|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
559-1044 |
3.21e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.15 E-value: 3.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 559 EQLSEAALKAMEEAVAQV--LEQDQRHLLESKQEKMQQLREKlcQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARM 636
Cdd:COG1196 280 ELELEEAQAEEYELLAELarLEQDIARLEERRRELEERLEEL--EEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 637 REEESQRLSwlRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQM-LEQLKEEIEASEKSEQAALN 715
Cdd:COG1196 358 AELAEAEEA--LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLErLERLEEELEELEEALAELEE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 716 AAKEKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQ--------------L 781
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEadyegflegvkaalL 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 782 QKCLGQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEH-QQVMAKAREQYEAEERKQRAELLGHLTG 860
Cdd:COG1196 516 LAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLkAAKAGRATFLPLDKIRARAALAAALARG 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 861 ELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQV 940
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 941 ALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQsqqlqkhfssLEAEAQKKQHLLREV 1020
Cdd:COG1196 676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQL----------EAEREELLEELLEEE 745
|
490 500
....*....|....*....|....
gi 578822059 1021 TVEENNASPHFEPDLHIEDLRKSL 1044
Cdd:COG1196 746 ELLEEEALEELPEPPDLEELEREL 769
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
609-1222 |
4.07e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.68 E-value: 4.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 609 RLHQQKEQSLS--SLRERLQKAIEEEEARMREEESQRLSWLRAQVQSsTQADEDQIRAEQEAsLQKLREELESQQKAERA 686
Cdd:COG1196 204 PLERQAEKAERyrELKEELKELEAELLLLKLRELEAELEELEAELEE-LEAELEELEAELAE-LEAELEELRLELEELEL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 687 SLEQKNRQmLEQLKEEIEASEKseQAALNAAKEKALQQLREQLEGERKEAVATLEkEHSAELERLCSSLEAkhrevvssl 766
Cdd:COG1196 282 ELEEAQAE-EYELLAELARLEQ--DIARLEERRRELEERLEELEEELAELEEELE-ELEEELEELEEELEE--------- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 767 QKKIQEAQQKEEAQLQKclgqvehrvhqksyhvagyehELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAE 846
Cdd:COG1196 349 AEEELEEAEAELAEAEE---------------------ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 847 ERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETA 926
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 927 RREKQQLLDvqrqvalksEEATATHQQLEEAQKEhTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSL 1006
Cdd:COG1196 488 EAAARLLLL---------LEAEADYEGFLEGVKA-ALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1007 EAEAQ----KKQHLLREVTVEENNASPHFEPDLHIEDLRKSLGTNQTKEvssslsqskEDLYLDSLSSHNVWHLLSAEGV 1082
Cdd:COG1196 558 VAAAAieylKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVAS---------DLREADARYYVLGDTLLGRTLV 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1083 ALRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELASAQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSAMRKGHNLLKK 1162
Cdd:COG1196 629 AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE 708
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1163 KEEKLNQLESSLWEEASDEGTLGGSPTKKAVTFDLSDMDSLSSESSESFSPPHREWWRQQ 1222
Cdd:COG1196 709 LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE 768
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
421-1019 |
5.17e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 87.50 E-value: 5.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 421 EDKDDSQSSQDELQSKQSKGLEERLSPPLPHEERAQSPPRslATEEEPPQGPEGQPEWKEAEELGEDSAASLSLQLSLQR 500
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK--AEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 501 EQAPSPPAACEKGKEQHSQAEELGPGQEEAEDPEEkvavsptppvspeVRSTEPVAPPEQLSEAALKAMEEAVAQVLEQD 580
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE-------------AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK 1378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 581 QRHLLESKQEKMQQLREKlcqeeeeeilrlhQQKEQSLSSLRERLQKAieeeearmrEEESQRLSWLRAQVQSSTQADED 660
Cdd:PTZ00121 1379 KADAAKKKAEEKKKADEA-------------KKKAEEDKKKADELKKA---------AAAKKKADEAKKKAEEKKKADEA 1436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 661 QIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVATL 740
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 741 EKEHSAELERLCSSLEAKHREVVsslqKKIQEAQQKEEAQLQKCLGQVEHRvhQKSYHVAGYEHELSSLLREKRQEVEGE 820
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKADEA----KKAEEKKKADELKKAEELKKAEEK--KKAEEAKKAEEDKNMALRKAEEAKKAE 1590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 821 HERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQ-EQHKRLEDLRRRHREQERKlq 899
