHGAFLDADIETAAADQEQLpSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE---QNNRDIAGIKDKLAKIREAR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 789 QELQTKLE-DCRSMIAELRVELKKANSKVCHTELLLS--------QVSQKLSNSESVQQQmeflnrqllvlgEVNELYLE 859
Cdd:pfam12128 407 DRQLAVAEdDLQALESELREQLEAGKLEFNEEEYRLKsrlgelklRLNQATATPELLLQL------------ENFDERIE 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564340089 860 QLQSKHPDTTKEVEMMK---TAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLE 920
Cdd:pfam12128 475 RAREEQEAANAEVERLQselRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLH 538
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
720-945 |
4.82e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.96 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 720 RAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQQQRDTMVT--QLHSQIRQLQHDREEFYNQSQELQTKLED 797
Cdd:pfam10174 504 HASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTnpEINDRIRLLEQEVARYKEESGKAQAEVER 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 798 CRSMIAELRVELKKANSKVCHTE-LLLSQV---SQKLSNSESVQQQMEFLNRQLLVLGEVNElylEQLQSKHPDTTKEvE 873
Cdd:pfam10174 584 LLGILREVENEKNDKDKKIAELEsLTLRQMkeqNKKVANIKHGQQEMKKKGAQLLEEARRRE---DNLADNSQQLQLE-E 659
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564340089 874 MMKtayrkELEKNRSHLLQQNQRLDASQRRVLELESLLAKkdhLLLEQKKYLEDV---KSQAsgqLLAAESRYEA 945
Cdd:pfam10174 660 LMG-----ALEKTRQELDATKARLSSTQQSLAEKDGHLTN---LRAERRKQLEEIlemKQEA---LLAAISEKDA 723
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
700-959 |
5.13e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.94 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 700 ERFKRQQHALRNRRLLRKVIRA---------AALEEHNAAMKDQLKL-----------------QEKDIQMWkvslQKEQ 753
Cdd:PRK10246 606 EEHERQLRLLSQRHELQGQIAAhnqqiiqyqQQIEQRQQQLLTALAGyaltlpqedeeaswlatRQQEAQSW----QQRQ 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 754 ARYSQLQQQ-------------RDTMVTQ------------------LHSQIRQLQHDREEFYNQSQELQTKLE------ 796
Cdd:PRK10246 682 NELTALQNRiqqltplletlpqSDDLPHSeetvaldnwrqvheqclsLHSQLQTLQQQDVLEAQRLQKAQAQFDtalqas 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 797 ---DCRSMIAEL-------RVELKKAN--SKVCHTELLLSQVSQKLSnsESVQQQMEFLNRQLLVlgEVNELYLEQL-QS 863
Cdd:PRK10246 762 vfdDQQAFLAALldeetltQLEQLKQNleNQRQQAQTLVTQTAQALA--QHQQHRPDGLDLTVTV--EQIQQELAQLaQQ 837
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 864 KHPDTTKEVEMmktayRKEL---EKNRSHLLQQNQRLDASQRRVLE---LESLLAKKD---HLLLEQKKYLEDVKSQASG 934
Cdd:PRK10246 838 LRENTTRQGEI-----RQQLkqdADNRQQQQALMQQIAQATQQVEDwgyLNSLIGSKEgdkFRKFAQGLTLDNLVWLANQ 912
|
330 340
....*....|....*....|....*
gi 564340089 935 QLLAAESRYEAQRKITRVLELEILD 959
Cdd:PRK10246 913 QLTRLHGRYLLQRKASEALELEVVD 937
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
753-946 |
5.88e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.65 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 753 QARYSQLQQQRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRSMIAELRVELKKANSKvcHTELLLSQVSQKLSN 832
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREK--HEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 833 SESVQQQMEFLNRQLLVLGEVNELY--LEQLQSKHPDTTKEVEMMK------TAYRKELEKNR----SHLLQQNQRLDAS 900
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEedIKTLTQRVLERETELERMKerakkaGAQRKEEEAERkqlqAKLQQTEEELRSL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564340089 901 QRRVLELESLLAKKDHLLLEqkkyLEDVKSQASgQLLAAESRYEAQ 946
Cdd:pfam07888 191 SKEFQELRNSLAQRDTQVLQ----LQDTITTLT-QKLTTAHRKEAE 231
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
716-905 |
7.62e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.71 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 716 RKVIRAAALEEHNAAMKDQLKLQEKDIqmwkvslqkEQaRYSQlQQQRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKL 795
Cdd:COG3096 498 RELLRRYRSQQALAQRLQQLRAQLAEL---------EQ-RLRQ-QQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 796 EDCRSMIAE-------LRVELKKANSKVchTEL----------------LLSQVSQKLSNSESVQQQMEFLnrqllvlge 852
Cdd:COG3096 567 EELEEQAAEaveqrseLRQQLEQLRARI--KELaarapawlaaqdalerLREQSGEALADSQEVTAAMQQL--------- 635
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564340089 853 vnelyLEQLqskhpdttkevemmktayrKELEKNRSHLLQQNQRLDASQRRVL 905
Cdd:COG3096 636 -----LERE-------------------REATVERDELAARKQALESQIERLS 664
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
700-966 |
8.11e-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: 40.34 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 700 ERFKRQQHALRNRRLLRKVIRA--AALEEHNAAMKDQLKLQEKDIQ-------MWKVSLQKEQARYSQLQQQRDTmVTQL 770
Cdd:TIGR00618 403 DILQREQATIDTRTSAFRDLQGqlAHAKKQQELQQRYAELCAAAITctaqcekLEKIHLQESAQSLKEREQQLQT-KEQI 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 771 HSQIRQLQHDREEFYNQSQELQTKLEDCRSMIAELRVELKKANSKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLlvl 850
Cdd:TIGR00618 482 HLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQR--- 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 851 gevnELYLEQLQSKHpDTTKEVEMMKTAYRKELEKNRS------HLLQQNQRLDASQRrvLELESLLAKKDHLLLEQKKY 924
Cdd:TIGR00618 559 ----ASLKEQMQEIQ-QSFSILTQCDNRSKEDIPNLQNitvrlqDLTEKLSEAEDMLA--CEQHALLRKLQPEQDLQDVR 631
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 564340089 925 LED-VKSQASGQLLAAESRYE---AQRKI------TRVLELEILDLYGRLEK 966
Cdd:TIGR00618 632 LHLqQCSQELALKLTALHALQltlTQERVrehalsIRVLPKELLASRQLALQ 683
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
705-810 |
9.85e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 38.73 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564340089 705 QQHALRNRRLLRKViraAALEEHNAAMKDQLKLQEKDiqmwKVSLQKEQARYSQLQQQRDTMvtQLHSQ-----IRQLQH 779
Cdd:pfam13851 50 SEIQQENKRLTEPL---QKAQEEVEELRKQLENYEKD----KQSLKNLKARLKVLEKELKDL--KWEHEvleqrFEKVER 120
|
90 100 110
....*....|....*....|....*....|....*
gi 564340089 780 DREEFYNQS----QELQTKLEdCRSMIAELRVELK 810
Cdd:pfam13851 121 ERDELYDKFeaaiQDVQQKTG-LKNLLLEKKLQAL 154
|
|
| |
