|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1121-1605 |
1.31e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.16 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1121 EQLSEAALKAMEEAVAQV--LEQDQRHLLESKQEKMQQLREKlcQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARM 1198
Cdd:COG1196 280 ELELEEAQAEEYELLAELarLEQDIARLEERRRELEERLEEL--EEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1199 REEESQRLSwlRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQM-LEQLKEEIEASEKSEQAALN 1277
Cdd:COG1196 358 AELAEAEEA--LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLErLERLEEELEELEEALAELEE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1278 AAKEKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQ--------------L 1343
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEadyegflegvkaalL 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1344 QKCLGQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEH-QQVMAKAREQYEAEERKQRAELLGHLTG 1422
Cdd:COG1196 516 LAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLkAAKAGRATFLPLDKIRARAALAAALARG 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1423 ELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQV 1502
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1503 ALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQsqqlqkhfsLEAEAQKKQHLLREVT 1582
Cdd:COG1196 676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQL---------EAEREELLEELLEEEE 746
|
490 500
....*....|....*....|...
gi 2462523740 1583 VEENNASPHFEPDLHIEDLRKSL 1605
Cdd:COG1196 747 LLEEEALEELPEPPDLEELEREL 769
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1171-1739 |
5.12e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 94.23 E-value: 5.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1171 RLHQQKEQSLS--SLRERLQKAIEEEEARMREEESQRLSWLRAQVQSsTQADEDQIRAEQEAsLQKLREELESQQKAERA 1248
Cdd:COG1196 204 PLERQAEKAERyrELKEELKELEAELLLLKLRELEAELEELEAELEE-LEAELEELEAELAE-LEAELEELRLELEELEL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1249 SLEQKNRQmLEQLKEEIEASEKseQAALNAAKEKALQQLREQLEGERKEAVATLEkEHSAELERLCSSLEAkhrevvssl 1328
Cdd:COG1196 282 ELEEAQAE-EYELLAELARLEQ--DIARLEERRRELEERLEELEEELAELEEELE-ELEEELEELEEELEE--------- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1329 QKKIQEAQQKEEAQLQKclgqvehrvhqksyhvagyehELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAE 1408
Cdd:COG1196 349 AEEELEEAEAELAEAEE---------------------ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1409 ERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETA 1488
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1489 RREKQQLLDvqrqvalksEEATATHQQLEEAQKEhTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSLE 1568
Cdd:COG1196 488 EAAARLLLL---------LEAEADYEGFLEGVKA-ALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1569 AEAQKKQHLLRevtveENNASPHFEPDLHIEDLRKSLGTNQTKEVSSSLSQSKEDL-YLDSLSSHNVWHLLSAEGVALRS 1647
Cdd:COG1196 558 VAAAAIEYLKA-----AKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLrEADARYYVLGDTLLGRTLVAARL 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1648 AKEFLVQQTRSMRRRQTALKAAQQHWRHELASAQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEK 1727
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA 712
|
570
....*....|..
gi 2462523740 1728 LNQLESSLWEEA 1739
Cdd:COG1196 713 EEERLEEELEEE 724
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
983-1623 |
9.96e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 94.05 E-value: 9.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 983 EDKDDSQSSQDELQSKQSKGLEERLSPPLPHEERAQSPPRslATEEEPPQGPEGQPEWKEAEELGEDSAASLSLQLSLQR 1062
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK--AEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1063 EQAPSPPAACEKGKEQHSQAEELGPGQEEAEDPEEkvavsptppvspeVRSTEPVAPPEQLSEAALKAMEEAVAQVLEQD 1142
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE-------------AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK 1378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1143 QRHLLESKQEKMQQLREKlcqeeeeeilrlhQQKEQSLSSLRERLQKAieeeearmrEEESQRLSWLRAQVQSSTQADED 1222
Cdd:PTZ00121 1379 KADAAKKKAEEKKKADEA-------------KKKAEEDKKKADELKKA---------AAAKKKADEAKKKAEEKKKADEA 1436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1223 QIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNA--AKEKAlQQLREQLEgERKEAVA 1300
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAeeAKKKA-DEAKKAAE-AKKKADE 1514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1301 TLEKEHSAELERLCSSLEAKHREVVsslqKKIQEAQQKEEAQLQKCLGQVEHRvhQKSYHVAGYEHELSSLLREKRQEVE 1380
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKADEA----KKAEEKKKADELKKAEELKKAEEK--KKAEEAKKAEEDKNMALRKAEEAKK 1588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1381 GEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVR---------QEQHKRLEDLRR 1451
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKkaeelkkaeEENKIKAAEEAK 1668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1452 RHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATaTHQQLEEAQKEHTHLLQSNQ 1531
Cdd:PTZ00121 1669 KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE-NKIKAEEAKKEAEEDKKKAE 1747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1532 QLReiLDELQARKLKLESQVDLLQAQSQQLQKHFSLEAEAQKKQHLLR--------------EVTVEENNasphfEPDLH 1597
Cdd:PTZ00121 1748 EAK--KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRmevdkkikdifdnfANIIEGGK-----EGNLV 1820
|
650 660
....*....|....*....|....*.
gi 2462523740 1598 IEDlRKSLGTNQTKEVSSSLSQSKED 1623
Cdd:PTZ00121 1821 IND-SKEMEDSAIKEVADSKNMQLEE 1845
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1121-1710 |
3.02e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.46 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1121 EQLSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKlcqeeeeeilrlHQQKEQSLSSLRERLQKAIEEEEARMRE 1200
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLE------------LEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1201 EESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQknrqmLEQLKEEIEASEKSEQAALNAAK 1280
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE-----AEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1281 EKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKclgqvehrvhqksyh 1360
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA--------------- 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1361 vagyEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELlghltgeLERLQRAHERELETVRq 1440
Cdd:COG1196 444 ----LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL-------LLEAEADYEGFLEGVK- 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1441 eqHKRLEDLRRRHREQERKLQDLELDLETrAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQ 1520
Cdd:COG1196 512 --AALLLAGLRGLAGAVAVLIGVEAAYEA-ALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAAL 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1521 KEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSLEAEAQKKQHLLREVTVEENNASPHFEPDLHIE- 1599
Cdd:COG1196 589 AAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRr 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1600 DLRKSLGTNQTKEVSSSLSQSKEDLYLDSLSSHNVWHLLSAEGVALRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELAS 1679
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
570 580 590
....*....|....*....|....*....|.
gi 2462523740 1680 AQEVAKDPPGIKALEDMRKNLEKETRHLDEM 1710
Cdd:COG1196 749 EEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
982-1738 |
3.48e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 85.58 E-value: 3.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 982 IEDKDDSQSSQDELQSKQSKGLEERLSPPLPHEERAQSPpRSLATEEeppqgpegqpeWKEAEELGEDSAASLSLQLSLQ 1061
Cdd:PTZ00121 1047 IIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKE-DNRADEA-----------TEEAFGKAEEAKKTETGKAEEA 1114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1062 REQAPSPPAACEKGKEQHSQAEELGPGQEEAEDPEEKVAVSPTPPVSpEVRSTEPVAPPEQL--SEAALKAMEEAVAQVL 1139
Cdd:PTZ00121 1115 RKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAE-DARKAEEARKAEDAkkAEAARKAEEVRKAEEL 1193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1140 ---------EQDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLR 1210
Cdd:PTZ00121 1194 rkaedarkaEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK 1273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1211 AQvqSSTQADEDQiRAEQEASLQKLREElESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKE--KALQQLR 1288
Cdd:PTZ00121 1274 AE--EARKADELK-KAEEKKKADEAKKA-EEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEakKAAEAAK 1349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1289 EQLEGERKEAVATLEKEHSAELE-----RLCSSLEAKHREV--VSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHV 1361
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKkeeakKKADAAKKKAEEKkkADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEE 1429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1362 AGYEHELSSLLREKRQEVE----GEHERRLDKMKEEHQQ------VMAKAREQYEAEERKQRAELLGHLTGELERLQRAH 1431
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEakkkAEEAKKAEEAKKKAEEakkadeAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK 1509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1432 ERELETVRQEQHKRLEDLRRRhrEQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVAL-KSEEAt 1510
Cdd:PTZ00121 1510 KKADEAKKAEEAKKADEAKKA--EEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALrKAEEA- 1586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1511 athQQLEEAQKEHThllqsnQQLREILDELQARKLKLESQvdllqaqSQQLQKHFSLEAEAQKKQHLLREVTVEENNASp 1590
Cdd:PTZ00121 1587 ---KKAEEARIEEV------MKLYEEEKKMKAEEAKKAEE-------AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA- 1649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1591 hfepdlhiEDLRKSLGTNQTKevssslsqskedlyldslsshnvwhllsaegvalrsaKEFLVQQTRSMRRRQTALKAAQ 1670
Cdd:PTZ00121 1650 --------EELKKAEEENKIK-------------------------------------AAEEAKKAEEDKKKAEEAKKAE 1684
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462523740 1671 QHWRHelaSAQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSA----MRKGHNLLKKKEEKLNQLESSLWEE 1738
Cdd:PTZ00121 1685 EDEKK---AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAeeenKIKAEEAKKEAEEDKKKAEEAKKDE 1753
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1284-1580 |
7.77e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.83 E-value: 7.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1284 LQQLREQLEGERKEAVATLE-KEHSAELERLCSSLEAKHREVVSSLQKKIQ---EAQQKEEAQLQKCLGQVEHRVHQksy 1359
Cdd:COG1196 195 LGELERQLEPLERQAEKAERyRELKEELKELEAELLLLKLRELEAELEELEaelEELEAELEELEAELAELEAELEE--- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1360 hvAGYEHELSSLLREKRQEVEGEHERRLDKM--KEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHE----- 1432
Cdd:COG1196 272 --LRLELEELELELEEAQAEEYELLAELARLeqDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEeleea 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1433 ----RELETVRQEQHKRLEDLRRRHREQERKLQDL---ELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALK 1505
Cdd:COG1196 350 eeelEEAEAELAEAEEALLEAEAELAEAEEELEELaeeLLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462523740 1506 SEEAT----ATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSLEAEAQKKQHLLRE 1580
Cdd:COG1196 430 LAELEeeeeEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1126-1551 |
8.90e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.47 E-value: 8.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1126 AALKAMEEAVAQVLEQDQRhlLESKQEKMQQLREKLcqeeeEEILRLHQQKEQSLSSLR---ERLQKAIEEEEARMREEe 1202
Cdd:PRK02224 206 ERLNGLESELAELDEEIER--YEEQREQARETRDEA-----DEVLEEHEERREELETLEaeiEDLRETIAETEREREEL- 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1203 SQRLSWLRAQVQ------SSTQADEDQIRAEQEASLQKlREELESQQKAERASLEQKnRQMLEQLKEEIE---------- 1266
Cdd:PRK02224 278 AEEVRDLRERLEeleeerDDLLAEAGLDDADAEAVEAR-REELEDRDEELRDRLEEC-RVAAQAHNEEAEslredaddle 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1267 --ASEKSEQAAlnaAKEKALQQLREQLEgERKEAVATLEKE-----------------HSAELERLCSSLEAKHREV--- 1324
Cdd:PRK02224 356 erAEELREEAA---ELESELEEAREAVE-DRREEIEELEEEieelrerfgdapvdlgnAEDFLEELREERDELREREael 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1325 ---VSSLQKKIQEAQQKEEAQlqKC--LGQ-VEHRVH-----QKSYHVAGYEHELSSLlREKRQEVEGEHER-------- 1385
Cdd:PRK02224 432 eatLRTARERVEEAEALLEAG--KCpeCGQpVEGSPHvetieEDRERVEELEAELEDL-EEEVEEVEERLERaedlveae 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1386 -RLDKMKEEHQQVMAKAREQYE-AEERKQRAELLGHLTGELErlqrAHERELETVRQEQHKRLEDLRRRHREQERKLQDL 1463
Cdd:PRK02224 509 dRIERLEERREDLEELIAERREtIEEKRERAEELRERAAELE----AEAEEKREAAAEAEEEAEEAREEVAELNSKLAEL 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1464 ELDLEtRAKDVKARLALLEVQEETA-----RREKQQLLDVQRQVALKSE-------EATATHQQLEEAQKEHTHLLQSNQ 1531
Cdd:PRK02224 585 KERIE-SLERIRTLLAAIADAEDEIerlreKREALAELNDERRERLAEKrerkrelEAEFDEARIEEAREDKERAEEYLE 663
|
490 500
....*....|....*....|
gi 2462523740 1532 QLREILDELQARKLKLESQV 1551
Cdd:PRK02224 664 QVEEKLDELREERDDLQAEI 683
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
873-1497 |
1.38e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.19 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 873 SEPAKASEKEAPEDTVDAGEEGSRREEAAK-EPKKKASALEEGSSDASQELEISEHMKEPQLSDSIASDPKSFHGLDFGF 951
Cdd:PTZ00121 1196 AEDARKAEAARKAEEERKAEEARKAEDAKKaEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE 1275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 952 RSRISEHLLDVDVLSPvlGGACRQAQQPLGIED---KDDSQSSQDELQSKQSKGLEERLSPPLPHEERAQSPPRSLATEE 1028
Cdd:PTZ00121 1276 EARKADELKKAEEKKK--ADEAKKAEEKKKADEakkKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1029 EPPQGPEGQPEWKEAEELGEDSAASLSLQLSLQREQAPSPPAACEKGKEQHSQAEELGPGQEEAEDPEEkvavspTPPVS 1108
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE------AKKKA 1427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1109 PEVRSTEPVappEQLSEAALKAmEEAVAQVLEQDQRHLLESKQE---KMQQLREKLCQEEEEEILRLHQQKEQSLSSLRE 1185
Cdd:PTZ00121 1428 EEKKKADEA---KKKAEEAKKA-DEAKKKAEEAKKAEEAKKKAEeakKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK 1503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1186 RLQKAIEEEEARMREEESQRLSWLRaQVQSSTQADEDQiRAEQEASLQKLR--EEL---ESQQKAERASLEQKNRQMLEQ 1260
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEAK-KAEEAKKADEAK-KAEEKKKADELKkaEELkkaEEKKKAEEAKKAEEDKNMALR 1581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1261 LKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKeavatlEKEHSAELERlcsslEAKHREVVSSLQKKIQEAQQKEE 1340
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE------AKIKAEELKK-----AEEEKKKVEQLKKKEAEEKKKAE 1650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1341 aQLQKclgqvehrvhqksyhvagyEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAEllghl 1420
Cdd:PTZ00121 1651 -ELKK-------------------AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE----- 1705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1421 tgELERLQRAHERELETVRQEQHKR---LEDLRRRHREQERKLQDLELDlETRAKDVKARLALLEVQEETARREKQQLLD 1497
Cdd:PTZ00121 1706 --ELKKKEAEEKKKAEELKKAEEENkikAEEAKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1227-1544 |
1.52e-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: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1227 EQEASLQKLREELESQQKAERASLEQKNRQMLE-----QLKEEIEASEKSEQAALNAAKEKALQQLREQ-----LEGERK 1296
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEKAREVERRRKLEEaekarQAEMDRQAAIYAEQERMAMERERELERIRQEerkreLERIRQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1297 EAVAtLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQlqkclgqveHRVHQKSYHVAGYEHELSSLLREKR 1376
Cdd:pfam17380 368 EEIA-MEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQ---------RKIQQQKVEMEQIRAEQEEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1377 QEVEGEHERRLDKMKEEH---QQVMAKAREQYEAEERKQRaellghltgELERLQRAHERELETVRQEQHKRLEDLRRRH 1453
Cdd:pfam17380 438 RRLEEERAREMERVRLEEqerQQQVERLRQQEEERKRKKL---------ELEKEKRDRKRAEEQRRKILEKELEERKQAM 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1454 REQERKLQDLELDLETRAKDVKARLALLEVQEEtarREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHthllqsnQQL 1533
Cdd:pfam17380 509 IEEERKRKLLEKEMEERQKAIYEEERRREAEEE---RRKQQEMEERRRIQEQMRKATEERSRLEAMERER-------EMM 578
|
330
....*....|.
gi 2462523740 1534 REILDELQARK 1544
Cdd:pfam17380 579 RQIVESEKARA 589
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1141-1742 |
5.84e-14 |
|
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: 77.79 E-value: 5.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1141 QDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQsLSSLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQAD 1220
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEK-LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1221 E-DQIRaEQEASLQKLREELESQQKAERASLEqKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEgeRKEAV 1299
Cdd:TIGR02168 387 KvAQLE-LQIASLNNEIERLEARLERLEDRRE-RLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE--RLEEA 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1300 ATLEKEHSAELERLCSSLEAKHREVVSslQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHV----------AGYEHELS 1369
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQA--RLDSLERLQENLEGFSEGVKALLKNQSGLSGILgvlselisvdEGYEAAIE 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1370 SLLREKRQEVEGEHE----------------------------------RRLDKMKEEHQQVMAKAREQYEAEERKQRAE 1415
Cdd:TIGR02168 541 AALGGRLQAVVVENLnaakkaiaflkqnelgrvtflpldsikgteiqgnDREILKNIEGFLGVAKDLVKFDPKLRKALSY 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1416 LLGH------LTGELERLQRAHEREL----------------------ETVRQEQHKRLEDLRRRHREQERKLQDLEL-- 1465
Cdd:TIGR02168 621 LLGGvlvvddLDNALELAKKLRPGYRivtldgdlvrpggvitggsaktNSSILERRREIEELEEKIEELEEKIAELEKal 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1466 -DLETRAKDVKARLALLEVQEETARRE----KQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDEL 1540
Cdd:TIGR02168 701 aELRKELEELEEELEQLRKELEELSRQisalRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1541 QARKLKLESQVDLLQAQSQQLQKHF-SLEAEAQK-KQHLLREVTVEENNASPHFEPDLHIEDLRKSLGTNQTKEVSSSLS 1618
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALdELRAELTLlNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1619 QSKEDLYLDSLSShnvwhllsaegvalrSAKEFLVQQTRSMRRRQTAlkaaqqhwRHELASAQEvakdppGIKALEDMRK 1698
Cdd:TIGR02168 861 IEELEELIEELES---------------ELEALLNERASLEEALALL--------RSELEELSE------ELRELESKRS 911
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2462523740 1699 NLEKETRHLDEMKSAMRkghNLLKKKEEKLNQLESSLWEEASDE 1742
Cdd:TIGR02168 912 ELRRELEELREKLAQLE---LRLEGLEVRIDNLQERLSEEYSLT 952
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1169-1523 |
1.60e-13 |
|
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: 76.63 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1169 ILRLHQQKEQSLSSLR------ERLQKAIEEeearmreeesqrlswLRAQVQS-STQADedqiRAEQeasLQKLREELES 1241
Cdd:TIGR02168 167 ISKYKERRKETERKLErtrenlDRLEDILNE---------------LERQLKSlERQAE----KAER---YKELKAELRE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1242 QQKAERA-SLEQKNRQmLEQLKEEIEASE---KSEQAALNAAKEK------ALQQLREQLEGERKE------AVATLEKE 1305
Cdd:TIGR02168 225 LELALLVlRLEELREE-LEELQEELKEAEeelEELTAELQELEEKleelrlEVSELEEEIEELQKElyalanEISRLEQQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1306 ---HSAELERLCSSLEAKHREVVSSLQKKiqEAQQKEEAQLQKCLGQVEHRVHqksyhvagyehELSSLLREKRQEVEgE 1382
Cdd:TIGR02168 304 kqiLRERLANLERQLEELEAQLEELESKL--DELAEELAELEEKLEELKEELE-----------SLEAELEELEAELE-E 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1383 HERRLDKMKEEHQQVmAKAREQYEAEERKQRAELlGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQD 1462
Cdd:TIGR02168 370 LESRLEELEEQLETL-RSKVAQLELQIASLNNEI-ERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEE 447
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462523740 1463 LELDLETRAKDVKARLALLEVQEETARrekQQLLDVQRQVALKSEEATATHQQLEEAQKEH 1523
Cdd:TIGR02168 448 ELEELQEELERLEEALEELREELEEAE---QALDAAERELAQLQARLDSLERLQENLEGFS 505
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1132-1739 |
2.33e-13 |
|
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: 75.78 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1132 EEAVAQVLEQDQRHLLESKQEKMQQLREKLCQeeeeeILRLHQQKEQSLSSLRERLQKAieeeeaRMREEESQRLSWLRA 1211
Cdd:TIGR00618 199 LTLRSQLLTLCTPCMPDTYHERKQVLEKELKH-----LREALQQTQQSHAYLTQKREAQ------EEQLKKQQLLKQLRA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1212 QVQSSTQadedqiraeQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALnaakEKALQQLREQL 1291
Cdd:TIGR00618 268 RIEELRA---------QEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSR----AKLLMKRAAHV 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1292 egerkeavatlekEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSL 1371
Cdd:TIGR00618 335 -------------KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1372 lrekrqevegeherrLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRR 1451
Cdd:TIGR00618 402 ---------------LDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1452 RHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLL--DVQRQVALKSEEATATHQQLEEaqkEHTHLLQS 1529
Cdd:TIGR00618 467 SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIhpNPARQDIDNPGPLTRRMQRGEQ---TYAQLETS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1530 NQQLREILDELQARKLKLESQVDLLQAQSQQ-LQKHFSLEAEAQKKQHLLREV---TVEENNASPHFEPDLHIEDLRKSL 1605
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASLKEQMQEIQQSFSIlTQCDNRSKEDIPNLQNITVRLqdlTEKLSEAEDMLACEQHALLRKLQP 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1606 GTNQtKEVSSSLSQSKEDLYLDSLSSHNVWHLLSAEGV--ALRSAKEFlvqQTRSMRRRQTALKAAQQ------HWRHEL 1677
Cdd:TIGR00618 624 EQDL-QDVRLHLQQCSQELALKLTALHALQLTLTQERVreHALSIRVL---PKELLASRQLALQKMQSekeqltYWKEML 699
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462523740 1678 ASAQEvakdppgikALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSLWEEA 1739
Cdd:TIGR00618 700 AQCQT---------LLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQA 752
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1132-1543 |
5.48e-13 |
|
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: 74.71 E-value: 5.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1132 EEAVAQVLEQDQRHL-LESKQEKMQQLREKLcQEEEEEILRLHQQKEQSLSSLRERLQkaieeeearmreEESQRLSWLR 1210
Cdd:TIGR02168 666 AKTNSSILERRREIEeLEEKIEELEEKIAEL-EKALAELRKELEELEEELEQLRKELE------------ELSRQISALR 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1211 AQVQSSTQadEDQIRAEQEASLQKLREELEsQQKAERASLEQKNRQMLEQLKEEIEasekSEQAALNAAKEkALQQLREQ 1290
Cdd:TIGR02168 733 KDLARLEA--EVEQLEERIAQLSKELTELE-AEIEELEERLEEAEEELAEAEAEIE----ELEAQIEQLKE-ELKALREA 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1291 LEGERKEavATLEKEHSAELERLCSSLEAKHREVVSSLQkkiQEAQQKEEAQLQkclgqvehrvhqksyhVAGYEHELSS 1370
Cdd:TIGR02168 805 LDELRAE--LTLLNEEAANLRERLESLERRIAATERRLE---DLEEQIEELSED----------------IESLAAEIEE 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1371 lLREKRQEVEGEHErRLDKMKEEHQQVMAKAREQYEAEERKQRaellghltgELERLQRAHERELETVRQEQHK---RLE 1447
Cdd:TIGR02168 864 -LEELIEELESELE-ALLNERASLEEALALLRSELEELSEELR---------ELESKRSELRRELEELREKLAQlelRLE 932
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1448 DLR-RRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRqVALKS-EEATATHQQLEEAQKEHTH 1525
Cdd:TIGR02168 933 GLEvRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGP-VNLAAiEEYEELKERYDFLTAQKED 1011
|
410
....*....|....*...
gi 2462523740 1526 LLQSNQQLREILDELQAR 1543
Cdd:TIGR02168 1012 LTEAKETLEEAIEEIDRE 1029
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1129-1624 |
7.75e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.18 E-value: 7.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1129 KAMEEAVAQVLEQDQRhlLESKQEKMQQLREKLcqeeeeEILRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSW 1208
Cdd:COG4913 221 PDTFEAADALVEHFDD--LERAHEALEDAREQI------ELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1209 LRAQVqsstqadeDQIRAEQEAsLQKLREELESQQKAERASLEQKNRQM-------LEQLKEEIEASEKSEQAALNAAK- 1280
Cdd:COG4913 293 LEAEL--------EELRAELAR-LEAELERLEARLDALREELDELEAQIrgnggdrLEQLEREIERLERELEERERRRAr 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1281 -EKALQQLREQLEGERkEAVATLEKEHSAELERLcSSLEAKHREVVSSLQKKIQEAqQKEEAQLQKCLGQVEHRVHQKSY 1359
Cdd:COG4913 364 lEALLAALGLPLPASA-EEFAALRAEAAALLEAL-EEELEALEEALAEAEAALRDL-RRELRELEAEIASLERRKSNIPA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1360 HVAGYEHELSSLLREKRQE---------------------------------VEGEHERR----LDKMKEEHQQVMAKAR 1402
Cdd:COG4913 441 RLLALRDALAEALGLDEAElpfvgelievrpeeerwrgaiervlggfaltllVPPEHYAAalrwVNRLHLRGRLVYERVR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1403 EQYEAEERKQRAEllGHLTGELE------------RLQR-------AHERELETVRQ---------EQHKRLE-DLRRRH 1453
Cdd:COG4913 521 TGLPDPERPRLDP--DSLAGKLDfkphpfrawleaELGRrfdyvcvDSPEELRRHPRaitragqvkGNGTRHEkDDRRRI 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1454 REQ-------ERKLQDLELD---LETRAKDVKARLALLEVQEETARREKQQLLDVQrQVALKSEEATATHQQLEEAQKEH 1523
Cdd:COG4913 599 RSRyvlgfdnRAKLAALEAElaeLEEELAEAEERLEALEAELDALQERREALQRLA-EYSWDEIDVASAEREIAELEAEL 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1524 THLLQSN---QQLREILDELQARKLKLESQVDllqaqsQQLQKHFSLEAEAQKKQHLLREVTVEENNASPHFEPDLHI-- 1598
Cdd:COG4913 678 ERLDASSddlAALEEQLEELEAELEELEEELD------ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAll 751
|
570 580
....*....|....*....|....*..