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKaEELKKAEEENKIKAAEEAK-- 1668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 900 dleldletRAKDVKARLALLEVQEETARREKQQLLDvqrqvalKSEEAtathQQLEEAQKEHTHLLQSNQQLREildELQ 979
Cdd:PTZ00121 1669 --------KAEEDKKKAEEAKKAEEDEKKAAEALKK-------EAEEA----KKAEELKKKEAEEKKKAEELKK---AEE 1726
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 578822059 980 ARKLKLEsQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLRE 1019
Cdd:PTZ00121 1727 ENKIKAE-EAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKE 1765
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
563-1142 |
4.17e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.22 E-value: 4.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 563 EAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQ 642
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 643 RLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLE--QKNRQMLEQLKEEIEASEKSEQAALNAAKEK 720
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEeaEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 721 ALQQLREQLEGERKEA-VATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHV 799
Cdd:COG1196 388 LLEALRAAAELAAQLEeLEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 800 AGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLtGELERLQRAHERELETVRQE 879
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAV-AVLIGVEAAYEAALEAALAA 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 880 QhkrledLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEAtathqqLEEAQK 959
Cdd:COG1196 547 A------LQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDL------READAR 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 960 EHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLREVTVEENnasphfepdlhIED 1039
Cdd:COG1196 615 YYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE-----------LEE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1040 LRKSLGTNQTKEVSSSLSQSKEDLyldslsshnvwHLLSAEGVALRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELASA 1119
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEEER-----------ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA 752
|
570 580
....*....|....*....|...
gi 578822059 1120 QEVAKDPPGIKALEDMRKNLEKE 1142
Cdd:COG1196 753 LEELPEPPDLEELERELERLERE 775
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
560-990 |
4.31e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.22 E-value: 4.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 560 QLSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKlcQEEEEEILRLhQQKEQSLSSLRERLQKAIEEEEARMREE 639
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA--AELAAQLEEL-EEAEEALLERLERLEEELEELEEALAEL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 640 ESQRLSWLRAQVQ-SSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRqmLEQLKEEIEASEKSEQAALNAAK 718
Cdd:COG1196 434 EEEEEEEEEALEEaAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE--AAARLLLLLEAEADYEGFLEGVK 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 719 EKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKC-LGQVEHRVHQKSY 797
Cdd:COG1196 512 AALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLpLDKIRARAALAAA 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 798 HVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEhqqVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVR 877
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLLGR---TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 878 QEQHKRLEDLRRRhREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEAtatHQQLEEA 957
Cdd:COG1196 669 ELLAALLEAEAEL-EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL---LEELLEE 744
|
410 420 430
....*....|....*....|....*....|...
gi 578822059 958 QKEHTHLLQSNQQLREILDELQARKLKLESQVD 990
Cdd:COG1196 745 EELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
722-1020 |
9.90e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.60 E-value: 9.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 722 LQQLREQLEGERKEAVATLE-KEHSAELERLCSSLEAKHREVVSSLQKKIQ---EAQQKEEAQLQKCLGQVEHRVHQksy 797
Cdd:COG1196 195 LGELERQLEPLERQAEKAERyRELKEELKELEAELLLLKLRELEAELEELEaelEELEAELEELEAELAELEAELEE--- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 798 hvAGYEHELSSLLREKRQEVEGEHERRLDKM--KEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHE----- 870
Cdd:COG1196 272 --LRLELEELELELEEAQAEEYELLAELARLeqDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEeleea 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 871 ----RELETVRQEQHKRLEDLRRRHREQERKLQDL---ELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALK 943
Cdd:COG1196 350 eeelEEAEAELAEAEEALLEAEAELAEAEEELEELaeeLLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 944 SEEAT----ATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLRE 1019
Cdd:COG1196 430 LAELEeeeeEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
|
.
