|
Name |
Accession |
Description |
Interval |
E-value |
| Angiomotin_C |
pfam12240 |
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ... |
634-840 |
8.42e-113 |
|
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 and 211 amino acids in length. This family is the C terminal region of angiomotin. Angiomotin regulates the action of angiogenesis inhibitor angiostatin. The C terminal region of angiomotin appears to be involved in directing the protein chemotactically.
Pssm-ID: 463503 [Multi-domain] Cd Length: 200 Bit Score: 345.60 E-value: 8.42e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 634 YVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKHGNGQPANMPEYNAPALLELVREKEERILALEADM 713
Cdd:pfam12240 1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 714 TKWEQKYLEESTIRHFAMNAAATAAAERDTTIINHSRNGSYgESSLeahiwqeEEEVVQANRRCQDMEYTIKNLHAKIIE 793
Cdd:pfam12240 81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSY-DSSF-------NEELLLANRRCQEMENRIKNLHAQILE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 530396371 794 KDAMIKVLQQRSRKDAGKTDSSSLRPARSVPSI-AAATGTHSRQTSLT 840
Cdd:pfam12240 153 KDAMIKVLQQRSRKDPGKTDQQSLRPARSVPSIsAAATGLHSRQTSLS 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
465-723 |
2.62e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 465 AIVERAQQMVEILTEENRVLHQELQgyyDNADKLHKFEKELQRISEAYESLVKSttkresldkamRNKLEGEIRRLHDFN 544
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAE-----------LARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 545 RDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKL 624
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 625 EEELREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKhgngqpanmpeynapALLELVREKEE 704
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---------------EAAEEEAELEE 456
|
250
....*....|....*....
gi 530396371 705 RILALEADMTKWEQKYLEE 723
Cdd:COG1196 457 EEEALLELLAELLEEAALL 475
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
459-804 |
7.73e-10 |
|
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: 63.15 E-value: 7.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 459 LGPDAFAIVEraQQMV-EILT---EENRVLHQELQGyydnADKLHKFEKE-LQRISEAYESLVKSTTKRESLDKAMrNKL 533
Cdd:TIGR02168 133 LGKRSYSIIE--QGKIsEIIEakpEERRAIFEEAAG----ISKYKERRKEtERKLERTRENLDRLEDILNELERQL-KSL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 534 EGEIRRLHDFnRDLRDRLETANRQLSSREYEghedkaaeghyasqnkEFLKEKEKLEMELAAVRTASEDHRRHIEILDQA 613
Cdd:TIGR02168 206 ERQAEKAERY-KELKAELRELELALLVLRLE----------------ELREELEELQEELKEAEEELEELTAELQELEEK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 614 LSNAQARVIKLEEELREKQayvekveKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKHgNGQPANMPEYNAP 693
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE-LESKLDELAEELA 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 694 ALLELVREKEERILALEADMTKWEQKYLE-ESTIR----HFAMNAAATAAAERDTTIINH--SRNGSYGEsSLEAHIWQE 766
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEElESRLEeleeQLETLRSKVAQLELQIASLNNeiERLEARLE-RLEDRRERL 419
|
330 340 350
....*....|....*....|....*....|....*...
gi 530396371 767 EEEVVQANRRCQDMEytIKNLHAKIIEKDAMIKVLQQR 804
Cdd:TIGR02168 420 QQEIEELLKKLEEAE--LKELQAELEELEEELEELQEE 455
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
462-723 |
1.30e-09 |
|
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: 62.39 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 462 DAFAIVERAQQMVEILTEENRVLHQELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRE-SLDKAMRNKLEGEIRRL 540
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEaRLSHSRIPEIQAELSKL 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 541 HDFNRDLRDRLETANRQLSSREYEGHedkaaeghYASQNKEFLKEK-EKLEMELAAVRTASEDHRRHIEILDQALSNAQA 619
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTLEKE--------YLEKEIQELQEQrIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 620 RVIKLEEELREKQAYVEKVEK----LQQALTQLQSACEKREQMERRLRTWLE---RELDALRTQQKHGNGQPANMPEYna 692
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLEaleEELSEIEDPKGEDEEIPEEELSL-- 953
|
250 260 270
....*....|....*....|....*....|.
gi 530396371 693 PALLELVREKEERILALEADMTKWEQKYLEE 723
Cdd:TIGR02169 954 EDVQAELQRVEEEIRALEPVNMLAIQEYEEV 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
465-711 |
2.14e-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: 61.61 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 465 AIVERAQQMVEILTEENRVLHQELQGYYDN-----------ADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKL 533
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQleeleskldelAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 534 EGEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKAAEGHYA--SQNKEFLkEKEKLEMELAAVRTASEDHRRHIEILD 611
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRErlQQEIEEL-LKKLEEAELKELQAELEELEEELEELQ 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 612 QALSNAQARVIKLEEELREKQayvEKVEKLQQALTQLQSACEKREQMERRLRTwlerELDALRTQQKHGNGQPANMpeyn 691
Cdd:TIGR02168 454 EELERLEEALEELREELEEAE---QALDAAERELAQLQARLDSLERLQENLEG----FSEGVKALLKNQSGLSGIL---- 522
|
250 260
....*....|....*....|
gi 530396371 692 aPALLELVREKEERILALEA 711
Cdd:TIGR02168 523 -GVLSELISVDEGYEAAIEA 541
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
468-724 |
4.42e-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: 4.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 468 ERAQQmveiLTEENRVLHQELQGYydnadKLHKFEKELQRISEAYESLvksTTKRESLDKAMRnKLEGEIRRLHDFNRDL 547
Cdd:COG1196 213 ERYRE----LKEELKELEAELLLL-----KLRELEAELEELEAELEEL---EAELEELEAELA-ELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 548 RDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEE 627
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 628 LREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKhgngqpanmpeynapALLELVREKEERIL 707
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE---------------ALLERLERLEEELE 424
|
250
....*....|....*..