gi 2462523740 1599 -EDLRKSLGTNQTKEVSSSLSQSKEDL 1624
Cdd:COG4913 752 eERFAAALGDAVERELRENLEERIDAL 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1122-1735 |
1.15e-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: 73.55 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1122 QLSEAALKAMEEAVAQVLEQ--DQRHLLESKQEKMQQLREKLcQEEEEEILRLHQ---QKEQSLSSLRERLQKAieeeeA 1196
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEEleSLEAELEELEAELEELESRL-EELEEQLETLRSkvaQLELQIASLNNEIERL-----E 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1197 RMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKN--RQMLEQLKEEIEASEKSEQA 1274
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEelREELEEAEQALDAAERELAQ 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1275 AlnAAKEKALQQLREQLEGERKEAVATLEKEH--SAELERLCSSLEAKHR-----EVV--SSLQ----KKIQEAQQKEEA 1341
Cdd:TIGR02168 487 L--QARLDSLERLQENLEGFSEGVKALLKNQSglSGILGVLSELISVDEGyeaaiEAAlgGRLQavvvENLNAAKKAIAF 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1342 QLQKCLGQVehrvhqksyhvagyehELSSLLREKRQEVEGEHERRLdkMKEEHQQVMAKAREQYEAEERKQRAELLGH-- 1419
Cdd:TIGR02168 565 LKQNELGRV----------------TFLPLDSIKGTEIQGNDREIL--KNIEGFLGVAKDLVKFDPKLRKALSYLLGGvl 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1420 ----LTGELERLQRAHEREL----------------------ETVRQEQHKRLEDLRRRHREQERKLQDLEL---DLETR 1470
Cdd:TIGR02168 627 vvddLDNALELAKKLRPGYRivtldgdlvrpggvitggsaktNSSILERRREIEELEEKIEELEEKIAELEKalaELRKE 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1471 AKDVKARLALLEVQEETARRE----KQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLK 1546
Cdd:TIGR02168 707 LEELEEELEQLRKELEELSRQisalRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1547 LESQVDLLQAQSQQLQKHF-SLEAEAQK-KQHLLREVTVEENNASPHFEPDLHIEDLRKSLGTNQTKEVSSSLSQSKEDL 1624
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALdELRAELTLlNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE 866
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1625 YLDSLSSHNVWHL-----LSAEGVALRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELASAQEVakdppgIKALEDMRKN 1699
Cdd:TIGR02168 867 LIEELESELEALLnerasLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR------LEGLEVRIDN 940
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 2462523740 1700 L-----EKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSL 1735
Cdd:TIGR02168 941 LqerlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1121-1742 |
2.08e-12 |
|
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: 72.70 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1121 EQLSEAALKAMEEAVAQVLEQDQRHLLEsKQEKMQQLREKLCQ--EEEEEILRLHQQKEQsLSSLRERLQKAIEEEEARM 1198
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELK-LQELKLKEQAKKALeyYQLKEKLELEEEYLL-YLDYLKLNEERIDLLQELL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1199 REEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQM------LEQLKEEIEASEKSE 1272
Cdd:pfam02463 247 RDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLerrkvdDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1273 QAALNAAKEKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQkCLGQVEH 1352
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE-LKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1353 RVHQKSYHVAGYEHELSSLLREKRQEVEGEhERRLDKMKEEHQQVMAKAREQYEAEERKQRAEllghltgELERLQRAHE 1432
Cdd:pfam02463 406 EAQLLLELARQLEDLLKEEKKEELEILEEE-EESIELKQGKLTEEKEELEKQELKLLKDELEL-------KKSEDLLKET 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1433 RELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALkSEEATAT 1512
Cdd:pfam02463 478 QLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV-IVEVSAT 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1513 HQQLEEAQKEHTHLLQSNQQLREIldELQARKLKLESQVDLLQAQSQQLQKHFSLEAEAQKKQHLLREVTVEEnNASPHF 1592
Cdd:pfam02463 557 ADEVEERQKLVRALTELPLGARKL--RLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEG-ILKDTE 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1593 EPDLHIEDLRKSLGTNQTKEVSSSLSQSKEDLYLDSLSshnvwhLLSAEGVALRSAKEFLVQQTRSMRRRQTALKAAQQH 1672
Cdd:pfam02463 634 LTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSEL------TKELLEIQELQEKAESELAKEEILRRQLEIKKKEQR 707
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1673 WRHELASAQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSLWEEASDE 1742
Cdd:pfam02463 708 EKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELA 777
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1120-1540 |
3.70e-12 |
|
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: 71.92 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1120 PEQLSEAALKAMEEAVAQVLEQDQRHLLESKQ---EKMQQL--------REKLCQEEEEEILRLHQQKEQSL-SSLRERL 1187
Cdd:TIGR00618 435 LQQRYAELCAAAITCTAQCEKLEKIHLQESAQslkEREQQLqtkeqihlQETRKKAVVLARLLELQEEPCPLcGSCIHPN 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1188 QKAIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEaSLQKLREELESQQKAERASLEQKNR--QMLEQLKEEI 1265
Cdd:TIGR00618 515 PARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK-QRASLKEQMQEIQQSFSILTQCDNRskEDIPNLQNIT 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1266 EASEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEA-----QQKEE 1340
Cdd:TIGR00618 594 VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHalsirVLPKE 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1341 --AQLQKCLGQVEHRVHQKSYHVAGYEHELSsLLREkrqevEGEHERRLDKMKEEHQQVMAKAREQYEAEE--------- 1409
Cdd:TIGR00618 674 llASRQLALQKMQSEKEQLTYWKEMLAQCQT-LLRE-----LETHIEEYDREFNEIENASSSLGSDLAAREdalnqslke 747
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1410 -RKQRAELLGHLTGELERLQRAHERELETVRQEQHKRlEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETA 1488
Cdd:TIGR00618 748 lMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLA-AEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETL 826
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2462523740 1489 RREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDEL 1540
Cdd:TIGR00618 827 VQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1125-1498 |
5.59e-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: 71.24 E-value: 5.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1125 EAALKAMEEAVAQVleQDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQsLSSLRERLQKAieeeearmreeeSQ 1204
Cdd:TIGR02168 683 EEKIEELEEKIAEL--EKALAELRKELEELEEELEQLRKELEELSRQISALRKD-LARLEAEVEQL------------EE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1205 RLSWLRAQVQSSTQADEDQIRAEQEASLQKLREElesqqkAERASLEQKNRQMLEQLKEEIEASeKSEQAALNAAKEKAl 1284
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAE------AEIEELEAQIEQLKEELKALREAL-DELRAELTLLNEEA- 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1285 QQLREQLEGERKEAVATlekehSAELERLCSSLEAKhREVVSSLQKKIQEAQQKEEAQlqkclgQVEHRVHQKSYHVAGY 1364
Cdd:TIGR02168 820 ANLRERLESLERRIAAT-----ERRLEDLEEQIEEL-SEDIESLAAEIEELEELIEEL------ESELEALLNERASLEE 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1365 EHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKareQYEAEERKQRAELLghLTGELERLQRAHERELETVRQEQHK 1444
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELRRELEELREK---LAQLELRLEGLEVR--IDNLQERLSEEYSLTLEEAEALENK 962
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1445 RLED---LRRRHREQERKLQDL---ELDLETRAKDVKARLALLEVQEETARREKQQLLDV 1498
Cdd:TIGR02168 963 IEDDeeeARRRLKRLENKIKELgpvNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEA 1022
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1147-1580 |
6.59e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 6.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1147 LESKQEKMQQLREKLcqeeeeeilRLHQQKEQSLSSLRERLQKAieeeeARMREEESQRLSWLRAQVQsstQADEDQIRA 1226
Cdd:COG4717 73 LKELEEELKEAEEKE---------EEYAELQEELEELEEELEEL-----EAELEELREELEKLEKLLQ---LLPLYQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1227 EQEASLQKLREELES--QQKAERASLEQKNRQMLEQLkEEIEASEKSEQAALNAAKEKALQQLREQLEgERKEAVATLEK 1304
Cdd:COG4717 136 ALEAELAELPERLEEleERLEELRELEEELEELEAEL-AELQEELEELLEQLSLATEEELQDLAEELE-ELQQRLAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1305 EhSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQV------EHRVHQKSYHVAGYEHELSSLLREKRQE 1378
Cdd:COG4717 214 E-LEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALlallglGGSLLSLILTIAGVLFLVLGLLALLFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1379 VEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQER 1458
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1459 KlqdlELDLETRAKDVKARLALLEvQEETARREKQQLLDVQRQVA--LKSEEATATHQQLEEAQKEHTHLLQSNQQLREI 1536
Cdd:COG4717 373 A----ALLAEAGVEDEEELRAALE-QAEEYQELKEELEELEEQLEelLGELEELLEALDEEELEEELEELEEELEELEEE 447
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2462523740 1537 LDELQARKLKLESQVDLLQAQSQQLQKHFSLEAEAQKKQHLLRE 1580
Cdd:COG4717 448 LEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1125-1540 |
6.88e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 6.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1125 EAALKAMEEAVAQVLE-QDQRHLLESKQEKMQQLREKLCQEEEE-EILRLHQQKEQSLSSLRERLQkaieeeearmreEE 1202
Cdd:COG4717 77 EEELKEAEEKEEEYAElQEELEELEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELA------------EL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1203 SQRLSWLRAQVQSSTQADEDQIRAEQEasLQKLREELESQQKAERASLEQKNRQMLEQLkEEIEASEKSEQAALNAAKEK 1282
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAE--LAELQEELEELLEQLSLATEEELQDLAEEL-EELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1283 aLQQLREQLEGERKEAVATLEKEHSAELERL-------------------------------------CSSLEAKHREVV 1325
Cdd:COG4717 222 -LEELEEELEQLENELEAAALEERLKEARLLlliaaallallglggsllsliltiagvlflvlgllalLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1326 SSLQKKIQEAQQK---EEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKA- 1401
Cdd:COG4717 301 GKEAEELQALPALeelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAg 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1402 ----------------REQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLEL 1465
Cdd:COG4717 381 vedeeelraaleqaeeYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEA 460
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462523740 1466 DLETRAKDvkARLALLEVQEETARREKQQLldVQRQVALKseeatATHQQLEEAQKEHTHLLQS--NQQLREILDEL 1540
Cdd:COG4717 461 ELEQLEED--GELAELLQELEELKAELREL--AEEWAALK-----LALELLEEAREEYREERLPpvLERASEYFSRL 528
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1073-1464 |
1.15e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.07 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1073 EKGKEQHSQAEELGpgqEEAEDPEEKVavsptppvspEVRSTEPVAPPEQLsEAALKAMEEAVAQVLEQDQRhlLESKQE 1152
Cdd:PRK02224 356 ERAEELREEAAELE---SELEEAREAV----------EDRREEIEELEEEI-EELRERFGDAPVDLGNAEDF--LEELRE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1153 KMQQLREKLCQEeeeeilrlhqqkEQSLSSLRERLQKAIEEEEARMREEESQrlswlraQVQSSTQADEDQIRAEQEASL 1232
Cdd:PRK02224 420 ERDELREREAEL------------EATLRTARERVEEAEALLEAGKCPECGQ-------PVEGSPHVETIEEDRERVEEL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1233 QKLREELESQQ-----KAERASLEQKNRQMLEQLKEEIEASEK--SEQAALNAAKEKALQQLREQLEGERKEAVATLEKE 1305
Cdd:PRK02224 481 EAELEDLEEEVeeveeRLERAEDLVEAEDRIERLEERREDLEEliAERRETIEEKRERAEELRERAAELEAEAEEKREAA 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1306 HSAELErlcsslEAKHREVVSSLQKKIQEAQQKEEAqlqkcLGQVEHRVHQksyhVAGYEHELSSlLREKR---QEVEGE 1382
Cdd:PRK02224 561 AEAEEE------AEEAREEVAELNSKLAELKERIES-----LERIRTLLAA----IADAEDEIER-LREKRealAELNDE 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1383 HERRLDKMKEEHQQVMAKAREQY--EAEERKQRAE-LLGHLTGELERLqRAHERELET----VRQEQhKRLEDLRRRHRE 1455
Cdd:PRK02224 625 RRERLAEKRERKRELEAEFDEARieEAREDKERAEeYLEQVEEKLDEL-REERDDLQAeigaVENEL-EELEELRERREA 702
|
....*....
gi 2462523740 1456 QERKLQDLE 1464
Cdd:PRK02224 703 LENRVEALE 711
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1121-1498 |
1.74e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1121 EQLSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKLcQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMRE 1200
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL-AEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1201 EESQRLSW---LRAQVQSSTQADEDQIRAEQEASLQKLREELEsQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALN 1277
Cdd:COG1196 525 AVAVLIGVeaaYEAALEAALAAALQNIVVEDDEVAAAAIEYLK-AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1278 AAKEKALQQLREQLEGERkEAVATLEKEHSAELERLCSSLEAKHREVvSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQK 1357
Cdd:COG1196 604 VASDLREADARYYVLGDT-LLGRTLVAARLEAALRRAVTLAGRLREV-TLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1358 SyhvagyehELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELET 1437
Cdd:COG1196 682 E--------ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAL 753
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462523740 1438 VRQEQHKRLEDLRRRHREQERKLQDLE---LDLETRAKDVKARLALLEVQEETARREKQQLLDV 1498
Cdd:COG1196 754 EELPEPPDLEELERELERLEREIEALGpvnLLAIEEYEELEERYDFLSEQREDLEEARETLEEA 817
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1242-1550 |
9.66e-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: 65.71 E-value: 9.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1242 QQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEgerkeavatlEKEHSAELERLcssLEAKH 1321
Cdd:pfam13868 33 RIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIE----------EREQKRQEEYE---EKLQE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1322 REVVSSLQKKIQEAQQKEEAQLQKclgqvehRVHQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKA 1401
Cdd:pfam13868 100 REQMDEIVERIQEEDQAEAEEKLE-------KQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEERE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1402 REQYEAEERKQR-AELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDlETRAKDVKARLAL 1480
Cdd:pfam13868 173 AEREEIEEEKEReIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQ-QAREEQIELKERR 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462523740 1481 LEVQEETARREKQQLLDVQR-QVALKSEEATATHQQLEEAQKEHTHLLQSNQQLR--EILDELQARKLKLESQ 1550
Cdd:pfam13868 252 LAEEAEREEEEFERMLRKQAeDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRaaEREEELEEGERLREEE 324
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1227-1476 |
1.10e-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: 67.00 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1227 EQEASLQKLREELESQQKAERASLEQKNRQMLEqLKEEIEA------------SEKSEQAALNAAKEKALQQLREQLEGE 1294
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSE-LEEEIEElqkelyalaneiSRLEQQKQILRERLANLERQLEELEAQ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1295 R----------KEAVATLEKEhSAELERLCSSLEAKHREvvssLQKKIQEAQQKEEAqLQKCLGQVEHRVHQKSYHVAGY 1364
Cdd:TIGR02168 325 LeeleskldelAEELAELEEK-LEELKEELESLEAELEE----LEAELEELESRLEE-LEEQLETLRSKVAQLELQIASL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1365 EHELSSLlrEKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHK 1444
Cdd:TIGR02168 399 NNEIERL--EARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
250 260 270
....*....|....*....|....*....|....
gi 2462523740 1445 RLEDLRRRHREQERK--LQDLELDLETRAKDVKA 1476
Cdd:TIGR02168 477 LDAAERELAQLQARLdsLERLQENLEGFSEGVKA 510
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1215-1732 |
1.43e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1215 SSTQADEDQIRAEQEASLQKLRE--ELESQQKAERASLE--QKNRQMLEQLKEEIEASEKSEQAALNAAK--EKALQQLR 1288
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREinEISSELPELREELEklEKEVKELEELKEEIEELEKELESLEGSKRklEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1289 EQLEGERKE-------------------AVATLEKEHSAELERL--CSSLEAKHREVVSSLQKKIQEAQQKEE--AQLQK 1345
Cdd:PRK03918 266 ERIEELKKEieeleekvkelkelkekaeEYIKLSEFYEEYLDELreIEKRLSRLEEEINGIEERIKELEEKEErlEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1346 CLGQVEHRVHQKSYHVAGYEhELSSLLREKRQEVEGEHERRLDKMKEEHQQVmAKAREQYEAEERKQRAELlGHLTGELE 1425
Cdd:PRK03918 346 KLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEKLEKELEEL-EKAKEEIEEEISKITARI-GELKKEIK 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1426 RLQRAHErELETVRQ---------EQHKRLEDLRRRHREQERKLQDLElDLETRAKDVKARLALLEVQeetarREKQQLL 1496
Cdd:PRK03918 423 ELKKAIE-ELKKAKGkcpvcgrelTEEHRKELLEEYTAELKRIEKELK-EIEEKERKLRKELRELEKV-----LKKESEL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1497 DVQRQVA--LKSEEATATHQQLEEAQKEHTHLlqsnQQLREILDELQARKLKLESQVDllqaqsqqlqkhfSLEAEAQKK 1574
Cdd:PRK03918 496 IKLKELAeqLKELEEKLKKYNLEELEKKAEEY----EKLKEKLIKLKGEIKSLKKELE-------------KLEELKKKL 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1575 QHLLREV-TVEENNASphfepdlhIEDLRKSLGTNQTKEVSSSLsQSKEDLYLDSLSSHNVWHLLSAEGVALRSAKEFLV 1653
Cdd:PRK03918 559 AELEKKLdELEEELAE--------LLKELEELGFESVEELEERL-KELEPFYNEYLELKDAEKELEREEKELKKLEEELD 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1654 Q----------QTRSMRRRQTALKAAQQHWRHE------LASAQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSAMRKG 1717
Cdd:PRK03918 630 KafeelaetekRLEELRKELEELEKKYSEEEYEelreeyLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709
|
570
....*....|....*
gi 2462523740 1718 HNLLKKKEEKLNQLE 1732
Cdd:PRK03918 710 KKELEKLEKALERVE 724
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1169-1739 |
1.87e-10 |
|
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: 66.53 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1169 ILRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERA 1248
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1249 SLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQlreQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSL 1328
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEK---KLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1329 QKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYE-A 1407
Cdd:pfam02463 321 KEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELElK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1408 EERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEET 1487
Cdd:pfam02463 401 SEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1488 ARREKQQLLDvqrqvaLKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSL 1567
Cdd:pfam02463 481 KLQEQLELLL------SRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVS 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1568 EAEAQKKQHLLREVTVEENNAsphfepdlhieDLRKSLGTNQTKEVSSSLSQSKEDLYLDSLSSHNVWHLLSAEGVALRS 1647
Cdd:pfam02463 555 ATADEVEERQKLVRALTELPL-----------GARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAK 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1648 AKEFLVQQTRSMRRRQTALKAAQ--QHWRHELASAQEVAKDPPGIKALEDMRKN--LEKETRHLDEMKSAMRKGHNLLKK 1723
Cdd:pfam02463 624 VVEGILKDTELTKLKESAKAKESglRKGVSLEEGLAEKSEVKASLSELTKELLEiqELQEKAESELAKEEILRRQLEIKK 703
|
570
....*....|....*.
gi 2462523740 1724 KEEKLNQLESSLWEEA 1739
Cdd:pfam02463 704 KEQREKEELKKLKLEA 719
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1122-1497 |
3.27e-10 |
|
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: 65.47 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1122 QLSEAALKAMEEAVAQVLE--QDQRHLLESKQEKMQQLREKLCQEeeeeiLRLHQQKEQSLSSLRERLQKaieeeearMR 1199
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEglKRELSSLQSELRRIENRLDELSQE-----LSDASRKIGEIEKEIEQLEQ--------EE 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1200 EEESQRLSWLRAQVQSSTQADEDQIR---------AEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIeaSEK 1270
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQEIENVKSelkeleariEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEV--SRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1271 SEQAALNAAKEKALQQLREQLEGERKEAVATLEkehsaelerlcssleakhrevvsSLQKKIQEAQQKEEAqLQKCLGQV 1350
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRI-----------------------DLKEQIKSIEKEIEN-LNGKKEEL 866
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1351 EHRVHQKSYHVAGYEHELSSLLREKRqevegEHERRLDKMKEEHQQvmAKAREQYEAEERKQRAELLGHLTGELERLQRA 1430
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKKERD-----ELEAQLRELERKIEE--LEAQIEKKRKRLSELKAKLEALEEELSEIEDP 939
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462523740 1431 HERELETVRQEQhkRLEDLRRRHREQERKLQDLElDLETRA----KDVKARLALLEVQEETARREKQQLLD 1497
Cdd:TIGR02169 940 KGEDEEIPEEEL--SLEDVQAELQRVEEEIRALE-PVNMLAiqeyEEVLKRLDELKEKRAKLEEERKAILE 1007
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1136-1478 |
4.98e-10 |
|
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: 63.40 E-value: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1136 AQVLEQDQRHLLESKQEK-----MQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLR 1210
Cdd:pfam13868 26 AQIAEKKRIKAEEKEEERrldemMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1211 AQVQssTQADEDQIRAEQEASLQKLREELEsQQKAERASLEQKNRQMLEQL----------KEEIEASEKSEQAALNAAK 1280
Cdd:pfam13868 106 IVER--IQEEDQAEAEEKLEKQRQLREEID-EFNEEQAEWKELEKEEEREEderileylkeKAEREEEREAEREEIEEEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1281 EKALQQLREQLEGERKeavatlEKEHSAEL--ERLCSSLEAKHRevvsslQKKIQEAQQKEEAQLQKCLGQVEHRVHqks 1358
Cdd:pfam13868 183 EREIARLRAQQEKAQD------EKAERDELraKLYQEEQERKER------QKEREEAEKKARQRQELQQAREEQIEL--- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1359 yhvagyehelssllREKRQEVEGEHERRLDKMKEEHQQVMAKaREQYEAEERKQRaellghltgelerlQRAHERELETV 1438
Cdd:pfam13868 248 --------------KERRLAEEAEREEEEFERMLRKQAEDEE-IEQEEAEKRRMK--------------RLEHRRELEKQ 298
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2462523740 1439 RQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARL 1478
Cdd:pfam13868 299 IEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1210-1551 |
1.79e-09 |
|
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: 63.43 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1210 RAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERAsLE---QKNRQMLEQLKEEIEASEKSE--QAALNAAKEKAL 1284
Cdd:COG3096 286 RALELRRELFGARRQLAEEQYRLVEMARELEELSARESD-LEqdyQAASDHLNLVQTALRQQEKIEryQEDLEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1285 QQ--LREQLEGERKEAVATLEkEHSAELERLCSSLeAKHREVVSSLQKKIQEAQQKEEAqlqkcLGQVEHRVHQKSYHVA 1362
Cdd:COG3096 365 EQeeVVEEAAEQLAEAEARLE-AAEEEVDSLKSQL-ADYQQALDVQQTRAIQYQQAVQA-----LEKARALCGLPDLTPE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1363 GYEHELSSLlREKRQEVegeHERRLDKmkEEHQQVMAKAREQYEaeerkQRAELLGHLTGELERLQrAHE--RE-LETVR 1439
Cdd:COG3096 438 NAEDYLAAF-RAKEQQA---TEEVLEL--EQKLSVADAARRQFE-----KAYELVCKIAGEVERSQ-AWQtaRElLRRYR 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1440 QEQH--KRLEDLRRRHREQERKL---QDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQ 1514
Cdd:COG3096 506 SQQAlaQRLQQLRAQLAELEQRLrqqQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQ 585
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462523740 1515 QLEE-----------------AQKEHTHL-------LQSNQQLREIL--------------DELQARKLKLESQV 1551
Cdd:COG3096 586 QLEQlrarikelaarapawlaAQDALERLreqsgeaLADSQEVTAAMqqllerereatverDELAARKQALESQI 660
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1209-1601 |
2.46e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 62.67 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1209 LRAQVQSStqadEDQIRAEQEAsLQKLREELEsQQKAERASLEQKNRQMLEQLKEEIEA---SEKSEQAalnaakEKALQ 1285
Cdd:PRK04863 291 LRRELYTS----RRQLAAEQYR-LVEMARELA-ELNEAESDLEQDYQAASDHLNLVQTAlrqQEKIERY------QADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1286 QLREQLEgERKEAVAtLEKEHSAELERLCSSLEakhrEVVSSLQKKIQEAQQKEEAQlQKCLGQVEHRVH-----QKSYH 1360
Cdd:PRK04863 359 ELEERLE-EQNEVVE-EADEQQEENEARAEAAE----EEVDELKSQLADYQQALDVQ-QTRAIQYQQAVQaleraKQLCG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1361 VAGYEHE-LSSLLREKRQEVEGEHERRLDKmkeEHQQVMAK-AREQYEaeerkQRAELLGHLTGELERlQRAHERELETV 1438
Cdd:PRK04863 432 LPDLTADnAEDWLEEFQAKEQEATEELLSL---EQKLSVAQaAHSQFE-----QAYQLVRKIAGEVSR-SEAWDVARELL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1439 RQ-EQHK----RLEDLRRRHREQERKLQdLELDLETRAKDVKARLAL-----LEVQEETARREkQQLLDVQRQVALKSEE 1508
Cdd:PRK04863 503 RRlREQRhlaeQLQQLRMRLSELEQRLR-QQQRAERLLAEFCKRLGKnlddeDELEQLQEELE-ARLESLSESVSEARER 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1509 ATATHQQLEEAQKEHTHLLQSNQQLREildeLQARKLKLESQVDLLQAQsqqlqkhfSLEAEAQKKQHLLREVTVEENN- 1587
Cdd:PRK04863 581 RMALRQQLEQLQARIQRLAARAPAWLA----AQDALARLREQSGEEFED--------SQDVTEYMQQLLERERELTVERd 648
|
410
....*....|....*.
gi 2462523740 1588 --ASPHFEPDLHIEDL 1601
Cdd:PRK04863 649 elAARKQALDEEIERL 664
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1208-1522 |
2.61e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1208 WLRAQVQSSTQADEDQIRAeQEASLQKLREELESQQKAERASLEQKNrQMLEQLKEEIEASEKSEQAALnaaKEKALQQL 1287
Cdd:TIGR02169 226 YELLKEKEALERQKEAIER-QLASLEEELEKLTEEISELEKRLEEIE-QLLEELNKKIKDLGEEEQLRV---KEKIGELE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1288 REQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEaQQKEEAQLQKCLGQVEHRVHQKSYHVAgyehE 1367
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEE-ERKRRDKLTEEYAELKEELEDLRAELE----E 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1368 LSSLLREKRQEVEgEHERRLDKMKEEHQQVMakaREQYEAEERKQRAEL-LGHLTGELERLQRAHeRELETvrqeqhkRL 1446
Cdd:TIGR02169 376 VDKEFAETRDELK-DYREKLEKLKREINELK---RELDRLQEELQRLSEeLADLNAAIAGIEAKI-NELEE-------EK 443
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462523740 1447 EDLRRRHREQERKLQDLELDLEtrakdvKARLALLEVQEETARREKQqlldvQRQVALKSEEATATHQQLEEAQKE 1522
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLS------KYEQELYDLKEEYDRVEKE-----LSKLQRELAEAEAQARASEERVRG 508
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1133-1508 |
3.01e-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: 62.43 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1133 EAVAQVLEQDQRHLLESKQekMQQLREKLcqeeeeeilrlhQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLRAQ 1212
Cdd:pfam05483 408 EELKKILAEDEKLLDEKKQ--FEKIAEEL------------KGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEV 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1213 VQSSTQADEDQIR-AEQEASLQKLR-EELESQQKAERASLEQKNRQ------------MLEQLkEEIEASEKSEQAALNA 1278
Cdd:pfam05483 474 EDLKTELEKEKLKnIELTAHCDKLLlENKELTQEASDMTLELKKHQediinckkqeerMLKQI-ENLEEKEMNLRDELES 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1279 AKEKALQQ-------LREQLEGERKEAVATLEKEHSAE-LERLCSSLeakhREVVSSLQKKIQEAQQKEEAQLQKC---- 1346
Cdd:pfam05483 553 VREEFIQKgdevkckLDKSEENARSIEYEVLKKEKQMKiLENKCNNL----KKQIENKNKNIEELHQENKALKKKGsaen 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1347 --LGQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEGE---HERRLDKMKEEHQQVMAKAREQYEAEERKQraellgHLT 1421
Cdd:pfam05483 629 kqLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKkisEEKLLEEVEKAKAIADEAVKLQKEIDKRCQ------HKI 702
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1422 GELERLQRAHERELETVRQEQHKRLEDLRRRHREQerklQDLELDLETRAKDVKARLALLEVQEETARREKQQL-LDVQR 1500
Cdd:pfam05483 703 AEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQ----SSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLkMEAKE 778
|
....*...
gi 2462523740 1501 QVALKSEE 1508
Cdd:pfam05483 779 NTAILKDK 786
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1125-1740 |
3.65e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.01 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1125 EAALKAMEEAVAQVLEQ--DQRHLLESKQEKMQQLREKLCQEEEEEILRLhQQKEQSLSSLRERLQKAIEEEEarmreee 1202
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEisELEKRLEEIEQLLEELNKKIKDLGEEEQLRV-KEKIGELEAEIASLERSIAEKE------- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1203 sQRLSWLRAQVQsstQADEDqiRAEQEASLQKLREELESQQKaERASLE---QKNRQMLEQLKEEIEASEKSEQAA---L 1276
Cdd:TIGR02169 315 -RELEDAEERLA---KLEAE--IDKLLAEIEELEREIEEERK-RRDKLTeeyAELKEELEDLRAELEEVDKEFAETrdeL 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1277 NAAKEK--ALQQLREQLEGERKEAVATLEKEHS--AELERLCSSLEAKHREVVS---SLQKKIQEAQQKEEaQLQKCLGQ 1349
Cdd:TIGR02169 388 KDYREKleKLKREINELKRELDRLQEELQRLSEelADLNAAIAGIEAKINELEEekeDKALEIKKQEWKLE-QLAADLSK 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1350 VEHRVHQKSYHVAGYEHELSSLLRE-------KRQEVEGEHERR-------------------LDKMKEEHQ-------- 1395
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRElaeaeaqARASEERVRGGRaveevlkasiqgvhgtvaqLGSVGERYAtaievaag 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1396 ----------QVMAKAREQYEAEERKQRAELLghltgELERLqRAHERELETVRQ-----------EQHKRLE------- 1447
Cdd:TIGR02169 547 nrlnnvvvedDAVAKEAIELLKRRKAGRATFL-----PLNKM-RDERRDLSILSEdgvigfavdlvEFDPKYEpafkyvf 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1448 ---------DLRRRHREQERkLQDLELDL-----------------ETRAKDVKARLALLEVQEETARREKQQLLD---- 1497
Cdd:TIGR02169 621 gdtlvvediEAARRLMGKYR-MVTLEGELfeksgamtggsraprggILFSRSEPAELQRLRERLEGLKRELSSLQSelrr 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1498 VQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQvdllqaqsqqlqkhfsLEAEAQKKQHL 1577
Cdd:TIGR02169 700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE----------------IENVKSELKEL 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1578 LREVTVEENNASphfEPDLHIEDLRKSLGTNQTKEVSSSLSQSKE-----DLYLDSL-SSHNVWHLLSAegvALRSAKEF 1651
Cdd:TIGR02169 764 EARIEELEEDLH---KLEEALNDLEARLSHSRIPEIQAELSKLEEevsriEARLREIeQKLNRLTLEKE---YLEKEIQE 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1652 LVQQTRSMRRRQTALKAAQQHWRHELAS-AQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQ 1730
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEElEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
|
730
....*....|
gi 2462523740 1731 LESSLWEEAS 1740
Cdd:TIGR02169 918 RLSELKAKLE 927
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1246-1742 |
4.55e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.59 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1246 ERAS--------LEQKNRQMLEQLKEEIEASEKSE-QAALNAAkEKALQQLREQL---EGERKEAVATLEK------EHS 1307
Cdd:PRK02224 169 ERASdarlgverVLSDQRGSLDQLKAQIEEKEEKDlHERLNGL-ESELAELDEEIeryEEQREQARETRDEadevleEHE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1308 AELERLcSSLEAKHREvvssLQKKIQEAQQKEEAqlqkclgqVEHRVHQKSYHVAGYEHELSSLLREkrQEVEGEHERRL 1387
Cdd:PRK02224 248 ERREEL-ETLEAEIED----LRETIAETEREREE--------LAEEVRDLRERLEELEEERDDLLAE--AGLDDADAEAV 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1388 DKMKEEHQQVMAKAREQYEaEERKQRAELLGHLTGELERLQRAHER--ELETVRQEQHKRLEDLRRRHREQERKLQDLEL 1465
Cdd:PRK02224 313 EARREELEDRDEELRDRLE-ECRVAAQAHNEEAESLREDADDLEERaeELREEAAELESELEEAREAVEDRREEIEELEE 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1466 DLEtrakDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQS------NQQL------ 1533
Cdd:PRK02224 392 EIE----ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecGQPVegsphv 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1534 ------REILDELQARKLKLESQVDLLQAQSQQLQKHFSLEAEAQKKQHllREVTVEEnnasphfepdlHIEDLRKSLgt 1607
Cdd:PRK02224 468 etieedRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEE--RREDLEE-----------LIAERRETI-- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1608 NQTKEVSSSLSQSKEDlyldslsshnvwhlLSAEGVALRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELASAQEVAKDP 1687
Cdd:PRK02224 533 EEKRERAEELRERAAE--------------LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLL 598
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2462523740 1688 PGIKALEDMRKNLEKETRHLDEMKSAMRKghnLLKKKEEKLNQLESSLWEEASDE 1742
Cdd:PRK02224 599 AAIADAEDEIERLREKREALAELNDERRE---RLAEKRERKRELEAEFDEARIEE 650
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1121-1738 |
4.60e-09 |
|
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: 61.91 E-value: 4.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1121 EQLSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMRE 1200
Cdd:pfam02463 287 ELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1201 EESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERAS--LEQKNRQMLEQLKEEIEASEKSEQAALNA 1278
Cdd:pfam02463 367 KLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARqlEDLLKEEKKEELEILEEEEESIELKQGKL 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1279 AKEKALQQLRE------QLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQK---CLGQ 1349
Cdd:pfam02463 447 TEEKEELEKQElkllkdELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGvggRIIS 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1350 VEHRVHQKSYHVAGYEHELSSLL-----REKRQEVEGEHERR---------------LDKMKEEHQQVMAKAREQYEAEE 1409
Cdd:pfam02463 527 AHGRLGDLGVAVENYKVAISTAVivevsATADEVEERQKLVRaltelplgarklrllIPKLKLPLKSIAVLEIDPILNLA 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1410 RKQRAELLGHLTGELERLQRAHERE-LETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEetA 1488
Cdd:pfam02463 607 QLDKATLEADEDDKRAKVVEGILKDtELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQE--K 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1489 RREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSLE 1568
Cdd:pfam02463 685 AESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEE 764
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1569 AEAQKKQHLLREVTVEENNASPHFEPDLHIEDLRKSLG-TNQTKEVSSSLSQSKEDLYLDSLSSH---NVWHLLSAEGVA 1644
Cdd:pfam02463 765 EKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEElRALEEELKEEAELLEEEQLLIEQEEKikeEELEELALELKE 844
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1645 LRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELASAQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKK 1724
Cdd:pfam02463 845 EQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIK 924
|
650
....*....|....
