|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1285-1805 |
2.03e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.32 E-value: 2.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1285 IRAEQQTALQRLREEAETLQKAERASLEQKSRRA------LEQLREQL-----EAEERSAQAALRAEKEAEKEATLLQLR 1353
Cdd:COG1196 194 ILGELERQLEPLERQAEKAERYRELKEELKELEAellllkLRELEAELeeleaELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1354 EQLE--GERREAVAGLEKKHSTELEQLCSSLEAKHREVISNLQKKIEgaQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQ 1431
Cdd:COG1196 274 LELEelELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE--LEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1432 ELSSLLRDKRQEVEREHErkmDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELEsvRQEQDQQL 1511
Cdd:COG1196 352 ELEEAEAELAEAEEALLE---AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER--LEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1512 EDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEH--- 1588
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYegf 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1589 ------THLLESKQQLRRAIDDLRVRRVELESQ---------VDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNA 1653
Cdd:COG1196 507 legvkaALLLAGLRGLAGAVAVLIGVEAAYEAAleaalaaalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARA 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1654 PPHPEPGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKEFLVR-------QTRSMRRRQT 1726
Cdd:COG1196 587 ALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVtlegeggSAGGSLTGGS 666
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798727 1727 ALKAAQQHWRHELASAQEVDEDLPGTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLESSLLEEVSDED 1805
Cdd:COG1196 667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1292-1646 |
4.97e-18 |
|
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: 91.27 E-value: 4.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1292 ALQRLREEAETLQKAERA---------SLEQKSRRAlEQLREqLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERRE 1362
Cdd:TIGR02168 177 TERKLERTRENLDRLEDIlnelerqlkSLERQAEKA-ERYKE-LKAELRELELALLVLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1363 avaglEKKHSTELEQLCSSLEAkHREVISNLQKKIEGAQQKeeaqlqesLGRAEQRTHQKVHQVIEYEQELSSLLRD-KR 1441
Cdd:TIGR02168 255 -----LEELTAELQELEEKLEE-LRLEVSELEEEIEELQKE--------LYALANEISRLEQQKQILRERLANLERQlEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1442 QEVEREH-ERKMDKMKEEhwqemaeareryEAEERKQRADLLGHLTGELERLRRAHE--RELESVRQEQDQQLEDLRRRH 1518
Cdd:TIGR02168 321 LEAQLEElESKLDELAEE------------LAELEEKLEELKEELESLEAELEELEAelEELESRLEELEEQLETLRSKV 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1519 RDQERKLQDLEAELSSrtkdVKARLAQLNVQEENMRKEKQLLLDAQRQAALEK--EEATATRRHLEEAKKEHTHLLESKQ 1596
Cdd:TIGR02168 389 AQLELQIASLNNEIER----LEARLERLEDRRERLQQEIEELLKKLEEAELKElqAELEELEEELEELQEELERLEEALE 464
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1597 QLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKE 1646
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1288-1658 |
4.86e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 84.58 E-value: 4.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1288 EQQTALQRLREEAETLQkAERASLEQKsRRALEQLREQLEAEERSAQAALRAEKEAEKEAtLLQLREQLEGERREAvagl 1367
Cdd:COG4913 285 FAQRRLELLEAELEELR-AELARLEAE-LERLEARLDALREELDELEAQIRGNGGDRLEQ-LEREIERLERELEER---- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1368 eKKHSTELEQLCSSLEAK---HREVISNLQKKIEGAQQK---EEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLR--- 1438
Cdd:COG4913 358 -ERRRARLEALLAALGLPlpaSAEEFAALRAEAAALLEAleeELEALEEALAEAEAALRDLRRELRELEAEIASLERrks 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1439 --DKRQ-------------------------EVEREHE----------------------------RKMDKMKEEH---W 1460
Cdd:COG4913 437 niPARLlalrdalaealgldeaelpfvgeliEVRPEEErwrgaiervlggfaltllvppehyaaalRWVNRLHLRGrlvY 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1461 QEMAEARERYEAEERKQRA-----------------DLLGHL--------TGELERLRRA--------HERELesvRQEQ 1507
Cdd:COG4913 517 ERVRTGLPDPERPRLDPDSlagkldfkphpfrawleAELGRRfdyvcvdsPEELRRHPRAitragqvkGNGTR---HEKD 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1508 DQQleDLRRRH---RDQERKLQDLEAE---LSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEeATATRRHL 1581
Cdd:COG4913 594 DRR--RIRSRYvlgFDNRAKLAALEAElaeLEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-VASAEREI 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1582 EEAKKEHTHLLESK---QQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPE 1658
Cdd:COG4913 671 AELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1231-1640 |
1.27e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.45 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1231 QQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERAS 1310
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1311 LEQKS--RRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKHSTELEQLCSSL---EAK 1385
Cdd:COG1196 456 EEEEAllELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLigvEAA 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1386 HREVI---------SNLQKKIEGAQQKEEAQLQESLGRAE---------QRTHQKVHQVIEYEQELSSLLRDKRQEVERE 1447
Cdd:COG1196 536 YEAALeaalaaalqNIVVEDDEVAAAAIEYLKAAKAGRATflpldkiraRAALAAALARGAIGAAVDLVASDLREADARY 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1448 HERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLT-----GELERLRRAHERELESVRQEQDQQLEDLRRRHRDQE 1522
Cdd:COG1196 616 YVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEggsagGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL 695
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1523 RKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESK-QQLRRA 1601
Cdd:COG1196 696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERElERLERE 775
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1958798727 1602 IDDL-RV-------------RRVELESQVDQLQTQSQRLQKHVSSLEAEVQRK 1640
Cdd:COG1196 776 IEALgPVnllaieeyeeleeRYDFLSEQREDLEEARETLEEAIEEIDRETRER 828
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1230-1814 |
2.02e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 82.88 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1230 YQQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQRLACLR--------AQVQSSTEA--FENQIRAEQQTALQRLR-- 1297
Cdd:PTZ00121 1081 FDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKkaedarkaEEARKAEDArkAEEARKAEDAKRVEIARka 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1298 EEA---ETLQKAERASLEQKSRRALEQLR--EQLEAEE-RSAQAALRAEKEAEKEatllQLREQLEGERREAVAGLEKKH 1371
Cdd:PTZ00121 1161 EDArkaEEARKAEDAKKAEAARKAEEVRKaeELRKAEDaRKAEAARKAEEERKAE----EARKAEDAKKAEAVKKAEEAK 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1372 STEleqlcssLEAKHREVISNLQ--KKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVER--- 1446
Cdd:PTZ00121 1237 KDA-------EEAKKAEEERNNEeiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEakk 1309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1447 --EHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGE--LERLRRAHER-ELESVRQEQDQQLEDLRRRHRDQ 1521
Cdd:PTZ00121 1310 kaEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEaaADEAEAAEEKaEAAEKKKEEAKKKADAAKKKAEE 1389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1522 ERKLQDLEA---ELSSRTKDVKARLAQLNVQEENMRK-EKQLLLDAQRQAALEKEEATATRRHLEEAKKEHThlLESKQQ 1597
Cdd:PTZ00121 1390 KKKADEAKKkaeEDKKKADELKKAAAAKKKADEAKKKaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEE--AKKKAE 1467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1598 LRRAIDDLRvRRVELESQVDQLQTQSQRLQKHVSSLE--AEVQRKQNILK--EMAAETNAPPHPEPGLHIEDLRKSLGTN 1673
Cdd:PTZ00121 1468 EAKKADEAK-KKAEEAKKADEAKKKAEEAKKKADEAKkaAEAKKKADEAKkaEEAKKADEAKKAEEAKKADEAKKAEEKK 1546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1674 ENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPGTK 1753
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958798727 1754 VLENVRKNLDEETKHLDEMKsamRKGHDLlkKKEEKLNQLESSLLEEVSDEDTLKGSSIKK 1814
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEK---KKAEEL--KKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1297-1653 |
1.46e-14 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 79.40 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1297 REEAETLQKAERASLEQKSRRALEQL--REQLEAEERSAQAALraekeaEKEATLLQLREQLEGERREavaglekkhstE 1374
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVerRRKLEEAEKARQAEM------DRQAAIYAEQERMAMERER-----------E 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1375 LEQLcsSLEAKHREVISNLQKKIegAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSsLLRDKRQEVEREHERKMDK 1454
Cdd:pfam17380 350 LERI--RQEERKRELERIRQEEI--AMEISRMRELERLQMERQQKNERVRQELEAARKVK-ILEEERQRKIQQQKVEMEQ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1455 MKEEhwQEmaeareryeaeERKQRadllghltgELERLRRAHERELESVRQEQ---DQQLEDLRRRHRDQERKLQDLEAE 1531
Cdd:pfam17380 425 IRAE--QE-----------EARQR---------EVRRLEEERAREMERVRLEEqerQQQVERLRQQEEERKRKKLELEKE 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1532 lssrtkdvkarlaqlnvqeenmrKEKQLLLDAQRQAALEKEEATATRRHLEEAKK--------EHTHLLESKQQLRRAID 1603
Cdd:pfam17380 483 -----------------------KRDRKRAEEQRRKILEKELEERKQAMIEEERKrkllekemEERQKAIYEEERRREAE 539
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1604 DLRVRRVELESQvDQLQTQSQRLQKHVSSLEAeVQRKQNILKEMAAETNA 1653
Cdd:pfam17380 540 EERRKQQEMEER-RRIQEQMRKATEERSRLEA-MEREREMMRQIVESEKA 587
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1270-1633 |
7.13e-14 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 77.69 E-value: 7.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1270 LRAQVQSSTEAfenqiRAEQQTALQRLREEAETLqKAERASLEQksrrALEQLREQLEaeerSAQAALR-AEKEAEKEAT 1348
Cdd:PRK04863 291 LRRELYTSRRQ-----LAAEQYRLVEMARELAEL-NEAESDLEQ----DYQAASDHLN----LVQTALRqQEKIERYQAD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1349 LLQLREQLEgERREAVAGL--------EKKHSTELEQLCSsleakhREVISNLQKKIEgAQQKEEAQLQES---LGRAEQ 1417
Cdd:PRK04863 357 LEELEERLE-EQNEVVEEAdeqqeeneARAEAAEEEVDEL------KSQLADYQQALD-VQQTRAIQYQQAvqaLERAKQ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1418 RTHQ---KVHQVIEYEQELssllRDKRQEVE---REHERKMDKMKEEHWQemaeareryeaeeRKQRADLLGHLTGELER 1491
Cdd:PRK04863 429 LCGLpdlTADNAEDWLEEF----QAKEQEATeelLSLEQKLSVAQAAHSQ-------------FEQAYQLVRKIAGEVSR 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1492 ----------LRRAHERELESVRQEQ-DQQLEDLRRRHRDQER--------------------KLQDLEAELSSRTKDVK 1540
Cdd:PRK04863 492 seawdvarelLRRLREQRHLAEQLQQlRMRLSELEQRLRQQQRaerllaefckrlgknlddedELEQLQEELEARLESLS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1541 ARLAQLNVQEENMR-KEKQLLLDAQRQAALEKE--EATATRRHLEEAKKEHthlLESKQQLRRAIDDLRVRRVELESQVD 1617
Cdd:PRK04863 572 ESVSEARERRMALRqQLEQLQARIQRLAARAPAwlAAQDALARLREQSGEE---FEDSQDVTEYMQQLLERERELTVERD 648
|
410
....*....|....*.
gi 1958798727 1618 QLQTQSQRLQKHVSSL 1633
Cdd:PRK04863 649 ELAARKQALDEEIERL 664
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1388-1800 |
1.45e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.64 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1388 EVISNLQKKIEGAQQ--KEEAQLQESLGRAEQRTHQKVHQVieyeQELSSLLRDKRQEVE--REHERKMDKMKEEhwqem 1463
Cdd:PRK03918 169 EVIKEIKRRIERLEKfiKRTENIEELIKEKEKELEEVLREI----NEISSELPELREELEklEKEVKELEELKEE----- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1464 aeareryEAEERKQRADLLGHLTGELERLR---------RAHERELESVRQEQDQ---------QLEDLRRRHRDQERKL 1525
Cdd:PRK03918 240 -------IEELEKELESLEGSKRKLEEKIReleerieelKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1526 QDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQR------------------QAALEKEEATATRRHLEEAKKE 1587
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKrleeleerhelyeeakakKEELERLKKRLTGLTPEKLEKE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1588 HTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKH-----VSSLEAEVQRKQNILKEMAAEtnapphpepglh 1662
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEEYTAE------------ 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1663 IEDLRKSLGTNENQEvsSSLSLSKEGIDLSMDSVRHFLSAEGVA--VRSAKEFLvrqtrsmrrRQTALKAAQQHWRhela 1740
Cdd:PRK03918 461 LKRIEKELKEIEEKE--RKLRKELRELEKVLKKESELIKLKELAeqLKELEEKL---------KKYNLEELEKKAE---- 525
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1741 SAQEVDEDLPGtkvLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLESSLLEE 1800
Cdd:PRK03918 526 EYEKLKEKLIK---LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1354-1867 |
1.63e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 76.31 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1354 EQLEGERREAVAGLEKKHSTELEQLCSsleaKHREVISNLQKKIEGAQQKE---EAQLQESLGRAEQRTHQKVHQVIEYE 1430
Cdd:pfam15921 248 EALKSESQNKIELLLQQHQDRIEQLIS----EHEVEITGLTEKASSARSQAnsiQSQLEIIQEQARNQNSMYMRQLSDLE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1431 QELSSLlRDKRQEVEREHERKMDKMKEEhwQEMAEARERYEAEERKQRADLLGHLTGELERL-RRAHERELE-SVRQEQD 1508
Cdd:pfam15921 324 STVSQL-RSELREAKRMYEDKIEELEKQ--LVLANSELTEARTERDQFSQESGNLDDQLQKLlADLHKREKElSLEKEQN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1509 QQLED-----------LRRRHRDQERKLQDLEAELSSRTKDVKARLAQ--LNVQEENMRKEKQLLLDAQRQAALEK---- 1571
Cdd:pfam15921 401 KRLWDrdtgnsitidhLRRELDDRNMEVQRLEALLKAMKSECQGQMERqmAAIQGKNESLEKVSSLTAQLESTKEMlrkv 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1572 -EEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEaEVQRKQNILKEMAAE 1650
Cdd:pfam15921 481 vEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR-NVQTECEALKLQMAE 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1651 TNAPphpepglhIEDLRKSLG-----TNENQEVSSSLSLSKEGIDLSMDSVRHFLSaEGVAVRSAKEFLVRQTRSM---- 1721
Cdd:pfam15921 560 KDKV--------IEILRQQIEnmtqlVGQHGRTAGAMQVEKAQLEKEINDRRLELQ-EFKILKDKKDAKIRELEARvsdl 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1722 -RRRQTALKAAQQHWRHELASAQEVDEDLPGTKVLENVRKNLDEETKHL--------DEMKSAMRKGHDLLKKKEEKLNQ 1792
Cdd:pfam15921 631 eLEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLkrnfrnksEEMETTTNKLKMQLKSAQSELEQ 710
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798727 1793 LESSLLE-EVSDEDTLKGS--SIKKVTFDLSDMDDLSSEsfescpLLHITPTPNSADPNKiHYLSSSLQRISSELNGV 1867
Cdd:pfam15921 711 TRNTLKSmEGSDGHAMKVAmgMQKQITAKRGQIDALQSK------IQFLEEAMTNANKEK-HFLKEEKNKLSQELSTV 781
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1416-1655 |
1.87e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.11 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1416 EQRTHQKVHQVIEYEQELSSLlrdkRQEVEREhERKMDKMK--EEHWQEMAEARERYEAEerKQRADLLGHLTGELE-RL 1492
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERA----HEALEDA-REQIELLEpiRELAERYAAARERLAEL--EYLRAALRLWFAQRRlEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1493 RRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALE-K 1571
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAlG 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1572 EEATATRRHLEEAKKEHTHLLES----KQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRkqnILKEM 1647
Cdd:COG4913 373 LPLPASAEEFAALRAEAAALLEAleeeLEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA---LRDAL 449
|
....*...
gi 1958798727 1648 AAETNAPP 1655
Cdd:COG4913 450 AEALGLDE 457
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1309-1651 |
2.55e-13 |
|
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: 75.87 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1309 ASLEQKSRRALEQLREqleAEERSAQAALraekeaeKEATLLQLREQLEGERREAV---AGLEKKHSTELEQLCSSLEAk 1385
Cdd:TIGR02169 166 AEFDRKKEKALEELEE---VEENIERLDL-------IIDEKRQQLERLRREREKAEryqALLKEKREYEGYELLKEKEA- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1386 HREVISNLQKKIEGaQQKEEAQLQESLGRAEQRTHqkvhqvieyeqELSSLLRDKRQEVEREHERKMDKMKEEhwqemae 1465
Cdd:TIGR02169 235 LERQKEAIERQLAS-LEEELEKLTEEISELEKRLE-----------EIEQLLEELNKKIKDLGEEEQLRVKEK------- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1466 areryeaeerkqradlLGHLTGELERLRRAherelesvrqeqdqqLEDLRRRHRDQERKLQDLEAELSSrtkdVKARLAQ 1545
Cdd:TIGR02169 296 ----------------IGELEAEIASLERS---------------IAEKERELEDAEERLAKLEAEIDK----LLAEIEE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1546 LNVQEENMRKEKQLLLDaqRQAALEKEEATaTRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQR 1625
Cdd:TIGR02169 341 LEREIEEERKRRDKLTE--EYAELKEELED-LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417
|
330 340
....*....|....*....|....*.
gi 1958798727 1626 LQKHVSSLEAEVQRKQNILKEMAAET 1651
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELEEEK 443
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1231-1829 |
1.54e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.64 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1231 QQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAFENQIRAEqqtALQRLREEAETLQKAERAS 1310
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKAD---AAKKKAEEAKKAAEAAKAE 1351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1311 lEQKSRRALEQLREQLEAEERSAQAALR----AEKEAEKEATLLQLREQLEGERREA----VAGLEKKHSTELEQlcssl 1382
Cdd:PTZ00121 1352 -AEAAADEAEAAEEKAEAAEKKKEEAKKkadaAKKKAEEKKKADEAKKKAEEDKKKAdelkKAAAAKKKADEAKK----- 1425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1383 EAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEqELSSLLRDKRQEVE-----REHERKMDKMKE 1457
Cdd:PTZ00121 1426 KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD-EAKKKAEEAKKADEakkkaEEAKKKADEAKK 1504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1458 EhwQEMAEARERYEAEERKQRADLL--GHLTGELERLRRAHE-------RELESVRQ-EQDQQLEDLRRRHRDQERKLQD 1527
Cdd:PTZ00121 1505 A--AEAKKKADEAKKAEEAKKADEAkkAEEAKKADEAKKAEEkkkadelKKAEELKKaEEKKKAEEAKKAEEDKNMALRK 1582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1528 LEaELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRV 1607
Cdd:PTZ00121 1583 AE-EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1608 RRVELESQVDQLQTQSQRLQKHvsslEAEVQRKQNILKEMAAETNapphpepglHIEDLRKSlgtnENQEVSSSLSLSKE 1687
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKA----EEDEKKAAEALKKEAEEAK---------KAEELKKK----EAEEKKKAEELKKA 1724
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1688 gidlsmDSVRHFLSAEgvAVRSAKEfLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPGT------KVLENVRKN 1761
Cdd:PTZ00121 1725 ------EEENKIKAEE--AKKEAEE-DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVieeeldEEDEKRRME 1795
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798727 1762 LDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLESSLLEEVSDEDTLKGSSIKKVTFDLSDMDDLSSES 1829
Cdd:PTZ00121 1796 VDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGED 1863
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1488-1751 |
1.62e-12 |
|
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: 73.17 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1488 ELERLRRAHERELesvrQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDV----------KARLAQLN-----VQEEN 1552
Cdd:TIGR02168 250 EAEEELEELTAEL----QELEEKLEELRLEVSELEEEIEELQKELYALANEIsrleqqkqilRERLANLErqleeLEAQL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1553 MRKEKQLLLDAQRQAALEKEEATATRRH------LEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRL 1626
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELesleaeLEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1627 QKHVSSLEAEVQRKQNIlkemaaetnapphpepglhIEDLRKSLGTNENQEVSSSLSLSKEGIdlsmdsvrHFLSAEGVA 1706
Cdd:TIGR02168 406 EARLERLEDRRERLQQE-------------------IEELLKKLEEAELKELQAELEELEEEL--------EELQEELER 458
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1958798727 1707 VRSAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPG 1751
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1215-1670 |
4.24e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1215 EEEEEkeekeeehwlYQQKEKSLSLLKTQLQkaaeeeekeeetqirEEESQRLACLRAQVQSSTEAFENQIRAEQQTALQ 1294
Cdd:COG1196 348 EAEEE----------LEEAEAELAEAEEALL---------------EAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1295 RLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKHSTE 1374
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1375 LEQLcssleAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVI----EYEQELSSLLRDKRQEVEREHER 1450
Cdd:COG1196 483 LEEL-----AEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIgveaAYEAALEAALAAALQNIVVEDDE 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1451 KMDKMKEEHWQEMAEARERYEAEERKQRADL-LGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLE 1529
Cdd:COG1196 558 VAAAAIEYLKAAKAGRATFLPLDKIRARAALaAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALR 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1530 AELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIddlrvrr 1609
Cdd:COG1196 638 RAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA------- 710
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958798727 1610 vELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPEPgLHIEDLRKSL 1670
Cdd:COG1196 711 -EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP-PDLEELEREL 769
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1476-1815 |
9.62e-12 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 69.16 E-value: 9.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1476 KQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRK 1555
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1556 EKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEA 1635
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1636 EVQR-----KQNILKEMAAETN-APPHPEPGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRS 1709
Cdd:COG4372 172 ELQAlseaeAEQALDELLKEANrNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1710 AKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPGTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEK 1789
Cdd:COG4372 252 LEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELA 331
|
330 340
....*....|....*....|....*.
gi 1958798727 1790 LNQLESSLLEEVSDEDTLKGSSIKKV 1815
Cdd:COG4372 332 LAILLAELADLLQLLLVGLLDNDVLE 357
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1270-1686 |
9.74e-12 |
|
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: 70.64 E-value: 9.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1270 LRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQ-KAERASLEQKSRRALEQLREQLEAEE------RSAQAALRAEKE 1342
Cdd:pfam12128 409 QLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKsRLGELKLRLNQATATPELLLQLENFDerieraREEQEAANAEVE 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1343 AEKEAtLLQLR----EQLEGERREAVAGLEKKhsTELEQLCSSLEAKHREVISNLQKkiegaqqkEEAQLQESLGR---A 1415
Cdd:pfam12128 489 RLQSE-LRQARkrrdQASEALRQASRRLEERQ--SALDELELQLFPQAGTLLHFLRK--------EAPDWEQSIGKvisP 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1416 EQRTHQKVHQVIEYEQELSSL------LRDKRQEV------EREHERKMDKMKEehwqemaeaRERYEAEERKQRADLLG 1483
Cdd:pfam12128 558 ELLHRTDLDPEVWDGSVGGELnlygvkLDLKRIDVpewaasEEELRERLDKAEE---------ALQSAREKQAAAEEQLV 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1484 HLTGELERLRRAHERELESV--------------RQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQ 1549
Cdd:pfam12128 629 QANGELEKASREETFARTALknarldlrrlfdekQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQ 708
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1550 EENMRKEKQLLLD----------AQRQAALEKEEaTATRRHLEEAKKEHTHLLESK--------------QQLRRAIDDL 1605
Cdd:pfam12128 709 KREARTEKQAYWQvvegaldaqlALLKAAIAARR-SGAKAELKALETWYKRDLASLgvdpdviaklkreiRTLERKIERI 787
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1606 RVRRVELESQVDQLQT----QSQRLQKHVSSLEAEVQRKQNILKEMAAETNapphpepgLHIEDLRKSLGTNENQEVSSS 1681
Cdd:pfam12128 788 AVRRQEVLRYFDWYQEtwlqRRPRLATQLSNIERAISELQQQLARLIADTK--------LRRAKLEMERKASEKQQVRLS 859
|
....*
gi 1958798727 1682 LSLSK 1686
Cdd:pfam12128 860 ENLRG 864
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1488-1650 |
1.13e-11 |
|
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: 66.87 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1488 ELERLRRAHERELESVRQEQD---QQLEDLRRRHRDQERKLQDLEAELssrtKDVKARLAQLNVQEENMRKEKQLlldaq 1564
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAaleARLEAAKTELEDLEKEIKRLELEI----EEVEARIKKYEEQLGNVRNNKEY----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1565 rqAALEKEEATATRRhLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQtqsQRLQKHVSSLEAEVQRKQNIL 1644
Cdd:COG1579 92 --EALQKEIESLKRR-ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK---AELDEELAELEAELEELEAER 165
|
....*.