gi 578822059 1020 V 1020
Cdd:COG1196 510 V 510
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
420-1177 |
2.77e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.64 E-value: 2.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 420 IEDKDDSQSSQDELQSKQSKGLEERLSPPLPHEERAQSPpRSLATEEeppqgpegqpeWKEAEELGEDSAASLSLQLSLQ 499
Cdd:PTZ00121 1047 IIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKE-DNRADEA-----------TEEAFGKAEEAKKTETGKAEEA 1114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 500 REQAPSPPAACEKGKEQHSQAEELGPGQEEAEDPEEKVAVSPTPPVSpEVRSTEPVAPPEQL--SEAALKAMEEAVAQVL 577
Cdd:PTZ00121 1115 RKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAE-DARKAEEARKAEDAkkAEAARKAEEVRKAEEL 1193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 578 ---------EQDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLR 648
Cdd:PTZ00121 1194 rkaedarkaEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK 1273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 649 AQvqSSTQADEDQiRAEQEASLQKLREElESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKE--KALQQLR 726
Cdd:PTZ00121 1274 AE--EARKADELK-KAEEKKKADEAKKA-EEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEakKAAEAAK 1349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 727 EQLEGERKEAVATLEKEHSAELERLcsslEAKHRevVSSLQKKIQEAQQKEEAQlqkclgqvehrvhQKSYHVAGYEHEL 806
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKE----EAKKK--ADAAKKKAEEKKKADEAK-------------KKAEEDKKKADEL 1410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 807 SSLLREKRQEVEGEHERRLDKMKEEHQQvmaKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLED 886
Cdd:PTZ00121 1411 KKAAAAKKKADEAKKKAEEKKKADEAKK---KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE 1487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 887 LRRRHREQERKLQDLELDLETRAKDVKARLAllevqeETARREKQqlldvqrqvALKSEEATATHQQLEEAQKEHTHLLQ 966
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKADEAKKA------EEAKKADE---------AKKAEEAKKADEAKKAEEKKKADELK 1552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 967 SNQQLREILDELQARKLKLESQvdllqaqsqqlQKHFSSLEAEAQKKqhlLREVTVEENNASPHFEPDLHIEDLRKSlgt 1046
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEE-----------DKNMALRKAEEAKK---AEEARIEEVMKLYEEEKKMKAEEAKKA--- 1615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1047 NQTKEVSSSLSQSKEDlyldslsSHNVWHLLSAEGVALRSAKEFL-VQQTRSMRRRQTALKAAQQHWRHELA-------- 1117
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEE-------KKKVEQLKKKEAEEKKKAEELKkAEEENKIKAAEEAKKAEEDKKKAEEAkkaeedek 1688
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578822059 1118 -SAQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSA----MRKGHNLLKKKEEKLNQLESSLWEE 1177
Cdd:PTZ00121 1689 kAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAeeenKIKAEEAKKEAEEDKKKAEEAKKDE 1753
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
579-1174 |
3.62e-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: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 579 QDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQsLSSLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQAD 658
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEK-LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 659 E-DQIRaEQEASLQKLREELESQQKAERASLEqKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEgeRKEAV 737
Cdd:TIGR02168 387 KvAQLE-LQIASLNNEIERLEARLERLEDRRE-RLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE--RLEEA 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 738 ATLEKEHSAELERLCSSLEAKHREVVSslQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHV----------AGYEHELS 807
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQA--RLDSLERLQENLEGFSEGVKALLKNQSGLSGILgvlselisvdEGYEAAIE 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 808 SLLREKRQEVEGEHE----------------------------------RRLDKMKEEHQQVMAKAREQYEAEERKQRAE 853
Cdd:TIGR02168 541 AALGGRLQAVVVENLnaakkaiaflkqnelgrvtflpldsikgteiqgnDREILKNIEGFLGVAKDLVKFDPKLRKALSY 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 854 LLGH------LTGELERLQRAHEREL----------------------ETVRQEQHKRLEDLRRRHREQERKLQDLEL-- 903