gi 2462523740 1725 EEKLNQLESSLWEE 1738
Cdd:pfam02463 925 EEAEILLKYEEEPE 938
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1128-1746 |
1.11e-08 |
|
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: 60.83 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1128 LKAMEEAVAQVLE-QDQRHLLESKQEKMQQLREKLCQEEEE----------EILRLHQQKEQSLSSLRERLQKAIEEEEA 1196
Cdd:TIGR00606 254 LKEIEHNLSKIMKlDNEIKALKSRKKQMEKDNSELELKMEKvfqgtdeqlnDLYHNHQRTVREKERELVDCQRELEKLNK 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1197 RMREEESQRLSWLRAQVQSSTQAD--EDQIRAEQEASLQ-KLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQ 1273
Cdd:TIGR00606 334 ERRLLNQEKTELLVEQGRLQLQADrhQEHIRARDSLIQSlATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1274 AALNAAKEKALQQLREQLEGERKEAVATLEKEhSAELERLCSSLeakhREVVSSLQK---------KIQEAQQKEEAQLQ 1344
Cdd:TIGR00606 414 CADLQSKERLKQEQADEIRDEKKGLGRTIELK-KEILEKKQEEL----KFVIKELQQlegssdrilELDQELRKAERELS 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1345 KClgQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEGEHErrLDKMKEEHQQVMAKAREQYEAEER------KQRAELLG 1418
Cdd:TIGR00606 489 KA--EKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQ--LNHHTTTRTQMEMLTKDKMDKDEQirkiksRHSDELTS 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1419 HL-----TGELERLQRAHERELETVR------QEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARlallEVQEET 1487
Cdd:TIGR00606 565 LLgyfpnKKQLEDWLHSKSKEINQTRdrlaklNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS----QDEESD 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1488 ARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVdllqaqSQQLQKHFSL 1567
Cdd:TIGR00606 641 LERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKL------RLAPDKLKST 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1568 EAEAQKKQHLLREVTVE-ENNASPHFEPDLHIEDLRkslgtNQTKEVSSSLSQSKEDLYLDSlsshnvwHLLSAEGVALR 1646
Cdd:TIGR00606 715 ESELKKKEKRRDEMLGLaPGRQSIIDLKEKEIPELR-----NKLQKVNRDIQRLKNDIEEQE-------TLLGTIMPEEE 782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1647 SAKEFLVQQTrSMRRRQTALKAAQQHWRHELASAQEVAKDppgiKALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEE 1726
Cdd:TIGR00606 783 SAKVCLTDVT-IMERFQMELKDVERKIAQQAAKLQGSDLD----RTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQE 857
|
650 660
....*....|....*....|
gi 2462523740 1727 KLNQLESSLWEEASDEGTLG 1746
Cdd:TIGR00606 858 QIQHLKSKTNELKSEKLQIG 877
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
984-1551 |
1.38e-08 |
|
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: 60.37 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 984 DKDDSQSSQDELQSKQSKGLEERLspplphEERAQSPPRSLAT-EEEPPQGPEGQPEWKEAEELGEDSAASLSLQLSLQR 1062
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCT------PCMPDTYHERKQVlEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQ 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1063 EQapsppaacekgKEQHSQAEELGPGQEEAEDPEEKVAVSP-TPPVSPEVRSTEPVAPPEQLSEAALKAMEEAVAQVLEQ 1141
Cdd:TIGR00618 261 LL-----------KQLRARIEELRAQEAVLEETQERINRARkAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1142 DQRHL-----LESKQEKMQQL-----------------REKLCQEEEEE--ILRLHQQKE------QSLSSLRERLQK-- 1189
Cdd:TIGR00618 330 RAAHVkqqssIEEQRRLLQTLhsqeihirdahevatsiREISCQQHTLTqhIHTLQQQKTtltqklQSLCKELDILQReq 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1190 -------------AIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELE--------SQQKAERA 1248
Cdd:TIGR00618 410 atidtrtsafrdlQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQqlqtkeqiHLQETRKK 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1249 SLEQKNRQMLEQLKEEIEASEKSEQAALNAAKE-KALQQLREQLEGERK---EAVATLEKEHSAELERLCSSLEAKHREV 1324
Cdd:TIGR00618 490 AVVLARLLELQEEPCPLCGSCIHPNPARQDIDNpGPLTRRMQRGEQTYAqleTSEEDVYHQLTSERKQRASLKEQMQEIQ 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1325 VSSLQKKIQEAQQKEEAQ-LQKCLGQVEHRVHQKSyhvagyEHELSSLLREKRQEVEGEHERRL--------DKMKEEHQ 1395
Cdd:TIGR00618 570 QSFSILTQCDNRSKEDIPnLQNITVRLQDLTEKLS------EAEDMLACEQHALLRKLQPEQDLqdvrlhlqQCSQELAL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1396 QVMAKAREQYEAEERKQRAELLGHLTGELERLQR--AHERELE-----------------TVRQEQHKRLEDLRRRHREQ 1456
Cdd:TIGR00618 644 KLTALHALQLTLTQERVREHALSIRVLPKELLASrqLALQKMQsekeqltywkemlaqcqTLLRELETHIEEYDREFNEI 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1457 ERKLQDLELDLETRAKdvkarlALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQkehtHLLQSNQQLREI 1536
Cdd:TIGR00618 724 ENASSSLGSDLAARED------ALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELS----HLAAEIQFFNRL 793
|
650
....*....|....*
gi 2462523740 1537 LDELQARKLKLESQV 1551
Cdd:TIGR00618 794 REEDTHLLKTLEAEI 808
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1273-1511 |
2.22e-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: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1273 QAALNAAKEKALQQLREQLEgERKEAVATLEKEHSAELERLcssleAKHREVVSSLQKKIQEAQQkEEAQLQKCLGQVEH 1352
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIA-ELEKELAALKKEEKALLKQL-----AALERRIAALARRIRALEQ-ELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1353 RVHQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRahe 1432
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA--- 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462523740 1433 rELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATA 1511
Cdd:COG4942 168 -ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1205-1550 |
2.96e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1205 RLSWLRAQVQSSTQADEDQIRAEQEASLQKLREEL---ESQQKAERASLEQKN---------RQMLEQLKEEIEASEKSE 1272
Cdd:PRK02224 188 SLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIeryEEQREQARETRDEADevleeheerREELETLEAEIEDLRETI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1273 qaalnAAKEKALQQLREQLEgERKEAVATLEKEHSAELERlcSSLEAKHREVVSSLqkkiQEAQQKEEAQLQKCLGQVEH 1352
Cdd:PRK02224 268 -----AETEREREELAEEVR-DLRERLEELEEERDDLLAE--AGLDDADAEAVEAR----REELEDRDEELRDRLEECRV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1353 RVHQKSYHVAGYEHELSSL------LREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEER-----KQRAELLGHLT 1421
Cdd:PRK02224 336 AAQAHNEEAESLREDADDLeeraeeLREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapVDLGNAEDFLE 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1422 GELERLQRAHER--ELETVRQEQHKRLEDLRR------------------------RHREQERKLQDLELDLETRAKDVK 1475
Cdd:PRK02224 416 ELREERDELREReaELEATLRTARERVEEAEAlleagkcpecgqpvegsphvetieEDRERVEELEAELEDLEEEVEEVE 495
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462523740 1476 ARLALLEVQEETARR---EKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREildelQARKLKLESQ 1550
Cdd:PRK02224 496 ERLERAEDLVEAEDRierLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKRE-----AAAEAEEEAE 568
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1141-1552 |
3.56e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.20 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1141 QDQRHLLESKQEKMQQLREKLcqeeeEEILRLHQQKEQSLSSLRERLQKaieeeearmreeesqrlswlraqVQSSTQAD 1220
Cdd:PRK04863 296 YTSRRQLAAEQYRLVEMAREL-----AELNEAESDLEQDYQAASDHLNL-----------------------VQTALRQQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1221 EDQIRAEqeASLQKLREELESQQKAERASLEQK--NRQMLEQLKEEIEaSEKSE----QAALNAAKEKALQQlreqlege 1294
Cdd:PRK04863 348 EKIERYQ--ADLEELEERLEEQNEVVEEADEQQeeNEARAEAAEEEVD-ELKSQladyQQALDVQQTRAIQY-------- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1295 rKEAVATLEKehsaeLERLC--SSLEAKhrevvsSLQKKIQEAQQKEEAQLQKCLgQVEHRVHQKSYHVAGYEHELSSLL 1372
Cdd:PRK04863 417 -QQAVQALER-----AKQLCglPDLTAD------NAEDWLEEFQAKEQEATEELL-SLEQKLSVAQAAHSQFEQAYQLVR 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1373 RekrqeVEGEHERrldkmKEEHQQVMAKAREqyeAEERKQRAELLGHLTGELERLQRAH--ERELETVRQEQHKRL---- 1446
Cdd:PRK04863 484 K-----IAGEVSR-----SEAWDVARELLRR---LREQRHLAEQLQQLRMRLSELEQRLrqQQRAERLLAEFCKRLgknl 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1447 ---EDLRRRHREQERKLQDLELDLET-RAKDVKARLALLEVQEETARREKQQLLDVQRQVAL-----KSEEATATHQQLE 1517
Cdd:PRK04863 551 ddeDELEQLQEELEARLESLSESVSEaRERRMALRQQLEQLQARIQRLAARAPAWLAAQDALarlreQSGEEFEDSQDVT 630
|
410 420 430
....*....|....*....|....*....|....*
gi 2462523740 1518 EAQKEHTHLLQSNQQLReilDELQARKLKLESQVD 1552
Cdd:PRK04863 631 EYMQQLLERERELTVER---DELAARKQALDEEIE 662
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1295-1588 |
3.83e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1295 RKEAVATLEKEhSAELERLcsslEAKHREVVSSLQKKIQEAQQKEEAQ-LQKCLGQVEHRVHQKSYHVAGYE-HELSSLL 1372
Cdd:TIGR02168 174 RKETERKLERT-RENLDRL----EDILNELERQLKSLERQAEKAERYKeLKAELRELELALLVLRLEELREElEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1373 REKRQEVEgEHERRLDKMKEEHQQVMAkarEQYEAEERKQRA-ELLGHLTGELERL------QRAHERELETVRQEQHKR 1445
Cdd:TIGR02168 249 KEAEEELE-ELTAELQELEEKLEELRL---EVSELEEEIEELqKELYALANEISRLeqqkqiLRERLANLERQLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1446 LEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQV-ALKSEEATATHQ---------- 1514
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLeTLRSKVAQLELQiaslnneier 404
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462523740 1515 ---QLEEAQKEHTHLLQSNQQLREILDElqARKLKLESQVDLLQAQSQQLQKHF-SLEAEAQKKQHLLREVTVEENNA 1588
Cdd:TIGR02168 405 leaRLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELeRLEEALEELREELEEAEQALDAA 480
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1383-1572 |
4.37e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1383 HERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELEtvRQEQHKRLEDLRRRHREQERKLQD 1462
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE--KLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1463 LEldleTRAKDVKARLALLEVQEETARREKQQLLDVQRQVA-LKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQ 1541
Cdd:COG4717 144 LP----ERLEELEERLEELRELEEELEELEAELAELQEELEeLLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190
....*....|....*....|....*....|.
gi 2462523740 1542 ARKLKLESQVDLLQAQSQQLQKHFSLEAEAQ 1572
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1128-1543 |
4.46e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1128 LKAMEEAVAQVLEQdQRHL--LESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKaieeeearmreeesqr 1205
Cdd:COG4913 237 LERAHEALEDAREQ-IELLepIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE---------------- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1206 lswLRAQVQSsTQADEDQIRAEQEASLQKLREelesqqkAERASLEQKNRQmLEQLKEEIEASEKSEQAALNAAK--EKA 1283
Cdd:COG4913 300 ---LRAELAR-LEAELERLEARLDALREELDE-------LEAQIRGNGGDR-LEQLEREIERLERELEERERRRArlEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1284 LQQLREQLEGERkEAVATLEKEHSAELERLcSSLEAKHREVVSSLQKKIQEAQqKEEAQLQKCLGQVEHRVHQKSYHVAG 1363
Cdd:COG4913 368 LAALGLPLPASA-EEFAALRAEAAALLEAL-EEELEALEEALAEAEAALRDLR-RELRELEAEIASLERRKSNIPARLLA 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1364 YEHELSSLLREKRQE---------------------------------VEGEHERR----LDKMKEEHQQVMAKAREQYE 1406
Cdd:COG4913 445 LRDALAEALGLDEAElpfvgelievrpeeerwrgaiervlggfaltllVPPEHYAAalrwVNRLHLRGRLVYERVRTGLP 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1407 AEERKQ-----------------RAELLGHL-----------TGELERLQRA-------------HE------------- 1432
Cdd:COG4913 525 DPERPRldpdslagkldfkphpfRAWLEAELgrrfdyvcvdsPEELRRHPRAitragqvkgngtrHEkddrrrirsryvl 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1433 ---------------RELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEetARREKQQLLD 1497
Cdd:COG4913 605 gfdnraklaaleaelAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAE--LEAELERLDA 682
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2462523740 1498 -------VQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQAR 1543
Cdd:COG4913 683 ssddlaaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1226-1485 |
4.88e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1226 AEQEASLQKLREELESQQKA-ERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKaLQQLREQLEGERKEaVATLEK 1304
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVlKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEE-YEKLKEKLIKLKGE-IKSLKK 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1305 EHS--AELERLCSSLEAKHREV---VSSLQKKIQEAQQKEEAQLQKCLGQVEhRVHQKSYHVAGYEHELSSLLREKRQEv 1379
Cdd:PRK03918 547 ELEklEELKKKLAELEKKLDELeeeLAELLKELEELGFESVEELEERLKELE-PFYNEYLELKDAEKELEREEKELKKL- 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1380 egehERRLDKMKEEHQQVMAKARE----------QYEAEERKQRAELLGHLTGELERLqRAHERELETVRQEQHKRLEDL 1449
Cdd:PRK03918 625 ----EEELDKAFEELAETEKRLEElrkeleelekKYSEEEYEELREEYLELSRELAGL-RAELEELEKRREEIKKTLEKL 699
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2462523740 1450 RRRHREQERKLQDLEL---------DLETRAKDVKARL---ALLEVQE 1485
Cdd:PRK03918 700 KEELEEREKAKKELEKlekalerveELREKVKKYKALLkerALSKVGE 747
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1229-1463 |
5.25e-08 |
|
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: 58.43 E-value: 5.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1229 EASLQKLRE---ELESQQKAERASlEQKNRQMLEQLKEEIEASEK-SEQAALNAAKEKA--LQQLREQLEgERKEAVATL 1302
Cdd:COG3096 835 EAELAALRQrrsELERELAQHRAQ-EQQLRQQLDQLKEQLQLLNKlLPQANLLADETLAdrLEELREELD-AAQEAQAFI 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1303 EK--EHSAELERLCSSLEAKhREVVSSLQKKIQEAQQKEEAQLQKC--LGQVEHRVHQKSYHVA----GYEHELSSLLRE 1374
Cdd:COG3096 913 QQhgKALAQLEPLVAVLQSD-PEQFEQLQADYLQAKEQQRRLKQQIfaLSEVVQRRPHFSYEDAvgllGENSDLNEKLRA 991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1375 KRQEVEGEHERRLDKMK------EEHQQVMAKAREQYEAeerkqRAELLGHLTGELERL---------QRAHER------ 1433
Cdd:COG3096 992 RLEQAEEARREAREQLRqaqaqySQYNQVLASLKSSRDA-----KQQTLQELEQELEELgvqadaeaeERARIRrdelhe 1066
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2462523740 1434 ----------ELETVRQEQHKRLEDLRRRHREQERKLQDL 1463
Cdd:COG3096 1067 elsqnrsrrsQLEKQLTRCEAEMDSLQKRLRKAERDYKQE 1106
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1138-1508 |
5.37e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1138 VLEQDQRHLLESKQEKMQQLREKLcQEEEEEILRLHQQKEQsLSSLRERLQKAIEEEEARMREEESQR-LSWLRAQVQSS 1216
Cdd:COG4913 603 VLGFDNRAKLAALEAELAELEEEL-AEAEERLEALEAELDA-LQERREALQRLAEYSWDEIDVASAEReIAELEAELERL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1217 TQADED-----QIRAEQEASLQKLREELEsQQKAERASLEQKnrqmLEQLKEEIEASekseQAALNAAKEKALQQLREQL 1291
Cdd:COG4913 681 DASSDDlaaleEQLEELEAELEELEEELD-ELKGEIGRLEKE----LEQAEEELDEL----QDRLEAAEDLARLELRALL 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1292 EGERKEA-VATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQkclgqvEHRVHQKSYHvaGYEHELSS 1370
Cdd:COG4913 752 EERFAAAlGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETA------DLDADLESLP--EYLALLDR 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1371 LLREKRQEVEGEHERRLDKMKEEH----QQVMAKAREqyEAEERkqraelLGHLTGELERLQRAHERELE-TVRQEQHKR 1445
Cdd:COG4913 824 LEEDGLPEYEERFKELLNENSIEFvadlLSKLRRAIR--EIKER------IDPLNDSLKRIPFGPGRYLRlEARPRPDPE 895
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462523740 1446 LEDLRRRHREQERKLQDLELDL-ETRAKDVKARLALLEVQE-ETARREKQQLLDVQRQVALKSEE 1508
Cdd:COG4913 896 VREFRQELRAVTSGASLFDEELsEARFAALKRLIERLRSEEeESDRRWRARVLDVRNHLEFDAEE 960
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1431-1747 |
5.84e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1431 HERELETVR-----QEQHKRLEDLRRrhrEQERKLQDLEL---------DLETRAKDVKARLALLEVQEETARRE--KQQ 1494
Cdd:TIGR02168 171 KERRKETERklertRENLDRLEDILN---ELERQLKSLERqaekaerykELKAELRELELALLVLRLEELREELEelQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1495 LLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFS-----LEA 1569
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEeleaqLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1570 EAQKKQHLLREVT-VEENNASphFEPDlhIEDLRKSLGT-NQTKEVSSSLSQSKEDLYLDslsshnvwhlLSAEGVALRS 1647
Cdd:TIGR02168 328 LESKLDELAEELAeLEEKLEE--LKEE--LESLEAELEElEAELEELESRLEELEEQLET----------LRSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1648 AKEFLVQQTRSMRRRQTALKAAQQHWRHELASAQEVAKDPpgikALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEK 1727
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA----ELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
330 340
....*....|....*....|
gi 2462523740 1728 LNQLESSLWEEASDEGTLGG 1747
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQA 489
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1363-1710 |
6.95e-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: 58.16 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1363 GYEHELSSLLREKRqEVEGEHERRLDKMKEEHQQV--MAKAREQYEAEERKQRAELlghltGELERLQRAHERELETVRQ 1440
Cdd:TIGR02169 685 GLKRELSSLQSELR-RIENRLDELSQELSDASRKIgeIEKEIEQLEQEEEKLKERL-----EELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1441 EqhkrLEDLRRRHREQERKLQDLELDLEtrakDVKARLALLEVQEETARREKqqlldVQRQVALKSEEATATHQQLEEAQ 1520
Cdd:TIGR02169 759 E----LKELEARIEELEEDLHKLEEALN----DLEARLSHSRIPEIQAELSK-----LEEEVSRIEARLREIEQKLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1521 KEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQqlqkhfSLEAEAQKKQHLLREVTVEennasphfepdlhIED 1600
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE------ELEEELEELEAALRDLESR-------------LGD 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1601 LRKslgtnQTKEVSSSLSQSKEdlyldslsshnvwhllsaegvALRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELASA 1680
Cdd:TIGR02169 887 LKK-----ERDELEAQLRELER---------------------KIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK 940
|
330 340 350
....*....|....*....|....*....|
gi 2462523740 1681 QEVAKDPPGIKALEDMRKNLEKETRHLDEM 1710
Cdd:TIGR02169 941 GEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1147-1738 |
7.81e-08 |
|
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: 57.82 E-value: 7.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1147 LESKQEKMQQLREKLCQeeeeeilrLHQQKEQSLSSLRERLQKAIEEEEARMReeesqrlswLRAQVQSSTQADEDQIRA 1226
Cdd:pfam15921 115 LQTKLQEMQMERDAMAD--------IRRRESQSQEDLRNQLQNTVHELEAAKC---------LKEDMLEDSNTQIEQLRK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1227 ---EQEASLQKLR------EELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLrEQLEGERKE 1297
Cdd:pfam15921 178 mmlSHEGVLQEIRsilvdfEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQL-EALKSESQN 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1298 AVATLEKEHSAELERLCSSLE----------AKHREVVSSLQKK---IQEAQQKEEAQLQKCLGQVEHRVHQksyhvagy 1364
Cdd:pfam15921 257 KIELLLQQHQDRIEQLISEHEveitgltekaSSARSQANSIQSQleiIQEQARNQNSMYMRQLSDLESTVSQ-------- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1365 eheLSSLLREKRQEVEgeherrlDKMKEEHQQVMAKAREQYEAE-ERKQRAELLGHLTGELERL-QRAHERELE-TVRQE 1441
Cdd:pfam15921 329 ---LRSELREAKRMYE-------DKIEELEKQLVLANSELTEARtERDQFSQESGNLDDQLQKLlADLHKREKElSLEKE 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1442 QHKRLED-----------LRRRHREQERKLQDLELDLETRAKDVKARL---------------------ALLEVQEETAR 1489
Cdd:pfam15921 399 QNKRLWDrdtgnsitidhLRRELDDRNMEVQRLEALLKAMKSECQGQMerqmaaiqgkneslekvssltAQLESTKEMLR 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1490 REKQQLldVQRQVALKSEEAT-----ATHQQLEEA------------------QKEHTHLLQSNQQLREILDELQARKLK 1546
Cdd:pfam15921 479 KVVEEL--TAKKMTLESSERTvsdltASLQEKERAieatnaeitklrsrvdlkLQELQHLKNEGDHLRNVQTECEALKLQ 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1547 ----------LESQVDLLQA--------QSQQLQKHFSLEAEAQKKQHLLREVTVEENNASPHFE------PDLHIEDLR 1602
Cdd:pfam15921 557 maekdkvieiLRQQIENMTQlvgqhgrtAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRelearvSDLELEKVK 636
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1603 KSLGTNQTKEVSSSLSQSKEDLYLDSLSSHNVWHLLSAEGVAL----RSAKEFLVQQTRSMRRRQTALKAAQQHWRHELA 1678
Cdd:pfam15921 637 LVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLkrnfRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLK 716
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1679 SAQevAKDPPGIKALEDMRKNLEKETRHLDEMKSAMR----------KGHNLLKKKEEKLNQLESSLWEE 1738
Cdd:pfam15921 717 SME--GSDGHAMKVAMGMQKQITAKRGQIDALQSKIQfleeamtnanKEKHFLKEEKNKLSQELSTVATE 784
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1206-1441 |
9.36e-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: 56.70 E-value: 9.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1206 LSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQknrqmLEQLKEEIEASEK------SEQAALNA- 1278
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ-----LAALERRIAALARriraleQELAALEAe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1279 -----AKEKALQQLREQLEGERKEAVATLEKEHSA-ELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEH 1352
Cdd:COG4942 85 laeleKEIAELRAELEAQKEELAELLRALYRLGRQpPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1353 RVHQKSYHVAgyehELSSLLREKRQEvegehERRLDKMKEEHQQVMAKAREQYEAEErkQRAELLGHLTGELERLQRAHE 1432
Cdd:COG4942 165 LRAELEAERA----ELEALLAELEEE-----RAALEALKAERQKLLARLEKELAELA--AELAELQQEAEELEALIARLE 233
|
....*....
gi 2462523740 1433 RELETVRQE 1441
Cdd:COG4942 234 AEAAAAAER 242
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1015-1339 |
9.36e-08 |
|
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: 57.07 E-value: 9.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1015 ERAQSPPRSLATEEEPPQGPEGQPEWKEAEELGEDsaaslslqlslqreQAPSPPAACEKGKEQHSQAEELGPgQEEAED 1094
Cdd:pfam09731 76 TGESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATK--------------DAAEAKAQLPKSEQEKEKALEEVL-KEAISK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1095 PEEKVAVSPTPPVSPEVRSTEPVAPPEQLSEAALKAMEEAVAQVLeqdqrHLLESKQEKMQQLREKLCQEEEEEILRLHQ 1174
Cdd:pfam09731 141 AESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSAL-----QKAEALAEKLKEVINLAKQSEEEAAPPLLD 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1175 QKEQSLSSLRERLQKAIEEEEArmreeeSQRLSWLRAQVQSSTqADEDQIRAEQEAS----------------------- 1231
Cdd:pfam09731 216 AAPETPPKLPEHLDNVEEKVEK------AQSLAKLVDQYKELV-ASERIVFQQELVSifpdiipvlkednllsnddlnsl 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1232 -------LQKLREELESQQKAERASLEQKnrqmLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEK 1304
Cdd:pfam09731 289 iahahreIDQLSKKLAELKKREEKHIERA----LEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEE 364
|
330 340 350
....*....|....*....|....*....|....*
gi 2462523740 1305 EHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKE 1339
Cdd:pfam09731 365 KLRTELERQAEAHEEHLKDVLVEQEIELQREFLQD 399
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1328-1734 |
9.58e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 9.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1328 LQKKIQEAQQKEE--AQLQKCLGQVEHRVHQKSYHVAGYEHELSSL-----LREKRQEVEgEHERRLDKMKEEHQQVMAK 1400
Cdd:COG4717 76 LEEELKEAEEKEEeyAELQEELEELEEELEELEAELEELREELEKLekllqLLPLYQELE-ALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1401 AREQYEAEERKQRAEllghltGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLET---RAKDVKAR 1477
Cdd:COG4717 155 LEELRELEEELEELE------AELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEaqeELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1478 LALLEVQEETArREKQQLLDVQRQVALKSE--EATATHQQLEEAQKEHTHLLQSNQQLREILDELQAR-KLKLESQVDll 1554
Cdd:COG4717 229 LEQLENELEAA-ALEERLKEARLLLLIAAAllALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAReKASLGKEAE-- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1555 qaqsqqlqkhfslEAEAQKKQHLLREVTVEENNASPHFEPDLHIEDLRKSLGT-NQTKEVSSSLSQSKEDLYLDSLSSHN 1633
Cdd:COG4717 306 -------------ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRiEELQELLREAEELEEELQLEELEQEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1634 VwHLLSAEGVALRSAKEFLVQQTrsmrRRQTALKAAQQHWRHELASAQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSA 1713
Cdd:COG4717 373 A-ALLAEAGVEDEEELRAALEQA----EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEE 447
|
410 420
....*....|....*....|.
gi 2462523740 1714 MRKGHNLLKKKEEKLNQLESS 1734
Cdd:COG4717 448 LEELREELAELEAELEQLEED 468
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1128-1506 |
9.92e-08 |
|
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: 57.27 E-value: 9.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1128 LKAMEEAVAQVLEQDQrhllESKQEKMQQLREKlcqeeeeeILRLHQQKEQ---SLSSLRERLQKAIeeeearmreeesQ 1204
Cdd:COG5185 248 LAQTSDKLEKLVEQNT----DLRLEKLGENAES--------SKRLNENANNlikQFENTKEKIAEYT------------K 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1205 RLSWLRAQVQSSTQADedqiRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQL------KEEIEASEKSEQAA--- 1275
Cdd:COG5185 304 SIDIKKATESLEEQLA----AAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLeaikeeIENIVGEVELSKSSeel 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1276 ------LNAAKEKALQQLREQlEGERKEAVATLE---KEHSAELERLCSSLEAKHREVvsslqkkiqEAQQKEEAQLQKC 1346
Cdd:COG5185 380 dsfkdtIESTKESLDEIPQNQ-RGYAQEILATLEdtlKAADRQIEELQRQIEQATSSN---------EEVSKLLNELISE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1347 LGQVEHRVhqksyhvagyEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREqyeaeerkqraellghLTGELER 1426
Cdd:COG5185 450 LNKVMREA----------DEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVST----------------LKATLEK 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1427 LQRAHERELETVRQEQHKRLEDLRRRHREQErklQDLELDLETRAKDVKARLALLE--VQEETARREKQQLLDVQRQVAL 1504
Cdd:COG5185 504 LRAKLERQLEGVRSKLDQVAESLKDFMRARG---YAHILALENLIPASELIQASNAktDGQAANLRTAVIDELTQYLSTI 580
|
..
