|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1147-1632 |
1.76e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.77 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1147 EQLSEAALKAMEEAVAQV--LEQDQRHLLESKQEKMQQLREKlcQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARM 1224
Cdd:COG1196 280 ELELEEAQAEEYELLAELarLEQDIARLEERRRELEERLEEL--EEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1225 REEESQRLSwlRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQM-LEQLKEEIEASEKSEQAALN 1303
Cdd:COG1196 358 AELAEAEEA--LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLErLERLEEELEELEEALAELEE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1304 AAKEKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQ--------------L 1369
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEadyegflegvkaalL 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1370 QKCLGQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEH-QQVMAKAREQYEAEERKQRAELLGHLTG 1448
Cdd:COG1196 516 LAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLkAAKAGRATFLPLDKIRARAALAAALARG 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1449 ELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQV 1528
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1529 ALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQsqqlqkhfssLEAEAQKKQHLLREV 1608
Cdd:COG1196 676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQL----------EAEREELLEELLEEE 745
|
490 500
....*....|....*....|....
gi 530397889 1609 TVEENNASPHFEPDLHIEDLRKSL 1632
Cdd:COG1196 746 ELLEEEALEELPEPPDLEELEREL 769
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1197-1766 |
7.31e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 93.85 E-value: 7.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1197 RLHQQKEQSLS--SLRERLQKAIEEEEARMREEESQRLSWLRAQVQSsTQADEDQIRAEQEAsLQKLREELESQQKAERA 1274
Cdd:COG1196 204 PLERQAEKAERyrELKEELKELEAELLLLKLRELEAELEELEAELEE-LEAELEELEAELAE-LEAELEELRLELEELEL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1275 SLEQKNRQmLEQLKEEIEASEKseQAALNAAKEKALQQLREQLEGERKEAVATLEkEHSAELERLCSSLEAkhrevvssl 1354
Cdd:COG1196 282 ELEEAQAE-EYELLAELARLEQ--DIARLEERRRELEERLEELEEELAELEEELE-ELEEELEELEEELEE--------- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1355 QKKIQEAQQKEEAQLQKclgqvehrvhqksyhvagyehELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAE 1434
Cdd:COG1196 349 AEEELEEAEAELAEAEE---------------------ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1435 ERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETA 1514
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1515 RREKQQLLDvqrqvalksEEATATHQQLEEAQKEhTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSL 1594
Cdd:COG1196 488 EAAARLLLL---------LEAEADYEGFLEGVKA-ALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1595 EAEAQ----KKQHLLREVTVEENNASPHFEPDLHIEDLRKSLGTNQTKEvssslsqskEDLYLDSLSSHNVWHLLSAEGV 1670
Cdd:COG1196 558 VAAAAieylKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVAS---------DLREADARYYVLGDTLLGRTLV 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1671 ALRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELASAQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSAMRKGHNLLKK 1750
Cdd:COG1196 629 AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE 708
|
570
....*....|....*.
gi 530397889 1751 KEEKLNQLESSLWEEA 1766
Cdd:COG1196 709 LAEAEEERLEEELEEE 724
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1009-1607 |
1.30e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 93.67 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1009 EDKDDSQSSQDELQSKQSKGLEERLSPPLPHEERAQSPPRslATEEEPPQGPEGQPEWKEAEELGEDSAASLSLQLSLQR 1088
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK--AEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1089 EQAPSPPAACEKGKEQHSQAEELGPGQEEAEDPEEkvavsptppvspeVRSTEPVAPPEQLSEAALKAMEEAVAQVLEQD 1168
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE-------------AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK 1378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1169 QRHLLESKQEKMQQLREKlcqeeeeeilrlhQQKEQSLSSLRERLQKAieeeearmrEEESQRLSWLRAQVQSSTQADED 1248
Cdd:PTZ00121 1379 KADAAKKKAEEKKKADEA-------------KKKAEEDKKKADELKKA---------AAAKKKADEAKKKAEEKKKADEA 1436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1249 QIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNA--AKEKAlQQLREQLEgERKEAVA 1326
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAeeAKKKA-DEAKKAAE-AKKKADE 1514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1327 TLEKEHSAELERLCSSLEAKHREVVsslqKKIQEAQQKEEAQLQKCLGQVEHRvhQKSYHVAGYEHELSSLLREKRQEVE 1406
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKADEA----KKAEEKKKADELKKAEELKKAEEK--KKAEEAKKAEEDKNMALRKAEEAKK 1588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1407 GEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQ-EQHKRLEDLRRRHREQERK 1485
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKaEELKKAEEENKIKAAEEAK 1668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1486 lqdleldletRAKDVKARLALLEVQEETARREKQQLLDvqrqvalKSEEAtathQQLEEAQKEHTHLLQSNQQLREildE 1565
Cdd:PTZ00121 1669 ----------KAEEDKKKAEEAKKAEEDEKKAAEALKK-------EAEEA----KKAEELKKKEAEEKKKAEELKK---A 1724
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 530397889 1566 LQARKLKLEsQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLRE 1607
Cdd:PTZ00121 1725 EEENKIKAE-EAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKE 1765
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1147-1730 |
2.38e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.84 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1147 EQLSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKLcQEEEEEILRL---HQQKEQSLSSLRERLQKAIEEEEAR 1223
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAEL-AELEAELEELrleLEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1224 MREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLE--QKNRQMLEQLKEEIEASEKSEQAA 1301
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEeaEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1302 LNAAKEKALQQLREQLEGERKEA-VATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRV 1380
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEeLEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1381 HQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLtGELERLQRAHERE 1460
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAV-AVLIGVEAAYEAA 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1461 LETVRQEQhkrledLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEAtathq 1540
Cdd:COG1196 540 LEAALAAA------LQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDL----- 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1541 qLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLREVTVEENnasphfe 1620
Cdd:COG1196 609 -READARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE------- 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1621 pdlhIEDLRKSLGTNQTKEVSSSLSQSKEDLyldslsshnvwHLLSAEGVALRSAKEFLVQQTRSMRRRQTALKAAQQHW 1700
Cdd:COG1196 681 ----LEELAERLAEEELELEEALLAEEEEER-----------ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
570 580 590
....*....|....*....|....*....|
gi 530397889 1701 RHELASAQEVAKDPPGIKALEDMRKNLEKE 1730
Cdd:COG1196 746 ELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1148-1578 |
2.78e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.84 E-value: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1148 QLSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKlcQEEEEEILRLhQQKEQSLSSLRERLQKAIEEEEARMREE 1227
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA--AELAAQLEEL-EEAEEALLERLERLEEELEELEEALAEL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1228 ESQRLSWLRAQVQ-SSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRqmLEQLKEEIEASEKSEQAALNAAK 1306
Cdd:COG1196 434 EEEEEEEEEALEEaAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE--AAARLLLLLEAEADYEGFLEGVK 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1307 EKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKC-LGQVEHRVHQKSY 1385
Cdd:COG1196 512 AALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLpLDKIRARAALAAA 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1386 HVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEhqqVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVR 1465
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLLGR---TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1466 QEQHKRLEDLRRRhREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEAtatHQQLEEA 1545
Cdd:COG1196 669 ELLAALLEAEAEL-EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL---LEELLEE 744
|
410 420 430
....*....|....*....|....*....|...
gi 530397889 1546 QKEHTHLLQSNQQLREILDELQARKLKLESQVD 1578
Cdd:COG1196 745 EELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1008-1765 |
2.19e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 86.35 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1008 IEDKDDSQSSQDELQSKQSKGLEERLSPPLPHEERAQSPpRSLATEEeppqgpegqpeWKEAEELGEDSAASLSLQLSLQ 1087
Cdd:PTZ00121 1047 IIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKE-DNRADEA-----------TEEAFGKAEEAKKTETGKAEEA 1114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1088 REQAPSPPAACEKGKEQHSQAEELGPGQEEAEDPEEKVAVSPTPPVSpEVRSTEPVAPPEQL--SEAALKAMEEAVAQVL 1165
Cdd:PTZ00121 1115 RKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAE-DARKAEEARKAEDAkkAEAARKAEEVRKAEEL 1193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1166 ---------EQDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLR 1236
Cdd:PTZ00121 1194 rkaedarkaEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK 1273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1237 AQvqSSTQADEDQiRAEQEASLQKLREElESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKE--KALQQLR 1314
Cdd:PTZ00121 1274 AE--EARKADELK-KAEEKKKADEAKKA-EEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEakKAAEAAK 1349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1315 EQLEGERKEAVATLEKEHSAELERLcsslEAKHRevVSSLQKKIQEAQQKEEAQlqkclgqvehrvhQKSYHVAGYEHEL 1394
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKE----EAKKK--ADAAKKKAEEKKKADEAK-------------KKAEEDKKKADEL 1410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1395 SSLLREKRQEVE----GEHERRLDKMKEehqqvmaKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHK 1470
Cdd:PTZ00121 1411 KKAAAAKKKADEakkkAEEKKKADEAKK-------KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1471 RLEDLRRRHREQERKLQDLELDLETRAKDVKARLAllevqeETARREKQqlldvqrqvALKSEEATATHQQLEEAQKEHT 1550
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA------EEAKKADE---------AKKAEEAKKADEAKKAEEKKKA 1548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1551 HLLQSNQQLREILDELQARKLKLESQvdllqaqsqqlQKHFSSLEAEAQKKqhlLREVTVEENNASPHFEPDLHIEDLRK 1630
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKAEEAKKAEE-----------DKNMALRKAEEAKK---AEEARIEEVMKLYEEEKKMKAEEAKK 1614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1631 SlgtNQTKEVSSSLSQSKEDlyldslsSHNVWHLLSAEGVALRSAKEFL-VQQTRSMRRRQTALKAAQQHWRHELA---- 1705
Cdd:PTZ00121 1615 A---EEAKIKAEELKKAEEE-------KKKVEQLKKKEAEEKKKAEELKkAEEENKIKAAEEAKKAEEDKKKAEEAkkae 1684
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530397889 1706 -----SAQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSA----MRKGHNLLKKKEEKLNQLESSLWEE 1765
Cdd:PTZ00121 1685 edekkAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAeeenKIKAEEAKKEAEEDKKKAEEAKKDE 1753
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1167-1762 |
3.40e-16 |
|
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: 85.11 E-value: 3.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1167 QDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQsLSSLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQAD 1246
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEK-LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1247 E-DQIRaEQEASLQKLREELESQQKAERASLEqKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEgeRKEAV 1325
Cdd:TIGR02168 387 KvAQLE-LQIASLNNEIERLEARLERLEDRRE-RLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE--RLEEA 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1326 ATLEKEHSAELERLCSSLEAKHREVVSslQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHV----------AGYEHELS 1395
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQA--RLDSLERLQENLEGFSEGVKALLKNQSGLSGILgvlselisvdEGYEAAIE 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1396 SLLREKRQEVEGEHE----------------------------------RRLDKMKEEHQQVMAKAREQYEAEERKQRAE 1441
Cdd:TIGR02168 541 AALGGRLQAVVVENLnaakkaiaflkqnelgrvtflpldsikgteiqgnDREILKNIEGFLGVAKDLVKFDPKLRKALSY 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1442 LLGH------LTGELERLQRAHEREL----------------------ETVRQEQHKRLEDLRRRHREQERKLQDLEL-- 1491
Cdd:TIGR02168 621 LLGGvlvvddLDNALELAKKLRPGYRivtldgdlvrpggvitggsaktNSSILERRREIEELEEKIEELEEKIAELEKal 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1492 -DLETRAKDVKARLALLEVQEETARRE----KQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDEL 1566
Cdd:TIGR02168 701 aELRKELEELEEELEQLRKELEELSRQisalRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1567 QARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQK-KQHLLREVTVEENNASPHFEPDLHIEDLRKSLGTNQTKEVSSSLS 1645
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDELRAELTLlNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1646 QSKEDLYLDSLSSHNVWHL-----LSAEGVALRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELASAQEVakdppgIKAL 1720
Cdd:TIGR02168 861 IEELEELIEELESELEALLnerasLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR------LEGL 934
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 530397889 1721 EDMRKNL-----EKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSL 1762
Cdd:TIGR02168 935 EVRIDNLqerlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1310-1608 |
4.71e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.60 E-value: 4.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1310 LQQLREQLEGERKEAVATLE-KEHSAELERLCSSLEAKHREVVSSLQKKIQ---EAQQKEEAQLQKCLGQVEHRVHQksy 1385
Cdd:COG1196 195 LGELERQLEPLERQAEKAERyRELKEELKELEAELLLLKLRELEAELEELEaelEELEAELEELEAELAELEAELEE--- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1386 hvAGYEHELSSLLREKRQEVEGEHERRLDKM--KEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHE----- 1458
Cdd:COG1196 272 --LRLELEELELELEEAQAEEYELLAELARLeqDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEeleea 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1459 ----RELETVRQEQHKRLEDLRRRHREQERKLQDL---ELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALK 1531
Cdd:COG1196 350 eeelEEAEAELAEAEEALLEAEAELAEAEEELEELaeeLLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1532 SEEAT----ATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLRE 1607
Cdd:COG1196 430 LAELEeeeeEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
|
.
gi 530397889 1608 V 1608
Cdd:COG1196 510 V 510
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1158-1766 |
8.01e-15 |
|
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: 80.78 E-value: 8.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1158 EEAVAQVLEQDQRHLLESKQEKMQQLREKLCQeeeeeILRLHQQKEQSLSSLRERLQKAieeeeaRMREEESQRLSWLRA 1237
Cdd:TIGR00618 199 LTLRSQLLTLCTPCMPDTYHERKQVLEKELKH-----LREALQQTQQSHAYLTQKREAQ------EEQLKKQQLLKQLRA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1238 QVQSSTQadedqiraeQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALnaakEKALQQLREQL 1317
Cdd:TIGR00618 268 RIEELRA---------QEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSR----AKLLMKRAAHV 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1318 egerkeavatlekEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSL 1397
Cdd:TIGR00618 335 -------------KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1398 lrekrqevegeherrLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRR 1477
Cdd:TIGR00618 402 ---------------LDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1478 RHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLL--DVQRQVALKSEEATATHQQLEEaqkEHTHLLQS 1555
Cdd:TIGR00618 467 SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIhpNPARQDIDNPGPLTRRMQRGEQ---TYAQLETS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1556 NQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLREV---TVEENNASPHFEPDLHIEDLRKSL 1632
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLqdlTEKLSEAEDMLACEQHALLRKLQP 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1633 GTNQtKEVSSSLSQSKEDLYLDSLSSHNVWHLLSAEGV--ALRSAKEFlvqQTRSMRRRQTALKAAQQ------HWRHEL 1704
Cdd:TIGR00618 624 EQDL-QDVRLHLQQCSQELALKLTALHALQLTLTQERVreHALSIRVL---PKELLASRQLALQKMQSekeqltYWKEML 699
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530397889 1705 ASAQEvakdppgikALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSLWEEA 1766
Cdd:TIGR00618 700 AQCQT---------LLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQA 752
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1152-1577 |
8.45e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.47 E-value: 8.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1152 AALKAMEEAVAQVLEQDQRhlLESKQEKMQQLREKLcqeeeEEILRLHQQKEQSLSSLR---ERLQKAIEEEEARMREEe 1228
Cdd:PRK02224 206 ERLNGLESELAELDEEIER--YEEQREQARETRDEA-----DEVLEEHEERREELETLEaeiEDLRETIAETEREREEL- 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1229 SQRLSWLRAQVQ------SSTQADEDQIRAEQEASLQKlREELESQQKAERASLEQKnRQMLEQLKEEIE---------- 1292
Cdd:PRK02224 278 AEEVRDLRERLEeleeerDDLLAEAGLDDADAEAVEAR-REELEDRDEELRDRLEEC-RVAAQAHNEEAEslredaddle 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1293 --ASEKSEQAAlnaAKEKALQQLREQLEgERKEAVATLEKE-----------------HSAELERLCSSLEAKHREV--- 1350
Cdd:PRK02224 356 erAEELREEAA---ELESELEEAREAVE-DRREEIEELEEEieelrerfgdapvdlgnAEDFLEELREERDELREREael 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1351 ---VSSLQKKIQEAQQKEEAQlqKC--LGQ-VEHRVH-----QKSYHVAGYEHELSSLlREKRQEVEGEHER-------- 1411
Cdd:PRK02224 432 eatLRTARERVEEAEALLEAG--KCpeCGQpVEGSPHvetieEDRERVEELEAELEDL-EEEVEEVEERLERaedlveae 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1412 -RLDKMKEEHQQVMAKAREQYE-AEERKQRAELLGHLTGELErlqrAHERELETVRQEQHKRLEDLRRRHREQERKLQDL 1489
Cdd:PRK02224 509 dRIERLEERREDLEELIAERREtIEEKRERAEELRERAAELE----AEAEEKREAAAEAEEEAEEAREEVAELNSKLAEL 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1490 ELDLEtRAKDVKARLALLEVQEETA-----RREKQQLLDVQRQVALKSE-------EATATHQQLEEAQKEHTHLLQSNQ 1557
Cdd:PRK02224 585 KERIE-SLERIRTLLAAIADAEDEIerlreKREALAELNDERRERLAEKrerkrelEAEFDEARIEEAREDKERAEEYLE 663
|
490 500
....*....|....*....|
gi 530397889 1558 QLREILDELQARKLKLESQV 1577
Cdd:PRK02224 664 QVEEKLDELREERDDLQAEI 683
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1253-1570 |
1.12e-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: 79.78 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1253 EQEASLQKLREELESQQKAERASLEQKNRQMLE-----QLKEEIEASEKSEQAALNAAKEKALQQLREQ-----LEGERK 1322
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEKAREVERRRKLEEaekarQAEMDRQAAIYAEQERMAMERERELERIRQEerkreLERIRQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1323 EAVAtLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQlqkclgqveHRVHQKSYHVAGYEHELSSLLREKR 1402
Cdd:pfam17380 368 EEIA-MEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQ---------RKIQQQKVEMEQIRAEQEEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1403 QEVEGEHERRLDKMKEEH---QQVMAKAREQYEAEERKQRaellghltgELERLQRAHERELETVRQEQHKRLEDLRRRH 1479
Cdd:pfam17380 438 RRLEEERAREMERVRLEEqerQQQVERLRQQEEERKRKKL---------ELEKEKRDRKRAEEQRRKILEKELEERKQAM 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1480 REQERKLQDLELDLETRAKDVKARLALLEVQEEtarREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHthllqsnQQL 1559
Cdd:pfam17380 509 IEEERKRKLLEKEMEERQKAIYEEERRREAEEE---RRKQQEMEERRRIQEQMRKATEERSRLEAMERER-------EMM 578
|
330
....*....|.
gi 530397889 1560 REILDELQARK 1570
Cdd:pfam17380 579 RQIVESEKARA 589
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
899-1523 |
1.33e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.19 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 899 SEPAKASEKEAPEDTVDAGEEGSRREEAAK-EPKKKASALEEGSSDASQELEISEHMKEPQLSDSIASDPKSFHGLDFGF 977
Cdd:PTZ00121 1196 AEDARKAEAARKAEEERKAEEARKAEDAKKaEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE 1275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 978 RSRISEHLLDVDVLSPvlGGACRQAQQPLGIED---KDDSQSSQDELQSKQSKGLEERLSPPLPHEERAQSPPRSLATEE 1054
Cdd:PTZ00121 1276 EARKADELKKAEEKKK--ADEAKKAEEKKKADEakkKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1055 EPPQGPEGQPEWKEAEELGEDSAASLSLQLSLQREQAPSPPAACEKGKEQHSQAEELGPGQEEAEDPEEkvavspTPPVS 1134
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE------AKKKA 1427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1135 PEVRSTEPVappEQLSEAALKAmEEAVAQVLEQDQRHLLESKQE---KMQQLREKLCQEEEEEILRLHQQKEQSLSSLRE 1211
Cdd:PTZ00121 1428 EEKKKADEA---KKKAEEAKKA-DEAKKKAEEAKKAEEAKKKAEeakKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK 1503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1212 RLQKAIEEEEARMREEESQRLSWLRaQVQSSTQADEDQiRAEQEASLQKLR--EEL---ESQQKAERASLEQKNRQMLEQ 1286
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEAK-KAEEAKKADEAK-KAEEKKKADELKkaEELkkaEEKKKAEEAKKAEEDKNMALR 1581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1287 LKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKeavatlEKEHSAELERlcsslEAKHREVVSSLQKKIQEAQQKEE 1366
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE------AKIKAEELKK-----AEEEKKKVEQLKKKEAEEKKKAE 1650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1367 aQLQKclgqvehrvhqksyhvagyEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAEllghl 1446
Cdd:PTZ00121 1651 -ELKK-------------------AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE----- 1705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1447 tgELERLQRAHERELETVRQEQHKR---LEDLRRRHREQERKLQDLELDlETRAKDVKARLALLEVQEETARREKQQLLD 1523
Cdd:PTZ00121 1706 --ELKKKEAEEKKKAEELKKAEEENkikAEEAKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1247-1576 |
4.38e-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: 78.17 E-value: 4.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1247 EDQIRAEQE--ASLQKLREELESQQKaeraSLEQKNRQMlEQLKEeIEASEKSEQAALNAAKEKALQQLREQLEGERKEA 1324
Cdd:TIGR02168 178 ERKLERTREnlDRLEDILNELERQLK----SLERQAEKA-ERYKE-LKAELRELELALLVLRLEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1325 VaTLEKEHSAELERLCSSLEAkHREVVSSLQKKIQEAQQKEEA---QLQKCLGQVEHRVHQKSYHVAGYEHELSSLLREK 1401
Cdd:TIGR02168 252 E-EELEELTAELQELEEKLEE-LRLEVSELEEEIEELQKELYAlanEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1402 RQEVE-GEHERRLDKMKEEHQQVMAKAREQYEAEERKQRaellghltgELERLQRAHERELETVRQEQH---KRLEDLRR 1477
Cdd:TIGR02168 330 SKLDElAEELAELEEKLEELKEELESLEAELEELEAELE---------ELESRLEELEEQLETLRSKVAqleLQIASLNN 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1478 RHREQERKLQDLEldlETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATH-QQLEEAQKEHTHLLQSN 1556
Cdd:TIGR02168 401 EIERLEARLERLE---DRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLeEALEELREELEEAEQAL 477
|
330 340
....*....|....*....|
gi 530397889 1557 QQLREILDELQARKLKLESQ 1576
Cdd:TIGR02168 478 DAAERELAQLQARLDSLERL 497
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1154-1651 |
1.62e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.49 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1154 LKAMEEAVAQVLEQdQRHL--LESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKaieeeearmreeesqr 1231
Cdd:COG4913 237 LERAHEALEDAREQ-IELLepIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE---------------- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1232 lswLRAQVQSsTQADEDQIRAEQEASLQKLREelesqqkAERASLEQKNRQmLEQLKEEIEASEKSEQAALNAAK--EKA 1309
Cdd:COG4913 300 ---LRAELAR-LEAELERLEARLDALREELDE-------LEAQIRGNGGDR-LEQLEREIERLERELEERERRRArlEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1310 LQQLREQLEGERkEAVATLEKEHSAELERLcSSLEAKHREVVSSLQKKIQEAQqKEEAQLQKCLGQVEHRVHQKSYHVAG 1389
Cdd:COG4913 368 LAALGLPLPASA-EEFAALRAEAAALLEAL-EEELEALEEALAEAEAALRDLR-RELRELEAEIASLERRKSNIPARLLA 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1390 YEHELSSLLREKRQE---------------------------------VEGEHERR----LDKMKEEHQQVMAKAREQYE 1432
Cdd:COG4913 445 LRDALAEALGLDEAElpfvgelievrpeeerwrgaiervlggfaltllVPPEHYAAalrwVNRLHLRGRLVYERVRTGLP 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1433 AEERKQRAEllGHLTGELE------------RLQR-------AHERELETVRQ---------EQHKRLE-DLRRRHREQ- 1482
Cdd:COG4913 525 DPERPRLDP--DSLAGKLDfkphpfrawleaELGRrfdyvcvDSPEELRRHPRaitragqvkGNGTRHEkDDRRRIRSRy 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1483 ------ERKLQDLELD---LETRAKDVKARLALLEVQEETARREKQQLLDVQrQVALKSEEATATHQQLEEAQKEHTHLL 1553
Cdd:COG4913 603 vlgfdnRAKLAALEAElaeLEEELAEAEERLEALEAELDALQERREALQRLA-EYSWDEIDVASAEREIAELEAELERLD 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1554 QSN---QQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLREVtveENNASPHFEPDLhIEDLRK 1630
Cdd:COG4913 682 ASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA---EDLARLELRALL-EERFAA 757
|
570 580
....*....|....*....|.
gi 530397889 1631 SLGTNQTKEVSSSLSQSKEDL 1651
Cdd:COG4913 758 ALGDAVERELRENLEERIDAL 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1083-1608 |
2.22e-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: 75.86 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1083 QLSLQREQAPSppAACEKGKEQHSQAEELGPGQEEAEDPEEKVAvsptppvspEVRSTEPVAppEQLSEAALKAMEE--- 1159
Cdd:TIGR02168 320 ELEAQLEELES--KLDELAEELAELEEKLEELKEELESLEAELE---------ELEAELEEL--ESRLEELEEQLETlrs 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1160 AVAQVLEQ-----DQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMREEEsQRLSW 1234
Cdd:TIGR02168 387 KVAQLELQiaslnNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE-EALEE 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1235 LRAQVQSSTQA------DEDQIRAEQeASLQKLREELESQQKAERASLEQKNR--QMLEQLKEEIEASEKSEqAALNAAK 1306
Cdd:TIGR02168 466 LREELEEAEQAldaaerELAQLQARL-DSLERLQENLEGFSEGVKALLKNQSGlsGILGVLSELISVDEGYE-AAIEAAL 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1307 EKALQQLREQLEGERKEAVATLEKEHS-----AELERLC-SSLEAKHRE------------------------------- 1349
Cdd:TIGR02168 544 GGRLQAVVVENLNAAKKAIAFLKQNELgrvtfLPLDSIKgTEIQGNDREilkniegflgvakdlvkfdpklrkalsyllg 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1350 ---VVSSLQ------KKIQE------------------------------AQQKEEAQLQKCLGQVEHRVHQKSYHVAGY 1390
Cdd:TIGR02168 624 gvlVVDDLDnalelaKKLRPgyrivtldgdlvrpggvitggsaktnssilERRREIEELEEKIEELEEKIAELEKALAEL 703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1391 EHELSSLLREKRQevegeherrLDKMKEEHQQVMAKAREQYEAEERKQRAellghLTGELERLQRAHErELETVRQEQHK 1470
Cdd:TIGR02168 704 RKELEELEEELEQ---------LRKELEELSRQISALRKDLARLEAEVEQ-----LEERIAQLSKELT-ELEAEIEELEE 768
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1471 RLEDLRRRHREQERKLQDLELDLETRAKDVKA-RLALLEVQEEtARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEH 1549
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKAlREALDELRAE-LTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 530397889 1550 THLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLREV 1608
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1158-1569 |
4.87e-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: 75.09 E-value: 4.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1158 EEAVAQVLEQDQRHL-LESKQEKMQQLREKLcQEEEEEILRLHQQKEQSLSSLRERLQkaieeeearmreEESQRLSWLR 1236
Cdd:TIGR02168 666 AKTNSSILERRREIEeLEEKIEELEEKIAEL-EKALAELRKELEELEEELEQLRKELE------------ELSRQISALR 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1237 AQVQSSTQadEDQIRAEQEASLQKLREELEsQQKAERASLEQKNRQMLEQLKEEIEasekSEQAALNAAKEkALQQLREQ 1316
Cdd:TIGR02168 733 KDLARLEA--EVEQLEERIAQLSKELTELE-AEIEELEERLEEAEEELAEAEAEIE----ELEAQIEQLKE-ELKALREA 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1317 LEGERKEavATLEKEHSAELERLCSSLEAKHREVVSSLQkkiQEAQQKEEAQLQkclgqvehrvhqksyhVAGYEHELSS 1396
Cdd:TIGR02168 805 LDELRAE--LTLLNEEAANLRERLESLERRIAATERRLE---DLEEQIEELSED----------------IESLAAEIEE 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1397 lLREKRQEVEGEHErRLDKMKEEHQQVMAKAREQYEAEERKQRaellghltgELERLQRAHERELETVRQEQHK---RLE 1473
Cdd:TIGR02168 864 -LEELIEELESELE-ALLNERASLEEALALLRSELEELSEELR---------ELESKRSELRRELEELREKLAQlelRLE 932
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1474 DLR-RRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRqVALKS-EEATATHQQLEEAQKEHTH 1551
Cdd:TIGR02168 933 GLEvRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGP-VNLAAiEEYEELKERYDFLTAQKED 1011
|
410
....*....|....*...