Cdd:TIGR02168 621 LLGGvlvvddLDNALELAKKLRPGYRivtldgdlvrpggvitggsaktNSSILERRREIEELEEKIEELEEKIAELEKal 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 904 -DLETRAKDVKARLALLEVQEETARRE----KQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDEL 978
Cdd:TIGR02168 701 aELRKELEELEEELEQLRKELEELSRQisalRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 979 QARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQK-KQHLLREVTVEENNASPHFEPDLHIEDLRKSLGTNQTKEVSSSLS 1057
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDELRAELTLlNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1058 QSKEDLYLDSLSSHNVWHL-----LSAEGVALRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELASAQEVakdppgIKAL 1132
Cdd:TIGR02168 861 IEELEELIEELESELEALLnerasLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR------LEGL 934
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 578822059 1133 EDMRKNL-----EKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSL 1174
Cdd:TIGR02168 935 EVRIDNLqerlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
559-1149 |
4.88e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.67 E-value: 4.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 559 EQLSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKLCQEEEEeilrlHQQKEQSLSSLRERLQKAieeeeaRMRe 638
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE-----LEELRLELEELELELEEA------QAE- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 639 eesqrlswLRAQVQSSTQADEDQIRA-EQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAA 717
Cdd:COG1196 290 --------EYELLAELARLEQDIARLeERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 718 KEKALQQLREQLEGERKEAVATLEKEHSAELERlcsslEAKHREVVSSLQKKIQEAQQKEEAQLQKclgqvehrvhqksy 797
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEALRA-----AAELAAQLEELEEAEEALLERLERLEEE-------------- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 798 hVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVR 877
Cdd:COG1196 423 -LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 878 QEQHKRLEDLRRRHREQERKLQ---DLELDLETRAKDV---KARLALLEVQEETARREKQQLLDVQRQVALKSEEATATH 951
Cdd:COG1196 502 DYEGFLEGVKAALLLAGLRGLAgavAVLIGVEAAYEAAleaALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDK 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 952 QQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHfSSLEAEAQKKQHLLREVTVEENNASPHF 1031
Cdd:COG1196 582 IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARL-EAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1032 EPDLHIE-DLRKSLGTNQTKEVSSSLSQSKEDLYLDSLSSHNVWHLLSAEGVALRSAKEFLVQQTRSMRRRQTALKAAQQ 1110
Cdd:COG1196 661 SLTGGSRrELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
570 580 590
....*....|....*....|....*....|....*....
gi 578822059 1111 HWRHELASAQEVAKDPPGIKALEDMRKNLEKETRHLDEM 1149
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
665-982 |
1.71e-13 |
|
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: 75.55 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 665 EQEASLQKLREELESQQKAERASLEQKNRQMLE-----QLKEEIEASEKSEQAALNAAKEKALQQLREQ-----LEGERK 734
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEKAREVERRRKLEEaekarQAEMDRQAAIYAEQERMAMERERELERIRQEerkreLERIRQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 735 EAVAtLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQlqkclgqveHRVHQKSYHVAGYEHELSSLLREKR 814
Cdd:pfam17380 368 EEIA-MEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQ---------RKIQQQKVEMEQIRAEQEEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 815 QEVEGEHERRLDKMKEEH---QQVMAKAREQYEAEERKQRaellghltgELERLQRAHERELETVRQEQHKRLEDLRRRH 891
Cdd:pfam17380 438 RRLEEERAREMERVRLEEqerQQQVERLRQQEEERKRKKL---------ELEKEKRDRKRAEEQRRKILEKELEERKQAM 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 892 REQERKLQDLELDLETRAKDVKARLALLEVQEEtarREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHthllqsnQQL 971
Cdd:pfam17380 509 IEEERKRKLLEKEMEERQKAIYEEERRREAEEE---RRKQQEMEERRRIQEQMRKATEERSRLEAMERER-------EMM 578
|
330
....*....|.