gi 2462523740 1505 KS 1506
Cdd:COG5185 581 ES 582
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1370-1735 |
1.14e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1370 SLLREKRQEVEgeheRRLDKMKEEHQQVMAKARE---QYEAEERK-QRAELLGHLTGELERLQRA--------HERELET 1437
Cdd:TIGR02168 168 SKYKERRKETE----RKLERTRENLDRLEDILNElerQLKSLERQaEKAERYKELKAELRELELAllvlrleeLREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1438 VRQEqhkrLEDLRRRHREQERKLQDLELDLETrakdvkARLALLEVQEETARREK------QQLLDVQRQVALKSEEATA 1511
Cdd:TIGR02168 244 LQEE----LKEAEEELEELTAELQELEEKLEE------LRLEVSELEEEIEELQKelyalaNEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1512 THQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDllqaqsqqlqkhfSLEAEAQKKQHLLREVTveennasph 1591
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE-------------SLEAELEELEAELEELE--------- 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1592 fepdLHIEDLRKSLGTnqtkeVSSSLSQSKEDLYLdslsshnvwhlLSAEGVALRSAKEFLVQQTRSMRRRQTALKAAQQ 1671
Cdd:TIGR02168 372 ----SRLEELEEQLET-----LRSKVAQLELQIAS-----------LNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462523740 1672 HWRHELASAQEVAKDppgiKALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSL 1735
Cdd:TIGR02168 432 EAELKELQAELEELE----EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1323-1738 |
2.01e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1323 EVVSSLQKKIQEAQQ--KEEAQLQKCLGQVEHRVHQKSYHVagyeHELSSLLREKRQEVEGEHER--RLDKMKEEhqqvM 1398
Cdd:PRK03918 169 EVIKEIKRRIERLEKfiKRTENIEELIKEKEKELEEVLREI----NEISSELPELREELEKLEKEvkELEELKEE----I 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1399 AKAREQYEAEERKQRA--ELLGHLTGELERLqRAHERELETVRQE---------QHKRLEDLRRRHREQERKLQDLELDL 1467
Cdd:PRK03918 241 EELEKELESLEGSKRKleEKIRELEERIEEL-KKEIEELEEKVKElkelkekaeEYIKLSEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1468 ETRAKDVKARLALLEVQEETARREKQQLLDVQRQV------ALKSEEATATHQQLEEAQKEHTHLlqSNQQLREILDELQ 1541
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKELEKRLeeleerHELYEEAKAKKEELERLKKRLTGL--TPEKLEKELEELE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1542 ARKLKLESQVDLLQAQSQqlqkhfSLEAEAQKKQHLLREVTvEENNASPHFEPDLHiEDLRKSLGTNQTKEVSSSLSQSK 1621
Cdd:PRK03918 398 KAKEEIEEEISKITARIG------ELKKEIKELKKAIEELK-KAKGKCPVCGRELT-EEHRKELLEEYTAELKRIEKELK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1622 EdlyLDSLSSHnvwhlLSAEGVALRSakeFLVQQTRSMRRRQTA--LKAAQQHWR-HELASAQEVAKDPPGIK----ALE 1694
Cdd:PRK03918 470 E---IEEKERK-----LRKELRELEK---VLKKESELIKLKELAeqLKELEEKLKkYNLEELEKKAEEYEKLKekliKLK 538
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2462523740 1695 DMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSLWEE 1738
Cdd:PRK03918 539 GEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1123-1311 |
2.03e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 55.94 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1123 LSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKlcqeeeeeILRLHQQKEQSLSSLRERLQkaieeeearmreee 1202
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEE--------IHKLRNEFEKELRERRNELQ-------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1203 sqrlswlraQVQSSTQADEDQIRAEQEaSLQKLREELESQQKaeraSLEQKNRQmLEQLKEEIEASEKSEQAAL----NA 1278
Cdd:PRK12704 86 ---------KLEKRLLQKEENLDRKLE-LLEKREEELEKKEK----ELEQKQQE-LEKKEEELEELIEEQLQELerisGL 150
|
170 180 190
....*....|....*....|....*....|....*
gi 2462523740 1279 AKEKALQQLREQLEGE-RKEAVATL-EKEHSAELE 1311
Cdd:PRK12704 151 TAEEAKEILLEKVEEEaRHEAAVLIkEIEEEAKEE 185
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1125-1552 |
2.42e-07 |
|
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: 56.34 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1125 EAALKAMEEAVAQVLEQDQRHLLESKQekmqqLREKLCQEEEEeiLRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQ 1204
Cdd:pfam01576 130 EAKIKKLEEDILLLEDQNSKLSKERKL-----LEERISEFTSN--LAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1205 RLSWLRAQVQSSTQADE--DQIR------AEQEASLQKLREELES------QQKAERASLEQKNRQMLEQLKEEIEASEk 1270
Cdd:pfam01576 203 RQELEKAKRKLEGESTDlqEQIAelqaqiAELRAQLAKKEEELQAalarleEETAQKNNALKKIRELEAQISELQEDLE- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1271 SEQAALNAAkEKALQQLREQLEGERKEAVATL-----EKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQK 1345
Cdd:pfam01576 282 SERAARNKA-EKQRRDLGEELEALKTELEDTLdttaaQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1346 CLGQVEHRVHQKS---YHVAGYEHELSSLLREKR--QEVEGEHERRLDKMKEEHQQVMAKAREQyeAEERKQRAELLGHL 1420
Cdd:pfam01576 361 LTEQLEQAKRNKAnleKAKQALESENAELQAELRtlQQAKQDSEHKRKKLEGQLQELQARLSES--ERQRAELAEKLSKL 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1421 TGELERLQRAHErELETVRQEQHKRLEDLrrrhreqERKLQDLE--LDLETRAK------------DVKARLALLEVQEE 1486
Cdd:pfam01576 439 QSELESVSSLLN-EAEGKNIKLSKDVSSL-------ESQLQDTQelLQEETRQKlnlstrlrqledERNSLQEQLEEEEE 510
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462523740 1487 TARREKQQLLDVQRQVA---LKSEEATATHQQLEEAQKEHTHLLQS-NQQLRE---ILDELQARKLKLESQVD 1552
Cdd:pfam01576 511 AKRNVERQLSTLQAQLSdmkKKLEEDAGTLEALEEGKKRLQRELEAlTQQLEEkaaAYDKLEKTKNRLQQELD 583
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1209-1348 |
2.87e-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: 53.14 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1209 LRAQVQSSTQADED------QIRAEQEASLQKLREELEsQQKAERASLEQKnrqmLEQLKEEIEASEKSEQAALNAAKE- 1281
Cdd:pfam04012 9 VRANIHEGLDKAEDpekmleQAIRDMQSELVKARQALA-QTIARQKQLERR----LEQQTEQAKKLEEKAQAALTKGNEe 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462523740 1282 ---KALQQlREQLEG--ERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQK-KIQEAQQKEEAQLQKCLG 1348
Cdd:pfam04012 84 larEALAE-KKSLEKqaEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLlKARLKAAKAQEAVQTSLG 155
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1226-1415 |
3.61e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 55.17 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1226 AEQEASLQKLREELESQQKAERASLEQKnrQMLEQLKEEIEAsEKSEQAALNAAKEKALQQLREQLEgERKEAvatLEKE 1305
Cdd:PRK12704 36 AEEEAKRILEEAKKEAEAIKKEALLEAK--EEIHKLRNEFEK-ELRERRNELQKLEKRLLQKEENLD-RKLEL---LEKR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1306 hSAELERLCSSLEAKHREvvssLQKKIQEAQQKEEAQLQKCLgqvehrvhqksyHVAGYEHElssllrEKRQEVegeher 1385
Cdd:PRK12704 109 -EEELEKKEKELEQKQQE----LEKKEEELEELIEEQLQELE------------RISGLTAE------EAKEIL------ 159
|
170 180 190
....*....|....*....|....*....|
gi 2462523740 1386 rLDKMKEEHQQVMAKAREQYEaEERKQRAE 1415
Cdd:PRK12704 160 -LEKVEEEARHEAAVLIKEIE-EEAKEEAD 187
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1139-1551 |
3.88e-07 |
|
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: 55.41 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1139 LEQDQRHLLESKQEKMQQLREKlcqeeEEEILRLHQQKEQSLSSL---RERLQKAIEEEEARmreeeSQRLSWLRAQVQS 1215
Cdd:TIGR04523 223 LKKQNNQLKDNIEKKQQEINEK-----TTEISNTQTQLNQLKDEQnkiKKQLSEKQKELEQN-----NKKIKELEKQLNQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1216 STQADEDQIRAEQEASLQKLREELESQQKAERASLEQ--KNRQMLEQLKEEIEASEKSEQAalnaaKEKALQQLREQLEg 1293
Cdd:TIGR04523 293 LKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQisQNNKIISQLNEQISQLKKELTN-----SESENSEKQRELE- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1294 ERKEAVATLEKEHSAELERLcSSLEAKHREVVSSLQKKIQEAQQKEE--AQLQKCLGQVEHRVHQKSYHVAGYEHELSSL 1371
Cdd:TIGR04523 367 EKQNEIEKLKKENQSYKQEI-KNLESQINDLESKIQNQEKLNQQKDEqiKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1372 lREKRQEVEGEHERrLDKMKEEHQQVMAKAREQYEAEER--KQRAELLGHLTGELERLQRaHERELE------TVRQEQH 1443
Cdd:TIGR04523 446 -TNQDSVKELIIKN-LDNTRESLETQLKVLSRSINKIKQnlEQKQKELKSKEKELKKLNE-EKKELEekvkdlTKKISSL 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1444 K-RLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQE---------------ETARREKQQLL--------DVQ 1499
Cdd:TIGR04523 523 KeKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEknkeieelkqtqkslKKKQEEKQELIdqkekekkDLI 602
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2462523740 1500 RQVALKSEEATATHQQLEEAQKEhthllqsNQQLREILDELQARKLKLESQV 1551
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEKAKKE-------NEKLSSIIKNIKSKKNKLKQEV 647
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1143-1351 |
5.58e-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: 54.00 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1143 QRHLLESKQEKMQQLREKLcqEEEEEILRLHQQKEQSLSSLRERLQKAIEeEEARMREEESQRLSWLRAQVQsSTQADED 1222
Cdd:COG4942 18 QADAAAEAEAELEQLQQEI--AELEKELAALKKEEKALLKQLAALERRIA-ALARRIRALEQELAALEAELA-ELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1223 QIRAEQEASLQKLREELESQQKAERASLEQ------------KNRQMLEQLKEEIEaseksEQAALNAAKEKALQQLREQ 1290
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLAlllspedfldavRRLQYLKYLAPARR-----EQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462523740 1291 LEGERKEaVATLEKEHSAELERLcSSLEAKHREVVSSLQKKIQEAQ------QKEEAQLQKCLGQVE 1351
Cdd:COG4942 169 LEAERAE-LEALLAELEEERAAL-EALKAERQKLLARLEKELAELAaelaelQQEAEELEALIARLE 233
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1121-1536 |
5.87e-07 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 54.53 E-value: 5.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1121 EQLSEAALKAMEEAVAQVLEQD-----QRHLLESKQEKMQQLREKLCQ-EEEEEILRLHQQKEQSLSSLRERLQKAIEEE 1194
Cdd:COG5278 113 EALIDQWLAELEQVIALRRAGGleaalALVRSGEGKALMDEIRARLLLlALALAALLLAAAALLLLLLALAALLALAELL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1195 EARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQA 1274
Cdd:COG5278 193 LLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1275 ALNAAKEKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQkclgQVEHRV 1354
Cdd:COG5278 273 LLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAA----ALALLA 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1355 HQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERE 1434
Cdd:COG5278 349 ALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEAL 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1435 LETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQ 1514
Cdd:COG5278 429 AEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAAL 508
|
410 420
....*....|....*....|..
gi 2462523740 1515 QLEEAQKEHTHLLQSNQQLREI 1536
Cdd:COG5278 509 LLAAAEAALAAALAAALASAEL 530
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1128-1498 |
8.59e-07 |
|
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: 54.46 E-value: 8.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1128 LKAMEEAVAQ------VLEQDQRHLLESKQEKMQQLREKLCQ-----EEEEEILRLHQQKEQSLSSLRERLQKAIEEEEA 1196
Cdd:pfam12128 310 LSAADAAVAKdrseleALEDQHGAFLDADIETAAADQEQLPSwqselENLEERLKALTGKHQDVTAKYNRRRSKIKEQNN 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1197 RMREEESQRLSWLR-------AQVQSSTQADEDQIRAEQEASLQKLREE-LESQQKAERASLEQKNRQMLEQLKEEIEAS 1268
Cdd:pfam12128 390 RDIAGIKDKLAKIReardrqlAVAEDDLQALESELREQLEAGKLEFNEEeYRLKSRLGELKLRLNQATATPELLLQLENF 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1269 E------KSEQAALNAAKEkALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHreVVSSLQKKIQEAQQKEEAQ 1342
Cdd:pfam12128 470 DerieraREEQEAANAEVE-RLQSELRQARKRRDQASEALRQASRRLEERQSALDELEL--QLFPQAGTLLHFLRKEAPD 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1343 LQKCLGQVE-----HRVHQKSYHVAGYEHELSSL----LREKRQEV------EGEHERRLDKMKEEHQQVMAKAREQYEA 1407
Cdd:pfam12128 547 WEQSIGKVIspellHRTDLDPEVWDGSVGGELNLygvkLDLKRIDVpewaasEEELRERLDKAEEALQSAREKQAAAEEQ 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1408 eerkqraelLGHLTGELERLQRAHERELETV--------------RQEQHKRLEDLRRRHREQERKLQDLELDLETRAKD 1473
Cdd:pfam12128 627 ---------LVQANGELEKASREETFARTALknarldlrrlfdekQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKK 697
|
410 420
....*....|....*....|....*
gi 2462523740 1474 VKARLALLEVQEETARREKQQLLDV 1498
Cdd:pfam12128 698 HQAWLEEQKEQKREARTEKQAYWQV 722
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1257-1547 |
1.04e-06 |
|
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: 53.12 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1257 MLEQLKEEIEASEKSEQAALNAAKEK-ALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEA 1335
Cdd:pfam15558 13 MLARHKEEQRMRELQQQAALAWEELRrRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1336 QQKEEAQLQKclgqVEHRVHQKsyhvagyehelsslLREKRQEVEG---EHERRLdKMKEEHQQVMaKAREQYEAEERKQ 1412
Cdd:pfam15558 93 ESRWREQAED----QENQRQEK--------------LERARQEAEQrkqCQEQRL-KEKEEELQAL-REQNSLQLQERLE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1413 RAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLqDLELDLeTRAKDVKARLALLEVQE--ETARR 1490
Cdd:pfam15558 153 EACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELLRRL-SLEQSL-QRSQENYEQLVEERHRElrEKAQK 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462523740 1491 EKQQLLDVQRQVALKSEEATATHQQLEEA-----QKEHTHLLQSNQQLREILDELQARKLKL 1547
Cdd:pfam15558 231 EEEQFQRAKWRAEEKEEERQEHKEALAELadrkiQQARQVAHKTVQDKAQRARELNLEREKN 292
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1226-1476 |
1.26e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.81 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1226 AEQEASLQKLREELeSQQKAERASLEQKNRQM---LEQLKEEIEASEKSE-QAAL--NAAKEKALQQLREQLEgERKEAV 1299
Cdd:PRK04863 833 ADPEAELRQLNRRR-VELERALADHESQEQQQrsqLEQAKEGLSALNRLLpRLNLlaDETLADRVEEIREQLD-EAEEAK 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1300 ATLEK--EHSAELERLCSSLEAKHREVvSSLQKKIQEAQQKEEAQLQKC--LGQVEHRVHQKSYHVA----GYEHELSSL 1371
Cdd:PRK04863 911 RFVQQhgNALAQLEPIVSVLQSDPEQF-EQLKQDYQQAQQTQRDAKQQAfaLTEVVQRRAHFSYEDAaemlAKNSDLNEK 989
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1372 LREKRQEVEGEherrLDKMKEEHQQ----------VMAKAREQYEA-----EERKQRAELLG-HLTGELERLQRAHEREL 1435
Cdd:PRK04863 990 LRQRLEQAEQE----RTRAREQLRQaqaqlaqynqVLASLKSSYDAkrqmlQELKQELQDLGvPADSGAEERARARRDEL 1065
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2462523740 1436 etvrqeqHKRLEDLRRRHREQERKLQDLELDLETRAKDVKA 1476
Cdd:PRK04863 1066 -------HARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRK 1099
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
1211-1409 |
1.35e-06 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 53.33 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1211 AQVQSSTQADEDQIRAEQEAslQKLREELESQQKAERasleQKNRQMLEQLKEEIEASEKSEQAALNaaKEKALQQLREQ 1290
Cdd:PRK00106 62 AKRESKALKKELLLEAKEEA--RKYREEIEQEFKSER----QELKQIESRLTERATSLDRKDENLSS--KEKTLESKEQS 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1291 LE------GERKEAVATLEKEHSAELERLCSSLEAKHREVVsslqkkiqeaqqkeeaqlqkcLGQVEHRVhqksyhvagy 1364
Cdd:PRK00106 134 LTdkskhiDEREEQVEKLEEQKKAELERVAALSQAEAREII---------------------LAETENKL---------- 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462523740 1365 EHELSSLLREKRQEVegehERRLDKM-KEEHQQVMAKAREQYEAEE 1409
Cdd:PRK00106 183 THEIATRIREAEREV----KDRSDKMaKDLLAQAMQRLAGEYVTEQ 224
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1361-1539 |
1.63e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.86 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1361 VAGYEHELSSLLREKRQEVEGEHERRLDKMKEEhqqvMAKAREQYEAEERKQRAELlghltGELERLQRAHERELEtvrq 1440
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIKKEALLEAKEE----IHKLRNEFEKELRERRNEL-----QKLEKRLLQKEENLD---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1441 eqhKRLEDLRRRhreqERKLQDLELDLETRAKDVKARlallevQEETARREKQQLLDVQRQVALKSEEATAthQQLEEAQ 1520
Cdd:PRK12704 100 ---RKLELLEKR----EEELEKKEKELEQKQQELEKK------EEELEELIEEQLQELERISGLTAEEAKE--ILLEKVE 164
|
170
....*....|....*....
gi 2462523740 1521 KEHTHllQSNQQLREILDE 1539
Cdd:PRK12704 165 EEARH--EAAVLIKEIEEE 181
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1238-1581 |
1.69e-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: 53.19 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1238 ELESQQKAERASLEQKNRQMlEQLKEEIEASEKSEQAALNAAKE---------KALQQLREQLEGERKEA---------- 1298
Cdd:pfam05483 272 QLEEKTKLQDENLKELIEKK-DHLTKELEDIKMSLQRSMSTQKAleedlqiatKTICQLTEEKEAQMEELnkakaahsfv 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1299 -------VATLEKEHSAELERLCSSlEAKHREVVSSLQKKIQEAQQK---------EEAQLQKCLGQVEHRVHQK----- 1357
Cdd:pfam05483 351 vtefeatTCSLEELLRTEQQRLEKN-EDQLKIITMELQKKSSELEEMtkfknnkevELEELKKILAEDEKLLDEKkqfek 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1358 -SYHVAGYEHELSSLLREKRQEVEG-EHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGH---LTGELERL-QRAH 1431
Cdd:pfam05483 430 iAEELKGKEQELIFLLQAREKEIHDlEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHcdkLLLENKELtQEAS 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1432 ERELETVRQEQH------------KRLEDLRRRHREQERKLQDLELDLETRAKDVKARLallEVQEETARREKQQLLDVQ 1499
Cdd:pfam05483 510 DMTLELKKHQEDiinckkqeermlKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKL---DKSEENARSIEYEVLKKE 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1500 RQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREI-------LDELQARKLKLESQVDLLQAQSQQLQKHFSLEAEAQ 1572
Cdd:pfam05483 587 KQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKgsaenkqLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDK 666
|
410
....*....|.
gi 2462523740 1573 K--KQHLLREV 1581
Cdd:pfam05483 667 KisEEKLLEEV 677
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1384-1549 |
1.76e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.86 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1384 ERRLDKMKEEHQQVMAKAREqyEAEERKQRAELlghltgelerlqrahereleTVRQEQHKRLEDLRRRHREQERKLQDL 1463
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKK--EAEAIKKEALL--------------------EAKEEIHKLRNEFEKELRERRNELQKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1464 EldletraKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHthllqsNQQLREI--LDELQ 1541
Cdd:PRK12704 88 E-------KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQ------LQELERIsgLTAEE 154
|
....*...
gi 2462523740 1542 ARKLKLES 1549
Cdd:PRK12704 155 AKEILLEK 162
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1409-1688 |
2.15e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1409 ERKQRAELLGHLTGELERLQRAHErELETVRqEQHKRLEDLRRRHREQERKLQDLEL--DLETRAKDVKA--RLALLEVQ 1484
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHE-ALEDAR-EQIELLEPIRELAERYAAARERLAEleYLRAALRLWFAqrRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1485 EETARREKQQLldvQRQVALKSEEATATHQQLEEAQKEHthLLQSNQQLREILDELQARKLKLESQvdllqaqsqqlqkh 1564
Cdd:COG4913 297 LEELRAELARL---EAELERLEARLDALREELDELEAQI--RGNGGDRLEQLEREIERLERELEER-------------- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1565 fslEAEAQKKQHLLREVtveennaspHFEPDLHIEDLRKSLgtNQTKEVSSSLSQSKEDLyldslssHNVWHLLSAEGVA 1644
Cdd:COG4913 358 ---ERRRARLEALLAAL---------GLPLPASAEEFAALR--AEAAALLEALEEELEAL-------EEALAEAEAALRD 416
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2462523740 1645 LRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELASAQEVAKDPP 1688
Cdd:COG4913 417 LRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAEL 460
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1125-1543 |
2.57e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1125 EAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKLCQEEeeeilRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQ 1204
Cdd:COG4913 311 LERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLE-----RELEERERRRARLEALLAALGLPLPASAEEFAAL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1205 RLSW--LRAQVQSSTQADEDQiRAEQEASLQKLREELEsQQKAERASLEQKN-------RQMLEQLKEEIEASE------ 1269
Cdd:COG4913 386 RAEAaaLLEALEEELEALEEA-LAEAEAALRDLRRELR-ELEAEIASLERRKsniparlLALRDALAEALGLDEaelpfv 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1270 ------KSEQAALNAAKEKAL-----------------------QQLREQLEGERKEAVATLEKEHSAELERLCSSLEAK 1320
Cdd:COG4913 464 gelievRPEEERWRGAIERVLggfaltllvppehyaaalrwvnrLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFK 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1321 ----HREVVSSLQKKIQEAQQKEEAQLQKC------LGQV--EHRVHQK-------SYHVAGYE-----HELSSLLREKR 1376
Cdd:COG4913 544 phpfRAWLEAELGRRFDYVCVDSPEELRRHpraitrAGQVkgNGTRHEKddrrrirSRYVLGFDnraklAALEAELAELE 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1377 QEVEgEHERRLDKMKEEHQQvMAKAREQYEAEERKQRAEL--------LGHLTGELERLQRAHE--RELETVRQEQHKRL 1446
Cdd:COG4913 624 EELA-EAEERLEALEAELDA-LQERREALQRLAEYSWDEIdvasaereIAELEAELERLDASSDdlAALEEQLEELEAEL 701
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1447 EDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQ-KEHTH 1525
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIdALRAR 781
|
490
....*....|....*...
gi 2462523740 1526 LLQSNQQLREILDELQAR 1543
Cdd:COG4913 782 LNRAEEELERAMRAFNRE 799
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1227-1460 |
3.13e-06 |
|
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: 50.04 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1227 EQEASLQKLREelesQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAAlnaakeKALQQLREQLEGERKEAVATLEK-E 1305
Cdd:pfam15665 11 EHEAEIQALKE----AHEEEIQQILAETREKILQYKSKIGEELDLKRRI------QTLEESLEQHERMKRQALTEFEQyK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1306 HSAELERLCssLEAKHREVVSSLQKKIQEAQQKEEAQLQKclgqvehrvhqksyhvagyehelsslLREKRQEVEGEHER 1385
Cdd:pfam15665 81 RRVEERELK--AEAEHRQRVVELSREVEEAKRAFEEKLES--------------------------FEQLQAQFEQEKRK 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462523740 1386 RLDKMKEEHQQVMAKAREQYEAEERKqraellghLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKL 1460
Cdd:pfam15665 133 ALEELRAKHRQEIQELLTTQRAQSAS--------SLAEQEKLEELHKAELESLRKEVEDLRKEKKKLAEEYEQKL 199
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1224-1581 |
3.17e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1224 IRAEQEASLQKLREELESQQkaerASLEQKNRQMLEQLKEEIEASEksEQAALNAAKEKALQQLREQLEGERKEavatlE 1303
Cdd:COG4717 43 IRAMLLERLEKEADELFKPQ----GRKPELNLKELKELEEELKEAE--EKEEEYAELQEELEELEEELEELEAE-----L 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1304 KEHSAELERLcssleakhrEVVSSLQKKIQEAQQKEE--AQLQKCLGQVEHRVHQksyhVAGYEHELSSlLREKRQEVEG 1381
Cdd:COG4717 112 EELREELEKL---------EKLLQLLPLYQELEALEAelAELPERLEELEERLEE----LRELEEELEE-LEAELAELQE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1382 EHERRLDKMKEEHQQVMAKAREQYEA--EERKQRAELLGHLTGELERLQRAHER-ELETVRQEQHKRLEDLRR------- 1451
Cdd:COG4717 178 ELEELLEQLSLATEEELQDLAEELEElqQRLAELEEELEEAQEELEELEEELEQlENELEAAALEERLKEARLllliaaa 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1452 -----------------------------------------RHREQERKLQDLELDLETRAKDVKARLALLEVQEETARR 1490
Cdd:COG4717 258 llallglggsllsliltiagvlflvlgllallflllarekaSLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1491 EKQQLLDVQRQVALKSEEATATHQQL--EEAQKEHTHLLQSNQ-----QLREILD------ELQARKLKLESQVDLLQAQ 1557
Cdd:COG4717 338 ELLELLDRIEELQELLREAEELEEELqlEELEQEIAALLAEAGvedeeELRAALEqaeeyqELKEELEELEEQLEELLGE 417
|
410 420
....*....|....*....|....
gi 2462523740 1558 SQQLQKHFSLEAEAQKKQHLLREV 1581
Cdd:COG4717 418 LEELLEALDEEELEEELEELEEEL 441
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1211-1342 |
3.74e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 51.38 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1211 AQVQSSTQADEDQIRAEQEAslQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQ 1290
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQER--QKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAK 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462523740 1291 LEGERK-------EAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQ 1342
Cdd:TIGR02794 128 QAAEAKakaeaeaERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAE 186
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1223-1339 |
5.08e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.75 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1223 QIRAEQEA-SLQKLREELESQQKaeraSLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVAT 1301
Cdd:PRK00409 529 ERELEQKAeEAEALLKEAEKLKE----ELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASV 604
|
90 100 110
....*....|....*....|....*....|....*...
gi 2462523740 1302 LEKEHSAELERLCSSLEAKHREvvsslqKKIQEAQQKE 1339
Cdd:PRK00409 605 KAHELIEARKRLNKANEKKEKK------KKKQKEKQEE 636
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1373-1545 |
5.37e-06 |
|
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: 50.69 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1373 REKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRR 1452
Cdd:pfam13868 31 KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1453 HREQERKLQD-LELDLETR---AKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHT---- 1524
Cdd:pfam13868 111 QEEDQAEAEEkLEKQRQLReeiDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIarlr 190
|
170 180
....*....|....*....|.
gi 2462523740 1525 HLLQSNQQLREILDELQARKL 1545
Cdd:pfam13868 191 AQQEKAQDEKAERDELRAKLY 211
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
59-89 |
6.91e-06 |
|
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: 44.44 E-value: 6.91e-06
10 20 30
....*....|....*....|....*....|.
