|
Name |
Accession |
Description |
Interval |
E-value |
| Angiomotin_C |
pfam12240 |
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ... |
605-811 |
1.25e-112 |
|
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: 344.44 E-value: 1.25e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 605 YVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKHGNGQPANMPEYNAPALLELVREKEERILALEADM 684
Cdd:pfam12240 1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 685 TKWEQKYLEESTIRHFAMNAAATAAAERDTTIINHSRNGSYgESSLeahiwqeEEEVVQANRRCQDMEYTIKNLHAKIIE 764
Cdd:pfam12240 81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSY-DSSF-------NEELLLANRRCQEMENRIKNLHAQILE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 22027646 765 KDAMIKVLQQRSRKDAGKTDSSSLRPARSVPSI-AAATGTHSRQTSLT 811
Cdd:pfam12240 153 KDAMIKVLQQRSRKDPGKTDQQSLRPARSVPSIsAAATGLHSRQTSLS 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
436-694 |
2.89e-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: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 436 AIVERAQQMVEILTEENRVLHQELQgyyDNADKLHKFEKELQRISEAYESLVKSttkresldkamRNKLEGEIRRLHDFN 515
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAE-----------LARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 516 RDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKL 595
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 596 EEELREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKhgngqpanmpeynapALLELVREKEE 675
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---------------EAAEEEAELEE 456
|
250
....*....|....*....
gi 22027646 676 RILALEADMTKWEQKYLEE 694
Cdd:COG1196 457 EEEALLELLAELLEEAALL 475
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
430-775 |
8.57e-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: 62.77 E-value: 8.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 430 LGPDAFAIVEraQQMV-EILT---EENRVLHQELQGyydnADKLHKFEKE-LQRISEAYESLVKSTTKRESLDKAMrNKL 504
Cdd:TIGR02168 133 LGKRSYSIIE--QGKIsEIIEakpEERRAIFEEAAG----ISKYKERRKEtERKLERTRENLDRLEDILNELERQL-KSL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 505 EGEIRRLHDFnRDLRDRLETANRQLSSREYEghedkaaeghyasqnkEFLKEKEKLEMELAAVRTASEDHRRHIEILDQA 584
Cdd:TIGR02168 206 ERQAEKAERY-KELKAELRELELALLVLRLE----------------ELREELEELQEELKEAEEELEELTAELQELEEK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 585 LSNAQARVIKLEEELREKQayvekveKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKHgNGQPANMPEYNAP 664
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE-LESKLDELAEELA 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 665 ALLELVREKEERILALEADMTKWEQKYLE-ESTIR----HFAMNAAATAAAERDTTIINH--SRNGSYGEsSLEAHIWQE 737
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEElESRLEeleeQLETLRSKVAQLELQIASLNNeiERLEARLE-RLEDRRERL 419
|
330 340 350
....*....|....*....|....*....|....*...
gi 22027646 738 EEEVVQANRRCQDMEytIKNLHAKIIEKDAMIKVLQQR 775
Cdd:TIGR02168 420 QQEIEELLKKLEEAE--LKELQAELEELEEELEELQEE 455
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
433-694 |
1.39e-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: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 433 DAFAIVERAQQMVEILTEENRVLHQELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRE-SLDKAMRNKLEGEIRRL 511
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEaRLSHSRIPEIQAELSKL 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 512 HDFNRDLRDRLETANRQLSSREYEGHedkaaeghYASQNKEFLKEK-EKLEMELAAVRTASEDHRRHIEILDQALSNAQA 590
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTLEKE--------YLEKEIQELQEQrIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 591 RVIKLEEELREKQAYVEKVEK----LQQALTQLQSACEKREQMERRLRTWLE---RELDALRTQQKHGNGQPANMPEYna 663
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLEaleEELSEIEDPKGEDEEIPEEELSL-- 953
|
250 260 270
....*....|....*....|....*....|.
gi 22027646 664 PALLELVREKEERILALEADMTKWEQKYLEE 694
Cdd:TIGR02169 954 EDVQAELQRVEEEIRALEPVNMLAIQEYEEV 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
436-682 |
2.52e-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: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 436 AIVERAQQMVEILTEENRVLHQELQGYYDN-----------ADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKL 504
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQleeleskldelAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 505 EGEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKAAEGHYA--SQNKEFLkEKEKLEMELAAVRTASEDHRRHIEILD 582
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRErlQQEIEEL-LKKLEEAELKELQAELEELEEELEELQ 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 583 QALSNAQARVIKLEEELREKQayvEKVEKLQQALTQLQSACEKREQMERRLRTwlerELDALRTQQKHGNGQPANMpeyn 662
Cdd:TIGR02168 454 EELERLEEALEELREELEEAE---QALDAAERELAQLQARLDSLERLQENLEG----FSEGVKALLKNQSGLSGIL---- 522
|
250 260
....*....|....*....|
gi 22027646 663 aPALLELVREKEERILALEA 682
Cdd:TIGR02168 523 -GVLSELISVDEGYEAAIEA 541
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
439-695 |
4.91e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 4.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 439 ERAQQmveiLTEENRVLHQELQGYydnadKLHKFEKELQRISEAYESLvksTTKRESLDKAMRnKLEGEIRRLHDFNRDL 518
Cdd:COG1196 213 ERYRE----LKEELKELEAELLLL-----KLRELEAELEELEAELEEL---EAELEELEAELA-ELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 519 RDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEE 598
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 599 LREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKhgngqpanmpeynapALLELVREKEERIL 678
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE---------------ALLERLERLEEELE 424
|
250
....*....|....*..