gi 530396371 708 ALEADMTKWEQKYLEES 724
Cdd:COG1196 425 ELEEALAELEEEEEEEE 441
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
493-677 |
1.08e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.54 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 493 DNADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEgEIRRLHDFNRDLRDRLETAnrqlssREYEGHEDKAAE 572
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAEYSWDEIDVASAE------REIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 573 ghyASQNKEFLKEkekLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQAltQLQSAC 652
Cdd:COG4913 680 ---LDASSDDLAA---LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALL 751
|
170 180 190
....*....|....*....|....*....|.
gi 530396371 653 EKR------EQMERRLRTWLERELDALRTQQ 677
Cdd:COG4913 752 EERfaaalgDAVERELRENLEERIDALRARL 782
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
462-701 |
1.40e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 462 DAFAIVERAQQMVEilteenrvlH-QELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESLDkAMRNKL-----EG 535
Cdd:COG4913 219 EEPDTFEAADALVE---------HfDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELE-YLRAALrlwfaQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 536 EIRRLHDFNRDLRDRLETANRQLS--SREYEGHEDK--AAEGHYASQNkefLKEKEKLEMELAAVRTASEDHRRHIEILD 611
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELErlEARLDALREEldELEAQIRGNG---GDRLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 612 QALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKHGNGQPANMPEYN 691
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRA---EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
250
....*....|
gi 530396371 692 APALLELVRE 701
Cdd:COG4913 443 LALRDALAEA 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
506-794 |
5.11e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 506 QRISEAYESLVKSTTKRESLDKAmRNKLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKAAEGHYASQN------ 579
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKA-LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIaqlske 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 580 -KEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQsacEKREQM 658
Cdd:TIGR02168 756 lTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA---ELTLLNEEAANLR---ERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 659 ERRLRTWlERELDALRTQQKHGNGQPANmpeyNAPALLELVREKEErilaLEADMTKWEQKYLEESTIRHfamnAAATAA 738
Cdd:TIGR02168 830 ERRIAAT-ERRLEDLEEQIEELSEDIES----LAAEIEELEELIEE----LESELEALLNERASLEEALA----LLRSEL 896
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 530396371 739 AERDTTIINHSRNGSYGESSLEAhiwqEEEEVVQANRRCQDMEYTIKNLHAKIIEK 794
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEE----LREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
465-674 |
5.13e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 465 AIVERAQQMVEILTEE---NRVLHQELQ-GYYDNADK-LHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEG---E 536
Cdd:PRK03918 129 AIYIRQGEIDAILESDesrEKVVRQILGlDDYENAYKnLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvlrE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 537 IRRLHDFNRDLRDRLETANRQLssREYEGHEDKAAEghYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILD----- 611
Cdd:PRK03918 209 INEISSELPELREELEKLEKEV--KELEELKEEIEE--LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEekvke 284
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530396371 612 ----QALSNAQARVIKLEEELREKQAYVEK-VEKLQQALTQLQSACEKREQMERRLRtWLERELDALR 674
Cdd:PRK03918 285 lkelKEKAEEYIKLSEFYEEYLDELREIEKrLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELE 351
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
486-669 |
5.92e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 486 QELQGYYDNADKLHKFEKELQRISEAYESLvksttkRESLDKAmRNKLEGEIRRLhdfnRDLRDRLETANRQLSSREYEG 565
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKL------EEELDKA-FEELAETEKRL----EELRKELEELEKKYSEEEYEE 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 566 HEDkaaeghyasqnkeflkEKEKLEMELAAVRTASEDHRRHIEILDQALSnaqarviKLEEELREKQAYVEKVEKLQQAL 645
Cdd:PRK03918 664 LRE----------------EYLELSRELAGLRAELEELEKRREEIKKTLE-------KLKEELEEREKAKKELEKLEKAL 720
|
170 180
....*....|....*....|....