gi 2462523740 59 PGEWKPCQDITGDIYYFNFANGQSMWDHPCD 89
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1212-1544 |
6.99e-06 |
|
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: 51.01 E-value: 6.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1212 QVQSSTQADEDQIRAEQEASLQKLREELESqqkaeraslEQKNRQMLEQLKEEIEASEKsEQAALNAAKEKALQQLREQL 1291
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELDELLES---------EEKNREEVEELKDKYRELRK-TLLANRFSYGPAIDELEKQL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1292 EgerkeavaTLEKEHSaELERLCSS---LEAkhREVVSSLQKKIQEAQQKEE------AQLQKCL-GQVEhrvhqksyhv 1361
Cdd:pfam06160 156 A--------EIEEEFS-QFEELTESgdyLEA--REVLEKLEEETDALEELMEdipplyEELKTELpDQLE---------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1362 agyehELSSLLRE-KRQEVEGEH---ERRLDKMKEEHQQVMA--KAREQYEAEerkqraELLGHLTGELERLQRAHEREL 1435
Cdd:pfam06160 215 -----ELKEGYREmEEEGYALEHlnvDKEIQQLEEQLEENLAllENLELDEAE------EALEEIEERIDQLYDLLEKEV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1436 ETvRQEQHKRLEDLRRRHREQERKLQDLELDLETrakdVKARLALLEVQEETARREKQQLLDVQRQVAL---KSEEATAT 1512
Cdd:pfam06160 284 DA-KKYVEKNLPEIEDYLEHAEEQNKELKEELER----VQQSYTLNENELERVRGLEKQLEELEKRYDEiveRLEEKEVA 358
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2462523740 1513 H-----------QQLEEAQKEHTHLLQSNQQLREilDELQARK 1544
Cdd:pfam06160 359 YselqeeleeilEQLEEIEEEQEEFKESLQSLRK--DELEARE 399
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1303-1547 |
7.30e-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: 51.28 E-value: 7.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1303 EKEHSAELERLCSSLEAKHREVvsSLQKKIQEAQQKEEAQLQKclgqvehrvhQKSYHVagyEHELSSLlrekrqevegE 1382
Cdd:pfam17380 291 EKFEKMEQERLRQEKEEKAREV--ERRRKLEEAEKARQAEMDR----------QAAIYA---EQERMAM----------E 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1383 HERRLDKMK-EEHQQVMAKAREQYEAEERKQraellghlTGELERLQRAHERELETVRQE-----QHKRLEDlrrrhrEQ 1456
Cdd:pfam17380 346 RERELERIRqEERKRELERIRQEEIAMEISR--------MRELERLQMERQQKNERVRQEleaarKVKILEE------ER 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1457 ERKLQDLELDLET-RAKDVKARLALLEVQEETARRE----KQQLLDVQRQVA-LKSEEATATHQQLEEAQKEHTHLLQSN 1530
Cdd:pfam17380 412 QRKIQQQKVEMEQiRAEQEEARQREVRRLEEERAREmervRLEEQERQQQVErLRQQEEERKRKKLELEKEKRDRKRAEE 491
|
250
....*....|....*..
gi 2462523740 1531 QQLREILDELQARKLKL 1547
Cdd:pfam17380 492 QRRKILEKELEERKQAM 508
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1125-1386 |
9.58e-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: 50.89 E-value: 9.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1125 EAALKAMEEAVAQVLEQD-QRHLLESKQEKMQQLREKLCQEEEEEIL---RLHQQKEQSLSSLRERL-----QKAIEEEE 1195
Cdd:pfam17380 332 QAAIYAEQERMAMERERElERIRQEERKRELERIRQEEIAMEISRMReleRLQMERQQKNERVRQELeaarkVKILEEER 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1196 ARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLR-EELESQQKAE--RASLEQKNRQMLEQLKEEIEASEKSE 1272
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRlEEQERQQQVErlRQQEEERKRKKLELEKEKRDRKRAEE 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1273 QAALNAAKEKALQQlREQLEGERKEAVatLEKEhsaelerlcssLEAKHREVVSSLQKKIQEAQQKEEAQLQKclgqvEH 1352
Cdd:pfam17380 492 QRRKILEKELEERK-QAMIEEERKRKL--LEKE-----------MEERQKAIYEEERRREAEEERRKQQEMEE-----RR 552
|
250 260 270
....*....|....*....|....*....|....*..
gi 2462523740 1353 RVHQKSYHVAGYEHELSSLLREK---RQEVEGEHERR 1386
Cdd:pfam17380 553 RIQEQMRKATEERSRLEAMERERemmRQIVESEKARA 589
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1210-1345 |
1.02e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.19 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1210 RAQVQSSTQADEDQIR--AEQEASLQKLREELESQQKAERAslEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKAlqql 1287
Cdd:PRK09510 80 QRKKKEQQQAEELQQKqaAEQERLKQLEKERLAAQEQKKQA--EEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEA---- 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462523740 1288 rEQLEGERKEAVATLEKEHSAELERLCSSlEAKHREVVSSLQKKIQEAQQKEEAQLQK 1345
Cdd:PRK09510 154 -KRAAAAAKKAAAEAKKKAEAEAAKKAAA-EAKKKAEAEAAAKAAAEAKKKAEAEAKK 209
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1174-1730 |
1.29e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.56 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1174 QQKEQSLSSLRERLQKAieeeearmrEEESQRLSWLRAQVQSSTQADEDQIRAEQeaslqklreELESQQKAERASLEQK 1253
Cdd:pfam01576 8 QAKEEELQKVKERQQKA---------ESELKELEKKHQQLCEEKNALQEQLQAET---------ELCAEAEEMRARLAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1254 nRQMLEQLKEEIEA--SEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKEHsaeLERLcsSLEAKhrevvsslQKK 1331
Cdd:pfam01576 70 -KQELEEILHELESrlEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQ---LEKV--TTEAK--------IKK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1332 IQEAQQKEEAQ---LQKCLGQVEHRVHQKSYHVAGYEHELSSL--LREKRQEVEGEHERRLDKmKEEHQQVMAKAREQYE 1406
Cdd:pfam01576 136 LEEDILLLEDQnskLSKERKLLEERISEFTSNLAEEEEKAKSLskLKNKHEAMISDLEERLKK-EEKGRQELEKAKRKLE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1407 AEE----------RKQRAELLGHLTGELERLQRAHER-ELETVRQEQhkrledLRRRHREQERKLQDLELDLET----RA 1471
Cdd:pfam01576 215 GEStdlqeqiaelQAQIAELRAQLAKKEEELQAALARlEEETAQKNN------ALKKIRELEAQISELQEDLESeraaRN 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1472 KDVKARLALLE-----------------VQEETARREKQQLLDVQRQValkSEEATATHQQLEEAQKEHThllQSNQQLR 1534
Cdd:pfam01576 289 KAEKQRRDLGEelealkteledtldttaAQQELRSKREQEVTELKKAL---EEETRSHEAQLQEMRQKHT---QALEELT 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1535 EILDELQARKLKLEsqvdllqaqsqqLQKHfSLEAEAQKKQHLLREVT---VEENNASPHFEPDLHIEDLRKSLGTNQTK 1611
Cdd:pfam01576 363 EQLEQAKRNKANLE------------KAKQ-ALESENAELQAELRTLQqakQDSEHKRKKLEGQLQELQARLSESERQRA 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1612 EVSSSLsqSKEDLYLDSLSShnvwHLLSAEGVALRSAK-------------EFLVQQTR-----SMRRRQTALKAA--QQ 1671
Cdd:pfam01576 430 ELAEKL--SKLQSELESVSS----LLNEAEGKNIKLSKdvsslesqlqdtqELLQEETRqklnlSTRLRQLEDERNslQE 503
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1672 HWRHELASAQEVAKDPPGIKA-LEDMRKNLEKETRHLDEMKSAMRKghnlLKKKEEKLNQ 1730
Cdd:pfam01576 504 QLEEEEEAKRNVERQLSTLQAqLSDMKKKLEEDAGTLEALEEGKKR----LQRELEALTQ 559
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1141-1510 |
1.30e-05 |
|
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: 49.89 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1141 QDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQsLSSLRERLQKAIEEEEARMREEESQRLSWLRAqvQSSTQAD 1220
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRE-LESRVAELKEELRQSREKHEELEEKYKELSAS--SEELSEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1221 EDQIRAEQEASLQKLREELESQQKAERASLEQKNRqmLEQLKEEIE---ASEKSEQaalnaAKEKALQQLREQLEGERKE 1297
Cdd:pfam07888 117 KDALLAQRAAHEARIRELEEDIKTLTQRVLERETE--LERMKERAKkagAQRKEEE-----AERKQLQAKLQQTEEELRS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1298 AVATLEKEHSAELERLCSSLEAkhREVVSSLQKKIQEAQQKEEA--QLQKCLGQVEHRVHQKSYHVAGYEHELSSLLREK 1375
Cdd:pfam07888 190 LSKEFQELRNSLAQRDTQVLQL--QDTITTLTQKLTTAHRKEAEneALLEELRSLQERLNASERKVEGLGEELSSMAAQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1376 RQEVEGEHERRLDKMKEEHQQVMA-------KAREQYEAEERKQRAEL----LGHLTGELERLQRAHEREletvRQEQHK 1444
Cdd:pfam07888 268 DRTQAELHQARLQAAQLTLQLADAslalregRARWAQERETLQQSAEAdkdrIEKLSAELQRLEERLQEE----RMEREK 343
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462523740 1445 RLEDL-------RRRHREQERKLQDLeldletrakdvKARLALLEVQEETARREKQQLLDVQRQVALKSEEAT 1510
Cdd:pfam07888 344 LEVELgrekdcnRVQLSESRRELQEL-----------KASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVA 405
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1143-1581 |
1.38e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.56 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1143 QRHLLESKQEKMQQLREKLCQEEEE--EILRLHQQKEQSLSSLRERLQK-----AIEEEEARMREEESQRLSWLRAQVQS 1215
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESElkELEKKHQQLCEEKNALQEQLQAetelcAEAEEMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1216 STQADEDQIRAEQ------EASLQKLREELESQQKA------ERASLEQKNRQMLEQL-----------KE----EIEAS 1268
Cdd:pfam01576 83 RLEEEEERSQQLQnekkkmQQHIQDLEEQLDEEEAArqklqlEKVTTEAKIKKLEEDIllledqnsklsKErkllEERIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1269 EKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKEHSA--ELERLCSSLEAKH---REVVSSLQKKIQEAQ---QKEE 1340
Cdd:pfam01576 163 EFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGrqELEKAKRKLEGEStdlQEQIAELQAQIAELRaqlAKKE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1341 AQLQKCLGQVEHRVHQKSyHVAGYEHELSSLLREKRQEVEGEHERR-------------LDKMKEEHQQVMAKAREQYEA 1407
Cdd:pfam01576 243 EELQAALARLEEETAQKN-NALKKIRELEAQISELQEDLESERAARnkaekqrrdlgeeLEALKTELEDTLDTTAAQQEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1408 eeRKQRAELLGHLTGELERLQRAHERELETVRQ-------------EQHKR-----------LEDLRRRHREQERKLQDL 1463
Cdd:pfam01576 322 --RSKREQEVTELKKALEEETRSHEAQLQEMRQkhtqaleelteqlEQAKRnkanlekakqaLESENAELQAELRTLQQA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1464 ELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLE----EAQKEHTHLLQSNQQLREILDE 1539
Cdd:pfam01576 400 KQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEgkniKLSKDVSSLESQLQDTQELLQE 479
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2462523740 1540 LQARKLKLESQVDLLQAQSQQLQKHfsLEAEAQKKQHLLREV 1581
Cdd:pfam01576 480 ETRQKLNLSTRLRQLEDERNSLQEQ--LEEEEEAKRNVERQL 519
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1225-1585 |
1.42e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 49.91 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1225 RAEQEASLQKLREEL--ESQQKAERASLEQKNRQMLEQLKEEIEAS-EKSEQAALNAAKEKALQQLREQLEG-------- 1293
Cdd:COG5278 85 RAEIDELLAELRSLTadNPEQQARLDELEALIDQWLAELEQVIALRrAGGLEAALALVRSGEGKALMDEIRArllllala 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1294 -ERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSLL 1372
Cdd:COG5278 165 lAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALAL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1373 REKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRR 1452
Cdd:COG5278 245 LLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1453 HREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQ 1532
Cdd:COG5278 325 LAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAA 404
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2462523740 1533 LREILDELQARKLKLESQVDLLQAQSQQLQKHFSLEAEAQKKQHLLREVTVEE 1585
Cdd:COG5278 405 EAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALA 457
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1094-1382 |
1.46e-05 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 50.24 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1094 DPEEKVAVSPTPPVSPEVRSTEPVAP--PEQLSEA----------ALKAMEEAVAQVLEQDQRHLLESK--QEKMQQLRE 1159
Cdd:PLN03229 414 DPERKVNMKKREAVKTPVRELEGEVEklKEQILKAkessskpselALNEMIEKLKKEIDLEYTEAVIAMglQERLENLRE 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1160 KLCQEEEE----------EILRLHQQKEQSLS------SLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQADEDq 1223
Cdd:PLN03229 494 EFSKANSQdqlmhpvlmeKIEKLKDEFNKRLSrapnylSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMD- 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1224 iRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASE----KSEQAALNAAKEKALQQLREQLEGERKEAV 1299
Cdd:PLN03229 573 -RPEIKEKMEALKAEVASSGASSGDELDDDLKEKVEKMKKEIELELagvlKSMGLEVIGVTKKNKDTAEQTPPPNLQEKI 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1300 ATLEKEHSAELERLCSSLEAKHRevVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGyehelSSLLREKRQEV 1379
Cdd:PLN03229 652 ESLNEEINKKIERVIRSSDLKSK--IELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEALN-----SSELKEKFEEL 724
|
...
gi 2462523740 1380 EGE 1382
Cdd:PLN03229 725 EAE 727
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1409-1550 |
1.50e-05 |
|
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: 48.38 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1409 ERKQRAELLGHLTGELERLqrahERELETVRqeqhKRLEDLRRRHREQERKLQDLELDLET---RAKDVKARLAL----- 1480
Cdd:COG1579 18 ELDRLEHRLKELPAELAEL----EDELAALE----ARLEAAKTELEDLEKEIKRLELEIEEveaRIKKYEEQLGNvrnnk 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462523740 1481 ----LEVQEETARREKQQL----LDVQRQVALKSEEATATHQQLEEAQKEHTHLLqsnQQLREILDELQARKLKLESQ 1550
Cdd:COG1579 90 eyeaLQKEIESLKRRISDLedeiLELMERIEELEEELAELEAELAELEAELEEKK---AELDEELAELEAELEELEAE 164
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1298-1543 |
1.53e-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: 49.38 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1298 AVATLEKEHSAELERLcssleakhREVVSSLQKKIQEaQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSL---LRE 1374
Cdd:COG4942 17 AQADAAAEAEAELEQL--------QQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRIRALEQELAALeaeLAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1375 KRQEVEgEHERRLDKMKEEHQQVMAKAreqyEAEERKQRAELLGHLTGELERLQRAheRELETVRQEQHKRLEDLRRrhr 1454
Cdd:COG4942 88 LEKEIA-ELRAELEAQKEELAELLRAL----YRLGRQPPLALLLSPEDFLDAVRRL--QYLKYLAPARREQAEELRA--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1455 eqerKLQDLElDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEeatathQQLEEAQKEHTHLLQSNQQLR 1534
Cdd:COG4942 158 ----DLAELA-ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE------KELAELAAELAELQQEAEELE 226
|
....*....
gi 2462523740 1535 EILDELQAR 1543
Cdd:COG4942 227 ALIARLEAE 235
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1141-1631 |
1.58e-05 |
|
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: 50.11 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1141 QDQRHLLESKQEKMQQLREKlCQEEEEEILRLHQQK--------------EQSLSS---LRERLQKAIEEEEARMREEES 1203
Cdd:pfam05483 257 KDLTFLLEESRDKANQLEEK-TKLQDENLKELIEKKdhltkeledikmslQRSMSTqkaLEEDLQIATKTICQLTEEKEA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1204 QRLSWLRAQVQSSTqadedqIRAEQEASLQKLREELESQQKaeraSLEqKNRQMLEQLKEEIE--ASEKSEQAALNAAKE 1281
Cdd:pfam05483 336 QMEELNKAKAAHSF------VVTEFEATTCSLEELLRTEQQ----RLE-KNEDQLKIITMELQkkSSELEEMTKFKNNKE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1282 KALQQLREQLeGERKEAVatlekEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEaqlqkclgQVEHRVHQKSYHV 1361
Cdd:pfam05483 405 VELEELKKIL-AEDEKLL-----DEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEI--------QLTAIKTSEEHYL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1362 AGYEHELSSLLREKRQEVE-GEHERRL----DKMKEEHQQVMAKAREQYE--AEERKQRAELLGHLTgELERLQRAHERE 1434
Cdd:pfam05483 471 KEVEDLKTELEKEKLKNIElTAHCDKLllenKELTQEASDMTLELKKHQEdiINCKKQEERMLKQIE-NLEEKEMNLRDE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1435 LETVRQEQHKRLEDLR---RRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLdvQRQVALKsEEATA 1511
Cdd:pfam05483 550 LESVREEFIQKGDEVKcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELH--QENKALK-KKGSA 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1512 THQQLE----EAQKEHTHLLQSNQQLREILD----ELQARKLKLESQVDLLQAQSQQLQKHFSLEAEAQKK-QHLLRE-V 1581
Cdd:pfam05483 627 ENKQLNayeiKVNKLELELASAKQKFEEIIDnyqkEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRcQHKIAEmV 706
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1582 TVEENNASPHfepDLHIEDLRKSLGTNQTKEVSSSLSQSKEDLYLDSLSS 1631
Cdd:pfam05483 707 ALMEKHKHQY---DKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKA 753
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
58-87 |
1.70e-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: 1.70e-05
10 20 30
....*....|....*....|....*....|
gi 2462523740 58 LPGEWKPCQDITGDIYYFNFANGQSMWDHP 87
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1177-1374 |
1.95e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1177 EQSLSSLRERLQKAieeeearmreeeSQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQknrq 1256
Cdd:COG3206 181 EEQLPELRKELEEA------------EAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA---- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1257 mleqLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKEHS------AELERLCSSLEAKHREVVSSLQK 1330
Cdd:COG3206 245 ----LRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPdvialrAQIAALRAQLQQEAQRILASLEA 320
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462523740 1331 KIQEAQQkEEAQLQKCLGQVEHRVHQksyhVAGYEHELSSLLRE 1374
Cdd:COG3206 321 ELEALQA-REASLQAQLAQLEARLAE----LPELEAELRRLERE 359
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1097-1493 |
3.13e-05 |
|
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: 48.98 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1097 EKVAVSPTPPVSPEVRSTEPVAPPEQLSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKLcqeeeeeilrlhQQK 1176
Cdd:pfam09731 99 SEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHT------------DSL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1177 EQSLSSLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIrAEQEASLQKLREELESQQKAERAslEQKNRQ 1256
Cdd:pfam09731 167 KEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLL-DAAPETPPKLPEHLDNVEEKVEK--AQSLAK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1257 MLEQLKEEIEASEkseqaalnaakekalQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVvSSLQKKIQEAQ 1336
Cdd:pfam09731 244 LVDQYKELVASER---------------IVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREI-DQLSKKLAELK 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1337 QKEEAQLQKCLGQVEHrvhqksyhvagyehELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEerkqrael 1416
Cdd:pfam09731 308 KREEKHIERALEKQKE--------------ELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEK-------- 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1417 lghLTGELERLQRAHERELETVRQEQHkrlEDLRRRHR-------EQERKLQDLELD-LETRAKDVKARLALLEVQEETA 1488
Cdd:pfam09731 366 ---LRTELERQAEAHEEHLKDVLVEQE---IELQREFLqdikekvEEERAGRLLKLNeLLANLKGLEKATSSHSEVEDEN 439
|
....*
gi 2462523740 1489 RREKQ 1493
Cdd:pfam09731 440 RKAQQ 444
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1206-1504 |
3.35e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1206 LSWLRAQVQSSTQADEDQIRAEqeasLQKLREELESQQK---AERASLEQKNRQmLEQLKEEIEASEKSEQAALN--AAK 1280
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEE----LEQLREELEQAREeleQLEEELEQARSE-LEQLEEELEELNEQLQAAQAelAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1281 EKALQQLREQLEGERKEaVATLEKEhSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEE--AQLQKCLGQVEHRVHQKS 1358
Cdd:COG4372 100 QEELESLQEEAEELQEE-LEELQKE-RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEqlESLQEELAALEQELQALS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1359 yhVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETV 1438
Cdd:COG4372 178 --EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462523740 1439 RQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVAL 1504
Cdd:COG4372 256 ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAAL 321
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1126-1338 |
3.50e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 48.54 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1126 AALKAMEEAVAQVLEQdqrhlLESKQEKMQQLrEKLCQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMRE----- 1200
Cdd:PRK11637 75 AQLKKQEEAISQASRK-----LRETQNTLNQL-NKQIDELNASIAKLEQQQAAQERLLAAQLDAAFRQGEHTGLQlilsg 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1201 EESQRLSWLRAQVQSSTQADEDQIraeqeASLQKLREELeSQQKAErasLEQKNRQMLEQLKEEIEASEKSEQA------ 1274
Cdd:PRK11637 149 EESQRGERILAYFGYLNQARQETI-----AELKQTREEL-AAQKAE---LEEKQSQQKTLLYEQQAQQQKLEQArnerkk 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462523740 1275 ---ALNAAKEKALQQLRE--QLEGERKEAVATLEKEHSAELERlcsslEAKHREVVsslQKKIQEAQQK 1338
Cdd:PRK11637 220 tltGLESSLQKDQQQLSElrANESRLRDSIARAEREAKARAER-----EAREAARV---RDKQKQAKRK 280
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1047-1481 |
3.85e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.74 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1047 GEDSAASLSLQLSLQREQAPSP-------PAACEKGKEQHSQAEELGPGQEEAED---PEEKVAVSPTPPVSPEVRSTEP 1116
Cdd:PLN02939 3 AAESAALLSHGCGPIRSRAPFYlpsrrrlAVSCRARRRGFSSQQKKKRGKNIAPKqrsSNSKLQSNTDENGQLENTSLRT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1117 VAPPEQLSE--------AALKAMEEAVAQVLEQdQRHLLESKQEKMQQLRE--KLCQEEEEEILRLHQQKEQSLSSL--- 1183
Cdd:PLN02939 83 VMELPQKSTssdddhnrASMQRDEAIAAIDNEQ-QTNSKDGEQLSDFQLEDlvGMIQNAEKNILLLNQARLQALEDLeki 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1184 ---RERLQKAIEEEEarmreeesQRLSWLRAQVQSSTQadeDQIRAE-QEASLQKLREELESQQKAERASLEQKNRQmLE 1259
Cdd:PLN02939 162 lteKEALQGKINILE--------MRLSETDARIKLAAQ---EKIHVEiLEEQLEKLRNELLIRGATEGLCVHSLSKE-LD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1260 QLKEEieasekseqaalNAAKEKALQQLREQLE--GERKEAVATLEKEHSAeLERLCSSLEAK---HREVVSSLQKKIQE 1334
Cdd:PLN02939 230 VLKEE------------NMLLKDDIQFLKAELIevAETEERVFKLEKERSL-LDASLRELESKfivAQEDVSKLSPLQYD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1335 AQQKEEAQLQKCLGQVEHRVHQksyhvagyehelSSLLREKRQEVegehERRLDKMKEEHQQVMAKAREQYEAEERKQRA 1414
Cdd:PLN02939 297 CWWEKVENLQDLLDRATNQVEK------------AALVLDQNQDL----RDKVDKLEASLKEANVSKFSSYKVELLQQKL 360
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462523740 1415 ELLGhltgelERLQRAHERELETVR--QEQHKRLEDLRRRHREQERKlQDLELDLETRAKDVKARLALL 1481
Cdd:PLN02939 361 KLLE------ERLQASDHEIHSYIQlyQESIKEFQDTLSKLKEESKK-RSLEHPADDMPSEFWSRILLL 422
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1142-1547 |
3.90e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1142 DQRHLLESKQEKMQQLREklcqeeeeeiLRLHQQKEQSLSSLRERLQKaieeeearmreeesqrlswlRAQVQSSTQADE 1221
Cdd:PRK04863 507 EQRHLAEQLQQLRMRLSE----------LEQRLRQQQRAERLLAEFCK--------------------RLGKNLDDEDEL 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1222 DQIRAEQEASLQKLREELESQqkAERASLEqknRQMLEQLKEEIEASEKSEQAALNAakEKALQQLREQLEGERKEAVA- 1300
Cdd:PRK04863 557 EQLQEELEARLESLSESVSEA--RERRMAL---RQQLEQLQARIQRLAARAPAWLAA--QDALARLREQSGEEFEDSQDv 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1301 ------TLEKEHSAELERlcSSLEAKHRevvsSLQKKIQEAQQKEEAQLQKCLGQVEH-------------RVHQKSYHV 1361
Cdd:PRK04863 630 teymqqLLERERELTVER--DELAARKQ----ALDEEIERLSQPGGSEDPRLNALAERfggvllseiyddvSLEDAPYFS 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1362 AGY--------------------------------EHELSSLlREKRQEVE----------GEHERRLDKMKEEhqQVMA 1399
Cdd:PRK04863 704 ALYgparhaivvpdlsdaaeqlagledcpedlyliEGDPDSF-DDSVFSVEelekavvvkiADRQWRYSRFPEV--PLFG 780
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1400 K-AREQYEAE---ERKQRAELLGHLTGELERLQRAHERELETVRQ--------EQHKRLEDLRRRHREQERKLQDLE--- 1464
Cdd:PRK04863 781 RaAREKRIEQlraEREELAERYATLSFDVQKLQRLHQAFSRFIGShlavafeaDPEAELRQLNRRRVELERALADHEsqe 860
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1465 LDLETRAKDVKARLALL--------------------EVQEETARREKQQLLDVQRQVALKSEEATAthQQLEEAQKEHT 1524
Cdd:PRK04863 861 QQQRSQLEQAKEGLSALnrllprlnlladetladrveEIREQLDEAEEAKRFVQQHGNALAQLEPIV--SVLQSDPEQFE 938
|
490 500
....*....|....*....|...
gi 2462523740 1525 HLLQSNQQLREILDELQARKLKL 1547
Cdd:PRK04863 939 QLKQDYQQAQQTQRDAKQQAFAL 961
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1121-1448 |
4.21e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1121 EQLSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKAieEEEARMRE 1200
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA--EEELAEAE 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1201 EESQRLSWLRAQVQSSTQADEDQIRAEQEA------SLQKLREELESQQKAERAS------LEQKNRQMLEQLkEEIEAS 1268
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALREALDELRAEltllneEAANLRERLESLERRIAATerrledLEEQIEELSEDI-ESLAAE 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1269 EKSEQAALNAAKE--KALQQLREQLEGERKEAVATLEK------EHSAELERLCSSLEAKhREVVSSLQKKIQEAQQKEE 1340
Cdd:TIGR02168 861 IEELEELIEELESelEALLNERASLEEALALLRSELEElseelrELESKRSELRRELEEL-REKLAQLELRLEGLEVRID 939
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1341 AQLQKC--LGQVEHRVHQKSYhvagyehelssllrEKRQEVEGEHERRLDKMKEEHQQ---VMAKAREQYEAEErkqraE 1415
Cdd:TIGR02168 940 NLQERLseEYSLTLEEAEALE--------------NKIEDDEEEARRRLKRLENKIKElgpVNLAAIEEYEELK-----E 1000
|
330 340 350
....*....|....*....|....*....|....*.
gi 2462523740 1416 LLGHLTGELERLQRAHERELETVRQ---EQHKRLED 1448
Cdd:TIGR02168 1001 RYDFLTAQKEDLTEAKETLEEAIEEidrEARERFKD 1036
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
57-87 |
4.22e-05 |
|
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: 42.20 E-value: 4.22e-05
10 20 30
....*....|....*....|....*....|.
gi 2462523740 57 PLPGEWKPCQDITGDIYYFNFANGQSMWDHP 87
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKP 31
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1204-1590 |
4.64e-05 |
|
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: 48.89 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1204 QRLSWLRAQVQSSTQaDEDQIRAEQEaslQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKseQAALNAAKEKA 1283
Cdd:TIGR00606 591 DRLAKLNKELASLEQ-NKNHINNELE---SKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSK--QRAMLAGATAV 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1284 LQQLREQLEGERKEAVATLEK--EHSAELERLCSSLEAKHReVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQksyhV 1361
Cdd:TIGR00606 665 YSQFITQLTDENQSCCPVCQRvfQTEAELQEFISDLQSKLR-LAPDKLKSTESELKKKEKRRDEMLGLAPGRQSI----I 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1362 AGYEHELSSLlREKRQEVEGEHERRLDKMKEEHQQVmakarEQYEAEErkQRAELLGHLTGELERLQrahereletvrqe 1441
Cdd:TIGR00606 740 DLKEKEIPEL-RNKLQKVNRDIQRLKNDIEEQETLL-----GTIMPEE--ESAKVCLTDVTIMERFQ------------- 798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1442 qhKRLEDLRRRHREQERKLQDLELDLEtrakdvkarlalleVQEetARREKQQLLDVQRQVALKSEEatatHQQLEEAQK 1521
Cdd:TIGR00606 799 --MELKDVERKIAQQAAKLQGSDLDRT--------------VQQ--VNQEKQEKQHELDTVVSKIEL----NRKLIQDQQ 856
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462523740 1522 EHTHLLQSNqqlreiLDELQARKLKLESQVDLLQAQSQQlqkhfsLEAEAQKKQHLLREVTVEENNASP 1590
Cdd:TIGR00606 857 EQIQHLKSK------TNELKSEKLQIGTNLQRRQQFEEQ------LVELSTEVQSLIREIKDAKEQDSP 913
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1218-1290 |
5.31e-05 |
|
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: 45.16 E-value: 5.31e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462523740 1218 QADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQ 1290
Cdd:COG0711 47 KEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAE 119
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1222-1510 |
5.84e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.22 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1222 DQIRA--EQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKsEQAALNAAKEKA---LQQLREQLE---G 1293
Cdd:pfam00038 18 DKVRFleQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTV-ERARLQLELDNLrlaAEDFRQKYEdelN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1294 ERKEA---VATLEKE-HSAELERLcssleakhrevvsSLQKKIQEAQqkEEAQLQKCLGQVEHRvhqksyhvagyehELS 1369
Cdd:pfam00038 97 LRTSAendLVGLRKDlDEATLARV-------------DLEAKIESLK--EELAFLKKNHEEEVR-------------ELQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1370 SLLREKRQEVEGEHERRLDKmkeehQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKrLEDL 1449
Cdd:pfam00038 149 AQVSDTQVNVEMDAARKLDL-----TSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEE-ITEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1450 RRR----------HREQ----ERKLQDLELDLETRAKDVKARLALLEVQ-----EETAR--REKQQLLDVqrQVALKSEE 1508
Cdd:pfam00038 223 RRTiqsleielqsLKKQkaslERQLAETEERYELQLADYQELISELEAElqetrQEMARqlREYQELLNV--KLALDIEI 300
|
..