gi 22027646 679 ALEADMTKWEQKYLEES 695
Cdd:COG1196 425 ELEEALAELEEEEEEEE 441
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
464-648 |
1.08e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 464 DNADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEgEIRRLHDFNRDLRDRLETAnrqlssREYEGHEDKAAE 543
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAEYSWDEIDVASAE------REIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 544 ghyASQNKEFLKEkekLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQAltQLQSAC 623
Cdd:COG4913 680 ---LDASSDDLAA---LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALL 751
|
170 180 190
....*....|....*....|....*....|.
gi 22027646 624 EKR------EQMERRLRTWLERELDALRTQQ 648
Cdd:COG4913 752 EERfaaalgDAVERELRENLEERIDALRARL 782
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
433-672 |
1.42e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 433 DAFAIVERAQQMVEilteenrvlH-QELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESLDkAMRNKL-----EG 506
Cdd:COG4913 219 EEPDTFEAADALVE---------HfDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELE-YLRAALrlwfaQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 507 EIRRLHDFNRDLRDRLETANRQLS--SREYEGHEDK--AAEGHYASQNkefLKEKEKLEMELAAVRTASEDHRRHIEILD 582
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELErlEARLDALREEldELEAQIRGNG---GDRLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 583 QALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKHGNGQPANMPEYN 662
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRA---EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
250
....*....|
gi 22027646 663 APALLELVRE 672
Cdd:COG4913 443 LALRDALAEA 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
477-765 |
5.40e-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: 56.99 E-value: 5.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 477 QRISEAYESLVKSTTKRESLDKAmRNKLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKAAEGHYASQN------ 550
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKA-LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIaqlske 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 551 -KEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQsacEKREQM 629
Cdd:TIGR02168 756 lTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA---ELTLLNEEAANLR---ERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 630 ERRLRTWlERELDALRTQQKHGNGQPANmpeyNAPALLELVREKEErilaLEADMTKWEQKYLEESTIRHfamnAAATAA 709
Cdd:TIGR02168 830 ERRIAAT-ERRLEDLEEQIEELSEDIES----LAAEIEELEELIEE----LESELEALLNERASLEEALA----LLRSEL 896
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 22027646 710 AERDTTIINHSRNGSYGESSLEAhiwqEEEEVVQANRRCQDMEYTIKNLHAKIIEK 765
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEE----LREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
436-645 |
6.36e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 6.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 436 AIVERAQQMVEILTEE---NRVLHQELQ-GYYDNADK-LHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEG---E 507
Cdd:PRK03918 129 AIYIRQGEIDAILESDesrEKVVRQILGlDDYENAYKnLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvlrE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 508 IRRLHDFNRDLRDRLETANRQLssREYEGHEDKAAEghYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILD----- 582
Cdd:PRK03918 209 INEISSELPELREELEKLEKEV--KELEELKEEIEE--LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEekvke 284
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22027646 583 ----QALSNAQARVIKLEEELREKQAYVEK-VEKLQQALTQLQSACEKREQMERRLRtWLERELDALR 645
Cdd:PRK03918 285 lkelKEKAEEYIKLSEFYEEYLDELREIEKrLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELE 351
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
457-640 |
6.59e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 6.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 457 QELQGYYDNADKLHKFEKELQRISEAYESLvksttkRESLDKAmRNKLEGEIRRLhdfnRDLRDRLETANRQLSSREYEG 536
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKL------EEELDKA-FEELAETEKRL----EELRKELEELEKKYSEEEYEE 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 537 HEDkaaeghyasqnkeflkEKEKLEMELAAVRTASEDHRRHIEILDQALSnaqarviKLEEELREKQAYVEKVEKLQQAL 616
Cdd:PRK03918 664 LRE----------------EYLELSRELAGLRAELEELEKRREEIKKTLE-------KLKEELEEREKAKKELEKLEKAL 720
|
170 180
....*....|....*....|....