gi 530397889 1552 LLQSNQQLREILDELQAR 1569
Cdd:TIGR02168 1012 LTEAKETLEEAIEEIDRE 1029
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1146-1566 |
2.94e-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: 72.31 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1146 PEQLSEAALKAMEEAVAQVLEQDQRHLLESKQ---EKMQQL--------REKLCQEEEEEILRLHQQKEQSL-SSLRERL 1213
Cdd:TIGR00618 435 LQQRYAELCAAAITCTAQCEKLEKIHLQESAQslkEREQQLqtkeqihlQETRKKAVVLARLLELQEEPCPLcGSCIHPN 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1214 QKAIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEaSLQKLREELESQQKAERASLEQKNR--QMLEQLKEEI 1291
Cdd:TIGR00618 515 PARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK-QRASLKEQMQEIQQSFSILTQCDNRskEDIPNLQNIT 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1292 EASEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEA-----QQKEE 1366
Cdd:TIGR00618 594 VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHalsirVLPKE 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1367 --AQLQKCLGQVEHRVHQKSYHVAGYEHELSsLLREkrqevEGEHERRLDKMKEEHQQVMAKAREQYEAEE--------- 1435
Cdd:TIGR00618 674 llASRQLALQKMQSEKEQLTYWKEMLAQCQT-LLRE-----LETHIEEYDREFNEIENASSSLGSDLAAREdalnqslke 747
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1436 -RKQRAELLGHLTGELERLQRAHERELETVRQEQHKRlEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETA 1514
Cdd:TIGR00618 748 lMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLA-AEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETL 826
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 530397889 1515 RREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDEL 1566
Cdd:TIGR00618 827 VQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1151-1524 |
4.96e-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: 71.63 E-value: 4.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1151 EAALKAMEEAVAQVleQDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQsLSSLRERLQKAieeeearmreeeSQ 1230
Cdd:TIGR02168 683 EEKIEELEEKIAEL--EKALAELRKELEELEEELEQLRKELEELSRQISALRKD-LARLEAEVEQL------------EE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1231 RLSWLRAQVQSSTQADEDQIRAEQEASLQKLREElesqqkAERASLEQKNRQMLEQLKEEIEASeKSEQAALNAAKEKAl 1310
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAE------AEIEELEAQIEQLKEELKALREAL-DELRAELTLLNEEA- 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1311 QQLREQLEGERKEAVATlekehSAELERLCSSLEAKhREVVSSLQKKIQEAQQKEEAQlqkclgQVEHRVHQKSYHVAGY 1390
Cdd:TIGR02168 820 ANLRERLESLERRIAAT-----ERRLEDLEEQIEEL-SEDIESLAAEIEELEELIEEL------ESELEALLNERASLEE 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1391 EHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKareQYEAEERKQRAELLghLTGELERLQRAHERELETVRQEQHK 1470
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELRRELEELREK---LAQLELRLEGLEVR--IDNLQERLSEEYSLTLEEAEALENK 962
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1471 RLED---LRRRHREQERKLQDL---ELDLETRAKDVKARLALLEVQEETARREKQQLLDV 1524
Cdd:TIGR02168 963 IEDDeeeARRRLKRLENKIKELgpvNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEA 1022
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1151-1566 |
5.22e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.95 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1151 EAALKAMEEAVAQVLE-QDQRHLLESKQEKMQQLREKLCQEEEE-EILRLHQQKEQSLSSLRERLQkaieeeearmreEE 1228
Cdd:COG4717 77 EEELKEAEEKEEEYAElQEELEELEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELA------------EL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1229 SQRLSWLRAQVQSSTQADEDQIRAEQEasLQKLREELESQQKAERASLEQKNRQMLEQLkEEIEASEKSEQAALNAAKEK 1308
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAE--LAELQEELEELLEQLSLATEEELQDLAEEL-EELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1309 aLQQLREQLEGERKEAVATLEKEHSAELERL-------------------------------------CSSLEAKHREVV 1351
Cdd:COG4717 222 -LEELEEELEQLENELEAAALEERLKEARLLlliaaallallglggsllsliltiagvlflvlgllalLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1352 SSLQKKIQEAQQK---EEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKA- 1427
Cdd:COG4717 301 GKEAEELQALPALeelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAg 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1428 ----------------REQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLEL 1491
Cdd:COG4717 381 vedeeelraaleqaeeYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEA 460
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530397889 1492 DLETRAKDvkARLALLEVQEETARREKQQLldVQRQVALKseeatATHQQLEEAQKEHTHLLQS--NQQLREILDEL 1566
Cdd:COG4717 461 ELEQLEED--GELAELLQELEELKAELREL--AEEWAALK-----LALELLEEAREEYREERLPpvLERASEYFSRL 528
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1173-1761 |
5.72e-12 |
|
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: 71.30 E-value: 5.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1173 LESKQEKMQQLREKLCQeeeeeilrLHQQKEQSLSSLRERLQKAIEEEEARMReeesqrlswLRAQVQSSTQADEDQIRA 1252
Cdd:pfam15921 115 LQTKLQEMQMERDAMAD--------IRRRESQSQEDLRNQLQNTVHELEAAKC---------LKEDMLEDSNTQIEQLRK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1253 ---EQEASLQKLR------EELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLrEQLEGERKE 1323
Cdd:pfam15921 178 mmlSHEGVLQEIRsilvdfEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQL-EALKSESQN 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1324 AVATLEKEHSAELERLCSSLE----------AKHREVVSSLQKK---IQEAQQKEEAQLQKCLGQVEHRVHQksyhvagy 1390
Cdd:pfam15921 257 KIELLLQQHQDRIEQLISEHEveitgltekaSSARSQANSIQSQleiIQEQARNQNSMYMRQLSDLESTVSQ-------- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1391 eheLSSLLREKRQEVEgeherrlDKMKEEHQQVMAKAREQYEAE-ERKQRAELLGHLTGELERL-QRAHERELE-TVRQE 1467
Cdd:pfam15921 329 ---LRSELREAKRMYE-------DKIEELEKQLVLANSELTEARtERDQFSQESGNLDDQLQKLlADLHKREKElSLEKE 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1468 QHKRLEDlrrRHREQERKLQDLELDLETRAKDVKARLALLE-VQEETARREKQQLLDVQrqvalkseeatATHQQLEEAQ 1546
Cdd:pfam15921 399 QNKRLWD---RDTGNSITIDHLRRELDDRNMEVQRLEALLKaMKSECQGQMERQMAAIQ-----------GKNESLEKVS 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1547 KEHTHLLQSNQQLREILDELQARKLKLESqvdllqaqsqqLQKHFSSLEAEAQKKQHLLR----EVTVEENNASPHFEPD 1622
Cdd:pfam15921 465 SLTAQLESTKEMLRKVVEELTAKKMTLES-----------SERTVSDLTASLQEKERAIEatnaEITKLRSRVDLKLQEL 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1623 LHIEDLRKSLGTNQTKEVSSSLSQSKEDLYLDSLSSH--NVWHLLSAEGvalRSAKEFLVQQTRsmrrrqtaLKAAQQHW 1700
Cdd:pfam15921 534 QHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQieNMTQLVGQHG---RTAGAMQVEKAQ--------LEKEINDR 602
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530397889 1701 RHELASAQEVA-KDPPGIKALEDMRKNLEKETRHLDEMKSA-MRKGHNLLKKKEEKLNQLESS 1761
Cdd:pfam15921 603 RLELQEFKILKdKKDAKIRELEARVSDLELEKVKLVNAGSErLRAVKDIKQERDQLLNEVKTS 665
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1099-1490 |
1.02e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.45 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1099 EKGKEQHSQAEELGpgqEEAEDPEEKVavsptppvspEVRSTEPVAPPEQLsEAALKAMEEAVAQVLEQDQRhlLESKQE 1178
Cdd:PRK02224 356 ERAEELREEAAELE---SELEEAREAV----------EDRREEIEELEEEI-EELRERFGDAPVDLGNAEDF--LEELRE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1179 KMQQLREKLCQEeeeeilrlhqqkEQSLSSLRERLQKAIEEEEARMREEESQrlswlraQVQSSTQADEDQIRAEQEASL 1258
Cdd:PRK02224 420 ERDELREREAEL------------EATLRTARERVEEAEALLEAGKCPECGQ-------PVEGSPHVETIEEDRERVEEL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1259 QKLREELESQQ-----KAERASLEQKNRQMLEQLKEEIEASEK--SEQAALNAAKEKALQQLREQLEGERKEAVATLEKE 1331
Cdd:PRK02224 481 EAELEDLEEEVeeveeRLERAEDLVEAEDRIERLEERREDLEEliAERRETIEEKRERAEELRERAAELEAEAEEKREAA 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1332 HSAELErlcsslEAKHREVVSSLQKKIQEAQQKEEAqlqkcLGQVEHRVHQksyhVAGYEHELSSLlREKR---QEVEGE 1408
Cdd:PRK02224 561 AEAEEE------AEEAREEVAELNSKLAELKERIES-----LERIRTLLAA----IADAEDEIERL-REKRealAELNDE 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1409 HERRLDKMKEEHQQVMAKAREQY--EAEERKQRAE-LLGHLTGELERLqRAHERELET----VRQEQhKRLEDLRRRHRE 1481
Cdd:PRK02224 625 RRERLAEKRERKRELEAEFDEARieEAREDKERAEeYLEQVEEKLDEL-REERDDLQAeigaVENEL-EELEELRERREA 702
|
....*....
gi 530397889 1482 QERKLQDLE 1490
Cdd:PRK02224 703 LENRVEALE 711
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1173-1577 |
1.29e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.80 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1173 LESKQEKMQQLREKLcqeeeeeilRLHQQKEQSLSSLRERLQKAieeeeARMREEESQRLSWLRAQVQsstQADEDQIRA 1252
Cdd:COG4717 73 LKELEEELKEAEEKE---------EEYAELQEELEELEEELEEL-----EAELEELREELEKLEKLLQ---LLPLYQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1253 EQEASLQKLREELES--QQKAERASLEQKNRQMLEQLkEEIEASEKSEQAALNAAKEKALQQLREQLEgERKEAVATLEK 1330
Cdd:COG4717 136 ALEAELAELPERLEEleERLEELRELEEELEELEAEL-AELQEELEELLEQLSLATEEELQDLAEELE-ELQQRLAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1331 EhSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQV------EHRVHQKSYHVAGYEHELSSLLREKRQE 1404
Cdd:COG4717 214 E-LEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALlallglGGSLLSLILTIAGVLFLVLGLLALLFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1405 VEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQER 1484
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1485 KlqdlELDLETRAKDVKARLALLEvQEETARREKQQLLDVQRQVA--LKSEEATATHQQLEEAQKEHTHLLQSNQQLREI 1562
Cdd:COG4717 373 A----ALLAEAGVEDEEELRAALE-QAEEYQELKEELEELEEQLEelLGELEELLEALDEEELEEELEELEEELEELEEE 447
|
410
....*....|....*
gi 530397889 1563 LDELQARKLKLESQV 1577
Cdd:COG4717 448 LEELREELAELEAEL 462
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1147-1524 |
1.61e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1147 EQLSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKLcQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMRE 1226
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL-AEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1227 EESQRLSW---LRAQVQSSTQADEDQIRAEQEASLQKLREELEsQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALN 1303
Cdd:COG1196 525 AVAVLIGVeaaYEAALEAALAAALQNIVVEDDEVAAAAIEYLK-AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1304 AAKEKALQQLREQLEGERkEAVATLEKEHSAELERLCSSLEAKHREVvSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQK 1383
Cdd:COG1196 604 VASDLREADARYYVLGDT-LLGRTLVAARLEAALRRAVTLAGRLREV-TLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1384 SyhvagyehELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELET 1463
Cdd:COG1196 682 E--------ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAL 753
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530397889 1464 VRQEQHKRLEDLRRRHREQERKLQDLE---LDLETRAKDVKARLALLEVQEETARREKQQLLDV 1524
Cdd:COG1196 754 EELPEPPDLEELERELERLEREIEALGpvnLLAIEEYEELEERYDFLSEQREDLEEARETLEEA 817
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1294-1632 |
1.76e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 69.71 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1294 SEKSEQAALNAAKEKA-LQQLREQLEGERKEAVATLEKEHSAELER--LCSSLEAKHREVvSSLQKKIQEAQQKEEAQLQ 1370
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAeLQRLRERLEGLKRELSSLQSELRRIENRLdeLSQELSDASRKI-GEIEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1371 KcLGQVEHRVHQKSyhvagyehelssllrEKRQEVEGEHERrLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGEL 1450
Cdd:TIGR02169 738 R-LEELEEDLSSLE---------------QEIENVKSELKE-LEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAEL 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1451 erlqraheRELETVRQEQHKRLEDLrrrhreqERKLQDLELDLEtrakdvkarLALLEVQEETARRE--KQQLLDVQRQV 1528
Cdd:TIGR02169 801 --------SKLEEEVSRIEARLREI-------EQKLNRLTLEKE---------YLEKEIQELQEQRIdlKEQIKSIEKEI 856
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1529 ALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLREV 1608
Cdd:TIGR02169 857 ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
330 340
....*....|....*....|....
gi 530397889 1609 TVEENNASPHFEPDLHIEDLRKSL 1632
Cdd:TIGR02169 937 EDPKGEDEEIPEEELSLEDVQAEL 960
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1147-1769 |
2.19e-11 |
|
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: 69.62 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1147 EQLSEAALKAMEEAVAQVLEQDQRHLLEsKQEKMQQLREKLCQ--EEEEEILRLHQQKEQsLSSLRERLQKAIEEEEARM 1224
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELK-LQELKLKEQAKKALeyYQLKEKLELEEEYLL-YLDYLKLNEERIDLLQELL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1225 REEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQM------LEQLKEEIEASEKSE 1298
Cdd:pfam02463 247 RDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLerrkvdDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1299 QAALNAAKEKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQkCLGQVEH 1378
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE-LKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1379 RVHQKSYHVAGYEHELSSLLREKRQEVEGEhERRLDKMKEEHQQVMAKAREQYEAEERKQRAEllghltgELERLQRAHE 1458
Cdd:pfam02463 406 EAQLLLELARQLEDLLKEEKKEELEILEEE-EESIELKQGKLTEEKEELEKQELKLLKDELEL-------KKSEDLLKET 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1459 RELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALkSEEATAT 1538
Cdd:pfam02463 478 QLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV-IVEVSAT 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1539 HQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKhfsSLEAEAQKKQHLLREVTVEEnNASPH 1618
Cdd:pfam02463 557 ADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQ---LDKATLEADEDDKRAKVVEG-ILKDT 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1619 FEPDLHIEDLRKSLGTNQTKEVSSSLSQSKEDLYLDSLSshnvwhLLSAEGVALRSAKEFLVQQTRSMRRRQTALKAAQQ 1698
Cdd:pfam02463 633 ELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSEL------TKELLEIQELQEKAESELAKEEILRRQLEIKKKEQ 706
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530397889 1699 HWRHELASAQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSLWEEASDE 1769
Cdd:pfam02463 707 REKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELA 777
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1407-1775 |
2.85e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1407 GEHERRLDKMKEEHQQVMaKAREQYEAEERKQRAELLGHLT---GELERLQRAHER------ELETVRQEQHKRLEDLRR 1477
Cdd:TIGR02168 196 NELERQLKSLERQAEKAE-RYKELKAELRELELALLVLRLEelrEELEELQEELKEaeeeleELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1478 RHREQERKLQDLEldleTRAKDVKARLALLEVQEETARREKQQLldvQRQVALKSEEATATHQQLEEAQKEHThllqsnq 1557
Cdd:TIGR02168 275 EVSELEEEIEELQ----KELYALANEISRLEQQKQILRERLANL---ERQLEELEAQLEELESKLDELAEELA------- 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1558 QLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLREVTVEENNASPHFEP-DLHIEDLRKSLgtNQ 1636
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERlEARLERLEDRR--ER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1637 TKEVSSSLSQSKEDLYLDSLSSHNVwhLLSAEGVALRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELASAQEvakdppG 1716
Cdd:TIGR02168 419 LQQEIEELLKKLEEAELKELQAELE--ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA------R 490
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530397889 1717 IKALEDMRKNLEKETRhldemksamrkGHNLLKKKEEKLNQLESSLWE--------EASDEGTLGGS 1775
Cdd:TIGR02168 491 LDSLERLQENLEGFSE-----------GVKALLKNQSGLSGILGVLSElisvdegyEAAIEAALGGR 546
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1268-1576 |
5.98e-11 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 66.10 E-value: 5.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1268 QQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEgerkeavatlEKEHSAELERLcssLEAKH 1347
Cdd:pfam13868 33 RIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIE----------EREQKRQEEYE---EKLQE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1348 REVVSSLQKKIQEAQQKEEAQLQKclgqvehRVHQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKA 1427
Cdd:pfam13868 100 REQMDEIVERIQEEDQAEAEEKLE-------KQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEERE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1428 REQYEAEERKQR-AELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDlETRAKDVKARLAL 1506
Cdd:pfam13868 173 AEREEIEEEKEReIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQ-QAREEQIELKERR 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530397889 1507 LEVQEETARREKQQLLDVQR-QVALKSEEATATHQQLEEAQKEHTHLLQSNQQLR--EILDELQARKLKLESQ 1576
Cdd:pfam13868 252 LAEEAEREEEEFERMLRKQAeDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRaaEREEELEEGERLREEE 324
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1241-1759 |
1.11e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1241 SSTQADEDQIRAEQEASLQKLRE--ELESQQKAERASLE--QKNRQMLEQLKEEIEASEKSEQAALNAAK--EKALQQLR 1314
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREinEISSELPELREELEklEKEVKELEELKEEIEELEKELESLEGSKRklEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1315 EQLEGERKE-------------------AVATLEKEHSAELERL--CSSLEAKHREVVSSLQKKIQEAQQKEE--AQLQK 1371
Cdd:PRK03918 266 ERIEELKKEieeleekvkelkelkekaeEYIKLSEFYEEYLDELreIEKRLSRLEEEINGIEERIKELEEKEErlEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1372 CLGQVEHRVHQKSYHVAGYEhELSSLLREKRQEVEGEHERRLDKMKEEHQQVmAKAREQYEAEERKQRAELlGHLTGELE 1451
Cdd:PRK03918 346 KLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEKLEKELEEL-EKAKEEIEEEISKITARI-GELKKEIK 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1452 RLQRAHErELETVRQ---------EQHKRLEDLRRRHREQERKLQDLElDLETRAKDVKARLALLEVQeetarREKQQLL 1522
Cdd:PRK03918 423 ELKKAIE-ELKKAKGkcpvcgrelTEEHRKELLEEYTAELKRIEKELK-EIEEKERKLRKELRELEKV-----LKKESEL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1523 DVQRQVA--LKSEEATATHQQLEEAQKEHTHLlqsnQQLREILDELQARKLKLESQVdllqaqsqqlqkhfSSLEAEAQK 1600
Cdd:PRK03918 496 IKLKELAeqLKELEEKLKKYNLEELEKKAEEY----EKLKEKLIKLKGEIKSLKKEL--------------EKLEELKKK 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1601 KQHLLREV-TVEENNASphfepdlhIEDLRKSLGTNQTKEVSSSLsQSKEDLYLDSLSSHNVWHLLSAEGVALRSAKEFL 1679
Cdd:PRK03918 558 LAELEKKLdELEEELAE--------LLKELEELGFESVEELEERL-KELEPFYNEYLELKDAEKELEREEKELKKLEEEL 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1680 VQ----------QTRSMRRRQTALKAAQQHWRHE------LASAQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSAMRK 1743
Cdd:PRK03918 629 DKafeelaetekRLEELRKELEELEKKYSEEEYEelreeyLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREK 708
|
570
....*....|....*.
gi 530397889 1744 GHNLLKKKEEKLNQLE 1759
Cdd:PRK03918 709 AKKELEKLEKALERVE 724
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1162-1504 |
2.51e-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: 64.17 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1162 AQVLEQDQRHLLESKQEK-----MQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLR 1236
Cdd:pfam13868 26 AQIAEKKRIKAEEKEEERrldemMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1237 AQVQssTQADEDQIRAEQEASLQKLREELEsQQKAERASLEQKNRQMLEQL----------KEEIEASEKSEQAALNAAK 1306
Cdd:pfam13868 106 IVER--IQEEDQAEAEEKLEKQRQLREEID-EFNEEQAEWKELEKEEEREEderileylkeKAEREEEREAEREEIEEEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1307 EKALQQLREQLEGERKeavatlEKEHSAEL--ERLCSSLEAKHRevvsslQKKIQEAQQKEEAQLQKCLGQVEHRVHqks 1384
Cdd:pfam13868 183 EREIARLRAQQEKAQD------EKAERDELraKLYQEEQERKER------QKEREEAEKKARQRQELQQAREEQIEL--- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1385 yhvagyehelssllREKRQEVEGEHERRLDKMKEEHQQVMAKaREQYEAEERKQRaellghltgelerlQRAHERELETV 1464
Cdd:pfam13868 248 --------------KERRLAEEAEREEEEFERMLRKQAEDEE-IEQEEAEKRRMK--------------RLEHRRELEKQ 298
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 530397889 1465 RQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARL 1504
Cdd:pfam13868 299 IEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1195-1766 |
2.64e-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: 65.76 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1195 ILRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERA 1274
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1275 SLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQlreQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSL 1354
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEK---KLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1355 QKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYE-A 1433
Cdd:pfam02463 321 KEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELElK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1434 EERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEET 1513
Cdd:pfam02463 401 SEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1514 ARREKQQLLDvqrqvaLKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSS 1593
Cdd:pfam02463 481 KLQEQLELLL------SRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVS 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1594 -LEAEAQKKQHLLREVTVEENNASPHFEPDLHIEDLRKSLGTnqtkevssslsqsKEDLYLDSLSSHNVWHLLSAEGVAL 1672
Cdd:pfam02463 555 aTADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV-------------LEIDPILNLAQLDKATLEADEDDKR 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1673 RSAKEFLVQQTRSMRRRQTALKAAQ--QHWRHELASAQEVAKDPPGIKALEDMRKN--LEKETRHLDEMKSAMRKGHNLL 1748
Cdd:pfam02463 622 AKVVEGILKDTELTKLKESAKAKESglRKGVSLEEGLAEKSEVKASLSELTKELLEiqELQEKAESELAKEEILRRQLEI 701
|
570
....*....|....*...
gi 530397889 1749 KKKEEKLNQLESSLWEEA 1766
Cdd:pfam02463 702 KKKEQREKEELKKLKLEA 719
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1148-1523 |
3.07e-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: 65.86 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1148 QLSEAALKAMEEAVAQVLE--QDQRHLLESKQEKMQQLREKLCQEeeeeiLRLHQQKEQSLSSLRERLQKaieeeearMR 1225
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEglKRELSSLQSELRRIENRLDELSQE-----LSDASRKIGEIEKEIEQLEQ--------EE 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1226 EEESQRLSWLRAQVQSSTQADEDQIR---------AEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIeaSEK 1296
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQEIENVKSelkeleariEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEV--SRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1297 SEQAALNAAKEKALQQLREQLEGERKEAVATLEkehsaelerlcssleakhrevvsSLQKKIQEAQQKEEAqLQKCLGQV 1376
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRI-----------------------DLKEQIKSIEKEIEN-LNGKKEEL 866
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1377 EHRVHQKSYHVAGYEHELSSLLREKRqevegEHERRLDKMKEEHQQvmAKAREQYEAEERKQRAELLGHLTGELERLQRA 1456
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKKERD-----ELEAQLRELERKIEE--LEAQIEKKRKRLSELKAKLEALEEELSEIEDP 939
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530397889 1457 HERELETVRQEQhkRLEDLRRRHREQERKLQDLElDLETRA----KDVKARLALLEVQEETARREKQQLLD 1523
Cdd:TIGR02169 940 KGEDEEIPEEEL--SLEDVQAELQRVEEEIRALE-PVNMLAiqeyEEVLKRLDELKEKRAKLEEERKAILE 1007
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1234-1548 |
2.33e-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: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1234 WLRAQVQSSTQADEDQIRAeQEASLQKLREELESQQKAERASLEQKNrQMLEQLKEEIEASEKSEQAALnaaKEKALQQL 1313
Cdd:TIGR02169 226 YELLKEKEALERQKEAIER-QLASLEEELEKLTEEISELEKRLEEIE-QLLEELNKKIKDLGEEEQLRV---KEKIGELE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1314 REQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEaQQKEEAQLQKCLGQVEHRVHQKSYHVAgyehE 1393
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEE-ERKRRDKLTEEYAELKEELEDLRAELE----E 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1394 LSSLLREKRQEVEgEHERRLDKMKEEHQQVMakaREQYEAEERKQRAEL-LGHLTGELERLQRAHeRELETvrqeqhkRL 1472
Cdd:TIGR02169 376 VDKEFAETRDELK-DYREKLEKLKREINELK---RELDRLQEELQRLSEeLADLNAAIAGIEAKI-NELEE-------EK 443
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530397889 1473 EDLRRRHREQERKLQDLELDLEtrakdvKARLALLEVQEETARREKQqlldvQRQVALKSEEATATHQQLEEAQKE 1548
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 ... |
1159-1534 |
3.11e-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: 62.05 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1159 EAVAQVLEQDQRHLLESKQekMQQLREKLcqeeeeeilrlhQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLRAQ 1238
Cdd:pfam05483 408 EELKKILAEDEKLLDEKKQ--FEKIAEEL------------KGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEV 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1239 VQSSTQADEDQIR-AEQEASLQKLR-EELESQQKAERASLEQKNRQ------------MLEQLkEEIEASEKSEQAALNA 1304
Cdd:pfam05483 474 EDLKTELEKEKLKnIELTAHCDKLLlENKELTQEASDMTLELKKHQediinckkqeerMLKQI-ENLEEKEMNLRDELES 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1305 AKEKALQQ-------LREQLEGERKEAVATLEKEHSAE-LERLCSSLeakhREVVSSLQKKIQEAQQKEEAQLQKC---- 1372
Cdd:pfam05483 553 VREEFIQKgdevkckLDKSEENARSIEYEVLKKEKQMKiLENKCNNL----KKQIENKNKNIEELHQENKALKKKGsaen 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1373 --LGQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEGE---HERRLDKMKEEHQQVMAKAREQYEAEERKQraellgHLT 1447
Cdd:pfam05483 629 kqLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKkisEEKLLEEVEKAKAIADEAVKLQKEIDKRCQ------HKI 702
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1448 GELERLQRAHERELETVRQEQHKRLEDLRRRHREQerklQDLELDLETRAKDVKARLALLEVQEETARREKQQL-LDVQR 1526
Cdd:pfam05483 703 AEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQ----SSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLkMEAKE 778
|
....*...
gi 530397889 1527 QVALKSEE 1534
Cdd:pfam05483 779 NTAILKDK 786
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1151-1767 |
3.16e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.39 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1151 EAALKAMEEAVAQVLEQ--DQRHLLESKQEKMQQLREKLCQEEEEEILRLhQQKEQSLSSLRERLQKAIEEEEarmreee 1228
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEisELEKRLEEIEQLLEELNKKIKDLGEEEQLRV-KEKIGELEAEIASLERSIAEKE------- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1229 sQRLSWLRAQVQsstQADEDqiRAEQEASLQKLREELESQQKaERASLE---QKNRQMLEQLKEEIEASEKSEQAA---L 1302
Cdd:TIGR02169 315 -RELEDAEERLA---KLEAE--IDKLLAEIEELEREIEEERK-RRDKLTeeyAELKEELEDLRAELEEVDKEFAETrdeL 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1303 NAAKEK--ALQQLREQLEGERKEAVATLEKEHS--AELERLCSSLEAKHREVVS---SLQKKIQEAQQKEEaQLQKCLGQ 1375
Cdd:TIGR02169 388 KDYREKleKLKREINELKRELDRLQEELQRLSEelADLNAAIAGIEAKINELEEekeDKALEIKKQEWKLE-QLAADLSK 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1376 VEHRVHQKSYHVAGYEHELSSLLRE-------KRQEVEGEHERR-------------------LDKMKEEHQ-------- 1421
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRElaeaeaqARASEERVRGGRaveevlkasiqgvhgtvaqLGSVGERYAtaievaag 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1422 ----------QVMAKAREQYEAEERKQRAELLghltgELERLqRAHERELETVRQ-----------EQHKRLE------- 1473
Cdd:TIGR02169 547 nrlnnvvvedDAVAKEAIELLKRRKAGRATFL-----PLNKM-RDERRDLSILSEdgvigfavdlvEFDPKYEpafkyvf 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1474 ---------DLRRRHREQERkLQDLELDL-----------------ETRAKDVKARLALLEVQEETARREKQQLLD---- 1523
Cdd:TIGR02169 621 gdtlvvediEAARRLMGKYR-MVTLEGELfeksgamtggsraprggILFSRSEPAELQRLRERLEGLKRELSSLQSelrr 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1524 VQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQH 1603
Cdd:TIGR02169 700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEE 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1604 LLREVtveENNASPHFEPDL--HIEDLRKSLGTNQtkEVSSSLSQSKEDLYLDSLSshnvwhllsaegvaLRSAKEFLVQ 1681
Cdd:TIGR02169 780 ALNDL---EARLSHSRIPEIqaELSKLEEEVSRIE--ARLREIEQKLNRLTLEKEY--------------LEKEIQELQE 840
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1682 QTRSMRRRQTALKAAQQHWRHELAS-AQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQLES 1760
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEElEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
....*..