gi 530396371 646 TQLQsacEKREQMeRRLRTWLERE 669
Cdd:PRK03918 721 ERVE---ELREKV-KKYKALLKER 740
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
487-668 |
1.42e-07 |
|
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: 53.39 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 487 ELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDLRDRLETANRQL----SSRE 562
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 563 YEG--HEDKAAEghyasqnkeflKEKEKLEMELAAVRTAsedhrrhIEILDQALSNAQARVIKLEEELREKQA-YVEKVE 639
Cdd:COG1579 91 YEAlqKEIESLK-----------RRISDLEDEILELMER-------IEELEEELAELEAELAELEAELEEKKAeLDEELA 152
|
170 180 190
....*....|....*....|....*....|
gi 530396371 640 KLQQALTQLQSACEK-REQMERRLRTWLER 668
Cdd:COG1579 153 ELEAELEELEAEREElAAKIPPELLALYER 182
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
505-681 |
1.50e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 505 LQRISEAYESLVKSTTKRESLDKAMRNKLEGEIRRL---HDFNRDLRDRLETANRQLSS--REYEGHEDKAAEGHYASQN 579
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAeekEEEYAELQEELEELEEELEEleAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 580 KEFLKEKEKLEMELAAVRTASEDHRRHIEI---LDQALSNAQARVIKLEEELREKQAY------------VEKVEKLQQA 644
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEElreLEEELEELEAELAELQEELEELLEQlslateeelqdlAEELEELQQR 207
|
170 180 190
....*....|....*....|....*....|....*..
gi 530396371 645 LTQLQsacEKREQMERRLRTwLERELDALRTQQKHGN 681
Cdd:COG4717 208 LAELE---EELEEAQEELEE-LEEELEQLENELEAAA 240
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
496-704 |
2.72e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 496 DKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRnKLEGEIRRLHDFNRDLRDRLETanrqlSSREYEGHEDKAAEghy 575
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELKEEIEELEKELE-SLEGSKRKLEEKIRELEERIEE-----LKKEIEELEEKVKE--- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 576 asqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKR 655
Cdd:PRK03918 285 ----LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER 360
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 530396371 656 EQMERRLRTwLERELDALRTQQKhgngqpANMPEYNAPALLELVREKEE 704
Cdd:PRK03918 361 HELYEEAKA-KKEELERLKKRLT------GLTPEKLEKELEELEKAKEE 402
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
493-677 |
1.08e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.40 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 493 DNADKLHKFEKELQ-RISEAYESLVKSTTKRESLDKaMRNKLEGEIRRLHDFNR---DLRDRLETANRQLSSREYEGHED 568
Cdd:pfam01576 145 DQNSKLSKERKLLEeRISEFTSNLAEEEEKAKSLSK-LKNKHEAMISDLEERLKkeeKGRQELEKAKRKLEGESTDLQEQ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 569 KAaegHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTql 648
Cdd:pfam01576 224 IA---ELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLG-- 298
|
170 180
....*....|....*....|....*....
gi 530396371 649 qsacekrEQMErRLRTWLERELDALRTQQ 677
Cdd:pfam01576 299 -------EELE-ALKTELEDTLDTTAAQQ 319
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
468-724 |
4.89e-05 |
|
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: 47.51 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 468 ERAQQMVEIlteENRVLHQELQgyydnadkLHKFEKELQRISEAYE---SLVKSTTKRESLDKAMRNKlEGEIRRLHDFN 544
Cdd:pfam10174 182 ERTRRIAEA---EMQLGHLEVL--------LDQKEKENIHLREELHrrnQLQPDPAKTKALQTVIEMK-DTKISSLERNI 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 545 RDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKeFLKEK--------EKLEMELAAVRTASE-------DHRRHIEI 609
Cdd:pfam10174 250 RDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSK-FMKNKidqlkqelSKKESELLALQTKLEtltnqnsDCKQHIEV 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 610 LDQALSNAQARVIKLEEE-------LREKQAYVEKVEKLQQALTQ----LQSACEKREQM----ERRLRTwLERELDALR 674
Cdd:pfam10174 329 LKESLTAKEQRAAILQTEvdalrlrLEEKESFLNKKTKQLQDLTEekstLAGEIRDLKDMldvkERKINV-LQKKIENLQ 407
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530396371 675 TQQKHGNGQPANMPEY------------NAPALLE-LVREKEERILALEADMTKWEQKYLEES 724
Cdd:pfam10174 408 EQLRDKDKQLAGLKERvkslqtdssntdTALTTLEeALSEKERIIERLKEQREREDRERLEEL 470
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
502-641 |
6.23e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.77 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 502 EKELQRISEAYESLVKST-TKRESLDKAMRnKLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKAAEghyasqNK 580