gi 22027646 617 TQLQsacEKREQMeRRLRTWLERE 640
Cdd:PRK03918 721 ERVE---ELREKV-KKYKALLKER 740
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
458-639 |
1.89e-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: 53.00 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 458 ELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDLRDRLETANRQL----SSRE 533
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 534 YEG--HEDKAAEghyasqnkeflKEKEKLEMELAAVRTAsedhrrhIEILDQALSNAQARVIKLEEELREKQA-YVEKVE 610
Cdd:COG1579 91 YEAlqKEIESLK-----------RRISDLEDEILELMER-------IEELEEELAELEAELAELEAELEEKKAeLDEELA 152
|
170 180 190
....*....|....*....|....*....|
gi 22027646 611 KLQQALTQLQSACEK-REQMERRLRTWLER 639
Cdd:COG1579 153 ELEAELEELEAEREElAAKIPPELLALYER 182
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
476-652 |
1.61e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 476 LQRISEAYESLVKSTTKRESLDKAMRNKLEGEIRRL---HDFNRDLRDRLETANRQLSS--REYEGHEDKAAEGHYASQN 550
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAeekEEEYAELQEELEELEEELEEleAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 551 KEFLKEKEKLEMELAAVRTASEDHRRHIEI---LDQALSNAQARVIKLEEELREKQAY------------VEKVEKLQQA 615
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEElreLEEELEELEAELAELQEELEELLEQlslateeelqdlAEELEELQQR 207
|
170 180 190
....*....|....*....|....*....|....*..
gi 22027646 616 LTQLQsacEKREQMERRLRTwLERELDALRTQQKHGN 652
Cdd:COG4717 208 LAELE---EELEEAQEELEE-LEEELEQLENELEAAA 240
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
467-675 |
3.25e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 467 DKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRnKLEGEIRRLHDFNRDLRDRLETanrqlSSREYEGHEDKAAEghy 546
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELKEEIEELEKELE-SLEGSKRKLEEKIRELEERIEE-----LKKEIEELEEKVKE--- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 547 asqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKR 626
Cdd:PRK03918 285 ----LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER 360
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 22027646 627 EQMERRLRTwLERELDALRTQQKhgngqpANMPEYNAPALLELVREKEE 675
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 ... |
464-648 |
1.33e-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: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 464 DNADKLHKFEKELQ-RISEAYESLVKSTTKRESLDKaMRNKLEGEIRRLHDFNR---DLRDRLETANRQLSSREYEGHED 539
Cdd:pfam01576 145 DQNSKLSKERKLLEeRISEFTSNLAEEEEKAKSLSK-LKNKHEAMISDLEERLKkeeKGRQELEKAKRKLEGESTDLQEQ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 540 KAaegHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTql 619
Cdd:pfam01576 224 IA---ELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLG-- 298
|
170 180
....*....|....*....|....*....
gi 22027646 620 qsacekrEQMErRLRTWLERELDALRTQQ 648
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 ... |
439-695 |
6.41e-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: 46.74 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 439 ERAQQMVEIlteENRVLHQELQgyydnadkLHKFEKELQRISEAYE---SLVKSTTKRESLDKAMRNKlEGEIRRLHDFN 515
Cdd:pfam10174 182 ERTRRIAEA---EMQLGHLEVL--------LDQKEKENIHLREELHrrnQLQPDPAKTKALQTVIEMK-DTKISSLERNI 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 516 RDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKeFLKEK--------EKLEMELAAVRTASE-------DHRRHIEI 580
Cdd:pfam10174 250 RDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSK-FMKNKidqlkqelSKKESELLALQTKLEtltnqnsDCKQHIEV 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 581 LDQALSNAQARVIKLEEE-------LREKQAYVEKVEKLQQALTQ----LQSACEKREQM----ERRLRTwLERELDALR 645
Cdd:pfam10174 329 LKESLTAKEQRAAILQTEvdalrlrLEEKESFLNKKTKQLQDLTEekstLAGEIRDLKDMldvkERKINV-LQKKIENLQ 407
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22027646 646 TQQKHGNGQPANMPEY------------NAPALLE-LVREKEERILALEADMTKWEQKYLEES 695
Cdd:pfam10174 408 EQLRDKDKQLAGLKERvkslqtdssntdTALTTLEeALSEKERIIERLKEQREREDRERLEEL 470
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
473-612 |
6.65e-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: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 473 EKELQRISEAYESLVKST-TKRESLDKAMRnKLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKAAEghyasqNK 551
Cdd:COG2433 387 EKELPEEEPEAEREKEHEeRELTEEEEEIR-RLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEE------RR 459
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22027646 552 EFLKEKE--KLEMELAAVRTASEDHRRHIEILdqalsnaQARVIKLEE----ELREKQAYVEKVEKL 612
Cdd:COG2433 460 EIRKDREisRLDREIERLERELEEERERIEEL-------KRKLERLKElwklEHSGELVPVKVVEKF 519
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
473-699 |
6.88e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.61 E-value: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 473 EKELQRISEAYESLVKSTTKRESLDKAMRnklegEIRRLHDFNRDLRDRLETANrqLSSREYEgheDKAAEghyasqnKE 552
Cdd:COG0497 154 EELLEEYREAYRAWRALKKELEELRADEA-----ERARELDLLRFQLEELEAAA--LQPGEEE---ELEEE-------RR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 553 FLKEKEKLemeLAAVRTAsedhrrhIEILDQALSNAQARVIKLEEELREKQAYVEK----VEKLQQALTQLQSACEK--- 625