gi 578822059 972 REILDELQARK 982
Cdd:pfam17380 579 RQIVESEKARA 589
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
311-935 |
5.07e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.41 E-value: 5.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 311 SEPAKASEKEAPEDTVDAGEEGSRREEAAK-EPKKKASALEEGSSDASQELEISEHMKEPQLSDSIASDPKSFHGLDFGF 389
Cdd:PTZ00121 1196 AEDARKAEAARKAEEERKAEEARKAEDAKKaEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE 1275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 390 RSRISEHLLDVDVLSPvlGGACRQAQQPLGIED---KDDSQSSQDELQSKQSKGLEERLSPPLPHEERAQSPPRSLATEE 466
Cdd:PTZ00121 1276 EARKADELKKAEEKKK--ADEAKKAEEKKKADEakkKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 467 EPPQGPEGQPEWKEAEELGEDSAASLSLQLSLQREQAPSPPAACEKGKEQHSQAEELGPGQEEAEDPEEkvavspTPPVS 546
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE------AKKKA 1427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 547 PEVRSTEPVappEQLSEAALKAmEEAVAQVLEQDQRHLLESKQE---KMQQLREKLCQEEEEEILRLHQQKEQSLSSLRE 623
Cdd:PTZ00121 1428 EEKKKADEA---KKKAEEAKKA-DEAKKKAEEAKKAEEAKKKAEeakKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK 1503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 624 RLQKAIEEEEARMREEESQRLSWLRaQVQSSTQADEDQiRAEQEASLQKLR--EEL---ESQQKAERASLEQKNRQMLEQ 698
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEAK-KAEEAKKADEAK-KAEEKKKADELKkaEELkkaEEKKKAEEAKKAEEDKNMALR 1581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 699 LKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKeavatlEKEHSAELERlcsslEAKHREVVSSLQKKIQEAQQKEE 778
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE------AKIKAEELKK-----AEEEKKKVEQLKKKEAEEKKKAE 1650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 779 aQLQKclgqvehrvhqksyhvagyEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAEllghl 858
Cdd:PTZ00121 1651 -ELKK-------------------AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE----- 1705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 859 tgELERLQRAHERELETVRQEQHKR---LEDLRRRHREQERKLQDLELDlETRAKDVKARLALLEVQEETARREKQQLLD 935
Cdd:PTZ00121 1706 --ELKKKEAEEKKKAEELKKAEEENkikAEEAKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
564-989 |
1.31e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 72.77 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 564 AALKAMEEAVAQVLEQDQRhlLESKQEKMQQLREKLcqeeeEEILRLHQQKEQSLSSLRERLQK--AIEEEEARMREEES 641
Cdd:PRK02224 206 ERLNGLESELAELDEEIER--YEEQREQARETRDEA-----DEVLEEHEERREELETLEAEIEDlrETIAETEREREELA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 642 QRLSWLRAQVQ------SSTQADEDQIRAEQEASLQKlREELESQQKAERASLEQKnRQMLEQLKEEIE----------- 704
Cdd:PRK02224 279 EEVRDLRERLEeleeerDDLLAEAGLDDADAEAVEAR-REELEDRDEELRDRLEEC-RVAAQAHNEEAEslredaddlee 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 705 -ASEKSEQAAlnaAKEKALQQLREQLEgERKEAVATLEKE-----------------HSAELERLCSSLEAKHREV---- 762
Cdd:PRK02224 357 rAEELREEAA---ELESELEEAREAVE-DRREEIEELEEEieelrerfgdapvdlgnAEDFLEELREERDELREREaele 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 763 --VSSLQKKIQEAQQ-KEEAQLQKCLGQVEHRVH-----QKSYHVAGYEHELSSLlREKRQEVEGEHER---------RL 825
Cdd:PRK02224 433 atLRTARERVEEAEAlLEAGKCPECGQPVEGSPHvetieEDRERVEELEAELEDL-EEEVEEVEERLERaedlveaedRI 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 826 DKMKEEHQQVMAKAREQYE-AEERKQRAELLGHLTGELErlqrAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELD 904
Cdd:PRK02224 512 ERLEERREDLEELIAERREtIEEKRERAEELRERAAELE----AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKER 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 905 LEtRAKDVKARLALLEVQEETA-----RREKQQLLDVQRQVALKSE-------EATATHQQLEEAQKEHTHLLQSNQQLR 972
Cdd:PRK02224 588 IE-SLERIRTLLAAIADAEDEIerlreKREALAELNDERRERLAEKrerkrelEAEFDEARIEEAREDKERAEEYLEQVE 666
|
490
....*....|....*..