gi 1958798727 1645 KEMAAE 1650
Cdd:COG1579 166 EELAAK 171
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1222-1797 |
1.16e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.47 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1222 EKEEEhwLYQQKEKSLSLLKtqlQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAF------ENQIRAEQQTA--- 1292
Cdd:TIGR02168 334 ELAEE--LAELEEKLEELKE---ELESLEAELEELEAELEELESRLEELEEQLETLRSKVaqlelqIASLNNEIERLear 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1293 -------LQRLREEAETL-QKAERASLEQKSRR--ALEQLREQLEAEERSAQAALRAEKE--AEKEATLLQLREQLE--G 1358
Cdd:TIGR02168 409 lerledrRERLQQEIEELlKKLEEAELKELQAEleELEEELEELQEELERLEEALEELREelEEAEQALDAAERELAqlQ 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1359 ERREAVAGLEKKHSTELEQLCSSLEAKHR--EVISNLQKKIEGAQQKE---EAQLQESLGRAEQRTHQKVHQVIEY-EQ- 1431
Cdd:TIGR02168 489 ARLDSLERLQENLEGFSEGVKALLKNQSGlsGILGVLSELISVDEGYEaaiEAALGGRLQAVVVENLNAAKKAIAFlKQn 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1432 --------ELSSLLRDKRQEVEREHerkmdKMKEEHWQEMAEARERYEAEERKQRADLLGH------LTGELERLRRAHE 1497
Cdd:TIGR02168 569 elgrvtflPLDSIKGTEIQGNDREI-----LKNIEGFLGVAKDLVKFDPKLRKALSYLLGGvlvvddLDNALELAKKLRP 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1498 REL----------------------ESVRQEQDQQLEDLRRRHRDQERKLQDLEAELssrtKDVKARLAQLNVQEENMRK 1555
Cdd:TIGR02168 644 GYRivtldgdlvrpggvitggsaktNSSILERRREIEELEEKIEELEEKIAELEKAL----AELRKELEELEEELEQLRK 719
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1556 EKQLLLDAQRQAALEKEEATATRRHLEE----AKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVS 1631
Cdd:TIGR02168 720 ELEELSRQISALRKDLARLEAEVEQLEEriaqLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1632 SLEAEVQRKQNILKEM---------AAETNAPPHPEPGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDL--------SMD 1694
Cdd:TIGR02168 800 ALREALDELRAELTLLneeaanlreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIeeleseleALL 879
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1695 SVRHFLSAEGVAVRSAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQevdEDLPGTKV-LENVRKNLDEETK-HLDEM 1772
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE---LRLEGLEVrIDNLQERLSEEYSlTLEEA 956
|
650 660
....*....|....*....|....*
gi 1958798727 1773 KSAMRKGHDLLKKKEEKLNQLESSL 1797
Cdd:TIGR02168 957 EALENKIEDDEEEARRRLKRLENKI 981
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1479-1808 |
1.31e-11 |
|
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: 70.10 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1479 ADLLGHLTGELERLRrAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAE---LSSRTKDVKARLAQLNVQEENMRK 1555
Cdd:TIGR02169 680 RERLEGLKRELSSLQ-SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEeekLKERLEELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1556 EKQLLLD--AQRQAALEKEEAtatrrhlEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSL 1633
Cdd:TIGR02169 759 ELKELEAriEELEEDLHKLEE-------ALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1634 EAEVQRKQNILKEMAAETNapphpEPGLHIEDLRKSLGTNENQEVSSSLS---LSKEGIDLSMDsvRHFLSAEGVAVRSA 1710
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIK-----SIEKEIENLNGKKEELEEELEELEAAlrdLESRLGDLKKE--RDELEAQLRELERK 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1711 KEFLVRQTRSMRRRQTALKAAQQHWRHELAS----AQEVDEDLPGTKVLENVRKNLDEETKHLDEMKSA-MR-------- 1777
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEiedpKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVnMLaiqeyeev 984
|
330 340 350
....*....|....*....|....*....|..
gi 1958798727 1778 -KGHDLLKKKEEKLNQLESSLLEEVSDEDTLK 1808
Cdd:TIGR02169 985 lKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1367-1815 |
1.33e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 70.05 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1367 LEKKHsTELEQLCSSLEAKHREVISNLQKKiegaqQKEEAQLQESLgraeQRTHQKVHQVIEYEQELSSLLRDKRQEVER 1446
Cdd:TIGR04523 209 KIQKN-KSLESQISELKKQNNQLKDNIEKK-----QQEINEKTTEI----SNTQTQLNQLKDEQNKIKKQLSEKQKELEQ 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1447 eHERKMDkmkeehwqemaeareryeaeerkqradllghltgELERLRRAHERELESVRQEQDQQL-EDLRRRHRDQERKL 1525
Cdd:TIGR04523 279 -NNKKIK----------------------------------ELEKQLNQLKSEISDLNNQKEQDWnKELKSELKNQEKKL 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1526 QDLEAELSSRTKdvkaRLAQLNVQEENMRKEKQlllDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDL 1605
Cdd:TIGR04523 324 EEIQNQISQNNK----IISQLNEQISQLKKELT---NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1606 RVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRkqniLKEMAAETNApphpepglHIEDLrkslgTNENqevsSSLSLS 1685
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER----LKETIIKNNS--------EIKDL-----TNQD----SVKELI 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1686 KEGIDLSMDSVRHFLSAegvavrsakeflvrQTRSMRRRQTALKAAQqhwrhelasaQEVDEDLPGTKVLENVRKNLDEE 1765
Cdd:TIGR04523 456 IKNLDNTRESLETQLKV--------------LSRSINKIKQNLEQKQ----------KELKSKEKELKKLNEEKKELEEK 511
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1958798727 1766 TKHL----DEMKSAMRKGHDLLKKKEEKLNQLESSLLEevsDEDTLKGSSIKKV 1815
Cdd:TIGR04523 512 VKDLtkkiSSLKEKIEKLESEKKEKESKISDLEDELNK---DDFELKKENLEKE 562
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1227-1800 |
1.52e-11 |
|
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: 70.00 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1227 HWLYQQKEKSLsllktqlqkaaeeeekeeetqireEESQRLACLRAQVQSSTEAFENQIR--AEQQTALQRLREEAETLQ 1304
Cdd:TIGR00618 242 HAYLTQKREAQ------------------------EEQLKKQQLLKQLRARIEELRAQEAvlEETQERINRARKAAPLAA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1305 KAER-ASLEQKSRRALEQLREQ---LEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAvaglEKKHSTELEQLCS 1380
Cdd:TIGR00618 298 HIKAvTQIEQQAQRIHTELQSKmrsRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDA----HEVATSIREISCQ 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1381 SLEAKHRevISNLQKKIEGAQQKEEAQLQESLG-RAEQrtHQKVHQVIEYEQELSSLLRDKRQEverEHERKMDKMKEEH 1459
Cdd:TIGR00618 374 QHTLTQH--IHTLQQQKTTLTQKLQSLCKELDIlQREQ--ATIDTRTSAFRDLQGQLAHAKKQQ---ELQQRYAELCAAA 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1460 WQEmaeareryeaeerkqradllghlTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKlqdleaelssrtKDV 1539
Cdd:TIGR00618 447 ITC-----------------------TAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRK------------KAV 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1540 KARLAQLNVQEENMRKEKQLLLDAQRQAALEKEeatATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQL 1619
Cdd:TIGR00618 492 VLARLLELQEEPCPLCGSCIHPNPARQDIDNPG---PLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEI 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1620 QTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPE---------------PGLHIEDLRKSLGTNENQEVSSSLSL 1684
Cdd:TIGR00618 569 QQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEdmlaceqhallrklqPEQDLQDVRLHLQQCSQELALKLTAL 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1685 SKEGIDLSMDSVRHflsaegvAVRSAKEFlvrQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPGTKVLENVRKNLDe 1764
Cdd:TIGR00618 649 HALQLTLTQERVRE-------HALSIRVL---PKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYD- 717
|
570 580 590
....*....|....*....|....*....|....*.
gi 1958798727 1765 etKHLDEMKSAMRKGHDLLKKKEEKLNQLESSLLEE 1800
Cdd:TIGR00618 718 --REFNEIENASSSLGSDLAAREDALNQSLKELMHQ 751
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1265-1650 |
1.63e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.41 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1265 QRLACLRAQVQSSTEafENQIRAEQQTALQRLREEAETLQkAERASLEQKSRR------ALEQLREQLEAEERSAQAALR 1338
Cdd:COG4717 71 KELKELEEELKEAEE--KEEEYAELQEELEELEEELEELE-AELEELREELEKlekllqLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1339 AEKEAEKEATLLQLREQLEGERREAvagleKKHSTELEQLCSSLEAKHREVISNLQKKIEGAQQkEEAQLQESLGRAEQR 1418
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAEL-----AELQEELEELLEQLSLATEEELQDLAEELEELQQ-RLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1419 THQKVHQVIEYEQELSSLlrDKRQEVEREH----------------------------------------ERKMDKMKEE 1458
Cdd:COG4717 222 LEELEEELEQLENELEAA--ALEERLKEARlllliaaallallglggsllsliltiagvlflvlgllallFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1459 HWQEMAEARERYEAEERKQRAdllghLTGELERLRRAHERELESVRqEQDQQLEDLRRRHRDQERklQDLEAELSSRTKD 1538
Cdd:COG4717 300 LGKEAEELQALPALEELEEEE-----LEELLAALGLPPDLSPEELL-ELLDRIEELQELLREAEE--LEEELQLEELEQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1539 VKARLAQLNVQEENMRKEKqlLLDAQRQAALEKEEATATRRhLEEAKKEHTHLLE--SKQQLRRAIDDLRVRRVELESQV 1616
Cdd:COG4717 372 IAALLAEAGVEDEEELRAA--LEQAEEYQELKEELEELEEQ-LEELLGELEELLEalDEEELEEELEELEEELEELEEEL 448
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1958798727 1617 DQLQTQSQRLQKHVSSLE---------AEVQRKQNILKEMAAE 1650
Cdd:COG4717 449 EELREELAELEAELEQLEedgelaellQELEELKAELRELAEE 491
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1291-1803 |
2.04e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.56 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1291 TALQRLREEAETLQKAERASLE-QKSRRALEQLREQLE-----AEERSAQAALRAEKEAEKEATLLQLREQLEGERREAV 1364
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDaREQIELLEPIRELAEryaaaRERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1365 AGLEKKHStELEQLCSSLEAKHREvisnLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLlrdkrqEV 1444
Cdd:COG4913 305 ARLEAELE-RLEARLDALREELDE----LEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL------GL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1445 EREHERKMDKMKEEHWQEMAEARERYEAEERKQRAdllghltgELERLRRAHERELESVRQEqdqqLEDLRRRH----RD 1520
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEEALA--------EAEAALRDLRRELRELEAE----IASLERRKsnipAR 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1521 QERKLQDLEAELSSRTKDVK--ARLAQLNVQEENMRK--EKQL------LL--DAQRQAALEKEEATATRRHL--EEAK- 1585
Cdd:COG4913 442 LLALRDALAEALGLDEAELPfvGELIEVRPEEERWRGaiERVLggfaltLLvpPEHYAAALRWVNRLHLRGRLvyERVRt 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1586 ---------------------KEHT------HLL---------ESKQQLR---RAI----------------DDLRVRRV 1610
Cdd:COG4913 522 glpdperprldpdslagkldfKPHPfrawleAELgrrfdyvcvDSPEELRrhpRAItragqvkgngtrhekdDRRRIRSR 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1611 ------------ELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILkemAAETNAPPHPEPGLHIEDLRKSLGTNENQev 1678
Cdd:COG4913 602 yvlgfdnraklaALEAELAELEEELAEAEERLEALEAELDALQERR---EALQRLAEYSWDEIDVASAEREIAELEAE-- 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1679 ssslslsKEGIDLSMDSVRHfLSAEGVAVRSAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPGTKVLEnV 1758
Cdd:COG4913 677 -------LERLDASSDDLAA-LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE-L 747
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1958798727 1759 RKNLDE--ETKHLDEMKSAMRKG-HDLLKKKEEKLNQLESSLLEEVSD 1803
Cdd:COG4913 748 RALLEErfAAALGDAVERELRENlEERIDALRARLNRAEEELERAMRA 795
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1284-1824 |
2.75e-11 |
|
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: 69.05 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1284 QIRAEQQTALQRLREEAETLQKAERASleQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQlegERREA 1363
Cdd:pfam01576 493 QLEDERNSLQEQLEEEEEAKRNVERQL--STLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLE---EKAAA 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1364 VAGLEKKHS---TELEQLCSSLEaKHREVISNLQKKIEGAQQ--KEE----AQLQESLGRAEQRTHQKVHQVIEYEQELS 1434
Cdd:pfam01576 568 YDKLEKTKNrlqQELDDLLVDLD-HQRQLVSNLEKKQKKFDQmlAEEkaisARYAEERDRAEAEAREKETRALSLARALE 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1435 SLLrDKRQEVEREHERKMDKMKEehwqemaeareryeaeeRKQRADLLGHLTGELERLRRAHERELESVRqEQDQQLED- 1513
Cdd:pfam01576 647 EAL-EAKEELERTNKQLRAEMED-----------------LVSSKDDVGKNVHELERSKRALEQQVEEMK-TQLEELEDe 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1514 --------LRRRHRDQ------ERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEA----T 1575
Cdd:pfam01576 708 lqatedakLRLEVNMQalkaqfERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELeaqiD 787
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1576 ATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRvelesqvDQLQTQSQRLQKHVSSLEAEVQRKQNILK---------- 1645
Cdd:pfam01576 788 AANKGREEAVKQLKKLQAQMKDLQRELEEARASR-------DEILAQSKESEKKLKNLEAELLQLQEDLAaserarrqaq 860
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1646 ----EMAAETNAPPHPEPGLHIE----DLRKSLGTNENQEVSSSLSLSKE---GIDLSMDSVRHFLSAEGVA---VRSAK 1711
Cdd:pfam01576 861 qerdELADEIASGASGKSALQDEkrrlEARIAQLEEELEEEQSNTELLNDrlrKSTLQVEQLTTELAAERSTsqkSESAR 940
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1712 EFLVRQTRSMRRR--------QTALKAAQQHWRHELASA-----QEVDEDLPGTKVLENVRKNL-------DEETKHLDE 1771
Cdd:pfam01576 941 QQLERQNKELKAKlqemegtvKSKFKSSIAALEAKIAQLeeqleQESRERQAANKLVRRTEKKLkevllqvEDERRHADQ 1020
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1958798727 1772 MKSAMRKGHDLLKkkeeklnQLESSlLEEVSDEDTLKGSSIKKVTFDLSDMDD 1824
Cdd:pfam01576 1021 YKDQAEKGNSRMK-------QLKRQ-LEEAEEEASRANAARRKLQRELDDATE 1065
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1319-1828 |
2.77e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.91 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1319 LEQLREQLEAEERSAQAALRAEK-EAEKEATLLQLREQLEGerreavaglekKHSTELEQLCSSLEAKHREV---ISNLQ 1394
Cdd:PRK02224 158 LLQLGKLEEYRERASDARLGVERvLSDQRGSLDQLKAQIEE-----------KEEKDLHERLNGLESELAELdeeIERYE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1395 KKIEGAQQKEEAqLQESLGRAEQRthqkvhqvieyEQELSSLLR--DKRQEVEREHERKMDKMKEEhwqemaearERYEA 1472
Cdd:PRK02224 227 EQREQARETRDE-ADEVLEEHEER-----------REELETLEAeiEDLRETIAETEREREELAEE---------VRDLR 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1473 EERKQRADLLGHLTGELErLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARlaqlnvQEEN 1552
Cdd:PRK02224 286 ERLEELEEERDDLLAEAG-LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL------EERA 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1553 MrkekqlllDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSS 1632
Cdd:PRK02224 359 E--------ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1633 LEAEVQRKQNILKEMAAETNAPPHPEPGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKE 1712
Cdd:PRK02224 431 LEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDR 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1713 FlvrqTRSMRRRQTALKAAQQHwrhelasAQEVDEDlpgTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQ 1792
Cdd:PRK02224 511 I----ERLEERREDLEELIAER-------RETIEEK---RERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
490 500 510
....*....|....*....|....*....|....*.
gi 1958798727 1793 LESSLLEEVSDEDTLkgssiKKVTFDLSDMDDLSSE 1828
Cdd:PRK02224 577 LNSKLAELKERIESL-----ERIRTLLAAIADAEDE 607
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1264-1635 |
3.50e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 68.83 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1264 SQRLACLRAQVQSSTEafenqIRAEQQTALQRLREEAETLQKAERAsLEQKSRRALEQLREqleaeersAQAALR-AEKE 1342
Cdd:COG3096 284 SERALELRRELFGARR-----QLAEEQYRLVEMARELEELSARESD-LEQDYQAASDHLNL--------VQTALRqQEKI 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1343 AEKEATLLQLREQLEgERREAVAGLEKKHSTELEQLCSSlEAKHREVISNL---QKKIEgAQQKEEAQLQ---ESLGRAE 1416
Cdd:COG3096 350 ERYQEDLEELTERLE-EQEEVVEEAAEQLAEAEARLEAA-EEEVDSLKSQLadyQQALD-VQQTRAIQYQqavQALEKAR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1417 QRTHQ---KVHQVIEYEQELssllRDKRQEVE---REHERKMDKMKEEHWQemaeareryeaeeRKQRADLLGHLTGELE 1490
Cdd:COG3096 427 ALCGLpdlTPENAEDYLAAF----RAKEQQATeevLELEQKLSVADAARRQ-------------FEKAYELVCKIAGEVE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1491 R----------LRRAHERELESVRQEQ-DQQLEDLRRRHRDQERkLQDLEAELSSRTKDVKARLAQLnvqEENMRKEKQL 1559
Cdd:COG3096 490 RsqawqtarelLRRYRSQQALAQRLQQlRAQLAELEQRLRQQQN-AERLLEEFCQRIGQQLDAAEEL---EELLAELEAQ 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1560 LLDAQRQAALEKEEATATRRHLEEAKKEHTHL------------------------LESKQQLRRAIDDLRVRRVELESQ 1615
Cdd:COG3096 566 LEELEEQAAEAVEQRSELRQQLEQLRARIKELaarapawlaaqdalerlreqsgeaLADSQEVTAAMQQLLEREREATVE 645
|
410 420
....*....|....*....|
gi 1958798727 1616 VDQLQTQSQRLQKHVSSLEA 1635
Cdd:COG3096 646 RDELAARKQALESQIERLSQ 665
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1286-1615 |
5.98e-11 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 66.10 E-value: 5.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1286 RAEQQTALQRLREEAETLQKAERasLEQKSRRALEQLREQLEAEERSAQAAlRAEKEAEKEATLLQLREQLEGERREAVA 1365
Cdd:pfam13868 44 RLDEMMEEERERALEEEEEKEEE--RKEERKRYRQELEEQIEEREQKRQEE-YEEKLQEREQMDEIVERIQEEDQAEAEE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1366 GLEKKHSTELE-QLCSSLEAKHREvisnlQKKIEgaQQKEEAQLQESLG----RAEQRTHQKVHQVIEYEQELSSLLrdK 1440
Cdd:pfam13868 121 KLEKQRQLREEiDEFNEEQAEWKE-----LEKEE--EREEDERILEYLKekaeREEEREAEREEIEEEKEREIARLR--A 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1441 RQEVEREHERKMDKMKEEHWQEmaeareryeaeerkqradllghltgELERLRRAHERELESVRQEQDQQLEDLRRRHRD 1520
Cdd:pfam13868 192 QQEKAQDEKAERDELRAKLYQE-------------------------EQERKERQKEREEAEKKARQRQELQQAREEQIE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1521 QERKLQDLEAElssrtKDVKARLAQLNVQEENMRKEKQlllDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRR 1600
Cdd:pfam13868 247 LKERRLAEEAE-----REEEEFERMLRKQAEDEEIEQE---EAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGE 318
|
330
....*....|....*...
gi 1958798727 1601 AIDDL---RVRRVELESQ 1615
Cdd:pfam13868 319 RLREEeaeRRERIEEERQ 336
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1230-1635 |
1.20e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.71 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1230 YQQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAFENqiRAEQQTALQRLREEAETLQKAERA 1309
Cdd:COG4717 104 LEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEE--LRELEEELEELEAELAELQEELEE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1310 SLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEK-EATLLQLREQLEGERREAVAGLEKKHSTELEQL---------- 1378
Cdd:COG4717 182 LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEaQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallal 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1379 --CSSLEAKHREVISNLQKKIEGA-------QQKEEAQLQESLGRAEQRTHQKVHQvieyEQELSSLLRDKRQEVEREHE 1449
Cdd:COG4717 262 lgLGGSLLSLILTIAGVLFLVLGLlallfllLAREKASLGKEAEELQALPALEELE----EEELEELLAALGLPPDLSPE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1450 RKMDKMKE-EHWQEMaeareryeaeeRKQRADLlghltgELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDL 1528
Cdd:COG4717 338 ELLELLDRiEELQEL-----------LREAEEL------EEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQEL 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1529 eaelssrtkdvKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATaTRRHLEEAKKEHTHLLESKQQLRRAIDDLR-- 1606
Cdd:COG4717 401 -----------KEELEELEEQLEELLGELEELLEALDEEELEEELEE-LEEELEELEEELEELREELAELEAELEQLEed 468
|
410 420
....*....|....*....|....*....
gi 1958798727 1607 VRRVELESQVDQLQTQSQRLQKHVSSLEA 1635
Cdd:COG4717 469 GELAELLQELEELKAELRELAEEWAALKL 497
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1276-1803 |
1.58e-10 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 66.31 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1276 SSTEAFENQIRAEQQTALQRLREEAETLQKAeraSLEQKSRraleqlreqLEAEERSAQAALRAEKEAEKEATLLQ---- 1351
Cdd:pfam07111 58 SQALSQQAELISRQLQELRRLEEEVRLLRET---SLQQKMR---------LEAQAMELDALAVAEKAGQAEAEGLRaala 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1352 ----LREQL-EGERREavagLEKKHSTELEQLcSSLEAKHREVISNLQKKIEGAQQK----------EEAQLQESLGRAE 1416
Cdd:pfam07111 126 gaemVRKNLeEGSQRE----LEEIQRLHQEQL-SSLTQAHEEALSSLTSKAEGLEKSlnsletkragEAKQLAEAQKEAE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1417 QRTHQ--KVHQVIEYEQELSSLLRD----------KRQEVEREHERKMDKMKeeHWQEMAEARERYEAEERKQRADLLGH 1484
Cdd:pfam07111 201 LLRKQlsKTQEELEAQVTLVESLRKyvgeqvppevHSQTWELERQELLDTMQ--HLQEDRADLQATVELLQVRVQSLTHM 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1485 LTGELERLRRAHErELESVRQEQDQQLEDLRRRHRDQ------ERKLQDLEAelSSRTKDVKARLAQLNVQEENMRKEKQ 1558
Cdd:pfam07111 279 LALQEEELTRKIQ-PSDSLEPEFPKKCRSLLNRWREKvfalmvQLKAQDLEH--RDSVKQLRGQVAELQEQVTSQSQEQA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1559 LLLDA--QRQAALEKEEATATRRHLE-----EAKKEHTHLLES-KQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHV 1630
Cdd:pfam07111 356 ILQRAlqDKAAEVEVERMSAKGLQMElsraqEARRRQQQQTASaEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLS 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1631 SSLEAEVQRKQNI---------LKEMAAETNAPPHPEP------GLHIEDLRKslgtnENQEVSSSLSLSKEGIDLSMDS 1695
Cdd:pfam07111 436 NRLSYAVRKVHTIkglmarkvaLAQLRQESCPPPPPAPpvdadlSLELEQLRE-----ERNRLDAELQLSAHLIQQEVGR 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1696 VRHFLSAEgvavrsakeflvrqtrsmrrRQTALKAAQQhWRHELASAQEVDEDLpgTKVLENVRKNLDEETKHLDEMKSA 1775
Cdd:pfam07111 511 AREQGEAE--------------------RQQLSEVAQQ-LEQELQRAQESLASV--GQQLEVARQGQQESTEEAASLRQE 567
|
570 580
....*....|....*....|....*....
gi 1958798727 1776 MRKGHDLLKKK-EEKLNQLESSLLEEVSD 1803
Cdd:pfam07111 568 LTQQQEIYGQAlQEKVAEVETRLREQLSD 596
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1187-1801 |
1.85e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1187 EKEeeeeeekeeegeeeekeekeeeeeeeeeeekeekeeehwlyQQKEKSLSLLKTQLQKaaeeeekeeetqireeesqr 1266
Cdd:COG1196 253 AEL-----------------------------------------EELEAELAELEAELEE-------------------- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1267 lacLRAQVQSSTEAFEnqiraEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKE 1346
Cdd:COG1196 272 ---LRLELEELELELE-----EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1347 ATLLQLREQLEG--ERREAVAGLEKKHSTELEQLCSSLEAKHREVISNLQKKIEgaQQKEEAQLQESLGRAEQRTHQKVH 1424
Cdd:COG1196 344 EELEEAEEELEEaeAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE--LAAQLEELEEAEEALLERLERLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1425 QVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELESVR 1504
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1505 QEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARL---AQLNVQEENMRKEKqlllDAQRQAALEKEEAtATRRHL 1581
Cdd:COG1196 502 DYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALeaaLAAALQNIVVEDDE----VAAAAIEYLKAAK-AGRATF 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1582 EEAKKEHTHLLESKQQLRRAIDDlrvRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAaetnapphpepGL 1661
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGA---AVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV-----------TL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1662 HIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKEFLVRQTRSMRRRQTALKAAQQHWRHELAS 1741
Cdd:COG1196 643 AGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELE 722
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798727 1742 AQEVDEDLpgTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLESSL--LEEV 1801
Cdd:COG1196 723 EEALEEQL--EAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIeaLGPV 782
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1231-1538 |
5.04e-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: 65.08 E-value: 5.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1231 QQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLqKAERAS 1310
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA-EAEIEE 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1311 LEQKSRRALEQLrEQLEAEERSAQAALRAEKE--AEKEATLLQLREQLEGERREAVAGLEKKHSTELEQLCSSLE-AKHR 1387
Cdd:TIGR02168 787 LEAQIEQLKEEL-KALREALDELRAELTLLNEeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEiEELE 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1388 EVISNLQKKIEGAQqKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMD----KMKEEHWQEM 1463
Cdd:TIGR02168 866 ELIEELESELEALL-NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRleglEVRIDNLQER 944
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1464 AEARERYEAEERKQ----RADLLGHLTGELERLRRAHER----------ELESVRQEQD---QQLEDLRRRHRDQERKLQ 1526
Cdd:TIGR02168 945 LSEEYSLTLEEAEAlenkIEDDEEEARRRLKRLENKIKElgpvnlaaieEYEELKERYDfltAQKEDLTEAKETLEEAIE 1024
|
330
....*....|..