Cdd:COG0497 217 RLSNAEKL---REALQEA-------LEALSGGEGGALDLLGQALRALERLAEYDPSlaelAERLESALIELEEAASElrr 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 626 -REQME---RRLRTWLEReLDALRT-QQKHGnGQPANMPEY--NAPALLELVREKEERILALEADMTKWEQKYLEE---- 694
Cdd:COG0497 287 yLDSLEfdpERLEEVEER-LALLRRlARKYG-VTVEELLAYaeELRAELAELENSDERLEELEAELAEAEAELLEAaekl 364
|
....*
gi 22027646 695 STIRH 699
Cdd:COG0497 365 SAARK 369
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
466-649 |
1.25e-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: 45.53 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 466 ADKLHKFEKELQRISE---AYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDLRDRLETANRQLSS---------RE 533
Cdd:COG4942 19 ADAAAEAEAELEQLQQeiaELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekeiaelrAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 534 YEGHEDKAAE---GHYASQNKEFLK------EKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQA 604
Cdd:COG4942 99 LEAQKEELAEllrALYRLGRQPPLAlllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 22027646 605 YVEKVEKLQQALTQLQSaceKREQMERRLRTWLERELDALRTQQK 649
Cdd:COG4942 179 LLAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQ 220
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
467-639 |
1.40e-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: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 467 DKLHKFEKELQRISEAYESLVKsttKRESLDKAMrNKLEGEIRRLHDFNRDLRDRLETANRQLSsreyeGHEDKAAEGHY 546
Cdd:cd07596 11 DYILKLEEQLKKLSKQAQRLVK---RRRELGSAL-GEFGKALIKLAKCEEEVGGELGEALSKLG-----KAAEELSSLSE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 547 ASQNKEFLKEKEKLEMEL---AAVRTASEDH---RRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQ----QAL 616
Cdd:cd07596 82 AQANQELVKLLEPLKEYLrycQAVKETLDDRadaLLTLQSLKKDLASKKAQLEKLKAAPGIKPA---KVEELEeeleEAE 158
|
170 180
....*....|....*....|...
gi 22027646 617 TQLQSACEKREQMERRLRTWLER 639
Cdd:cd07596 159 SALEEARKRYEEISERLKEELKR 181
|
|
| PilO |
COG3167 |
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures]; |
583-644 |
1.48e-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: 1.48e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22027646 583 QALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQsacEKREQMERRLRTwlERELDAL 644
Cdd:COG3167 46 EELEELEAEEAQLKQELEKKQAKAANLPALKAQLEELE---QQLGELLKQLPS--KAEVPAL 102
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
492-686 |
2.18e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 492 KRESLDKamrnkLEGEIRRLHDfnRDLRDRLETANRQLSS-----REYEGHEDKAAEGHYASQN-----KEFLKEKEKLE 561
Cdd:PRK02224 185 QRGSLDQ-----LKAQIEEKEE--KDLHERLNGLESELAEldeeiERYEEQREQARETRDEADEvleehEERREELETLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 562 MELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKREqmerrlrTWLEREL 641
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRD-------EELRDRL 330
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 22027646 642 DALRTQQKHGNGQPANMPEyNAPALLELVREKEERILALEADMTK 686
Cdd:PRK02224 331 EECRVAAQAHNEEAESLRE-DADDLEERAEELREEAAELESELEE 374
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
448-633 |
2.48e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 448 LTEENRvlhQELQGYYdnADKLHKFEKELQRISEAYESLVKSTTKresLDKAMRNklEGEIRRLH---DFNRDLRDRLET 524
Cdd:PRK03918 445 LTEEHR---KELLEEY--TAELKRIEKELKEIEEKERKLRKELRE---LEKVLKK--ESELIKLKelaEQLKELEEKLKK 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 525 ANRQ---LSSREYEGHEDKAA--EGHYASQNKEfLKEKEKLEMELAAVRTASED-HRRHIEILDQALSNAQARVIKLEEE 598
Cdd:PRK03918 515 YNLEeleKKAEEYEKLKEKLIklKGEIKSLKKE-LEKLEELKKKLAELEKKLDElEEELAELLKELEELGFESVEELEER 593
|
170 180 190
....*....|....*....|....*....|....*
gi 22027646 599 LREKQAYVEKVEKLQQALTQLQSACEKREQMERRL 633
Cdd:PRK03918 594 LKELEPFYNEYLELKDAEKELEREEKELKKLEEEL 628
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
547-792 |
2.67e-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: 44.37 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 547 ASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQsacEKR 626
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ---ELAALEAELAELE---KEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 627 EQMERRLRTWLERELDALRTQQKHG---------NGQPANMPEYNAPALLELVREKEERILALEADMTKWEQKYLEESTI 697
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 698 RHFAMNAAATAAAERDttiinhsrngsygesSLEAHIWQEEEEVVQANRRCQDMEYTIKNLHAKIIEKDAMIKVLQQRSR 777
Cdd:COG4942 173 RAELEALLAELEEERA---------------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
250
....*....|....*
gi 22027646 778 KDAGKTDSSSLRPAR 792
Cdd:COG4942 238 AAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
439-614 |
3.40e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 439 ERAQQMVEILTEENRVLHQELQGYYDNADKLHKFEKELQRISEAYESLvksttkresldKAMRNKLEGEIRRLHDFNR-- 516
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL-----------REELEKLEKLLQLLPLYQEle 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 517 DLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELA--------AVRTASEDHRRH---IEILDQAL 585
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqlslateeELQDLAEELEELqqrLAELEEEL 215
|
170 180
....*....|....*....|....*....