gi 578822059 973 EILDELQARKLKLESQV 989
Cdd:PRK02224 667 EKLDELREERDDLQAEI 683
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
670-988 |
1.62e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.78 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 670 LQKLREELESQQKaeraSLEQKNRQMlEQLKEeIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVaTLEKEHSAELE 749
Cdd:TIGR02168 191 LEDILNELERQLK----SLERQAEKA-ERYKE-LKAELRELELALLVLRLEELREELEELQEELKEAE-EELEELTAELQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 750 RLCSSLEAkHREVVSSLQKKIQEAQQKEEA---QLQKCLGQVEHRVHQKSYHVAGYEHELSSLLREKRQEVE-GEHERRL 825
Cdd:TIGR02168 264 ELEEKLEE-LRLEVSELEEEIEELQKELYAlanEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDElAEELAEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 826 DKMKEEHQQVMAKAREQYEAEERKQRaellghltgELERLQRAHERELETVRQEQH---KRLEDLRRRHREQERKLQDLE 902
Cdd:TIGR02168 343 EEKLEELKEELESLEAELEELEAELE---------ELESRLEELEEQLETLRSKVAqleLQIASLNNEIERLEARLERLE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 903 ldlETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATH-QQLEEAQKEHTHLLQSNQQLREILDELQAR 981
Cdd:TIGR02168 414 ---DRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLeEALEELREELEEAEQALDAAERELAQLQAR 490
|
....*..
gi 578822059 982 KLKLESQ 988
Cdd:TIGR02168 491 LDSLERL 497
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
570-1178 |
3.19e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 71.54 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 570 EEAVAQVLEQDQRHLLESKQEKMQQLREKLCQEEEEEilrlhQQKEQSLSSLRERLQKAieeeeaRMREEESQRLSWLRA 649
Cdd:TIGR00618 199 LTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREAL-----QQTQQSHAYLTQKREAQ------EEQLKKQQLLKQLRA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 650 QVQSSTQadedqiraeQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALnaakEKALQQLREQL 729
Cdd:TIGR00618 268 RIEELRA---------QEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSR----AKLLMKRAAHV 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 730 egerkeavatlekEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSL 809
Cdd:TIGR00618 335 -------------KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 810 lrekrqevegeherrLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRR 889
Cdd:TIGR00618 402 ---------------LDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 890 RHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLL--DVQRQVALKSEEATATHQQLEEaqkEHTHLLQS 967
Cdd:TIGR00618 467 SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIhpNPARQDIDNPGPLTRRMQRGEQ---TYAQLETS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 968 NQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLREV---TVEENNASPHFEPDLHIEDLRKSL 1044
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLqdlTEKLSEAEDMLACEQHALLRKLQP 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1045 GTNQtKEVSSSLSQSKEDLYLDSLSSHNVWHLLSAEGV--ALRSAKEFlvqQTRSMRRRQTALKAAQQ------HWRHEL 1116
Cdd:TIGR00618 624 EQDL-QDVRLHLQQCSQELALKLTALHALQLTLTQERVreHALSIRVL---PKELLASRQLALQKMQSekeqltYWKEML 699
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578822059 1117 ASAQEvakdppgikALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSLWEEA 1178
Cdd:TIGR00618 700 AQCQT---------LLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQA 752
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
567-1063 |
9.52e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.94 E-value: 9.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 567 KAMEEAVAQVLEQDQRhlLESKQEKMQQLREKLcqeeeeEILRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSW 646