Cdd:COG2433 387 EKELPEEEPEAEREKEHEeRELTEEEEEIR-RLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEE------RR 459
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530396371 581 EFLKEKE--KLEMELAAVRTASEDHRRHIEILdqalsnaQARVIKLEE----ELREKQAYVEKVEKL 641
Cdd:COG2433 460 EIRKDREisRLDREIERLERELEEERERIEEL-------KRKLERLKElwklEHSGELVPVKVVEKF 519
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
502-728 |
8.40e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.22 E-value: 8.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 502 EKELQRISEAYESLVKSTTKRESLDKAMRnklegEIRRLHDFNRDLRDRLETANrqLSSREYEgheDKAAEghyasqnKE 581
Cdd:COG0497 154 EELLEEYREAYRAWRALKKELEELRADEA-----ERARELDLLRFQLEELEAAA--LQPGEEE---ELEEE-------RR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 582 FLKEKEKLemeLAAVRTAsedhrrhIEILDQALSNAQARVIKLEEELREKQAYVEK----VEKLQQALTQLQSACEK--- 654
Cdd:COG0497 217 RLSNAEKL---REALQEA-------LEALSGGEGGALDLLGQALRALERLAEYDPSlaelAERLESALIELEEAASElrr 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 655 -REQME---RRLRTWLEReLDALRT-QQKHGnGQPANMPEY--NAPALLELVREKEERILALEADMTKWEQKYLEE---- 723
Cdd:COG0497 287 yLDSLEfdpERLEEVEER-LALLRRlARKYG-VTVEELLAYaeELRAELAELENSDERLEELEAELAEAEAELLEAaekl 364
|
....*
gi 530396371 724 STIRH 728
Cdd:COG0497 365 SAARK 369
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
495-678 |
9.08e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 9.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 495 ADKLHKFEKELQRISE---AYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDLRDRLETANRQLSS---------RE 562
Cdd:COG4942 19 ADAAAEAEAELEQLQQeiaELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekeiaelrAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 563 YEGHEDKAAE---GHYASQNKEFLK------EKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQA 633
Cdd:COG4942 99 LEAQKEELAEllrALYRLGRQPPLAlllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 530396371 634 YVEKVEKLQQALTQLQSaceKREQMERRLRTWLERELDALRTQQK 678
Cdd:COG4942 179 LLAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQ 220
|
|
| PilO |
COG3167 |
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures]; |
612-673 |
1.49e-04 |
|
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
Pssm-ID: 442400 [Multi-domain] Cd Length: 202 Bit Score: 43.78 E-value: 1.49e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530396371 612 QALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQsacEKREQMERRLRTwlERELDAL 673
Cdd:COG3167 46 EELEELEAEEAQLKQELEKKQAKAANLPALKAQLEELE---QQLGELLKQLPS--KAEVPAL 102
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
496-668 |
1.52e-04 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 44.27 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 496 DKLHKFEKELQRISEAYESLVKsttKRESLDKAMrNKLEGEIRRLHDFNRDLRDRLETANRQLSsreyeGHEDKAAEGHY 575
Cdd:cd07596 11 DYILKLEEQLKKLSKQAQRLVK---RRRELGSAL-GEFGKALIKLAKCEEEVGGELGEALSKLG-----KAAEELSSLSE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 576 ASQNKEFLKEKEKLEMEL---AAVRTASEDH---RRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQ----QAL 645
Cdd:cd07596 82 AQANQELVKLLEPLKEYLrycQAVKETLDDRadaLLTLQSLKKDLASKKAQLEKLKAAPGIKPA---KVEELEeeleEAE 158
|
170 180
....*....|....*....|...
gi 530396371 646 TQLQSACEKREQMERRLRTWLER 668
Cdd:cd07596 159 SALEEARKRYEEISERLKEELKR 181
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
576-821 |
1.99e-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: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 576 ASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQsacEKR 655
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ---ELAALEAELAELE---KEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 656 EQMERRLRTWLERELDALRTQQKHG---------NGQPANMPEYNAPALLELVREKEERILALEADMTKWEQKYLEESTI 726
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 727 RHFAMNAAATAAAERDttiinhsrngsygesSLEAHIWQEEEEVVQANRRCQDMEYTIKNLHAKIIEKDAMIKVLQQRSR 806
Cdd:COG4942 173 RAELEALLAELEEERA---------------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
250
....*....|....*
gi 530396371 807 KDAGKTDSSSLRPAR 821
Cdd:COG4942 238 AAAERTPAAGFAALK 252
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
477-662 |
2.25e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 477 LTEENRvlhQELQGYYdnADKLHKFEKELQRISEAYESLVKSTTKresLDKAMRNklEGEIRRLH---DFNRDLRDRLET 553