gi 530397889 1761 SLWEEAS 1767
Cdd:TIGR02169 921 ELKAKLE 927
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1154-1773 |
7.78e-09 |
|
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: 61.22 E-value: 7.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1154 LKAMEEAVAQVLE-QDQRHLLESKQEKMQQLREKLCQEEEE----------EILRLHQQKEQSLSSLRERLQKAIEEEEA 1222
Cdd:TIGR00606 254 LKEIEHNLSKIMKlDNEIKALKSRKKQMEKDNSELELKMEKvfqgtdeqlnDLYHNHQRTVREKERELVDCQRELEKLNK 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1223 RMREEESQRLSWLRAQVQSSTQAD--EDQIRAEQEASLQ-KLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQ 1299
Cdd:TIGR00606 334 ERRLLNQEKTELLVEQGRLQLQADrhQEHIRARDSLIQSlATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1300 AALNAAKEKALQQLREQLEGERKEAVATLEKEhSAELERLCSSLeakhREVVSSLQK---------KIQEAQQKEEAQLQ 1370
Cdd:TIGR00606 414 CADLQSKERLKQEQADEIRDEKKGLGRTIELK-KEILEKKQEEL----KFVIKELQQlegssdrilELDQELRKAERELS 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1371 KClgQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEGEHErrLDKMKEEHQQVMAKAREQYEAEER------KQRAELLG 1444
Cdd:TIGR00606 489 KA--EKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQ--LNHHTTTRTQMEMLTKDKMDKDEQirkiksRHSDELTS 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1445 HL-----TGELERLQRAHERELETVR------QEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARlallEVQEET 1513
Cdd:TIGR00606 565 LLgyfpnKKQLEDWLHSKSKEINQTRdrlaklNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS----QDEESD 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1514 ARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSS 1593
Cdd:TIGR00606 641 LERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKK 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1594 LEAEaqkKQHLLREVTVEENnasphfEPDLHIEDLRKSlgTNQTKEVSSSLSQSKEDLYLDSlsshnvwHLLSAEGVALR 1673
Cdd:TIGR00606 721 KEKR---RDEMLGLAPGRQS------IIDLKEKEIPEL--RNKLQKVNRDIQRLKNDIEEQE-------TLLGTIMPEEE 782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1674 SAKEFLVQQTrSMRRRQTALKAAQQHWRHELASAQEVAKDppgiKALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEE 1753
Cdd:TIGR00606 783 SAKVCLTDVT-IMERFQMELKDVERKIAQQAAKLQGSDLD----RTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQE 857
|
650 660
....*....|....*....|
gi 530397889 1754 KLNQLESSLWEEASDEGTLG 1773
Cdd:TIGR00606 858 QIQHLKSKTNELKSEKLQIG 877
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1010-1577 |
8.18e-09 |
|
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: 61.14 E-value: 8.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1010 DKDDSQSSQDELQSKQSKGLEERLspplphEERAQSPPRSLAT-EEEPPQGPEGQPEWKEAEELGEDSAASLSLQLSLQR 1088
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCT------PCMPDTYHERKQVlEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQ 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1089 EQapsppaacekgKEQHSQAEELGPGQEEAEDPEEKVAVSP-TPPVSPEVRSTEPVAPPEQLSEAALKAMEEAVAQVLEQ 1167
Cdd:TIGR00618 261 LL-----------KQLRARIEELRAQEAVLEETQERINRARkAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1168 DQRHL-----LESKQEKMQQL-----------------REKLCQEEEEE--ILRLHQQKE------QSLSSLRERLQK-- 1215
Cdd:TIGR00618 330 RAAHVkqqssIEEQRRLLQTLhsqeihirdahevatsiREISCQQHTLTqhIHTLQQQKTtltqklQSLCKELDILQReq 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1216 -------------AIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELE--------SQQKAERA 1274
Cdd:TIGR00618 410 atidtrtsafrdlQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQqlqtkeqiHLQETRKK 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1275 SLEQKNRQMLEQLKEEIEASEKSEQAALNAAKE-KALQQLREQLEGERK---EAVATLEKEHSAELERLcSSLEAKHREV 1350
Cdd:TIGR00618 490 AVVLARLLELQEEPCPLCGSCIHPNPARQDIDNpGPLTRRMQRGEQTYAqleTSEEDVYHQLTSERKQR-ASLKEQMQEI 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1351 VSSLQKKIQEAQQ-KEEAQ-LQKCLGQVEHRVHQKSyhvagyEHELSSLLREKRQEVEGEHERRL--------DKMKEEH 1420
Cdd:TIGR00618 569 QQSFSILTQCDNRsKEDIPnLQNITVRLQDLTEKLS------EAEDMLACEQHALLRKLQPEQDLqdvrlhlqQCSQELA 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1421 QQVMAKAREQYEAEERKQRAELLGHLTGELERLQR--AHERELE-----------------TVRQEQHKRLEDLRRRHRE 1481
Cdd:TIGR00618 643 LKLTALHALQLTLTQERVREHALSIRVLPKELLASrqLALQKMQsekeqltywkemlaqcqTLLRELETHIEEYDREFNE 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1482 QERKLQDLELDLETRAKdvkarlALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQkehtHLLQSNQQLRE 1561
Cdd:TIGR00618 723 IENASSSLGSDLAARED------ALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELS----HLAAEIQFFNR 792
|
650
....*....|....*.
gi 530397889 1562 ILDELQARKLKLESQV 1577
Cdd:TIGR00618 793 LREEDTHLLKTLEAEI 808
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1457-1774 |
9.82e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 9.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1457 HERELETVR-----QEQHKRLEDLRRrhrEQERKLQDLEL---------DLETRAKDVKARLALLEVQEETARRE--KQQ 1520
Cdd:TIGR02168 171 KERRKETERklertRENLDRLEDILN---ELERQLKSLERqaekaerykELKAELRELELALLVLRLEELREELEelQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1521 LLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAE--- 1597
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQlee 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1598 -AQKKQHLLREVT-VEENNASphFEPDlhIEDLRKSLGT-NQTKEVSSSLSQSKEDLYLDslsshnvwhlLSAEGVALRS 1674
Cdd:TIGR02168 328 lESKLDELAEELAeLEEKLEE--LKEE--LESLEAELEElEAELEELESRLEELEEQLET----------LRSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1675 AKEFLVQQTRSMRRRQTALKAAQQHWRHELASAQEVAKDPpgikALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEK 1754
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA----ELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
330 340
....*....|....*....|
gi 530397889 1755 LNQLESSLWEEASDEGTLGG 1774
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQA 489
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1151-1616 |
1.44e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 60.19 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1151 EAALKAMEEAVAQVLEQDQRHLLESKQekmqqLREKLCQEEEEeiLRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQ 1230
Cdd:pfam01576 130 EAKIKKLEEDILLLEDQNSKLSKERKL-----LEERISEFTSN--LAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1231 RLSWLRAQVQSSTQADE--DQIR------AEQEASLQKLREELES------QQKAERASLEQKNRQMLEQLKEEIEASEk 1296
Cdd:pfam01576 203 RQELEKAKRKLEGESTDlqEQIAelqaqiAELRAQLAKKEEELQAalarleEETAQKNNALKKIRELEAQISELQEDLE- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1297 SEQAALNAAkEKALQQLREQLEGERKEAVATL-----EKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQK 1371
Cdd:pfam01576 282 SERAARNKA-EKQRRDLGEELEALKTELEDTLdttaaQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1372 CLGQVEHRVHQKS---YHVAGYEHELSSLLREKR--QEVEGEHERRLDKMKEEHQQVMAKAREQyeAEERKQRAELLGHL 1446
Cdd:pfam01576 361 LTEQLEQAKRNKAnleKAKQALESENAELQAELRtlQQAKQDSEHKRKKLEGQLQELQARLSES--ERQRAELAEKLSKL 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1447 TGELERLQRAHErELETVRQEQHKRLEDLrrrhreqERKLQDLE--LDLETRAK------------DVKARLALLEVQEE 1512
Cdd:pfam01576 439 QSELESVSSLLN-EAEGKNIKLSKDVSSL-------ESQLQDTQelLQEETRQKlnlstrlrqledERNSLQEQLEEEEE 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1513 TARREKQQLLDVQRQVA---LKSEEATATHQQLEEAQKEHTHLLQS-NQQLRE---ILDELQARKLKLESQVDLLQAQSQ 1585
Cdd:pfam01576 511 AKRNVERQLSTLQAQLSdmkKKLEEDAGTLEALEEGKKRLQRELEAlTQQLEEkaaAYDKLEKTKNRLQQELDDLLVDLD 590
|
490 500 510
....*....|....*....|....*....|.
gi 530397889 1586 QLQKHFSSLEaeaqKKQHLLREVTVEENNAS 1616
Cdd:pfam01576 591 HQRQLVSNLE----KKQKKFDQMLAEEKAIS 617
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1299-1537 |
1.92e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1299 QAALNAAKEKALQQLREQLEgERKEAVATLEKEHSAELERLcssleAKHREVVSSLQKKIQEAQQkEEAQLQKCLGQVEH 1378
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIA-ELEKELAALKKEEKALLKQL-----AALERRIAALARRIRALEQ-ELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1379 RVHQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRahe 1458
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA--- 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530397889 1459 rELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATA 1537
Cdd:COG4942 168 -ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1272-1769 |
2.25e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.67 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1272 ERAS--------LEQKNRQMLEQLKEEIEASEKSE-QAALNAAkEKALQQLREQL---EGERKEAVATLEK------EHS 1333
Cdd:PRK02224 169 ERASdarlgverVLSDQRGSLDQLKAQIEEKEEKDlHERLNGL-ESELAELDEEIeryEEQREQARETRDEadevleEHE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1334 AELERLcSSLEAKHREvvssLQKKIQEAQQKEEAqlqkclgqVEHRVHQKSYHVAGYEHELSSLLREkrQEVEGEHERRL 1413
Cdd:PRK02224 248 ERREEL-ETLEAEIED----LRETIAETEREREE--------LAEEVRDLRERLEELEEERDDLLAE--AGLDDADAEAV 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1414 DKMKEEHQQVMAKAREQYEaEERKQRAELLGHLTGELERLQRAHER--ELETVRQEQHKRLEDLRRRHREQERKLQDLEL 1491
Cdd:PRK02224 313 EARREELEDRDEELRDRLE-ECRVAAQAHNEEAESLREDADDLEERaeELREEAAELESELEEAREAVEDRREEIEELEE 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1492 DLEtrakDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQS------NQQLR----- 1560
Cdd:PRK02224 392 EIE----ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecGQPVEgsphv 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1561 EILDELQARKLKLESQVDLLQAQSQQLQKHFSSLE--AEAQKKQHLLREV--TVEEnnasphfepdlHIEDLRKSLgtNQ 1636
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDLEEEVEEVEERLERAEdlVEAEDRIERLEERreDLEE-----------LIAERRETI--EE 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1637 TKEVSSSLSQSKEDlyldslsshnvwhlLSAEGVALRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELASAQEVAKDPPG 1716
Cdd:PRK02224 535 KRERAEELRERAAE--------------LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAA 600
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 530397889 1717 IKALEDMRKNLEKETRHLDEMKSAMRKghnLLKKKEEKLNQLESSLWEEASDE 1769
Cdd:PRK02224 601 IADAEDEIERLREKREALAELNDERRE---RLAEKRERKRELEAEFDEARIEE 650
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1389-1737 |
2.52e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1389 GYEHELSSLLREKRqEVEGEHERRLDKMKEEHQQV--MAKAREQYEAEERKQRAELlghltGELERLQRAHERELETVRQ 1466
Cdd:TIGR02169 685 GLKRELSSLQSELR-RIENRLDELSQELSDASRKIgeIEKEIEQLEQEEEKLKERL-----EELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1467 EqhkrLEDLRRRHREQERKLQDLELDLEtrakDVKARLALLEVQEETARREKQQLlDVQRQVAlkseeatathqQLEEAQ 1546
Cdd:TIGR02169 759 E----LKELEARIEELEEDLHKLEEALN----DLEARLSHSRIPEIQAELSKLEE-EVSRIEA-----------RLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1547 KEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLREVTVEennasphfepdlhIE 1626
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR-------------LG 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1627 DLRKslgtnQTKEVSSSLSQSKEdlyldslsshnvwhllsaegvALRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELAS 1706
Cdd:TIGR02169 886 DLKK-----ERDELEAQLRELER---------------------KIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDP 939
|
330 340 350
....*....|....*....|....*....|.
gi 530397889 1707 AQEVAKDPPGIKALEDMRKNLEKETRHLDEM 1737
Cdd:TIGR02169 940 KGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1231-1576 |
2.93e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.28 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1231 RLSWLRAQVQSSTQADEDQIRAEQEASLQKLREEL---ESQQKAERASLEQKN---------RQMLEQLKEEIEASEKSE 1298
Cdd:PRK02224 188 SLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIeryEEQREQARETRDEADevleeheerREELETLEAEIEDLRETI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1299 qaalnAAKEKALQQLREQLEgERKEAVATLEKEHSAELERlcSSLEAKHREVVSSLqkkiQEAQQKEEAQLQKCLGQVEH 1378
Cdd:PRK02224 268 -----AETEREREELAEEVR-DLRERLEELEEERDDLLAE--AGLDDADAEAVEAR----REELEDRDEELRDRLEECRV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1379 RVHQKSYHVAGYEHELSSL------LREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEER-----KQRAELLGHLT 1447
Cdd:PRK02224 336 AAQAHNEEAESLREDADDLeeraeeLREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapVDLGNAEDFLE 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1448 GELERLQRAHER--ELETVRQEQHKRLEDLRR------------------------RHREQERKLQDLELDLETRAKDVK 1501
Cdd:PRK02224 416 ELREERDELREReaELEATLRTARERVEEAEAlleagkcpecgqpvegsphvetieEDRERVEELEAELEDLEEEVEEVE 495
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530397889 1502 ARLALLEVQEETARR---EKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREildelQARKLKLESQ 1576
Cdd:PRK02224 496 ERLERAEDLVEAEDRierLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKRE-----AAAEAEEEAE 568
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1147-1765 |
3.07e-08 |
|
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: 59.21 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1147 EQLSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMRE 1226
Cdd:pfam02463 287 ELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1227 EESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERAS--LEQKNRQMLEQLKEEIEASEKSEQAALNA 1304
Cdd:pfam02463 367 KLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARqlEDLLKEEKKEELEILEEEEESIELKQGKL 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1305 AKEKALQQLRE------QLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQK---CLGQ 1375
Cdd:pfam02463 447 TEEKEELEKQElkllkdELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGvggRIIS 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1376 VEHRVHQKSYHVAGYEHELSSLL-----REKRQEVEGEHERR---------------LDKMKEEHQQVMAKAREQYEAEE 1435
Cdd:pfam02463 527 AHGRLGDLGVAVENYKVAISTAVivevsATADEVEERQKLVRaltelplgarklrllIPKLKLPLKSIAVLEIDPILNLA 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1436 RKQRAELLGHLTGELERLQRAHERE-LETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEetA 1514
Cdd:pfam02463 607 QLDKATLEADEDDKRAKVVEGILKDtELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQE--K 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1515 RREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQvDLLQAQSQQLQKHFSSL 1594
Cdd:pfam02463 685 AESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKID-EEEEEEEKSRLKKEEKE 763
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1595 EAEAQKKQHLLREVTVEENNASPHFEPDLHIEDLRKSLG-TNQTKEVSSSLSQSKEDLYLDSLSSH---NVWHLLSAEGV 1670
Cdd:pfam02463 764 EEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEElRALEEELKEEAELLEEEQLLIEQEEKikeEELEELALELK 843
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1671 ALRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELASAQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSAMRKGHNLLKK 1750
Cdd:pfam02463 844 EEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERI 923
|
650
....*....|....*
gi 530397889 1751 KEEKLNQLESSLWEE 1765
Cdd:pfam02463 924 KEEAEILLKYEEEPE 938
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1409-1578 |
4.29e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1409 HERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELEtvRQEQHKRLEDLRRRHREQERKLQD 1488
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE--KLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1489 LEldleTRAKDVKARLALLEVQEETARREKQQLLDVQRQVA-LKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQ 1567
Cdd:COG4717 144 LP----ERLEELEERLEELRELEEELEELEAELAELQEELEeLLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170
....*....|.
gi 530397889 1568 ARKLKLESQVD 1578
Cdd:COG4717 220 EELEELEEELE 230
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1252-1511 |
4.32e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 4.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1252 AEQEASLQKLREELESQQKA-ERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKaLQQLREQLEGERKEaVATLEK 1330
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVlKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEE-YEKLKEKLIKLKGE-IKSLKK 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1331 EHS--AELERLCSSLEAKHREV---VSSLQKKIQEAQQKEEAQLQKCLGQVEhRVHQKSYHVAGYEHELSSLLREKRQEv 1405
Cdd:PRK03918 547 ELEklEELKKKLAELEKKLDELeeeLAELLKELEELGFESVEELEERLKELE-PFYNEYLELKDAEKELEREEKELKKL- 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1406 egehERRLDKMKEEHQQVMAKARE----------QYEAEERKQRAELLGHLTGELERLqRAHERELETVRQEQHKRLEDL 1475
Cdd:PRK03918 625 ----EEELDKAFEELAETEKRLEElrkeleelekKYSEEEYEELREEYLELSRELAGL-RAELEELEKRREEIKKTLEKL 699
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 530397889 1476 RRRHREQERKLQDLEL---------DLETRAKDVKARL---ALLEVQE 1511
Cdd:PRK03918 700 KEELEEREKAKKELEKlekalerveELREKVKKYKALLkerALSKVGE 747
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1349-1765 |
5.04e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1349 EVVSSLQKKIQEAQQ--KEEAQLQKCLGQVEHRVHQKSYHVagyeHELSSLLREKRQEVEGEHER--RLDKMKEEhqqvM 1424
Cdd:PRK03918 169 EVIKEIKRRIERLEKfiKRTENIEELIKEKEKELEEVLREI----NEISSELPELREELEKLEKEvkELEELKEE----I 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1425 AKAREQYEAEERKQRA--ELLGHLTGELERLqRAHERELETVRQE---------QHKRLEDLRRRHREQERKLQDLELDL 1493
Cdd:PRK03918 241 EELEKELESLEGSKRKleEKIRELEERIEEL-KKEIEELEEKVKElkelkekaeEYIKLSEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1494 ETRAKDVKARLALLEVQEETARREKQQLLDVQRQV------ALKSEEATATHQQLEEAQKEHTHLlqSNQQLREILDELQ 1567
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKELEKRLeeleerHELYEEAKAKKEELERLKKRLTGL--TPEKLEKELEELE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1568 ARKLKLESQVDLLQAQSQQLQKHFSSLEA------EAQKKQHLL-REVTveennasphfepdlhiEDLRKSLGTNQTKEV 1640
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKKaieelkKAKGKCPVCgRELT----------------EEHRKELLEEYTAEL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1641 SSSLSQSKEdlyLDSLSSHnvwhlLSAEGVALRSakeFLVQQTRSMRRRQTA--LKAAQQHWR-HELASAQEVAKDPPGI 1717
Cdd:PRK03918 462 KRIEKELKE---IEEKERK-----LRKELRELEK---VLKKESELIKLKELAeqLKELEEKLKkYNLEELEKKAEEYEKL 530
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 530397889 1718 K----ALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSLWEE 1765
Cdd:PRK03918 531 KekliKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1257-1515 |
5.14e-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: 5.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1257 SLQKLREELES-QQKAERAsleQKNRQMLEQLKEEIE--ASEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKEHS 1333
Cdd:COG4913 229 ALVEHFDDLERaHEALEDA---REQIELLEPIRELAEryAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1334 AELERL--CSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSLlrekrQEVEGEHER 1411
Cdd:COG4913 306 RLEAELerLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL-----GLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1412 RLDKMKEEHQQvmakAREQYEAEERKQRAELlghltGELERLQRAHERELETVRQEqhkrLEDLRRRHREQERKLQDLEL 1491
Cdd:COG4913 381 EFAALRAEAAA----LLEALEEELEALEEAL-----AEAEAALRDLRRELRELEAE----IASLERRKSNIPARLLALRD 447
|
250 260
....*....|....*....|....*...
gi 530397889 1492 DLETRAKDVKARLA----LLEVQEETAR 1515
Cdd:COG4913 448 ALAEALGLDEAELPfvgeLIEVRPEEER 475
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1164-1534 |
5.18e-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: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1164 VLEQDQRHLLESKQEKMQQLREKLcQEEEEEILRLHQQKEQsLSSLRERLQKAIEEEEARMREEESQR-LSWLRAQVQSS 1242
Cdd:COG4913 603 VLGFDNRAKLAALEAELAELEEEL-AEAEERLEALEAELDA-LQERREALQRLAEYSWDEIDVASAEReIAELEAELERL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1243 TQADED-----QIRAEQEASLQKLREELEsQQKAERASLEQKnrqmLEQLKEEIEASekseQAALNAAKEKALQQLREQL 1317
Cdd:COG4913 681 DASSDDlaaleEQLEELEAELEELEEELD-ELKGEIGRLEKE----LEQAEEELDEL----QDRLEAAEDLARLELRALL 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1318 EGERKEA-VATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQkclgqvEHRVHQKSYHvaGYEHELSS 1396
Cdd:COG4913 752 EERFAAAlGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETA------DLDADLESLP--EYLALLDR 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1397 LLREKRQEVEGEHERRLDKMKEEH----QQVMAKAREqyEAEERkqraelLGHLTGELERLQRAHERELE-TVRQEQHKR 1471
Cdd:COG4913 824 LEEDGLPEYEERFKELLNENSIEFvadlLSKLRRAIR--EIKER------IDPLNDSLKRIPFGPGRYLRlEARPRPDPE 895
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530397889 1472 LEDLRRRHREQERKLQDLELDL-ETRAKDVKARLALLEVQE-ETARREKQQLLDVQRQVALKSEE 1534
Cdd:COG4913 896 VREFRQELRAVTSGASLFDEELsEARFAALKRLIERLRSEEeESDRRWRARVLDVRNHLEFDAEE 960
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1255-1489 |
5.29e-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: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1255 EASLQKLRE---ELESQQKAERASlEQKNRQMLEQLKEEIEASEK-SEQAALNAAKEKA--LQQLREQLEgERKEAVATL 1328
Cdd:COG3096 835 EAELAALRQrrsELERELAQHRAQ-EQQLRQQLDQLKEQLQLLNKlLPQANLLADETLAdrLEELREELD-AAQEAQAFI 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1329 EK--EHSAELERLCSSLEAKhREVVSSLQKKIQEAQQKEEAQLQKC--LGQVEHRVHQKSYHVA----GYEHELSSLLRE 1400
Cdd:COG3096 913 QQhgKALAQLEPLVAVLQSD-PEQFEQLQADYLQAKEQQRRLKQQIfaLSEVVQRRPHFSYEDAvgllGENSDLNEKLRA 991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1401 KRQEVEGEHERRLDKMK------EEHQQVMAKAREQYEAeerkqRAELLGHLTGELERL---------QRAHER------ 1459
Cdd:COG3096 992 RLEQAEEARREAREQLRqaqaqySQYNQVLASLKSSRDA-----KQQTLQELEQELEELgvqadaeaeERARIRrdelhe 1066
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 530397889 1460 ----------ELETVRQEQHKRLEDLRRRHREQERKLQDL 1489
Cdd:COG3096 1067 elsqnrsrrsQLEKQLTRCEAEMDSLQKRLRKAERDYKQE 1106
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1354-1761 |
5.49e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 5.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1354 LQKKIQEAQQKEE--AQLQKCLGQVEHRVHQKSYHVAGYEHELSSL-----LREKRQEVEgEHERRLDKMKEEHQQVMAK 1426
Cdd:COG4717 76 LEEELKEAEEKEEeyAELQEELEELEEELEELEAELEELREELEKLekllqLLPLYQELE-ALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1427 AREQYEAEERKQRAEllghltGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLET---RAKDVKAR 1503
Cdd:COG4717 155 LEELRELEEELEELE------AELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEaqeELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1504 LALLEVQEETArREKQQLLDVQRQVALKSE--EATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQvdllq 1581
Cdd:COG4717 229 LEQLENELEAA-ALEERLKEARLLLLIAAAllALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK----- 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1582 aqsqqlqkhfSSLEAEAQKKQHLLREVTVEENNASPHFEPDLHIEDLRKSLGT-NQTKEVSSSLSQSKEDLYLDSLSSHN 1660
Cdd:COG4717 303 ----------EAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRiEELQELLREAEELEEELQLEELEQEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1661 VwHLLSAEGVALRSAKEFLVQQTrsmrRRQTALKAAQQHWRHELASAQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSA 1740
Cdd:COG4717 373 A-ALLAEAGVEDEEELRAALEQA----EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEE 447
|
410 420
....*....|....*....|.
gi 530397889 1741 MRKGHNLLKKKEEKLNQLESS 1761
Cdd:COG4717 448 LEELREELAELEAELEQLEED 468
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1232-1467 |
8.11e-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: 8.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1232 LSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQknrqmLEQLKEEIEASEK------SEQAALNA- 1304
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ-----LAALERRIAALARriraleQELAALEAe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1305 -----AKEKALQQLREQLEGERKEAVATLEKEHSA-ELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEH 1378
Cdd:COG4942 85 laeleKEIAELRAELEAQKEELAELLRALYRLGRQpPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1379 RVHQKSYHVAgyehELSSLLREKRQEvegehERRLDKMKEEHQQVMAKAREQYEAEErkQRAELLGHLTGELERLQRAHE 1458
Cdd:COG4942 165 LRAELEAERA----ELEALLAELEEE-----RAALEALKAERQKLLARLEKELAELA--AELAELQQEAEELEALIARLE 233
|
....*....
gi 530397889 1459 RELETVRQE 1467
Cdd:COG4942 234 AEAAAAAER 242
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1041-1365 |
8.88e-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: 57.46 E-value: 8.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1041 ERAQSPPRSLATEEEPPQGPEGQPEWKEAEELGEDsaaslslqlslqreQAPSPPAACEKGKEQHSQAEELGPgQEEAED 1120
Cdd:pfam09731 76 TGESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATK--------------DAAEAKAQLPKSEQEKEKALEEVL-KEAISK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1121 PEEKVAVSPTPPVSPEVRSTEPVAPPEQLSEAALKAMEEAVAQVLeqdqrHLLESKQEKMQQLREKLCQEEEEEILRLHQ 1200
Cdd:pfam09731 141 AESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSAL-----QKAEALAEKLKEVINLAKQSEEEAAPPLLD 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1201 QKEQSLSSLRERLQKAIEEEEArmreeeSQRLSWLRAQVQSSTqADEDQIRAEQEAS----------------------- 1257
Cdd:pfam09731 216 AAPETPPKLPEHLDNVEEKVEK------AQSLAKLVDQYKELV-ASERIVFQQELVSifpdiipvlkednllsnddlnsl 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1258 -------LQKLREELESQQKAERASLEQKnrqmLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEK 1330
Cdd:pfam09731 289 iahahreIDQLSKKLAELKKREEKHIERA----LEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEE 364
|
330 340 350
....*....|....*....|....*....|....*
gi 530397889 1331 EHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKE 1365
Cdd:pfam09731 365 KLRTELERQAEAHEEHLKDVLVEQEIELQREFLQD 399
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1154-1532 |
9.02e-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: 9.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1154 LKAMEEAVAQVLEQDQrhllESKQEKMQQLREKlcqeeeeeILRLHQQKEQ---SLSSLRERLQKAIeeeearmreeesQ 1230
Cdd:COG5185 248 LAQTSDKLEKLVEQNT----DLRLEKLGENAES--------SKRLNENANNlikQFENTKEKIAEYT------------K 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1231 RLSWLRAQVQSSTQADedqiRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKE----------EIEASEKSEQA 1300
Cdd:COG5185 304 SIDIKKATESLEEQLA----AAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAikeeienivgEVELSKSSEEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1301 -----ALNAAKEKALQQLREQlEGERKEAVATLE---KEHSAELERLCSSLEAKHREVvsslqkkiqEAQQKEEAQLQKC 1372
Cdd:COG5185 380 dsfkdTIESTKESLDEIPQNQ-RGYAQEILATLEdtlKAADRQIEELQRQIEQATSSN---------EEVSKLLNELISE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1373 LGQVEHRVhqksyhvagyEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREqyeaeerkqraellghLTGELER 1452
Cdd:COG5185 450 LNKVMREA----------DEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVST----------------LKATLEK 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1453 LQRAHERELETVRQEQHKRLEDLRRRHREQErklQDLELDLETRAKDVKARLALLE--VQEETARREKQQLLDVQRQVAL 1530
Cdd:COG5185 504 LRAKLERQLEGVRSKLDQVAESLKDFMRARG---YAHILALENLIPASELIQASNAktDGQAANLRTAVIDELTQYLSTI 580
|
..
gi 530397889 1531 KS 1532
Cdd:COG5185 581 ES 582
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1149-1337 |
1.92e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 55.94 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1149 LSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKlcqeeeeeILRLHQQKEQSLSSLRERLQkaieeeearmreee 1228
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEE--------IHKLRNEFEKELRERRNELQ-------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1229 sqrlswlraQVQSSTQADEDQIRAEQEaSLQKLREELESQQKaeraSLEQKNRQmLEQLKEEIEASEKSEQAAL----NA 1304
Cdd:PRK12704 86 ---------KLEKRLLQKEENLDRKLE-LLEKREEELEKKEK----ELEQKQQE-LEKKEEELEELIEEQLQELerisGL 150
|
170 180 190
....*....|....*....|....*....|....*
gi 530397889 1305 AKEKALQQLREQLEGE-RKEAVATL-EKEHSAELE 1337
Cdd:PRK12704 151 TAEEAKEILLEKVEEEaRHEAAVLIkEIEEEAKEE 185
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1235-1374 |
2.18e-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: 53.53 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1235 LRAQVQSSTQADED------QIRAEQEASLQKLREELEsQQKAERASLEQKnrqmLEQLKEEIEASEKSEQAALNAAKE- 1307
Cdd:pfam04012 9 VRANIHEGLDKAEDpekmleQAIRDMQSELVKARQALA-QTIARQKQLERR----LEQQTEQAKKLEEKAQAALTKGNEe 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530397889 1308 ---KALQQlREQLEG--ERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQK-KIQEAQQKEEAQLQKCLG 1374
Cdd:pfam04012 84 larEALAE-KKSLEKqaEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLlKARLKAAKAQEAVQTSLG 155
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1288-1766 |
2.69e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1288 KEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKEHSAElerlcsslEAKHREVVsslqKKIQEAQQKEEA 1367
Cdd:PTZ00121 1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAE--------EARKAEDA----RKAEEARKAEDA 1151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1368 QLQKCLGQVEhrvhqksyhvagyEHELSSLLREKRQEVEGEHERRLDKMKEEHQqvMAKAREQYEAEERKQRAELLghlt 1447
Cdd:PTZ00121 1152 KRVEIARKAE-------------DARKAEEARKAEDAKKAEAARKAEEVRKAEE--LRKAEDARKAEAARKAEEER---- 1212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1448 gELERLQRAHE-RELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQR 1526
Cdd:PTZ00121 1213 -KAEEARKAEDaKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKK 1291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1527 QVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLR 1606
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1607 EVTVEENNASphfEPDLHIEDLRKSlgtNQTKEVSSSLSQSKEDLYLDSLSSHNVwHLLSAEGVALRSAKEfLVQQTRSM 1686
Cdd:PTZ00121 1372 KKEEAKKKAD---AAKKKAEEKKKA---DEAKKKAEEDKKKADELKKAAAAKKKA-DEAKKKAEEKKKADE-AKKKAEEA 1443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1687 RRRQTALKAAQqhwrhELASAQEVAKDPPGIKALEDMRKNLEkETRHLDEMK----SAMRKGHNLLKKKEEKLNQLESSL 1762
Cdd:PTZ00121 1444 KKADEAKKKAE-----EAKKAEEAKKKAEEAKKADEAKKKAE-EAKKADEAKkkaeEAKKKADEAKKAAEAKKKADEAKK 1517
|
....