gi 1958798727 1527 DLEAELSSRTKD 1538
Cdd:TIGR02168 1025 EIDREARERFKD 1036
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1488-1650 |
7.51e-10 |
|
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: 63.24 E-value: 7.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1488 ELERLRRAhERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRK------------ 1555
Cdd:COG4942 42 ELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyrlgrqp 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1556 EKQLLL------DAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKH 1629
Cdd:COG4942 121 PLALLLspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL 200
|
170 180
....*....|....*....|.
gi 1958798727 1630 VSSLEAEVQRKQNILKEMAAE 1650
Cdd:COG4942 201 LARLEKELAELAAELAELQQE 221
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1234-1605 |
1.01e-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: 63.93 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1234 EKSLSLLKTQLqkaaeeeekeeetqireeesQRLACLRAQVQSSTEAFENQIRaEQQTALQRLREEAETLqkaeRASLEQ 1313
Cdd:TIGR02169 687 KRELSSLQSEL--------------------RRIENRLDELSQELSDASRKIG-EIEKEIEQLEQEEEKL----KERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1314 kSRRALEQLREQLEAEERSaQAALRAEKEaEKEATLLQLREQLEG-ERREAVAGLEK--KHSTELEQLCSSLEAKHREVI 1390
Cdd:TIGR02169 742 -LEEDLSSLEQEIENVKSE-LKELEARIE-ELEEDLHKLEEALNDlEARLSHSRIPEiqAELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1391 SNLQKKiegaqQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKR--QEVEREHERKMDKMKEEhwqemaeare 1468
Cdd:TIGR02169 819 QKLNRL-----TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEelEEELEELEAALRDLESR---------- 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1469 ryeaeerkqradlLGHLTGELERLrRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKA------- 1541
Cdd:TIGR02169 884 -------------LGDLKKERDEL-EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipee 949
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798727 1542 RLAQLNVQEENMRKEKQLL-LDAQRQAALEKEEATATRrhLEEAKKEHTHLLESKQQLRRAIDDL 1605
Cdd:TIGR02169 950 ELSLEDVQAELQRVEEEIRaLEPVNMLAIQEYEEVLKR--LDELKEKRAKLEEERKAILERIEEY 1012
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1287-1793 |
1.10e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.98 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1287 AEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQleAEERSAQAALRAEKEAEKEatllQLREQLEGERREAVAG 1366
Cdd:pfam15921 84 SHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEM--QMERDAMADIRRRESQSQE----DLRNQLQNTVHELEAA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1367 ------LEKKHSTELEQLcSSLEAKHREVISNLQKKIEGAQQKEEAQLQE----------SLGRAEQRTHQKVHQVIEY- 1429
Cdd:pfam15921 158 kclkedMLEDSNTQIEQL-RKMMLSHEGVLQEIRSILVDFEEASGKKIYEhdsmstmhfrSLGSAISKILRELDTEISYl 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1430 -------EQELSSLLRDKRQEVE---REHERKMDKMKEEHWQEmaeareryeaeerkqradllghLTGELERLRRAhere 1499
Cdd:pfam15921 237 kgrifpvEDQLEALKSESQNKIElllQQHQDRIEQLISEHEVE----------------------ITGLTEKASSA---- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1500 lESVRQEQDQQLEDLRRRHRDQE----RKLQDLEAELSSRTKDVKarlaqlnvqeENMRKEKQLLLDAQRQAALEKEEAT 1575
Cdd:pfam15921 291 -RSQANSIQSQLEIIQEQARNQNsmymRQLSDLESTVSQLRSELR----------EAKRMYEDKIEELEKQLVLANSELT 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1576 ATRRHLEEAKKEHTHLlesKQQLRRAIDDLRVRRVELESQVDQLQTQSQR----------LQKHVSSLEAEVQRKQNILK 1645
Cdd:pfam15921 360 EARTERDQFSQESGNL---DDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitidhLRRELDDRNMEVQRLEALLK 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1646 EMAAETNapphpepGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKEFLVRQTRSMRRRQ 1725
Cdd:pfam15921 437 AMKSECQ-------GQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKE 509
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798727 1726 TALKAAQQHWRHELASAQEVDEDLPGTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQL 1793
Cdd:pfam15921 510 RAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQL 577
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1293-1651 |
1.26e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1293 LQRLREEAETLQKA---ERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLE- 1368
Cdd:COG4717 48 LERLEKEADELFKPqgrKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1369 -------KKHSTELEQLCSSLEA--KHREVISNLQKKIEGAQQ---KEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSL 1436
Cdd:COG4717 128 lplyqelEALEAELAELPERLEEleERLEELRELEEELEELEAelaELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1437 LRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRAD---------------------------------LLG 1483
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallallglggsllsliltiagvlflvlgLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1484 HLTGELERLRRAHERELESVR-QEQDQQLEDLR-RRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLL 1561
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQaLPALEELEEEElEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1562 DAQRQAAL-------EKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVR-----RVELESQVDQLQTQSQRLQKH 1629
Cdd:COG4717 368 LEQEIAALlaeagveDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELlealdEEELEEELEELEEELEELEEE 447
|
410 420
....*....|....*....|..
gi 1958798727 1630 VSSLEAEVQRKQNILKEMAAET 1651
Cdd:COG4717 448 LEELREELAELEAELEQLEEDG 469
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1271-1588 |
2.25e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1271 RAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLE--QKSRRALEQLREQLEAEERSAQAALRAEKEAEKEAT 1348
Cdd:COG4717 172 LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEelEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1349 LLQL----------------------------------------REQLEGERREAVAGLEKKHSTELEQLCSSLEAKHre 1388
Cdd:COG4717 252 LLIAaallallglggsllsliltiagvlflvlgllallflllarEKASLGKEAEELQALPALEELEEEELEELLAALG-- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1389 VISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQkvHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEehWQEMAEARE 1468
Cdd:COG4717 330 LPPDLSPEELLELLDRIEELQELLREAEELEEE--LQLEELEQEIAALLAEAGVEDEEELRAALEQAEE--YQELKEELE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1469 RYeaeerkqRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDvkARLAQLNV 1548
Cdd:COG4717 406 EL-------EEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED--GELAELLQ 476
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1958798727 1549 QEENMRKEKQLLldAQRQAALEKEEATAtRRHLEEAKKEH 1588
Cdd:COG4717 477 ELEELKAELREL--AEEWAALKLALELL-EEAREEYREER 513
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1276-1719 |
2.25e-09 |
|
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: 62.82 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1276 SSTEAFENQIRAEQQTALQrLREEAETlQKAEraslEQKSRRALEQLREQLEAEERSAQAALRAEKEA----EKEATLLQ 1351
Cdd:pfam05483 310 STQKALEEDLQIATKTICQ-LTEEKEA-QMEE----LNKAKAAHSFVVTEFEATTCSLEELLRTEQQRleknEDQLKIIT 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1352 LREQLEGERREAVAGLEKKHSTELEQLCSSLEAKHREVISNLQ-KKIEGAQQKEEAQLQESLGRAEQRTHQ---KVHQVI 1427
Cdd:pfam05483 384 MELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfEKIAEELKGKEQELIFLLQAREKEIHDleiQLTAIK 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1428 EYEQELSSLLRDKRQEVEREHERKM------DKMKEEHwQEMAEARERYEAEERKQRADLLGHLTGElERLRRAHER--- 1498
Cdd:pfam05483 464 TSEEHYLKEVEDLKTELEKEKLKNIeltahcDKLLLEN-KELTQEASDMTLELKKHQEDIINCKKQE-ERMLKQIENlee 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1499 -------ELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEK 1571
Cdd:pfam05483 542 kemnlrdELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALK 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1572 EEATATRRHLE----EAKKEHTHLLESKQQLRRAID----DLRVRRVELESQVDQLQtQSQRLQKHVSSLEAEV-QRKQN 1642
Cdd:pfam05483 622 KKGSAENKQLNayeiKVNKLELELASAKQKFEEIIDnyqkEIEDKKISEEKLLEEVE-KAKAIADEAVKLQKEIdKRCQH 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1643 ILKEMAAETNAPPHPEPGLhIEDLRKSLG--TNENQEVSS---SLSLSKEGIDLSMDSVRHFLSAEgvavRSAKEFLVRQ 1717
Cdd:pfam05483 701 KIAEMVALMEKHKHQYDKI-IEERDSELGlyKNKEQEQSSakaALEIELSNIKAELLSLKKQLEIE----KEEKEKLKME 775
|
..
gi 1958798727 1718 TR 1719
Cdd:pfam05483 776 AK 777
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1478-1807 |
4.15e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1478 RADLLGHLTGELERLRRAHERELESV---RQEQDQQLEDLRRRHRDQERKLQDLEaELSSRTKDVKARLAQLNVQEENMR 1554
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNlkeLKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1555 KEKQLLLDAQRQAALEKEEATATRR--HLEEAKKEHTHLLESKQQLRRAIDDLRVRRVE------------LESQVDQLQ 1620
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERleELEERLEELRELEEELEELEAELAELQEELEElleqlslateeeLQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1621 TQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPEPGLHIEDLRKSLGTnenqeVSSSLSLSKEGIDLSMDSVRHF- 1699
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLI-----AAALLALLGLGGSLLSLILTIAg 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1700 -------LSAEGVAVRSAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPGTKVLENVRknldeetkHLDEM 1772
Cdd:COG4717 278 vlflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD--------RIEEL 349
|
330 340 350
....*....|....*....|....*....|....*...
gi 1958798727 1773 KSAMRKGHDLLKKKEEKLNQLE-SSLLEE--VSDEDTL 1807
Cdd:COG4717 350 QELLREAEELEEELQLEELEQEiAALLAEagVEDEEEL 387
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1271-1439 |
7.08e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 60.80 E-value: 7.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1271 RAQVQSSTEAFENQIR------AEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAE 1344
Cdd:COG3206 170 REEARKALEFLEEQLPelrkelEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1345 KE-----------ATLLQLREQ---LEGERREAVAGLEKKHST------ELEQLCSSLEAKHREVISNLQKKIEGAQQkE 1404
Cdd:COG3206 250 GSgpdalpellqsPVIQQLRAQlaeLEAELAELSARYTPNHPDvialraQIAALRAQLQQEAQRILASLEAELEALQA-R 328
|
170 180 190
....*....|....*....|....*....|....*
gi 1958798727 1405 EAQLQESLGRAEQRthqkVHQVIEYEQELSSLLRD 1439
Cdd:COG3206 329 EASLQAQLAQLEAR----LAELPELEAELRRLERE 359
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1179-1696 |
7.35e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1179 EKEEEEEEEKeeeeeeekeeegeeeekeekeeeeeeeeeeekeekeeehwlyQQKEKSLSLLKTQLQKAAEEEEKEEETQ 1258
Cdd:PTZ00121 1378 KKADAAKKKA------------------------------------------EEKKKADEAKKKAEEDKKKADELKKAAA 1415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1259 IREEESQrlacLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEaEERSAQAALR 1338
Cdd:PTZ00121 1416 AKKKADE----AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE-EAKKADEAKK 1490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1339 AEKEAEKEATLLQLREQLEGERREAVAGLEKKHSTELEQlcsSLEAKHREVIsnlqKKIEGAQQKEEAQLQESLGRAEQR 1418
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK---AEEAKKADEA----KKAEEKKKADELKKAEELKKAEEK 1563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1419 thQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHER 1498
Cdd:PTZ00121 1564 --KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1499 ELESVRQ-EQDQQLEDLRRRHRDQERKLQDLEA----ELSSRTKDVKARLAQLNVQEENMRKEKQLlldaQRQAALEKEE 1573
Cdd:PTZ00121 1642 EAEEKKKaEELKKAEEENKIKAAEEAKKAEEDKkkaeEAKKAEEDEKKAAEALKKEAEEAKKAEEL----KKKEAEEKKK 1717
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1574 ATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVElESQVDQLQTQSQRlqkhvsSLEAEVQRKQNILKEMAAETNA 1653
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKIAHLKKEEEK------KAEEIRKEKEAVIEEELDEEDE 1790
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1958798727 1654 PPHPEPGLHIEDLRKSL-----GTNENQEVsssLSLSKEGIDLSMDSV 1696
Cdd:PTZ00121 1791 KRRMEVDKKIKDIFDNFaniieGGKEGNLV---INDSKEMEDSAIKEV 1835
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1332-1577 |
8.05e-09 |
|
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: 59.78 E-value: 8.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1332 SAQAALRAEKEAEKEATLLQLREQLEgERREAVAGLEKKHSTELEQLcSSLEAKhrevISNLQKKIEgAQQKEEAQLQES 1411
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIA-ELEKELAALKKEEKALLKQL-AALERR----IAALARRIR-ALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1412 LGRAEQRTHQKVHQVIEYEQELSSLLRdkRQEVEREHERKMDKMKEEHWQEMAEARE--RYEAEERKQRADLLGHLTGEL 1489
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLR--ALYRLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1490 ERLRRAHERE---LESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRtkdvKARLAQLNVQEENMRKekqlLLDAQRQ 1566
Cdd:COG4942 163 AALRAELEAEraeLEALLAELEEERAALEALKAERQKLLARLEKELAEL----AAELAELQQEAEELEA----LIARLEA 234
|
250
....*....|.
gi 1958798727 1567 AALEKEEATAT 1577
Cdd:COG4942 235 EAAAAAERTPA 245
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1283-1637 |
8.39e-09 |
|
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: 60.96 E-value: 8.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1283 NQIRAEQQTALQRLREEAEtlqKAERASLEQKSR-----RALEQLREQLEAEERsAQAALRAEKEA---EKEATLLQLRE 1354
Cdd:pfam01576 607 DQMLAEEKAISARYAEERD---RAEAEAREKETRalslaRALEEALEAKEELER-TNKQLRAEMEDlvsSKDDVGKNVHE 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1355 qLEGERREAVAGLE--KKHSTELE-QLCSSLEAKHRevisnLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQ 1431
Cdd:pfam01576 683 -LERSKRALEQQVEemKTQLEELEdELQATEDAKLR-----LEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1432 ELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLR----------RAHERELE 1501
Cdd:pfam01576 757 ELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARasrdeilaqsKESEKKLK 836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1502 SVRQEQDQQLEDL-----RRRHRDQERklQDLEAELSSRTKD----------VKARLAQLNVQEENMRKEKQLLLDAQRQ 1566
Cdd:pfam01576 837 NLEAELLQLQEDLaaserARRQAQQER--DELADEIASGASGksalqdekrrLEARIAQLEEELEEEQSNTELLNDRLRK 914
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798727 1567 AALEKE----EATATRRHLEEAKKehthlleSKQQLRRAIDDLRVRRVELESQVDQLQTQSqrlqkhVSSLEAEV 1637
Cdd:pfam01576 915 STLQVEqlttELAAERSTSQKSES-------ARQQLERQNKELKAKLQEMEGTVKSKFKSS------IAALEAKI 976
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1288-1577 |
1.43e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 60.14 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1288 EQQTALQRLREEAETLQKAERASlEQKSRRALEQLREQLEAEeRSAQAALRAEKE---AEKEATLLQLREQ-----LEGE 1359
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEKAR-EVERRRKLEEAEKARQAE-MDRQAAIYAEQErmaMERERELERIRQEerkreLERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1360 RREAVAgLEKKHSTELEQLCSSLEAKHREVISNL-------------QKKI-------EGAQQKEEAQLQESLGRAEQRT 1419
Cdd:pfam17380 366 RQEEIA-MEISRMRELERLQMERQQKNERVRQELeaarkvkileeerQRKIqqqkvemEQIRAEQEEARQREVRRLEEER 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1420 HQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQ---EMAEARERYEAEERKQRADLlghltgELERLRRAH 1496
Cdd:pfam17380 445 AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRkraEEQRRKILEKELEERKQAMI------EEERKRKLL 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1497 ERELEsvrQEQDQQLEDLRRRHRDQERKLQdLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATA 1576
Cdd:pfam17380 519 EKEME---ERQKAIYEEERRREAEEERRKQ-QEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
.
gi 1958798727 1577 T 1577
Cdd:pfam17380 595 T 595
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1363-1642 |
1.89e-08 |
|
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: 58.62 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1363 AVAGLEKKHSTELEQLcssleakhREVISNLQKKIEgAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSsLLRDKRQ 1442
Cdd:COG4942 17 AQADAAAEAEAELEQL--------QQEIAELEKELA-ALKKEEKALLKQLAALERRIAALARRIRALEQELA-ALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1443 EVEREhERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAheRELESVRQEQDQQLEDLRRRhrdqe 1522
Cdd:COG4942 87 ELEKE-IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRL--QYLKYLAPARREQAEELRAD----- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1523 rklqdleaelssrtkdvKARLAQLNVQEENMRKEKQLLLDAQRQAalekeeatatRRHLEEAKKEHTHLLESkqqlrrai 1602
Cdd:COG4942 159 -----------------LAELAALRAELEAERAELEALLAELEEE----------RAALEALKAERQKLLAR-------- 203
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1958798727 1603 ddLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQN 1642
Cdd:COG4942 204 --LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1265-1547 |
2.01e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1265 QRLACLRAQVQSSTEAFE--NQIRAEQQTALQRLREEAETLQKAERASLEQKS----RRALEQLREQLEAEERSAQAALR 1338
Cdd:COG4913 610 AKLAALEAELAELEEELAeaEERLEALEAELDALQERREALQRLAEYSWDEIDvasaEREIAELEAELERLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1339 AEKEAEK-EATLLQLREQLEgERREAVAGLEKKHsTELEQLCSSLEAKhrevisnLQKKIEGAQQKEEAQLQESLGRAEQ 1417
Cdd:COG4913 690 LEEQLEElEAELEELEEELD-ELKGEIGRLEKEL-EQAEEELDELQDR-------LEAAEDLARLELRALLEERFAAALG 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1418 RTHQKvhqviEYEQELSSLLRDKRQEVEREHERKMDKMKE--EHWQemaeareryeaeerkqraDLLGHLTGELERLrRA 1495
Cdd:COG4913 761 DAVER-----ELRENLEERIDALRARLNRAEEELERAMRAfnREWP------------------AETADLDADLESL-PE 816
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1958798727 1496 HERELESVRQEQDQQLED--LRRRHRDQERKLQDLEAELSSRTKDVKARLAQLN 1547
Cdd:COG4913 817 YLALLDRLEEDGLPEYEErfKELLNENSIEFVADLLSKLRRAIREIKERIDPLN 870
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1264-1804 |
2.02e-08 |
|
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: 59.70 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1264 SQRLACLRAQVQSSTEAFENQIRAeqqtalqrlreeaetlQKAERASLE---QKSRRALEQLREQLEAEERSAQAALRAE 1340
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEE----------------ERKRRDKLTeeyAELKEELEDLRAELEEVDKEFAETRDEL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1341 KEAEKEATLLQ-LREQLEGERREAVAGLEKKHS--TELEQLCSSLEAKHREVIS---NLQKKIEGAQQKEEaQLQESLGR 1414
Cdd:TIGR02169 388 KDYREKLEKLKrEINELKRELDRLQEELQRLSEelADLNAAIAGIEAKINELEEekeDKALEIKKQEWKLE-QLAADLSK 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1415 AEQRTHQKVHQVIEYEQELSSLlrdKRQEVEREHERKMdkmkeehWQEMAEARERYEAEERKQRADLLGhLTGELERLRR 1494
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKL---QRELAEAEAQARA-------SEERVRGGRAVEEVLKASIQGVHG-TVAQLGSVGE 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1495 AHERELES---------------------------------------VRQEQ---------------------DQQLE-- 1512
Cdd:TIGR02169 536 RYATAIEVaagnrlnnvvveddavakeaiellkrrkagratflplnkMRDERrdlsilsedgvigfavdlvefDPKYEpa 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1513 --------------DLRRRHRDQERkLQDLEAEL-----------------SSRTKDVKARLAQLNVQEENMRKEKQLLL 1561
Cdd:TIGR02169 616 fkyvfgdtlvvediEAARRLMGKYR-MVTLEGELfeksgamtggsraprggILFSRSEPAELQRLRERLEGLKRELSSLQ 694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1562 DAQRQAaleKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQ 1641
Cdd:TIGR02169 695 SELRRI---ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1642 NILKEMAAETNAPPHPEPGLHIEDLRKSLgtNENQEVSSSLSLSKEGIDLSMDSvrhfLSAEGVAVRSAKEFLVRQTRSM 1721
Cdd:TIGR02169 772 EDLHKLEEALNDLEARLSHSRIPEIQAEL--SKLEEEVSRIEARLREIEQKLNR----LTLEKEYLEKEIQELQEQRIDL 845
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1722 RRRQTALKAAQQHWRHELASAQEVDEDLPG-TKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLESSL--- 1797
Cdd:TIGR02169 846 KEQIKSIEKEIENLNGKKEELEEELEELEAaLRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELkak 925
|
....*..
gi 1958798727 1798 LEEVSDE 1804
Cdd:TIGR02169 926 LEALEEE 932
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1286-1627 |
2.33e-08 |
|
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: 59.42 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1286 RAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKE--------ATLLQLREQLE 1357
Cdd:pfam01576 325 REQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESEnaelqaelRTLQQAKQDSE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1358 GERREAVAGLEK--------------------KHSTELEQLCSSLEAKHREVIsNLQKKIEGAqqkeEAQLQESLGRAEQ 1417
Cdd:pfam01576 405 HKRKKLEGQLQElqarlseserqraelaeklsKLQSELESVSSLLNEAEGKNI-KLSKDVSSL----ESQLQDTQELLQE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1418 RTHQKV---HQVIEYEQELSSLLrdKRQEVEREHERKMDKMKEEHWQEMaeareryeAEERKQRADLLGHLTGeLERLRR 1494
Cdd:pfam01576 480 ETRQKLnlsTRLRQLEDERNSLQ--EQLEEEEEAKRNVERQLSTLQAQL--------SDMKKKLEEDAGTLEA-LEEGKK 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1495 AHERELESVRQ---EQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKA------RLAQLNVQEENMRKEKQLLLDAQR 1565
Cdd:pfam01576 549 RLQRELEALTQqleEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNlekkqkKFDQMLAEEKAISARYAEERDRAE 628
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798727 1566 QAALEKE-EATATRRHLEEAKKEHTHLLESKQQLRRAIDDL---------------RVRRVeLESQVDQLQTQSQRLQ 1627
Cdd:pfam01576 629 AEAREKEtRALSLARALEEALEAKEELERTNKQLRAEMEDLvsskddvgknvheleRSKRA-LEQQVEEMKTQLEELE 705
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1227-1573 |
3.49e-08 |
|
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: 58.96 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1227 HWLYQQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAFENQIRAEQqtalqRLREEAETLQKA 1306
Cdd:pfam05483 468 HYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEE-----RMLKQIENLEEK 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1307 ErasleQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQlegerreavaglekKHSTELEQLCSSLeakh 1386
Cdd:pfam05483 543 E-----MNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKE--------------KQMKILENKCNNL---- 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1387 REVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVhQVIEYEQELSSLlRDKRQEVEREHERKMD--KMKEEHWQEMA 1464
Cdd:pfam05483 600 KKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEI-KVNKLELELASA-KQKFEEIIDNYQKEIEdkKISEEKLLEEV 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1465 EARERYEAEERKQRADL---LGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKA 1541
Cdd:pfam05483 678 EKAKAIADEAVKLQKEIdkrCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLS 757
|
330 340 350
....*....|....*....|....*....|..