gi 22027646 586 SNAQARVIKLEEELREKQAYVEKVEKLQQ 614
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEER 244
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
445-629 |
3.51e-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: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 445 VEILTEENRVLHQELQGYYDNADKLHKFEKEL---------------QRISEAYESLVKSTTKResldkamRNKLEgEIR 509
Cdd:cd00176 35 VEALLKKHEALEAELAAHEERVEALNELGEQLieeghpdaeeiqerlEELNQRWEELRELAEER-------RQRLE-EAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 510 RLHDFNRDLRD---RLETANRQLSSREYEGHEDKAaeghyasqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALS 586
Cdd:cd00176 107 DLQQFFRDADDleqWLEEKEAALASEDLGKDLESV---------EELLKKHKELEEELEAHEPRLKSLNELAEELLEEGH 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 22027646 587 NAQARVIKleeelrekqayvEKVEKLQQALTQLQSACEKREQM 629
Cdd:cd00176 178 PDADEEIE------------EKLEELNERWEELLELAEERQKK 208
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
443-782 |
3.71e-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: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 443 QMVEILTEENRVLHQELQGYYDNADKLHKFEKELQRISEAYESL-VKSTTKRESLDKAMRNKLEGEIRRlhdfnrDLRDR 521
Cdd:TIGR02169 146 DFISMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLdLIIDEKRQQLERLRREREKAERYQ------ALLKE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 522 LetanrqlssREYEGhedkaaeghyasqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELRE 601
Cdd:TIGR02169 220 K---------REYEG--------------YELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 602 KQAYV------------EKVEKLQQALTQLQ---SACEKR-EQMERRLRTwLERELDALRTQQKHGNGQpanmpeynapa 665
Cdd:TIGR02169 277 LNKKIkdlgeeeqlrvkEKIGELEAEIASLErsiAEKERElEDAEERLAK-LEAEIDKLLAEIEELERE----------- 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 666 LLELVREKE---ERILALEADMTKWEQKYLEESTirHFAMNAAATAAAERDTTIINHSRNgsygesSLEAHIWQEEEEVV 742
Cdd:TIGR02169 345 IEEERKRRDkltEEYAELKEELEDLRAELEEVDK--EFAETRDELKDYREKLEKLKREIN------ELKRELDRLQEELQ 416
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 22027646 743 QANRRCQDMEYTIKNLHAKIIEKDAMIKVLQQRSRKDAGK 782
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK 456
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
436-629 |
3.83e-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: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 436 AIVERAQQMVEILTEENRVLHQE-LQGYYDNADKLHKFEKELQRISEAYESLVKS----TTKRESLDKAMRNKLEGEIRR 510
Cdd:pfam12128 315 AAVAKDRSELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERLKALTGKhqdvTAKYNRRRSKIKEQNNRDIAG 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 511 LHDfnrDLRDRLETANRQLSSRE--YEGHEDKAAEGHYAsQNKEFLKEKEKLEMELAAVR------TASEDHRRHIEILD 582
Cdd:pfam12128 395 IKD---KLAKIREARDRQLAVAEddLQALESELREQLEA-GKLEFNEEEYRLKSRLGELKlrlnqaTATPELLLQLENFD 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 22027646 583 QALSNAQ-------ARVIKLEEELRE-KQAYVEKVEKLQQA---LTQLQSACEKREQM 629
Cdd:pfam12128 471 ERIERAReeqeaanAEVERLQSELRQaRKRRDQASEALRQAsrrLEERQSALDELELQ 528
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
439-699 |
4.03e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 439 ERAQQMVEILTEENRVLHQELQGYydnadKLHKFEKELQRISEAYESLvkstTKRESLDKAMRNKLEGEIRRLhdfnRDL 518
Cdd:PRK03918 361 HELYEEAKAKKEELERLKKRLTGL-----TPEKLEKELEELEKAKEEI----EEEISKITARIGELKKEIKEL----KKA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 519 RDRLETANRQ--LSSREYEGHEDKAAEGHY-------ASQNKEFLKEKEKLEMELAAVRTASEDHRRHI---EILDQaLS 586
Cdd:PRK03918 428 IEELKKAKGKcpVCGRELTEEHRKELLEEYtaelkriEKELKEIEEKERKLRKELRELEKVLKKESELIklkELAEQ-LK 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 587 NAQAR-----VIKLEEELREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTwLERELDALRTQQKHGNGQPANMPey 661
Cdd:PRK03918 507 ELEEKlkkynLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE-LEKKLDELEEELAELLKELEELG-- 583
|
250 260 270
....*....|....*....|....*....|....*...