gi 2462523740 1509 AT 1510
Cdd:pfam00038 301 AT 302
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1215-1415 |
6.42e-05 |
|
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: 48.02 E-value: 6.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1215 SSTQADEDQIRAEQeASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGE 1294
Cdd:pfam15709 329 EQEKASRDRLRAER-AEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1295 RKEAVatlekEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQkclgqvehrvhqksyhvagyehelssllRE 1374
Cdd:pfam15709 408 RKQRL-----QLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQ----------------------------RQ 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462523740 1375 KRQEVE-GEHERRLDKMKEEH------QQVMAKAREQYEAEERKQRAE 1415
Cdd:pfam15709 455 KELEMQlAEEQKRLMEMAEEErleyqrQKQEAEEKARLEAEERRQKEE 502
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1238-1544 |
6.54e-05 |
|
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: 48.21 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1238 ELESQQKAERASLEQKNRQMLEqLKEEIeASEKSEQAALnaakEKALQQLREQLEGERKEAVA-TLEKEHSAELER---- 1312
Cdd:pfam07111 321 QLKAQDLEHRDSVKQLRGQVAE-LQEQV-TSQSQEQAIL----QRALQDKAAEVEVERMSAKGlQMELSRAQEARRrqqq 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1313 LCSSLEAKHREVVSSLqKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYeHELSSLLREK------RQE-------- 1378
Cdd:pfam07111 395 QTASAEEQLKFVVNAM-SSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKV-HTIKGLMARKvalaqlRQEscpppppa 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1379 --VEGEHERRLDKMKEEH--------------QQVMAKAREQYEAEeRKQRAELLGHLTGELERLQRAHE---RELETVR 1439
Cdd:pfam07111 473 ppVDADLSLELEQLREERnrldaelqlsahliQQEVGRAREQGEAE-RQQLSEVAQQLEQELQRAQESLAsvgQQLEVAR 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1440 QEQHKRLED---LRRRHREQE----RKLQDLELDLETRAKDvkaRLALLEVQEETARREKQQLLDVQRQVALKSEEATAT 1512
Cdd:pfam07111 552 QGQQESTEEaasLRQELTQQQeiygQALQEKVAEVETRLRE---QLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKER 628
|
330 340 350
....*....|....*....|....*....|..
gi 2462523740 1513 HQQLEEAQKEHTHllQSNQQLREILDELQARK 1544
Cdd:pfam07111 629 NQELRRLQDEARK--EEGQRLARRVQELERDK 658
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1222-1341 |
6.57e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 46.36 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1222 DQIRAEQEASLQKLREELeSQQKAERASLEQKnrqmLEQLKEEIEASEKSEQAALNAAKE----KALQQlREQLEGERKE 1297
Cdd:COG1842 29 DQAIRDMEEDLVEARQAL-AQVIANQKRLERQ----LEELEAEAEKWEEKARLALEKGREdlarEALER-KAELEAQAEA 102
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2462523740 1298 AVATLEkEHSAELERLcssleakhREVVSSLQKKIQEAQQKEEA 1341
Cdd:COG1842 103 LEAQLA-QLEEQVEKL--------KEALRQLESKLEELKAKKDT 137
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1222-1415 |
7.45e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 48.29 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1222 DQIRAEQEASLQ--KLREELESQQKAERASLEQK----NRQMLEQLKEEIEASEKSEQAALNAAKEKAL----QQLREQL 1291
Cdd:NF012221 1532 DNVVATSESSQQadAVSKHAKQDDAAQNALADKEraeaDRQRLEQEKQQQLAAISGSQSQLESTDQNALetngQAQRDAI 1611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1292 EGERKEAVATLEK------------EHSAEL---------ERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQkclgQV 1350
Cdd:NF012221 1612 LEESRAVTKELTTlaqgldaldsqaTYAGESgdqwrnpfaGGLLDRVQEQLDDAKKISGKQLADAKQRHVDNQQ----KV 1687
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462523740 1351 EHRVHQKSYHVA-GYEHELSSLLREKRQEVEGEhERRLDKMKEEHQQVMAKAREQYEAEERKQRAE 1415
Cdd:NF012221 1688 KDAVAKSEAGVAqGEQNQANAEQDIDDAKADAE-KRKDDALAKQNEAQQAESDANAAANDAQSRGE 1752
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1206-1549 |
7.85e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.13 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1206 LSWLRAQ-VQSSTQADEDQIRAE-QEASLQKlreeleSQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAakEKA 1283
Cdd:PRK10929 9 MAWLLSWgAYAATAPDEKQITQElEQAKAAK------TPAQAEIVEALQSALNWLEERKGSLERAKQYQQVIDNF--PKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1284 LQQLREQLEGERKE--------AVATLEKE------HSAELERLCSSLEAKHREVVSSLQkkiQEAQQKEEAqlQKCLGQ 1349
Cdd:PRK10929 81 SAELRQQLNNERDEprsvppnmSTDALEQEilqvssQLLEKSRQAQQEQDRAREISDSLS---QLPQQQTEA--RRQLNE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1350 VEHRVH-------------------QKSYHVAGY-EHELSSLLREKRQEVEgehERRLDKMKEEHQQVMAK--------- 1400
Cdd:PRK10929 156 IERRLQtlgtpntplaqaqltalqaESAALKALVdELELAQLSANNRQELA---RLRSELAKKRSQQLDAYlqalrnqln 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1401 AREQYEAEERKQRAELLGHLTGEL-----ERLQRahERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLET---RAK 1472
Cdd:PRK10929 233 SQRQREAERALESTELLAEQSGDLpksivAQFKI--NRELSQALNQQAQRMDLIASQQRQAASQTLQVRQALNTlreQSQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1473 DVKARLALLE-VQEETAR---REKQQLLD-------VQRqvaLKSEEATATHQQLEEAQKEHTHLLQSNQQlrEILDE-L 1540
Cdd:PRK10929 311 WLGVSNALGEaLRAQVARlpeMPKPQQLDtemaqlrVQR---LRYEDLLNKQPQLRQIRQADGQPLTAEQN--RILDAqL 385
|
....*....
gi 2462523740 1541 QARKLKLES 1549
Cdd:PRK10929 386 RTQRELLNS 394
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
797-1144 |
8.03e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 47.86 E-value: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 797 SQPEEKKDVSLDSDAAGPPTPCKPSSPGADSSLSSAvgkgRQGSGARPGLPEKEENEKSEPKicRNLVTPKADPTGSEPA 876
Cdd:PHA03307 45 SDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAP----ANESRSTPTWSLSTLAPASPAR--EGSPTPPGPSSPDPPP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 877 KASEKEAPEDTVDAGEEGSRREEAAKEPKKKASALEEGSSDASQEleiSEHMKEPQLSDSIASDPKSFHGL-----DFGF 951
Cdd:PHA03307 119 PTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVA---SDAASSRQAALPLSSPEETARAPssppaEPPP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 952 RSRISEHLLDVDVLSPVLGGACRQAQQPLGIEDKDDSQSSQDELQSKQSKGLEE--RLSPPLPHEERAQSPPRSLATEEE 1029
Cdd:PHA03307 196 STPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWgpENECPLPRPAPITLPTRIWEASGW 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1030 PPQGPEGQPEWKEAEELGEDSAAS--------LSLQLSLQREQAPSPPAACEKGKEQHSQAEELG--PGQEEAEDPEEKV 1099
Cdd:PHA03307 276 NGPSSRPGPASSSSSPRERSPSPSpsspgsgpAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAvsPGPSPSRSPSPSR 355
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2462523740 1100 AVSPTPPVSPEVRSTEPVAPPEQLSEAALKAMEEAVAQVLEQDQR 1144
Cdd:PHA03307 356 PPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARR 400
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1395-1524 |
8.06e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.90 E-value: 8.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1395 QQVMAKAREQYEAEERK-----QRAEllghltgELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLEt 1469
Cdd:PRK00409 501 ENIIEEAKKLIGEDKEKlneliASLE-------ELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAE- 572
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462523740 1470 rakdVKARLALLEVQEETARREKQ-QLLDVQRQVALKSEEATATHQQLEEAQKEHT 1524
Cdd:PRK00409 573 ----KEAQQAIKEAKKEADEIIKElRQLQKGGYASVKAHELIEARKRLNKANEKKE 624
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1372-1589 |
8.94e-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: 8.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1372 LREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEER-KQRAELLGHLTGELERLQR---AHERELETVRQEQHKRLE 1447
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiAALARRIRALEQELAALEAelaELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1448 DLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQValksEEATATHQQLEEAQKEHTHLL 1527
Cdd:COG4942 105 ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL----AELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462523740 1528 QSNQQLREILDELQARKLK----LESQVDLLQAQSQQlqkhfsLEAEAQKKQHLLREVTVEENNAS 1589
Cdd:COG4942 181 AELEEERAALEALKAERQKllarLEKELAELAAELAE------LQQEAEELEALIARLEAEAAAAA 240
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1142-1501 |
1.17e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.12 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1142 DQRHLLESKQEKMQQLREKlcqeeeeeILRLHQQ---KEQSLSSLRERLQKaieeeearmreeesqrlswlrAQVQSSTQ 1218
Cdd:pfam10174 384 DLKDMLDVKERKINVLQKK--------IENLQEQlrdKDKQLAGLKERVKS---------------------LQTDSSNT 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1219 ----ADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQmLEQLKEEIEAS--EKSEQ-AALNAAKEKA-------- 1283
Cdd:pfam10174 435 dtalTTLEEALSEKERIIERLKEQREREDRERLEELESLKKE-NKDLKEKVSALqpELTEKeSSLIDLKEHAsslassgl 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1284 -----LQQLREQLEGERKEAVAT---LEKEHSAEL-ERLCSSLEAKHREVVSSLQKKIQEAQ--QKEEAQLQKCLGQVEH 1352
Cdd:pfam10174 514 kkdskLKSLEIAVEQKKEECSKLenqLKKAHNAEEaVRTNPEINDRIRLLEQEVARYKEESGkaQAEVERLLGILREVEN 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1353 RVHQKSYHVAgyEHELSSLLREKRQEVEGEHERRLDK-MKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERL---- 1427
Cdd:pfam10174 594 EKNDKDKKIA--ELESLTLRQMKEQNKKVANIKHGQQeMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTrqel 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1428 -----------QRAHERE--LETVRQEqhkrledlRRRHREQERKLQDLELDLETRAKDvkARLALLEV--------QEE 1486
Cdd:pfam10174 672 datkarlsstqQSLAEKDghLTNLRAE--------RRKQLEEILEMKQEALLAAISEKD--ANIALLELssskkkktQEE 741
|
410
....*....|....*..
gi 2462523740 1487 TA--RREKQQLLDVQRQ 1501
Cdd:pfam10174 742 VMalKREKDRLVHQLKQ 758
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1408-1614 |
1.17e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1408 EERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEET 1487
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1488 ARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDEL-------QARKLKLESQVDLLQAQSQQ 1560
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELqseiaerEEELKELEEQLESLQEELAA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462523740 1561 LQKHFSLEAEAQKKQHlLREVTVEENNASPHFEPDLHIEDLRKSLGTNQTKEVS 1614
Cdd:COG4372 169 LEQELQALSEAEAEQA-LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELL 221
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1368-1522 |
1.75e-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: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1368 LSSLLREKRQEV-EGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRaellghltgELERLQRAH-ERELETVRQEQHKR 1445
Cdd:COG2268 186 LDALGRRKIAEIiRDARIAEAEAERETEIAIAQANREAEEAELEQER---------EIETARIAEaEAELAKKKAEERRE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1446 LEDLRRR-----HREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLL--DVQRQVALKSEEATATHQQlEE 1518
Cdd:COG2268 257 AETARAEaeaayEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKpaEAEKQAAEAEAEAEAEAIR-AK 335
|
....
gi 2462523740 1519 AQKE 1522
Cdd:COG2268 336 GLAE 339
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1220-1530 |
1.99e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.40 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1220 DEDQIRAEQEASlQKLREELESQQKAERASLEQKNRQMLEQ---------LKEEIEASEKSEQAALN---AAKEKALQQL 1287
Cdd:pfam02029 1 IEDEEEAARERR-RRAREERRRQKEEEEPSGQVTESVEPNEhnsyeedseLKPSGQGGLDEEEAFLDrtaKREERRQKRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1288 REQLEGE----------------RKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQlqkclgQVE 1351
Cdd:pfam02029 80 QEALERQkefdptiadekesvaeRKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVR------QAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1352 HRVHQKSYHVAgyEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAkaREQYEAEERKQRAELLGHLTGELERLQRAH 1431
Cdd:pfam02029 154 EEGEEEEDKSE--EAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLD--QKRGHPEVKSQNGEEEVTKLKVTTKRRQGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1432 ERELETVRQEQH------KRLEDLRRRHREQER--------KLQDLELDLETRAKDVKARLALLEvqEETARREKQQLld 1497
Cdd:pfam02029 230 LSQSQEREEEAEvfleaeQKLEELRRRRQEKESeefeklrqKQQEAELELEELKKKREERRKLLE--EEEQRRKQEEA-- 305
|
330 340 350
....*....|....*....|....*....|...
gi 2462523740 1498 vQRQVAlKSEEATATHQQLEEAQKEHTHLLQSN 1530
Cdd:pfam02029 306 -ERKLR-EEEEKRRMKEEIERRRAEAAEKRQKL 336
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1328-1499 |
2.47e-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: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1328 LQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHV-AGY------------------------EHELSSLLREKrqEVEGE 1382
Cdd:cd16269 107 CKQNEEASSKRCQALLQELSAPLEEKISQGSYSVpGGYqlyledreklvekyrqvprkgvkaEEVLQEFLQSK--EAEAE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1383 HERRLDKMKEEHQQVMAKAREQYEAEErkQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQD 1462
Cdd:cd16269 185 AILQADQALTEKEKEIEAERAKAEAAE--QERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALE 262
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462523740 1463 LELDLETRakdvkarlALLEVQEETARREKQQLLDVQ 1499
Cdd:cd16269 263 SKLKEQEA--------LLEEGFKEQAELLQEEIRSLK 291
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
983-1324 |
2.65e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 983 EDKDDSQSSQDELQSKqsKGLEERLSPPLPHEERAQSPPRSLATEEEPPQGpEGQPEWKEAE-------ELGEDSAASLS 1055
Cdd:TIGR02169 671 SEPAELQRLRERLEGL--KRELSSLQSELRRIENRLDELSQELSDASRKIG-EIEKEIEQLEqeeeklkERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1056 lQLSLQREQAPSPPAACEKGKEQhsQAEELGPGQEEAEDPEEKVAVSPTPPVSPEVRSTEpvappEQLS--EAALKAMEE 1133
Cdd:TIGR02169 748 -SLEQEIENVKSELKELEARIEE--LEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLE-----EEVSriEARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1134 AVaQVLEQDQRHLLESKQEKMQQLRE------KLCQEEEEEILRL---------HQQKEQSLSSLRERLQKAIEEEEARM 1198
Cdd:TIGR02169 820 KL-NRLTLEKEYLEKEIQELQEQRIDlkeqikSIEKEIENLNGKKeeleeeleeLEAALRDLESRLGDLKKERDELEAQL 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1199 REEEsQRLSWLRAQVQsstqaDEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQM-LEQLKEEIEASEKsEQAALN 1277
Cdd:TIGR02169 899 RELE-RKIEELEAQIE-----KKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELsLEDVQAELQRVEE-EIRALE 971
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2462523740 1278 AAKEKALQQLREQLE--GERKEAVATLEKEHSAELERLcSSLEAKHREV 1324
Cdd:TIGR02169 972 PVNMLAIQEYEEVLKrlDELKEKRAKLEEERKAILERI-EEYEKKKREV 1019
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1139-1475 |
2.98e-04 |
|
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: 45.78 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1139 LEQDQRHLLESKQEKMQQLREKlcQEEEEEILRLHQQKEQSLSSLRERLQKaieeeearmreeesqrlswLRAQVQSSTQ 1218
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEK--QNEIEKLKKENQSYKQEIKNLESQIND-------------------LESKIQNQEK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1219 adEDQIRAEQEASLQKLREELESQQKAERASLEqKNRQMLEQLKEEIEASEKsEQAALNAAKEKALQQLrEQLEGERKEA 1298
Cdd:TIGR04523 406 --LNQQKDEQIKKLQQEKELLEKEIERLKETII-KNNSEIKDLTNQDSVKEL-IIKNLDNTRESLETQL-KVLSRSINKI 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1299 VATLEKEhSAELERLCSSLEAKHREV------VSSLQKKIQEAQQKEEaQLQKCLGQVEHRVHQKSYHVAGYEHELSSLL 1372
Cdd:TIGR04523 481 KQNLEQK-QKELKSKEKELKKLNEEKkeleekVKDLTKKISSLKEKIE-KLESEKKEKESKISDLEDELNKDDFELKKEN 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1373 REKrqeVEGEHERRLDKMKEEHQQVMAKARE------QYEAEERKQRAELLghltgELERLQRAHERELETVRQEqHKRL 1446
Cdd:TIGR04523 559 LEK---EIDEKNKEIEELKQTQKSLKKKQEEkqelidQKEKEKKDLIKEIE-----EKEKKISSLEKELEKAKKE-NEKL 629
|
330 340
....*....|....*....|....*....
gi 2462523740 1447 EdlrrrhrEQERKLQDLELDLETRAKDVK 1475
Cdd:TIGR04523 630 S-------SIIKNIKSKKNKLKQEVKQIK 651
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1319-1495 |
3.01e-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: 44.53 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1319 AKHREVVSSLQKKIQEAQQkEEAQLQKCLGQVEHRVHqksyhvagyehELSSLLREKRQEVEgEHERRLDKMKEehQQVM 1398
Cdd:COG1579 20 DRLEHRLKELPAELAELED-ELAALEARLEAAKTELE-----------DLEKEIKRLELEIE-EVEARIKKYEE--QLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1399 AKAREQYEAeerkqraellghLTGELERLQRAHErELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARL 1478
Cdd:COG1579 85 VRNNKEYEA------------LQKEIESLKRRIS-DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170
....*....|....*..
gi 2462523740 1479 ALLEVQEETARREKQQL 1495
Cdd:COG1579 152 AELEAELEELEAEREEL 168
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1266-1550 |
3.29e-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: 46.10 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1266 EASEKSEQAAlnaAKEKALQQLREQLEGERKEAVAtLEKEHsAELERLCSSLEAKHREVVSSLQKkIQEAQQKEEAqlqk 1345
Cdd:COG3096 279 ERRELSERAL---ELRRELFGARRQLAEEQYRLVE-MAREL-EELSARESDLEQDYQAASDHLNL-VQTALRQQEK---- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1346 clgqvehrvhqksyhVAGYEHELSSLlrekrqevegehERRLdkmkEEHQQVMAKAREQY-EAEERKQRAEL-LGHLTGE 1423
Cdd:COG3096 349 ---------------IERYQEDLEEL------------TERL----EEQEEVVEEAAEQLaEAEARLEAAEEeVDSLKSQ 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1424 LERLQRA----HERELEtVRQ-----EQHKRL-----------EDLRRRHREQERKLQDLELDLETRAKDVKArlallev 1483
Cdd:COG3096 398 LADYQQAldvqQTRAIQ-YQQavqalEKARALcglpdltpenaEDYLAAFRAKEQQATEEVLELEQKLSVADA------- 469
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462523740 1484 qeetARREKQQLLDVQRQVA--LKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARklkLESQ 1550
Cdd:COG3096 470 ----ARRQFEKAYELVCKIAgeVERSQAWQTARELLRRYRSQQALAQRLQQLRAQLAELEQR---LRQQ 531
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1315-1522 |
3.70e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1315 SSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHqksyhvagyehelssllrEKRQEVEGEHERRLDKMKEEH 1394
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIH------------------KLRNEFEKELRERRNELQKLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1395 QQVMAKareqyeaEER-KQRAELLGHLTGELErlqrAHERELETVRQEQHKRLEDLRRRHREQERKLQDL-ELDLEtrak 1472
Cdd:PRK12704 89 KRLLQK-------EENlDRKLELLEKREEELE----KKEKELEQKQQELEKKEEELEELIEEQLQELERIsGLTAE---- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1473 dvKARLALLEVQEETARREKQQLLdvqRQValkSEEATathqqlEEAQKE 1522
Cdd:PRK12704 154 --EAKEILLEKVEEEARHEAAVLI---KEI---EEEAK------EEADKK 189
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1367-1548 |
4.04e-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: 43.90 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1367 ELSSLLREKRQEVEGEH--ERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRaHERELETVRQEQHK 1444
Cdd:pfam04012 33 DMQSELVKARQALAQTIarQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELAREALAEKKSLEK-QAEALETQLAQQRS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1445 RLEDLRRRHREQERKLQDLELDLETrakdVKARLALLEVQEETArrekqqlldvQRQVALKSEEATATHQQLEEAQKEht 1524
Cdd:pfam04012 112 AVEQLRKQLAALETKIQQLKAKKNL----LKARLKAAKAQEAVQ----------TSLGSLSTSSATDSFERIEEKIEE-- 175
|
170 180
....*....|....*....|....
gi 2462523740 1525 hlLQSNQQLREILDELQARKLKLE 1548
Cdd:pfam04012 176 --REARADAAAELASAVDLDAKLE 197
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
1233-1335 |
4.49e-04 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 42.90 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1233 QKLREELESQQKAERASLEQKNRQmLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAvatlEKEhsaeler 1312
Cdd:COG2825 42 KAAQKKLEKEFKKRQAELQKLEKE-LQALQEKLQKEAATLSEEERQKKERELQKKQQELQRKQQEA----QQD------- 109
|
90 100
....*....|....*....|...
gi 2462523740 1313 lcssLEAKHREVVSSLQKKIQEA 1335
Cdd:COG2825 110 ----LQKRQQELLQPILEKIQKA 128
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1231-1735 |
4.75e-04 |
|
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: 45.40 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1231 SLQKLREELESQQKAERASLEQKNrQMLEQLKEEIeaseKSEQAALNAAKEKaLQQLREQLEGERKEAVATLEK--EHSA 1308
Cdd:TIGR04523 215 SLESQISELKKQNNQLKDNIEKKQ-QEINEKTTEI----SNTQTQLNQLKDE-QNKIKKQLSEKQKELEQNNKKikELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1309 ELERLCSSLEAKHREVVSSLQKKIQE---AQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSL----------LREK 1375
Cdd:TIGR04523 289 QLNQLKSEISDLNNQKEQDWNKELKSelkNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSesensekqreLEEK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1376 RQEVEgeherRLDKMKEEHQQVMAKAREQYEAEERK--QRAELLGHLTGELERLQRAHEreletVRQEQHKRLEDLRRRH 1453
Cdd:TIGR04523 369 QNEIE-----KLKKENQSYKQEIKNLESQINDLESKiqNQEKLNQQKDEQIKKLQQEKE-----LLEKEIERLKETIIKN 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1454 REQERKLQDLELDLETRAKDVKARLALLEVQEETARRE----KQQLLDVQRQVALKSEEA---TATHQQLEEAQKEhthL 1526
Cdd:TIGR04523 439 NSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSinkiKQNLEQKQKELKSKEKELkklNEEKKELEEKVKD---L 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1527 LQSNQQLREILDELQARKLKLESQVDllqaqsqqlqkhfSLEAEAQKKqhllrevtveennasphfEPDLHIEDLRKSLG 1606
Cdd:TIGR04523 516 TKKISSLKEKIEKLESEKKEKESKIS-------------DLEDELNKD------------------DFELKKENLEKEID 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1607 TNQTKevsssLSQSKEDlyldslsshnvwhllsaegvalrsakeflvqqtrsmrrrQTALKAAQQHwrhelasAQEVAKD 1686
Cdd:TIGR04523 565 EKNKE-----IEELKQT---------------------------------------QKSLKKKQEE-------KQELIDQ 593
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2462523740 1687 ppgikaLEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSL 1735
Cdd:TIGR04523 594 ------KEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI 636
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1206-1731 |
4.82e-04 |
|
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: 45.20 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1206 LSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQqkaerasLEQKNRQMLeQLKEEIEaseKSEQAALNAAKEKALQ 1285
Cdd:pfam10174 164 LEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVL-------LDQKEKENI-HLREELH---RRNQLQPDPAKTKALQ 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1286 QLREQLE---GERKEAVATLEKE-----HSAELERLCSSLEAKHREVVSSLQK----KIQEAQQ---KEEAQLQKCLGQV 1350
Cdd:pfam10174 233 TVIEMKDtkiSSLERNIRDLEDEvqmlkTNGLLHTEDREEEIKQMEVYKSHSKfmknKIDQLKQelsKKESELLALQTKL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1351 EHRVHQKS---YHVAGYEHELSSllREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYE--AEERkqraellGHLTGELE 1425
Cdd:pfam10174 313 ETLTNQNSdckQHIEVLKESLTA--KEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQdlTEEK-------STLAGEIR 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1426 RLQR---AHERELETVrqeqHKRLEDLRRRHREQERKLQDLE---LDLETRAKDVKARLALLEvqeeTARREKQQLLDvq 1499
Cdd:pfam10174 384 DLKDmldVKERKINVL----QKKIENLQEQLRDKDKQLAGLKervKSLQTDSSNTDTALTTLE----EALSEKERIIE-- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1500 rqvALKSEEATATHQQLEEAQKehthLLQSNQQLREILDELQARKLKLESQVDLLQAQSQ--------QLQKHFSLEAEA 1571
Cdd:pfam10174 454 ---RLKEQREREDRERLEELES----LKKENKDLKEKVSALQPELTEKESSLIDLKEHASslassglkKDSKLKSLEIAV 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1572 QKK---------QHLLREVTVEENNASPHFepDLHIEDLRKSLGTNQTKevsSSLSQSKEDLYLDSLSSHNVWHLLSAEG 1642
Cdd:pfam10174 527 EQKkeecsklenQLKKAHNAEEAVRTNPEI--NDRIRLLEQEVARYKEE---SGKAQAEVERLLGILREVENEKNDKDKK 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1643 VAlrSAKEFLVQQTRSMRRRQTALKAAQQHWRHELAS-------AQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSAMR 1715
Cdd:pfam10174 602 IA--ELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQlleearrREDNLADNSQQLQLEELMGALEKTRQELDATKARLS 679
|
570
....*....|....*.
gi 2462523740 1716 KGHNLLKKKEEKLNQL 1731
Cdd:pfam10174 680 STQQSLAEKDGHLTNL 695
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1125-1337 |
4.85e-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: 45.33 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1125 EAALKAMEEAVAQVleqdqrhlleSKQEKMQQLREKLCQeeeeeiLRLHQQKEQSLSSLRERLQKAieeeearmreeeSQ 1204
Cdd:COG3096 475 EKAYELVCKIAGEV----------ERSQAWQTARELLRR------YRSQQALAQRLQQLRAQLAEL------------EQ 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1205 RLswlRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKN----------RQMLEQLKEEIEASEKSEQA 1274
Cdd:COG3096 527 RL---RQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAaeaveqrselRQQLEQLRARIKELAARAPA 603
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1275 ALNAAkeKALQQLREQLEGERKEAVA-------TLEKEHSAELERlcSSLEAKHREvvssLQKKIQEAQQ 1337
Cdd:COG3096 604 WLAAQ--DALERLREQSGEALADSQEvtaamqqLLEREREATVER--DELAARKQA----LESQIERLSQ 665
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1278-1522 |
4.96e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1278 AAKEKALQQLREQLEgERKEAVATLEKEhSAELERLcssLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQk 1357
Cdd:PRK04863 782 AAREKRIEQLRAERE-ELAERYATLSFD-VQKLQRL---HQAFSRFIGSHLAVAFEADPEAELRQLNRRRVELERALAD- 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1358 syhVAGYEHELSSLLREKRQEVEG--EHERRLDKMKEEH-QQVMAKAREQ-YEAEERKQRAELLGHLTGELERLQ---RA 1430
Cdd:PRK04863 856 ---HESQEQQQRSQLEQAKEGLSAlnRLLPRLNLLADETlADRVEEIREQlDEAEEAKRFVQQHGNALAQLEPIVsvlQS 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1431 HERELETVRQeQHKRLEDLRRRHREQERKLQDL-----ELDLETRAKDV----------KARLALLEVQEETAR---REK 1492
Cdd:PRK04863 933 DPEQFEQLKQ-DYQQAQQTQRDAKQQAFALTEVvqrraHFSYEDAAEMLaknsdlneklRQRLEQAEQERTRAReqlRQA 1011
|
250 260 270
....*....|....*....|....*....|..
gi 2462523740 1493 QQLLD--VQRQVALKSeEATATHQQLEEAQKE 1522
Cdd:PRK04863 1012 QAQLAqyNQVLASLKS-SYDAKRQMLQELKQE 1042
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1221-1345 |
5.23e-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: 43.76 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1221 EDQIRAEQEA--SLQKLREELESQQKAERASLEQKNRQM--------LEQLKEEIEASEKSEQAAlnaakEKALQQLREQ 1290
Cdd:COG1579 44 EARLEAAKTEleDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnnkeYEALQKEIESLKRRISDL-----EDEILELMER 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2462523740 1291 LEgERKEAVATLEKEHsAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQK 1345
Cdd:COG1579 119 IE-ELEEELAELEAEL-AELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
1237-1552 |
6.21e-04 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 44.17 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1237 EELESQQKAERASLEQKNrQMLEQLKEEIEASEKSEQAALNAAKEKA--LQQLREQLEGERKEAVATLEKehsaeLERLC 1314
Cdd:pfam09728 3 ARELMQLLNKLDSPEEKL-AALCKKYAELLEEMKRLQKDLKKLKKKQdqLQKEKDQLQSELSKAILAKSK-----LEKLC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1315 SSLEAKHREVVSSLQKKIQEAQQKEE---AQLQKCLGQVEHRVHQKSYHVAGYEHElSSLLREKRQEVEGEHERR----- 1386
Cdd:pfam09728 77 RELQKQNKKLKEESKKLAKEEEEKRKelsEKFQSTLKDIQDKMEEKSEKNNKLREE-NEELREKLKSLIEQYELRelhfe 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1387 -LDKMKEEHQQ-VMAKAREQYEAEERKQRaellghltgelerlqrahERELETVRQEQhKRLEDLRrrhrEQERKLQD-L 1463
Cdd:pfam09728 156 kLLKTKELEVQlAEAKLQQATEEEEKKAQ------------------EKEVAKARELK-AQVQTLS----ETEKELREqL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1464 ELDLEtRAKDVKARLALLEVQEETARREKQQLLDVQRQValkSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQAR 1543
Cdd:pfam09728 213 NLYVE-KFEEFQDTLNKSNEVFTTFKKEMEKMSKKIKKL---EKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKK 288
|
....*....