gi 1958798727 1542 RLAQLNVQEEnmRKEKqLLLDAQRQAALEKEE 1573
Cdd:pfam05483 758 LKKQLEIEKE--EKEK-LKMEAKENTAILKDK 786
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1505-1653 |
3.69e-08 |
|
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: 56.47 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1505 QEQDQQLEDLRRRHRDQERKLQDLEAELssrtKDVKARLAQLNVQEENMRKEKqllldAQRQAALEKEEATATR--RHLE 1582
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDEL----AALEARLEAAKTELEDLEKEI-----KRLELEIEEVEARIKKyeEQLG 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958798727 1583 EAK--KEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNA 1653
Cdd:COG1579 84 NVRnnKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1273-1804 |
4.02e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.49 E-value: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1273 QVQSSTEAFENQiraEQQTALQRLREEAETLQKAERASLEQ--KSRRALEQLREQLEAeersaqaaLRAEKEaEKEATLL 1350
Cdd:TIGR04523 292 QLKSEISDLNNQ---KEQDWNKELKSELKNQEKKLEEIQNQisQNNKIISQLNEQISQ--------LKKELT-NSESENS 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1351 QLREQLEgERREAVAGLEKKHSTELEQLcSSLEAKhrevISNLQKKIEgAQQKEEAQLQESLgraeqRTHQKVHQVIEYE 1430
Cdd:TIGR04523 360 EKQRELE-EKQNEIEKLKKENQSYKQEI-KNLESQ----INDLESKIQ-NQEKLNQQKDEQI-----KKLQQEKELLEKE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1431 QE-LSSLLRDKRQEVEREHERKMDKMKEEhwqemaeareryeaeerkqradllghltgelerlrraheRELESVRQEQDQ 1509
Cdd:TIGR04523 428 IErLKETIIKNNSEIKDLTNQDSVKELII---------------------------------------KNLDNTRESLET 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1510 QLEDLRRRHRDQERKLQDLEAELSSRTKDVKarlaQLNVQEENMrKEKQLLLDAQRQAALEKEEAtatrrhLEEAKKEht 1589
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKELK----KLNEEKKEL-EEKVKDLTKKISSLKEKIEK------LESEKKE-- 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1590 hlLESK-QQLRRAI--DDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAEtnapphpepglhIEDL 1666
Cdd:TIGR04523 536 --KESKiSDLEDELnkDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE------------KKDL 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1667 RKSLGTNEnqevSSSLSLSKEgIDLSMDSVRHfLSAEGVAVRSAKEFLVRQTRSMrrrQTALKAAQQHWRHELASAQEVD 1746
Cdd:TIGR04523 602 IKEIEEKE----KKISSLEKE-LEKAKKENEK-LSSIIKNIKSKKNKLKQEVKQI---KETIKEIRNKWPEIIKKIKESK 672
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798727 1747 EDLpgTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLN-QLESSLLEEVSDE 1804
Cdd:TIGR04523 673 TKI--DDIIELMKDWLKELSLHYKKYITRMIRIKDLPKLEEKYKEiEKELKKLDEFSKE 729
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1283-1650 |
5.38e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 57.24 E-value: 5.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1283 NQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEaeersaqaalraEKEAEKEATLLQLREQLEgERre 1362
Cdd:pfam13868 21 NKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEE------------ERKEERKRYRQELEEQIE-ER-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1363 avaglEKKHSTELEQlcsslEAKHREVISNLQKKIegaqQKEEAQLQESLGRAEQRTHQKVHQVIEyeqelsslLRDKRQ 1442
Cdd:pfam13868 86 -----EQKRQEEYEE-----KLQEREQMDEIVERI----QEEDQAEAEEKLEKQRQLREEIDEFNE--------EQAEWK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1443 EVEREHERKMDKMKEEHWQEMAeareryeaeerKQRADLlghltgELERLRRAHERELESVRQEQDQQLEDLRRRHRDQe 1522
Cdd:pfam13868 144 ELEKEEEREEDERILEYLKEKA-----------EREEER------EAEREEIEEEKEREIARLRAQQEKAQDEKAERDE- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1523 rklqdleaelssrtkdvkarLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEhthlLESKQQLRRAI 1602
Cdd:pfam13868 206 --------------------LRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKER----RLAEEAEREEE 261
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1958798727 1603 DDLRVRRVELES-QVDQLQTQSQRL--QKHVSSLEAEVQ-RKQNILKEMAAE 1650
Cdd:pfam13868 262 EFERMLRKQAEDeEIEQEEAEKRRMkrLEHRRELEKQIEeREEQRAAEREEE 313
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1254-1638 |
6.49e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 6.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1254 EEETQIREEESQRLACLRAQVQSSTEAFENQIRaEQQTALQRLREEAETLqkAERASLEQKSRRALEQLREQLEAEERSA 1333
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVR-DLRERLEELEEERDDL--LAEAGLDDADAEAVEARREELEDRDEEL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1334 QAALR----AEKEAEKEATLL-----QLREQLEgERREAVAGLEkkhsTELEQLCSSLEaKHREVISNLQKKIEGAqQKE 1404
Cdd:PRK02224 327 RDRLEecrvAAQAHNEEAESLredadDLEERAE-ELREEAAELE----SELEEAREAVE-DRREEIEELEEEIEEL-RER 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1405 EAQLQESLGRAEQR------THQKVHqviEYEQELSSLLRDKRQEVErEHERKMDKMK-EEHWQEMAEARERYEAEERKQ 1477
Cdd:PRK02224 400 FGDAPVDLGNAEDFleelreERDELR---EREAELEATLRTARERVE-EAEALLEAGKcPECGQPVEGSPHVETIEEDRE 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1478 RADllghltgELERLRRAHERELESVRQEQDqQLEDLRRRHRDQERKLQDLEAeLSSRTKDVKARLAQLNVQEENMRKEK 1557
Cdd:PRK02224 476 RVE-------ELEAELEDLEEEVEEVEERLE-RAEDLVEAEDRIERLEERRED-LEELIAERRETIEEKRERAEELRERA 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1558 QLL---LDAQRQAALEK-EEATATRRHLEEAKKEHTHLLESKQQLRR-------------AIDDLRVRRVELESQVDQLQ 1620
Cdd:PRK02224 547 AELeaeAEEKREAAAEAeEEAEEAREEVAELNSKLAELKERIESLERirtllaaiadaedEIERLREKREALAELNDERR 626
|
410
....*....|....*...
gi 1958798727 1621 TQSQRLQKHVSSLEAEVQ 1638
Cdd:PRK02224 627 ERLAEKRERKRELEAEFD 644
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1497-1650 |
1.03e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1497 ERELESVRQEQDQ---QLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEkQLLLDAQ-------RQ 1566
Cdd:COG3883 43 QAELEELNEEYNElqaELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYL-DVLLGSEsfsdfldRL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1567 AALEKEeATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKE 1646
Cdd:COG3883 122 SALSKI-ADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAE 200
|
....
gi 1958798727 1647 MAAE 1650
Cdd:COG3883 201 LEAE 204
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1270-1648 |
1.13e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.22 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1270 LRAQVQSSTEAFENqIRAEQQTALQRLREeAETLQKAERASLEQKSRRA-LEQLREQLEAEERSAQAALRA-------EK 1341
Cdd:PRK01156 303 YKNDIENKKQILSN-IDAEINKYHAIIKK-LSVLQKDYNDYIKKKSRYDdLNNQILELEGYEMDYNSYLKSieslkkkIE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1342 EAEKEATLLQLREQLEGERREAVAGLEKKHSTELEQLCSSLEAKhrevISNLQKKIEGAQQKEEaQLQESLGRAEQR--- 1418
Cdd:PRK01156 381 EYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSK----VSSLNQRIRALRENLD-ELSRNMEMLNGQsvc 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1419 ----TH---QKVHQVIEYEQELSSLLRDKRQEVERE------HERKMDKMKEEHWQEMAEARERYEAEERKQRADLlGHL 1485
Cdd:PRK01156 456 pvcgTTlgeEKSNHIINHYNEKKSRLEEKIREIEIEvkdideKIVDLKKRKEYLESEEINKSINEYNKIESARADL-EDI 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1486 TGELERLRRAHERELESVRQEQDQQLEDLRRRHRD-----QERKLQDLEA------ELSSRTKDVKARLAQLNVQEE--- 1551
Cdd:PRK01156 535 KIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSwlnalAVISLIDIETnrsrsnEIKKQLNDLESRLQEIEIGFPddk 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1552 ---------------------NMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHT-HLLESK---QQLRRAIDDLR 1606
Cdd:PRK01156 615 syidksireieneannlnnkyNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITsRINDIEdnlKKSRKALDDAK 694
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1958798727 1607 VRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMA 1648
Cdd:PRK01156 695 ANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIG 736
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1273-1639 |
2.07e-07 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 56.60 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1273 QVQSSTEAFENQIRAEQQTALQRLREEAETLQKAerasleQKSRRALE-------QLREQLEAEERSAQAALRAEKEAEK 1345
Cdd:PRK10929 34 QAKAAKTPAQAEIVEALQSALNWLEERKGSLERA------KQYQQVIDnfpklsaELRQQLNNERDEPRSVPPNMSTDAL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1346 EATLLQLREQLEGERREAVAGLEKKH--STELEQLCSSLEAKHR---EVISNLQKKIEGAQQKEEAQLqeSLGRAEQRTH 1420
Cdd:PRK10929 108 EQEILQVSSQLLEKSRQAQQEQDRAReiSDSLSQLPQQQTEARRqlnEIERRLQTLGTPNTPLAQAQL--TALQAESAAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1421 Q-KVHqvieyEQELSSLLRDKRQEVEReherkmdkMKEEHWQEmaeareryeaeeRKQRADL-LGHLTGELERLR-RAHE 1497
Cdd:PRK10929 186 KaLVD-----ELELAQLSANNRQELAR--------LRSELAKK------------RSQQLDAyLQALRNQLNSQRqREAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1498 RELESVRQEQDQQlEDLRRRHRDQERKLQDLEAElssrtkdvkarlaqLNVQEENMrkekQLLLDAQRQAA---LEKEEA 1574
Cdd:PRK10929 241 RALESTELLAEQS-GDLPKSIVAQFKINRELSQA--------------LNQQAQRM----DLIASQQRQAAsqtLQVRQA 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798727 1575 TATRRHLEEAKKEHTHLLES-------------KQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQR 1639
Cdd:PRK10929 302 LNTLREQSQWLGVSNALGEAlraqvarlpempkPQQLDTEMAQLRVQRLRYEDLLNKQPQLRQIRQADGQPLTAEQNR 379
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1489-1650 |
2.20e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.18 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1489 LERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAE-----LSSRTKDVKARLAQLNVQeenmrkekqlLLDA 1563
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKnglvdLSEEAKLLLQQLSELESQ----------LAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1564 QRQAALEKEEATATRRHLEEAKKEHTHLLESK--QQLRRAIDDLRVRR--------------VELESQVDQLQTQ-SQRL 1626
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELLQSPviQQLRAQLAELEAELaelsarytpnhpdvIALRAQIAALRAQlQQEA 311
|
170 180
....*....|....*....|....
gi 1958798727 1627 QKHVSSLEAEVQRKQNILKEMAAE 1650
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQ 335
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1563-1811 |
3.69e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1563 AQRQAALE--KEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRK 1640
Cdd:COG4942 23 AEAEAELEqlQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1641 QNILKEMAAE---TNAPPHPEPGLHIEDLrkslgtnenQEVSSSLSLskegidlsMDSVRHFLSAEGVAVRSAKEFLVRQ 1717
Cdd:COG4942 103 KEELAELLRAlyrLGRQPPLALLLSPEDF---------LDAVRRLQY--------LKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1718 TRS---MRRRQTALKAAQQHWRHELASAQEVDEDLpgtkvLENVRKNLDEETKHLDEmksamrkghdlLKKKEEKLNQLE 1794
Cdd:COG4942 166 RAEleaERAELEALLAELEEERAALEALKAERQKL-----LARLEKELAELAAELAE-----------LQQEAEELEALI 229
|
250
....*....|....*..
gi 1958798727 1795 SSLLEEVSDEDTLKGSS 1811
Cdd:COG4942 230 ARLEAEAAAAAERTPAA 246
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1272-1584 |
3.85e-07 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 55.15 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1272 AQVQSSTEAFENQIRAEQ---QTALQRLREEAETLQK---AERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEK 1345
Cdd:pfam09731 161 AHTDSLKEASDTAEISREkatDSALQKAEALAEKLKEvinLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQS 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1346 EATLL-QLREQLEGERREAVAGLEKKH------STELEQLCS----SLEAKHREVISNLQKKIEGAQQKEEAQLQESL-G 1413
Cdd:pfam09731 241 LAKLVdQYKELVASERIVFQQELVSIFpdiipvLKEDNLLSNddlnSLIAHAHREIDQLSKKLAELKKREEKHIERALeK 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1414 RAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEhwqemaeareryeaeerkqradllghLTGELERLR 1493
Cdd:pfam09731 321 QKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEK--------------------------LRTELERQA 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1494 RAHERELESVRQEQDQQLEdlRRRHRD------QERKLQDLE-AELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQR- 1565
Cdd:pfam09731 375 EAHEEHLKDVLVEQEIELQ--REFLQDikekveEERAGRLLKlNELLANLKGLEKATSSHSEVEDENRKAQQLWLAVEAl 452
|
330
....*....|....*....
gi 1958798727 1566 QAALEKEEATATRRHLEEA 1584
Cdd:pfam09731 453 RSTLEDGSADSRPRPLVRE 471
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1263-1628 |
4.18e-07 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 54.86 E-value: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1263 ESQRLACLRAQVQSSTEAFEN--QIRAEQQTALQRLREEAETLQK---AERASLEQksrrALEQLREQL-EAEERSAQAA 1336
Cdd:pfam06160 91 IEELLDDIEEDIKQILEELDEllESEEKNREEVEELKDKYRELRKtllANRFSYGP----AIDELEKQLaEIEEEFSQFE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1337 LRAEK----EAEKEatLLQLREQLE--GERREAVAGLEKKHSTEL-EQLcSSLEAKHREVI--------SNLQKKIEGAq 1401
Cdd:pfam06160 167 ELTESgdylEAREV--LEKLEEETDalEELMEDIPPLYEELKTELpDQL-EELKEGYREMEeegyalehLNVDKEIQQL- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1402 qkeEAQLQESLGRAEQRTHQKVHQVIE-YEQELSSLLRDKRQEVEREH--ERKMDKMKE--EHWQEMAEareryeaeerk 1476
Cdd:pfam06160 243 ---EEQLEENLALLENLELDEAEEALEeIEERIDQLYDLLEKEVDAKKyvEKNLPEIEDylEHAEEQNK----------- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1477 qradllgHLTGELERLRRA---HERELESVRQEQDqQLEDLRRRHRDQERKLQDLEA---ELSSRTKDVKARLAQLNVQE 1550
Cdd:pfam06160 309 -------ELKEELERVQQSytlNENELERVRGLEK-QLEELEKRYDEIVERLEEKEVaysELQEELEEILEQLEEIEEEQ 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1551 ENMRKEKQLL----LDAQRQAALEKEEATATRRHLEeakKEH---------THLLESKQQLRRAIDDLRVRRV---ELES 1614
Cdd:pfam06160 381 EEFKESLQSLrkdeLEAREKLDEFKLELREIKRLVE---KSNlpglpesylDYFFDVSDEIEDLADELNEVPLnmdEVNR 457
|
410
....*....|....
gi 1958798727 1615 QVDQLQTQSQRLQK 1628
Cdd:pfam06160 458 LLDEAQDDVDTLYE 471
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1290-1677 |
4.34e-07 |
|
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: 54.96 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1290 QTALQRLREEAETLQKAERASleqKSRRALEQLREQLEAEERSAQAALRAEKEAEKEatlLQLREQLEGERREAVAGLEK 1369
Cdd:COG5185 184 LTLGLLKGISELKKAEPSGTV---NSIKESETGNLGSESTLLEKAKEIINIEEALKG---FQDPESELEDLAQTSDKLEK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1370 --KHSTELEQ--LCSSLEAKHR--EVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSsllrdkrqE 1443
Cdd:COG5185 258 lvEQNTDLRLekLGENAESSKRlnENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELE--------E 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1444 VEREHERKMDKMKEEHWQEmaeaRERYEAEERKQRADLlGHLTGElERLRRAhERELESVRQEQDQQLEDLRRRHRDQER 1523
Cdd:COG5185 330 SKRETETGIQNLTAEIEQG----QESLTENLEAIKEEI-ENIVGE-VELSKS-SEELDSFKDTIESTKESLDEIPQNQRG 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1524 KLQDLEAELSSRTKDVKARLAQLNVQ--------EENMRKEKQLLLDAQRQAALEKEEATAtrrHLEEAKKEHthllesK 1595
Cdd:COG5185 403 YAQEILATLEDTLKAADRQIEELQRQieqatssnEEVSKLLNELISELNKVMREADEESQS---RLEEAYDEI------N 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1596 QQLRRAIDDLRVRRVELESQVDQLQTQsqrLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPEPGLHI---EDLRKSLGT 1672
Cdd:COG5185 474 RSVRSKKEDLNEELTQIESRVSTLKAT---LEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHIlalENLIPASEL 550
|
....*
gi 1958798727 1673 NENQE 1677
Cdd:COG5185 551 IQASN 555
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1283-1720 |
5.02e-07 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 54.91 E-value: 5.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1283 NQIRAEQQTALQRLRE--EAETLQKAERASLEQKSRRALEQLREQLEA-EERSAQAALRAEKEAEKEATLLQLREQLEGE 1359
Cdd:COG5278 82 EEARAEIDELLAELRSltADNPEQQARLDELEALIDQWLAELEQVIALrRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1360 RREAVAGLEKKHSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRD 1439
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1440 KRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHR 1519
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1520 DQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLR 1599
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1600 RAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPEPGLHIEDLRKSLGTNENQEVS 1679
Cdd:COG5278 402 AAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAA 481
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1958798727 1680 SSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKEFLVRQTRS 1720
Cdd:COG5278 482 AALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALA 522
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1283-1576 |
5.39e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1283 NQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEA--EERSAQAALRAEKEAEKEATLLQLREQLEGEr 1360
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKEleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGE- 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1361 reaVAGLEKkhstELEQLcSSLEAKHREVISNLQKKiegaqqkeEAQLQESLGRAEQRTHQKVHQVIEYEQELSSL---- 1436
Cdd:PRK03918 541 ---IKSLKK----ELEKL-EELKKKLAELEKKLDEL--------EEELAELLKELEELGFESVEELEERLKELEPFyney 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1437 --LRDKRQEVEREhERKMDKMKEEHWQ--EMAEARERYEAEERKQRADLLGHLTGE-LERLRRAH---ERELESVRQEqd 1508
Cdd:PRK03918 605 leLKDAEKELERE-EKELKKLEEELDKafEELAETEKRLEELRKELEELEKKYSEEeYEELREEYlelSRELAGLRAE-- 681
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958798727 1509 qqLEDLRRRHRDQERKLQDLEAELSSRTK------DVKARLAQLNVQEENMRKEKQLLldaqRQAALEKEEATA 1576
Cdd:PRK03918 682 --LEELEKRREEIKKTLEKLKEELEEREKakkeleKLEKALERVEELREKVKKYKALL----KERALSKVGEIA 749
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1481-1653 |
5.44e-07 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 54.30 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1481 LLGHLTGELERLRRAHER--ELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTK-----------------DVKA 1541
Cdd:pfam19220 32 LIEPIEAILRELPQAKSRllELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVArlakleaalreaeaakeELRI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1542 RLAQLNVQEENMrkEKQLLLDAQRQAALEKE------EATATRRHLEEAKKEhthLLESKQQLRRAIDDLRVRRVELESQ 1615
Cdd:pfam19220 112 ELRDKTAQAEAL--ERQLAAETEQNRALEEEnkalreEAQAAEKALQRAEGE---LATARERLALLEQENRRLQALSEEQ 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958798727 1616 VDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNA 1653
Cdd:pfam19220 187 AAELAELTRRLAELETQLDATRARLRALEGQLAAEQAE 224
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1488-1590 |
6.97e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.40 E-value: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1488 ELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDL---EAELSSRTKDVKARLAQLNVQEENM-RKEKQLLLDA 1563
Cdd:PRK12704 65 EIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLekrEEELEKKEKELEQKQQELEKKEEELeELIEEQLQEL 144
|
90 100
....*....|....*....|....*..
gi 1958798727 1564 QRQAALEKEEATAtrRHLEEAKKEHTH 1590
Cdd:PRK12704 145 ERISGLTAEEAKE--ILLEKVEEEARH 169
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1490-1653 |
7.10e-07 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 51.99 E-value: 7.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1490 ERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKdvKARLAqLNVQEENMRKEKqllldAQRQAAL 1569
Cdd:pfam04012 24 EKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEE--KAQAA-LTKGNEELAREA-----LAEKKSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1570 EKeeatatrrHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQL--QTQSQRLQKHV---------SSLEAEVQ 1638
Cdd:pfam04012 96 EK--------QAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLkaRLKAAKAQEAVqtslgslstSSATDSFE 167
|
170
....*....|....*
gi 1958798727 1639 RKQNILKEMAAETNA 1653
Cdd:pfam04012 168 RIEEKIEEREARADA 182
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1267-1649 |
1.20e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.19 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1267 LACLRAQVQSSTEAFENQIraEQQTALQRLREEAETLQK--AERASLEQKSRRALEQLREQLEAEERSAQA-------AL 1337
Cdd:COG3096 559 LAELEAQLEELEEQAAEAV--EQRSELRQQLEQLRARIKelAARAPAWLAAQDALERLREQSGEALADSQEvtaamqqLL 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1338 RAEKEAEKEATLLQLR-EQLEGERRE--AVAGLEkkhSTELEQLCSSL-------------------------EAKHREV 1389
Cdd:COG3096 637 EREREATVERDELAARkQALESQIERlsQPGGAE---DPRLLALAERLggvllseiyddvtledapyfsalygPARHAIV 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1390 ISNLQ--KK--------------IEG-----------AQQKEEA--------QLQES-------LGRAE----------- 1416
Cdd:COG3096 714 VPDLSavKEqlagledcpedlylIEGdpdsfddsvfdAEELEDAvvvklsdrQWRYSrfpevplFGRAArekrleelrae 793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1417 ------------------QRTHQKVHQVI----------EYEQELSsLLRDKRQEVEREHERKMDKMKeeHWQEmaeare 1468
Cdd:COG3096 794 rdelaeqyakasfdvqklQRLHQAFSQFVgghlavafapDPEAELA-ALRQRRSELERELAQHRAQEQ--QLRQ------ 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1469 ryEAEERKQRADLLGHLTGELERLRRA-HERELESVRQEQDQQLEDLR--RRHRDQERKLQDLEAELSSRTKD---VKAR 1542
Cdd:COG3096 865 --QLDQLKEQLQLLNKLLPQANLLADEtLADRLEELREELDAAQEAQAfiQQHGKALAQLEPLVAVLQSDPEQfeqLQAD 942
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1543 LAQLNVQEENMRKEKQLLLD-AQRQAALEKEEAtatrrhlEEAKKEHTHLLES-KQQLRRAIDDLRVRRVELESQVDQLQ 1620
Cdd:COG3096 943 YLQAKEQQRRLKQQIFALSEvVQRRPHFSYEDA-------VGLLGENSDLNEKlRARLEQAEEARREAREQLRQAQAQYS 1015
|
490 500
....*....|....*....|....*....
gi 1958798727 1621 TQSQRLQKHVSSLEAEVQRKQNILKEMAA 1649
Cdd:COG3096 1016 QYNQVLASLKSSRDAKQQTLQELEQELEE 1044
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1163-1605 |
1.58e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1163 RLCREEEEEEkeeeeeekeeeeeeekeeeeeeekeeegeeeekeekeeeeeeeeeeekeekeeehwLYQQKEKSLSLLKt 1242
Cdd:TIGR02168 672 ILERRREIEE--------------------------------------------------------LEEKIEELEEKIA- 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1243 qlqkaaeeeekeeetqireEESQRLACLRAQVQSSTEAFEnQIRAEQQTALQRLREEAETLQKAERASlEQKSRRALEQL 1322
Cdd:TIGR02168 695 -------------------ELEKALAELRKELEELEEELE-QLRKELEELSRQISALRKDLARLEAEV-EQLEERIAQLS 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1323 REQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGErreaVAGLEKKHSTELEQLcSSLEAKHREVISNLQKKIEGAQ- 1401
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ----IEQLKEELKALREAL-DELRAELTLLNEEAANLRERLEs 828
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1402 -QKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSlLRDKRQEVEREHERKmDKMKEEHWQEMAEARERYEAEERKQRAD 1480
Cdd:TIGR02168 829 lERRIAATERRLEDLEEQIEELSEDIESLAAEIEE-LEELIEELESELEAL-LNERASLEEALALLRSELEELSEELREL 906
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1481 L--LGHLTGELERLRR---AHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLnvqeENMRK 1555
Cdd:TIGR02168 907 EskRSELRRELEELREklaQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRL----ENKIK 982
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1556 EkqllLDAQRQAALEKEEATATRRhlEEAKKEHTHLLESKQQLRRAIDDL 1605
Cdd:TIGR02168 983 E----LGPVNLAAIEEYEELKERY--DFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1265-1810 |
1.69e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1265 QRLACLRAQVQSSTEAFEnQIRAEQ---QTALQRLREEAETLQKAERASLEQKSRR--ALEQLREQLEAEErSAQAALRA 1339
Cdd:TIGR02169 364 EELEDLRAELEEVDKEFA-ETRDELkdyREKLEKLKREINELKRELDRLQEELQRLseELADLNAAIAGIE-AKINELEE 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1340 EKEA------EKEATLLQLREQLEGERREavagLEKKhSTELEQLCSSLEAKHREVISNL-QKKIEGAQQKEEAQLQESL 1412
Cdd:TIGR02169 442 EKEDkaleikKQEWKLEQLAADLSKYEQE----LYDL-KEEYDRVEKELSKLQRELAEAEaQARASEERVRGGRAVEEVL 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1413 GRAEQRTHQKVHQVIEYEQELSSLLR----------------DKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERK 1476
Cdd:TIGR02169 517 KASIQGVHGTVAQLGSVGERYATAIEvaagnrlnnvvveddaVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSED 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1477 QRADLLGHL-----------------TGELERLRRAHE----------------------------RELESVRQEQDQQL 1511
Cdd:TIGR02169 597 GVIGFAVDLvefdpkyepafkyvfgdTLVVEDIEAARRlmgkyrmvtlegelfeksgamtggsrapRGGILFSRSEPAEL 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1512 EDLRRRhrdqerkLQDLEAELSS----------RTKDVKARLAQLNVQEENMRKEKQLLldaQRQAALEKEEATATRRHL 1581
Cdd:TIGR02169 677 QRLRER-------LEGLKRELSSlqselrrienRLDELSQELSDASRKIGEIEKEIEQL---EQEEEKLKERLEELEEDL 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1582 EEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQL-----QTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNApph 1656
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR--- 823
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1657 pepglhiEDLRKSLGTNENQEVSSSLSLSKEGIDlsmdsvrhflsaegvavrsakeflvrqtrSMRRRQTALKAAQQHWR 1736
Cdd:TIGR02169 824 -------LTLEKEYLEKEIQELQEQRIDLKEQIK-----------------------------SIEKEIENLNGKKEELE 867
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798727 1737 HELASAQEVDEDLpgTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLE---SSLLEEVSDEDTLKGS 1810
Cdd:TIGR02169 868 EELEELEAALRDL--ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKaklEALEEELSEIEDPKGE 942
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1195-1650 |
2.18e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1195 EkeeegeeeekeekeeeeeeeeeeekeekeeehwlyqQKEKSLSLLKTQLqkaaeeeekeeetqirEEESQRLACLRAQV 1274
Cdd:TIGR02168 450 E------------------------------------ELQEELERLEEAL----------------EELREELEEAEQAL 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1275 QsSTEAFENQIRAEqQTALQRLREEAETLQKAERASLEQKSRRA--LEQLREQLEAEE-------------------RSA 1333
Cdd:TIGR02168 478 D-AAERELAQLQAR-LDSLERLQENLEGFSEGVKALLKNQSGLSgiLGVLSELISVDEgyeaaieaalggrlqavvvENL 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1334 QAALRA----EKEAEKEATLLQLRE----QLEGERREAVAGLEKKHSTELEqlCSSLEAKHREVIS-------------- 1391
Cdd:TIGR02168 556 NAAKKAiaflKQNELGRVTFLPLDSikgtEIQGNDREILKNIEGFLGVAKD--LVKFDPKLRKALSyllggvlvvddldn 633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1392 --NLQKKIEG------------------------------AQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSL--- 1436
Cdd:TIGR02168 634 alELAKKLRPgyrivtldgdlvrpggvitggsaktnssilERRREIEELEEKIEELEEKIAELEKALAELRKELEELeee 713
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1437 LRDKRQEVERE----HERKMDKMKEEHWQEmaeARERYEAEERKQRADLLGHLTGELERLR--RAHERELESVRQEQDQQ 1510
Cdd:TIGR02168 714 LEQLRKELEELsrqiSALRKDLARLEAEVE---QLEERIAQLSKELTELEAEIEELEERLEeaEEELAEAEAEIEELEAQ 790
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1511 LEDLRRRHRDQERKLQDLEAELSsrtkDVKARLAQLNVQEENMRKE----KQLLLDAQRQAALEKEEATA-------TRR 1579
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAELT----LLNEEAANLRERLESLERRiaatERRLEDLEEQIEELSEDIESlaaeieeLEE 866
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1580 HLEEAKKEHTHLLESKQQLRRAIDDLRVRRV-------ELESQVDQLQTQSQRLQKHVSSLEAEVQR-KQNI--LKEMAA 1649
Cdd:TIGR02168 867 LIEELESELEALLNERASLEEALALLRSELEelseelrELESKRSELRRELEELREKLAQLELRLEGlEVRIdnLQERLS 946
|
.