gi 22027646 662 napalLELVREKEERILALEadmtKWEQKYLEESTIRH 699
Cdd:PRK03918 584 -----FESVEELEERLKELE----PFYNEYLELKDAEK 612
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
553-691 |
4.62e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 553 FLKEKEKLEMELAAVRTASEDHRRHIEILDQAlsnaQARVIKLEEELREKQAYVEKVEKLQQALT----------QLQSA 622
Cdd:COG4717 69 NLKELKELEEELKEAEEKEEEYAELQEELEEL----EEELEELEAELEELREELEKLEKLLQLLPlyqelealeaELAEL 144
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22027646 623 CEKREQMERRLRTW--LERELDALRTQQKHGNGQPANMPEYNAPALLELVREKEERILALEADMTKWEQKY 691
Cdd:COG4717 145 PERLEELEERLEELreLEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
454-694 |
4.93e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.94 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 454 VLHQELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRnKLEGEIRRLHDFNRDLRDRLEtanrqlssrE 533
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK-KILAEDEKLLDEKKQFEKIAE---------E 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 534 YEGHEDkaaEGHYASQNKEflKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEE-----LREKQAYVEK 608
Cdd:pfam05483 434 LKGKEQ---ELIFLLQARE--KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHcdkllLENKELTQEA 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 609 VEKLQQALTQLQSACEKREQMERRLR---------TWLERELDALRTQQKHGNGQ---PANMPEYNAPALLELVREKEER 676
Cdd:pfam05483 509 SDMTLELKKHQEDIINCKKQEERMLKqienleekeMNLRDELESVREEFIQKGDEvkcKLDKSEENARSIEYEVLKKEKQ 588
|
250 260
....*....|....*....|....
gi 22027646 677 ILALEADMTKWEQ------KYLEE 694
Cdd:pfam05483 589 MKILENKCNNLKKqienknKNIEE 612
|
|
| PRK10361 |
PRK10361 |
DNA recombination protein RmuC; Provisional |
541-651 |
5.50e-04 |
|
DNA recombination protein RmuC; Provisional
Pssm-ID: 182409 [Multi-domain] Cd Length: 475 Bit Score: 43.43 E-value: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 541 AAEGHYASQNKEFLKEKEKLEMELAAVR---TASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKV-----EKL 612
Cdd:PRK10361 22 FASYQHAQQKAEQLAEREEMVAELSAAKqqiTQSEHWRAECELLNNEVRSLQSINTSLEADLREVTTRMEAAqqhadDKI 101
|
90 100 110
....*....|....*....|....*....|....*....
gi 22027646 613 QQALTQLQSACEKREQMERRLRTWLERELDALRTQQKHG 651
Cdd:PRK10361 102 RQMINSEQRLSEQFENLANRIFEHSNRRVDEQNRQSLNS 140
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
548-694 |
7.89e-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: 42.22 E-value: 7.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 548 SQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQSAcekRE 627
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA---RIKKYEEQLGNVRNN---KE 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22027646 628 QMErrlrtwLERELDALRTQQKHGngqpanmpEYNAPALLELVREKEERILALEADMTKWEQKYLEE 694
Cdd:COG1579 91 YEA------LQKEIESLKRRISDL--------EDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
548-811 |
1.07e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 548 SQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEEL----REKQAYVEKVEKLQQALTQLQSAC 623
Cdd:COG4372 52 EELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELeslqEEAEELQEELEELQKERQDLEQQR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 624 EKREQMERRLRTWL---ERELDALRTQQKHGNGQ-------PANMPEYNAPALLELVREKEERILALEADMTKWEQKYLE 693
Cdd:COG4372 132 KQLEAQIAELQSEIaerEEELKELEEQLESLQEElaaleqeLQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIES 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 694 ESTIRHFAMNAAATAAAER----DTTIINHSRNGSYGESSLEAHIWQEEEEVVQANRRCQDMEYTIKNLHAKIIEKDAMI 769
Cdd:COG4372 212 LPRELAEELLEAKDSLEAKlglaLSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEA 291
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 22027646 770 KVLQQRSRKDAGKTDSSSLRPARSVPSIAAATGTHSRQTSLT 811
Cdd:COG4372 292 ALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