gi 530397889 1763 WEEA 1766
Cdd:PTZ00121 1518 AEEA 1521
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1165-1577 |
3.21e-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: 55.80 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1165 LEQDQRHLLESKQEKMQQLREKlcqeeEEEILRLHQQKEQSLSSL---RERLQKAIEEEEARmreeeSQRLSWLRAQVQS 1241
Cdd:TIGR04523 223 LKKQNNQLKDNIEKKQQEINEK-----TTEISNTQTQLNQLKDEQnkiKKQLSEKQKELEQN-----NKKIKELEKQLNQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1242 STQADEDQIRAEQEASLQKLREELESQQKAERASLEQ--KNRQMLEQLKEEIEASEKSEQAalnaaKEKALQQLREQLEg 1319
Cdd:TIGR04523 293 LKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQisQNNKIISQLNEQISQLKKELTN-----SESENSEKQRELE- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1320 ERKEAVATLEKEHSAELERLcSSLEAKHREVVSSLQKKIQEAQQKEE--AQLQKCLGQVEHRVHQKSYHVAGYEHELSSL 1397
Cdd:TIGR04523 367 EKQNEIEKLKKENQSYKQEI-KNLESQINDLESKIQNQEKLNQQKDEqiKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1398 lREKRQEVEGEHERrLDKMKEEHQQVMAKAREQYEAEER--KQRAELLGHLTGELERLQRaHERELE------TVRQEQH 1469
Cdd:TIGR04523 446 -TNQDSVKELIIKN-LDNTRESLETQLKVLSRSINKIKQnlEQKQKELKSKEKELKKLNE-EKKELEekvkdlTKKISSL 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1470 K-RLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQE---------------ETARREKQQLL--------DVQ 1525
Cdd:TIGR04523 523 KeKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEknkeieelkqtqkslKKKQEEKQELIdqkekekkDLI 602
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 530397889 1526 RQVALKSEEATATHQQLEEAQKEhthllqsNQQLREILDELQARKLKLESQV 1577
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEKAKKE-------NEKLSSIIKNIKSKKNKLKQEV 647
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1252-1441 |
3.45e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 55.17 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1252 AEQEASLQKLREELESQQKAERASLEQKnrQMLEQLKEEIEAsEKSEQAALNAAKEKALQQLREQLEgERKEAvatLEKE 1331
Cdd:PRK12704 36 AEEEAKRILEEAKKEAEAIKKEALLEAK--EEIHKLRNEFEK-ELRERRNELQKLEKRLLQKEENLD-RKLEL---LEKR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1332 hSAELERLCSSLEAKHREvvssLQKKIQEAQQKEEAQLQKCLgqvehrvhqksyHVAGYEHElssllrEKRQEVegeher 1411
Cdd:PRK12704 109 -EEELEKKEKELEQKQQE----LEKKEEELEELIEEQLQELE------------RISGLTAE------EAKEIL------ 159
|
170 180 190
....*....|....*....|....*....|
gi 530397889 1412 rLDKMKEEHQQVMAKAREQYEaEERKQRAE 1441
Cdd:PRK12704 160 -LEKVEEEARHEAAVLIKEIE-EEAKEEAD 187
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1167-1578 |
4.30e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.35 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1167 QDQRHLLESKQEKMQQLREKLcqeeeEEILRLHQQKEQSLSSLRERLQKaieeeearmreeesqrlswlraqVQSSTQAD 1246
Cdd:PRK04863 296 YTSRRQLAAEQYRLVEMAREL-----AELNEAESDLEQDYQAASDHLNL-----------------------VQTALRQQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1247 EDQIRAEqeASLQKLREELESQQKAERASLEQK--NRQMLEQLKEEIEaSEKSE----QAALNAAKEKALQQlreqlege 1320
Cdd:PRK04863 348 EKIERYQ--ADLEELEERLEEQNEVVEEADEQQeeNEARAEAAEEEVD-ELKSQladyQQALDVQQTRAIQY-------- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1321 rKEAVATLEKehsaeLERLC--SSLEAKhrevvsSLQKKIQEAQQKEEAQLQKCLgQVEHRVHQKSYHVAGYEHELSSLL 1398
Cdd:PRK04863 417 -QQAVQALER-----AKQLCglPDLTAD------NAEDWLEEFQAKEQEATEELL-SLEQKLSVAQAAHSQFEQAYQLVR 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1399 RekrqeVEGEHERrldkmKEEHQQVMAKAREqyeAEERKQRAELLGHLTGELERLQRahereletvRQEQHKRLEDLRR- 1477
Cdd:PRK04863 484 K-----IAGEVSR-----SEAWDVARELLRR---LREQRHLAEQLQQLRMRLSELEQ---------RLRQQQRAERLLAe 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1478 ------RHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQL-LDVQR-----------QVAL-----KSEE 1534
Cdd:PRK04863 542 fckrlgKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLqARIQRlaarapawlaaQDALarlreQSGE 621
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 530397889 1535 ATATHQQLEEAQKEHTHLLQSNQQLReilDELQARKLKLESQVD 1578
Cdd:PRK04863 622 EFEDSQDVTEYMQQLLERERELTVER---DELAARKQALDEEIE 662
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1236-1596 |
4.38e-07 |
|
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: 55.34 E-value: 4.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1236 RAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERAsLE---QKNRQMLEQLKEEIEASEKSE--QAALNAAKEKAL 1310
Cdd:COG3096 286 RALELRRELFGARRQLAEEQYRLVEMARELEELSARESD-LEqdyQAASDHLNLVQTALRQQEKIEryQEDLEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1311 QQ--LREQLEGERKEAVATLEkEHSAELERLCSSLeAKHREVVSSLQKKIQEAQQKEEAqlqkcLGQVEHRVHQKSYHVA 1388
Cdd:COG3096 365 EQeeVVEEAAEQLAEAEARLE-AAEEEVDSLKSQL-ADYQQALDVQQTRAIQYQQAVQA-----LEKARALCGLPDLTPE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1389 GYEHELSSLlREKRQEVegeHERRLDKmkEEHQQVMAKAREQYEaeerkQRAELLGHLTGELERLQrAHE--RE-LETVR 1465
Cdd:COG3096 438 NAEDYLAAF-RAKEQQA---TEEVLEL--EQKLSVADAARRQFE-----KAYELVCKIAGEVERSQ-AWQtaRElLRRYR 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1466 QEQH--KRLEDLRRRHREQERKL---QDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQ 1540
Cdd:COG3096 506 SQQAlaQRLQQLRAQLAELEQRLrqqQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQ 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1541 QLEE-----------------AQKEHTHL-------LQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEA 1596
Cdd:COG3096 586 QLEQlrarikelaarapawlaAQDALERLreqsgeaLADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQ 665
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1169-1377 |
4.55e-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: 54.38 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1169 QRHLLESKQEKMQQLREKLcqEEEEEILRLHQQKEQSLSSLRERLQKAIEeEEARMREEESQRLSWLRAQVQsSTQADED 1248
Cdd:COG4942 18 QADAAAEAEAELEQLQQEI--AELEKELAALKKEEKALLKQLAALERRIA-ALARRIRALEQELAALEAELA-ELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1249 QIRAEQEASLQKLREELESQQKAERASLEQ------------KNRQMLEQLKEEIEaseksEQAALNAAKEKALQQLREQ 1316
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLAlllspedfldavRRLQYLKYLAPARR-----EQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530397889 1317 LEGERKEaVATLEKEHSAELERLcSSLEAKHREVVSSLQKKIQEAQ------QKEEAQLQKCLGQVE 1377
Cdd:COG4942 169 LEAERAE-LEALLAELEEERAAL-EALKAERQKLLARLEKELAELAaelaelQQEAEELEALIARLE 233
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1147-1562 |
5.51e-07 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 54.53 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1147 EQLSEAALKAMEEAVAQVLEQD-----QRHLLESKQEKMQQLREKLCQ-EEEEEILRLHQQKEQSLSSLRERLQKAIEEE 1220
Cdd:COG5278 113 EALIDQWLAELEQVIALRRAGGleaalALVRSGEGKALMDEIRARLLLlALALAALLLAAAALLLLLLALAALLALAELL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1221 EARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQA 1300
Cdd:COG5278 193 LLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1301 ALNAAKEKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQkclgQVEHRV 1380
Cdd:COG5278 273 LLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAA----ALALLA 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1381 HQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERE 1460
Cdd:COG5278 349 ALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEAL 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1461 LETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQ 1540
Cdd:COG5278 429 AEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAAL 508
|
410 420
....*....|....*....|..
gi 530397889 1541 QLEEAQKEHTHLLQSNQQLREI 1562
Cdd:COG5278 509 LLAAAEAALAAALAAALASAEL 530
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1200-1757 |
5.77e-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: 54.80 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1200 QQKEQSLSSLRERLQKAieeeearmrEEESQRLSWLRAQVQSSTQADEDQIRAEQeaslqklreELESQQKAERASLEQK 1279
Cdd:pfam01576 8 QAKEEELQKVKERQQKA---------ESELKELEKKHQQLCEEKNALQEQLQAET---------ELCAEAEEMRARLAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1280 nRQMLEQLKEEIEA--SEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKEHsaeLERLcsSLEAKhrevvsslQKK 1357
Cdd:pfam01576 70 -KQELEEILHELESrlEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQ---LEKV--TTEAK--------IKK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1358 IQEAQQKEEAQ---LQKCLGQVEHRVHQKSYHVAGYEHELSSL--LREKRQEVEGEHERRLDKmKEEHQQVMAKAREQYE 1432
Cdd:pfam01576 136 LEEDILLLEDQnskLSKERKLLEERISEFTSNLAEEEEKAKSLskLKNKHEAMISDLEERLKK-EEKGRQELEKAKRKLE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1433 AEE----------RKQRAELLGHLTGELERLQRAHER-ELETVRQEQhkrledLRRRHREQERKLQDLELDLET----RA 1497
Cdd:pfam01576 215 GEStdlqeqiaelQAQIAELRAQLAKKEEELQAALARlEEETAQKNN------ALKKIRELEAQISELQEDLESeraaRN 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1498 KDVKARLALLE-----------------VQEETARREKQQLLDVQRQValkSEEATATHQQLEEAQKEHThllQSNQQLR 1560
Cdd:pfam01576 289 KAEKQRRDLGEelealkteledtldttaAQQELRSKREQEVTELKKAL---EEETRSHEAQLQEMRQKHT---QALEELT 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1561 EILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLR--EVTVEENNASpHFEPDLHIEDLRKSLGTNQTK 1638
Cdd:pfam01576 363 EQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKklEGQLQELQAR-LSESERQRAELAEKLSKLQSE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1639 --EVSSSLSQSKEDLY-----LDSLSSHnvwhllsaegvaLRSAKEFLVQQTR-----SMRRRQTALKAA--QQHWRHEL 1704
Cdd:pfam01576 442 leSVSSLLNEAEGKNIklskdVSSLESQ------------LQDTQELLQEETRqklnlSTRLRQLEDERNslQEQLEEEE 509
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 530397889 1705 ASAQEVAKDPPGIKA-LEDMRKNLEKETRHLDEMKSAMRKghnlLKKKEEKLNQ 1757
Cdd:pfam01576 510 EAKRNVERQLSTLQAqLSDMKKKLEEDAGTLEALEEGKKR----LQRELEALTQ 559
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1283-1607 |
6.72e-07 |
|
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: 53.89 E-value: 6.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1283 MLEQLKEEIEASEKSEQAALNAAKEK-ALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEA 1361
Cdd:pfam15558 13 MLARHKEEQRMRELQQQAALAWEELRrRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1362 QQKEEAQLQKclgqVEHRVHQKsyhvagyehelsslLREKRQEVEG---EHERRLdKMKEEHQQVMaKAREQYEAEERKQ 1438
Cdd:pfam15558 93 ESRWREQAED----QENQRQEK--------------LERARQEAEQrkqCQEQRL-KEKEEELQAL-REQNSLQLQERLE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1439 RAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLqDLELDLeTRAKDVKARLALLEVQE--ETARR 1516
Cdd:pfam15558 153 EACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELLRRL-SLEQSL-QRSQENYEQLVEERHRElrEKAQK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1517 EKQQLLDVQRQVALKSEEatathqqleeaQKEHthllqsnqqlREILDELQARKLKLESQVdlLQAQSQQLQKHFSSLEA 1596
Cdd:pfam15558 231 EEEQFQRAKWRAEEKEEE-----------RQEH----------KEALAELADRKIQQARQV--AHKTVQDKAQRARELNL 287
|
330
....*....|.
gi 530397889 1597 EAQKKQHLLRE 1607
Cdd:pfam15558 288 EREKNHHILKL 298
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1154-1524 |
8.08e-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: 8.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1154 LKAMEEAVAQ------VLEQDQRHLLESKQEKMQQLREKLCQ-----EEEEEILRLHQQKEQSLSSLRERLQKAIEEEEA 1222
Cdd:pfam12128 310 LSAADAAVAKdrseleALEDQHGAFLDADIETAAADQEQLPSwqselENLEERLKALTGKHQDVTAKYNRRRSKIKEQNN 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1223 RMREEESQRLSWLR-------AQVQSSTQADEDQIRAEQEASLQKLREE-LESQQKAERASLEQKNRQMLEQLKEEIEAS 1294
Cdd:pfam12128 390 RDIAGIKDKLAKIReardrqlAVAEDDLQALESELREQLEAGKLEFNEEeYRLKSRLGELKLRLNQATATPELLLQLENF 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1295 E------KSEQAALNAAKEkALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHreVVSSLQKKIQEAQQKEEAQ 1368
Cdd:pfam12128 470 DerieraREEQEAANAEVE-RLQSELRQARKRRDQASEALRQASRRLEERQSALDELEL--QLFPQAGTLLHFLRKEAPD 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1369 LQKCLGQVE-----HRVHQKSYHVAGYEHELSSL----LREKRQEV------EGEHERRLDKMKEEHQQVMAKAREQYEA 1433
Cdd:pfam12128 547 WEQSIGKVIspellHRTDLDPEVWDGSVGGELNLygvkLDLKRIDVpewaasEEELRERLDKAEEALQSAREKQAAAEEQ 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1434 eerkqraelLGHLTGELERLQRAHERELETV--------------RQEQHKRLEDLRRRHREQERKLQDLELDLETRAKD 1499
Cdd:pfam12128 627 ---------LVQANGELEKASREETFARTALknarldlrrlfdekQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKK 697
|
410 420
....*....|....*....|....*
gi 530397889 1500 VKARLALLEVQEETARREKQQLLDV 1524
Cdd:pfam12128 698 HQAWLEEQKEQKREARTEKQAYWQV 722
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1169-1609 |
1.13e-06 |
|
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: 54.03 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1169 QRHLLESKQEKMQQLREKLCQEEEE--EILRLHQQKEQSLSSLRERLQK-----AIEEEEARMREEESQRLSWLRAQVQS 1241
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESElkELEKKHQQLCEEKNALQEQLQAetelcAEAEEMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1242 STQADEDQIRAEQ------EASLQKLREELESQQKA------ERASLEQKNRQMLEQL-----------KE----EIEAS 1294
Cdd:pfam01576 83 RLEEEEERSQQLQnekkkmQQHIQDLEEQLDEEEAArqklqlEKVTTEAKIKKLEEDIllledqnsklsKErkllEERIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1295 EKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKEHSA--ELERLCSSLEAKH---REVVSSLQKKIQEAQ---QKEE 1366
Cdd:pfam01576 163 EFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGrqELEKAKRKLEGEStdlQEQIAELQAQIAELRaqlAKKE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1367 AQLQKCLGQVEHRVHQKSyHVAGYEHELSSLLREKRQEVEGEHERR-------------LDKMKEEHQQVMAKAREQYEA 1433
Cdd:pfam01576 243 EELQAALARLEEETAQKN-NALKKIRELEAQISELQEDLESERAARnkaekqrrdlgeeLEALKTELEDTLDTTAAQQEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1434 eeRKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLEldletrakdvKARLALlevqeET 1513
Cdd:pfam01576 322 --RSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLE----------KAKQAL-----ES 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1514 ARREKQQLLDVQRQVALKSEEA-TATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFS 1592
Cdd:pfam01576 385 ENAELQAELRTLQQAKQDSEHKrKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVS 464
|
490
....*....|....*..
gi 530397889 1593 SLEAEAQKKQHLLREVT 1609
Cdd:pfam01576 465 SLESQLQDTQELLQEET 481
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1252-1502 |
1.20e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.19 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1252 AEQEASLQKLREELeSQQKAERASLEQKNRQM---LEQLKEEIEASEKSE-QAAL--NAAKEKALQQLREQLEgERKEAV 1325
Cdd:PRK04863 833 ADPEAELRQLNRRR-VELERALADHESQEQQQrsqLEQAKEGLSALNRLLpRLNLlaDETLADRVEEIREQLD-EAEEAK 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1326 ATLEK--EHSAELERLCSSLEAKHREVvSSLQKKIQEAQQKEEAQLQKC--LGQVEHRVHQKSYHVA----GYEHELSSL 1397
Cdd:PRK04863 911 RFVQQhgNALAQLEPIVSVLQSDPEQF-EQLKQDYQQAQQTQRDAKQQAfaLTEVVQRRAHFSYEDAaemlAKNSDLNEK 989
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1398 LREKRQEVEGEherrLDKMKEEHQQ----------VMAKAREQYEA-----EERKQRAELLG-HLTGELERLQRAHEREL 1461
Cdd:PRK04863 990 LRQRLEQAEQE----RTRAREQLRQaqaqlaqynqVLASLKSSYDAkrqmlQELKQELQDLGvPADSGAEERARARRDEL 1065
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 530397889 1462 etvrqeqHKRLEDLRRRHREQERKLQDLELDLETRAKDVKA 1502
Cdd:PRK04863 1066 -------HARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRK 1099
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
1237-1435 |
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 530397889 1237 AQVQSSTQADEDQIRAEQEAslQKLREELESQQKAERasleQKNRQMLEQLKEEIEASEKSEQAALNaaKEKALQQLREQ 1316
Cdd:PRK00106 62 AKRESKALKKELLLEAKEEA--RKYREEIEQEFKSER----QELKQIESRLTERATSLDRKDENLSS--KEKTLESKEQS 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1317 LE------GERKEAVATLEKEHSAELERLCSSLEAKHREVVsslqkkiqeaqqkeeaqlqkcLGQVEHRVhqksyhvagy 1390
Cdd:PRK00106 134 LTdkskhiDEREEQVEKLEEQKKAELERVAALSQAEAREII---------------------LAETENKL---------- 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 530397889 1391 EHELSSLLREKRQEVegehERRLDKM-KEEHQQVMAKAREQYEAEE 1435
Cdd:PRK00106 183 THEIATRIREAEREV----KDRSDKMaKDLLAQAMQRLAGEYVTEQ 224
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1412-1632 |
1.47e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1412 RLDKMKEEHQQVMAkAREqyEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLEL 1491
Cdd:COG4913 226 AADALVEHFDDLER-AHE--ALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1492 D---LETRAKDVKARLALLEVQEETARREKQQlLDVQRQVALKSEEATAThQQLEEAQKEHTHLlqsNQQLREI------ 1562
Cdd:COG4913 303 ElarLEAELERLEARLDALREELDELEAQIRG-NGGDRLEQLEREIERLE-RELEERERRRARL---EALLAALglplpa 377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530397889 1563 -LDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLREVTVE----ENNASPHfepDLHIEDLRKSL 1632
Cdd:COG4913 378 sAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEiaslERRKSNI---PARLLALRDAL 449
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1310-1687 |
1.51e-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: 53.57 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1310 LQQLREQLEGERKEAVATLEKEHSAELERLCS--------------SLEAKHREVVSSLQ--KKIQEAQQKEEAQLQ--- 1370
Cdd:pfam05483 50 LEQVANSGDCHYQEGLKDSDFENSEGLSRLYSklykeaekikkwkvSIEAELKQKENKLQenRKIIEAQRKAIQELQfen 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1371 -KCLGQVEHRVHQKSYHVA--GYEHELSSLLRE---------KRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQ 1438
Cdd:pfam05483 130 eKVSLKLEEEIQENKDLIKenNATRHLCNLLKEtcarsaektKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1439 RAELLGHLTGELERLQRAhERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARR-- 1516
Cdd:pfam05483 210 RLEMHFKLKEDHEKIQHL-EEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKEli 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1517 EKQQLL---------DVQRQVALKS--EE----ATATHQQL---EEAQKEHTHLLQSNQQLreILDELQARKLKLESQVD 1578
Cdd:pfam05483 289 EKKDHLtkeledikmSLQRSMSTQKalEEdlqiATKTICQLteeKEAQMEELNKAKAAHSF--VVTEFEATTCSLEELLR 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1579 LLQAQSQQLQKHFSSLEAEAQKKQHLLREVTVEENNAsphfepDLHIEDLRKSLGTNQT--------KEVSSSLSQSKED 1650
Cdd:pfam05483 367 TEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNK------EVELEELKKILAEDEKlldekkqfEKIAEELKGKEQE 440
|
410 420 430
....*....|....*....|....*....|....*..
gi 530397889 1651 LYLDSLSSHNVWHLLSAEGVALRSAKEFLVQQTRSMR 1687
Cdd:pfam05483 441 LIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLK 477
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1387-1565 |
1.60e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.24 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1387 VAGYEHELSSLLREKRQEVEGEHERRLDKMKEEhqqvMAKAREQYEAEERKQRAELlghltGELERLQRAHERELEtvrq 1466
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIKKEALLEAKEE----IHKLRNEFEKELRERRNEL-----QKLEKRLLQKEENLD---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1467 eqhKRLEDLRRRhreqERKLQDLELDLETRAKDVKARlallevQEETARREKQQLLDVQRQVALKSEEATAthQQLEEAQ 1546
Cdd:PRK12704 100 ---RKLELLEKR----EEELEKKEKELEQKQQELEKK------EEELEELIEEQLQELERISGLTAEEAKE--ILLEKVE 164
|
170
....*....|....*....
gi 530397889 1547 KEHTHllQSNQQLREILDE 1565
Cdd:PRK12704 165 EEARH--EAAVLIKEIEEE 181
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1410-1575 |
1.67e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.86 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1410 ERRLDKMKEEHQQVMAKAREqyEAEERKQRAELlghltgelerlqrahereleTVRQEQHKRLEDLRRRHREQERKLQDL 1489
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKK--EAEAIKKEALL--------------------EAKEEIHKLRNEFEKELRERRNELQKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1490 EldletraKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHthllqsNQQLREI--LDELQ 1567
Cdd:PRK12704 88 E-------KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQ------LQELERIsgLTAEE 154
|
....*...
gi 530397889 1568 ARKLKLES 1575
Cdd:PRK12704 155 AKEILLEK 162
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1398-1601 |
1.96e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1398 LREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEER-KQRAELLGHLTGELERLQR---AHERELETVRQEQHKRLE 1473
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiAALARRIRALEQELAALEAelaELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1474 DLRRRHREQERKLQDLELDLETRAKDVKA---RLALL----EVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQ 1546
Cdd:COG4942 105 ELAELLRALYRLGRQPPLALLLSPEDFLDavrRLQYLkylaPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 530397889 1547 KEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKK 1601
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1151-1569 |
2.42e-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: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1151 EAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKLCQEEeeeilRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQ 1230
Cdd:COG4913 311 LERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLE-----RELEERERRRARLEALLAALGLPLPASAEEFAAL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1231 RLSW--LRAQVQSSTQADEDQiRAEQEASLQKLREELEsQQKAERASLEQKN-------RQMLEQLKEEIEASE------ 1295
Cdd:COG4913 386 RAEAaaLLEALEEELEALEEA-LAEAEAALRDLRRELR-ELEAEIASLERRKsniparlLALRDALAEALGLDEaelpfv 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1296 ------KSEQAALNAAKEKAL-----------------------QQLREQLEGERKEAVATLEKEHSAELERLCSSLEAK 1346
Cdd:COG4913 464 gelievRPEEERWRGAIERVLggfaltllvppehyaaalrwvnrLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFK 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1347 ----HREVVSSLQKKIQEAQQKEEAQLQKC------LGQV--EHRVHQK-------SYHVAGYE-----HELSSLLREKR 1402
Cdd:COG4913 544 phpfRAWLEAELGRRFDYVCVDSPEELRRHpraitrAGQVkgNGTRHEKddrrrirSRYVLGFDnraklAALEAELAELE 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1403 QEVEgEHERRLDKMKEEHQQvMAKAREQYEAEERKQRAEL--------LGHLTGELERLQRAHE--RELETVRQEQHKRL 1472
Cdd:COG4913 624 EELA-EAEERLEALEAELDA-LQERREALQRLAEYSWDEIdvasaereIAELEAELERLDASSDdlAALEEQLEELEAEL 701
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1473 EDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQ-KEHTH 1551
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIdALRAR 781
|
490
....*....|....*...
gi 530397889 1552 LLQSNQQLREILDELQAR 1569
Cdd:COG4913 782 LNRAEEELERAMRAFNRE 799
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1435-1715 |
2.72e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1435 ERKQRAELLGHLTGELERLQRAHErELETVRqEQHKRLEDLRRRHREQERKLQDLEL--DLETRAKDVKA--RLALLEVQ 1510
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHE-ALEDAR-EQIELLEPIRELAERYAAARERLAEleYLRAALRLWFAqrRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1511 EETARREKQQLldvQRQVALKSEEATATHQQLEEAQKEHthLLQSNQQLREILDELQARKLKLESQvdllqaqsqqlqkh 1590
Cdd:COG4913 297 LEELRAELARL---EAELERLEARLDALREELDELEAQI--RGNGGDRLEQLEREIERLERELEER-------------- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1591 fsslEAEAQKKQHLLREVtveennaspHFEPDLHIEDLRKSLgtNQTKEVSSSLSQSKEDLyldslssHNVWHLLSAEGV 1670
Cdd:COG4913 358 ----ERRRARLEALLAAL---------GLPLPASAEEFAALR--AEAAALLEALEEELEAL-------EEALAEAEAALR 415
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 530397889 1671 ALRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELASAQEVAKDPP 1715
Cdd:COG4913 416 DLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAEL 460
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1253-1486 |
2.73e-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: 50.43 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1253 EQEASLQKLREelesQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAAlnaakeKALQQLREQLEGERKEAVATLEK-E 1331
Cdd:pfam15665 11 EHEAEIQALKE----AHEEEIQQILAETREKILQYKSKIGEELDLKRRI------QTLEESLEQHERMKRQALTEFEQyK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1332 HSAELERLCssLEAKHREVVSSLQKKIQEAQQKEEAQLQKclgqvehrvhqksyhvagyehelsslLREKRQEVEGEHER 1411
Cdd:pfam15665 81 RRVEERELK--AEAEHRQRVVELSREVEEAKRAFEEKLES--------------------------FEQLQAQFEQEKRK 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530397889 1412 RLDKMKEEHQQVMAKAREQYEAEERKqraellghLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKL 1486
Cdd:pfam15665 133 ALEELRAKHRQEIQELLTTQRAQSAS--------SLAEQEKLEELHKAELESLRKEVEDLRKEKKKLAEEYEQKL 199
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1237-1368 |
2.97e-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: 51.77 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1237 AQVQSSTQADEDQIRAEQEAslQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQ 1316
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQER--QKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAK 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 530397889 1317 LEGERK-------EAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQ 1368
Cdd:TIGR02794 128 QAAEAKakaeaeaERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAE 186
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1329-1607 |
3.25e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.43 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1329 EKEHSAELERLCSSLEAKHREVvsSLQKKIQEAQQKEEAQLQKclgqvehrvhQKSYHVagyEHELSSLlrekrqevegE 1408
Cdd:pfam17380 291 EKFEKMEQERLRQEKEEKAREV--ERRRKLEEAEKARQAEMDR----------QAAIYA---EQERMAM----------E 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1409 HERRLDKMK-EEHQQVMAKAREQYEAEERKQraellghlTGELERLQRAHERELETVRQE-----QHKRLEDlrrrhrEQ 1482
Cdd:pfam17380 346 RERELERIRqEERKRELERIRQEEIAMEISR--------MRELERLQMERQQKNERVRQEleaarKVKILEE------ER 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1483 ERKLQDLELDLET-RAKDVKARLALLEVQEETARREKQQLldvqRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLRE 1561
Cdd:pfam17380 412 QRKIQQQKVEMEQiRAEQEEARQREVRRLEEERAREMERV----RLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRK 487
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 530397889 1562 ILDELqaRKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLRE 1607
Cdd:pfam17380 488 RAEEQ--RRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYE 531
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1250-1615 |
3.42e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1250 IRAEQEASLQKLREELESQQkaerASLEQKNRQMLEQLKEEIEASEksEQAALNAAKEKALQQLREQLEGERKEavatlE 1329
Cdd:COG4717 43 IRAMLLERLEKEADELFKPQ----GRKPELNLKELKELEEELKEAE--EKEEEYAELQEELEELEEELEELEAE-----L 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1330 KEHSAELERLcssleakhrEVVSSLQKKIQEAQQKEE--AQLQKCLGQVEHRVHQksyhVAGYEHELSSlLREKRQEVEG 1407
Cdd:COG4717 112 EELREELEKL---------EKLLQLLPLYQELEALEAelAELPERLEELEERLEE----LRELEEELEE-LEAELAELQE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1408 EHERRLDKMKEEHQQVMAKAREQYEA--EERKQRAELLGHLTGELERLQRAHER-ELETVRQEQHKRLEDLRR------- 1477
Cdd:COG4717 178 ELEELLEQLSLATEEELQDLAEELEElqQRLAELEEELEEAQEELEELEEELEQlENELEAAALEERLKEARLllliaaa 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1478 -----------------------------------------RHREQERKLQDLELDLETRAKDVKARLALLEVQEETARR 1516
Cdd:COG4717 258 llallglggsllsliltiagvlflvlgllallflllarekaSLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1517 EKQQLLDVQRQVALKSEEATATHQQL--EEAQKEHTHLLQSNQ-----QLREILD------ELQARKLKLESQVDLLQAQ 1583
Cdd:COG4717 338 ELLELLDRIEELQELLREAEELEEELqlEELEQEIAALLAEAGvedeeELRAALEqaeeyqELKEELEELEEQLEELLGE 417
|
410 420 430
....*....|....*....|....*....|....