Cdd:PRK03918 445 LTEEHR---KELLEEY--TAELKRIEKELKEIEEKERKLRKELRE---LEKVLKK--ESELIKLKelaEQLKELEEKLKK 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 554 ANRQ---LSSREYEGHEDKAA--EGHYASQNKEfLKEKEKLEMELAAVRTASED-HRRHIEILDQALSNAQARVIKLEEE 627
Cdd:PRK03918 515 YNLEeleKKAEEYEKLKEKLIklKGEIKSLKKE-LEKLEELKKKLAELEKKLDElEEELAELLKELEELGFESVEELEER 593
|
170 180 190
....*....|....*....|....*....|....*
gi 530396371 628 LREKQAYVEKVEKLQQALTQLQSACEKREQMERRL 662
Cdd:PRK03918 594 LKELEPFYNEYLELKDAEKELEREEKELKKLEEEL 628
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
521-715 |
2.47e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 521 KRESLDKamrnkLEGEIRRLHDfnRDLRDRLETANRQLSS-----REYEGHEDKAAEGHYASQN-----KEFLKEKEKLE 590
Cdd:PRK02224 185 QRGSLDQ-----LKAQIEEKEE--KDLHERLNGLESELAEldeeiERYEEQREQARETRDEADEvleehEERREELETLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 591 MELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKREqmerrlrTWLEREL 670
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRD-------EELRDRL 330
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 530396371 671 DALRTQQKHGNGQPANMPEyNAPALLELVREKEERILALEADMTK 715
Cdd:PRK02224 331 EECRVAAQAHNEEAESLRE-DADDLEERAEELREEAAELESELEE 374
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
468-728 |
3.16e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 468 ERAQQMVEILTEENRVLHQELQGYydnadKLHKFEKELQRISEAYESLvkstTKRESLDKAMRNKLEGEIRRLhdfnRDL 547
Cdd:PRK03918 361 HELYEEAKAKKEELERLKKRLTGL-----TPEKLEKELEELEKAKEEI----EEEISKITARIGELKKEIKEL----KKA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 548 RDRLETANRQ--LSSREYEGHEDKAAEGHY-------ASQNKEFLKEKEKLEMELAAVRTASEDHRRHI---EILDQaLS 615
Cdd:PRK03918 428 IEELKKAKGKcpVCGRELTEEHRKELLEEYtaelkriEKELKEIEEKERKLRKELRELEKVLKKESELIklkELAEQ-LK 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 616 NAQAR-----VIKLEEELREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTwLERELDALRTQQKHGNGQPANMPey 690
Cdd:PRK03918 507 ELEEKlkkynLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE-LEKKLDELEEELAELLKELEELG-- 583
|
250 260 270
....*....|....*....|....*....|....*...
gi 530396371 691 napalLELVREKEERILALEadmtKWEQKYLEESTIRH 728
Cdd:PRK03918 584 -----FESVEELEERLKELE----PFYNEYLELKDAEK 612
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
468-643 |
3.18e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 468 ERAQQMVEILTEENRVLHQELQGYYDNADKLHKFEKELQRISEAYESLvksttkresldKAMRNKLEGEIRRLHDFNR-- 545
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL-----------REELEKLEKLLQLLPLYQEle 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 546 DLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELA--------AVRTASEDHRRH---IEILDQAL 614
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqlslateeELQDLAEELEELqqrLAELEEEL 215
|
170 180
....*....|....*....|....*....
gi 530396371 615 SNAQARVIKLEEELREKQAYVEKVEKLQQ 643
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEER 244
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
472-811 |
3.25e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 472 QMVEILTEENRVLHQELQGYYDNADKLHKFEKELQRISEAYESL-VKSTTKRESLDKAMRNKLEGEIRRlhdfnrDLRDR 550
Cdd:TIGR02169 146 DFISMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLdLIIDEKRQQLERLRREREKAERYQ------ALLKE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 551 LetanrqlssREYEGhedkaaeghyasqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELRE 630
Cdd:TIGR02169 220 K---------REYEG--------------YELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 631 KQAYV------------EKVEKLQQALTQLQ---SACEKR-EQMERRLRTwLERELDALRTQQKHGNGQpanmpeynapa 694
Cdd:TIGR02169 277 LNKKIkdlgeeeqlrvkEKIGELEAEIASLErsiAEKERElEDAEERLAK-LEAEIDKLLAEIEELERE----------- 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 695 LLELVREKE---ERILALEADMTKWEQKYLEESTirHFAMNAAATAAAERDTTIINHSRNgsygesSLEAHIWQEEEEVV 771
Cdd:TIGR02169 345 IEEERKRRDkltEEYAELKEELEDLRAELEEVDK--EFAETRDELKDYREKLEKLKREIN------ELKRELDRLQEELQ 416
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 530396371 772 QANRRCQDMEYTIKNLHAKIIEKDAMIKVLQQRSRKDAGK 811
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK 456
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
465-658 |
3.68e-04 |
|
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: 44.44 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 465 AIVERAQQMVEILTEENRVLHQE-LQGYYDNADKLHKFEKELQRISEAYESLVKS----TTKRESLDKAMRNKLEGEIRR 539