gi 1958798727 1650 E 1650
Cdd:TIGR02168 947 E 947
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1486-1813 |
2.50e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1486 TGELERLRRAHERELESVRQEqdqqLEDLRRRHRDQERKLQDLEAELSsRTKDVKARLAQLNVQEENMRKEKQLLLDAQR 1565
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLRE----INEISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRKLEEKIR 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1566 Q-----AALEK-----EEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLE- 1634
Cdd:PRK03918 263 EleeriEELKKeieelEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEe 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1635 -----AEVQRKQNILKE--------MAAETNAPPHPEP--GLHIEDLRKSLGTNEN--QEVSSSL--------SLSKEGI 1689
Cdd:PRK03918 343 lkkklKELEKRLEELEErhelyeeaKAKKEELERLKKRltGLTPEKLEKELEELEKakEEIEEEIskitarigELKKEIK 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1690 DLsMDSVRHFLSAEGVAVRSAKEFLVRQTRSMRRRQTA-LKAAqqhwRHELASAQEVDEDLpgTKVLENVRKNLDEETKH 1768
Cdd:PRK03918 423 EL-KKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAeLKRI----EKELKEIEEKERKL--RKELRELEKVLKKESEL 495
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958798727 1769 LdemksAMRKGHDLLKKKEEKLNQLESSLLEEVSDE-DTLKGSSIK 1813
Cdd:PRK03918 496 I-----KLKELAEQLKELEEKLKKYNLEELEKKAEEyEKLKEKLIK 536
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1231-1530 |
2.68e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.43 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1231 QQKEKSLSLL--KTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAER 1308
Cdd:pfam17380 303 QEKEEKAREVerRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELER 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1309 ASLEQKSRRalEQLREQLEAEER-SAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKHSTELEQLcsSLEAKHR 1387
Cdd:pfam17380 383 LQMERQQKN--ERVRQELEAARKvKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERV--RLEEQER 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1388 evisnlQKKIEGAQQKEEAQLQESLG-----RAEQRTHQKVHQVIEYEQElssllRDKRQEVEREHERKMDKMKEEHWQE 1462
Cdd:pfam17380 459 ------QQQVERLRQQEEERKRKKLElekekRDRKRAEEQRRKILEKELE-----ERKQAMIEEERKRKLLEKEMEERQK 527
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798727 1463 MAEARERYEAEERKQRADLlghltgELERLRRAHEREL----ESVRQEQDQQLEDLRRRHRDQERKLQDLEA 1530
Cdd:pfam17380 528 AIYEEERRREAEEERRKQQ------EMEERRRIQEQMRkateERSRLEAMEREREMMRQIVESEKARAEYEA 593
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1313-1579 |
3.22e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1313 QKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQlreqlegERREAVAGLEKKHSTELEqlcssLEAKHREvISN 1392
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQ-------ERREALQRLAEYSWDEID-----VASAERE-IAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1393 LQKKIEGAQQ--KEEAQLQESLGRAEQRthqkvhqvieyEQELSSLLRDKRQEvEREHERKMDKMKEEHWQEMAEARERY 1470
Cdd:COG4913 673 LEAELERLDAssDDLAALEEQLEELEAE-----------LEELEEELDELKGE-IGRLEKELEQAEEELDELQDRLEAAE 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1471 EAEERKQRADLlghltgeLERLRRAHERELES-VRQEQDQQLEDLRRRHRDQERKL---------------QDLEAELSS 1534
Cdd:COG4913 741 DLARLELRALL-------EERFAAALGDAVEReLRENLEERIDALRARLNRAEEELeramrafnrewpaetADLDADLES 813
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1958798727 1535 RTkDVKARLAQLnVQEENMRKE---KQLLLDAQRQ------AALEKEEATATRR 1579
Cdd:COG4913 814 LP-EYLALLDRL-EEDGLPEYEerfKELLNENSIEfvadllSKLRRAIREIKER 865
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1304-1541 |
4.25e-06 |
|
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: 51.30 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1304 QKAERASLEQK---SRRALEQLREQLEAEERSAQAALRAEKEAEKE-ATLLQLREQLEGERREAVAGLEKKhSTELEQLC 1379
Cdd:COG4942 18 QADAAAEAEAEleqLQQEIAELEKELAALKKEEKALLKQLAALERRiAALARRIRALEQELAALEAELAEL-EKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1380 SSLEAKhREVISNLQKKIEGAQQKEEAQL---QESLGRAEQRThQKVHQVIEYEQELSSLLRDKRQEVEReherkmdkmK 1456
Cdd:COG4942 97 AELEAQ-KEELAELLRALYRLGRQPPLALllsPEDFLDAVRRL-QYLKYLAPARREQAEELRADLAELAA---------L 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1457 EEHWQEMAEARERYEAEERKQRADLLghltgELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRT 1536
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALE-----ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
....*
gi 1958798727 1537 KDVKA 1541
Cdd:COG4942 241 ERTPA 245
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
1486-1646 |
4.71e-06 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 49.38 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1486 TGELERLRRAHERELESVRQEQdQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQeenMRKEKQLLldaQR 1565
Cdd:pfam14988 49 TAELQTQLLQKEKEQASLKKEL-QALRPFAKLKESQEREIQDLEEEKEKVRAETAEKDREAHLQ---FLKEKALL---EK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1566 QAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEaevQRKQNILK 1645
Cdd:pfam14988 122 QLQELRILELGERATRELKRKAQALKLAAKQALSEFCRSIKRENRQLQKELLQLIQETQALEAIKSKLE---NRKQRLKE 198
|
.
gi 1958798727 1646 E 1646
Cdd:pfam14988 199 E 199
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1226-1836 |
4.98e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.65 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1226 EHWLYQQKEK-SLSLLKTQlqkaaeeeekeEETQIREEESQRLACLRAQVQSSTEAFEnQIRAEQQTA-LQ---RLREEA 1300
Cdd:pfam05483 154 RHLCNLLKETcARSAEKTK-----------KYEYEREETRQVYMDLNNNIEKMILAFE-ELRVQAENArLEmhfKLKEDH 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1301 ETLQKaerasLEQKSRRaleqlreqlEAEERSAQAALRAEKEAEKEATLLQLREQLEgERREAVAGLEKKHSTELEQLCS 1380
Cdd:pfam05483 222 EKIQH-----LEEEYKK---------EINDKEKQVSLLLIQITEKENKMKDLTFLLE-ESRDKANQLEEKTKLQDENLKE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1381 SLEAKH------REVISNLQKKIEgAQQKEEAQLQESLGRAEQRTHQKVHQ--------------VIEYEQ---ELSSLL 1437
Cdd:pfam05483 287 LIEKKDhltkelEDIKMSLQRSMS-TQKALEEDLQIATKTICQLTEEKEAQmeelnkakaahsfvVTEFEAttcSLEELL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1438 RDKRQEVER-EHERKMDKM----KEEHWQEMAEARERYEAEERKqradlLGHLTGELERLRRaHERELESVRQEQDQQLE 1512
Cdd:pfam05483 366 RTEQQRLEKnEDQLKIITMelqkKSSELEEMTKFKNNKEVELEE-----LKKILAEDEKLLD-EKKQFEKIAEELKGKEQ 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1513 DLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEK-----------QLLLDAQR----------QAALEK 1571
Cdd:pfam05483 440 ELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKlknieltahcdKLLLENKEltqeasdmtlELKKHQ 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1572 EEATATRRHLEEAKKEHTHLLESKQQLRraiDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAET 1651
Cdd:pfam05483 520 EDIINCKKQEERMLKQIENLEEKEMNLR---DELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKC 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1652 NapphpepGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKEFLVRQTRSMRRRQTALKAA 1731
Cdd:pfam05483 597 N-------NLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKIS 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1732 QQHWRHELASAQE-VDEDLpgtkvleNVRKNLDEETKH-LDEMKSAMRKGHD--------------LLKKKEEKLNQLES 1795
Cdd:pfam05483 670 EEKLLEEVEKAKAiADEAV-------KLQKEIDKRCQHkIAEMVALMEKHKHqydkiieerdselgLYKNKEQEQSSAKA 742
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1958798727 1796 SLLEEVSDEDTLKGSSIKKVTFDLSDMDDLSSESFESCPLL 1836
Cdd:pfam05483 743 ALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAIL 783
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1265-1658 |
6.55e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 51.75 E-value: 6.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1265 QRLACLRAQVQSSTE---AFENQIRAEQQTALQRL----REEAETLQKAERASLEqksrRALEQLREQLEAEERSAQAA- 1336
Cdd:NF041483 134 QELAERRQTVESHVNenvAWAEQLRARTESQARRLldesRAEAEQALAAARAEAE----RLAEEARQRLGSEAESARAEa 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1337 ----LRAEKEAEK----------EAT--LLQLREQLEGERREAvagleKKHSTEL----EQLCSSLEAKHREVISNLQKK 1396
Cdd:NF041483 210 eailRRARKDAERllnaastqaqEATdhAEQLRSSTAAESDQA-----RRQAAELsraaEQRMQEAEEALREARAEAEKV 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1397 IEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVER-------EHERKMDKMKEEHWQEMAEARER 1469
Cdd:NF041483 285 VAEAKEAAAKQLASAESANEQRTRTAKEEIARLVGEATKEAEALKAEAEQaladaraEAEKLVAEAAEKARTVAAEDTAA 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1470 YEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQErklQDLEAELSSRTKDVKARLAQLNVQ 1549
Cdd:NF041483 365 QLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQA---EQLKGAAKDDTKEYRAKTVELQEE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1550 EENMRKEKQLLL------------DAQRQAALEKEEATATRRHL----------------EEAKKEHTHLLESKQQLRRA 1601
Cdd:NF041483 442 ARRLRGEAEQLRaeavaegerirgEARREAVQQIEEAARTAEELltkakadadelrstatAESERVRTEAIERATTLRRQ 521
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798727 1602 IDDL--RVR------RVELESQVDQLQTQSQRlqkHVSSLEAEVQRKQNILKEMAAETNAPPHPE 1658
Cdd:NF041483 522 AEETleRTRaeaerlRAEAEEQAEEVRAAAER---AARELREETERAIAARQAEAAEELTRLHTE 583
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1487-1651 |
7.43e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.05 E-value: 7.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1487 GELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDV---KARLAQLNVQEENMRKEKQLLLDA 1563
Cdd:pfam07888 44 AELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHeelEEKYKELSASSEELSEEKDALLAQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1564 -----QRQAALEKEEATATRRHLEeakkEHTHLLESKQQLRRAIDDLRvrrvELESQVDQLQTQSQRLQKHVSSLEAEVQ 1638
Cdd:pfam07888 124 raaheARIRELEEDIKTLTQRVLE----RETELERMKERAKKAGAQRK----EEEAERKQLQAKLQQTEEELRSLSKEFQ 195
|
170
....*....|...
gi 1958798727 1639 RKQNILKEMAAET 1651
Cdd:pfam07888 196 ELRNSLAQRDTQV 208
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1316-1646 |
9.07e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1316 RRALEQLREQLEAE-----ERSAQAALRAEK--------------------EAEKEATLLQLREQLeGERREAVAGLEKK 1370
Cdd:PRK04863 781 RAAREKRIEQLRAEreelaERYATLSFDVQKlqrlhqafsrfigshlavafEADPEAELRQLNRRR-VELERALADHESQ 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1371 HSTELEQLCSSleakhREVISNLQKKI-------EGAQQKEEAQLQESLGRAEQ-----RTHQKvhQVIEYEQELSSLlr 1438
Cdd:PRK04863 860 EQQQRSQLEQA-----KEGLSALNRLLprlnllaDETLADRVEEIREQLDEAEEakrfvQQHGN--ALAQLEPIVSVL-- 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1439 dkrqeveREHERKMDKMKEEHWQemaearERYEAEERKQRADLLGHLtgeleRLRRAHERELESVR-QEQDQQL-EDLRR 1516
Cdd:PRK04863 931 -------QSDPEQFEQLKQDYQQ------AQQTQRDAKQQAFALTEV-----VQRRAHFSYEDAAEmLAKNSDLnEKLRQ 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1517 RHRDQERKLQDLEAELssrtKDVKARLAQLNvqeenmrkekqllldaQRQAALeKEEATATRRHLEEAKKEHTHL----- 1591
Cdd:PRK04863 993 RLEQAEQERTRAREQL----RQAQAQLAQYN----------------QVLASL-KSSYDAKRQMLQELKQELQDLgvpad 1051
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798727 1592 --LESKqqlrraiddLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKE 1646
Cdd:PRK04863 1052 sgAEER---------ARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRK 1099
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1231-1450 |
1.14e-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: 50.15 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1231 QQKEKSLSLLKTQLQKAAEEEEKEEETQIREEesQRLACLRAQVQSSTE---AFENQIrAEQQTALQRLREEAETLQKae 1307
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALL--KQLAALERRIAALARrirALEQEL-AALEAELAELEKEIAELRA-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1308 raSLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKhSTELEQLCSSLEAKHR 1387
Cdd:COG4942 98 --ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD-LAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798727 1388 EVISNLQKKIE-----GAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHER 1450
Cdd:COG4942 175 ELEALLAELEEeraalEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1287-1566 |
1.17e-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: 50.59 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1287 AEQQTALQRLREEAETLQKAERASLEQkSRRALEQLREQLEAeersaqaaLRAEKeAEKEATLLQLREQLEGERREAVAG 1366
Cdd:pfam10174 446 SEKERIIERLKEQREREDRERLEELES-LKKENKDLKEKVSA--------LQPEL-TEKESSLIDLKEHASSLASSGLKK 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1367 LEKKHSTELE-----QLCSSLEAKHREV----------------ISNLQKkiEGAQQKEEA--------QLQESLGRAEQ 1417
Cdd:pfam10174 516 DSKLKSLEIAveqkkEECSKLENQLKKAhnaeeavrtnpeindrIRLLEQ--EVARYKEESgkaqaeveRLLGILREVEN 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1418 RTHQKVHQVIEYEQELSSLLRDKRQEVeREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRR--- 1494
Cdd:pfam10174 594 EKNDKDKKIAELESLTLRQMKEQNKKV-ANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQeld 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1495 AHERELESVRQ---EQDQQLEDLRRRHRDQ-----ERKLQDLEAELSSrtKDVKARLAQLN------VQEENM--RKEKQ 1558
Cdd:pfam10174 673 ATKARLSSTQQslaEKDGHLTNLRAERRKQleeilEMKQEALLAAISE--KDANIALLELSsskkkkTQEEVMalKREKD 750
|
....*...
gi 1958798727 1559 LLLDAQRQ 1566
Cdd:pfam10174 751 RLVHQLKQ 758
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1489-1643 |
1.48e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 49.25 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1489 LERLRRAHERELESVRQEqDQQLedlrrrhRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRqAA 1568
Cdd:smart00787 142 LEGLKEGLDENLEGLKED-YKLL-------MKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAK-EK 212
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798727 1569 LEKEEatatrRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKH----VSSLEAEVQRKQNI 1643
Cdd:smart00787 213 LKKLL-----QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFtfkeIEKLKEQLKLLQSL 286
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1270-1426 |
1.51e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 48.28 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1270 LRAQVQSSTEAFENQIRAEQQTalqrLREEAETLQKAERASLEQK-SRRALEQLREQLEAE----ERSAQAALRAEKE-- 1342
Cdd:COG1842 10 IRANINALLDKAEDPEKMLDQA----IRDMEEDLVEARQALAQVIaNQKRLERQLEELEAEaekwEEKARLALEKGREdl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1343 ----AEKEATLLQLREQLEgerreavaglekkhsTELEQLcSSLEAKHREVISNLQKKIEGA-QQKEEAQLQESLGRAEQ 1417
Cdd:COG1842 86 areaLERKAELEAQAEALE---------------AQLAQL-EEQVEKLKEALRQLESKLEELkAKKDTLKARAKAAKAQE 149
|
....*....
gi 1958798727 1418 RTHQKVHQV 1426
Cdd:COG1842 150 KVNEALSGI 158
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
58-87 |
1.53e-05 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 43.26 E-value: 1.53e-05
10 20 30
....*....|....*....|....*....|
gi 1958798727 58 LPKGWKPCQNITGDLYYFNFDTGQSIWDHP 87
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1416-1643 |
1.72e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1416 EQRTHQKVHQVIEYEQELSSLLRDKRQEVErEHERKMDKMKEEHW----QEMAEARERYEAEERKQRADLLGHLTgELER 1491
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELE-EAEAALEEFRQKNGlvdlSEEAKLLLQQLSELESQLAEARAELA-EAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1492 LRRAHERELESVRQE-----QDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKE-KQLLLDAQR 1565
Cdd:COG3206 241 RLAALRAQLGSGPDAlpellQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEaQRILASLEA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798727 1566 QAALEKEEATATRRHLEEAKKEHTHLLESKQQLRraiddlRVRRvELESQVDQLQTQSQRLQkhvsslEAEVQRKQNI 1643
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPELEAELR------RLER-EVEVARELYESLLQRLE------EARLAEALTV 385
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1383-1640 |
2.03e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 49.26 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1383 EAKHREV--ISNLQKKIEGA---QQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKE 1457
Cdd:pfam15558 14 LARHKEEqrMRELQQQAALAweeLRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1458 EHWQEmaearerYEAEERKQRadllghltgeLERLRRAHERElESVRQEQDQQL---EDLRRRHRDQERKLQDLEAELSS 1534
Cdd:pfam15558 94 SRWRE-------QAEDQENQR----------QEKLERARQEA-EQRKQCQEQRLkekEEELQALREQNSLQLQERLEEAC 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1535 RTKDVKARLAQLNVQEENMRKE-----KQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRaiddlRVRR 1609
Cdd:pfam15558 156 HKRQLKEREEQKKVQENNLSELlnhqaRKVLVDCQAKAEELLRRLSLEQSLQRSQENYEQLVEERHRELRE-----KAQK 230
|
250 260 270
....*....|....*....|....*....|...
gi 1958798727 1610 VELESQVDQLQT--QSQRLQKHVSSLEAEVQRK 1640
Cdd:pfam15558 231 EEEQFQRAKWRAeeKEEERQEHKEALAELADRK 263
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1283-1571 |
2.14e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 48.88 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1283 NQIRAEQQTALQRLREEAETLQKAERASLEQKSR------------RALEQLREQ--LEAEERSAQAA---LRAEKEAEK 1345
Cdd:pfam15558 88 QVIEKESRWREQAEDQENQRQEKLERARQEAEQRkqcqeqrlkekeEELQALREQnsLQLQERLEEAChkrQLKEREEQK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1346 EATLLQLREQLEGERREAvaGLEKKHSTELEQLCSSLEAKHREVISNLQKKIE-------GAQQKEEAQLQESLGRAEQR 1418
Cdd:pfam15558 168 KVQENNLSELLNHQARKV--LVDCQAKAEELLRRLSLEQSLQRSQENYEQLVEerhrelrEKAQKEEEQFQRAKWRAEEK 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1419 THQ-KVHQvieyeqELSSLLRDKRQEVEREHERKMDKMKEEHWQEmaeareryeAEERKQRADLLghLTGELERLRRAHE 1497
Cdd:pfam15558 246 EEErQEHK------EALAELADRKIQQARQVAHKTVQDKAQRARE---------LNLEREKNHHI--LKLKVEKEEKCHR 308
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958798727 1498 RELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKarlaqlnvQEENMRKEKQLLLDAQRQAALEK 1571
Cdd:pfam15558 309 EGIKEAIKKKEQRSEQISREKEATLEEARKTARASFHMREKVR--------EETNNRTFDKMALEAQLHASLQR 374
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1264-1408 |
2.56e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 49.32 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1264 SQRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRaLEQLREQLEAE-----ERSAQAALR 1338
Cdd:PRK12705 32 AKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEER-LVQKEEQLDARaekldNLENQLEER 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1339 AEKEAEKEATLLQLREQLEgERREAVAGLEKKHSTELeqLCSSLEAKhreviSNLQKKIEGAQQKEEAQL 1408
Cdd:PRK12705 111 EKALSARELELEELEKQLD-NELYRVAGLTPEQARKL--LLKLLDAE-----LEEEKAQRVKKIEEEADL 172
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1289-1814 |
2.69e-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: 49.44 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1289 QQTALQRLREEAETLQKAErasleQKSRRALEQLREQLEAEERSAqAALRAEKEA------EKEATLLQLREQLE--GER 1360
Cdd:pfam10174 301 KESELLALQTKLETLTNQN-----SDCKQHIEVLKESLTAKEQRA-AILQTEVDAlrlrleEKESFLNKKTKQLQdlTEE 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1361 REAVAGlekkhstELEQLCSSLEAKHREvISNLQKKIEgaqqkeeaqlqeslgraeqrthqkvhqvieyeqELSSLLRDK 1440
Cdd:pfam10174 375 KSTLAG-------EIRDLKDMLDVKERK-INVLQKKIE---------------------------------NLQEQLRDK 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1441 RQEVEREHERkMDKMKEEHWQEMAEARERYEAEERKQRAdllghltgeLERLRRAHERElesvRQEQDQQLEDLRRRHRD 1520
Cdd:pfam10174 414 DKQLAGLKER-VKSLQTDSSNTDTALTTLEEALSEKERI---------IERLKEQRERE----DRERLEELESLKKENKD 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1521 QERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAkkehtHLLESKQQLRR 1600
Cdd:pfam10174 480 LKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKA-----HNAEEAVRTNP 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1601 AIDDlRVRrvELESQVDQLQTQSQRLQkhvssleAEVQRKQNILKEMAAETNapphpepglhieDLRKSLGTNENQEVSS 1680
Cdd:pfam10174 555 EIND-RIR--LLEQEVARYKEESGKAQ-------AEVERLLGILREVENEKN------------DKDKKIAELESLTLRQ 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1681 SLSLSKEGIDLSmdsvrhflSAEGVAVRSAKEFLVRQtrsmRRRQTALKAAQQHWRHE--LASAQEVDEDLPGTKV-LEN 1757
Cdd:pfam10174 613 MKEQNKKVANIK--------HGQQEMKKKGAQLLEEA----RRREDNLADNSQQLQLEelMGALEKTRQELDATKArLSS 680
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958798727 1758 VRKNLDEETKHLDEMKSAMRkghdllKKKEEKLNQLESSLLEEVSDEDT----LKGSSIKK 1814
Cdd:pfam10174 681 TQQSLAEKDGHLTNLRAERR------KQLEEILEMKQEALLAAISEKDAnialLELSSSKK 735
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1265-1642 |
2.95e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.57 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1265 QRLACLRAQVQSSTEAFEnQIRaEQQTALQRLREEA-----ETLQ------KAERASLEQKSR------RALEQLREQLE 1327
Cdd:COG3096 850 RELAQHRAQEQQLRQQLD-QLK-EQLQLLNKLLPQAnlladETLAdrleelREELDAAQEAQAfiqqhgKALAQLEPLVA 927
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1328 AEERSAQ--AALRAEKEAEKEaTLLQLREQLEG-----ERREAVAglekkHSTELEQLCSSleakhreviSNLQKKIEga 1400
Cdd:COG3096 928 VLQSDPEqfEQLQADYLQAKE-QQRRLKQQIFAlsevvQRRPHFS-----YEDAVGLLGEN---------SDLNEKLR-- 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1401 QQKEEAQLQESlgRAEQRTHQKVHQVIEYEQELSSLL--RDKRQEVEREHERKMdkmkeehwQEMAEARERYEAEERKQR 1478
Cdd:COG3096 991 ARLEQAEEARR--EAREQLRQAQAQYSQYNQVLASLKssRDAKQQTLQELEQEL--------EELGVQADAEAEERARIR 1060
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1479 ADllgHLTGELERLRrAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELS------------SRTKDVKARLA-- 1544
Cdd:COG3096 1061 RD---ELHEELSQNR-SRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVqakagwcavlrlARDNDVERRLHrr 1136
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1545 QLNVQE-ENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHL---LESKQQLRRAI-------DD----LRVRR 1609
Cdd:COG3096 1137 ELAYLSaDELRSMSDKALGALRLAVADNEHLRDALRLSEDPRRPERKVqfyIAVYQHLRERIrqdiirtDDpveaIEQME 1216
|
410 420 430
....*....|....*....|....*....|....*....