gi 530397889 1584 SQQLQKHFS--SLEAEAQKKQHLLREVTVEENNA 1615
Cdd:COG4717 418 LEELLEALDeeELEEELEELEEELEELEEELEEL 451
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1399-1571 |
4.01e-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: 51.07 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1399 REKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRR 1478
Cdd:pfam13868 31 KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1479 HREQERKLQD-LELDLETR---AKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHT---- 1550
Cdd:pfam13868 111 QEEDQAEAEEkLEKQRQLReeiDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIarlr 190
|
170 180
....*....|....*....|.
gi 530397889 1551 HLLQSNQQLREILDELQARKL 1571
Cdd:pfam13868 191 AQQEKAQDEKAERDELRAKLY 211
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1230-1569 |
4.37e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.43 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1230 QRLSWLRAQVQSSTQADEDQIRAEQEA-SLQKLREELESQ---QKAERASLEQKNRQMLEQLKEEIEASE--KSEQAALN 1303
Cdd:pfam07888 42 ERAELLQAQEAANRQREKEKERYKRDReQWERQRRELESRvaeLKEELRQSREKHEELEEKYKELSASSEelSEEKDALL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1304 AAKEKALQQLREQLEGERKEAVATLEKEhsAELERLcssleaKHREVVSSLQKKIQEAQQKeeaQLQKCLGQVEHRVHQK 1383
Cdd:pfam07888 122 AQRAAHEARIRELEEDIKTLTQRVLERE--TELERM------KERAKKAGAQRKEEEAERK---QLQAKLQQTEEELRSL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1384 SYHVAGYEHEL----SSLLR-----EKRQEVEGEHERRLDKMKEEHQQvMAKAREQYEAEERKqrAELLGHLTGELERLQ 1454
Cdd:pfam07888 191 SKEFQELRNSLaqrdTQVLQlqdtiTTLTQKLTTAHRKEAENEALLEE-LRSLQERLNASERK--VEGLGEELSSMAAQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1455 RAHERELETVRQEQHK---RLEDLRRRHRE------QERK--LQDLELDLETRAKDVKARLALLE-VQEETARREKQQL- 1521
Cdd:pfam07888 268 DRTQAELHQARLQAAQltlQLADASLALREgrarwaQEREtlQQSAEADKDRIEKLSAELQRLEErLQEERMEREKLEVe 347
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 530397889 1522 ----LDVQR-QVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQAR 1569
Cdd:pfam07888 348 lgreKDCNRvQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQR 400
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1264-1561 |
4.46e-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: 52.03 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1264 ELESQQKAERASLEQKNRQMlEQLKEEIEASEKSEQAALNAAKE---------KALQQLREQLEGERKEA---------- 1324
Cdd:pfam05483 272 QLEEKTKLQDENLKELIEKK-DHLTKELEDIKMSLQRSMSTQKAleedlqiatKTICQLTEEKEAQMEELnkakaahsfv 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1325 -------VATLEKEHSAELERLCSSlEAKHREVVSSLQKKIQEAQQK---------EEAQLQKCLGQVEHRVHQK----- 1383
Cdd:pfam05483 351 vtefeatTCSLEELLRTEQQRLEKN-EDQLKIITMELQKKSSELEEMtkfknnkevELEELKKILAEDEKLLDEKkqfek 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1384 -SYHVAGYEHELSSLLREKRQEVEG-EHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGH---LTGELERL-QRAH 1457
Cdd:pfam05483 430 iAEELKGKEQELIFLLQAREKEIHDlEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHcdkLLLENKELtQEAS 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1458 ERELETVRQEQH------------KRLEDLRRRHREQERKLQDLELDLETRAKDVKARLallEVQEETARREKQQLLDVQ 1525
Cdd:pfam05483 510 DMTLELKKHQEDiinckkqeermlKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKL---DKSEENARSIEYEVLKKE 586
|
330 340 350
....*....|....*....|....*....|....*.
gi 530397889 1526 RQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLRE 1561
Cdd:pfam05483 587 KQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1249-1365 |
5.11e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.75 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1249 QIRAEQEA-SLQKLREELESQQKaeraSLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVAT 1327
Cdd:PRK00409 529 ERELEQKAeEAEALLKEAEKLKE----ELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASV 604
|
90 100 110
....*....|....*....|....*....|....*...
gi 530397889 1328 LEKEHSAELERLCSSLEAKHREvvsslqKKIQEAQQKE 1365
Cdd:PRK00409 605 KAHELIEARKRLNKANEKKEKK------KKKQKEKQEE 636
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1238-1570 |
6.57e-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: 6.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1238 QVQSSTQADEDQIRAEQEASLQKLREELESqqkaeraslEQKNRQMLEQLKEEIEASEKsEQAALNAAKEKALQQLREQL 1317
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELDELLES---------EEKNREEVEELKDKYRELRK-TLLANRFSYGPAIDELEKQL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1318 EgerkeavaTLEKEHSaELERLCSS---LEAkhREVVSSLQKKIQEAQQKEE------AQLQKCL-GQVEhrvhqksyhv 1387
Cdd:pfam06160 156 A--------EIEEEFS-QFEELTESgdyLEA--REVLEKLEEETDALEELMEdipplyEELKTELpDQLE---------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1388 agyehELSSLLRE-KRQEVEGEH---ERRLDKMKEEHQQVMA--KAREQYEAEerkqraELLGHLTGELERLQRAHEREL 1461
Cdd:pfam06160 215 -----ELKEGYREmEEEGYALEHlnvDKEIQQLEEQLEENLAllENLELDEAE------EALEEIEERIDQLYDLLEKEV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1462 ETvRQEQHKRLEDLRRRHREQERKLQDLELDLETrakdVKARLALLEVQEETARREKQQLLDVQRQVAL---KSEEATAT 1538
Cdd:pfam06160 284 DA-KKYVEKNLPEIEDYLEHAEEQNKELKEELER----VQQSYTLNENELERVRGLEKQLEELEKRYDEiveRLEEKEVA 358
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 530397889 1539 H-----------QQLEEAQKEHTHLLQSNQQLREilDELQARK 1570
Cdd:pfam06160 359 YselqeeleeilEQLEEIEEEQEEFKESLQSLRK--DELEARE 399
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
59-89 |
7.00e-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: 7.00e-06
10 20 30
....*....|....*....|....*....|.
gi 530397889 59 PGEWKPCQDITGDIYYFNFANGQSMWDHPCD 89
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1151-1412 |
7.80e-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: 7.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1151 EAALKAMEEAVAQVLEQD-QRHLLESKQEKMQQLREKLCQEEEEEIL---RLHQQKEQSLSSLRERL-----QKAIEEEE 1221
Cdd:pfam17380 332 QAAIYAEQERMAMERERElERIRQEERKRELERIRQEEIAMEISRMReleRLQMERQQKNERVRQELeaarkVKILEEER 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1222 ARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLR-EELESQQKAE--RASLEQKNRQMLEQLKEEIEASEKSE 1298
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRlEEQERQQQVErlRQQEEERKRKKLELEKEKRDRKRAEE 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1299 QAALNAAKEKALQQlREQLEGERKEAVatLEKEhsaelerlcssLEAKHREVVSSLQKKIQEAQQKEEAQLQKclgqvEH 1378
Cdd:pfam17380 492 QRRKILEKELEERK-QAMIEEERKRKL--LEKE-----------MEERQKAIYEEERRREAEEERRKQQEMEE-----RR 552
|
250 260 270
....*....|....*....|....*....|....*..
gi 530397889 1379 RVHQKSYHVAGYEHELSSLLREK---RQEVEGEHERR 1412
Cdd:pfam17380 553 RIQEQMRKATEERSRLEAMERERemmRQIVESEKARA 589
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1236-1371 |
8.83e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.19 E-value: 8.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1236 RAQVQSSTQADEDQIR--AEQEASLQKLREELESQQKAERAslEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKAlqql 1313
Cdd:PRK09510 80 QRKKKEQQQAEELQQKqaAEQERLKQLEKERLAAQEQKKQA--EEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEA---- 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 530397889 1314 rEQLEGERKEAVATLEKEHSAELERLCSSlEAKHREVVSSLQKKIQEAQQKEEAQLQK 1371
Cdd:PRK09510 154 -KRAAAAAKKAAAEAKKKAEAEAAKKAAA-EAKKKAEAEAAAKAAAEAKKKAEAEAKK 209
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1251-1647 |
9.78e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 50.68 E-value: 9.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1251 RAEQEASLQKLREEL--ESQQKAERASLEQKNRQMLEQLKEEIEAS-EKSEQAALNAAKEKALQQLREQLEGERKEAVAT 1327
Cdd:COG5278 85 RAEIDELLAELRSLTadNPEQQARLDELEALIDQWLAELEQVIALRrAGGLEAALALVRSGEGKALMDEIRARLLLLALA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1328 LEKEHSAELERLcsSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEG 1407
Cdd:COG5278 165 LAALLLAAAALL--LLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALAL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1408 EHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQ 1487
Cdd:COG5278 243 ALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1488 DLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQ 1567
Cdd:COG5278 323 AALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAA 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1568 ARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLREVTVEENNASPHFEPDLHIEDLRKSLGTNQTKEVSSSLSQS 1647
Cdd:COG5278 403 AAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAA 482
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1324-1569 |
1.23e-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: 49.76 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1324 AVATLEKEHSAELERLcssleakhREVVSSLQKKIQEaQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSL---LRE 1400
Cdd:COG4942 17 AQADAAAEAEAELEQL--------QQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRIRALEQELAALeaeLAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1401 KRQEVEgEHERRLDKMKEEHQQVMAKAREQyeaeERKQRAELLGHLTGELERLQRAheRELETVRQEQHKRLEDLRRrhr 1480
Cdd:COG4942 88 LEKEIA-ELRAELEAQKEELAELLRALYRL----GRQPPLALLLSPEDFLDAVRRL--QYLKYLAPARREQAEELRA--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1481 eqerKLQDLElDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEeatathQQLEEAQKEHTHLLQSNQQLR 1560
Cdd:COG4942 158 ----DLAELA-ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE------KELAELAAELAELQQEAEELE 226
|
....*....
gi 530397889 1561 EILDELQAR 1569
Cdd:COG4942 227 ALIARLEAE 235
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1435-1576 |
1.30e-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: 48.77 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1435 ERKQRAELLGHLTGELERLqrahERELETVRqeqhKRLEDLRRRHREQERKLQDLELDLET---RAKDVKARLAL----- 1506
Cdd:COG1579 18 ELDRLEHRLKELPAELAEL----EDELAALE----ARLEAAKTELEDLEKEIKRLELEIEEveaRIKKYEEQLGNvrnnk 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530397889 1507 ----LEVQEETARREKQQL----LDVQRQVALKSEEATATHQQLEEAQKEHTHLLqsnQQLREILDELQARKLKLESQ 1576
Cdd:COG1579 90 eyeaLQKEIESLKRRISDLedeiLELMERIEELEEELAELEAELAELEAELEEKK---AELDEELAELEAELEELEAE 164
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1232-1600 |
1.39e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.44 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1232 LSWLRAQ-VQSSTQADEDQIRAE-QEASLQKlreeleSQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAakEKA 1309
Cdd:PRK10929 9 MAWLLSWgAYAATAPDEKQITQElEQAKAAK------TPAQAEIVEALQSALNWLEERKGSLERAKQYQQVIDNF--PKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1310 LQQLREQLEGERKE--------AVATLEKE------HSAELERLCSSLEAKHREVVSSLQkkiQEAQQKEEAqlQKCLGQ 1375
Cdd:PRK10929 81 SAELRQQLNNERDEprsvppnmSTDALEQEilqvssQLLEKSRQAQQEQDRAREISDSLS---QLPQQQTEA--RRQLNE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1376 VEHRVH-------------------QKSYHVAGY-EHELSSLLREKRQEVEgehERRLDKMKEEHQQVMAK--------- 1426
Cdd:PRK10929 156 IERRLQtlgtpntplaqaqltalqaESAALKALVdELELAQLSANNRQELA---RLRSELAKKRSQQLDAYlqalrnqln 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1427 AREQYEAEERKQRAELLGHLTGEL-----ERLQRahERELETVRQEQHKRLEDLRRRHReqerklqdleldlETRAKDVK 1501
Cdd:PRK10929 233 SQRQREAERALESTELLAEQSGDLpksivAQFKI--NRELSQALNQQAQRMDLIASQQR-------------QAASQTLQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1502 ARLALlevqeeTARREKQQLLDVQRQV--ALKSEEAtathqQLEEAQKEhthllqsnQQLREILDELQARKLKLESQVDL 1579
Cdd:PRK10929 298 VRQAL------NTLREQSQWLGVSNALgeALRAQVA-----RLPEMPKP--------QQLDTEMAQLRVQRLRYEDLLNK 358
|
410 420
....*....|....*....|.
gi 530397889 1580 LQAQSQQLQKHFSSLEAEAQK 1600
Cdd:PRK10929 359 QPQLRQIRQADGQPLTAEQNR 379
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1120-1408 |
1.39e-05 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 50.24 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1120 DPEEKVAVSPTPPVSPEVRSTEPVAP--PEQLSEA----------ALKAMEEAVAQVLEQDQRHLLESK--QEKMQQLRE 1185
Cdd:PLN03229 414 DPERKVNMKKREAVKTPVRELEGEVEklKEQILKAkessskpselALNEMIEKLKKEIDLEYTEAVIAMglQERLENLRE 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1186 KLCQEEEE----------EILRLHQQKEQSLS------SLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQADEDq 1249
Cdd:PLN03229 494 EFSKANSQdqlmhpvlmeKIEKLKDEFNKRLSrapnylSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMD- 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1250 iRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASE----KSEQAALNAAKEKALQQLREQLEGERKEAV 1325
Cdd:PLN03229 573 -RPEIKEKMEALKAEVASSGASSGDELDDDLKEKVEKMKKEIELELagvlKSMGLEVIGVTKKNKDTAEQTPPPNLQEKI 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1326 ATLEKEHSAELERLCSSLEAKHRevVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGyehelSSLLREKRQEV 1405
Cdd:PLN03229 652 ESLNEEINKKIERVIRSSDLKSK--IELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEALN-----SSELKEKFEEL 724
|
...
gi 530397889 1406 EGE 1408
Cdd:PLN03229 725 EAE 727
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
58-87 |
1.72e-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: 1.72e-05
10 20 30
....*....|....*....|....*....|
gi 530397889 58 LPGEWKPCQDITGDIYYFNFANGQSMWDHP 87
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1232-1530 |
2.30e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1232 LSWLRAQVQSSTQADEDQIRAEqeasLQKLREELESQQK---AERASLEQKNRQmLEQLKEEIEASEKSEQAALN--AAK 1306
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEE----LEQLREELEQAREeleQLEEELEQARSE-LEQLEEELEELNEQLQAAQAelAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1307 EKALQQLREQLEGERKEaVATLEKEhSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEE--AQLQKCLGQVEHRVHQKS 1384
Cdd:COG4372 100 QEELESLQEEAEELQEE-LEELQKE-RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEqlESLQEELAALEQELQALS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1385 yhVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETV 1464
Cdd:COG4372 178 --EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530397889 1465 RQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVAL 1530
Cdd:COG4372 256 ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAAL 321
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1434-1641 |
2.44e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1434 EERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEET 1513
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1514 ARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSS 1593
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 530397889 1594 LEAEAQ-----KKQHLLREVTVEENNASPHFEPDLHIEDLRKSLGTNQTKEVS 1641
Cdd:COG4372 169 LEQELQalseaEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELL 221
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1123-1519 |
2.55e-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: 49.37 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1123 EKVAVSPTPPVSPEVRSTEPVAPPEQLSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKLcqeeeeeilrlhQQK 1202
Cdd:pfam09731 99 SEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHT------------DSL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1203 EQSLSSLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIrAEQEASLQKLREELESQQKAERAslEQKNRQ 1282
Cdd:pfam09731 167 KEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLL-DAAPETPPKLPEHLDNVEEKVEK--AQSLAK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1283 MLEQLKEEIEASEkseqaalnaakekalQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVvSSLQKKIQEAQ 1362
Cdd:pfam09731 244 LVDQYKELVASER---------------IVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREI-DQLSKKLAELK 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1363 QKEEAQLQKCLGQVEHrvhqksyhvagyehELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEerkqrael 1442
Cdd:pfam09731 308 KREEKHIERALEKQKE--------------ELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEK-------- 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1443 lghLTGELERLQRAHERELETVRQEQHkrlEDLRRRHR-------EQERKLQDLELD-LETRAKDVKARLALLEVQEETA 1514
Cdd:pfam09731 366 ---LRTELERQAEAHEEHLKDVLVEQE---IELQREFLqdikekvEEERAGRLLKLNeLLANLKGLEKATSSHSEVEDEN 439
|
....*
gi 530397889 1515 RREKQ 1519
Cdd:pfam09731 440 RKAQQ 444
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1152-1364 |
3.01e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 48.92 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1152 AALKAMEEAVAQVLEQdqrhlLESKQEKMQQLrEKLCQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMRE----- 1226
Cdd:PRK11637 75 AQLKKQEEAISQASRK-----LRETQNTLNQL-NKQIDELNASIAKLEQQQAAQERLLAAQLDAAFRQGEHTGLQlilsg 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1227 EESQRLSWLRAQVQSSTQADEDQIraeqeASLQKLREELeSQQKAErasLEQKNRQMLEQLKEEIEASEKSEQA------ 1300
Cdd:PRK11637 149 EESQRGERILAYFGYLNQARQETI-----AELKQTREEL-AAQKAE---LEEKQSQQKTLLYEQQAQQQKLEQArnerkk 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530397889 1301 ---ALNAAKEKALQQLRE--QLEGERKEAVATLEKEHSAELERlcsslEAKHREVVsslQKKIQEAQQK 1364
Cdd:PRK11637 220 tltGLESSLQKDQQQLSElrANESRLRDSIARAEREAKARAER-----EAREAARV---RDKQKQAKRK 280
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1265-1546 |
3.34e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1265 LESQQKAERASLEQKNRQMLEQLKEeieASEKSEQAalnaakEKALQQLREQlegerkEAVATLEKEHSAELERLcSSLE 1344
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPE---LRKELEEA------EAALEEFRQK------NGLVDLSEEAKLLLQQL-SELE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1345 AKHREvvssLQKKIQEAQQKEEaQLQKCLGQVEHRVHQKSyhvagyEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVM 1424
Cdd:COG3206 226 SQLAE----ARAELAEAEARLA-ALRAQLGSGPDALPELL------QSPVIQQLRAQLAELEAELAELSARYTPNHPDVI 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1425 AKareqyeaeeRKQRAELLGHLTGELERLQRAHERELETVRQeqhkRLEDLRRRHREQERKLQDLeldletrakdvkarl 1504
Cdd:COG3206 295 AL---------RAQIAALRAQLQQEAQRILASLEAELEALQA----REASLQAQLAQLEARLAEL--------------- 346
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 530397889 1505 allevqeetARREkQQLLDVQRQVALKSEEATATHQQLEEAQ 1546
Cdd:COG3206 347 ---------PELE-AELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1158-1769 |
3.52e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.20 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1158 EEAVAQVLEQDQRHLLESKQEKMQQLREKLcQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMreeeSQRLSWLRA 1237
Cdd:pfam02463 234 LNEERIDLLQELLRDEQEEIESSKQEIEKE-EEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELK----SELLKLERR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1238 QVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEqknRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQL 1317
Cdd:pfam02463 309 KVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELE---IKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESER 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1318 EGERKEAV-------------ATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKs 1384
Cdd:pfam02463 386 LSSAAKLKeeelelkseeekeAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDE- 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1385 yhvagYEHELSSLLREKRQEVEGE--HERRLDKMKEEHQQVMA-KAREQYEAEERKQRAELLGHLTGELERLQRAHERE- 1460
Cdd:pfam02463 465 -----LELKKSEDLLKETQLVKLQeqLELLLSRQKLEERSQKEsKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVe 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1461 --------LETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQE--ETARREKQQLLDVQRQVAL 1530
Cdd:pfam02463 540 nykvaistAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEidPILNLAQLDKATLEADEDD 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1531 KSEEATATHQQLEEAQKEHTHLLQSNQQLREI--LDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLREV 1608
Cdd:pfam02463 620 KRAKVVEGILKDTELTKLKESAKAKESGLRKGvsLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQL 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1609 TVEENNASPHFEP-DLHIEDLRKSLGTNQTKEVSSSLSQSKEDLYLDSLSSHNVWHLLSA-EGVALRSAKEFLVQQTRSM 1686
Cdd:pfam02463 700 EIKKKEQREKEELkKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKeEKEEEKSELSLKEKELAEE 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1687 RRRQTALKAAQQHWRHELASAQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSLWEEA 1766
Cdd:pfam02463 780 REKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERL 859
|
...
gi 530397889 1767 SDE 1769
Cdd:pfam02463 860 EEE 862
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1147-1474 |
3.80e-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: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1147 EQLSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKAieEEEARMRE 1226
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA--EEELAEAE 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1227 EESQRLSWLRAQVQSSTQADEDQIRAEQEA------SLQKLREELESQQKAERAS------LEQKNRQMLEQLkEEIEAS 1294
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALREALDELRAEltllneEAANLRERLESLERRIAATerrledLEEQIEELSEDI-ESLAAE 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1295 EKSEQAALNAAKE--KALQQLREQLEGERKEAVATLEK------EHSAELERLCSSLEAKhREVVSSLQKKIQEAQQKEE 1366
Cdd:TIGR02168 861 IEELEELIEELESelEALLNERASLEEALALLRSELEElseelrELESKRSELRRELEEL-REKLAQLELRLEGLEVRID 939
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1367 AQLQKC--LGQVEHRVHQKSYhvagyehelssllrEKRQEVEGEHERRLDKMKEEHQQ---VMAKAREQYEAEErkqraE 1441
Cdd:TIGR02168 940 NLQERLseEYSLTLEEAEALE--------------NKIEDDEEEARRRLKRLENKIKElgpVNLAAIEEYEELK-----E 1000
|
330 340 350
....*....|....*....|....*....|....*.
gi 530397889 1442 LLGHLTGELERLQRAHERELETVRQ---EQHKRLED 1474
Cdd:TIGR02168 1001 RYDFLTAQKEDLTEAKETLEEAIEEidrEARERFKD 1036
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1168-1607 |
4.20e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1168 DQRHLLESKQEKMQQLREklcqeeeeeiLRLHQQKEQSLSSLRERLQKaieeeearmreeesqrlswlRAQVQSSTQADE 1247
Cdd:PRK04863 507 EQRHLAEQLQQLRMRLSE----------LEQRLRQQQRAERLLAEFCK--------------------RLGKNLDDEDEL 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1248 DQIRAEQEASLQKLREELESQqkAERASLEqknRQMLEQLKEEIEASEKSEQAALNAakEKALQQLREQLEGERKEAVA- 1326
Cdd:PRK04863 557 EQLQEELEARLESLSESVSEA--RERRMAL---RQQLEQLQARIQRLAARAPAWLAA--QDALARLREQSGEEFEDSQDv 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1327 ------TLEKEHSAELERlcSSLEAKHRevvsSLQKKIQEAQQKEEAQLQKCLGQVEH-------------RVHQKSYHV 1387
Cdd:PRK04863 630 teymqqLLERERELTVER--DELAARKQ----ALDEEIERLSQPGGSEDPRLNALAERfggvllseiyddvSLEDAPYFS 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1388 AGY--------------------------------EHELSSLlREKRQEVE----------GEHERRLDKMKEEhqQVMA 1425
Cdd:PRK04863 704 ALYgparhaivvpdlsdaaeqlagledcpedlyliEGDPDSF-DDSVFSVEelekavvvkiADRQWRYSRFPEV--PLFG 780
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1426 K-AREQYEAE---ERKQRAELLGHLTGELERLQRAHERELETVRQ--------EQHKRLEDLRRRHREQERKLQDLE--- 1490
Cdd:PRK04863 781 RaAREKRIEQlraEREELAERYATLSFDVQKLQRLHQAFSRFIGShlavafeaDPEAELRQLNRRRVELERALADHEsqe 860
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1491 LDLETRAKDVKARLALL--------------------EVQEETARRE--------------------------------- 1517
Cdd:PRK04863 861 QQQRSQLEQAKEGLSALnrllprlnlladetladrveEIREQLDEAEeakrfvqqhgnalaqlepivsvlqsdpeqfeql 940
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1518 -------KQQLLDVQRQV-ALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQK 1589
Cdd:PRK04863 941 kqdyqqaQQTQRDAKQQAfALTEVVQRRAHFSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQ 1020
|
570
....*....|....*...
gi 530397889 1590 HFSSLEAEAQKKQHLLRE 1607
Cdd:PRK04863 1021 VLASLKSSYDAKRQMLQE 1038
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
57-87 |
4.28e-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: 4.28e-05
10 20 30
....*....|....*....|....*....|.
gi 530397889 57 PLPGEWKPCQDITGDIYYFNFANGQSMWDHP 87
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKP 31
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1231-1762 |
4.80e-05 |
|
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: 48.48 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1231 RLSWLRAQVQSSTQADEDQIR--AEQEASLQKLREELESQQKA------ERASLEQKnrqmLEQLKEEIEaSEKSEQAAL 1302
Cdd:TIGR04523 146 EIKKKEKELEKLNNKYNDLKKqkEELENELNLLEKEKLNIQKNidkiknKLLKLELL----LSNLKKKIQ-KNKSLESQI 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1303 NAAKEKAlQQLREQLEGERKEAVATLEKEHSAElERLcSSLEAKHREVVSSLQKKIQEAQQKEeaqlqKCLGQVEHRVHQ 1382
Cdd:TIGR04523 221 SELKKQN-NQLKDNIEKKQQEINEKTTEISNTQ-TQL-NQLKDEQNKIKKQLSEKQKELEQNN-----KKIKELEKQLNQ 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1383 ksyhvagYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEA-----EERKQRAELLGHLTGELERLQRah 1457
Cdd:TIGR04523 293 -------LKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIisqlnEQISQLKKELTNSESENSEKQR-- 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1458 erELEtvrqEQHKRLEDLRRrhrEQERKLQDLElDLETRAKDVKARLallEVQEETARREKQQLLDVQRQVALKSEEATA 1537
Cdd:TIGR04523 364 --ELE----EKQNEIEKLKK---ENQSYKQEIK-NLESQINDLESKI---QNQEKLNQQKDEQIKKLQQEKELLEKEIER 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1538 THQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLREVT-----VEE 1612
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNeekkeLEE 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1613 NNASPHFEPDLHIEDLRKSlgTNQTKEVSSSLSQSKEDLylDSLSSHNVWHLLsaEGVALRSAKEfLVQqtrsMRRRQTA 1692
Cdd:TIGR04523 511 KVKDLTKKISSLKEKIEKL--ESEKKEKESKISDLEDEL--NKDDFELKKENL--EKEIDEKNKE-IEE----LKQTQKS 579
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1693 LKAAQQHwrhelasAQEVAKDppgikaLEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSL 1762
Cdd:TIGR04523 580 LKKKQEE-------KQELIDQ------KEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI 636
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1244-1316 |
4.85e-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: 45.55 E-value: 4.85e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530397889 1244 QADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQ 1316
Cdd:COG0711 47 KEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAE 119
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1248-1536 |
5.24e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.61 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1248 DQIRA--EQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKsEQAALNAAKEKA---LQQLREQLE---G 1319
Cdd:pfam00038 18 DKVRFleQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTV-ERARLQLELDNLrlaAEDFRQKYEdelN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1320 ERKEA---VATLEKE-HSAELERLcssleakhrevvsSLQKKIQEAQqkEEAQLQKCLGQVEHRvhqksyhvagyehELS 1395
Cdd:pfam00038 97 LRTSAendLVGLRKDlDEATLARV-------------DLEAKIESLK--EELAFLKKNHEEEVR-------------ELQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1396 SLLREKRQEVEGEHERRLDKmkeehQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKrLEDL 1475
Cdd:pfam00038 149 AQVSDTQVNVEMDAARKLDL-----TSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEE-ITEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1476 RRR----------HREQ----ERKLQDLELDLETRAKDVKARLALLEVQ-----EETAR--REKQQLLDVqrQVALKSEE 1534
Cdd:pfam00038 223 RRTiqsleielqsLKKQkaslERQLAETEERYELQLADYQELISELEAElqetrQEMARqlREYQELLNV--KLALDIEI 300
|
..