438-625 |
2.28e-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: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 438 VERAQQMVEILTEENRVLHQELQGYYDNADKLHKFEKELQR-ISEAYESLVKSTTKRESLDKAMRNkLEGEIRRLHDFNR 516
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESeLEALLNERASLEEALALLRSELEE-LSEELRELESKRS 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 517 DLRDRLETANRQLSS--REYEGHEDKAAeghyasQNKEFLKEKEKLEMELAAvrtasedhrRHIEILDQALSNAQARVIK 594
Cdd:TIGR02168 912 ELRRELEELREKLAQleLRLEGLEVRID------NLQERLSEEYSLTLEEAE---------ALENKIEDDEEEARRRLKR 976
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 22027646 595 LE-----------------EELREKQAYVEK-VEKLQQALTQLQSACEK 625
Cdd:TIGR02168 977 LEnkikelgpvnlaaieeyEELKERYDFLTAqKEDLTEAKETLEEAIEE 1025
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
466-648 |
2.63e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 466 ADKLHKFEKELQRISEAYESLVKSTtkreSLDKAMRNKLEGEIRRLHDFNRDLRDRLETANRQLS--SREYEGHEDKAAE 543
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEA----GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQahNEEAESLREDADD 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 544 ghYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQAL----------------------------SNAQARVIKL 595
Cdd:PRK02224 354 --LEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIeelrerfgdapvdlgnaedfleelreerDELREREAEL 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22027646 596 EEELREKQAYVEKVEKLQ---------QALTQLQSAC---EKREQMERrlrtwLERELDALRTQQ 648
Cdd:PRK02224 432 EATLRTARERVEEAEALLeagkcpecgQPVEGSPHVEtieEDRERVEE-----LEAELEDLEEEV 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
441-639 |
2.78e-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: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 441 AQQMVEILTEENRVLHQELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDLRD 520
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 521 RLETANRQLSSREY-----------------EGHEDKAAEGHYASQNKEFLKEK-EKLEMELAAVRTASEDHRRHIEILD 582
Cdd:COG4942 98 ELEAQKEELAELLRalyrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQaEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22027646 583 QALSNAQARVIKLEEELREKQayvEKVEKLQQALTQLQSACEKREQMERRLRTWLER 639
Cdd:COG4942 178 ALLAELEEERAALEALKAERQ---KLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
457-680 |
3.72e-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: 41.31 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 457 QELQGYYDN--------ADKLHKFEKELQRISEAYESLVKSTTK---------------RESLDKAMRNKLE--GEIRRL 511
Cdd:pfam01576 415 QELQARLSEserqraelAEKLSKLQSELESVSSLLNEAEGKNIKlskdvsslesqlqdtQELLQEETRQKLNlsTRLRQL 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 512 HDFNRDLRDRLETanrqlssreyEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRhieildqalsnAQAR 591
Cdd:pfam01576 495 EDERNSLQEQLEE----------EEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKR-----------LQRE 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 592 VIKLEEELREKQAYVEKVEK----LQQALTQLQSACEKREQ----MERRlrtwlERELDALRTQQKHGNGQPAnmpEYNA 663
Cdd:pfam01576 554 LEALTQQLEEKAAAYDKLEKtknrLQQELDDLLVDLDHQRQlvsnLEKK-----QKKFDQMLAEEKAISARYA---EERD 625
|
250
....*....|....*..
gi 22027646 664 PALLElVREKEERILAL 680
Cdd:pfam01576 626 RAEAE-AREKETRALSL 641
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
576-752 |
3.74e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 576 RHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTWLEREldALRTQQKHGngqp 655
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELE--ALEAELAEL---- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 656 anmpeynaPALLELVREKEERILALEADMTKWEQKYLEESTIRHFAMNAAATAAAERDTTIINHSRNGSYGESSLEAHIW 735
Cdd:COG4717 145 --------PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
170
....*....|....*..