gi 2462523740 1544 KLKLESQVD 1552
Cdd:pfam09728 289 LEKLENLCR 297
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
1387-1550 |
6.47e-04 |
|
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: 43.22 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1387 LDKMKEEHQQVMAKAREQY-----EAEERKQRAEL-LGHLTGELERLQRAHERELETVRQeQHKRLEDLRRRHREQERKL 1460
Cdd:pfam14988 9 LAKKTEEKQKKIEKLWNQYvqeceEIERRRQELASrYTQQTAELQTQLLQKEKEQASLKK-ELQALRPFAKLKESQEREI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1461 QDLELDLET--RAKDVKARLALLEVQEETARREKQ-QLLDVQRQVALKSEEATATHQQLEEAQK----EHTHLL-QSNQQ 1532
Cdd:pfam14988 88 QDLEEEKEKvrAETAEKDREAHLQFLKEKALLEKQlQELRILELGERATRELKRKAQALKLAAKqalsEFCRSIkRENRQ 167
|
170 180
....*....|....*....|....*
gi 2462523740 1533 LREIL-------DELQARKLKLESQ 1550
Cdd:pfam14988 168 LQKELlqliqetQALEAIKSKLENR 192
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1128-1490 |
6.99e-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: 44.26 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1128 LKAMEEAVAQVLEQDQRHLL----ESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKaieeeearMREEES 1203
Cdd:pfam15558 37 LRRRDQKRQETLERERRLLLqqsqEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAED--------QENQRQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1204 QRLSWLRAQVQSSTQADEDQIRaEQEASLQKLRE--ELESQQKAERASLEQKNRQMLEQLKeeIEASEKSEQAALNAAKE 1281
Cdd:pfam15558 109 EKLERARQEAEQRKQCQEQRLK-EKEEELQALREqnSLQLQERLEEACHKRQLKEREEQKK--VQENNLSELLNHQARKV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1282 KALQQLREQLEGERKeavaTLEKEHSAELERLCSSLEAKHREvvsslqkkIQEAQQKEEAQLQKclgqvehrvhqksyhv 1361
Cdd:pfam15558 186 LVDCQAKAEELLRRL----SLEQSLQRSQENYEQLVEERHRE--------LREKAQKEEEQFQR---------------- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1362 agyehelsslLREKRQEVEGEHERRLDKMKEEHQQVMAKAReQYEAEERKQRAELLGHLTGELERLQRAHERELEtvRQE 1441
Cdd:pfam15558 238 ----------AKWRAEEKEEERQEHKEALAELADRKIQQAR-QVAHKTVQDKAQRARELNLEREKNHHILKLKVE--KEE 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2462523740 1442 QHKR---LEDLRRRHREQERKLQDLELDLETRAKDVKARLALLE-VQEETARR 1490
Cdd:pfam15558 305 KCHRegiKEAIKKKEQRSEQISREKEATLEEARKTARASFHMREkVREETNNR 357
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1233-1338 |
7.17e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 41.80 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1233 QKLREELESQQKAERASLEQKNRQmLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKehsaeler 1312
Cdd:smart00935 17 KAAQKQLEKEFKKRQAELEKLEKE-LQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQK-------- 87
|
90 100
....*....|....*....|....*.
gi 2462523740 1313 lcssleaKHREVVSSLQKKIQEAQQK 1338
Cdd:smart00935 88 -------RQQEELQKILDKINKAIKE 106
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1217-1497 |
7.42e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 44.63 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1217 TQADEDQIRAEQEASLQKLREELESQQKAERasleqKNRQMLEQLKEEIEASEKSEQAALNAAKEkaLQQLREQLEGERK 1296
Cdd:pfam05667 217 AAAQEWEEEWNSQGLASRLTPEEYRKRKRTK-----LLKRIAEQLRSAALAGTEATSGASRSAQD--LAELLSSFSGSST 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1297 EAVATLEKEHSAELERLCSSLEAKHREVVSSLQKK----IQEAQQKEEAQLQKCLGQVEHRVHQksyhvagYEHELSSLL 1372
Cdd:pfam05667 290 TDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVEteeeLQQQREEELEELQEQLEDLESSIQE-------LEKEIKKLE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1373 REKRQ-EVEGEHERRLDKMKEEHQQVMAKAREQY-EAEER--------KQRAELLGHLTGELERLQRAHERELETVRQEQ 1442
Cdd:pfam05667 363 SSIKQvEEELEELKEQNEELEKQYKVKKKTLDLLpDAEENiaklqalvDASAQRLVELAGQWEKHRVPLIEEYRALKEAK 442
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462523740 1443 HKRLEdlrrrhrEQERKLQDLEldlETRAKdvkarlaLLEVQEETARRE--KQQLLD 1497
Cdd:pfam05667 443 SNKED-------ESQRKLEEIK---ELREK-------IKEVAEEAKQKEelYKQLVA 482
|
|
| Ax_dynein_light |
pfam10211 |
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ... |
1222-1293 |
7.57e-04 |
|
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organizms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.
Pssm-ID: 463000 [Multi-domain] Cd Length: 187 Bit Score: 42.56 E-value: 7.57e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462523740 1222 DQIRAEQEASLQKLREELESQQKaERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKeKALQQLREQLEG 1293
Cdd:pfam10211 118 EQGKAELEKKIADLEEEKEELEK-QVAELKAKCEAIEKREEERRQAEEKKHAEEIAFLK-KTNQQLKAQLER 187
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1144-1577 |
8.36e-04 |
|
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: 44.36 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1144 RHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLR--ERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQADE 1221
Cdd:pfam09731 33 RDFFEEYIPYGEEVVLYALGEDPPLAPKPKTFRPLQPSVVSavTGESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1222 DQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNA------AKEKALQQLREQLEGER 1295
Cdd:pfam09731 113 AEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDSLKEAsdtaeiSREKATDSALQKAEALA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1296 KEAVATLEKEHSAELERLcSSLEAKHREVVSSLQKKIQEAQQKEEA--QLQKCLGQVEHRVH----QKSYHVAGYEHELS 1369
Cdd:pfam09731 193 EKLKEVINLAKQSEEEAA-PPLLDAAPETPPKLPEHLDNVEEKVEKaqSLAKLVDQYKELVAseriVFQQELVSIFPDII 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1370 SLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKqraellghltgeLERLQRAHERELETVRQEQHKRLEDL 1449
Cdd:pfam09731 272 PVLKEDNLLSNDDLNSLIAHAHREIDQLSKKLAELKKREEKH------------IERALEKQKEELDKLAEELSARLEEV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1450 RRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLdvqrqvalkseeatathQQLEEAQKEHTHLLQS 1529
Cdd:pfam09731 340 RAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLV-----------------EQEIELQREFLQDIKE 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2462523740 1530 nqqlrEILDELQARKLKLESQVDLLQAQSQQLQKHFSLEAEAQKKQHL 1577
Cdd:pfam09731 403 -----KVEEERAGRLLKLNELLANLKGLEKATSSHSEVEDENRKAQQL 445
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1250-1544 |
1.02e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1250 LEQKNRQMLEQLKEEIEASEKSeQAALNAAKEKaLQQLREQLEGERK---EAVATLEKEHS------AELERLCSS---L 1317
Cdd:PRK04778 117 IEEDIEQILEELQELLESEEKN-REEVEQLKDL-YRELRKSLLANRFsfgPALDELEKQLEnleeefSQFVELTESgdyV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1318 EAkhREVVSSLQKKIQEAQQKEE------AQLQKCL-GQVEhrvhqksyhvagyehELSSLLREkrQEVEGEH------E 1384
Cdd:PRK04778 195 EA--REILDQLEEELAALEQIMEeipellKELQTELpDQLQ---------------ELKAGYRE--LVEEGYHldhldiE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1385 RRLDKMKEEHQQVMAkareQYEAEERKQRAELLGHLTGELERLQRAHERELETvRQEQHKRLEDLRRRHREQERKLQDLE 1464
Cdd:PRK04778 256 KEIQDLKEQIDENLA----LLEELDLDEAEEKNEEIQERIDQLYDILEREVKA-RKYVEKNSDTLPDFLEHAKEQNKELK 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1465 LDLETrakdVKARLALLEVQEETARREKQQLLDVQRQVaLKSEEATATHQ---------------QLEEAQKEHTHLLQS 1529
Cdd:PRK04778 331 EEIDR----VKQSYTLNESELESVRQLEKQLESLEKQY-DEITERIAEQEiayselqeeleeilkQLEEIEKEQEKLSEM 405
|
330
....*....|....*
gi 2462523740 1530 NQQLREilDELQARK 1544
Cdd:PRK04778 406 LQGLRK--DELEARE 418
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1364-1522 |
1.14e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1364 YEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAEllghLTGELERLQRAHEreletVRQEQH 1443
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREE----LQREEERLVQKEE-----QLDARA 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462523740 1444 KRLEDLRRRHREQERKLQDLELDLETRAKDVKARlaLLEVQEETARREKQQLLDvQRQVALKSEEATATHQQLEEAQKE 1522
Cdd:PRK12705 98 EKLDNLENQLEEREKALSARELELEELEKQLDNE--LYRVAGLTPEQARKLLLK-LLDAELEEEKAQRVKKIEEEADLE 173
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1259-1345 |
1.18e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 41.03 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1259 EQLKEEIEASEKSEQAALNAaKEKALQQLREQLEGERkeavATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQK 1338
Cdd:smart00935 17 KAAQKQLEKEFKKRQAELEK-LEKELQKLKEKLQKDA----ATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQE 91
|
....*..
gi 2462523740 1339 EEAQLQK 1345
Cdd:smart00935 92 ELQKILD 98
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1424-1596 |
1.22e-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: 42.60 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1424 LERLQRAHER--ELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDV--Q 1499
Cdd:COG1579 9 LLDLQELDSEldRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1500 RQV-ALKSEEATATHQQ--LEEAQKEHTHLLqsnQQLREILDELQARKLKLESQVDLLQAqsqqlqkhfSLEAEAQKKQH 1576
Cdd:COG1579 89 KEYeALQKEIESLKRRIsdLEDEILELMERI---EELEEELAELEAELAELEAELEEKKA---------ELDEELAELEA 156
|
170 180
....*....|....*....|
gi 2462523740 1577 LLREVTVEENNASPHFEPDL 1596
Cdd:COG1579 157 ELEELEAEREELAAKIPPEL 176
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1178-1517 |
1.48e-03 |
|
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: 43.59 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1178 QSLSSLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQ---QKAERASLEQKN 1254
Cdd:pfam07111 59 QALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAAlagAEMVRKNLEEGS 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1255 RQMLEqlkeEIEASEKSEQAALNAAKEKALQQLREQLEGERKeAVATLEKEHSAELERLcsSLEAKHREVvssLQKKIQE 1334
Cdd:pfam07111 139 QRELE----EIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEK-SLNSLETKRAGEAKQL--AEAQKEAEL---LRKQLSK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1335 AQQKEEAQ------LQKCLG-QVEHRVHQKSYHVAGYEH-ELSSLLREKRQEVEGEHE---------RRLDKMKEEHQQV 1397
Cdd:pfam07111 209 TQEELEAQvtlvesLRKYVGeQVPPEVHSQTWELERQELlDTMQHLQEDRADLQATVEllqvrvqslTHMLALQEEELTR 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1398 MAKAREQYEAEERKQRAELLGH-------LTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQ---ERKLQDLELDL 1467
Cdd:pfam07111 289 KIQPSDSLEPEFPKKCRSLLNRwrekvfaLMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQailQRALQDKAAEV 368
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1468 ETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLE 1517
Cdd:pfam07111 369 EVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLE 418
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1038-1478 |
1.49e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.67 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1038 PEWKEAEELGEDSAASLSLQLslQREQAPSPPAACEKGKEQHSQAEE-LGPGQEEAEDPEEKVAVsptppVSPEVrstEP 1116
Cdd:pfam12128 567 PEVWDGSVGGELNLYGVKLDL--KRIDVPEWAASEEELRERLDKAEEaLQSAREKQAAAEEQLVQ-----ANGEL---EK 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1117 VAPPEQLSEAALKAMEEAVAQ---VLEQDQRHLLES-------KQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRER 1186
Cdd:pfam12128 637 ASREETFARTALKNARLDLRRlfdEKQSEKDKKNKAlaerkdsANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEK 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1187 LQKaiEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKL--REELESQQKAERASLEQK------NRQML 1258
Cdd:pfam12128 717 QAY--WQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLgvDPDVIAKLKREIRTLERKieriavRRQEV 794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1259 ---EQLKEEIEASEKSEQAALNAAKEKALQQLREQL---EGERKEAVATLEKEHSAeLERLCSSLEAKHREVVSSLQK-- 1330
Cdd:pfam12128 795 lryFDWYQETWLQRRPRLATQLSNIERAISELQQQLarlIADTKLRRAKLEMERKA-SEKQQVRLSENLRGLRCEMSKla 873
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1331 KIQEAQQKEEAQLQ--KCLGQVEHRVHQKSYHVAGYEHELS---SLLREKRQEVEGEHERRLdkMKEEHQQVMAKAREQY 1405
Cdd:pfam12128 874 TLKEDANSEQAQGSigERLAQLEDLKLKRDYLSESVKKYVEhfkNVIADHSGSGLAETWESL--REEDHYQNDKGIRLLD 951
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462523740 1406 EAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQ---DLELDLEtRAKDVKARL 1478
Cdd:pfam12128 952 YRKLVPYLEQWFDVRVPQSIMVLREQVSILGVDLTEFYDVLADFDRRIASFSRELQrevGEEAFFE-GVSESAVRI 1026
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
1327-1522 |
1.61e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 41.81 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1327 SLQKKIQEAQQK-EEAQL-QKCLGQVEHRvHQKSYH-VAGYEHELSSLLREKRQEVEgeherrldKMKEEHQQVMAKARE 1403
Cdd:pfam15619 15 ELQNELAELQSKlEELRKeNRLLKRLQKR-QEKALGkYEGTESELPQLIARHNEEVR--------VLRERLRRLQEKERD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1404 QyEAEERKQRAELLgHLTGELERLQR-AHERELETvRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLAlle 1482
Cdd:pfam15619 86 L-ERKLKEKEAELL-RLRDQLKRLEKlSEDKNLAE-REELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLA--- 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462523740 1483 vqeetarREKQQLLDVQRQVALKSEEATATHQQLEEAQKE 1522
Cdd:pfam15619 160 -------AEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1222-1543 |
1.62e-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: 43.36 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1222 DQIRAEQEASLQKLREELESQQ--------------KAERASLEQK------NRQMLEQLKEEIEASEKSEQAALNAAKE 1281
Cdd:pfam15964 359 EQLKSELERQKERLEKELASQQekraqekealrkemKKEREELGATmlalsqNVAQLEAQVEKVTREKNSLVSQLEEAQK 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1282 KALQQ----------LREQLEG---ERKEAvatlEKEHSAELERLCSSLEAKHREV------VSSLQKKIQEAQQK---- 1338
Cdd:pfam15964 439 QLASQemdvtkvcgeMRYQLNQtkmKKDEA----EKEHREYRTKTGRQLEIKDQEIeklgleLSESKQRLEQAQQDaara 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1339 --EEAQLQKCLGQVEHRVHqksyhvagyeheLSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAEL 1416
Cdd:pfam15964 515 reECLKLTELLGESEHQLH------------LTRLEKESIQQSFSNEAKAQALQAQQREQELTQKMQQMEAQHDKTVNEQ 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1417 LGHLTGelerlQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLL 1496
Cdd:pfam15964 583 YSLLTS-----QNTFIAKLKEECCTLAKKLEEITQKSRSEVEQLSQEKEYLQDRLEKLQKRNEELEEQCVQHGRMHERMK 657
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2462523740 1497 DVQRQVALKSEeatATHQQLEEAQKEHTHLLQSNQQLREILDELQAR 1543
Cdd:pfam15964 658 QRLRQLDKHCQ---ATAQQLVQLLSKQNQLFKERQNLTEEVQSLRSQ 701
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
1213-1342 |
1.64e-03 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 43.55 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1213 VQSSTQADEDQI-RAEQEASL-----QKLREELESQQKAEraSLEQKNRQMLEQLKEEIEASEKSEQaalnaakEKALQQ 1286
Cdd:PRK00290 494 ITASSGLSDEEIeRMVKDAEAnaeedKKRKELVEARNQAD--SLIYQTEKTLKELGDKVPADEKEKI-------EAAIKE 564
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462523740 1287 LREQLEGERKEAVatleKEHSAELErlcssleakhrEVVSSLQKKIQEAQQKEEAQ 1342
Cdd:PRK00290 565 LKEALKGEDKEAI----KAKTEELT-----------QASQKLGEAMYQQAQAAQGA 605
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
1425-1545 |
1.74e-03 |
|
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.
Pssm-ID: 462259 [Multi-domain] Cd Length: 353 Bit Score: 42.67 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1425 ERLQRAHERELETVRQEQHkrLEDLRRRHREQERKLQDLELDLETRAKDVKA-RLALLEVQEETARREKQQLLDVQRQVA 1503
Cdd:pfam07767 199 ELLQKAVEAEKKRLKEEEK--LERVLEKIAESAATAEAREEKRKTKAQRNKEkRRKEEEREAKEEKALKKKLAQLERLKE 276
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2462523740 1504 LKSEEAtathQQLEEAQKEHTHLLQSNQQLREILDELQARKL 1545
Cdd:pfam07767 277 IAKEIA----EKEKEREEKAEARKREKRKKKKEEKKLRPRKL 314
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1395-1545 |
1.81e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1395 QQVMAKAREQYEAEERKQR-------AELLGHLTgelERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLE--- 1464
Cdd:COG2433 353 ERVEKKVPPDVDRDEVKARvirglsiEEALEELI---EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEaev 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1465 LDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARK 1544
Cdd:COG2433 430 EELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGE 509
|
.
gi 2462523740 1545 L 1545
Cdd:COG2433 510 L 510
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
1282-1526 |
1.83e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 42.63 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1282 KALQQLREQLEGerkeaVATLEkEHSAELERLCSSLEAKHREVVSSLQKkiqeaQQKEEAQLQKCLGQVEHrvhqksyhv 1361
Cdd:pfam09728 1 KAARELMQLLNK-----LDSPE-EKLAALCKKYAELLEEMKRLQKDLKK-----LKKKQDQLQKEKDQLQS--------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1362 agyEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMakareqyeAEERKQRAELLGHLTGELErlqraherELETVRQE 1441
Cdd:pfam09728 61 ---ELSKAILAKSKLEKLCRELQKQNKKLKEESKKLA--------KEEEEKRKELSEKFQSTLK--------DIQDKMEE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1442 QHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLAL--LEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEA 1519
Cdd:pfam09728 122 KSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKTkeLEVQLAEAKLQQATEEEEKKAQEKEVAKARELKAQVQTL 201
|
....*..
gi 2462523740 1520 QKEHTHL 1526
Cdd:pfam09728 202 SETEKEL 208
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1125-1313 |
1.84e-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: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1125 EAALKAMEEAVAQVLEQdqrhlLESKQEKMQQLREKLcqeeeEEILRLHQQKEQSLSSLRERLQkaieeeearmreeesq 1204
Cdd:COG1579 23 EHRLKELPAELAELEDE-----LAALEARLEAAKTEL-----EDLEKEIKRLELEIEEVEARIK---------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1205 rlswlRAQVQSSTQADEDQIRA--EQEASLQKLREELESQQKAERASLEQKNRQmLEQLKEEIEASEK---SEQAALNAA 1279
Cdd:COG1579 77 -----KYEEQLGNVRNNKEYEAlqKEIESLKRRISDLEDEILELMERIEELEEE-LAELEAELAELEAeleEKKAELDEE 150
|
170 180 190
....*....|....*....|....*....|....
gi 2462523740 1280 KEKaLQQLREQLEGERKEAVATLEKEHSAELERL 1313
Cdd:COG1579 151 LAE-LEAELEELEAEREELAAKIPPELLALYERI 183
|
|
| DUF1978 |
pfam09321 |
Domain of unknown function (DUF1978); Members of this family are found in various hypothetical ... |
1373-1550 |
1.92e-03 |
|
Domain of unknown function (DUF1978); Members of this family are found in various hypothetical proteins produced by the bacterium Chlamydia pneumoniae. Their exact function has not, as yet, been identified.
Pssm-ID: 312723 [Multi-domain] Cd Length: 244 Bit Score: 42.22 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1373 REKRQEVEgEHERRLDKMKEEHQQ-VMAKAREQYEAEERKQRAELLGHLTGELER-LQRAHERELETVRQeqhkRLEDLR 1450
Cdd:pfam09321 53 RDALSEIS-RHELWEKKAHLKHLEsLYTQARDRFEKQSSKKNQKELEEAEQEYLSsWEDVKDQEIERVQE----RLQALQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1451 RRH-----REQERKLQD---LELDLETRAKDVKARL-ALLEVQEETARREKQQLLDV-----QRQVALKSEEATATHQQL 1516
Cdd:pfam09321 128 ALYpevsvSEEETEGQEtvtPTVDLETALGRIEESYrECVRDQEDYWKEEESKEVEMsaefrEEGGKKKSEEFQEQLGSL 207
|
170 180 190
....*....|....*....|....*....|....
gi 2462523740 1517 EEAQKEHThllqsnqqlrEILDELQARKLKLESQ 1550
Cdd:pfam09321 208 ERFLKEHS----------EELEVLEKHILKHESE 231
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1248-1341 |
1.96e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1248 ASLEQKNRQmLEQLKEEIEASEKsEQAALNAAKEKALQQLREQLEGERKEAVA--TLEKEHSAELERLCSSLEAKHrEVV 1325
Cdd:COG0542 411 EELDELERR-LEQLEIEKEALKK-EQDEASFERLAELRDELAELEEELEALKArwEAEKELIEEIQELKEELEQRY-GKI 487
|
90
....*....|....*.
gi 2462523740 1326 SSLQKKIQEAQQKEEA 1341
Cdd:COG0542 488 PELEKELAELEEELAE 503
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1225-1552 |
2.11e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1225 RAEQEASLQKL--REELESQQKAERASLEQ---------KNRQMLEQLKEEIEASE---KSEQAALNAAKEKALQQLREQ 1290
Cdd:PRK11281 38 EADVQAQLDALnkQKLLEAEDKLVQQDLEQtlalldkidRQKEETEQLKQQLAQAPaklRQAQAELEALKDDNDEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1291 LEgerKEAVATLEK---EHSAELERLCSSLEAKHREVVSS------LQKKIQEAQQkeeaQLQkclgqvehrvhqksyhv 1361
Cdd:PRK11281 118 LS---TLSLRQLESrlaQTLDQLQNAQNDLAEYNSQLVSLqtqperAQAALYANSQ----RLQ----------------- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1362 agyehELSSLLreKRQEVEGEHERRLDKMKEEHQQVMAKAREQYeaeerkQRAELLGH--LTgELERLQraheRELETVR 1439
Cdd:PRK11281 174 -----QIRNLL--KGGKVGGKALRPSQRVLLQAEQALLNAQNDL------QRKSLEGNtqLQ-DLLQKQ----RDYLTAR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1440 QEQhkrledlrrrhreQERKLQDL-ELDLETRAKDVKARLALLEVQEETARREKQQLldvqrqVALKSEEATATHQQLEE 1518
Cdd:PRK11281 236 IQR-------------LEHQLQLLqEAINSKRLTLSEKTVQEAQSQDEAARIQANPL------VAQELEINLQLSQRLLK 296
|
330 340 350
....*....|....*....|....*....|....
gi 2462523740 1519 AQKEHTHLLQSNQQLREILDELQARKLKLESQVD 1552
Cdd:PRK11281 297 ATEKLNTLTQQNLRVKNWLDRLTQSERNIKEQIS 330
|
|
| PRK11091 |
PRK11091 |
aerobic respiration control sensor protein ArcB; Provisional |
1433-1506 |
2.13e-03 |
|
aerobic respiration control sensor protein ArcB; Provisional
Pssm-ID: 236842 [Multi-domain] Cd Length: 779 Bit Score: 43.01 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1433 RELETVRQEQHK---RLEDLRRRHREQERKLQD----LELDLETRAKDVKARLALL-EVQEETARREKQQLLDVQRQVAL 1504
Cdd:PRK11091 78 EQLEESRQRLSRlvaKLEEMRERDLELNVQLKDniaqLNQEIAEREKAEEARQEAFeQLKNEIKEREETQIELEQQSSLL 157
|
..
gi 2462523740 1505 KS 1506
Cdd:PRK11091 158 RS 159
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1368-1541 |
2.30e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.81 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1368 LSSLLREKRQEvEGEHERRLDKMKEEhqqvmAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVR--QEQHKR 1445
Cdd:pfam05557 11 LSQLQNEKKQM-ELEHKRARIELEKK-----ASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElnRLKKKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1446 LEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTH 1525
Cdd:pfam05557 85 LEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSS 164
|
170
....*....|....*.
gi 2462523740 1526 LLQSNQQLREILDELQ 1541
Cdd:pfam05557 165 LAEAEQRIKELEFEIQ 180
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
974-1292 |
2.33e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 974 RQAQQPLGIEDKDDSQSSQDELQSKQSKGLEERLSpplpHEERAQSPPRSLATEEEPPQGPEGQ--PEWKEAEELGEDSA 1051
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEAD----YEGFLEGVKAALLLAGLRGLAGAVAvlIGVEAAYEAALEAA 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1052 ASLSLQLsLQREQAPSPPAACEKGKEQHSQAEELGPgqeeaeDPEEKVAVSPTPPVSPEVRSTEPVAPPEQLSEAALKAM 1131
Cdd:COG1196 544 LAAALQN-IVVEDDEVAAAAIEYLKAAKAGRATFLP------LDKIRARAALAAALARGAIGAAVDLVASDLREADARYY 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1132 EEAVAQVLEQDQRHLLESKQEKMQQLREKLcqeEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLRA 1211
Cdd:COG1196 617 VLGDTLLGRTLVAARLEAALRRAVTLAGRL---REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1212 QVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALN---AAKEKALQQLR 1288
Cdd:COG1196 694 ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPpdlEELERELERLE 773
|
....
gi 2462523740 1289 EQLE 1292
Cdd:COG1196 774 REIE 777
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1236-1541 |
2.37e-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: 43.24 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1236 REELESQQKAERASLEQKNRQMLEQLKEEIEasekSEQAALNAAKekalQQLREQLEGerkeavatlEKEHSAELERLCS 1315
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELE----KKHQQLCEEK----NALQEQLQA---------ETELCAEAEEMRA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1316 SLEAKHREVVSSLQKkiQEAQQKEEAQLQKCLGQVEHRVHQksyHVAGYEHELSS--LLREKRQEVEGEHERRLDKMkEE 1393
Cdd:pfam01576 65 RLAARKQELEEILHE--LESRLEEEEERSQQLQNEKKKMQQ---HIQDLEEQLDEeeAARQKLQLEKVTTEAKIKKL-EE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1394 HQQVMAKAREQYEaEERKQRAELLGHLTGELERlQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLEldletrakd 1473
Cdd:pfam01576 139 DILLLEDQNSKLS-KERKLLEERISEFTSNLAE-EEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELE--------- 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462523740 1474 vKARLAL----LEVQEETARReKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQ 1541
Cdd:pfam01576 208 -KAKRKLegesTDLQEQIAEL-QAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQ 277
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1424-1587 |
2.38e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1424 LERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLE-----LDLETRAKDVKARLALLEVQEETARRE------- 1491
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRqknglVDLSEEAKLLLQQLSELESQLAEARAElaeaear 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1492 ---------------------------KQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQS-NQQLREILDELQAR 1543
Cdd:COG3206 242 laalraqlgsgpdalpellqspviqqlRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILASLEAE 321
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462523740 1544 KLKLESQVDLLQAQSQQLQKHFSLEAEAQKKQH-LLREVTVEENN 1587
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAELPELEAELRrLEREVEVAREL 366
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1233-1338 |
2.38e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 40.25 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1233 QKLREELESQQKAERASLEQKNRQmLEQLKEEIEAsEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKehsaeler 1312
Cdd:pfam03938 18 KAAQAQLEKKFKKRQAELEAKQKE-LQKLYEELQK-DGALLEEEREEKEQELQKKEQELQQLQQKAQQELQK-------- 87
|
90 100
....*....|....*....|....*.
gi 2462523740 1313 lcssleaKHREVVSSLQKKIQEAQQK 1338
Cdd:pfam03938 88 -------KQQELLQPIQDKINKAIKE 106
|
|
| PRK14971 |
PRK14971 |
DNA polymerase III subunit gamma/tau; |
985-1239 |
2.49e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237874 [Multi-domain] Cd Length: 614 Bit Score: 42.84 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 985 KDDSQSSQDELQSKQSKGLEERLSPPLPHEERAQSP-PRSLATEEEPPQGPEGQPEWKEAEELGEDSAASLSLQLSLQRE 1063
Cdd:PRK14971 365 KGDDASGGRGPKQHIKPVFTQPAAAPQPSAAAAASPsPSQSSAAAQPSAPQSATQPAGTPPTVSVDPPAAVPVNPPSTAP 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1064 QAPSPPAACEKGKEQHSQAEELGPG-----QEEAEDPEEKVAVSPTPPvspevrstepvaPPEQLSEAALKAMEEAVAQV 1138
Cdd:PRK14971 445 QAVRPAQFKEEKKIPVSKVSSLGPStlrpiQEKAEQATGNIKEAPTGT------------QKEIFTEEDLQYYWQEFAGT 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1139 LEQDQRHLleskQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQ 1218
Cdd:PRK14971 513 RPQEEKAL----KETMINCRPKLLNGTTFEVAVDNELQEKELTNLIPDLLGFLRGRLKNSKITMTVRVSEPTEVNRAYSS 588
|
250 260
....*....|....*....|.
gi 2462523740 1219 ADEDQIRAEQEASLQKLREEL 1239
Cdd:PRK14971 589 VEKFQYLAQKNPALLELREEL 609
|
|
| PLC-beta_C |
pfam08703 |
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ... |
1223-1382 |
2.78e-03 |
|
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of phospholipase C beta.