gi 530397889 1535 AT 1536
Cdd:pfam00038 301 AT 302
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1241-1441 |
5.54e-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: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1241 SSTQADEDQIRAEQeASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGE 1320
Cdd:pfam15709 329 EQEKASRDRLRAER-AEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1321 RKEAVatlekEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQkclgqvehrvhqksyhvagyehelssllRE 1400
Cdd:pfam15709 408 RKQRL-----QLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQ----------------------------RQ 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 530397889 1401 KRQEVE-GEHERRLDKMKEEH------QQVMAKAREQYEAEERKQRAE 1441
Cdd:pfam15709 455 KELEMQlAEEQKRLMEMAEEErleyqrQKQEAEEKARLEAEERRQKEE 502
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1248-1367 |
5.81e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 46.36 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1248 DQIRAEQEASLQKLREELeSQQKAERASLEQKnrqmLEQLKEEIEASEKSEQAALNAAKE----KALQQlREQLEGERKE 1323
Cdd:COG1842 29 DQAIRDMEEDLVEARQAL-AQVIANQKRLERQ----LEELEAEAEKWEEKARLALEKGREdlarEALER-KAELEAQAEA 102
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 530397889 1324 AVATLEkEHSAELERLcssleakhREVVSSLQKKIQEAQQKEEA 1367
Cdd:COG1842 103 LEAQLA-QLEEQVEKL--------KEALRQLESKLEELKAKKDT 137
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1264-1570 |
5.85e-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: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1264 ELESQQKAERASLEQKNRQMLEqLKEEIeASEKSEQAALnaakEKALQQLREQLEGERKEAVA-TLEKEHSAELER---- 1338
Cdd:pfam07111 321 QLKAQDLEHRDSVKQLRGQVAE-LQEQV-TSQSQEQAIL----QRALQDKAAEVEVERMSAKGlQMELSRAQEARRrqqq 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1339 LCSSLEAKHREVVSSLqKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYeHELSSLLREK------RQE-------- 1404
Cdd:pfam07111 395 QTASAEEQLKFVVNAM-SSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKV-HTIKGLMARKvalaqlRQEscpppppa 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1405 --VEGEHERRLDKMKEEH--------------QQVMAKAREQYEAEeRKQRAELLGHLTGELERLQRAHE---RELETVR 1465
Cdd:pfam07111 473 ppVDADLSLELEQLREERnrldaelqlsahliQQEVGRAREQGEAE-RQQLSEVAQQLEQELQRAQESLAsvgQQLEVAR 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1466 QEQHKRLED---LRRRHREQE----RKLQDLELDLETRAKDvkaRLALLEVQEETARREKQQLLDVQRQVALKSEEATAT 1538
Cdd:pfam07111 552 QGQQESTEEaasLRQELTQQQeiygQALQEKVAEVETRLRE---QLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKER 628
|
330 340 350
....*....|....*....|....*....|..
gi 530397889 1539 HQQLEEAQKEHTHllQSNQQLREILDELQARK 1570
Cdd:pfam07111 629 NQELRRLQDEARK--EEGQRLARRVQELERDK 658
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1230-1600 |
6.35e-05 |
|
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: 48.19 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1230 QRLSWLRAQVQSSTQADEDQiraeQEASLQKLREELE--SQQKAERASLEQKNRQMLEQL---KEEIEASEK--SEQAAL 1302
Cdd:pfam15921 429 QRLEALLKAMKSECQGQMER----QMAAIQGKNESLEkvSSLTAQLESTKEMLRKVVEELtakKMTLESSERtvSDLTAS 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1303 NAAKEKALQQLREQLEGERKEAVATL--------EKEHSAELERLCSSLE---AKHREVVSSLQKKIQE----------- 1360
Cdd:pfam15921 505 LQEKERAIEATNAEITKLRSRVDLKLqelqhlknEGDHLRNVQTECEALKlqmAEKDKVIEILRQQIENmtqlvgqhgrt 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1361 --AQQKEEAQLQKCLGqvEHRVHQKSYHVagyehelsslLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEA--EER 1436
Cdd:pfam15921 585 agAMQVEKAQLEKEIN--DRRLELQEFKI----------LKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAvkDIK 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1437 KQRAELLGHLtgelerlqRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARR 1516
Cdd:pfam15921 653 QERDQLLNEV--------KTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGH 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1517 EKQQLLDVQRQVALKSEEATATH---QQLEE----AQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQK 1589
Cdd:pfam15921 725 AMKVAMGMQKQITAKRGQIDALQskiQFLEEamtnANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKE 804
|
410
....*....|.
gi 530397889 1590 HFSSLEAEAQK 1600
Cdd:pfam15921 805 KVANMEVALDK 815
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
823-1170 |
7.37e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 48.24 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 823 SQPEEKKDVSLDSDAAGPPTPCKPSSPGADSSLSSAvgkgRQGSGARPGLPEKEENEKSEPKicRNLVTPKADPTGSEPA 902
Cdd:PHA03307 45 SDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAP----ANESRSTPTWSLSTLAPASPAR--EGSPTPPGPSSPDPPP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 903 KASEKEAPEDTVDAGEEGSRREEAAKEPKKKASALEEGSSDASQEleiSEHMKEPQLSDSIASDPKSFHGL-----DFGF 977
Cdd:PHA03307 119 PTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVA---SDAASSRQAALPLSSPEETARAPssppaEPPP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 978 RSRISEHLLDVDVLSPVLGGACRQAQQPLGIEDKDDSQSSQDELQSKQSKGLEE--RLSPPLPHEERAQSPPRSLATEEE 1055
Cdd:PHA03307 196 STPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWgpENECPLPRPAPITLPTRIWEASGW 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1056 PPQGPEGQPEWKEAEELGEDSAAS--------LSLQLSLQREQAPSPPAACEKGKEQHSQAEELG--PGQEEAEDPEEKV 1125
Cdd:PHA03307 276 NGPSSRPGPASSSSSPRERSPSPSpsspgsgpAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAvsPGPSPSRSPSPSR 355
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 530397889 1126 AVSPTPPVSPEVRSTEPVAPPEQLSEAALKAMEEAVAQVLEQDQR 1170
Cdd:PHA03307 356 PPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARR 400
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1248-1441 |
7.56e-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: 7.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1248 DQIRAEQEASLQ--KLREELESQQKAERASLEQK----NRQMLEQLKEEIEASEKSEQAALNAAKEKAL----QQLREQL 1317
Cdd:NF012221 1532 DNVVATSESSQQadAVSKHAKQDDAAQNALADKEraeaDRQRLEQEKQQQLAAISGSQSQLESTDQNALetngQAQRDAI 1611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1318 EGERKEAVATLEK------------EHSAEL---------ERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQkclgQV 1376
Cdd:NF012221 1612 LEESRAVTKELTTlaqgldaldsqaTYAGESgdqwrnpfaGGLLDRVQEQLDDAKKISGKQLADAKQRHVDNQQ----KV 1687
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530397889 1377 EHRVHQKSYHVA-GYEHELSSLLREKRQEVEGEhERRLDKMKEEHQQVMAKAREQYEAEERKQRAE 1441
Cdd:NF012221 1688 KDAVAKSEAGVAqGEQNQANAEQDIDDAKADAE-KRKDDALAKQNEAQQAESDANAAANDAQSRGE 1752
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1421-1550 |
7.90e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.90 E-value: 7.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1421 QQVMAKAREQYEAEERK-----QRAEllghltgELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLEt 1495
Cdd:PRK00409 501 ENIIEEAKKLIGEDKEKlneliASLE-------ELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAE- 572
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 530397889 1496 rakdVKARLALLEVQEETARREKQ-QLLDVQRQVALKSEEATATHQQLEEAQKEHT 1550
Cdd:PRK00409 573 ----KEAQQAIKEAKKEADEIIKElRQLQKGGYASVKAHELIEARKRLNKANEKKE 624
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1168-1527 |
9.21e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.51 E-value: 9.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1168 DQRHLLESKQEKMQQLREKlcqeeeeeILRLHQQ---KEQSLSSLRERLQKaieeeearmreeesqrlswlrAQVQSSTQ 1244
Cdd:pfam10174 384 DLKDMLDVKERKINVLQKK--------IENLQEQlrdKDKQLAGLKERVKS---------------------LQTDSSNT 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1245 ----ADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQmLEQLKEEIEAS--EKSEQ-AALNAAKEKA-------- 1309
Cdd:pfam10174 435 dtalTTLEEALSEKERIIERLKEQREREDRERLEELESLKKE-NKDLKEKVSALqpELTEKeSSLIDLKEHAsslassgl 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1310 -----LQQLREQLEGERKEAVAT---LEKEHSAEL-ERLCSSLEAKHREVVSSLQKKIQEAQ--QKEEAQLQKCLGQVEH 1378
Cdd:pfam10174 514 kkdskLKSLEIAVEQKKEECSKLenqLKKAHNAEEaVRTNPEINDRIRLLEQEVARYKEESGkaQAEVERLLGILREVEN 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1379 RVHQKSYHVAgyEHELSSLLREKRQEVEGEHERRLDK-MKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERL---- 1453
Cdd:pfam10174 594 EKNDKDKKIA--ELESLTLRQMKEQNKKVANIKHGQQeMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTrqel 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1454 -----------QRAHERE--LETVRQEqhkrledlRRRHREQERKLQDLELDLETRAKDvkARLALLEV--------QEE 1512
Cdd:pfam10174 672 datkarlsstqQSLAEKDghLTNLRAE--------RRKQLEEILEMKQEALLAAISEKD--ANIALLELssskkkktQEE 741
|
410
....*....|....*..
gi 530397889 1513 TA--RREKQQLLDVQRQ 1527
Cdd:pfam10174 742 VMalKREKDRLVHQLKQ 758
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
1160-1577 |
1.04e-04 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 47.27 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1160 AVAQVLEQDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLRAQV 1239
Cdd:COG4995 12 ALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALALALLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1240 QSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAkEKALQQLREQLEG 1319
Cdd:COG4995 92 AALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAA-AAAAAAALLALAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1320 ERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSLLR 1399
Cdd:COG4995 171 ALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAAAAL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1400 EKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELET----VRQEQHKRLEDL 1475
Cdd:COG4995 251 AAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAAlallLLAALLLLLAAL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1476 RRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQ----VALKSEEATATHQQLEEAQKEHTH 1551
Cdd:COG4995 331 ALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALllllLALLAALLLLAAALLALAAAQLLR 410
|
410 420
....*....|....*....|....*.
gi 530397889 1552 LLQSNQQLREILDELQARKLKLESQV 1577
Cdd:COG4995 411 LLLAALALLLALAAYAAARLALLALI 436
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1232-1758 |
1.14e-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: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1232 LSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQqkaerasLEQKNRQMLeQLKEEIEaseKSEQAALNAAKEKALQ 1311
Cdd:pfam10174 164 LEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVL-------LDQKEKENI-HLREELH---RRNQLQPDPAKTKALQ 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1312 QLREQLE---GERKEAVATLEKE-----HSAELERLCSSLEAKHREVVSSLQK----KIQEAQQ---KEEAQLQKCLGQV 1376
Cdd:pfam10174 233 TVIEMKDtkiSSLERNIRDLEDEvqmlkTNGLLHTEDREEEIKQMEVYKSHSKfmknKIDQLKQelsKKESELLALQTKL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1377 EHRVHQKS---YHVAGYEHELSSllREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYE--AEERkqraellGHLTGELE 1451
Cdd:pfam10174 313 ETLTNQNSdckQHIEVLKESLTA--KEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQdlTEEK-------STLAGEIR 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1452 RLQR---AHERELETVrqeqHKRLEDLRRRHREQERKLQDLE---LDLETRAKDVKARLALLEvqeeTARREKQQLLDvq 1525
Cdd:pfam10174 384 DLKDmldVKERKINVL----QKKIENLQEQLRDKDKQLAGLKervKSLQTDSSNTDTALTTLE----EALSEKERIIE-- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1526 rqvALKSEEATATHQQLEEAQKehthLLQSNQQLREILDELQARKLKLES-------QVDLLQAQSQQLQKHFSSLEAEA 1598
Cdd:pfam10174 454 ---RLKEQREREDRERLEELES----LKKENKDLKEKVSALQPELTEKESslidlkeHASSLASSGLKKDSKLKSLEIAV 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1599 QKK---------QHLLREVTVEENNASPHFepDLHIEDLRKSLGTNQTKevsSSLSQSKEDLYLDSLSSHNVWHLLSAEG 1669
Cdd:pfam10174 527 EQKkeecsklenQLKKAHNAEEAVRTNPEI--NDRIRLLEQEVARYKEE---SGKAQAEVERLLGILREVENEKNDKDKK 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1670 VAlrSAKEFLVQQTRSMRRRQTALKAAQQHWRHELAS-------AQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSAMR 1742
Cdd:pfam10174 602 IA--ELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQlleearrREDNLADNSQQLQLEELMGALEKTRQELDATKARLS 679
|
570
....*....|....*.
gi 530397889 1743 KGHNLLKKKEEKLNQL 1758
Cdd:pfam10174 680 STQQSLAEKDGHLTNL 695
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1235-1578 |
1.17e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1235 LRAQVQSStqadEDQIRAEQEAsLQKLREELEsQQKAERASLEQKNRQMLEQLKEEIEA---SEKSEQAalnaakEKALQ 1311
Cdd:PRK04863 291 LRRELYTS----RRQLAAEQYR-LVEMARELA-ELNEAESDLEQDYQAASDHLNLVQTAlrqQEKIERY------QADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1312 QLREQLEgERKEAVAtLEKEHSAELERLCSSLEakhrEVVSSLQKKIQEAQQKEEAQlQKCLGQVEHRVH-----QKSYH 1386
Cdd:PRK04863 359 ELEERLE-EQNEVVE-EADEQQEENEARAEAAE----EEVDELKSQLADYQQALDVQ-QTRAIQYQQAVQaleraKQLCG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1387 VAGYEHE-LSSLLREKRQEVEGEHERRLDKmkeEHQQVMAK-AREQYEaeerkQRAELLGHLTGELERlQRAHERELETV 1464
Cdd:PRK04863 432 LPDLTADnAEDWLEEFQAKEQEATEELLSL---EQKLSVAQaAHSQFE-----QAYQLVRKIAGEVSR-SEAWDVARELL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1465 RQ-EQHK----RLEDLRRRHREQERKLQdLELDLETRAKDVKARLAL-----LEVQEETARREkQQLLDVQRQVALKSEE 1534
Cdd:PRK04863 503 RRlREQRhlaeQLQQLRMRLSELEQRLR-QQQRAERLLAEFCKRLGKnlddeDELEQLQEELE-ARLESLSESVSEARER 580
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 530397889 1535 ATATHQQLEEaqkehthllqsnqqlreildelqarklkLESQVD 1578
Cdd:PRK04863 581 RMALRQQLEQ----------------------------LQARIQ 596
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1394-1548 |
1.51e-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: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1394 LSSLLREKRQEV-EGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRaellghltgELERLQRAH-ERELETVRQEQHKR 1471
Cdd:COG2268 186 LDALGRRKIAEIiRDARIAEAEAERETEIAIAQANREAEEAELEQER---------EIETARIAEaEAELAKKKAEERRE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1472 LEDLRRR-----HREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLL--DVQRQVALKSEEATATHQQlEE 1544
Cdd:COG2268 257 AETARAEaeaayEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKpaEAEKQAAEAEAEAEAEAIR-AK 335
|
....
gi 530397889 1545 AQKE 1548
Cdd:COG2268 336 GLAE 339
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1246-1556 |
1.72e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.40 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1246 DEDQIRAEQEASlQKLREELESQQKAERASLEQKNRQMLEQ---------LKEEIEASEKSEQAALN---AAKEKALQQL 1313
Cdd:pfam02029 1 IEDEEEAARERR-RRAREERRRQKEEEEPSGQVTESVEPNEhnsyeedseLKPSGQGGLDEEEAFLDrtaKREERRQKRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1314 REQLEGE----------------RKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQlqkclgQVE 1377
Cdd:pfam02029 80 QEALERQkefdptiadekesvaeRKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVR------QAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1378 HRVHQKSYHVAgyEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAkaREQYEAEERKQRAELLGHLTGELERLQRAH 1457
Cdd:pfam02029 154 EEGEEEEDKSE--EAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLD--QKRGHPEVKSQNGEEEVTKLKVTTKRRQGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1458 ERELETVRQEQH------KRLEDLRRRHREQER--------KLQDLELDLETRAKDVKARLALLEvqEETARREKQQLld 1523
Cdd:pfam02029 230 LSQSQEREEEAEvfleaeQKLEELRRRRQEKESeefeklrqKQQEAELELEELKKKREERRKLLE--EEEQRRKQEEA-- 305
|
330 340 350
....*....|....*....|....*....|...
gi 530397889 1524 vQRQVAlKSEEATATHQQLEEAQKEHTHLLQSN 1556
Cdd:pfam02029 306 -ERKLR-EEEEKRRMKEEIERRRAEAAEKRQKL 336
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1354-1525 |
2.16e-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: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1354 LQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHV-AGY------------------------EHELSSLLREKrqEVEGE 1408
Cdd:cd16269 107 CKQNEEASSKRCQALLQELSAPLEEKISQGSYSVpGGYqlyledreklvekyrqvprkgvkaEEVLQEFLQSK--EAEAE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1409 HERRLDKMKEEHQQVMAKAREQYEAEErkQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQD 1488
Cdd:cd16269 185 AILQADQALTEKEKEIEAERAKAEAAE--QERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALE 262
|
170 180 190
....*....|....*....|....*....|....*..
gi 530397889 1489 LELDLETRakdvkarlALLEVQEETARREKQQLLDVQ 1525
Cdd:cd16269 263 SKLKEQEA--------LLEEGFKEQAELLQEEIRSLK 291
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1009-1350 |
2.49e-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: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1009 EDKDDSQSSQDELQSKqsKGLEERLSPPLPHEERAQSPPRSLATEEEPPQGpEGQPEWKEAE-------ELGEDSAASLS 1081
Cdd:TIGR02169 671 SEPAELQRLRERLEGL--KRELSSLQSELRRIENRLDELSQELSDASRKIG-EIEKEIEQLEqeeeklkERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1082 lQLSLQREQAPSPPAACEKGKEQhsQAEELGPGQEEAEDPEEKVAVSPTPPVSPEVRSTEpvappEQLS--EAALKAMEE 1159
Cdd:TIGR02169 748 -SLEQEIENVKSELKELEARIEE--LEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLE-----EEVSriEARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1160 AVaQVLEQDQRHLLESKQEKMQQLRE------KLCQEEEEEILRL---------HQQKEQSLSSLRERLQKAIEEEEARM 1224
Cdd:TIGR02169 820 KL-NRLTLEKEYLEKEIQELQEQRIDlkeqikSIEKEIENLNGKKeeleeeleeLEAALRDLESRLGDLKKERDELEAQL 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1225 REEEsQRLSWLRAQVQsstqaDEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQM-LEQLKEEIEASEKsEQAALN 1303
Cdd:TIGR02169 899 RELE-RKIEELEAQIE-----KKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELsLEDVQAELQRVEE-EIRALE 971
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 530397889 1304 AAKEKALQQLREQLE--GERKEAVATLEKEHSAELERLcSSLEAKHREV 1350
Cdd:TIGR02169 972 PVNMLAIQEYEEVLKrlDELKEKRAKLEEERKAILERI-EEYEKKKREV 1019
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1345-1521 |
2.52e-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: 44.92 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1345 AKHREVVSSLQKKIQEAQQkEEAQLQKCLGQVEHRVHqksyhvagyehELSSLLREKRQEVEgEHERRLDKMKEehQQVM 1424
Cdd:COG1579 20 DRLEHRLKELPAELAELED-ELAALEARLEAAKTELE-----------DLEKEIKRLELEIE-EVEARIKKYEE--QLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1425 AKAREQYEAeerkqraellghLTGELERLQRAHErELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARL 1504
Cdd:COG1579 85 VRNNKEYEA------------LQKEIESLKRRIS-DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170
....*....|....*..
gi 530397889 1505 ALLEVQEETARREKQQL 1521
Cdd:COG1579 152 AELEAELEELEAEREEL 168
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1165-1501 |
2.60e-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: 46.17 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1165 LEQDQRHLLESKQEKMQQLREKlcQEEEEEILRLHQQKEQSLSSLRERLQKaieeeearmreeesqrlswLRAQVQSSTQ 1244
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEK--QNEIEKLKKENQSYKQEIKNLESQIND-------------------LESKIQNQEK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1245 adEDQIRAEQEASLQKLREELESQQKAERASLEqKNRQMLEQLKEEIEASEKsEQAALNAAKEKALQQLrEQLEGERKEA 1324
Cdd:TIGR04523 406 --LNQQKDEQIKKLQQEKELLEKEIERLKETII-KNNSEIKDLTNQDSVKEL-IIKNLDNTRESLETQL-KVLSRSINKI 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1325 VATLEKEhSAELERLCSSLEAKHREV------VSSLQKKIQEAQQKEEaQLQKCLGQVEHRVHQKSYHVAGYEHELSSLL 1398
Cdd:TIGR04523 481 KQNLEQK-QKELKSKEKELKKLNEEKkeleekVKDLTKKISSLKEKIE-KLESEKKEKESKISDLEDELNKDDFELKKEN 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1399 REKrqeVEGEHERRLDKMKEEHQQVMAKARE------QYEAEERKQRAELLghltgELERLQRAHERELETVRQEqHKRL 1472
Cdd:TIGR04523 559 LEK---EIDEKNKEIEELKQTQKSLKKKQEEkqelidQKEKEKKDLIKEIE-----EKEKKISSLEKELEKAKKE-NEKL 629
|
330 340
....*....|....*....|....*....
gi 530397889 1473 EdlrrrhrEQERKLQDLELDLETRAKDVK 1501
Cdd:TIGR04523 630 S-------SIIKNIKSKKNKLKQEVKQIK 651
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1341-1548 |
3.51e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1341 SSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHqksyhvagyehelssllrEKRQEVEGEHERRLDKMKEEH 1420
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIH------------------KLRNEFEKELRERRNELQKLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1421 QQVMAKareqyeaEER-KQRAELLGHLTGELErlqrAHERELETVRQEQHKRLEDLRRRHREQERKLQDL-ELDLEtrak 1498
Cdd:PRK12704 89 KRLLQK-------EENlDRKLELLEKREEELE----KKEKELEQKQQELEKKEEELEELIEEQLQELERIsGLTAE---- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 530397889 1499 dvKARLALLEVQEETARREKQQLLdvqRQValkSEEATathqqlEEAQKE 1548
Cdd:PRK12704 154 --EAKEILLEKVEEEARHEAAVLI---KEI---EEEAK------EEADKK 189
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1394-1575 |
3.54e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1394 LSSLLREKRQEVEgEHERRLDKMKEEHQQVMAKAREQYEAEE----RKQRAELLGHLTgELERLQRAHERELETVRQE-- 1467
Cdd:COG3206 180 LEEQLPELRKELE-EAEAALEEFRQKNGLVDLSEEAKLLLQQlselESQLAEARAELA-EAEARLAALRAQLGSGPDAlp 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1468 ---QHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLL-DVQRQVALKSEEATATHQQLE 1543
Cdd:COG3206 258 ellQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILaSLEAELEALQAREASLQAQLA 337
|
170 180 190
....*....|....*....|....*....|..
gi 530397889 1544 EAQKEHTHLLQSNQQLREILDELQARKLKLES 1575
Cdd:COG3206 338 QLEARLAELPELEAELRRLEREVEVARELYES 369
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
1259-1361 |
3.92e-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: 43.29 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1259 QKLREELESQQKAERASLEQKNRQmLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAvatlEKEhsaeler 1338
Cdd:COG2825 42 KAAQKKLEKEFKKRQAELQKLEKE-LQALQEKLQKEAATLSEEERQKKERELQKKQQELQRKQQEA----QQD------- 109
|
90 100
....*....|....*....|...
gi 530397889 1339 lcssLEAKHREVVSSLQKKIQEA 1361
Cdd:COG2825 110 ----LQKRQQELLQPILEKIQKA 128
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1154-1516 |
4.25e-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: 45.03 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1154 LKAMEEAVAQVLEQDQRHLL----ESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKaieeeearMREEES 1229
Cdd:pfam15558 37 LRRRDQKRQETLERERRLLLqqsqEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAED--------QENQRQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1230 QRLSWLRAQVQSSTQADEDQIRaEQEASLQKLRE--ELESQQKAERASLEQKNRQMLEQLKeeIEASEKSEQAALNAAKE 1307
Cdd:pfam15558 109 EKLERARQEAEQRKQCQEQRLK-EKEEELQALREqnSLQLQERLEEACHKRQLKEREEQKK--VQENNLSELLNHQARKV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1308 KALQQLREQLEGERKeavaTLEKEHSAELERLCSSLEAKHREvvsslqkkIQEAQQKEEAQLQKclgqvehrvhqksyhv 1387
Cdd:pfam15558 186 LVDCQAKAEELLRRL----SLEQSLQRSQENYEQLVEERHRE--------LREKAQKEEEQFQR---------------- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1388 agyehelsslLREKRQEVEGEHERRLDKMKEEHQQVMAKAReQYEAEERKQRAELLGHLTGELERLQRAHERELEtvRQE 1467
Cdd:pfam15558 238 ----------AKWRAEEKEEERQEHKEALAELADRKIQQAR-QVAHKTVQDKAQRARELNLEREKNHHILKLKVE--KEE 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 530397889 1468 QHKR---LEDLRRRHREQERKLQDLELDLETRAKDVKARLALLE-VQEETARR 1516
Cdd:pfam15558 305 KCHRegiKEAIKKKEQRSEQISREKEATLEEARKTARASFHMREkVREETNNR 357
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1151-1363 |
4.49e-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: 45.71 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1151 EAALKAMEEAVAQVleqdqrhlleSKQEKMQQLREKLCQeeeeeiLRLHQQKEQSLSSLRERLQKAieeeearmreeeSQ 1230
Cdd:COG3096 475 EKAYELVCKIAGEV----------ERSQAWQTARELLRR------YRSQQALAQRLQQLRAQLAEL------------EQ 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1231 RLswlRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKN----------RQMLEQLKEEIEASEKSEQA 1300
Cdd:COG3096 527 RL---RQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAaeaveqrselRQQLEQLRARIKELAARAPA 603
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1301 ALNAAkeKALQQLREQLEGERKEAVA-------TLEKEHSAELERlcSSLEAKHREvvssLQKKIQEAQQ 1363
Cdd:COG3096 604 WLAAQ--DALERLREQSGEALADSQEvtaamqqLLEREREATVER--DELAARKQA----LESQIERLSQ 665
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1247-1371 |
4.89e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1247 EDQIRAEQEA--SLQKLREELESQQKAERASLEQKNRQM--------LEQLKEEIEASEKSEQAAlnaakEKALQQLREQ 1316
Cdd:COG1579 44 EARLEAAKTEleDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnnkeYEALQKEIESLKRRISDL-----EDEILELMER 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 530397889 1317 LEgERKEAVATLEKEHsAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQK 1371
Cdd:COG1579 119 IE-ELEEELAELEAEL-AELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
1413-1576 |
5.08e-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: 43.60 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1413 LDKMKEEHQQVMAKAREQY-----EAEERKQRAEL-LGHLTGELERLQRAHERELETVRQeQHKRLEDLRRRHREQERKL 1486
Cdd:pfam14988 9 LAKKTEEKQKKIEKLWNQYvqeceEIERRRQELASrYTQQTAELQTQLLQKEKEQASLKK-ELQALRPFAKLKESQEREI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1487 QDLELDLET--RAKDVKARLALLEVQEETARREKQ-QLLDVQRQVALKSEEATATHQQLEEAQK----EHTHLL-QSNQQ 1558
Cdd:pfam14988 88 QDLEEEKEKvrAETAEKDREAHLQFLKEKALLEKQlQELRILELGERATRELKRKAQALKLAAKqalsEFCRSIkRENRQ 167
|
170 180
....*....|....*....|....*
gi 530397889 1559 LREIL-------DELQARKLKLESQ 1576
Cdd:pfam14988 168 LQKELlqliqetQALEAIKSKLENR 192
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
1263-1578 |
5.28e-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: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1263 EELESQQKAERASLEQKNrQMLEQLKEEIEASEKSEQAALNAAKEKA--LQQLREQLEGERKEAVATLEKehsaeLERLC 1340
Cdd:pfam09728 3 ARELMQLLNKLDSPEEKL-AALCKKYAELLEEMKRLQKDLKKLKKKQdqLQKEKDQLQSELSKAILAKSK-----LEKLC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1341 SSLEAKHREVVSSLQKKIQEAQQKEE---AQLQKCLGQVEHRVHQKSYHVAGYEHElSSLLREKRQEVEGEHERR----- 1412
Cdd:pfam09728 77 RELQKQNKKLKEESKKLAKEEEEKRKelsEKFQSTLKDIQDKMEEKSEKNNKLREE-NEELREKLKSLIEQYELRelhfe 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1413 -LDKMKEEHQQ-VMAKAREQYEAEERKQRaellghltgelerlqrahERELETVRQEQhKRLEDLRrrhrEQERKLQD-L 1489
Cdd:pfam09728 156 kLLKTKELEVQlAEAKLQQATEEEEKKAQ------------------EKEVAKARELK-AQVQTLS----ETEKELREqL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1490 ELDLEtRAKDVKARLALLEVQEETARREKQQLLDVQRQValkSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQAR 1569
Cdd:pfam09728 213 NLYVE-KFEEFQDTLNKSNEVFTTFKKEMEKMSKKIKKL---EKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKK 288
|
....*....
gi 530397889 1570 KLKLESQVD 1578
Cdd:pfam09728 289 LEKLENLCR 297
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1259-1364 |
6.30e-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: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1259 QKLREELESQQKAERASLEQKNRQmLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKehsaeler 1338
Cdd:smart00935 17 KAAQKQLEKEFKKRQAELEKLEKE-LQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQK-------- 87
|
90 100
....*....|....*....|....*.