gi 22027646 736 QEEEEVVQANRRCQDME 752
Cdd:COG4717 217 EAQEELEELEEELEQLE 233
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
434-789 |
4.50e-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: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 434 AFAIVERAQQMVEILTEENRVLHQELQGYYdNADKLHKFEKELQRISEAYESLVKSTTKRE-SLDKAMR--NKLEGEIRR 510
Cdd:COG5185 54 DSLRVTLRSVINVLDGLNYQNDVKKSESSV-KARKFLKEKKLDTKILQEYVNSLIKLPNYEwSADILISllYLYKSEIVA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 511 LHDFNRDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQA 590
Cdd:COG5185 133 LKDELIKVEKLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESET 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 591 RVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDaLRTQQKHGNGQPANMPEYNAPALLELV 670
Cdd:COG5185 213 GNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTD-LRLEKLGENAESSKRLNENANNLIKQF 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 671 REKEERILALEAD-MTKWEQKYLEESTIRHFAMNAAATAAAERDTTIINHSRNGSYGESSLEAHIW--QEEEEVVQANRR 747
Cdd:COG5185 292 ENTKEKIAEYTKSiDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEaiKEEIENIVGEVE 371
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 22027646 748 CQDMEYTIKNLHAKI---IEKDAMIKVLQQRSRKDAGKTDSSSLR 789
Cdd:COG5185 372 LSKSSEELDSFKDTIestKESLDEIPQNQRGYAQEILATLEDTLK 416
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
450-694 |
4.76e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 450 EENRVLHQELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESldKAMRNKLEgEIRRLHDFNRDLRDRLETANRQL 529
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA--DEAKKKAE-EAKKAEEAKKKAEEAKKADEAKK 1477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 530 SSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEdhRRHIEILDQALSNAQARVIKLEEELReKQAYVEKV 609
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE--AKKADEAKKAEEAKKADEAKKAEEKK-KADELKKA 1554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 610 EKLQQAlTQLQSACEKREQMERRlRTWLERELDALRTQQKHGNGQPANMPEYNAPALLELVREKEERILALEADMTKWEQ 689
Cdd:PTZ00121 1555 EELKKA-EEKKKAEEAKKAEEDK-NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
....*
gi 22027646 690 KYLEE 694
Cdd:PTZ00121 1633 KKVEQ 1637
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
434-694 |
5.43e-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: 40.72 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 434 AFAIVERAQQMVEILTEENRVLHQELQGYYDNA-DKLHKFEKELQRISEAY----ESLVKSTTKRESLDKAMR------- 501
Cdd:TIGR00618 185 EFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYhERKQVLEKELKHLREALqqtqQSHAYLTQKREAQEEQLKkqqllkq 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 502 -----NKLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASED--- 573
Cdd:TIGR00618 265 lrariEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEeqr 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 574 ------HRRHIEILDQalsNAQARVIKleEELREKQAYVEKVEKLQQALT----QLQSACEKREQMERRLRTWLERELD- 642
Cdd:TIGR00618 345 rllqtlHSQEIHIRDA---HEVATSIR--EISCQQHTLTQHIHTLQQQKTtltqKLQSLCKELDILQREQATIDTRTSAf 419
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 22027646 643 -ALRTQQKHGNGQpaNMPEYNAPALLELVREKEERILALE-ADMTKWEQKYLEE 694
Cdd:TIGR00618 420 rDLQGQLAHAKKQ--QELQQRYAELCAAAITCTAQCEKLEkIHLQESAQSLKER 471
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
497-637 |
6.29e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 497 DKAMrNKLEGEIRRLHDF-------NRDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRT 569
Cdd:PRK09039 52 DSAL-DRLNSQIAELADLlslerqgNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 570 ASEDHRRHIEILDQALSNAQARVIKLEEEL-------REKQAyvekveKLQQALTQLQSACEKR-EQMER-------RLR 634
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALdasekrdRESQA------KIADLGRRLNVALAQRvQELNRyrseffgRLR 204
|
...
gi 22027646 635 TWL 637
Cdd:PRK09039 205 EIL 207
|
|
| Val_tRNA-synt_C |
pfam10458 |
Valyl tRNA synthetase tRNA binding arm; This domain is found at the C-terminus of Valyl tRNA ... |
555-620 |
6.82e-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: 36.09 E-value: 6.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22027646 555 KEKEKLEMELAAVRTasedhrrHIEILDQALSN------AQARVIklEEELREKQAYVEKVEKLQQALTQLQ 620
Cdd:pfam10458 4 KERARLEKELAKLQK-------EIERVQGKLANpgfvakAPAEVV--EEEKAKLAELEEQAEKLRERLSKLG 66
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
556-682 |
8.44e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 38.65 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 556 EKEKLEMELAAVRTASEDHRRHIEildQALSNAQ--------ARVIKLEEELREKQAYVEK----VEKLQQALTQLQSac 623
Cdd:COG1842 52 NQKRLERQLEELEAEAEKWEEKAR---LALEKGRedlarealERKAELEAQAEALEAQLAQleeqVEKLKEALRQLES-- 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 22027646 624 eKREQMERRLRTWLERElDALRTQQKhGNGQPANMPEYNAPALLELVrekEERILALEA 682
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 ... |
583-684 |
9.11e-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: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027646 583 QALSNAQARVIKLEEELREKQAYVEKVEK----LQQALTQLQSACEKREQMERRLRTwLERELDALrtQQKHGngqpanm 658
Cdd:pfam12325 12 QLVERLSSTIRRLEGELASLKEELARLEAqrdeARQEIVKLMKENEELKELKKELEE-LEKELKEL--EQRYE------- 81
|
90 100
....*....|....*....|....*.
gi 22027646 659 peynapALLELVREKEERILALEADM 684
Cdd:pfam12325 82 ------TTLELLGEKSEEVEELKADV 101
|
|
| |