gi 1958798727 1610 VELESQVDQLQTQSQRLQkhVSS------LEAEVQRKQN 1642
Cdd:COG3096 1217 IELARLTEELTSREQKLA--ISSesvaniIRKTIQREQN 1253
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1479-1673 |
3.34e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 48.22 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1479 ADLLGHLTGELERLRRAHERELESVRQEQDQQ---LEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLnvqEENMRK 1555
Cdd:pfam09787 28 ASLKEGSGVEGLDSSTALTLELEELRQERDLLreeIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQEL---EEQLAT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1556 EKQLLLDAQRQAALEKEEataTRRHLEEAKKEHTHLLESKQQLRRAIDDLRVR----------RVELESQVDQL------ 1619
Cdd:pfam09787 105 ERSARREAEAELERLQEE---LRYLEEELRRSKATLQSRIKDREAEIEKLRNQltsksqssssQSELENRLHQLtetliq 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958798727 1620 -QTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNapphPEPGLHIEDLRKSLGTN 1673
Cdd:pfam09787 182 kQTMLEALSTEKNSLVLQLERMEQQIKELQGEGS----NGTSINMEGISDGEGTR 232
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1497-1651 |
3.73e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1497 ERELESVRQEQDQQLEDlrrrhrDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLlldaqrqaaLEKEEata 1576
Cdd:PRK12704 48 KKEAEAIKKEALLEAKE------EIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL---------LEKRE--- 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798727 1577 trRHLEEAKKEHTHLLESKQQLRRAIDDLRvrrvelESQVDQLQtqsqrlqkHVSSLEAEvQRKQNILKEMAAET 1651
Cdd:PRK12704 110 --EELEKKEKELEQKQQELEKKEEELEELI------EEQLQELE--------RISGLTAE-EAKEILLEKVEEEA 167
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1300-1584 |
4.03e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1300 AETLQKAERASLEQKSRRALEQLREQLEaeerSAQAALRaekeaEKEATLLQLREQlegerrEAVAGLEKKHSTELEQLc 1379
Cdd:COG3206 158 AEAYLEQNLELRREEARKALEFLEEQLP----ELRKELE-----EAEAALEEFRQK------NGLVDLSEEAKLLLQQL- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1380 SSLEAKhrevISNLQKKIEGAQQKEEaQLQESLGRAEQRTHQKVhqvieyEQELSSLLRDKRQEVEREHERKMDKMKEEH 1459
Cdd:COG3206 222 SELESQ----LAEARAELAEAEARLA-ALRAQLGSGPDALPELL------QSPVIQQLRAQLAELEAELAELSARYTPNH 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1460 wQEMAEareryeaeerkqradllghLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELsSRTKDV 1539
Cdd:COG3206 291 -PDVIA-------------------LRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARL-AELPEL 349
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1958798727 1540 KARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEA 1584
Cdd:COG3206 350 EAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVIDPA 394
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1279-1451 |
4.67e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1279 EAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRaLEQLREQLEaeERSAQAALRAEKEAEKEATLLQLREQLEg 1358
Cdd:PRK12704 52 EAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKR-LLQKEENLD--RKLELLEKREEELEKKEKELEQKQQELE- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1359 ERREAVAGLEKKHSTELEQlcssleakhrevISNLqkkiegaqQKEEAQlQESLGRAEQrthqkvhqviEYEQELSSLLR 1438
Cdd:PRK12704 128 KKEEELEELIEEQLQELER------------ISGL--------TAEEAK-EILLEKVEE----------EARHEAAVLIK 176
|
170
....*....|...
gi 1958798727 1439 DKRQEVEREHERK 1451
Cdd:PRK12704 177 EIEEEAKEEADKK 189
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1493-1799 |
5.29e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.36 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1493 RRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEEN-------MRKEKQLLLDAQR 1565
Cdd:PLN02939 36 RARRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDdhnrasmQRDEAIAAIDNEQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1566 QAALEKEEATATRRhLEEakkehthLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILK 1645
Cdd:PLN02939 116 QTNSKDGEQLSDFQ-LED-------LVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1646 eMAAETNAppHPE-PGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVR-----HFLSAEGVAVRSAKEFLVRqtr 1719
Cdd:PLN02939 188 -LAAQEKI--HVEiLEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLlkddiQFLKAELIEVAETEERVFK--- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1720 sMRRRQTALKAAQQHWRHELASAQEVDEDLPGTKV------LENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEklnqL 1793
Cdd:PLN02939 262 -LEKERSLLDASLRELESKFIVAQEDVSKLSPLQYdcwwekVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDK----L 336
|
....*.
gi 1958798727 1794 ESSLLE 1799
Cdd:PLN02939 337 EASLKE 342
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
59-89 |
5.63e-05 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 41.74 E-value: 5.63e-05
10 20 30
....*....|....*....|....*....|.
gi 1958798727 59 PKGWKPCQNITGDLYYFNFDTGQSIWDHPCD 89
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1191-1828 |
6.52e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.43 E-value: 6.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1191 EEEEEKEEEGEEEEKEEKEEEEEEEEEEEKEEKEEEHWLYQQKEKSLSLLKTQ--------------LQKAAEEEEKEEE 1256
Cdd:pfam02463 282 KLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKeeieelekelkeleIKREAEEEEEEEL 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1257 TQIREEESQRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERAS--LEQKSRRALEQLREQLEAEER--S 1332
Cdd:pfam02463 362 EKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARqlEDLLKEEKKEELEILEEEEESieL 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1333 AQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKHSTELEQLCSSLEAKHRE------------------------ 1388
Cdd:pfam02463 442 KQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEErsqkeskarsglkvllalikdgvg 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1389 ----VISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVER------------------ 1446
Cdd:pfam02463 522 griiSAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLipklklplksiavleidp 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1447 -------------------------EHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELE 1501
Cdd:pfam02463 602 ilnlaqldkatleadeddkrakvveGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQEL 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1502 SVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHL 1581
Cdd:pfam02463 682 QEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEE 761
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1582 EEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPEPGL 1661
Cdd:pfam02463 762 KEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALE 841
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1662 HIEDLR---------KSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKEFLVRQTRSMRRRQTALKAAQ 1732
Cdd:pfam02463 842 LKEEQKleklaeeelERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEE 921
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1733 qhWRHELASAQEVDEDLPGTKVLENVRKNLDEETKHLDEMKSAMRkghdLLKKKEEKLNQLESSLLEEVSDEdtlkgssi 1812
Cdd:pfam02463 922 --RIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKR----LLLAKEELGKVNLMAIEEFEEKE-------- 987
|
730
....*....|....*.
gi 1958798727 1813 KKVTFDLSDMDDLSSE 1828
Cdd:pfam02463 988 ERYNKDELEKERLEEE 1003
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1229-1570 |
7.16e-05 |
|
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: 48.03 E-value: 7.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1229 LYQQKEKslsllktqlqkaaeeeekeeetqireeeSQRLACLRAQVQSSTEAFENQIRA--EQQTALQRLREEAETLQKA 1306
Cdd:COG5185 270 LGENAES----------------------------SKRLNENANNLIKQFENTKEKIAEytKSIDIKKATESLEEQLAAA 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1307 E-RASLEQKSRR---ALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKhSTELEQLCSSL 1382
Cdd:COG5185 322 EaEQELEESKREtetGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIEST-KESLDEIPQNQ 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1383 EAKHREVISNLQKKIeGAQQKEEAQLQeslgRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQE 1462
Cdd:COG5185 401 RGYAQEILATLEDTL-KAADRQIEELQ----RQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRS 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1463 mAEARERYEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQErklQDLEAELSSRTKDVKAR 1542
Cdd:COG5185 476 -VRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARG---YAHILALENLIPASELI 551
|
330 340 350
....*....|....*....|....*....|
gi 1958798727 1543 LAQLNVQEENM--RKEKQLLLDAQRQAALE 1570
Cdd:COG5185 552 QASNAKTDGQAanLRTAVIDELTQYLSTIE 581
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1400-1632 |
8.67e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.74 E-value: 8.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1400 AQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVER--EHERKMD---KMKEEHWQEMAEARERYEAEE 1474
Cdd:PRK10929 20 ATAPDEKQITQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLERakQYQQVIDnfpKLSAELRQQLNNERDEPRSVP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1475 RKQRADllghltgELE-RLRRAHERELESVR---QEQD-------------QQLEDLRRRHRDQERKLQDL--------E 1529
Cdd:PRK10929 100 PNMSTD-------ALEqEILQVSSQLLEKSRqaqQEQDrareisdslsqlpQQQTEARRQLNEIERRLQTLgtpntplaQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1530 AELSSRTKDVKARLAQLNvqeenmrkekQLLLdAQRQAALEKEEAtatRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRR 1609
Cdd:PRK10929 173 AQLTALQAESAALKALVD----------ELEL-AQLSANNRQELA---RLRSELAKKRSQQLDAYLQALRNQLNSQRQRE 238
|
250 260
....*....|....*....|....*
gi 1958798727 1610 VE--LESqVDQLQTQSQRLQKHVSS 1632
Cdd:PRK10929 239 AEraLES-TELLAEQSGDLPKSIVA 262
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1553-1809 |
9.07e-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: 47.07 E-value: 9.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1553 MRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSS 1632
Cdd:COG4942 1 MRKLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1633 LEAEVQRKQNilkemaaetnapphpepglHIEDLRKSLGTNENQEVSSSLSLSKEGidlSMDSVRHFLSAEGV--AVRSA 1710
Cdd:COG4942 81 LEAELAELEK-------------------EIAELRAELEAQKEELAELLRALYRLG---RQPPLALLLSPEDFldAVRRL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1711 K------EFLVRQTRSMRRRQTALKAAQQhwrhELASAQevdedlpgtKVLENVRKNLDEETKHLDEMKSAMRKghdLLK 1784
Cdd:COG4942 139 QylkylaPARREQAEELRADLAELAALRA----ELEAER---------AELEALLAELEEERAALEALKAERQK---LLA 202
|
250 260
....*....|....*....|....*
gi 1958798727 1785 KKEEKLNQLESSLLEEVSDEDTLKG 1809
Cdd:COG4942 203 RLEKELAELAAELAELQQEAEELEA 227
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1271-1409 |
9.22e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.17 E-value: 9.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1271 RAQVQSSTEAFENQIRAE---QQTALQRLREEAETLQKAERASL---EQKSRRALEQLREQLEAEERSAQAAlrAEKEAE 1344
Cdd:COG2268 194 IAEIIRDARIAEAEAEREteiAIAQANREAEEAELEQEREIETAriaEAEAELAKKKAEERREAETARAEAE--AAYEIA 271
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798727 1345 KEATLLQLREQLEGERREAVAGLEKKhsteleqlcsSLEAKHREVISNLQKKIEG----AQQKEEAQLQ 1409
Cdd:COG2268 272 EANAEREVQRQLEIAEREREIELQEK----------EAEREEAELEADVRKPAEAekqaAEAEAEAEAE 330
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1416-1805 |
1.33e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.35 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1416 EQRTHQKVHQVIEYEQELSSLLRDK--RQEVEREHERKMDKMKEEHWQEMAEARERYEAEERK--QRADLLGHLTG---E 1488
Cdd:TIGR00606 201 KVQEHQMELKYLKQYKEKACEIRDQitSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKimKLDNEIKALKSrkkQ 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1489 LERLRRAHERELESVRQEQDQQLEDLRRRH----RDQERKLQDLEAELSSRTKDVK-------------ARLA-QLNVQE 1550
Cdd:TIGR00606 281 MEKDNSELELKMEKVFQGTDEQLNDLYHNHqrtvREKERELVDCQRELEKLNKERRllnqektellveqGRLQlQADRHQ 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1551 ENMRKEKQLLLDAQRQAALEKEEATA-------------TRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVD 1617
Cdd:TIGR00606 361 EHIRARDSLIQSLATRLELDGFERGPfserqiknfhtlvIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGR 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1618 QLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPphpepglhiEDLRKSLG------TNENQEVSSSLSLSKEGIDL 1691
Cdd:TIGR00606 441 TIELKKEILEKKQEELKFVIKELQQLEGSSDRILELD---------QELRKAERelskaeKNSLTETLKKEVKSLQNEKA 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1692 SMDSVRHFLSAEGVAVRSAKEFLvRQTRSMRRRQTalKAAQQ----HWRHELASAQEVDeDLPGTKVLENVRKNLDEETK 1767
Cdd:TIGR00606 512 DLDRKLRKLDQEMEQLNHHTTTR-TQMEMLTKDKM--DKDEQirkiKSRHSDELTSLLG-YFPNKKQLEDWLHSKSKEIN 587
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1958798727 1768 HLDE---------MKSAMRKGH--DLLKKKEEKLNQLESSLLEEVSDED 1805
Cdd:TIGR00606 588 QTRDrlaklnkelASLEQNKNHinNELESKEEQLSSYEDKLFDVCGSQD 636
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1232-1584 |
1.42e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.25 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1232 QKEKSLSLLKTQLqkaaeeeekeeetqireeesqrlaclrAQVQSSTEafENQIRAEQ-QTALQRLrEEAETLQKAERAS 1310
Cdd:COG3096 386 AAEEEVDSLKSQL---------------------------ADYQQALD--VQQTRAIQyQQAVQAL-EKARALCGLPDLT 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1311 LEQKSRRaLEQLREQLEA---EERSAQAALRAEKEAEKE-ATLLQLREQLEGE--RREAvaglekkHSTELEQLCSSLEA 1384
Cdd:COG3096 436 PENAEDY-LAAFRAKEQQateEVLELEQKLSVADAARRQfEKAYELVCKIAGEveRSQA-------WQTARELLRRYRSQ 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1385 KHRevisnlqkkiegAQQkeEAQLQESLGRAEQRTHQKvHQVIEYEQELSsllrdKRQEVEREHERKMDKMKEEHWQema 1464
Cdd:COG3096 508 QAL------------AQR--LQQLRAQLAELEQRLRQQ-QNAERLLEEFC-----QRIGQQLDAAEELEELLAELEA--- 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1465 eareryeaeerkQRADLLGHLTGELERlRRAHERELESVRQEQdQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLA 1544
Cdd:COG3096 565 ------------QLEELEEQAAEAVEQ-RSELRQQLEQLRARI-KELAARAPAWLAAQDALERLREQSGEALADSQEVTA 630
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1958798727 1545 QLnvqeenmrkekQLLLDAQRQAALEKEEATATRRHLEEA 1584
Cdd:COG3096 631 AM-----------QQLLEREREATVERDELAARKQALESQ 659
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1279-1374 |
1.48e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 46.40 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1279 EAFENQIRAEQQTALQRLREEAETLQKAERASLE-----QKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLR 1353
Cdd:COG2268 256 EAETARAEAEAAYEIAEANAEREVQRQLEIAEREreielQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAK 335
|
90 100
....*....|....*....|.
gi 1958798727 1354 EQLEGERREAVAGLEKKHSTE 1374
Cdd:COG2268 336 GLAEAEGKRALAEAWNKLGDA 356
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1264-1538 |
1.62e-04 |
|
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: 46.89 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1264 SQRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQleaEERSAQAALRAEKEA 1343
Cdd:TIGR00618 609 MLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVL---PKELLASRQLALQKM 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1344 EKEatllqlREQLEGERREAVAGLEKKHSTELEQLCSSleaKHREVISNLQKKIEGAQQKEEAQLQESLGRAE-QRTHQK 1422
Cdd:TIGR00618 686 QSE------KEQLTYWKEMLAQCQTLLRELETHIEEYD---REFNEIENASSSLGSDLAAREDALNQSLKELMhQARTVL 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1423 VHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHE----- 1497
Cdd:TIGR00618 757 KARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEqflsr 836
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958798727 1498 -RELESVRQEQDQQLEDLRRRHRDQERKLQDlEAELSSRTKD 1538
Cdd:TIGR00618 837 lEEKSATLGEITHQLLKYEECSKQLAQLTQE-QAKIIQLSDK 877
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1493-1789 |
1.91e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 46.18 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1493 RRAHERELESVRQEQDQQLEDLRRRhrDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKE 1572
Cdd:pfam15558 16 RHKEEQRMRELQQQAALAWEELRRR--DQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1573 EATAT---------RRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNI 1643
Cdd:pfam15558 94 SRWREqaedqenqrQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1644 LKEMAaetnapphpepgLHieDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFL---SAEGVAVRSAKEflvrQTRS 1720
Cdd:pfam15558 174 LSELL------------NH--QARKVLVDCQAKAEELLRRLSLEQSLQRSQENYEQLveeRHRELREKAQKE----EEQF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798727 1721 MRRRQTALKAAQQHWRHELASAQEVDEDLpgTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEK 1789
Cdd:pfam15558 236 QRAKWRAEEKEEERQEHKEALAELADRKI--QQARQVAHKTVQDKAQRARELNLEREKNHHILKLKVEK 302
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1232-1546 |
2.04e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1232 QKEKSLSLLKTQLQKAAeeeekeeetqireeesQRLACLRAQVQSSTEAfenqiRAEQQTALQRLREEAETLQKaERASL 1311
Cdd:COG4372 63 QLEEELEQARSELEQLE----------------EELEELNEQLQAAQAE-----LAQAQEELESLQEEAEELQE-ELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1312 eQKSRRALEQLREQLEAEERSAQAALraekeAEKEATLLQLREQLEGERREAVAGLEKKHSTELEQLCSSLEAKHREVIS 1391
Cdd:COG4372 121 -QKERQDLEQQRKQLEAQIAELQSEI-----AEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1392 NLQKKIEGAQQkEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEehwqemAEARERYE 1471
Cdd:COG4372 195 NAEKEEELAEA-EKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE------IEELELAI 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798727 1472 AEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQL 1546
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADL 342
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1277-1398 |
2.81e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 45.26 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1277 STEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRA-LEQLREQLEAEERSAQAALRaekeaekeatllQLREQ 1355
Cdd:cd16269 178 SKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEqQRELEQKLEDQERSYEEHLR------------QLKEK 245
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1958798727 1356 LEGERREAVAGLEKKHSTELEQLCSSLEAKHREVISNLQKKIE 1398
Cdd:cd16269 246 MEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIR 288
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1381-1546 |
3.12e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 45.13 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1381 SLEAKHREVISNLQKKIEGAQQKEE--AQLQES---------------LGRAEQRTHQKVHQVIEYEQELSSLlRDKRQE 1443
Cdd:pfam09787 1 NLESAKQELADYKQKAARILQSKEKliASLKEGsgvegldsstaltleLEELRQERDLLREEIQKLRGQIQQL-RTELQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1444 VEREHERKMDKMKEehwqemaeareryeaeerkQRADLLGHLTGElERLRRAHERELESVRQEQDQQLEDLRR------- 1516
Cdd:pfam09787 80 LEAQQQEEAESSRE-------------------QLQELEEQLATE-RSARREAEAELERLQEELRYLEEELRRskatlqs 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958798727 1517 RHRDQERKLQDLEAELSSRT------KDVKARLAQL 1546
Cdd:pfam09787 140 RIKDREAEIEKLRNQLTSKSqssssqSELENRLHQL 175
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
57-87 |
3.16e-04 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 39.89 E-value: 3.16e-04
10 20 30
....*....|....*....|....*....|.
gi 1958798727 57 PLPKGWKPCQNITGDLYYFNFDTGQSIWDHP 87
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKP 31
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1223-1799 |
3.16e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.19 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1223 KEEEHWL------------------YQQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAFEN- 1283
Cdd:TIGR00606 306 LYHNHQRtvrekerelvdcqrelekLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERg 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1284 -----QIRAEQQTALQRLREEAETLQK--AERASLEQKSRRALEQLREQLEAEERSAQaaLRAEKEAEKEATLLQLREQL 1356
Cdd:TIGR00606 386 pfserQIKNFHTLVIERQEDEAKTAAQlcADLQSKERLKQEQADEIRDEKKGLGRTIE--LKKEILEKKQEELKFVIKEL 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1357 EgerrEAVAGLEK--KHSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELs 1434
Cdd:TIGR00606 464 Q----QLEGSSDRilELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQME- 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1435 SLLRDKRQEVEReherkMDKMKEEHWQEMaeARERYEAEERKQRADLLGHLTGELERLRraheRELESVRQEQdQQLEDL 1514
Cdd:TIGR00606 539 MLTKDKMDKDEQ-----IRKIKSRHSDEL--TSLLGYFPNKKQLEDWLHSKSKEINQTR----DRLAKLNKEL-ASLEQN 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1515 RRRHRDQERKLQDLEAELSSRTKDVKARLAqLNVQEENMRKEkqlLLDAQRQAALEKEEATATRRHLEEAKKEHT----- 1589
Cdd:TIGR00606 607 KNHINNELESKEEQLSSYEDKLFDVCGSQD-EESDLERLKEE---IEKSSKQRAMLAGATAVYSQFITQLTDENQsccpv 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1590 --HLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAEtnapphpepglhIEDLR 1667
Cdd:TIGR00606 683 cqRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKE------------IPELR 750
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1668 kslgtNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEgvavRSAKEFLVRQTrSMRRRQTALKAAQQHWRHELASAQEVDE 1747
Cdd:TIGR00606 751 -----NKLQKVNRDIQRLKNDIEEQETLLGTIMPEE----ESAKVCLTDVT-IMERFQMELKDVERKIAQQAAKLQGSDL 820
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1958798727 1748 DLPGTKvlenVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLESSLLE 1799
Cdd:TIGR00606 821 DRTVQQ----VNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNE 868
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1282-1369 |
3.39e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 42.42 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1282 ENQIRAEQQTAlQRLREEAETLQK---AERASLEQKSRRALEQLREqlEAEERSAQAALRAEKEAEKEatLLQLREQLEG 1358
Cdd:cd06503 32 EEKIAESLEEA-EKAKEEAEELLAeyeEKLAEARAEAQEIIEEARK--EAEKIKEEILAEAKEEAERI--LEQAKAEIEQ 106
|
90
....*....|.
gi 1958798727 1359 ERREAVAGLEK 1369
Cdd:cd06503 107 EKEKALAELRK 117
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1297-1370 |
3.74e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 42.84 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1297 REE--AETLQKAERASLEQKsrRALEQLREQL------------EAEERSAQ--AALRAEKEAEKEATLLQLREQLEGER 1360
Cdd:PRK05759 36 RQKkiADGLAAAERAKKELE--LAQAKYEAQLaearaeaaeiieQAKKRAAQiiEEAKAEAEAEAARIKAQAQAEIEQER 113
|
90
....*....|
gi 1958798727 1361 REAVAGLEKK 1370
Cdd:PRK05759 114 KRAREELRKQ 123
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1265-1406 |
4.11e-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: 44.15 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1265 QRLACLRAQVQSSTEAFEnQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEErsaqaalRAEKEAE 1344
Cdd:COG1579 38 DELAALEARLEAAKTELE-DLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIESLK-------RRISDLE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798727 1345 KEatLLQLREQLEgERREAVAGLEKKHStELEQLCSSLEAKHREVISNLQKKIEGAQQKEEA 1406
Cdd:COG1579 110 DE--ILELMERIE-ELEEELAELEAELA-ELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1484-1618 |
4.20e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 45.09 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1484 HLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQER--------KLQDLEAELSSRTKDVKARLAQLNVQEENMRK 1555
Cdd:PRK12705 30 RLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRqearrereELQREEERLVQKEEQLDARAEKLDNLENQLEE 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1556 EKQLLLDA-------QRQAALEKEEATATRRhlEEAKKEHTHLLESKQQLRRAIddlRVRRVELESQVDQ 1618
Cdd:PRK12705 110 REKALSAReleleelEKQLDNELYRVAGLTP--EQARKLLLKLLDAELEEEKAQ---RVKKIEEEADLEA 174
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1493-1650 |
4.59e-04 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 45.42 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1493 RRAHERELESVRQEQDQQLEDLRRRhrDQERK-LQDLEAELSSRTKDVKARlaqlnvQEENMRKEKQLLLDAQRQAAL-- 1569
Cdd:pfam10168 556 REEIQKRVKLLKLQKEQQLQELQSL--EEERKsLSERAEKLAEKYEEIKDK------QEKLMRRCKKVLQRLNSQLPVls 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1570 --EKEEatatrrhleeaKKEHTHLLESKQQLRRAIDDLRVRrveLESQVDQLQTQSQRLQKHVSSLEAEvQRK--QNILK 1645
Cdd:pfam10168 628 daEREM-----------KKELETINEQLKHLANAIKQAKKK---MNYQRYQIAKSQSIRKKSSLSLSEK-QRKtiKEILK 692
|
....*
gi 1958798727 1646 EMAAE 1650
Cdd:pfam10168 693 QLGSE 697
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
1488-1615 |
4.78e-04 |
|
Type III secretion protein YscO; This family contains the bacterial type III secretion protein YscO, which is approximately 150 residues long. YscO has been shown to be required for high-level expression and secretion of the anti-host proteins V antigen and Yops in Yersinia pestis.