gi 530397889 1339 lcssleaKHREVVSSLQKKIQEAQQK 1364
Cdd:smart00935 88 -------RQQEELQKILDKINKAIKE 106
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1243-1523 |
6.92e-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: 6.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1243 TQADEDQIRAEQEASLQKLREELESQQKAERasleqKNRQMLEQLKEEIEASEKSEQAALNAAKEkaLQQLREQLEGERK 1322
Cdd:pfam05667 217 AAAQEWEEEWNSQGLASRLTPEEYRKRKRTK-----LLKRIAEQLRSAALAGTEATSGASRSAQD--LAELLSSFSGSST 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1323 EAVATLEKEHSAELERLCSSLEAKHREVVSSLQKK----IQEAQQKEEAQLQKCLGQVEHRVHQksyhvagYEHELSSLL 1398
Cdd:pfam05667 290 TDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVEteeeLQQQREEELEELQEQLEDLESSIQE-------LEKEIKKLE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1399 REKRQ-EVEGEHERRLDKMKEEHQQVMAKAREQY-EAEER--------KQRAELLGHLTGELERLQRAHERELETVRQEQ 1468
Cdd:pfam05667 363 SSIKQvEEELEELKEQNEELEKQYKVKKKTLDLLpDAEENiaklqalvDASAQRLVELAGQWEKHRVPLIEEYRALKEAK 442
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 530397889 1469 HKRLEdlrrrhrEQERKLQDLEldlETRAKdvkarlaLLEVQEETARRE--KQQLLD 1523
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 ... |
1248-1319 |
7.19e-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: 7.19e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530397889 1248 DQIRAEQEASLQKLREELESQQKaERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKeKALQQLREQLEG 1319
Cdd:pfam10211 118 EQGKAELEKKIADLEEEKEELEK-QVAELKAKCEAIEKREEERRQAEEKKHAEEIAFLK-KTNQQLKAQLER 187
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1450-1614 |
8.08e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 8.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1450 LERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLE-----LDLETRAKDVKARLALLEVQEETARRE------- 1517
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRqknglVDLSEEAKLLLQQLSELESQLAEARAElaeaear 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1518 ---------------------------KQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQS-NQQLREILDELQAR 1569
Cdd:COG3206 242 laalraqlgsgpdalpellqspviqqlRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILASLEAE 321
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 530397889 1570 KLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLREVTVEENN 1614
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVAREL 366
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1276-1570 |
9.97e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 9.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1276 LEQKNRQMLEQLKEEIEASEKSeQAALNAAKEKaLQQLREQLEGERK---EAVATLEKEHS------AELERLCSS---L 1343
Cdd:PRK04778 117 IEEDIEQILEELQELLESEEKN-REEVEQLKDL-YRELRKSLLANRFsfgPALDELEKQLEnleeefSQFVELTESgdyV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1344 EAkhREVVSSLQKKIQEAQQKEE------AQLQKCL-GQVEhrvhqksyhvagyehELSSLLREkrQEVEGEH------E 1410
Cdd:PRK04778 195 EA--REILDQLEEELAALEQIMEeipellKELQTELpDQLQ---------------ELKAGYRE--LVEEGYHldhldiE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1411 RRLDKMKEEHQQVMAkareQYEAEERKQRAELLGHLTGELERLQRAHERELETvRQEQHKRLEDLRRRHREQERKLQDLE 1490
Cdd:PRK04778 256 KEIQDLKEQIDENLA----LLEELDLDEAEEKNEEIQERIDQLYDILEREVKA-RKYVEKNSDTLPDFLEHAKEQNKELK 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1491 LDLETrakdVKARLALLEVQEETARREKQQLLDVQRQVaLKSEEATATHQ---------------QLEEAQKEHTHLLQS 1555
Cdd:PRK04778 331 EEIDR----VKQSYTLNESELESVRQLEKQLESLEKQY-DEITERIAEQEiayselqeeleeilkQLEEIEKEQEKLSEM 405
|
330
....*....|....*
gi 530397889 1556 NQQLREilDELQARK 1570
Cdd:PRK04778 406 LQGLRK--DELEARE 418
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1450-1633 |
1.03e-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: 42.99 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1450 LERLQRAHER--ELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDV--Q 1525
Cdd:COG1579 9 LLDLQELDSEldRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1526 RQV-ALKSEEATATHQQ--LEEAQKEHTHLLqsnQQLREILDELQARKLKLESQVDLLQaqsqqlqkhfSSLEAEAQKKQ 1602
Cdd:COG1579 89 KEYeALQKEIESLKRRIsdLEDEILELMERI---EELEEELAELEAELAELEAELEEKK----------AELDEELAELE 155
|
170 180 190
....*....|....*....|....*....|...
gi 530397889 1603 HLLREVTVEENNASPHFEPDL--HIEDLRKSLG 1633
Cdd:COG1579 156 AELEELEAEREELAAKIPPELlaLYERIRKRKN 188
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1285-1371 |
1.07e-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: 41.42 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1285 EQLKEEIEASEKSEQAALNAaKEKALQQLREQLEGERkeavATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQK 1364
Cdd:smart00935 17 KAAQKQLEKEFKKRQAELEK-LEKELQKLKEKLQKDA----ATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQE 91
|
....*..
gi 530397889 1365 EEAQLQK 1371
Cdd:smart00935 92 ELQKILD 98
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1390-1548 |
1.15e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1390 YEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAEllghLTGELERLQRAHEreletVRQEQH 1469
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREE----LQREEERLVQKEE-----QLDARA 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530397889 1470 KRLEDLRRRHREQERKLQDLELDLETRAKDVKARlaLLEVQEETARREKQQLLDvQRQVALKSEEATATHQQLEEAQKE 1548
Cdd:PRK12705 98 EKLDNLENQLEEREKALSARELELEELEKQLDNE--LYRVAGLTPEQARKLLLK-LLDAELEEEKAQRVKKIEEEADLE 173
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1064-1504 |
1.32e-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: 44.06 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1064 PEWKEAEELGEDSAASLSLQLslQREQAPSPPAACEKGKEQHSQAEE-LGPGQEEAEDPEEKVAVsptppVSPEVrstEP 1142
Cdd:pfam12128 567 PEVWDGSVGGELNLYGVKLDL--KRIDVPEWAASEEELRERLDKAEEaLQSAREKQAAAEEQLVQ-----ANGEL---EK 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1143 VAPPEQLSEAALKAMEEAVAQ---VLEQDQRHLLES-------KQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRER 1212
Cdd:pfam12128 637 ASREETFARTALKNARLDLRRlfdEKQSEKDKKNKAlaerkdsANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEK 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1213 LQKaiEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKL--REELESQQKAERASLEQK------NRQML 1284
Cdd:pfam12128 717 QAY--WQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLgvDPDVIAKLKREIRTLERKieriavRRQEV 794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1285 ---EQLKEEIEASEKSEQAALNAAKEKALQQLREQL---EGERKEAVATLEKEHSAeLERLCSSLEAKHREVVSSLQK-- 1356
Cdd:pfam12128 795 lryFDWYQETWLQRRPRLATQLSNIERAISELQQQLarlIADTKLRRAKLEMERKA-SEKQQVRLSENLRGLRCEMSKla 873
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1357 KIQEAQQKEEAQLQ--KCLGQVEHRVHQKSYHVAGYEHELS---SLLREKRQEVEGEHERRLdkMKEEHQQVMAKAREQY 1431
Cdd:pfam12128 874 TLKEDANSEQAQGSigERLAQLEDLKLKRDYLSESVKKYVEhfkNVIADHSGSGLAETWESL--REEDHYQNDKGIRLLD 951
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530397889 1432 EAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQ---DLELDLEtRAKDVKARL 1504
Cdd:pfam12128 952 YRKLVPYLEQWFDVRVPQSIMVLREQVSILGVDLTEFYDVLADFDRRIASFSRELQrevGEEAFFE-GVSESAVRI 1026
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
1353-1548 |
1.35e-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: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1353 SLQKKIQEAQQK-EEAQL-QKCLGQVEHRvHQKSYH-VAGYEHELSSLLREKRQEVEgeherrldKMKEEHQQVMAKARE 1429
Cdd:pfam15619 15 ELQNELAELQSKlEELRKeNRLLKRLQKR-QEKALGkYEGTESELPQLIARHNEEVR--------VLRERLRRLQEKERD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1430 QyEAEERKQRAELLgHLTGELERLQR-AHERELETvRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLAlle 1508
Cdd:pfam15619 86 L-ERKLKEKEAELL-RLRDQLKRLEKlSEDKNLAE-REELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLA--- 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 530397889 1509 vqeetarREKQQLLDVQRQVALKSEEATATHQQLEEAQKE 1548
Cdd:pfam15619 160 -------AEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
1451-1571 |
1.49e-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: 43.05 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1451 ERLQRAHERELETVRQEQHkrLEDLRRRHREQERKLQDLELDLETRAKDVKA-RLALLEVQEETARREKQQLLDVQRQVA 1529
Cdd:pfam07767 199 ELLQKAVEAEKKRLKEEEK--LERVLEKIAESAATAEAREEKRKTKAQRNKEkRRKEEEREAKEEKALKKKLAQLERLKE 276
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 530397889 1530 LKSEEAtathQQLEEAQKEHTHLLQSNQQLREILDELQARKL 1571
Cdd:pfam07767 277 IAKEIA----EKEKEREEKAEARKREKRKKKKEEKKLRPRKL 314
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1204-1543 |
1.49e-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: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1204 QSLSSLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQ---QKAERASLEQKN 1280
Cdd:pfam07111 59 QALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAAlagAEMVRKNLEEGS 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1281 RQMLEqlkeEIEASEKSEQAALNAAKEKALQQLREQLEGERKeAVATLEKEHSAELERLcsSLEAKHREVvssLQKKIQE 1360
Cdd:pfam07111 139 QRELE----EIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEK-SLNSLETKRAGEAKQL--AEAQKEAEL---LRKQLSK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1361 AQQKEEAQ------LQKCLG-QVEHRVHQKSYHVAGYEH-ELSSLLREKRQEVEGEHE---------RRLDKMKEEHQQV 1423
Cdd:pfam07111 209 TQEELEAQvtlvesLRKYVGeQVPPEVHSQTWELERQELlDTMQHLQEDRADLQATVEllqvrvqslTHMLALQEEELTR 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1424 MAKAREQYEAEERKQRAELLGH-------LTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQ---ERKLQDLELDL 1493
Cdd:pfam07111 289 KIQPSDSLEPEFPKKCRSLLNRwrekvfaLMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQailQRALQDKAAEV 368
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 530397889 1494 ETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLE 1543
Cdd:pfam07111 369 EVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLE 418
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
1308-1552 |
1.56e-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: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1308 KALQQLREQLEGerkeaVATLEkEHSAELERLCSSLEAKHREVVSSLQKkiqeaQQKEEAQLQKCLGQVEHrvhqksyhv 1387
Cdd:pfam09728 1 KAARELMQLLNK-----LDSPE-EKLAALCKKYAELLEEMKRLQKDLKK-----LKKKQDQLQKEKDQLQS--------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1388 agyEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMakareqyeAEERKQRAELLGHLTGELErlqraherELETVRQE 1467
Cdd:pfam09728 61 ---ELSKAILAKSKLEKLCRELQKQNKKLKEESKKLA--------KEEEEKRKELSEKFQSTLK--------DIQDKMEE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1468 QHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLAL--LEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEA 1545
Cdd:pfam09728 122 KSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKTkeLEVQLAEAKLQQATEEEEKKAQEKEVAKARELKAQVQTL 201
|
....*..
gi 530397889 1546 QKEHTHL 1552
Cdd:pfam09728 202 SETEKEL 208
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
903-1315 |
1.56e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 903 KASEKEAPEDTVDAGEEGSRREEAAK--EPKKKASALEEGSSDA---SQELEISEHMKEPQLSDSIASDPKSFHGLDFGF 977
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAKKADEAKKkaEEAKKADEAKKKAEEAkkkADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 978 RSRISEHLLDVDvlspvlggACRQAQQplgIEDKDDSQSSQDELQSKQSKGLEERLSPPLPHEERAQSPPRslATEEEPP 1057
Cdd:PTZ00121 1532 EAKKADEAKKAE--------EKKKADE---LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE--ARIEEVM 1598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1058 QGPEGQPEWKEAEELGEDSAASLSLQLSLQREQAPSPPAACEKGKEQHSQAEELGPGQEEAE--DPEEKVAVSPTPPVSP 1135
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikAAEEAKKAEEDKKKAE 1678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1136 EVRSTEPvapPEQLSEAALKAMEEAVAQVLEqdqrhlLESKQEKMQQLREKLCQEEEEEILRLHQQKEQSlsslRERLQK 1215
Cdd:PTZ00121 1679 EAKKAEE---DEKKAAEALKKEAEEAKKAEE------LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEA----EEDKKK 1745
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1216 AieeEEARMREEESQRLswlrAQVQSSTQADEDQIRAEQEASLQklrEELESQQKAERASLEQKNRQMLEQLKEEIEASE 1295
Cdd:PTZ00121 1746 A---EEAKKDEEEKKKI----AHLKKEEEKKAEEIRKEKEAVIE---EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGK 1815
|
410 420
....*....|....*....|
gi 530397889 1296 KSeQAALNAAKEKALQQLRE 1315
Cdd:PTZ00121 1816 EG-NLVINDSKEMEDSAIKE 1834
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1248-1569 |
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 530397889 1248 DQIRAEQEASLQKLREELESQQ--------------KAERASLEQK------NRQMLEQLKEEIEASEKSEQAALNAAKE 1307
Cdd:pfam15964 359 EQLKSELERQKERLEKELASQQekraqekealrkemKKEREELGATmlalsqNVAQLEAQVEKVTREKNSLVSQLEEAQK 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1308 KALQQ----------LREQLEG---ERKEAvatlEKEHSAELERLCSSLEAKHREV------VSSLQKKIQEAQQK---- 1364
Cdd:pfam15964 439 QLASQemdvtkvcgeMRYQLNQtkmKKDEA----EKEHREYRTKTGRQLEIKDQEIeklgleLSESKQRLEQAQQDaara 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1365 --EEAQLQKCLGQVEHRVHqksyhvagyeheLSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAEL 1442
Cdd:pfam15964 515 reECLKLTELLGESEHQLH------------LTRLEKESIQQSFSNEAKAQALQAQQREQELTQKMQQMEAQHDKTVNEQ 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1443 LGHLTGelerlQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLL 1522
Cdd:pfam15964 583 YSLLTS-----QNTFIAKLKEECCTLAKKLEEITQKSRSEVEQLSQEKEYLQDRLEKLQKRNEELEEQCVQHGRMHERMK 657
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 530397889 1523 DVQRQVALKSEeatATHQQLEEAQKEHTHLLQSNQQLREILDELQAR 1569
Cdd:pfam15964 658 QRLRQLDKHCQ---ATAQQLVQLLSKQNQLFKERQNLTEEVQSLRSQ 701
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
1239-1368 |
1.62e-03 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 43.55 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1239 VQSSTQADEDQI-RAEQEASL-----QKLREELESQQKAEraSLEQKNRQMLEQLKEEIEASEKSEQaalnaakEKALQQ 1312
Cdd:PRK00290 494 ITASSGLSDEEIeRMVKDAEAnaeedKKRKELVEARNQAD--SLIYQTEKTLKELGDKVPADEKEKI-------EAAIKE 564
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 530397889 1313 LREQLEGERKEAVatleKEHSAELErlcssleakhrEVVSSLQKKIQEAQQKEEAQ 1368
Cdd:PRK00290 565 LKEALKGEDKEAI----KAKTEELT-----------QASQKLGEAMYQQAQAAQGA 605
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1151-1339 |
1.64e-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: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1151 EAALKAMEEAVAQVLEQdqrhlLESKQEKMQQLREKLcqeeeEEILRLHQQKEQSLSSLRERLQkaieeeearmreeesq 1230
Cdd:COG1579 23 EHRLKELPAELAELEDE-----LAALEARLEAAKTEL-----EDLEKEIKRLELEIEEVEARIK---------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1231 rlswlRAQVQSSTQADEDQIRA--EQEASLQKLREELESQQKAERASLEQKNRQmLEQLKEEIEASEK---SEQAALNAA 1305
Cdd:COG1579 77 -----KYEEQLGNVRNNKEYEAlqKEIESLKRRISDLEDEILELMERIEELEEE-LAELEAELAELEAeleEKKAELDEE 150
|
170 180 190
....*....|....*....|....*....|....
gi 530397889 1306 KEKaLQQLREQLEGERKEAVATLEKEHSAELERL 1339
Cdd:COG1579 151 LAE-LEAELEELEAEREELAAKIPPELLALYERI 183
|
|
| DUF1978 |
pfam09321 |
Domain of unknown function (DUF1978); Members of this family are found in various hypothetical ... |
1399-1576 |
1.73e-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: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1399 REKRQEVEgEHERRLDKMKEEHQQ-VMAKAREQYEAEERKQRAELLGHLTGELER-LQRAHERELETVRQeqhkRLEDLR 1476
Cdd:pfam09321 53 RDALSEIS-RHELWEKKAHLKHLEsLYTQARDRFEKQSSKKNQKELEEAEQEYLSsWEDVKDQEIERVQE----RLQALQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1477 RRH-----REQERKLQD---LELDLETRAKDVKARL-ALLEVQEETARREKQQLLDV-----QRQVALKSEEATATHQQL 1542
Cdd:pfam09321 128 ALYpevsvSEEETEGQEtvtPTVDLETALGRIEESYrECVRDQEDYWKEEESKEVEMsaefrEEGGKKKSEEFQEQLGSL 207
|
170 180 190
....*....|....*....|....*....|....
gi 530397889 1543 EEAQKEHThllqsnqqlrEILDELQARKLKLESQ 1576
Cdd:pfam09321 208 ERFLKEHS----------EELEVLEKHILKHESE 231
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1421-1571 |
1.78e-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: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1421 QQVMAKAREQYEAEERKQR-------AELLGHLTgelERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLE--- 1490
Cdd:COG2433 353 ERVEKKVPPDVDRDEVKARvirglsiEEALEELI---EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEaev 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1491 LDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARK 1570
Cdd:COG2433 430 EELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGE 509
|
.
gi 530397889 1571 L 1571
Cdd:COG2433 510 L 510
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1274-1367 |
1.94e-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: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1274 ASLEQKNRQmLEQLKEEIEASEKsEQAALNAAKEKALQQLREQLEGERKEAVA--TLEKEHSAELERLCSSLEAKHrEVV 1351
Cdd:COG0542 411 EELDELERR-LEQLEIEKEALKK-EQDEASFERLAELRDELAELEEELEALKArwEAEKELIEEIQELKEELEQRY-GKI 487
|
90
....*....|....*.
gi 530397889 1352 SSLQKKIQEAQQKEEA 1367
Cdd:COG0542 488 PELEKELAELEEELAE 503
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1259-1364 |
1.99e-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: 40.64 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1259 QKLREELESQQKAERASLEQKNRQmLEQLKEEIEAsEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKehsaeler 1338
Cdd:pfam03938 18 KAAQAQLEKKFKKRQAELEAKQKE-LQKLYEELQK-DGALLEEEREEKEQELQKKEQELQQLQQKAQQELQK-------- 87
|
90 100
....*....|....*....|....*.
gi 530397889 1339 lcssleaKHREVVSSLQKKIQEAQQK 1364
Cdd:pfam03938 88 -------KQQELLQPIQDKINKAIKE 106
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1251-1578 |
2.03e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1251 RAEQEASLQKL--REELESQQKAERASLEQ---------KNRQMLEQLKEEIEASE---KSEQAALNAAKEKALQQLREQ 1316
Cdd:PRK11281 38 EADVQAQLDALnkQKLLEAEDKLVQQDLEQtlalldkidRQKEETEQLKQQLAQAPaklRQAQAELEALKDDNDEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1317 LEgerKEAVATLEK---EHSAELERLCSSLEAKHREVVSS------LQKKIQEAQQkeeaQLQkclgqvehrvhqksyhv 1387
Cdd:PRK11281 118 LS---TLSLRQLESrlaQTLDQLQNAQNDLAEYNSQLVSLqtqperAQAALYANSQ----RLQ----------------- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1388 agyehELSSLLreKRQEVEGEHERRLDKMKEEHQQVMAKAREQYeaeerkQRAELLGH--LTgELERLQraheRELETVR 1465
Cdd:PRK11281 174 -----QIRNLL--KGGKVGGKALRPSQRVLLQAEQALLNAQNDL------QRKSLEGNtqLQ-DLLQKQ----RDYLTAR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1466 QEQhkrledlrrrhreQERKLQDL-ELDLETRAKDVKARLALLEVQEETARREKQQLldVQRQvalkSEEATATHQQLEE 1544
Cdd:PRK11281 236 IQR-------------LEHQLQLLqEAINSKRLTLSEKTVQEAQSQDEAARIQANPL--VAQE----LEINLQLSQRLLK 296
|
330 340 350
....*....|....*....|....*....|....
gi 530397889 1545 AQKEHTHLLQSNQQLREILDELQARKLKLESQVD 1578
Cdd:PRK11281 297 ATEKLNTLTQQNLRVKNWLDRLTQSERNIKEQIS 330
|
|
| PRK11091 |
PRK11091 |
aerobic respiration control sensor protein ArcB; Provisional |
1459-1532 |
2.14e-03 |
|
aerobic respiration control sensor protein ArcB; Provisional
Pssm-ID: 236842 [Multi-domain] Cd Length: 779 Bit Score: 43.01 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1459 RELETVRQEQHK---RLEDLRRRHREQERKLQD----LELDLETRAKDVKARLALL-EVQEETARREKQQLLDVQRQVAL 1530
Cdd:PRK11091 78 EQLEESRQRLSRlvaKLEEMRERDLELNVQLKDniaqLNQEIAEREKAEEARQEAFeQLKNEIKEREETQIELEQQSSLL 157
|
..
gi 530397889 1531 KS 1532
Cdd:PRK11091 158 RS 159
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1394-1567 |
2.22e-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: 43.19 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1394 LSSLLREKRQEvEGEHERRLDKMKEEhqqvmAKAREQYEAEERKQRAELLGHLTGELERLQRAHE---RELETVRQEQhK 1470
Cdd:pfam05557 11 LSQLQNEKKQM-ELEHKRARIELEKK-----ASALKRQLDRESDRNQELQKRIRLLEKREAEAEEalrEQAELNRLKK-K 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1471 RLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHT 1550
Cdd:pfam05557 84 YLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQS 163
|
170
....*....|....*..
gi 530397889 1551 HLLQSNQQLREILDELQ 1567
Cdd:pfam05557 164 SLAEAEQRIKELEFEIQ 180
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1304-1479 |
2.30e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1304 AAKEKALQQLREQLeGERKEAVATLEKEHsAELERLCSSLEAKHREV---VSSLQKKIQEAQQKEEaQLQKCLGQVehrv 1380
Cdd:COG1579 13 QELDSELDRLEHRL-KELPAELAELEDEL-AALEARLEAAKTELEDLekeIKRLELEIEEVEARIK-KYEEQLGNV---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1381 hQKSYHVAGYEHELSSLlrEKRQEVEGEHERRLDKMKEEHQQVMAKAREQYE------AEERKQRAELLGHLTGELERLQ 1454
Cdd:COG1579 86 -RNNKEYEALQKEIESL--KRRISDLEDEILELMERIEELEEELAELEAELAeleaelEEKKAELDEELAELEAELEELE 162
|
170 180
....*....|....*....|....*
gi 530397889 1455 RAHERELETVRQEQHKRLEDLRRRH 1479
Cdd:COG1579 163 AEREELAAKIPPELLALYERIRKRK 187
|
|
| PLC-beta_C |
pfam08703 |
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ... |
1249-1408 |
2.36e-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: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1249 QIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVATL 1328
Cdd:pfam08703 2 QVRELKERLEQELLELREEQYEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1329 EK--EHSAELERLCSSLEAKH-REVVSS---LQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHV-AGYEHELSSLLREK 1401
Cdd:pfam08703 82 KKrtSDKAAQERLKKEINNSHiQEVVQSikqLEEKQKRRQEKLEEKQAECLQQIKEEEPQLQAELnAEYEEKLKGLPAEV 161
|
....*..
gi 530397889 1402 RQEVEGE 1408
Cdd:pfam08703 162 RESVKSC 168
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1151-1499 |
2.49e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1151 EAALKAMEEAVAQVleQDQRHLLESKQEKMQQLREKLCQEEEEEilrlhQQKEQSLSSLRERLQKAieeeearmreeeSQ 1230
Cdd:COG4372 34 RKALFELDKLQEEL--EQLREELEQAREELEQLEEELEQARSEL-----EQLEEELEELNEQLQAA------------QA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1231 RLSWLRAQVQSsTQADEDQIRAEQEAsLQKLREELESQQKAERASLEQKNRQM-------------LEQLKEEIEASEKS 1297
Cdd:COG4372 95 ELAQAQEELES-LQEEAEELQEELEE-LQKERQDLEQQRKQLEAQIAELQSEIaereeelkeleeqLESLQEELAALEQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1298 EQAALNAAKEKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVE 1377
Cdd:COG4372 173 LQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1378 HRVHQKSYHVAGYEhelssLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAH 1457
Cdd:COG4372 253 EEVILKEIEELELA-----ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 530397889 1458 ERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKD 1499
Cdd:COG4372 328 LELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| PRK14971 |
PRK14971 |
DNA polymerase III subunit gamma/tau; |
1011-1265 |
2.50e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237874 [Multi-domain] Cd Length: 614 Bit Score: 42.84 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1011 KDDSQSSQDELQSKQSKGLEERLSPPLPHEERAQSP-PRSLATEEEPPQGPEGQPEWKEAEELGEDSAASLSLQLSLQRE 1089
Cdd:PRK14971 365 KGDDASGGRGPKQHIKPVFTQPAAAPQPSAAAAASPsPSQSSAAAQPSAPQSATQPAGTPPTVSVDPPAAVPVNPPSTAP 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1090 QAPSPPAACEKGKEQHSQAEELGPG-----QEEAEDPEEKVAVSPTPPvspevrstepvaPPEQLSEAALKAMEEAVAQV 1164
Cdd:PRK14971 445 QAVRPAQFKEEKKIPVSKVSSLGPStlrpiQEKAEQATGNIKEAPTGT------------QKEIFTEEDLQYYWQEFAGT 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1165 LEQDQRHLleskQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQ 1244
Cdd:PRK14971 513 RPQEEKAL----KETMINCRPKLLNGTTFEVAVDNELQEKELTNLIPDLLGFLRGRLKNSKITMTVRVSEPTEVNRAYSS 588
|
250 260
....*....|....*....|.
gi 530397889 1245 ADEDQIRAEQEASLQKLREEL 1265
Cdd:PRK14971 589 VEKFQYLAQKNPALLELREEL 609
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1254-1648 |
2.52e-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: 43.11 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1254 QEASLQKLREELESQQKAERASLEQKNR------QMLEQLKEEIEASEKSEQAALNAAKEKALQ--------QLREQLEG 1319
Cdd:TIGR00606 502 EVKSLQNEKADLDRKLRKLDQEMEQLNHhtttrtQMEMLTKDKMDKDEQIRKIKSRHSDELTSLlgyfpnkkQLEDWLHS 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1320 ERKEAVATleKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKC--------LGQVEHRVHQKSYH---VA 1388
Cdd:TIGR00606 582 KSKEINQT--RDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCgsqdeesdLERLKEEIEKSSKQramLA 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1389 GYEHELSSLLREKRQEVEGEHE--RRLDKMKEEHQQVMAKAREQYEAEERKQRAellghLTGELERLQRAHERELETVRQ 1466
Cdd:TIGR00606 660 GATAVYSQFITQLTDENQSCCPvcQRVFQTEAELQEFISDLQSKLRLAPDKLKS-----TESELKKKEKRRDEMLGLAPG 734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1467 EQH------KRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEE------TARREKQQLLDVQRQVA----- 1529
Cdd:TIGR00606 735 RQSiidlkeKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVcltdvtIMERFQMELKDVERKIAqqaak 814
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1530 LKSEEATATHQQL----EEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLL 1605
Cdd:TIGR00606 815 LQGSDLDRTVQQVnqekQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELS 894
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 530397889 1606 REVTVEENNASPHFEPDLHIEDLRKSLGTNQTKEVSSSLSQSK 1648
Cdd:TIGR00606 895 TEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNK 937
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
1240-1467 |
3.02e-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: 42.51 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1240 QSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKE------EIEASEKSEQAALN---AAKEKAl 1310
Cdd:pfam15450 213 ESTRLKAESSLREELEGRWQKLQELTEERLRALQGQREQEEGHLLEQCRGldaavvQLTKFVRQNQVSLNrvlLAEQKA- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1311 QQLREQLEGERKEAVATLEKEhsaELERLCSSLEAKHREVVSSLQKKIQEAQQKEE--AQLQKCLGQVEHRVHQKSYHVA 1388
Cdd:pfam15450 292 RDAKGQLEESQAGELASYVQE---NLEAVQLAGELAQQETQGALELLQEKSQVLEGsvAELVRQVKDLSDHFLALSWRLD 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1389 GYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRA------ELLGHLTGELERLQ---RAHER 1459
Cdd:pfam15450 369 LQEQTLGLKLSEAKKEWEGAERKSLEDLAQWQKEVAAHLREVQEKVDSLPRQieavsdKCVLHKSDSDLKISaegKAREF 448
|
....*...
gi 530397889 1460 ELETVRQE 1467
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 ... |
1248-1316 |
3.09e-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: 3.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1248 DQIRAEQEASLQKLREELESQ-QKAERASLEQKNrQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQ 1316
Cdd:cd06503 50 EELLAEYEEKLAEARAEAQEIiEEARKEAEKIKE-EILAEAKEEAERILEQAKAEIEQEKEKALAELRKE 118
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1395-1515 |
3.12e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1395 SSLLREKRQEVEgeherRLDKMKEEHQQvmAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQE-QHKRLE 1473
Cdd:PRK11448 141 ENLLHALQQEVL-----TLKQQLELQAR--EKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKaAETSQE 213
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 530397889 1474 DLRRRHREQERKLQDLELD-LETRAK-DVKARLALLEVQEETAR 1515
Cdd:PRK11448 214 RKQKRKEITDQAAKRLELSeEETRILiDQQLRKAGWEADSKTLR 257
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1450-1569 |
3.71e-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: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1450 LERLQRAHERELETVRQEqhkrLEDLRRRHREQERKLQDLELDLETRAKdvKARLALLEVQEETARREKQQLLDVQRQVA 1529
Cdd:pfam04012 27 LEQAIRDMQSELVKARQA----LAQTIARQKQLERRLEQQTEQAKKLEE--KAQAALTKGNEELAREALAEKKSLEKQAE 100
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 530397889 1530 LKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQAR 1569
Cdd:pfam04012 101 ALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKAR 140
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1433-1650 |
3.81e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1433 AEERKQRAELLGHLTGELERLQRaherELETVRQEQHKRLEDLRRRHREQER---KLQDLELDLETRAKDVKARLALLEV 1509
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLRE----ELEQAREELEQLEEELEQARSELEQleeELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1510 QEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQK 1589
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530397889 1590 HFSSLEAEAQKKQHLLREVTVEENNASPHFEPDLHIEDLRKSLGTNQTKEVSSSLSQSKED 1650
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
|
|
| PRK02292 |
PRK02292 |
V-type ATP synthase subunit E; Provisional |
1239-1376 |
4.18e-03 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 235026 [Multi-domain] Cd Length: 188 Bit Score: 40.37 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1239 VQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSE--QAALNAAKEkALQQLREQ 1316
Cdd:PRK02292 10 IRDEARARASEIRAEADEEAEEIIAEAEADAEEILEDREAEAEREIEQLREQELSSAKLEakRERLNARKE-VLEDVRNQ 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530397889 1317 LEgerkEAVATLEKEHSAELER-LCSSLEAKHREVVSS------LQKKIQEAQQKEEAQLQKCLGQV 1376
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 ... |
1246-1330 |
4.35e-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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).