Cdd:pfam12128 315 AAVAKDRSELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERLKALTGKhqdvTAKYNRRRSKIKEQNNRDIAG 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 540 LHDfnrDLRDRLETANRQLSSRE--YEGHEDKAAEGHYAsQNKEFLKEKEKLEMELAAVR------TASEDHRRHIEILD 611
Cdd:pfam12128 395 IKD---KLAKIREARDRQLAVAEddLQALESELREQLEA-GKLEFNEEEYRLKSRLGELKlrlnqaTATPELLLQLENFD 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 530396371 612 QALSNAQ-------ARVIKLEEELRE-KQAYVEKVEKLQQA---LTQLQSACEKREQM 658
Cdd:pfam12128 471 ERIERAReeqeaanAEVERLQSELRQaRKRRDQASEALRQAsrrLEERQSALDELELQ 528
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
474-658 |
3.94e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 42.82 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 474 VEILTEENRVLHQELQGYYDNADKLHKFEKEL---------------QRISEAYESLVKSTTKResldkamRNKLEgEIR 538
Cdd:cd00176 35 VEALLKKHEALEAELAAHEERVEALNELGEQLieeghpdaeeiqerlEELNQRWEELRELAEER-------RQRLE-EAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 539 RLHDFNRDLRD---RLETANRQLSSREYEGHEDKAaeghyasqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALS 615
Cdd:cd00176 107 DLQQFFRDADDleqWLEEKEAALASEDLGKDLESV---------EELLKKHKELEEELEAHEPRLKSLNELAEELLEEGH 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 530396371 616 NAQARVIKleeelrekqayvEKVEKLQQALTQLQSACEKREQM 658
Cdd:cd00176 178 PDADEEIE------------EKLEELNERWEELLELAEERQKK 208
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
483-723 |
4.10e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.33 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 483 VLHQELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRnKLEGEIRRLHDFNRDLRDRLEtanrqlssrE 562
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK-KILAEDEKLLDEKKQFEKIAE---------E 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 563 YEGHEDkaaEGHYASQNKEflKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEE-----LREKQAYVEK 637
Cdd:pfam05483 434 LKGKEQ---ELIFLLQARE--KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHcdkllLENKELTQEA 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 638 VEKLQQALTQLQSACEKREQMERRLR---------TWLERELDALRTQQKHGNGQ---PANMPEYNAPALLELVREKEER 705
Cdd:pfam05483 509 SDMTLELKKHQEDIINCKKQEERMLKqienleekeMNLRDELESVREEFIQKGDEvkcKLDKSEENARSIEYEVLKKEKQ 588
|
250 260
....*....|....*....|....
gi 530396371 706 ILALEADMTKWEQ------KYLEE 723
Cdd:pfam05483 589 MKILENKCNNLKKqienknKNIEE 612
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
582-720 |
4.47e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 582 FLKEKEKLEMELAAVRTASEDHRRHIEILDQAlsnaQARVIKLEEELREKQAYVEKVEKLQQALT----------QLQSA 651
Cdd:COG4717 69 NLKELKELEEELKEAEEKEEEYAELQEELEEL----EEELEELEAELEELREELEKLEKLLQLLPlyqelealeaELAEL 144
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530396371 652 CEKREQMERRLRTW--LERELDALRTQQKHGNGQPANMPEYNAPALLELVREKEERILALEADMTKWEQKY 720
Cdd:COG4717 145 PERLEELEERLEELreLEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
|
| PRK10361 |
PRK10361 |
DNA recombination protein RmuC; Provisional |
570-680 |
5.32e-04 |
|
DNA recombination protein RmuC; Provisional
Pssm-ID: 182409 [Multi-domain] Cd Length: 475 Bit Score: 43.82 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 570 AAEGHYASQNKEFLKEKEKLEMELAAVR---TASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKV-----EKL 641
Cdd:PRK10361 22 FASYQHAQQKAEQLAEREEMVAELSAAKqqiTQSEHWRAECELLNNEVRSLQSINTSLEADLREVTTRMEAAqqhadDKI 101
|
90 100 110
....*....|....*....|....*....|....*....
gi 530396371 642 QQALTQLQSACEKREQMERRLRTWLERELDALRTQQKHG 680
Cdd:PRK10361 102 RQMINSEQRLSEQFENLANRIFEHSNRRVDEQNRQSLNS 140
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
577-723 |
6.17e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 577 SQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQSAcekRE 656
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA---RIKKYEEQLGNVRNN---KE 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530396371 657 QMErrlrtwLERELDALRTQQKHGngqpanmpEYNAPALLELVREKEERILALEADMTKWEQKYLEE 723
Cdd:COG1579 91 YEA------LQKEIESLKRRISDL--------EDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
577-840 |
7.41e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 7.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 577 SQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEEL----REKQAYVEKVEKLQQALTQLQSAC 652
Cdd:COG4372 52 EELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELeslqEEAEELQEELEELQKERQDLEQQR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 653 EKREQMERRLRTWL---ERELDALRTQQKHGNGQ-------PANMPEYNAPALLELVREKEERILALEADMTKWEQKYLE 722