Pssm-ID: 399954 [Multi-domain] Cd Length: 148 Bit Score: 42.39 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1488 ELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSR--------------TKDVKARLAQLNVQEENM 1553
Cdd:pfam07321 3 RLLRVKHLREDRAEKAVKRQEQALAAARAAHQQAQASLQDYRAWRPQEeqrlyaeiqgklvlLKELEKVKQQVALLRENE 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798727 1554 RKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQ 1615
Cdd:pfam07321 83 ADLEKQVAEARQQLEAEREALRQARQALAEARRAVEKFAELVRLVQAEELRQQERQEEQELE 144
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
1291-1639 |
5.24e-04 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 45.18 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1291 TALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKK 1370
Cdd:COG2203 342 IAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1371 HSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLR------DKRQEV 1444
Cdd:COG2203 422 LLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLllllllALLALS 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1445 EREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERK 1524
Cdd:COG2203 502 ALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSVLLIELAL 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1525 LQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDD 1604
Cdd:COG2203 582 ALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALALASLVLLRALLA 661
|
330 340 350
....*....|....*....|....*....|....*
gi 1958798727 1605 LRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQR 1639
Cdd:COG2203 662 TELDLILDSSLLLGLLLLGALLLLGGGLALLLSIG 696
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1417-1650 |
5.39e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1417 QRTHQKVHQVI----------EYEQELSsLLRDKRQEVEREHERkmdkmkeehwQEMAEARERYEAEERKQRADLLGHLT 1486
Cdd:PRK04863 813 QRLHQAFSRFIgshlavafeaDPEAELR-QLNRRRVELERALAD----------HESQEQQQRSQLEQAKEGLSALNRLL 881
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1487 GELERLRR-AHERELESVRQEQDQQLEDLR--RRHRDQERKLQDLEAELSSRTKD---VKARLAQLNVQEENMRKEKQLL 1560
Cdd:PRK04863 882 PRLNLLADeTLADRVEEIREQLDEAEEAKRfvQQHGNALAQLEPIVSVLQSDPEQfeqLKQDYQQAQQTQRDAKQQAFAL 961
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1561 LD-AQRQAALEKEEAtatrrhlEEAKKEHTHLLES-KQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQkhvsSLEAEVQ 1638
Cdd:PRK04863 962 TEvVQRRAHFSYEDA-------AEMLAKNSDLNEKlRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLA----SLKSSYD 1030
|
250
....*....|..
gi 1958798727 1639 RKQNILKEMAAE 1650
Cdd:PRK04863 1031 AKRQMLQELKQE 1042
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1307-1615 |
6.15e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.86 E-value: 6.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1307 ERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKeatllqlreqLEGERREAVAglEKKHSTELEQLCSSLEAK- 1385
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHN----------SYEEDSELKP--SGQGGLDEEEAFLDRTAKr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1386 HREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVErEHERKMDKMKEEHWQEMAE 1465
Cdd:pfam02029 72 EERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEE-ETEIREKEYQENKWSTEVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1466 ARERYEAEERKQRADLlghlTGELERLRRAHERELESVRQEQDQQLED---LRRRHRDQERKLQDLEAELSSRTKDVKAR 1542
Cdd:pfam02029 151 QAEEEGEEEEDKSEEA----EEVPTENFAKEEVKDEKIKKEKKVKYESkvfLDQKRGHPEVKSQNGEEEVTKLKVTTKRR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1543 LAQLNV-----QEENMRKEKQLLLDAQRQ--AALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQ 1615
Cdd:pfam02029 227 QGGLSQsqereEEAEVFLEAEQKLEELRRrrQEKESEEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAE 306
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1284-1397 |
6.32e-04 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 42.08 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1284 QIRAEQQTALQRLREEAETLqkaeRASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLegeRREA 1363
Cdd:COG0711 52 AALAEYEEKLAEARAEAAEI----IAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEV---ADLA 124
|
90 100 110
....*....|....*....|....*....|....
gi 1958798727 1364 VAGLEKKHSTELEqlcsslEAKHREVISNLQKKI 1397
Cdd:COG0711 125 VAIAEKILGKELD------AAAQAALVDRFIAEL 152
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1265-1410 |
6.38e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 42.64 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1265 QRLACLRAQVQSSTEAFENQIRAEqqtaLQRLREEAETLQKAERASLEQKsrraLEQLREQLEAEERSAQAALRAEKEAe 1344
Cdd:pfam01442 44 KDLEEVRAKLEPYLEELQAKLGQN----VEELRQRLEPYTEELRKRLNAD----AEELQEKLAPYGEELRERLEQNVDA- 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958798727 1345 keatllqLREQLEGERREAVAGLEKKhsteLEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQE 1410
Cdd:pfam01442 115 -------LRARLAPYAEELRQKLAER----LEELKESLAPYAEEVQAQLSQRLQELREKLEPQAED 169
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1461-1606 |
6.44e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.70 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1461 QEMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQER---KLQDLEAELSSRTK 1537
Cdd:PRK12705 33 KEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDAraeKLDNLENQLEEREK 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798727 1538 DVKARLAQLNVQEENMRKEkqllldAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLR 1606
Cdd:PRK12705 113 ALSARELELEELEKQLDNE------LYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAE 175
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
1284-1369 |
7.05e-04 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 41.53 E-value: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1284 QIRAEQQTALQRLREEAETLqkaeRASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGerrEA 1363
Cdd:pfam00430 51 AALAEAEQQLKEARAEAQEI----IENAKKRAEKLKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVA---LA 123
|
....*.
gi 1958798727 1364 VAGLEK 1369
Cdd:pfam00430 124 VQIAEK 129
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1537-1637 |
7.77e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.69 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1537 KDVKARLAQLNVQEENMRKEKQLLlDAQRQAALEKEEATATRRH--LEEAKKEHTHLLESKQQLRRAIDDLRVRRVELES 1614
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEA-SFERLAELRDELAELEEELeaLKARWEAEKELIEEIQELKEELEQRYGKIPELEK 492
|
90 100
....*....|....*....|...
gi 1958798727 1615 QVDQLQtqsQRLQKHVSSLEAEV 1637
Cdd:COG0542 493 ELAELE---EELAELAPLLREEV 512
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1194-1808 |
7.98e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.58 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1194 EEKEEEGEEEEKEEKEEEEEEEEEEEKEEKEEEHWLYQQKEKSLSLLKTQLQkaaeeEEKEEETQIREEESQRLACLRAQ 1273
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLY-----LDYLKLNEERIDLLQELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1274 VQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRraLEQLREQLEAEERSAQAALRAEKEAEKEATLLQLR 1353
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE--EEELKSELLKLERRKVDDEEKLKESEKEKKKAEKE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1354 EQLEGERREAVAGLEKKH--STELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQrTHQKVHQVIEYEQ 1431
Cdd:pfam02463 330 LKKEKEEIEELEKELKELeiKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE-ELELKSEEEKEAQ 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1432 ELSSLLRDKRQEVEREHERKMDKMKE-EHWQEMAEARERYEAEERKQRADLLGHLTGELER--LRRAHERELESVRQEQD 1508
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEELEILEEeEESIELKQGKLTEEKEELEKQELKLLKDELELKKseDLLKETQLVKLQEQLEL 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1509 QQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQlnvQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEh 1588
Cdd:pfam02463 489 LLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRII---SAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQ- 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1589 tHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPEPGLHIEDLRK 1668
Cdd:pfam02463 565 -KLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKA 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1669 SLGTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEgvAVRSAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDED 1748
Cdd:pfam02463 644 KESGLRKGVSLEEGLAEKSEVKASLSELTKELLEI--QELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEE 721
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958798727 1749 LPGTKVLENVRKN----LDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLESSLLEEVSDEDTLK 1808
Cdd:pfam02463 722 LLADRVQEAQDKIneelKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEK 785
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1510-1655 |
8.06e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 42.59 E-value: 8.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1510 QLEDLRRRHRDQERKLQDLEAE---LSSRTKDVKARLAQLNVQEENMRKEKQLLLDAqrqaaleKEEATATRRHLEEAKK 1586
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQEnkrLTEPLQKAQEEVEELRKQLENYEKDKQSLKNL-------KARLKVLEKELKDLKW 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1587 EHTHLLESKQQLRRAIDDLRVRRVELESQVDQ-LQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPP 1655
Cdd:pfam13851 107 EHEVLEQRFEKVERERDELYDKFEAAIQDVQQkTGLKNLLLEKKLQALGETLEKKEAQLNEVLAAANLDP 176
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1231-1613 |
8.18e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.26 E-value: 8.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1231 QQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAFENQIRAEQQTAlQRLREEAETLQKAERAS 1310
Cdd:COG3064 8 KAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAA-ELAAEAAKKLAEAEKAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1311 LEQKSRRALEQLREQLEAEERS----------AQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKHSTELEQLCS 1380
Cdd:COG3064 87 AEAEKKAAAEKAKAAKEAEAAAaaekaaaaaeKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1381 SLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVER--------EHERKM 1452
Cdd:COG3064 167 AAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAalaaveatEEAALG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1453 DKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAEl 1532
Cdd:COG3064 247 GAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAG- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1533 SSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVEL 1612
Cdd:COG3064 326 ALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRL 405
|
.
gi 1958798727 1613 E 1613
Cdd:COG3064 406 D 406
|
|
| FliJ |
COG2882 |
Flagellar biosynthesis chaperone FliJ [Cell motility]; |
1348-1453 |
8.27e-04 |
|
Flagellar biosynthesis chaperone FliJ [Cell motility];
Pssm-ID: 442129 [Multi-domain] Cd Length: 142 Bit Score: 41.81 E-value: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1348 TLLQLREQLEGERREAVAGLEKKHSTELEQLcSSLEAKHREVISNLQKKIEGA-------------QQKEEA--QLQESL 1412
Cdd:COG2882 9 TLLDLAEKEEDEAARELGQAQQALEQAEEQL-EQLEQYREEYEQRLQQKLQQGlsaaqlrnyqqfiARLDEAieQQQQQV 87
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1958798727 1413 GRAEQRTHQKVHQVIEYEQELSSL--LRDKRQEVEREHERKMD 1453
Cdd:COG2882 88 AQAEQQVEQARQAWLEARQERKALekLKERRREEERQEENRRE 130
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1287-1413 |
8.43e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 42.74 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1287 AEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLeAEERSAQAALRAEKEAEKEATLLQLREQLEgERREAVAG 1366
Cdd:pfam04012 45 LAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEEL-AREALAEKKSLEKQAEALETQLAQQRSAVE-QLRKQLAA 122
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1958798727 1367 LEKKhsteLEQlcssLEAKHREVISNLQkkiegaQQKEEAQLQESLG 1413
Cdd:pfam04012 123 LETK----IQQ----LKAKKNLLKARLK------AAKAQEAVQTSLG 155
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1189-1651 |
8.49e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 8.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1189 EEEEEEEKEEEGEEEEKEEKEEEEEEEEEEEkeekeeehwLYQQKEKSLSLLKtqlQKAAEEEEKEEETQIREEESQRLA 1268
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEE---------VRDLRERLEELEE---ERDDLLAEAGLDDADAEAVEARRE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1269 CLRA----------QVQSSTEAFENQIRAEQQTAL------QRLREEAETLQKAERASLEQ--KSRRALEQLREQLEAEE 1330
Cdd:PRK02224 318 ELEDrdeelrdrleECRVAAQAHNEEAESLREDADdleeraEELREEAAELESELEEAREAveDRREEIEELEEEIEELR 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1331 --------------------RSAQAALRaEKEAEKEATLLQLREQLE---------------------------GERREA 1363
Cdd:PRK02224 398 erfgdapvdlgnaedfleelREERDELR-EREAELEATLRTARERVEeaealleagkcpecgqpvegsphvetiEEDRER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1364 VAGLEkkhsTELEQLcssleakhREVISNLQKKIEGAQQKEEAQ-----LQESLGRAEQRTHQKvHQVIEYEQELSSLLR 1438
Cdd:PRK02224 477 VEELE----AELEDL--------EEEVEEVEERLERAEDLVEAEdrierLEERREDLEELIAER-RETIEEKRERAEELR 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1439 DKRQEVEREHERKMDKMKEEHwqEMAEARERYEAEERKQRADllghLTGELERLRRAheRELESVRQEQDQQLEDLRRRH 1518
Cdd:PRK02224 544 ERAAELEAEAEEKREAAAEAE--EEAEEAREEVAELNSKLAE----LKERIESLERI--RTLLAAIADAEDEIERLREKR 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1519 RD-QERKLQDLE--AELSSRTKDVKARLAQLNVQEenMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESk 1595
Cdd:PRK02224 616 EAlAELNDERRErlAEKRERKRELEAEFDEARIEE--AREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE- 692
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958798727 1596 qqlrraIDDLRVRRVELESQVDQLQT---QSQRLQKHVSSLEAEVqRKQNI--LKEMAAET 1651
Cdd:PRK02224 693 ------LEELRERREALENRVEALEAlydEAEELESMYGDLRAEL-RQRNVetLERMLNET 746
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1273-1410 |
8.94e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.03 E-value: 8.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1273 QVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERasLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQL 1352
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQ--LEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798727 1353 REQLEGERREAVAGL----EKKHSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQE 1410
Cdd:PRK09510 148 KAEAEAKRAAAAAKKaaaeAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKK 209
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1344-1648 |
9.43e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 9.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1344 EKEATLLQLREQLEGERREAvagleKKHSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEaqlqeslgraeqrthqKV 1423
Cdd:COG1340 8 SSLEELEEKIEELREEIEEL-----KEKRDELNEELKELAEKRDELNAQVKELREEAQELRE----------------KR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1424 HQVIEYEQELssllRDKRQEVEREHERKMDKMKEehwqemaeareryeaeeRKQRADLLGHLTGELERLRRAHERElesv 1503
Cdd:COG1340 67 DELNEKVKEL----KEERDELNEKLNELREELDE-----------------LRKELAELNKAGGSIDKLRKEIERL---- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1504 rqEQDQQLEDLRRrhrDQERKLQDLEAELSSRTKDVKarlaQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRrhlEE 1583
Cdd:COG1340 122 --EWRQQTEVLSP---EEEKELVEKIKELEKELEKAK----KALEKNEKLKELRAELKELRKEAEEIHKKIKELA---EE 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798727 1584 AKKEHTHLLESKQQ---LRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMA 1648
Cdd:COG1340 190 AQELHEEMIELYKEadeLRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALK 257
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
1488-1592 |
9.45e-04 |
|
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.
Pssm-ID: 463600 [Multi-domain] Cd Length: 139 Bit Score: 41.39 E-value: 9.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1488 ELERLRRAHERELESVRQEQDQQLEDLRRRHR-DQERKLQDLEAELSSRTKDVKA---RLAQLNVQEE-NMRKEKQLLLD 1562
Cdd:pfam12474 26 ELEQLERQQKQQIEKLEQRQTQELRRLPKRIRaEQKKRLKMFRESLKQEKKELKQeveKLPKFQRKEAkRQRKEELELEQ 105
|
90 100 110
....*....|....*....|....*....|
gi 1958798727 1563 AQRQAALEKEEATATRRHLEEAKKEHTHLL 1592
Cdd:pfam12474 106 KHEELEFLQAQSEALERELQQLQNEKRKEL 135
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1265-1348 |
1.01e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 41.70 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1265 QRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLeaeerSAQAALRAEKEAE 1344
Cdd:COG0711 59 EKLAEARAEAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEV-----ADLAVAIAEKILG 133
|
....
gi 1958798727 1345 KEAT 1348
Cdd:COG0711 134 KELD 137
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1476-1647 |
1.09e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.91 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1476 KQRADLLGHLtgelerlrraherelesvrQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTkdvkARLAQLNVQeenmRK 1555
Cdd:PRK11637 68 QQRASLLAQL-------------------KKQEEAISQASRKLRETQNTLNQLNKQIDELN----ASIAKLEQQ----QA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1556 EKQLLLDAQRQAALEKEEATATRRHL--EEAKKEH------THLLESKQQlrrAIDDLRVRRVELESQVDQL---QTQSQ 1624
Cdd:PRK11637 121 AQERLLAAQLDAAFRQGEHTGLQLILsgEESQRGErilayfGYLNQARQE---TIAELKQTREELAAQKAELeekQSQQK 197
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958798727 1625 RL------------------QKHVSSLEAEVQRKQNILKEM 1647
Cdd:PRK11637 198 TLlyeqqaqqqkleqarnerKKTLTGLESSLQKDQQQLSEL 238
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1264-1571 |
1.17e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1264 SQRLACLRAQV---QSSTEAFENQIRAEQQTAL-----QRLREEAETLQKAERA-----SLEQKSRRALEQLREQLEAEE 1330
Cdd:PRK04863 799 AERYATLSFDVqklQRLHQAFSRFIGSHLAVAFeadpeAELRQLNRRRVELERAladheSQEQQQRSQLEQAKEGLSALN 878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1331 RSA-QAALRAEKEAEKEATllQLREQLEgERREAVAGLEK--KHSTELEQLCSSLEAKHREvISNLQKKIEGAQQKEEAQ 1407
Cdd:PRK04863 879 RLLpRLNLLADETLADRVE--EIREQLD-EAEEAKRFVQQhgNALAQLEPIVSVLQSDPEQ-FEQLKQDYQQAQQTQRDA 954
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1408 ------LQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKE---EHWQEMAEARERYEAEERKQr 1478
Cdd:PRK04863 955 kqqafaLTEVVQRRAHFSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQaqaQLAQYNQVLASLKSSYDAKR- 1033
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1479 aDLLGHLTGELERLR-RAHERELESVRQEQDQQLEDLR--RRHRDQ-ERKLQDLEAELSSRTKDVKA---RLAQLNVQEE 1551
Cdd:PRK04863 1034 -QMLQELKQELQDLGvPADSGAEERARARRDELHARLSanRSRRNQlEKQLTFCEAEMDNLTKKLRKlerDYHEMREQVV 1112
|
330 340
....*....|....*....|
gi 1958798727 1552 NMRKEKQLLLDAQRQAALEK 1571
Cdd:PRK04863 1113 NAKAGWCAVLRLVKDNGVER 1132
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1287-1635 |
1.27e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1287 AEQQTALQRLREEAETLQKAERAslEQKSRRALEQLREQLEAEERSAQAALR---------AEKEAEKEATLLQLREqle 1357
Cdd:pfam07888 83 AELKEELRQSREKHEELEEKYKE--LSASSEELSEEKDALLAQRAAHEARIReleediktlTQRVLERETELERMKE--- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1358 geRREAVAGLEKKHSTELEQLCSSLEAKHREV--ISNLQKKIEGAQQKEEAQLQEsLGRAEQRTHQKVHQVIEYEQELSS 1435
Cdd:pfam07888 158 --RAKKAGAQRKEEEAERKQLQAKLQQTEEELrsLSKEFQELRNSLAQRDTQVLQ-LQDTITTLTQKLTTAHRKEAENEA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1436 LLRDKRQEVEREHerkmdkmkeehwqemaeareryeaeERKQRADLLGHLTGELERLRRAHERELESVRQEQDQ---QLE 1512
Cdd:pfam07888 235 LLEELRSLQERLN-------------------------ASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQltlQLA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1513 DLRRRHR-DQERKLQDLEAELSSRTKDvKARLAQLNvqEENMRKEKQLLLDAQRQAALEKE---EATATRRHLEEAKKEH 1588
Cdd:pfam07888 290 DASLALReGRARWAQERETLQQSAEAD-KDRIEKLS--AELQRLEERLQEERMEREKLEVElgrEKDCNRVQLSESRREL 366
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1958798727 1589 THLLESkqqlrraiddLRVRRVELEsqvdQLQTQSQRLQKHVSSLEA 1635
Cdd:pfam07888 367 QELKAS----------LRVAQKEKE----QLQAEKQELLEYIRQLEQ 399
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
1293-1446 |
1.42e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 43.70 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1293 LQRLREEAE-TLQKAER--ASLEQKSRRALEQLREQLEAEERSAQ--AALRAEKEAEKeatllqLREQLEGERreavagl 1367
Cdd:PRK00106 26 MKSAKEAAElTLLNAEQeaVNLRGKAERDAEHIKKTAKRESKALKkeLLLEAKEEARK------YREEIEQEF------- 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798727 1368 eKKHSTELEQLcsslEAKHREVISNLQKKIEGAQQKEEAqlqesLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVER 1446
Cdd:PRK00106 93 -KSERQELKQI----ESRLTERATSLDRKDENLSSKEKT-----LESKEQSLTDKSKHIDEREEQVEKLEEQKKAELER 161
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1493-1641 |
1.49e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.32 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1493 RRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARlAQLNVQEENMRKEKQLLLDAQRQaalEKE 1572
Cdd:COG2268 216 IAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAE-AAYEIAEANAEREVQRQLEIAER---ERE 291
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798727 1573 EAtatrrhLEEAKKEhthllESKQQLRRAIddlrVRRVELESQVDQLQTQsqrlqkhvssLEAEVQRKQ 1641
Cdd:COG2268 292 IE------LQEKEAE-----REEAELEADV----RKPAEAEKQAAEAEAE----------AEAEAIRAK 335
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
1270-1410 |
1.68e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 43.32 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1270 LRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRaleqLREQLEAEERSAQAALRAEKEAEKEATL 1349
Cdd:PRK00106 58 IKKTAKRESKALKKELLLEAKEEARKYREEIEQEFKSERQELKQIESR----LTERATSLDRKDENLSSKEKTLESKEQS 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958798727 1350 LQLREQLEGERREAVAGLEKKHSTELEQLCSSLEAKHREVI-----SNLQKKIEGAQQKEEAQLQE 1410
Cdd:PRK00106 134 LTDKSKHIDEREEQVEKLEEQKKAELERVAALSQAEAREIIlaeteNKLTHEIATRIREAEREVKD 199
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1514-1797 |
1.72e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1514 LRRRHRDQERKLQDLEAELSsRTKDVKARLaqlnvqeenmrkEKQL-LLDAQRQAALEKEEATATRRHLEEA--KKEHTH 1590
Cdd:TIGR02168 170 YKERRKETERKLERTRENLD-RLEDILNEL------------ERQLkSLERQAEKAERYKELKAELRELELAllVLRLEE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1591 LLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAEtnapphpepglhIEDLrksl 1670
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE------------ISRL---- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1671 gtnENQevssslslskegidlsmdsVRHFlsaegvavRSAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLp 1750
Cdd:TIGR02168 301 ---EQQ-------------------KQIL--------RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL- 349
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958798727 1751 gTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLESSL 1797
Cdd:TIGR02168 350 -KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1384-1560 |
1.78e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1384 AKHREVISNLQKKIEgAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELssllRDKRQEVEREHERKMD--KMKEehwq 1461
Cdd:COG1579 20 DRLEHRLKELPAELA-ELEDELAALEARLEAAKTELEDLEKEIKRLELEI----EEVEARIKKYEEQLGNvrNNKE---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1462 emaeareryeaeerkqradlLGHLTGELERLRRAHErELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKA 1541
Cdd:COG1579 91 --------------------YEALQKEIESLKRRIS-DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
|
170
....*....|....*....