Pssm-ID: 432749 [Multi-domain] Cd Length: 181 Bit Score: 40.31 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1246 DEDQiRAEQEASLQKLREELESQQKA-ERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAK----EKALQQLREQLEGE 1320
Cdd:pfam12729 73 DPAE-RDELLKDIEELRAEIDKLLEKyEKTILTDEEKKLFAEFKENLNAYRAVRNKVLELAKagnkDEAYQLYKTEGRPA 151
|
90
....*....|
gi 530397889 1321 RKEAVATLEK 1330
Cdd:pfam12729 152 REAMIEALEE 161
|
|
| PRK13895 |
PRK13895 |
conjugal transfer protein TraM; Provisional |
1278-1348 |
4.90e-03 |
|
conjugal transfer protein TraM; Provisional
Pssm-ID: 184378 Cd Length: 144 Bit Score: 39.66 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1278 QKNRQ-MLEQLKEEIE---------ASEKSEQ---AALNAAKEKALQQLREQLegerKEAVATLEKEHSAELERLCSSLE 1344
Cdd:PRK13895 41 AKAQQeMLDQFKEELEsiasrwgddAKEKAERilnAALAASKEAMAKGMQEGA----KAAAEAVRREISASLAELAAPVR 116
|
....
gi 530397889 1345 AKHR 1348
Cdd:PRK13895 117 EARR 120
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1244-1370 |
4.95e-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: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1244 QADEDQIRAEQeASLQKLREELesQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEkALQQLREQLEGERKE 1323
Cdd:pfam00529 57 QAALDSAEAQL-AKAQAQVARL--QAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQA-QLAQAQIDLARRRVL 132
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 530397889 1324 AVATL-EKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQ 1370
Cdd:pfam00529 133 APIGGiSRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQA 180
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1233-1332 |
5.45e-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: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1233 SWLRAQVQSSTQADEDQIRAE---QEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKA 1309
Cdd:smart00935 13 SPAGKAAQKQLEKEFKKRQAElekLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEE 92
|
90 100
....*....|....*....|...
gi 530397889 1310 LQQLREQLegerKEAVATLEKEH 1332
Cdd:smart00935 93 LQKILDKI----NKAIKEVAKKK 111
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1411-1554 |
5.64e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.62 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1411 RRLDKMKEEHQQVMAKAREqyeaEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQER---KLQ 1487
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQK----EAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDAraeKLD 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530397889 1488 DLELDLETRAKDVKARLALLEVQEETARREKQQLL----DVQRQVALKSEEATATHQ--QLEEAQKEHTHLLQ 1554
Cdd:PRK12705 102 NLENQLEEREKALSARELELEELEKQLDNELYRVAgltpEQARKLLLKLLDAELEEEkaQRVKKIEEEADLEA 174
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
1235-1381 |
5.79e-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: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1235 LRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQM-LEQLKEEIEASEKseqaaLNAAKEKALQQL 1313
Cdd:pfam17060 106 LKEDVKSSPRSEADSLGTPIKVDLLRNLKPQESPETPRRINRKYKSLELrVESMKDELEFKDE-----TIMEKDRELTEL 180
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530397889 1314 REQLeGERKEAVATLEKEHS-----AELERLCSSLEA-KHREVVSSLQKKIQEaQQKEEAQLQKCLGQVEHRVH 1381
Cdd:pfam17060 181 TSTI-SKLKDKYDFLSREFEfykqhHEHGGNNSIKTAtKHEFIISELKRKLQE-QNRLIRILQEQIQFDPGALH 252
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1310-1504 |
5.98e-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: 39.94 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1310 LQQLREQLEGERKEAVATLEKEhsaeLERLCSSLEAKHREVVSSLQKKIQEAQQKeeaqlqkcLGQvehrvhqksyHVAG 1389
Cdd:pfam01442 13 AEELQEQLGPVAQELVDRLEKE----TEALRERLQKDLEEVRAKLEPYLEELQAK--------LGQ----------NVEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1390 YEHELSSLLREKRQEVEgeheRRLDKMKEEHQQVMAKAREQYEAEERKQRAellgHLTGELERLQRAHERELETVRQEQH 1469
Cdd:pfam01442 71 LRQRLEPYTEELRKRLN----ADAEELQEKLAPYGEELRERLEQNVDALRA----RLAPYAEELRQKLAERLEELKESLA 142
|
170 180 190
....*....|....*....|....*....|....*
gi 530397889 1470 KRLEDLRRRHREQerkLQDLELDLETRAKDVKARL 1504
Cdd:pfam01442 143 PYAEEVQAQLSQR---LQELREKLEPQAEDLREKL 174
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
1391-1522 |
6.00e-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: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1391 EHELSSLLREKRQEVEGEHERRLDKMKEE-HQQVMAKAREQYEAEERKQRAEllghltgelERLQRAHERELETVRQEQH 1469
Cdd:pfam15346 21 AKRVEEELEKRKDEIEAEVERRVEEARKImEKQVLEELEREREAELEEERRK---------EEEERKKREELERILEENN 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 530397889 1470 KRLEDLRRRHREQERKlqdlELDLETRAKDVKARLAllEVQEETARREKQQLL 1522
Cdd:pfam15346 92 RKIEEAQRKEAEERLA----MLEEQRRMKEERQRRE--KEEEEREKREQQKIL 138
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1141-1423 |
6.04e-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: 41.96 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1141 EPVAPPEQLSEAALKAMeeavaQVLEQDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLR------ERLQ 1214
Cdd:TIGR00606 775 GTIMPEEESAKVCLTDV-----TIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDtvvskiELNR 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1215 KAIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREEL--ESQQKAERASLEQKNRQMLEQLKEEI- 1291
Cdd:TIGR00606 850 KLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLirEIKDAKEQDSPLETFLEKDQQEKEELi 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1292 ---EASEKSEQAALNAAKEKALQQL--REQLEGERKEAVATLEKEHSAELERLCSSLEAKHREvvsslQKKIQEAQQKEE 1366
Cdd:TIGR00606 930 sskETSNKKAQDKVNDIKEKVKNIHgyMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKH-----QEKINEDMRLMR 1004
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 530397889 1367 AQLQKclGQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQV 1423
Cdd:TIGR00606 1005 QDIDT--QKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKL 1059
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1421-1607 |
6.32e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.22 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1421 QQVMAkAREQYEAEERKQRAELLGHLTGELE------RLQRAHERELETVRQEQHK---RLEDLRRRHREQERKLQDlEL 1491
Cdd:PRK11637 53 QQDIA-AKEKSVRQQQQQRASLLAQLKKQEEaisqasRKLRETQNTLNQLNKQIDElnaSIAKLEQQQAAQERLLAA-QL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1492 DLETRAKDVKArLALLEVQEETARREKQQ----LLDVQRQVALksEEATATHQQLEEAQKEhthLLQSNQQLREILDELQ 1567
Cdd:PRK11637 131 DAAFRQGEHTG-LQLILSGEESQRGERILayfgYLNQARQETI--AELKQTREELAAQKAE---LEEKQSQQKTLLYEQQ 204
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 530397889 1568 ARKLKLESqvdllqaQSQQLQKHFSSLEAEAQKKQHLLRE 1607
Cdd:PRK11637 205 AQQQKLEQ-------ARNERKKTLTGLESSLQKDQQQLSE 237
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
1420-1553 |
6.40e-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: 39.08 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1420 HQQVMAKAREQYEAEerkqRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHR-EQERKLQDLELDLETRAK 1498
Cdd:pfam12474 1 HQLQKEQQKDRFEQE----RQQLKKRYEKELEQLERQQKQQIEKLEQRQTQELRRLPKRIRaEQKKRLKMFRESLKQEKK 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 530397889 1499 DVKA---RLALLEVQEET-ARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLL 1553
Cdd:pfam12474 77 ELKQeveKLPKFQRKEAKrQRKEELELEQKHEELEFLQAQSEALERELQQLQNEKRKEL 135
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
1235-1318 |
6.49e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 39.55 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1235 LRAQVQSSTQADEDQIRAEQEAslQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQA---------ALNAA 1305
Cdd:PRK07352 66 LRQAAQALAEAQQKLAQAQQEA--ERIRADAKARAEAIRAEIEKQAIEDMARLKQTAAADLSAEQErviaqlrreAAELA 143
|
90
....*....|...
gi 530397889 1306 KEKALQQLREQLE 1318
Cdd:PRK07352 144 IAKAESQLPGRLD 156
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1246-1330 |
6.59e-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: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1246 DEDQIRAEQEasLQKLREELESQQKAERASLEQKnrqmLEQLKEEIEASEKSEQAA------LNAAKeKALQQLREQLEg 1319
Cdd:cd22656 171 DEGGAIARKE--IKDLQKELEKLNEEYAAKLKAK----IDELKALIADDEAKLAAAlrliadLTAAD-TDLDNLLALIG- 242
|
90
....*....|.
gi 530397889 1320 erkEAVATLEK 1330
Cdd:cd22656 243 ---PAIPALEK 250
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1229-1553 |
6.74e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.74 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1229 SQRLSWLRAQVQSSTQAdedQIRAEQEASLQKLREEL-ESQQKAE-------------RASLEQKNRQMLEQLKEEIEAS 1294
Cdd:NF041483 103 TQRILQEHAEHQARLQA---ELHTEAVQRRQQLDQELaERRQTVEshvnenvawaeqlRARTESQARRLLDESRAEAEQA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1295 EKSEQAALNAAKEKALQQLREQLEGERKEAVATLEK-----------------EHSAELERLCSSL-----EAKHR--EV 1350
Cdd:NF041483 180 LAAARAEAERLAEEARQRLGSEAESARAEAEAILRRarkdaerllnaastqaqEATDHAEQLRSSTaaesdQARRQaaEL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1351 VSSLQKKIQEAQQK---EEAQLQKCLGQVEHRVHQKsyhVAGYEHELSSLLREKRQEVE---GEHERRLDKMKEEHQQVM 1424
Cdd:NF041483 260 SRAAEQRMQEAEEAlreARAEAEKVVAEAKEAAAKQ---LASAESANEQRTRTAKEEIArlvGEATKEAEALKAEAEQAL 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1425 AKAREQYE-----AEERKQRA-----------------ELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQ 1482
Cdd:NF041483 337 ADARAEAEklvaeAAEKARTVaaedtaaqlakaartaeEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQ 416
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530397889 1483 ERKLQDLELD--LETRAKDVkarlallEVQEEtARR---EKQQLLD--VQRQVALKSEEATATHQQLEEAQKEHTHLL 1553
Cdd:NF041483 417 AEQLKGAAKDdtKEYRAKTV-------ELQEE-ARRlrgEAEQLRAeaVAEGERIRGEARREAVQQIEEAARTAEELL 486
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1260-1762 |
6.85e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1260 KLREELESQQKAERASLEQKNRQMLEQLKE-EIEASEKSEQAALNAAKEKALQQLREQLEGER----------KEAVATL 1328
Cdd:TIGR04523 113 KNDKEQKNKLEVELNKLEKQKKENKKNIDKfLTEIKKKEKELEKLNNKYNDLKKQKEELENELnllekeklniQKNIDKI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1329 EKEHSAeLERLCSSLEAKHREVvSSLQKKIQEAQQKEEaQLQKCLGQVEHRVHQKsyhvagyEHELSSLlREKRQEVEGE 1408
Cdd:TIGR04523 193 KNKLLK-LELLLSNLKKKIQKN-KSLESQISELKKQNN-QLKDNIEKKQQEINEK-------TTEISNT-QTQLNQLKDE 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1409 HERRLDKMKEEHQQVmakareqyeaeerKQRAELLGHLTGELERLqrahERELETVRQE-QHKRLEDLRRRHREQERKLQ 1487
Cdd:TIGR04523 262 QNKIKKQLSEKQKEL-------------EQNNKKIKELEKQLNQL----KSEISDLNNQkEQDWNKELKSELKNQEKKLE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1488 DLELDLETrakdvkarlallevQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQ 1567
Cdd:TIGR04523 325 EIQNQISQ--------------NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1568 ARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQK--KQHLLREVTVEENNASphfepdlhIEDLRKslgTNQTKEVS-SSL 1644
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELleKEIERLKETIIKNNSE--------IKDLTN---QDSVKELIiKNL 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1645 SQSKEDL--YLDSLSshnvwhllsaegvalrsakeflvqqtRSMRRRQTALKAAQqhwrhelasaQEVAKDPPGIKALED 1722
Cdd:TIGR04523 460 DNTRESLetQLKVLS--------------------------RSINKIKQNLEQKQ----------KELKSKEKELKKLNE 503
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 530397889 1723 MRKNLEKETRHL----DEMKSAMRKGHNLLKKKEEKLNQLESSL 1762
Cdd:TIGR04523 504 EKKELEEKVKDLtkkiSSLKEKIEKLESEKKEKESKISDLEDEL 547
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1263-1443 |
7.41e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1263 EELESQQKaeraSLEQKNRQmLEQLKEEIEAsekseqaalnaaKEKALQQLREQLEGERKEAVATLEKEhsaelerlcss 1342
Cdd:PRK00409 523 ASLEELER----ELEQKAEE-AEALLKEAEK------------LKEELEEKKEKLQEEEDKLLEEAEKE----------- 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1343 leakhrevvssLQKKIQEAqQKEEAQLQKCLgqvehRVHQKSYHVAGYEHELSsllrEKRQEVEGEHErrldkMKEEHQQ 1422
Cdd:PRK00409 575 -----------AQQAIKEA-KKEADEIIKEL-----RQLQKGGYASVKAHELI----EARKRLNKANE-----KKEKKKK 628
|
170 180
....*....|....*....|....*..
gi 530397889 1423 VMAKAREQYEAEER------KQRAELL 1443
Cdd:PRK00409 629 KQKEKQEELKVGDEvkylslGQKGEVL 655
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
1254-1537 |
7.52e-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: 41.36 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1254 QEASLQKLREELE-----SQQKAERASLEQKNRQMLEQL-KEEIEASEKSEQAALNAAkEKALQQLREQL-EGERKEAVA 1326
Cdd:pfam15450 40 EHATLSLLRELLQvrahvQLQDSELKQLRQEVQQAARAPeKEALEFPGPQNQNQMQAL-DKRLVEVREALtQIRRKQALQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1327 TLEKEHSAE-----LERLCSSL--EAKHREVV-SSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSLL 1398
Cdd:pfam15450 119 DSERKGAEQeanlrLTKLTGKLkqEEQGREAAcSALQKSQEEASQKVDHEVARMQAQVTKLGEEMSLRFLKREAKLCSFL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1399 R------EKRQEVEG----EHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQ 1468
Cdd:pfam15450 199 QksflalEKRMKASEstrlKAESSLREELEGRWQKLQELTEERLRALQGQREQEEGHLLEQCRGLDAAVVQLTKFVRQNQ 278
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530397889 1469 HKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATA 1537
Cdd:pfam15450 279 VSLNRVLLAEQKARDAKGQLEESQAGELASYVQENLEAVQLAGELAQQETQGALELLQEKSQVLEGSVA 347
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1276-1471 |
8.05e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 41.16 E-value: 8.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1276 LEQKNRQMLEQ-LKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKEHSAELErlcssLEAKHREVVSSL 1354
Cdd:PTZ00491 641 VDERTRDSLQKsVQLAIEITTKSQEAAARHQAELLEQEARGRLERQKMHDKAKAEEQRTKLLE-----LQAESAAVESSG 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1355 QKKiQEAQQKEEAQLQKClgqvehrvhQKSYHVAGyehelsslLREKRQEVEGEHErrLDKMKEEHQQvmakareqyEAE 1434
Cdd:PTZ00491 716 QSR-AEALAEAEARLIEA---------EAEVEQAE--------LRAKALRIEAEAE--LEKLRKRQEL---------ELE 766
|
170 180 190
....*....|....*....|....*....|....*..
gi 530397889 1435 ERKQRAELlghltgELERlqrahERELETVRQEQHKR 1471
Cdd:PTZ00491 767 YEQAQNEL------EIAK-----AKELADIEATKFER 792
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1167-1577 |
8.18e-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: 8.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1167 QDQRHLLESKQEKMQQLREKLC--QEEEEEILRLHQQKEQSLSSLRERLQ----------------KAIEEEEARMREEE 1228
Cdd:TIGR00606 206 QMELKYLKQYKEKACEIRDQITskEAQLESSREIVKSYENELDPLKNRLKeiehnlskimkldneiKALKSRKKQMEKDN 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1229 SQrLSWLRAQVQSSTQADEDQI-RAEQEASLQKLREELESQQKAERASleqKNRQMLEQLKEEIEASEKSEQAALNAAKE 1307
Cdd:TIGR00606 286 SE-LELKMEKVFQGTDEQLNDLyHNHQRTVREKERELVDCQRELEKLN---KERRLLNQEKTELLVEQGRLQLQADRHQE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1308 KALQ--------QLREQLEGERKEAVATLEKEHSAELERLCSSLEAKH-REVVSSLQKKIQEAqQKEEAQLQKCLGQVEH 1378
Cdd:TIGR00606 362 HIRArdsliqslATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTaAQLCADLQSKERLK-QEQADEIRDEKKGLGR 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1379 RVHQKSYHVAGYEHELSSLLREKrQEVEGEHERRLDKMKE--EHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRA 1456
Cdd:TIGR00606 441 TIELKKEILEKKQEELKFVIKEL-QQLEGSSDRILELDQElrKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRK 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1457 HERELETVRQEQHKrledlrrrhREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQvalKSEEAT 1536
Cdd:TIGR00606 520 LDQEMEQLNHHTTT---------RTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHS---KSKEIN 587
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 530397889 1537 ATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQV 1577
Cdd:TIGR00606 588 QTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKL 628
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1458-1576 |
8.20e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.81 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1458 ERELETVRQE------QHKRLEDLRRRHREQERKLQDleldletrakdvKARLALLEVQEETARR--EKQQLLDvqrqva 1529
Cdd:COG1842 36 EEDLVEARQAlaqviaNQKRLERQLEELEAEAEKWEE------------KARLALEKGREDLAREalERKAELE------ 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 530397889 1530 lksEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQ 1576
Cdd:COG1842 98 ---AQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKAR 141
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1240-1441 |
8.38e-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: 41.17 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1240 QSSTQADEDQIRAEQ-EASLQKLREELEsQQKAERASLEQKnrqmLEQLKEEIEASEKSEQAALNAAkeKALQQLREQLE 1318
Cdd:pfam05701 388 QAAQEAEEAKSLAQAaREELRKAKEEAE-QAKAAASTVESR----LEAVLKEIEAAKASEKLALAAI--KALQESESSAE 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1319 GERKEAVA---TLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQqkeeaqlqkclgqvehrvhqksyhvagyEHELS 1395
Cdd:pfam05701 461 STNQEDSPrgvTLSLEEYYELSKRAHEAEELANKRVAEAVSQIEEAK----------------------------ESELR 512
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 530397889 1396 SLlrEKRQEVEGEHERRLDKMKEEHQQVmAKARE---QYEAEERKQRAE 1441
Cdd:pfam05701 513 SL--EKLEEVNREMEERKEALKIALEKA-EKAKEgklAAEQELRKWRAE 558
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1242-1375 |
8.54e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 41.16 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1242 STQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKE--EIEASEKSEQAALNAAK------EKALQQL 1313
Cdd:PTZ00491 660 TTKSQEAAARHQAELLEQEARGRLERQKMHDKAKAEEQRTKLLELQAEsaAVESSGQSRAEALAEAEarlieaEAEVEQA 739
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530397889 1314 REQLEGERKEAVATLEKEHsAELErlcssLEAKHREVVSSL----QKKIQEAQQKEEAQLQKCLGQ 1375
Cdd:PTZ00491 740 ELRAKALRIEAEAELEKLR-KRQE-----LELEYEQAQNELeiakAKELADIEATKFERIVEALGR 799
|
|
| Sfi1 |
pfam08457 |
Sfi1 spindle body protein; This is a family of fungal spindle pole body proteins that play a ... |
1232-1568 |
8.66e-03 |
|
Sfi1 spindle body protein; This is a family of fungal spindle pole body proteins that play a role in spindle body duplication. They contain binding sites for calmodulin-like proteins called centrins which are present in microtubule-organizing centres.
Pssm-ID: 430007 [Multi-domain] Cd Length: 570 Bit Score: 41.13 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1232 LSWLRA---QVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEaseksEQAALNAA--- 1305
Cdd:pfam08457 141 LTWLRKfrtLREREQEAEAKRKRLLLSSALQIWSERTEAVQAAEQEADSFRRRKLLRRALDEWR-----IQARLEPAlrq 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1306 ---------KEKALQQLREQLEGERKEA-VATLEKEHSA----ELERLCSSLEAK--HREVVSSLQK-----------KI 1358
Cdd:pfam08457 216 vsakvdrriLRSALSVWKLRARMSRQAReVDRARILRNAwttwNDELRCKALRERidERLKLEALYKwvleerlrlfqRI 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1359 QEAQQKEEA------QLQKCLGQV-----EHRVHQKSYHVAGYEHELSSLLREKRQE---VEGEHERR-----LDKMKEE 1419
Cdd:pfam08457 296 REQRLKREVlstwvtNTRDTRTRLlrheeEFEEHRNRKLLRSKLLKWRDQLAEQREReiaANEFYAPRllqeaLDAWRER 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1420 HQQVmakarEQYEAEERKQRAELLghLTGELER-----LQRAHERELETVRQEQHKRLEDLRRRH----REQERKLQDLE 1490
Cdd:pfam08457 376 HQHV-----QKLEKWARDARFYFL--ATRTLKKwraatEESRRERRQDAYAQVRRKVKINLARRAlskwRSKAAEVADLE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1491 ldletrakdvkarlallevQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQ--QLREILDELQA 1568
Cdd:pfam08457 449 -------------------QQADQLRQNRLLEDAIELFDRWRERTAKRKQRAEDADQFYAEQLLRSYlaRWRERLRELRE 509
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1423-1577 |
9.03e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.85 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1423 VMAKAREQY--EAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEdlRRRHREQERKLQDLELDLETRAKDV 1500
Cdd:PRK12705 23 VLLKKRQRLakEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRE--REELQREEERLVQKEEQLDARAEKL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530397889 1501 KARLALLEVQEETARREKQQLLDVQRQVALKSEEATAthqqleeaqkehthlLQSNQQLREILDELQArKLKLESQV 1577
Cdd:PRK12705 101 DNLENQLEEREKALSARELELEELEKQLDNELYRVAG---------------LTPEQARKLLLKLLDA-ELEEEKAQ 161
|
|
| EVC2_like |
pfam12297 |
Ellis van Creveld protein 2 like protein; This family of proteins is found in eukaryotes. ... |
1391-1604 |
9.27e-03 |
|
Ellis van Creveld protein 2 like protein; This family of proteins is found in eukaryotes. Proteins in this family are typically between 571 and 1310 amino acids in length. There are two conserved sequence motifs: LPA and ELH. EVC2 is implicated in Ellis van Creveld chondrodysplastic dwarfism in humans. Mutations in this protein can give rise to this congenital condition. LIMBIN is a protein which shares around 80% sequence homology with EVC2 and it is implicated in a similar condition in bovine chondrodysplastic dwarfism.
Pssm-ID: 463525 [Multi-domain] Cd Length: 428 Bit Score: 40.84 E-value: 9.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1391 EHELSSLLREKRQEVEGE-HERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLghltgELERL-QRAHER---ELETVR 1465
Cdd:pfam12297 193 EKRMSSVFNKQFLAMEGRlQEEYERKMAALAAECNLETREKMEAQHQREMAEKE-----EAEELlKHADEQealECSSLL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1466 QEQHK-RLEDLRR----RHREQERKLQdleldletRAKDVKARLALLEVQEEtarrekqQLLDVQRQVALKSEEATATHQ 1540
Cdd:pfam12297 268 DKLHKlEQEHLQRslllRQEEDFAKAQ--------RQLAVFQRVELHKIFFT-------QLKEATRKGELKPEAAKRLLQ 332
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530397889 1541 QLEEAQkehthllqsnQQLREILDELQARKLKLESqvdllqaqsqqlqKHFSSLEAEAQKKQHL 1604
Cdd:pfam12297 333 DYSKIQ----------EQIEELMDFFQANQRYHLS-------------ERFAQREYLVQSLQSL 373
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1456-1768 |
9.36e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1456 AHERELETVRQEQHK---RLEDLRRRHREQERKLQDLELDLEtrakDVKARLALleVQEETARREKQQlldvQRQVALks 1532
Cdd:PRK04863 290 ELRRELYTSRRQLAAeqyRLVEMARELAELNEAESDLEQDYQ----AASDHLNL--VQTALRQQEKIE----RYQADL-- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1533 EEATAthqQLEEAQkehthllQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEA---QKKQHLLREVt 1609
Cdd:PRK04863 358 EELEE---RLEEQN-------EVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAiqyQQAVQALERA- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1610 vEENNASPHFEPDlHIEDLRKSLgTNQTKEVSSSLSQSKEDLylDSLSSHNVWHLLSAEGV-----------ALRSAKEF 1678
Cdd:PRK04863 427 -KQLCGLPDLTAD-NAEDWLEEF-QAKEQEATEELLSLEQKL--SVAQAAHSQFEQAYQLVrkiagevsrseAWDVAREL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1679 L---------VQQTRSMRRRQTALK---AAQQHWRHELASAQEVA-KDPPGIKALEDMRKNLEKETRHLDEMKSAMRKGH 1745
Cdd:PRK04863 502 LrrlreqrhlAEQLQQLRMRLSELEqrlRQQQRAERLLAEFCKRLgKNLDDEDELEQLQEELEARLESLSESVSEARERR 581
|
330 340
....*....|....*....|....*....
gi 530397889 1746 NLLKKKEEKLNQLESSL------WEEASD 1768
Cdd:PRK04863 582 MALRQQLEQLQARIQRLaarapaWLAAQD 610
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1244-1360 |
9.43e-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: 9.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1244 QADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEeieasekseqaalnaAKEKALQQLREQLEGERKE 1323
Cdd:cd16269 188 QADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQER---------------SYEEHLRQLKEKMEEEREN 252
|
90 100 110
....*....|....*....|....*....|....*..
gi 530397889 1324 AVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQE 1360
Cdd:cd16269 253 LLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRS 289
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1163-1607 |
9.54e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1163 QVLEQ--DQRHLLESKQEKMQQLREkLCQeeeeeilRLHQQkeQSLSSLRERLQKAIEEEEARMREEESQrLSWLRAQVQ 1240
Cdd:COG3096 499 ELLRRyrSQQALAQRLQQLRAQLAE-LEQ-------RLRQQ--QNAERLLEEFCQRIGQQLDAAEELEEL-LAELEAQLE 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1241 SSTQADEDQIraEQEASLQKLREELESQQK--AERASLEQKNRQMLEQLKEEIEASEKSEQAALNA-----AKEKALQQL 1313
Cdd:COG3096 568 ELEEQAAEAV--EQRSELRQQLEQLRARIKelAARAPAWLAAQDALERLREQSGEALADSQEVTAAmqqllEREREATVE 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1314 REQLEgERKEAvatLEKE----------HSAELERLCSSL-------------------------EAKHREVVSSLqkki 1358
Cdd:COG3096 646 RDELA-ARKQA---LESQierlsqpggaEDPRLLALAERLggvllseiyddvtledapyfsalygPARHAIVVPDL---- 717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1359 qEAQQKEEAQLQKCLGQV--------------------EHRVHQKS---------------YHVAGYEHELSSLLREKRQ 1403
Cdd:COG3096 718 -SAVKEQLAGLEDCPEDLyliegdpdsfddsvfdaeelEDAVVVKLsdrqwrysrfpevplFGRAAREKRLEELRAERDE 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1404 EVEGEHERRLDKMKEE--HQQV-------MAKA-REQYEAEERKQRAELlghltGELERLQRAHERELetvrQEQHKRLE 1473
Cdd:COG3096 797 LAEQYAKASFDVQKLQrlHQAFsqfvgghLAVAfAPDPEAELAALRQRR-----SELERELAQHRAQE----QQLRQQLD 867
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1474 DLRRRhREQERKLQDL-----ELDLETRAKDVKARL-ALLEVQEETAR-----REKQQLLDVQRQVALKSEEATATHQQL 1542
Cdd:COG3096 868 QLKEQ-LQLLNKLLPQanllaDETLADRLEELREELdAAQEAQAFIQQhgkalAQLEPLVAVLQSDPEQFEQLQADYLQA 946
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397889 1543 EEAQKE--------------HTHLLQS------------NQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEA 1596
Cdd:COG3096 947 KEQQRRlkqqifalsevvqrRPHFSYEdavgllgensdlNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKS 1026
|
570
....*....|.
gi 530397889 1597 EAQKKQHLLRE 1607
Cdd:COG3096 1027 SRDAKQQTLQE 1037
|
|
| |