Pssm-ID: 462571 [Multi-domain] Cd Length: 176 Bit Score: 40.82 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1223 QIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVATL 1302
Cdd:pfam08703 2 QVRELKERLEQELLELREEQYEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1303 EK--EHSAELERLCSSLEAKH-REVVSS---LQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHV-AGYEHELSSLLREK 1375
Cdd:pfam08703 82 KKrtSDKAAQERLKKEINNSHiQEVVQSikqLEEKQKRRQEKLEEKQAECLQQIKEEEPQLQAELnAEYEEKLKGLPAEV 161
|
....*..
gi 2462523740 1376 RQEVEGE 1382
Cdd:pfam08703 162 RESVKSC 168
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1278-1453 |
2.79e-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: 41.45 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1278 AAKEKALQQLREQLeGERKEAVATLEKEHsAELERLCSSLEAKHREV---VSSLQKKIQEAQQKEEaQLQKCLGQVehrv 1354
Cdd:COG1579 13 QELDSELDRLEHRL-KELPAELAELEDEL-AALEARLEAAKTELEDLekeIKRLELEIEEVEARIK-KYEEQLGNV---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1355 hQKSYHVAGYEHELSSLlrEKRQEVEGEHERRLDKMKEEHQQVMAKAREQYE------AEERKQRAELLGHLTGELERLQ 1428
Cdd:COG1579 86 -RNNKEYEALQKEIESL--KRRISDLEDEILELMERIEELEEELAELEAELAeleaelEEKKAELDEELAELEAELEELE 162
|
170 180
....*....|....*....|....*
gi 2462523740 1429 RAHERELETVRQEQHKRLEDLRRRH 1453
Cdd:COG1579 163 AEREELAAKIPPELLALYERIRKRK 187
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1369-1489 |
3.10e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1369 SSLLREKRQEVEgeherRLDKMKEEHQQvmAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQE-QHKRLE 1447
Cdd:PRK11448 141 ENLLHALQQEVL-----TLKQQLELQAR--EKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKaAETSQE 213
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2462523740 1448 DLRRRHREQERKLQDLELD-LETRAK-DVKARLALLEVQEETAR 1489
Cdd:PRK11448 214 RKQKRKEITDQAAKRLELSeEETRILiDQQLRKAGWEADSKTLR 257
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
1214-1441 |
3.38e-03 |
|
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.
Pssm-ID: 464723 [Multi-domain] Cd Length: 526 Bit Score: 42.13 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1214 QSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKE------EIEASEKSEQAALN---AAKEKAl 1284
Cdd:pfam15450 213 ESTRLKAESSLREELEGRWQKLQELTEERLRALQGQREQEEGHLLEQCRGldaavvQLTKFVRQNQVSLNrvlLAEQKA- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1285 QQLREQLEGERKEAVATLEKEhsaELERLCSSLEAKHREVVSSLQKKIQEAQQKEE--AQLQKCLGQVEHRVHQKSYHVA 1362
Cdd:pfam15450 292 RDAKGQLEESQAGELASYVQE---NLEAVQLAGELAQQETQGALELLQEKSQVLEGsvAELVRQVKDLSDHFLALSWRLD 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1363 GYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRA------ELLGHLTGELERLQ---RAHER 1433
Cdd:pfam15450 369 LQEQTLGLKLSEAKKEWEGAERKSLEDLAQWQKEVAAHLREVQEKVDSLPRQieavsdKCVLHKSDSDLKISaegKAREF 448
|
....*...
gi 2462523740 1434 ELETVRQE 1441
Cdd:pfam15450 449 EVEAMRQE 456
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1222-1290 |
3.39e-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: 39.73 E-value: 3.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1222 DQIRAEQEASLQKLREELESQ-QKAERASLEQKNrQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQ 1290
Cdd:cd06503 50 EELLAEYEEKLAEARAEAQEIiEEARKEAEKIKE-EILAEAKEEAERILEQAKAEIEQEKEKALAELRKE 118
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1125-1473 |
3.41e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1125 EAALKAMEEAVAQVleQDQRHLLESKQEKMQQLREKLCQEEEEEilrlhQQKEQSLSSLRERLQKAieeeearmreeeSQ 1204
Cdd:COG4372 34 RKALFELDKLQEEL--EQLREELEQAREELEQLEEELEQARSEL-----EQLEEELEELNEQLQAA------------QA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1205 RLSWLRAQVQSsTQADEDQIRAEQEAsLQKLREELESQQKAERASLEQKNRQM-------------LEQLKEEIEASEKS 1271
Cdd:COG4372 95 ELAQAQEELES-LQEEAEELQEELEE-LQKERQDLEQQRKQLEAQIAELQSEIaereeelkeleeqLESLQEELAALEQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1272 EQAALNAAKEKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVE 1351
Cdd:COG4372 173 LQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1352 HRVHQKSYHVAGYEhelssLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAH 1431
Cdd:COG4372 253 EEVILKEIEELELA-----ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2462523740 1432 ERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKD 1473
Cdd:COG4372 328 LELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1279-1548 |
3.49e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1279 AKEKALQQLREQLEGERKEAvatleKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEaQLQKCLGQV-EHRVHQK 1357
Cdd:COG1340 8 SSLEELEEKIEELREEIEEL-----KEKRDELNEELKELAEKRDELNAQVKELREEAQELRE-KRDELNEKVkELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1358 syhvagyehELSSLLREKRQEVEgEHERRLDKMKEEHQQVmAKAREQYEAEERKQraellghltgELERLQRAHERELET 1437
Cdd:COG1340 82 ---------ELNEKLNELREELD-ELRKELAELNKAGGSI-DKLRKEIERLEWRQ----------QTEVLSPEEEKELVE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1438 VRQEQHKRLEDLRRRHrEQERKLQdlELDLETRAKDVKARLALLEVQE--ETARREKQQLLDVQRQVALKSEEATATHQQ 1515
Cdd:COG1340 141 KIKELEKELEKAKKAL-EKNEKLK--ELRAELKELRKEAEEIHKKIKElaEEAQELHEEMIELYKEADELRKEADELHKE 217
|
250 260 270
....*....|....*....|....*....|....*..
gi 2462523740 1516 LEEAQKE----HTHLLQSNQQLREILDELQARKLKLE 1548
Cdd:COG1340 218 IVEAQEKadelHEEIIELQKELRELRKELKKLRKKQR 254
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1424-1543 |
3.90e-03 |
|
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: 40.82 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1424 LERLQRAHERELETVRQEqhkrLEDLRRRHREQERKLQDLELDLETRAKdvKARLALLEVQEETARREKQQLLDVQRQVA 1503
Cdd:pfam04012 27 LEQAIRDMQSELVKARQA----LAQTIARQKQLERRLEQQTEQAKKLEE--KAQAALTKGNEELAREALAEKKSLEKQAE 100
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2462523740 1504 LKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQAR 1543
Cdd:pfam04012 101 ALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKAR 140
|
|
| PRK02292 |
PRK02292 |
V-type ATP synthase subunit E; Provisional |
1213-1350 |
4.05e-03 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 235026 [Multi-domain] Cd Length: 188 Bit Score: 40.37 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1213 VQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSE--QAALNAAKEkALQQLREQ 1290
Cdd:PRK02292 10 IRDEARARASEIRAEADEEAEEIIAEAEADAEEILEDREAEAEREIEQLREQELSSAKLEakRERLNARKE-VLEDVRNQ 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462523740 1291 LEgerkEAVATLEKEHSAELER-LCSSLEAKHREVVSS------LQKKIQEAQQKEEAQLQKCLGQV 1350
Cdd:PRK02292 89 VE----DEIASLDGDKREELTKsLLDAADADGVRVYSRkddedlVKSLLSDYDGLEYAGNIDCLGGV 151
|
|
| 4HB_MCP_1 |
pfam12729 |
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ... |
1220-1304 |
4.29e-03 |
|
Four helix bundle sensory module for signal transduction; This family is a four helix bundle that operates as a ubiquitous sensory module in prokaryotic signal-transduction. The 4HB_MCP is always found between two predicted transmembrane helices indicating that it detects only extracellular signals. In many cases the domain is associated with a cytoplasmic HAMP domain suggesting that most proteins carrying the bundle might share the mechanism of transmembrane signalling which is well-characterized in E coli chemoreceptors. This domain recognizes citrate and TCA cycle intermediates, cis-aconitate, boric acid, Phenanthrene, pyrene and benzopyrene (Matilla et el., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 432749 [Multi-domain] Cd Length: 181 Bit Score: 40.31 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1220 DEDQiRAEQEASLQKLREELESQQKA-ERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAK----EKALQQLREQLEGE 1294
Cdd:pfam12729 73 DPAE-RDELLKDIEELRAEIDKLLEKyEKTILTDEEKKLFAEFKENLNAYRAVRNKVLELAKagnkDEAYQLYKTEGRPA 151
|
90
....*....|
gi 2462523740 1295 RKEAVATLEK 1304
Cdd:pfam12729 152 REAMIEALEE 161
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1218-1344 |
5.23e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 41.25 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1218 QADEDQIRAEQeASLQKLREELesQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEkALQQLREQLEGERKE 1297
Cdd:pfam00529 57 QAALDSAEAQL-AKAQAQVARL--QAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQA-QLAQAQIDLARRRVL 132
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2462523740 1298 AVATL-EKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQ 1344
Cdd:pfam00529 133 APIGGiSRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQA 180
|
|
| PRK13895 |
PRK13895 |
conjugal transfer protein TraM; Provisional |
1252-1322 |
5.32e-03 |
|
conjugal transfer protein TraM; Provisional
Pssm-ID: 184378 Cd Length: 144 Bit Score: 39.27 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1252 QKNRQ-MLEQLKEEIE---------ASEKSEQ---AALNAAKEKALQQLREQLegerKEAVATLEKEHSAELERLCSSLE 1318
Cdd:PRK13895 41 AKAQQeMLDQFKEELEsiasrwgddAKEKAERilnAALAASKEAMAKGMQEGA----KAAAEAVRREISASLAELAAPVR 116
|
....
gi 2462523740 1319 AKHR 1322
Cdd:PRK13895 117 EARR 120
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
1209-1355 |
5.71e-03 |
|
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. It seems that Mps2-Spc24 interaction may contribute to the localization of Spc24 and other kinetochore components to the inner plaque of the SPB.
Pssm-ID: 407228 [Multi-domain] Cd Length: 340 Bit Score: 41.11 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1209 LRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQM-LEQLKEEIEASEKseqaaLNAAKEKALQQL 1287
Cdd:pfam17060 106 LKEDVKSSPRSEADSLGTPIKVDLLRNLKPQESPETPRRINRKYKSLELrVESMKDELEFKDE-----TIMEKDRELTEL 180
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462523740 1288 REQLeGERKEAVATLEKEHS-----AELERLCSSLEA-KHREVVSSLQKKIQEaQQKEEAQLQKCLGQVEHRVH 1355
Cdd:pfam17060 181 TSTI-SKLKDKYDFLSREFEfykqhHEHGGNNSIKTAtKHEFIISELKRKLQE-QNRLIRILQEQIQFDPGALH 252
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1385-1528 |
5.71e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.62 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1385 RRLDKMKEEHQQVMAKAREqyeaEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQER---KLQ 1461
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQK----EAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDAraeKLD 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462523740 1462 DLELDLETRAKDVKARLALLEVQEETARREKQQLL----DVQRQVALKSEEATATHQ--QLEEAQKEHTHLLQ 1528
Cdd:PRK12705 102 NLENQLEEREKALSARELELEELEKQLDNELYRVAgltpEQARKLLLKLLDAELEEEkaQRVKKIEEEADLEA 174
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1207-1306 |
6.26e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.10 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1207 SWLRAQVQSSTQADEDQIRAE---QEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKA 1283
Cdd:smart00935 13 SPAGKAAQKQLEKEFKKRQAElekLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEE 92
|
90 100
....*....|....*....|...
gi 2462523740 1284 LQQLREQLegerKEAVATLEKEH 1306
Cdd:smart00935 93 LQKILDKI----NKAIKEVAKKK 111
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1115-1397 |
6.48e-03 |
|
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: 41.57 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1115 EPVAPPEQLSEAALKAMeeavaQVLEQDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLR------ERLQ 1188
Cdd:TIGR00606 775 GTIMPEEESAKVCLTDV-----TIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDtvvskiELNR 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1189 KAIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREEL--ESQQKAERASLEQKNRQMLEQLKEEI- 1265
Cdd:TIGR00606 850 KLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLirEIKDAKEQDSPLETFLEKDQQEKEELi 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1266 ---EASEKSEQAALNAAKEKALQQL--REQLEGERKEAVATLEKEHSAELERLCSSLEAKHREvvsslQKKIQEAQQKEE 1340
Cdd:TIGR00606 930 sskETSNKKAQDKVNDIKEKVKNIHgyMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKH-----QEKINEDMRLMR 1004
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462523740 1341 AQLQKclGQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQV 1397
Cdd:TIGR00606 1005 QDIDT--QKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKL 1059
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1220-1304 |
6.78e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.82 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1220 DEDQIRAEQEasLQKLREELESQQKAERASLEQKnrqmLEQLKEEIEASEKSEQAA------LNAAKeKALQQLREQLEg 1293
Cdd:cd22656 171 DEGGAIARKE--IKDLQKELEKLNEEYAAKLKAK----IDELKALIADDEAKLAAAlrliadLTAAD-TDLDNLLALIG- 242
|
90
....*....|.
gi 2462523740 1294 erkEAVATLEK 1304
Cdd:cd22656 243 ---PAIPALEK 250
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1229-1543 |
6.81e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1229 EASLQKLREELESQQkaerasLEQKNRQMLEQLKEEI-------------EASEKSEQAAlnaAKEKALQQLREQLEGER 1295
Cdd:PRK04863 236 EAALRENRMTLEAIR------VTQSDRDLFKHLITEStnyvaadymrhanERRVHLEEAL---ELRRELYTSRRQLAAEQ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1296 KEAVATLEKEhsAELERLCSSLEAKHREVVSSLQKkIQEAQQKEEaQLQKCLGQVEhrvhqksyhvagyehelssllrek 1375
Cdd:PRK04863 307 YRLVEMAREL--AELNEAESDLEQDYQAASDHLNL-VQTALRQQE-KIERYQADLE------------------------ 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1376 rqevegEHERRLdkmkEEHQQVMAKAREQY-EAEERKQRAEL-LGHLTGELERLQRAHEreletvrqEQHKRLEDLR--- 1450
Cdd:PRK04863 359 ------ELEERL----EEQNEVVEEADEQQeENEARAEAAEEeVDELKSQLADYQQALD--------VQQTRAIQYQqav 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1451 RRHREQERKLQDLELDLEtrakDVKARLALLEVQEETA---RREKQQLLDV------QRQVALKS----------EEATA 1511
Cdd:PRK04863 421 QALERAKQLCGLPDLTAD----NAEDWLEEFQAKEQEAteeLLSLEQKLSVaqaahsQFEQAYQLvrkiagevsrSEAWD 496
|
330 340 350
....*....|....*....|....*....|..
gi 2462523740 1512 THQQLEEAQKEHTHLLQSNQQLREILDELQAR 1543
Cdd:PRK04863 497 VARELLRRLREQRHLAEQLQQLRMRLSELEQR 528
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1284-1478 |
6.97e-03 |
|
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: 39.55 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1284 LQQLREQLEGERKEAVATLEKEhsaeLERLCSSLEAKHREVVSSLQKKIQEAQQKeeaqlqkcLGQvehrvhqksyHVAG 1363
Cdd:pfam01442 13 AEELQEQLGPVAQELVDRLEKE----TEALRERLQKDLEEVRAKLEPYLEELQAK--------LGQ----------NVEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1364 YEHELSSLLREKRQEVEgeheRRLDKMKEEHQQVMAKAREQYEAEERKQRAellgHLTGELERLQRAHERELETVRQEQH 1443
Cdd:pfam01442 71 LRQRLEPYTEELRKRLN----ADAEELQEKLAPYGEELRERLEQNVDALRA----RLAPYAEELRQKLAERLEELKESLA 142
|
170 180 190
....*....|....*....|....*....|....*
gi 2462523740 1444 KRLEDLRRRHREQerkLQDLELDLETRAKDVKARL 1478
Cdd:pfam01442 143 PYAEEVQAQLSQR---LQELREKLEPQAEDLREKL 174
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
1211-1585 |
7.04e-03 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 41.33 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1211 AQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQ 1290
Cdd:COG2203 338 DQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLA 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1291 LEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSS 1370
Cdd:COG2203 418 LEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLAL 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1371 LLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLR 1450
Cdd:COG2203 498 LALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSVLLI 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1451 RRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSN 1530
Cdd:COG2203 578 ELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALALASLVLLR 657
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2462523740 1531 QQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSLEAEAQKKQHLLREVTVEE 1585
Cdd:COG2203 658 ALLATELDLILDSSLLLGLLLLGALLLLGGGLALLLSIGLGLGVARLLQLSVLEV 712
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
1209-1292 |
7.09e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 39.55 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1209 LRAQVQSSTQADEDQIRAEQEAslQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQA---------ALNAA 1279
Cdd:PRK07352 66 LRQAAQALAEAQQKLAQAQQEA--ERIRADAKARAEAIRAEIEKQAIEDMARLKQTAAADLSAEQErviaqlrreAAELA 143
|
90
....*....|...
gi 2462523740 1280 KEKALQQLREQLE 1292
Cdd:PRK07352 144 IAKAESQLPGRLD 156
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
1365-1496 |
7.22e-03 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 39.26 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1365 EHELSSLLREKRQEVEGEHERRLDKMKEE-HQQVMAKAREQYEAEERKQRAEllghltgelERLQRAHERELETVRQEQH 1443
Cdd:pfam15346 21 AKRVEEELEKRKDEIEAEVERRVEEARKImEKQVLEELEREREAELEEERRK---------EEEERKKREELERILEENN 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2462523740 1444 KRLEDLRRRHREQERKlqdlELDLETRAKDVKARLAllEVQEETARREKQQLL 1496
Cdd:pfam15346 92 RKIEEAQRKEAEERLA----MLEEQRRMKEERQRRE--KEEEEREKREQQKIL 138
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1203-1527 |
7.41e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.35 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1203 SQRLSWLRAQVQSSTQAdedQIRAEQEASLQKLREEL-ESQQKAE-------------RASLEQKNRQMLEQLKEEIEAS 1268
Cdd:NF041483 103 TQRILQEHAEHQARLQA---ELHTEAVQRRQQLDQELaERRQTVEshvnenvawaeqlRARTESQARRLLDESRAEAEQA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1269 EKSEQAALNAAKEKALQQLREQLEGERKEAVATLEK-----------------EHSAELERLCSSL-----EAKHR--EV 1324
Cdd:NF041483 180 LAAARAEAERLAEEARQRLGSEAESARAEAEAILRRarkdaerllnaastqaqEATDHAEQLRSSTaaesdQARRQaaEL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1325 VSSLQKKIQEAQQK---EEAQLQKCLGQVEHRVHQKsyhVAGYEHELSSLLREKRQEVE---GEHERRLDKMKEEHQQVM 1398
Cdd:NF041483 260 SRAAEQRMQEAEEAlreARAEAEKVVAEAKEAAAKQ---LASAESANEQRTRTAKEEIArlvGEATKEAEALKAEAEQAL 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1399 AKAREQYE-----AEERKQRA-----------------ELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQ 1456
Cdd:NF041483 337 ADARAEAEklvaeAAEKARTVaaedtaaqlakaartaeEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQ 416
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462523740 1457 ERKLQDLELD--LETRAKDVkarlallEVQEEtARR---EKQQLLD--VQRQVALKSEEATATHQQLEEAQKEHTHLL 1527
Cdd:NF041483 417 AEQLKGAAKDdtKEYRAKTV-------ELQEE-ARRlrgEAEQLRAeaVAEGERIRGEARREAVQQIEEAARTAEELL 486
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
1394-1527 |
7.64e-03 |
|
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: 38.70 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1394 HQQVMAKAREQYEAEerkqRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHR-EQERKLQDLELDLETRAK 1472
Cdd:pfam12474 1 HQLQKEQQKDRFEQE----RQQLKKRYEKELEQLERQQKQQIEKLEQRQTQELRRLPKRIRaEQKKRLKMFRESLKQEKK 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462523740 1473 DVKA---RLALLEVQEET-ARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLL 1527
Cdd:pfam12474 77 ELKQeveKLPKFQRKEAKrQRKEELELEQKHEELEFLQAQSEALERELQQLQNEKRKEL 135
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
1228-1511 |
7.74e-03 |
|
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.
Pssm-ID: 464723 [Multi-domain] Cd Length: 526 Bit Score: 40.97 E-value: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1228 QEASLQKLREELE-----SQQKAERASLEQKNRQMLEQL-KEEIEASEKSEQAALNAAkEKALQQLREQL-EGERKEAVA 1300
Cdd:pfam15450 40 EHATLSLLRELLQvrahvQLQDSELKQLRQEVQQAARAPeKEALEFPGPQNQNQMQAL-DKRLVEVREALtQIRRKQALQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1301 TLEKEHSAE-----LERLCSSL--EAKHREVV-SSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSLL 1372
Cdd:pfam15450 119 DSERKGAEQeanlrLTKLTGKLkqEEQGREAAcSALQKSQEEASQKVDHEVARMQAQVTKLGEEMSLRFLKREAKLCSFL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1373 R------EKRQEVEG----EHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQ 1442
Cdd:pfam15450 199 QksflalEKRMKASEstrlKAESSLREELEGRWQKLQELTEERLRALQGQREQEEGHLLEQCRGLDAAVVQLTKFVRQNQ 278
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462523740 1443 HKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATA 1511
Cdd:pfam15450 279 VSLNRVLLAEQKARDAKGQLEESQAGELASYVQENLEAVQLAGELAQQETQGALELLQEKSQVLEGSVA 347
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1237-1417 |
7.88e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1237 EELESQQKaeraSLEQKNRQmLEQLKEEIEAsekseqaalnaaKEKALQQLREQLEGERKEAVATLEKEhsaelerlcss 1316
Cdd:PRK00409 523 ASLEELER----ELEQKAEE-AEALLKEAEK------------LKEELEEKKEKLQEEEDKLLEEAEKE----------- 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1317 leakhrevvssLQKKIQEAqQKEEAQLQKCLgqvehRVHQKSYHVAGYEHELSsllrEKRQEVEGEHErrldkMKEEHQQ 1396
Cdd:PRK00409 575 -----------AQQAIKEA-KKEADEIIKEL-----RQLQKGGYASVKAHELI----EARKRLNKANE-----KKEKKKK 628
|
170 180
....*....|....*....|....*..
gi 2462523740 1397 VMAKAREQYEAEER------KQRAELL 1417
Cdd:PRK00409 629 KQKEKQEELKVGDEvkylslGQKGEVL 655
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1250-1445 |
8.56e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 41.16 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1250 LEQKNRQMLEQ-LKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKEHSAELErlcssLEAKHREVVSSL 1328
Cdd:PTZ00491 641 VDERTRDSLQKsVQLAIEITTKSQEAAARHQAELLEQEARGRLERQKMHDKAKAEEQRTKLLE-----LQAESAAVESSG 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1329 QKKiQEAQQKEEAQLQKClgqvehrvhQKSYHVAGyehelsslLREKRQEVEGEHErrLDKMKEEHQQvmakareqyEAE 1408
Cdd:PTZ00491 716 QSR-AEALAEAEARLIEA---------EAEVEQAE--------LRAKALRIEAEAE--LEKLRKRQEL---------ELE 766
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462523740 1409 ERKQRAELlghltgELERlqrahERELETVRQEQHKR 1445
Cdd:PTZ00491 767 YEQAQNEL------EIAK-----AKELADIEATKFER 792
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1141-1551 |
8.70e-03 |
|
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: 41.19 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1141 QDQRHLLESKQEKMQQLREKLC--QEEEEEILRLHQQKEQSLSSLRERLQ----------------KAIEEEEARMREEE 1202
Cdd:TIGR00606 206 QMELKYLKQYKEKACEIRDQITskEAQLESSREIVKSYENELDPLKNRLKeiehnlskimkldneiKALKSRKKQMEKDN 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1203 SQrLSWLRAQVQSSTQADEDQI-RAEQEASLQKLREELESQQKAERASleqKNRQMLEQLKEEIEASEKSEQAALNAAKE 1281
Cdd:TIGR00606 286 SE-LELKMEKVFQGTDEQLNDLyHNHQRTVREKERELVDCQRELEKLN---KERRLLNQEKTELLVEQGRLQLQADRHQE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1282 KALQ--------QLREQLEGERKEAVATLEKEHSAELERLCSSLEAKH-REVVSSLQKKIQEAqQKEEAQLQKCLGQVEH 1352
Cdd:TIGR00606 362 HIRArdsliqslATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTaAQLCADLQSKERLK-QEQADEIRDEKKGLGR 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1353 RVHQKSYHVAGYEHELSSLLREKrQEVEGEHERRLDKMKE--EHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRA 1430
Cdd:TIGR00606 441 TIELKKEILEKKQEELKFVIKEL-QQLEGSSDRILELDQElrKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRK 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1431 HERELETVRQEQHKrledlrrrhREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQvalKSEEAT 1510
Cdd:TIGR00606 520 LDQEMEQLNHHTTT---------RTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHS---KSKEIN 587
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2462523740 1511 ATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQV 1551
Cdd:TIGR00606 588 QTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKL 628
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1397-1551 |
9.05e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.85 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1397 VMAKAREQY--EAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEdlRRRHREQERKLQDLELDLETRAKDV 1474
Cdd:PRK12705 23 VLLKKRQRLakEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRE--REELQREEERLVQKEEQLDARAEKL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462523740 1475 KARLALLEVQEETARREKQQLLDVQRQVALKSEEATAthqqleeaqkehthlLQSNQQLREILDELQArKLKLESQV 1551
Cdd:PRK12705 101 DNLENQLEEREKALSARELELEELEKQLDNELYRVAG---------------LTPEQARKLLLKLLDA-ELEEEKAQ 161
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1216-1349 |
9.16e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 41.16 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1216 STQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKE--EIEASEKSEQAALNAAK------EKALQQL 1287
Cdd:PTZ00491 660 TTKSQEAAARHQAELLEQEARGRLERQKMHDKAKAEEQRTKLLELQAEsaAVESSGQSRAEALAEAEarlieaEAEVEQA 739
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462523740 1288 REQLEGERKEAVATLEKEHsAELErlcssLEAKHREVVSSL----QKKIQEAQQKEEAQLQKCLGQ 1349
Cdd:PTZ00491 740 ELRAKALRIEAEAELEKLR-KRQE-----LELEYEQAQNELeiakAKELADIEATKFERIVEALGR 799
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1432-1550 |
9.43e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.81 E-value: 9.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1432 ERELETVRQE------QHKRLEDLRRRHREQERKLQDleldletrakdvKARLALLEVQEETARR--EKQQLLDvqrqva 1503
Cdd:COG1842 36 EEDLVEARQAlaqviaNQKRLERQLEELEAEAEKWEE------------KARLALEKGREDLAREalERKAELE------ 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2462523740 1504 lksEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQ 1550
Cdd:COG1842 98 ---AQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKAR 141
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1214-1415 |
9.46e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 40.78 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1214 QSSTQADEDQIRAEQ-EASLQKLREELEsQQKAERASLEQKnrqmLEQLKEEIEASEKSEQAALNAAkeKALQQLREQLE 1292
Cdd:pfam05701 388 QAAQEAEEAKSLAQAaREELRKAKEEAE-QAKAAASTVESR----LEAVLKEIEAAKASEKLALAAI--KALQESESSAE 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1293 GERKEAVA---TLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQqkeeaqlqkclgqvehrvhqksyhvagyEHELS 1369
Cdd:pfam05701 461 STNQEDSPrgvTLSLEEYYELSKRAHEAEELANKRVAEAVSQIEEAK----------------------------ESELR 512
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2462523740 1370 SLlrEKRQEVEGEHERRLDKMKEEHQQVmAKARE---QYEAEERKQRAE 1415
Cdd:pfam05701 513 SL--EKLEEVNREMEERKEALKIALEKA-EKAKEgklAAEQELRKWRAE 558
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1218-1334 |
9.63e-03 |
|
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: 40.25 E-value: 9.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523740 1218 QADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEeieasekseqaalnaAKEKALQQLREQLEGERKE 1297
Cdd:cd16269 188 QADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQER---------------SYEEHLRQLKEKMEEEREN 252
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462523740 1298 AVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQE 1334
Cdd:cd16269 253 LLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRS 289
|
|
| |