gi 1958798727 1542 RLAQLNVQEENMRKEKQLL 1560
Cdd:COG1579 150 ELAELEAELEELEAEREEL 168
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
1272-1639 |
1.90e-03 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 43.26 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1272 AQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQ 1351
Cdd:COG2203 338 DQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLA 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1352 LREQLEGERREAVAGLEKK-----HSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQV 1426
Cdd:COG2203 418 LEGLLLLDLLLLLLLLRRIlllrvLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLAL 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1427 IEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELESVRQE 1506
Cdd:COG2203 498 LALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSVLLI 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1507 QDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKK 1586
Cdd:COG2203 578 ELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALALASLVLLR 657
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1958798727 1587 EHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQR 1639
Cdd:COG2203 658 ALLATELDLILDSSLLLGLLLLGALLLLGGGLALLLSIGLGLGVARLLQLSVL 710
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1193-1647 |
1.94e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1193 EEEKEEEGEEEEKEEKEEEEEEEEEEEKEekeeehwlYQQKEKSLSLLKTQLqkaaeeeekeeetqireeeSQRLACLRA 1272
Cdd:PRK03918 276 EELEEKVKELKELKEKAEEYIKLSEFYEE--------YLDELREIEKRLSRL-------------------EEEINGIEE 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1273 QVQ--SSTEAFENQIR---AEQQTALQRLREEAETLQKAeRASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKE- 1346
Cdd:PRK03918 329 RIKelEEKEERLEELKkklKELEKRLEELEERHELYEEA-KAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEi 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1347 ATLLQLREQLE---GERREAVAGLEKKHST------EL-EQLCSSLEAKHREVISNLQKKIEGAQQKEEaQLQESLGRAE 1416
Cdd:PRK03918 408 SKITARIGELKkeiKELKKAIEELKKAKGKcpvcgrELtEEHRKELLEEYTAELKRIEKELKEIEEKER-KLRKELRELE 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1417 Q---------RTHQKVHQVIEYEQELSSLLRDKRQEVEREHErkmdKMKEEhwqemaeareryeaeerkqradlLGHLTG 1487
Cdd:PRK03918 487 KvlkkeseliKLKELAEQLKELEEKLKKYNLEELEKKAEEYE----KLKEK-----------------------LIKLKG 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1488 ELERLrrahERELESVrQEQDQQLEDLRRRHRDQERKLQDLEAELSSR----TKDVKARLAQLN------VQEENMRKEK 1557
Cdd:PRK03918 540 EIKSL----KKELEKL-EELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELEpfyneyLELKDAEKEL 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1558 QLLLDAQrqaALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDD-----LRVRRVELESQVDQLQTQSQRLQKHVSS 1632
Cdd:PRK03918 615 EREEKEL---KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREE 691
|
490
....*....|....*
gi 1958798727 1633 LEAEVQRKQNILKEM 1647
Cdd:PRK03918 692 IKKTLEKLKEELEER 706
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1481-1687 |
2.20e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1481 LLGHLTGELErlrrAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLL 1560
Cdd:PHA02562 189 KIDHIQQQIK----TYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1561 LDAQRQAALEKEEATATRRH---------LEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQ---- 1627
Cdd:PHA02562 265 AKIKSKIEQFQKVIKMYEKGgvcptctqqISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLelkn 344
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798727 1628 ------KHVSSLEAEVQRKQNILKEMAAETnaPPHPEPglhIEDLRKSLgtnenQEVSSSLS-LSKE 1687
Cdd:PHA02562 345 kistnkQSLITLVDKAKKVKAAIEELQAEF--VDNAEE---LAKLQDEL-----DKIVKTKSeLVKE 401
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1283-1355 |
2.27e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.11 E-value: 2.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958798727 1283 NQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRaekeAEKEATLLQLREQ 1355
Cdd:cd06503 50 EELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEILAEAKEEAERILEQAKAEIE----QEKEKALAELRKE 118
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1611-1800 |
2.38e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1611 ELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAEtnapphpepglhIEDLRKSLGTNEN--QEVSSSLSLSKEG 1688
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE------------LEDLEKEIKRLELeiEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1689 IDlsmdsvrhflsaegvAVRSAKEF--LVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLpgTKVLENVRKNLDEET 1766
Cdd:COG1579 82 LG---------------NVRNNKEYeaLQKEIESLKRRISDLEDEILELMERIEELEEELAEL--EAELAELEAELEEKK 144
|
170 180 190
....*....|....*....|....*....|....*
gi 1958798727 1767 KHLDEMKSAMRKGHDLLKKKEEKL-NQLESSLLEE 1800
Cdd:COG1579 145 AELDEELAELEAELEELEAEREELaAKIPPELLAL 179
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
1316-1639 |
2.41e-03 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 42.87 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1316 RRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKHSTELEQLCSSLEAKHREVISNLQK 1395
Cdd:COG2203 330 LELLEALADQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1396 KIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEER 1475
Cdd:COG2203 410 ADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLL 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1476 KQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRK 1555
Cdd:COG2203 490 LLLLLLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLL 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1556 EKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEA 1635
Cdd:COG2203 570 LGLSVLLIELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALA 649
|
....
gi 1958798727 1636 EVQR 1639
Cdd:COG2203 650 LASL 653
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1416-1597 |
2.48e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.63 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1416 EQRTHQKVHQVIEYEQELSSLLRDKRQEVEREherkmDKMKEEhwQEMAEARERYEAEERKQRAdllghltgELERLRRA 1495
Cdd:pfam15709 340 AERAEMRRLEVERKRREQEEQRRLQQEQLERA-----EKMREE--LELEQQRRFEEIRLRKQRL--------EEERQRQE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1496 HE-----RELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSS----RTKDVKARLAQLNVQEENMRKEKQLLLDAQRQ 1566
Cdd:pfam15709 405 EEerkqrLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEaekqRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQ 484
|
170 180 190
....*....|....*....|....*....|.
gi 1958798727 1567 AALEKEEATATRRHLEEAKKEHTHLLESKQQ 1597
Cdd:pfam15709 485 EAEEKARLEAEERRQKEEEAARLALEEAMKQ 515
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1509-1650 |
2.53e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1509 QQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLldaqrqaaleKEEATATRRHLEEAKKEH 1588
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQA----------REELEQLEEELEQARSEL 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798727 1589 THLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAE 1650
Cdd:COG4372 76 EQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQ 137
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1273-1627 |
2.67e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.89 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1273 QVQSSTEAFENQIRAEQQTALQ-------RLREE--AETLQKAERASLEQKSRRAL------------EQLREQLE---- 1327
Cdd:NF041483 87 QLRADAERELRDARAQTQRILQehaehqaRLQAElhTEAVQRRQQLDQELAERRQTveshvnenvawaEQLRARTEsqar 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1328 -------AEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLeKKHSTELEQLCSSLEAKHREVISNL-QKKIEG 1399
Cdd:NF041483 167 rlldesrAEAEQALAAARAEAERLAEEARQRLGSEAESARAEAEAIL-RRARKDAERLLNAASTQAQEATDHAeQLRSST 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1400 AQQKEEAQLQES-LGR-AEQRThqkvhqvieyeQELSSLLRDKRQEVerehERKMDKMKEEHWQEMAEARERYEAEERKQ 1477
Cdd:NF041483 246 AAESDQARRQAAeLSRaAEQRM-----------QEAEEALREARAEA----EKVVAEAKEAAAKQLASAESANEQRTRTA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1478 RAdllghltgELERLRRAHERELESVRQEQDQQLEDLRrrhrdQERKLQDLEAELSSRTKDVKARLAQL----NVQEENM 1553
Cdd:NF041483 311 KE--------EIARLVGEATKEAEALKAEAEQALADAR-----AEAEKLVAEAAEKARTVAAEDTAAQLakaaRTAEEVL 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798727 1554 RKEKQlllDAQRQAALEKEEATATRRHLE-EAKKEHTHLLESKQQLRRAIDD----LRVRRVELESQVDQLQTQSQRLQ 1627
Cdd:NF041483 378 TKASE---DAKATTRAAAEEAERIRREAEaEADRLRGEAADQAEQLKGAAKDdtkeYRAKTVELQEEARRLRGEAEQLR 453
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1272-1389 |
3.75e-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: 42.47 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1272 AQVQSSTEAFENQIRaEQQTALQRLREEAETLQKAERASLEQKsrraLEQLREQLEAEERSAQAALRAEKEAEKEatLLQ 1351
Cdd:pfam01576 934 QKSESARQQLERQNK-ELKAKLQEMEGTVKSKFKSSIAALEAK----IAQLEEQLEQESRERQAANKLVRRTEKK--LKE 1006
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1958798727 1352 LREQLEGERREAVAGLEK--KHSTELEQLCSSLEAKHREV 1389
Cdd:pfam01576 1007 VLLQVEDERRHADQYKDQaeKGNSRMKQLKRQLEEAEEEA 1046
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1291-1391 |
3.78e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1291 TALQRLREEAETLqKAERASLEQKSRRALEQLREQLEAEERSAQ---AALRAEKEAEKEAT--LLQLREQLEgERREAVA 1365
Cdd:COG0542 411 EELDELERRLEQL-EIEKEALKKEQDEASFERLAELRDELAELEeelEALKARWEAEKELIeeIQELKEELE-QRYGKIP 488
|
90 100
....*....|....*....|....*.
gi 1958798727 1366 GLEKKHsTELEQLCSSLEAKHREVIS 1391
Cdd:COG0542 489 ELEKEL-AELEEELAELAPLLREEVT 513
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1488-1583 |
3.82e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1488 ELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQA 1567
Cdd:COG0542 415 ELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKEL 494
|
90
....*....|....*.
gi 1958798727 1568 ALEKEEATATRRHLEE 1583
Cdd:COG0542 495 AELEEELAELAPLLRE 510
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1384-1587 |
3.90e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1384 AKHREVISNLQKKIEGAQqKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRD--KRQEVEREHERKMDKMKEEHWQ 1461
Cdd:COG3883 19 QAKQKELSELQAELEAAQ-AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1462 EMAEARERYEAEERKQRADLLGHLTGeLERLRRAHERELESVRQEQdQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKA 1541
Cdd:COG3883 98 SGGSVSYLDVLLGSESFSDFLDRLSA-LSKIADADADLLEELKADK-AELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958798727 1542 RLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKE 1587
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1503-1617 |
5.04e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1503 VRQEQDQQLEDLRrrhrDQERKLQDLEAELSSRTKD----VKARLAQLNVQEENMRKEKQLLLDAQRQaalEKEEATATR 1578
Cdd:COG0542 402 VRMEIDSKPEELD----ELERRLEQLEIEKEALKKEqdeaSFERLAELRDELAELEEELEALKARWEA---EKELIEEIQ 474
|
90 100 110
....*....|....*....|....*....|....*....
gi 1958798727 1579 RHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVD 1617
Cdd:COG0542 475 ELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVT 513
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1504-1650 |
5.05e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1504 RQEQDQQLEDLRRRHRDQERKLQDLEAEL----SSRTKDVKARLAQLNVQEENMRKEKQL--LLDAQRQAALEKEEATAT 1577
Cdd:PRK11281 75 IDRQKEETEQLKQQLAQAPAKLRQAQAELealkDDNDEETRETLSTLSLRQLESRLAQTLdqLQNAQNDLAEYNSQLVSL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1578 RRHLEEAKKEHTHLLESKQQLRRAIDDLRV--------------------------RRVELE----------SQVDQLQT 1621
Cdd:PRK11281 155 QTQPERAQAALYANSQRLQQIRNLLKGGKVggkalrpsqrvllqaeqallnaqndlQRKSLEgntqlqdllqKQRDYLTA 234
|
170 180
....*....|....*....|....*....
gi 1958798727 1622 QSQRLQKHVSSLEAEVQRKQNILKEMAAE 1650
Cdd:PRK11281 235 RIQRLEHQLQLLQEAINSKRLTLSEKTVQ 263
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
1265-1344 |
5.28e-03 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 39.22 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1265 QRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLeaeerSAQAALRAEKEAE 1344
Cdd:pfam00430 58 QQLKEARAEAQEIIENAKKRAEKLKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQV-----VALAVQIAEKLLE 132
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1279-1398 |
5.31e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1279 EAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRaLEQLREQLEAeersaqaaLRAEKE------AEKEATLLQL 1352
Cdd:COG2433 376 LSIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEE-IRRLEEQVER--------LEAEVEeleaelEEKDERIERL 446
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1958798727 1353 REQLEGERREAVAGLEK-----KHSTELEQLCSSLEAKhREVISNLQKKIE 1398
Cdd:COG2433 447 ERELSEARSEERREIRKdreisRLDREIERLERELEEE-RERIEELKRKLE 496
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1272-1653 |
5.33e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.09 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1272 AQVQSSTEAF------ENQIRAEQQTALQRL----REEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAA-LRA- 1339
Cdd:PRK10246 216 EQVQSLTASLqvltdeEKQLLTAQQQQQQSLnwltRLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPARqLRPh 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1340 -EKEAEKEATLLQLREQLEgerrEAVAGLEKKHSteleqlcssleakhrevisnLQKKIEGAQQKEEAQLQESLGRAEQ- 1417
Cdd:PRK10246 296 wERIQEQSAALAHTRQQIE----EVNTRLQSTMA--------------------LRARIRHHAAKQSAELQAQQQSLNTw 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1418 -RTHQKVHQvieYEQELSSLlrdkrqeveREH--ERKMDKMKEEHWQEmaeareryEAEERKQRADLLGHLTGELERLRR 1494
Cdd:PRK10246 352 lAEHDRFRQ---WNNELAGW---------RAQfsQQTSDREQLRQWQQ--------QLTHAEQKLNALPAITLTLTADEV 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1495 AHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQrqAALEKEEA 1574
Cdd:PRK10246 412 AAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVK--TICEQEAR 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1575 TAT----RRHLEEAK-------KEHThLLESKQQLRraIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNI 1643
Cdd:PRK10246 490 IKDleaqRAQLQAGQpcplcgsTSHP-AVEAYQALE--PGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESE 566
|
410
....*....|
gi 1958798727 1644 LKEMAAETNA 1653
Cdd:PRK10246 567 AQSLRQEEQA 576
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1282-1398 |
6.20e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 6.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1282 ENQIRAEQQTA-LQRLREEAETLQKaeraSLEQKsrraLEQLREQLEAE----ERSAQAALRAEKEaEKEATLLQLREQL 1356
Cdd:PRK00409 527 ELERELEQKAEeAEALLKEAEKLKE----ELEEK----KEKLQEEEDKLleeaEKEAQQAIKEAKK-EADEIIKELRQLQ 597
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1958798727 1357 EGERREAVAglekkhsTELEQLCSSLEAKHREVISNLQKKIE 1398
Cdd:PRK00409 598 KGGYASVKA-------HELIEARKRLNKANEKKEKKKKKQKE 632
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1187-1566 |
6.29e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1187 EKEEEEEEEKEEEGEEEEKeekeeeeeeeeeeekeekeeehwLYQQKEKSLSL--LKTQLQKAAEEEEKEEETQIREEES 1264
Cdd:TIGR02169 184 ENIERLDLIIDEKRQQLER-----------------------LRREREKAERYqaLLKEKREYEGYELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1265 Q---RLACLRAQVQSSTEAFEnQIRAEQQTALQRLREEAETLqkaeRASLEQKSRRALEQLREqLEAEERSAQaalRAEK 1341
Cdd:TIGR02169 241 AierQLASLEEELEKLTEEIS-ELEKRLEEIEQLLEELNKKI----KDLGEEEQLRVKEKIGE-LEAEIASLE---RSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1342 EAEKEAtllqlrEQLEGERREAVAGLEKKHStELEQLCSSLEAKHREVISnLQKKIEGAQQKEEAQLQEsLGRAEQRTHQ 1421
Cdd:TIGR02169 312 EKEREL------EDAEERLAKLEAEIDKLLA-EIEELEREIEEERKRRDK-LTEEYAELKEELEDLRAE-LEEVDKEFAE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1422 KVHQVIEYEQELSSLLRdKRQEVEREHERKMDKMKEEHwQEMAEARERYEAEERKQRAdllghLTGELERLR---RAHER 1498
Cdd:TIGR02169 383 TRDELKDYREKLEKLKR-EINELKRELDRLQEELQRLS-EELADLNAAIAGIEAKINE-----LEEEKEDKAleiKKQEW 455
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1499 ELESVRqeqdQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNV--QEENMRKEKQLLLDAQRQ 1566
Cdd:TIGR02169 456 KLEQLA----ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARAseERVRGGRAVEEVLKASIQ 521
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1506-1650 |
6.34e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.48 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1506 EQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQlNVQEENMRKEKQLLLDAQRQAalekeEATATRRHLEEAK 1585
Cdd:pfam15709 326 EKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQ-EQLERAEKMREELELEQQRRF-----EEIRLRKQRLEEE 399
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798727 1586 KEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAE 1650
Cdd:pfam15709 400 RQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEE 464
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1344-1651 |
6.45e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 41.43 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1344 EKEATLLQLREQLEGERREAVAGLEKKHSTELEQLCSSLEA--KHRE--VISNLQKKIEGAQQKEeAQLQESLGRAEQRT 1419
Cdd:pfam15964 219 RLELEKLKLLYEAKTEVLESQVKSLRKDLAESQKTCEDLKErlKHKEslVAASTSSRVGGLCLKC-AQHEAVLAQTHTNV 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1420 H-QKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKE-EHWQEMAEARERYEAEERKQradlLGHLTGELERLRRAHE 1497
Cdd:pfam15964 298 HmQTIERLTKERDDLMSALVSVRSSLAEAQQRESSAYEQvKQAVQMTEEANFEKTKALIQ----CEQLKSELERQKERLE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1498 RELES-----------VRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKD-------VKARLAQLNVQEENMRKEKQL 1559
Cdd:pfam15964 374 KELASqqekraqekeaLRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREknslvsqLEEAQKQLASQEMDVTKVCGE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1560 LLDAQRQAALEKEEA--------TATRRHLE----EAKKEHTHLLESKQQLRRAIDDLRVRRVELeSQVDQLQTQSQRlQ 1627
Cdd:pfam15964 454 MRYQLNQTKMKKDEAekehreyrTKTGRQLEikdqEIEKLGLELSESKQRLEQAQQDAARAREEC-LKLTELLGESEH-Q 531
|
330 340
....*....|....*....|....
gi 1958798727 1628 KHVSSLEAEvQRKQNILKEMAAET 1651
Cdd:pfam15964 532 LHLTRLEKE-SIQQSFSNEAKAQA 554
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1264-1370 |
7.12e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 40.03 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1264 SQRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQkaeraSLEQKSRRALEQLREQLEAEERSAqAALRAEKEA 1343
Cdd:pfam15665 95 RQRVVELSREVEEAKRAFEEKLESFEQLQAQFEQEKRKALE-----ELRAKHRQEIQELLTTQRAQSASS-LAEQEKLEE 168
|
90 100 110
....*....|....*....|....*....|
gi 1958798727 1344 EKEATLLQLREQLE---GERREAVAGLEKK 1370
Cdd:pfam15665 169 LHKAELESLRKEVEdlrKEKKKLAEEYEQK 198
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1301-1647 |
7.20e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.36 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1301 ETLQKAERasLEQK----SRRALEQLREQL-EAEERSAQAALRAEKEAEKEAT-LLQLREQLEGERREAVAGL---EKKH 1371
Cdd:PRK04778 61 QSEEKFEE--WRQKwdeiVTNSLPDIEEQLfEAEELNDKFRFRKAKHEINEIEsLLDLIEEDIEQILEELQELlesEEKN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1372 STELEQLcsslEAKHREV--------------ISNLQKKIEGAQQK-------------EEA-----QLQESLGRAEQrt 1419
Cdd:PRK04778 139 REEVEQL----KDLYRELrksllanrfsfgpaLDELEKQLENLEEEfsqfveltesgdyVEAreildQLEEELAALEQ-- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1420 hqKVHQVIEYEQELSSLLRDKRQEVEREHerkmDKMKEEHWqemaeareryeaeerkqradLLGHLtgelerlrrAHERE 1499
Cdd:PRK04778 213 --IMEEIPELLKELQTELPDQLQELKAGY----RELVEEGY--------------------HLDHL---------DIEKE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1500 LESVRQEQDQQLEDLRRRHRDQ-ERKLQDLEAEL----SSRTKDVKARlaqlNVQEENMRKEKQLLLDAQRQAALEKEEA 1574
Cdd:PRK04778 258 IQDLKEQIDENLALLEELDLDEaEEKNEEIQERIdqlyDILEREVKAR----KYVEKNSDTLPDFLEHAKEQNKELKEEI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1575 TATRR--HLEEAKKEHTHLLESK-QQLRRAIDD--------------LRVRRVELESQVDQLQTQSQRLQKHVSSLEAEV 1637
Cdd:PRK04778 334 DRVKQsyTLNESELESVRQLEKQlESLEKQYDEiteriaeqeiayseLQEELEEILKQLEEIEKEQEKLSEMLQGLRKDE 413
|
410
....*....|
gi 1958798727 1638 QRKQNILKEM 1647
Cdd:PRK04778 414 LEAREKLERY 423
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1476-1558 |
7.89e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 39.53 E-value: 7.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1476 KQRADLLG-HLT-GELE-RLRRAHE--RELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTK---DVK----ARL 1543
Cdd:pfam08614 61 QLREELAElYRSrGELAqRLVDLNEelQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKlnqDLQdelvALQ 140
|
90
....*....|....*
gi 1958798727 1544 AQLNVQEENMRKEKQ 1558
Cdd:pfam08614 141 LQLNMAEEKLRKLEK 155
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1282-1370 |
8.49e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 38.83 E-value: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1282 ENQIRAEQQTALQRLrEEAETLQKAERASLEQkSRRALEQLREQLEAE-ERSAQAALrAEKEAEKEATLLQLREQLEGER 1360
Cdd:PRK07353 38 EDYIRTNRAEAKERL-AEAEKLEAQYEQQLAS-ARKQAQAVIAEAEAEaDKLAAEAL-AEAQAEAQASKEKARREIEQQK 114
|
90
....*....|
gi 1958798727 1361 REAVAGLEKK 1370
Cdd:PRK07353 115 QAALAQLEQQ 124
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1282-1363 |
8.57e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 38.87 E-value: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1282 ENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSA--QAALRAEKEAEKEATLLQLREQLEGE 1359
Cdd:pfam05672 30 EEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAeeEAEEREQREQEEQERLQKQKEEAEAK 109
|
....
gi 1958798727 1360 RREA 1363
Cdd:pfam05672 110 AREE 113
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1290-1647 |
8.61e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.83 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1290 QTALQRLREE---AETLQKAERASLEQKSRRALE-QLR-EQLEAEERSAQA------ALR--AEKEAEKEATLLQLREQL 1356
Cdd:pfam05622 65 QKQLEQLQEEnfrLETARDDYRIKCEELEKEVLElQHRnEELTSLAEEAQAlkdemdILResSDKVKKLEATVETYKKKL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1357 E--GERREAVAGLEKKHSTELEQLCSSLEAKHREviSNLQKKIEGAQQkeeaQLQESLGRAEQRTHQKVHQVIEY---EQ 1431
Cdd:pfam05622 145 EdlGDLRRQVKLLEERNAEYMQRTLQLEEELKKA--NALRGQLETYKR----QVQELHGKLSEESKKADKLEFEYkklEE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1432 ELSSLLRDK-RQEVEREHERKMDKmkEEHWQEMAEARERYEAEERKQRADLLGHLTGEL------ERLRR-AHERELESV 1503
Cdd:pfam05622 219 KLEALQKEKeRLIIERDTLRETNE--ELRCAQLQQAELSQADALLSPSSDPGDNLAAEImpaeirEKLIRlQHENKMLRL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1504 RQEQ--DQQLEDLRRRHRDQERKLQDLEAELssrtkdvkaRLAQLNVQEenMRKEKQLLLDAQRQAALEKEEATATRRHL 1581
Cdd:pfam05622 297 GQEGsyRERLTELQQLLEDANRRKNELETQN---------RLANQRILE--LQQQVEELQKALQEQGSKAEDSSLLKQKL 365
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958798727 1582 EEAKKEHTHLLESKQQLRRAIDDLRvrrvelesqvdqlQTQSQRLQKHVSSLEAEVQRKQNILKEM 1647
Cdd:pfam05622 366 EEHLEKLHEAQSELQKKKEQIEELE-------------PKQDSNLAQKIDELQEALRKKDEDMKAM 418
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1522-1650 |
8.69e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 38.36 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1522 ERKLQDLEAelssrtkdvkaRLAQLnvqEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRA 1601
Cdd:pfam20492 5 EREKQELEE-----------RLKQY---EEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEES 70
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90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958798727 1602 IDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAE 1650
Cdd:pfam20492 71 AEMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREE 119
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| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1279-1418 |
8.81e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 39.00 E-value: 8.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1279 EAFENQIRAEQQTAlQRLREEAETLQKaerasleqKSRRALEQLREqlEAEERSAQAalRAEKEAEKEATLLQLREQLEG 1358
Cdd:COG0711 30 DERQEKIADGLAEA-ERAKEEAEAALA--------EYEEKLAEARA--EAAEIIAEA--RKEAEAIAEEAKAEAEAEAER 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1359 ERREAVAGLEKKHSTELEQLcssleakhREVISNLqkkiegAQQKEEAQLQESLGRAEQR 1418
Cdd:COG0711 97 IIAQAEAEIEQERAKALAEL--------RAEVADL------AVAIAEKILGKELDAAAQA 142
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| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1519-1645 |
9.46e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.81 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798727 1519 RDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKekqllLDAQRQAALEKEEatatrrhlEEAKKEhthLLESKQQL 1598
Cdd:COG1842 33 RDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEK-----WEEKARLALEKGR--------EDLARE---ALERKAEL 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1958798727 1599 RRAIDDLRVRRVELESQVDQLQTQSQRLQKHVssleAEVQRKQNILK 1645
Cdd:COG1842 97 EAQAEALEAQLAQLEEQVEKLKEALRQLESKL----EELKAKKDTLK 139
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|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
1272-1344 |
9.94e-03 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 40.21 E-value: 9.94e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958798727 1272 AQVQsstEAFENQIRAeqqtalQRLREEAETLQKAERASLEQKSRRALEqlREQLEAEERSAQAALRAEKEAE 1344
Cdd:COG0330 167 EEVQ---DAMEDRMKA------EREREAAILEAEGYREAAIIRAEGEAQ--RAIIEAEAYREAQILRAEGEAE 228
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