Cdd:COG4372 132 KQLEAQIAELQSEIaerEEELKELEEQLESLQEElaaleqeLQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIES 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 723 ESTIRHFAMNAAATAAAER----DTTIINHSRNGSYGESSLEAHIWQEEEEVVQANRRCQDMEYTIKNLHAKIIEKDAMI 798
Cdd:COG4372 212 LPRELAEELLEAKDSLEAKlglaLSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEA 291
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 530396371 799 KVLQQRSRKDAGKTDSSSLRPARSVPSIAAATGTHSRQTSLT 840
Cdd:COG4372 292 ALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
467-654 |
2.15e-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: 41.97 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 467 VERAQQMVEILTEENRVLHQELQGYYDNADKLHKFEKELQR-ISEAYESLVKSTTKRESLDKAMRNkLEGEIRRLHDFNR 545
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESeLEALLNERASLEEALALLRSELEE-LSEELRELESKRS 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 546 DLRDRLETANRQLSS--REYEGHEDKAAeghyasQNKEFLKEKEKLEMELAAvrtasedhrRHIEILDQALSNAQARVIK 623
Cdd:TIGR02168 912 ELRRELEELREKLAQleLRLEGLEVRID------NLQERLSEEYSLTLEEAE---------ALENKIEDDEEEARRRLKR 976
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 530396371 624 LE-----------------EELREKQAYVEK-VEKLQQALTQLQSACEK 654
Cdd:TIGR02168 977 LEnkikelgpvnlaaieeyEELKERYDFLTAqKEDLTEAKETLEEAIEE 1025
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
470-668 |
2.26e-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: 41.29 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 470 AQQMVEILTEENRVLHQELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDLRD 549
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 550 RLETANRQLSSREY-----------------EGHEDKAAEGHYASQNKEFLKEK-EKLEMELAAVRTASEDHRRHIEILD 611
Cdd:COG4942 98 ELEAQKEELAELLRalyrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQaEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 530396371 612 QALSNAQARVIKLEEELREKQayvEKVEKLQQALTQLQSACEKREQMERRLRTWLER 668
Cdd:COG4942 178 ALLAELEEERAALEALKAERQ---KLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
495-677 |
2.82e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 495 ADKLHKFEKELQRISEAYESLVKSTtkreSLDKAMRNKLEGEIRRLHDFNRDLRDRLETANRQLS--SREYEGHEDKAAE 572
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEA----GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQahNEEAESLREDADD 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 573 ghYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQAL----------------------------SNAQARVIKL 624
Cdd:PRK02224 354 --LEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIeelrerfgdapvdlgnaedfleelreerDELREREAEL 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530396371 625 EEELREKQAYVEKVEKLQ---------QALTQLQSAC---EKREQMERrlrtwLERELDALRTQQ 677
Cdd:PRK02224 432 EATLRTARERVEEAEALLeagkcpecgQPVEGSPHVEtieEDRERVEE-----LEAELEDLEEEV 491
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
486-709 |
3.06e-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: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 486 QELQGYYDN--------ADKLHKFEKELQRISEAYESLVKSTTK---------------RESLDKAMRNKLE--GEIRRL 540
Cdd:pfam01576 415 QELQARLSEserqraelAEKLSKLQSELESVSSLLNEAEGKNIKlskdvsslesqlqdtQELLQEETRQKLNlsTRLRQL 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 541 HDFNRDLRDRLETanrqlssreyEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRhieildqalsnAQAR 620
Cdd:pfam01576 495 EDERNSLQEQLEE----------EEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKR-----------LQRE 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 621 VIKLEEELREKQAYVEKVEK----LQQALTQLQSACEKREQ----MERRlrtwlERELDALRTQQKHGNGQPAnmpEYNA 692
Cdd:pfam01576 554 LEALTQQLEEKAAAYDKLEKtknrLQQELDDLLVDLDHQRQlvsnLEKK-----QKKFDQMLAEEKAISARYA---EERD 625
|
250
....*....|....*..
gi 530396371 693 PALLElVREKEERILAL 709
Cdd:pfam01576 626 RAEAE-AREKETRALSL 641
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
605-781 |
3.81e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 605 RHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTWLEREldALRTQQKHGngqp 684
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELE--ALEAELAEL---- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 685 anmpeynaPALLELVREKEERILALEADMTKWEQKYLEESTIRHFAMNAAATAAAERDTTIINHSRNGSYGESSLEAHIW 764
Cdd:COG4717 145 --------PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
170
....*....|....*..
gi 530396371 765 QEEEEVVQANRRCQDME 781
Cdd:COG4717 217 EAQEELEELEEELEQLE 233
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
479-723 |
4.03e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 479 EENRVLHQELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESldKAMRNKLEgEIRRLHDFNRDLRDRLETANRQL 558
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA--DEAKKKAE-EAKKAEEAKKKAEEAKKADEAKK 1477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 559 SSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEdhRRHIEILDQALSNAQARVIKLEEELReKQAYVEKV 638
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE--AKKADEAKKAEEAKKADEAKKAEEKK-KADELKKA 1554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 639 EKLQQAlTQLQSACEKREQMERRlRTWLERELDALRTQQKHGNGQPANMPEYNAPALLELVREKEERILALEADMTKWEQ 718
Cdd:PTZ00121 1555 EELKKA-EEKKKAEEAKKAEEDK-NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
....*
gi 530396371 719 KYLEE 723
Cdd:PTZ00121 1633 KKVEQ 1637
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
463-723 |
4.36e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 463 AFAIVERAQQMVEILTEENRVLHQELQGYYDNA-DKLHKFEKELQRISEAY----ESLVKSTTKRESLDKAMR------- 530
Cdd:TIGR00618 185 EFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYhERKQVLEKELKHLREALqqtqQSHAYLTQKREAQEEQLKkqqllkq 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 531 -----NKLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASED--- 602
Cdd:TIGR00618 265 lrariEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEeqr 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 603 ------HRRHIEILDQalsNAQARVIKleEELREKQAYVEKVEKLQQALT----QLQSACEKREQMERRLRTWLERELD- 671
Cdd:TIGR00618 345 rllqtlHSQEIHIRDA---HEVATSIR--EISCQQHTLTQHIHTLQQQKTtltqKLQSLCKELDILQREQATIDTRTSAf 419
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 530396371 672 -ALRTQQKHGNGQpaNMPEYNAPALLELVREKEERILALE-ADMTKWEQKYLEE 723
Cdd:TIGR00618 420 rDLQGQLAHAKKQ--QELQQRYAELCAAAITCTAQCEKLEkIHLQESAQSLKER 471
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
463-818 |
4.43e-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: 40.71 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 463 AFAIVERAQQMVEILTEENRVLHQELQGYYdNADKLHKFEKELQRISEAYESLVKSTTKRE-SLDKAMR--NKLEGEIRR 539
Cdd:COG5185 54 DSLRVTLRSVINVLDGLNYQNDVKKSESSV-KARKFLKEKKLDTKILQEYVNSLIKLPNYEwSADILISllYLYKSEIVA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 540 LHDFNRDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQA 619
Cdd:COG5185 133 LKDELIKVEKLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESET 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 620 RVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDaLRTQQKHGNGQPANMPEYNAPALLELV 699
Cdd:COG5185 213 GNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTD-LRLEKLGENAESSKRLNENANNLIKQF 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 700 REKEERILALEAD-MTKWEQKYLEESTIRHFAMNAAATAAAERDTTIINHSRNGSYGESSLEAHIW--QEEEEVVQANRR 776
Cdd:COG5185 292 ENTKEKIAEYTKSiDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEaiKEEIENIVGEVE 371
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 530396371 777 CQDMEYTIKNLHAKI---IEKDAMIKVLQQRSRKDAGKTDSSSLR 818
Cdd:COG5185 372 LSKSSEELDSFKDTIestKESLDEIPQNQRGYAQEILATLEDTLK 416
|
|
| Val_tRNA-synt_C |
pfam10458 |
Valyl tRNA synthetase tRNA binding arm; This domain is found at the C-terminus of Valyl tRNA ... |
584-649 |
4.93e-03 |
|
Valyl tRNA synthetase tRNA binding arm; This domain is found at the C-terminus of Valyl tRNA synthetases.
Pssm-ID: 431296 [Multi-domain] Cd Length: 66 Bit Score: 36.48 E-value: 4.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530396371 584 KEKEKLEMELAAVRTasedhrrHIEILDQALSN------AQARVIklEEELREKQAYVEKVEKLQQALTQLQ 649
Cdd:pfam10458 4 KERARLEKELAKLQK-------EIERVQGKLANpgfvakAPAEVV--EEEKAKLAELEEQAEKLRERLSKLG 66
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
526-666 |
6.40e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 526 DKAMrNKLEGEIRRLHDF-------NRDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRT 598
Cdd:PRK09039 52 DSAL-DRLNSQIAELADLlslerqgNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 599 ASEDHRRHIEILDQALSNAQARVIKLEEEL-------REKQAyvekveKLQQALTQLQSACEKR-EQMER-------RLR 663
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALdasekrdRESQA------KIADLGRRLNVALAQRvQELNRyrseffgRLR 204
|
...
gi 530396371 664 TWL 666
Cdd:PRK09039 205 EIL 207
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
585-711 |
7.41e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.04 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 585 EKEKLEMELAAVRTASEDHRRHIEildQALSNAQ--------ARVIKLEEELREKQAYVEK----VEKLQQALTQLQSac 652
Cdd:COG1842 52 NQKRLERQLEELEAEAEKWEEKAR---LALEKGRedlarealERKAELEAQAEALEAQLAQleeqVEKLKEALRQLES-- 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 530396371 653 eKREQMERRLRTWLERElDALRTQQKhGNGQPANMPEYNAPALLELVrekEERILALEA 711
Cdd:COG1842 127 -KLEELKAKKDTLKARA-KAAKAQEK-VNEALSGIDSDDATSALERM---EEKIEEMEA 179
|
|
| TMF_TATA_bd |
pfam12325 |
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil ... |
612-713 |
8.22e-03 |
|
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes. The proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMF1_TATA_bd is the most conserved part of the TMFs. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells. The Rab6-binding domain appears to be the same region as this C-terminal family.
Pssm-ID: 432481 [Multi-domain] Cd Length: 115 Bit Score: 37.14 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396371 612 QALSNAQARVIKLEEELREKQAYVEKVEK----LQQALTQLQSACEKREQMERRLRTwLERELDALrtQQKHGngqpanm 687
Cdd:pfam12325 12 QLVERLSSTIRRLEGELASLKEELARLEAqrdeARQEIVKLMKENEELKELKKELEE-LEKELKEL--EQRYE------- 81
|
90 100
....*....|....*....|....*.
gi 530396371 688 peynapALLELVREKEERILALEADM 713
Cdd:pfam12325 82 ------TTLELLGEKSEEVEELKADV 101
|
|
| |