Cdd:COG4913 221 PDTFEAADALVEHFDD--LERAHEALEDAREQI------ELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 647 LRAQVQSSTQADEDQirAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAK--EKALQQ 724
Cdd:COG4913 293 LEAELEELRAELARL--EAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRArlEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 725 LREQLEGERkEAVATLEKEHSAELERLcSSLEAKHREVVSSLQKKIQEAQqKEEAQLQKCLGQVEHRVHQKSYHVAGYEH 804
Cdd:COG4913 371 LGLPLPASA-EEFAALRAEAAALLEAL-EEELEALEEALAEAEAALRDLR-RELRELEAEIASLERRKSNIPARLLALRD 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 805 ELSSLLREKRQE---------------------------------VEGEHERR----LDKMKEEHQQVMAKAREQYEAEE 847
Cdd:COG4913 448 ALAEALGLDEAElpfvgelievrpeeerwrgaiervlggfaltllVPPEHYAAalrwVNRLHLRGRLVYERVRTGLPDPE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 848 RKQRAEllGHLTGELE------------RLQR-------AHERELET----------VRQEQHKRLEDLRRRHREQ---- 894
Cdd:COG4913 528 RPRLDP--DSLAGKLDfkphpfrawleaELGRrfdyvcvDSPEELRRhpraitragqVKGNGTRHEKDDRRRIRSRyvlg 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 895 ---ERKLQDLELD---LETRAKDVKARLALLEVQEETARREKQQLLDVQrQVALKSEEATATHQQLEEAQKEHTHLLQSN 968
Cdd:COG4913 606 fdnRAKLAALEAElaeLEEELAEAEERLEALEAELDALQERREALQRLA-EYSWDEIDVASAEREIAELEAELERLDASS 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 969 ---QQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLREVtveENNASPHFEPDLhIEDLRKSLG 1045
Cdd:COG4913 685 ddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA---EDLARLELRALL-EERFAAALG 760
|
570
....*....|....*...
gi 578822059 1046 TNQTKEVSSSLSQSKEDL 1063
Cdd:COG4913 761 DAVERELRENLEERIDAL 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
570-981 |
3.32e-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: 68.16 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 570 EEAVAQVLEQDQRhlLESKQEKMQQLREKLcqeeeeeilRLHQQKEQSLSSLRERLQKAIEEEEARMREEeSQRLSWLRA 649
Cdd:TIGR02168 666 AKTNSSILERRRE--IEELEEKIEELEEKI---------AELEKALAELRKELEELEEELEQLRKELEEL-SRQISALRK 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 650 QVQSSTQadEDQIRAEQEASLQKLREELEsQQKAERASLEQKNRQMLEQLKEEIEasekSEQAALNAAKEkALQQLREQL 729
Cdd:TIGR02168 734 DLARLEA--EVEQLEERIAQLSKELTELE-AEIEELEERLEEAEEELAEAEAEIE----ELEAQIEQLKE-ELKALREAL 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 730 EGERKEavATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEaqlqkclgqvehrvhqksyHVAGYEHELSSl 809
Cdd:TIGR02168 806 DELRAE--LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE-------------------DIESLAAEIEE- 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 810 LREKRQEVEGEHErRLDKMKEEHQQVMAKAREQYEAEERKQRaellghltgELERLQRAHERELETVRQEQHK---RLED 886
Cdd:TIGR02168 864 LEELIEELESELE-ALLNERASLEEALALLRSELEELSEELR---------ELESKRSELRRELEELREKLAQlelRLEG 933
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 887 LR-RRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRqVALKS-EEATATHQQLEEAQKEHTHL 964
Cdd:TIGR02168 934 LEvRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGP-VNLAAiEEYEELKERYDFLTAQKEDL 1012
|
410
....*....|....*..
gi 578822059 965 LQSNQQLREILDELQAR 981
Cdd:TIGR02168 1013 TEAKETLEEAIEEIDRE 1029
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
495-1020 |
3.62e-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: 68.16 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 495 QLSLQREQAPSppAACEKGKEQHSQAEELGPGQEEAEDPEEKVAvsptppvspEVRSTEPVAppEQLSEAALKAMEE--- 571
Cdd:TIGR02168 320 ELEAQLEELES--KLDELAEELAELEEKLEELKEELESLEAELE---------ELEAELEEL--ESRLEELEEQLETlrs 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 572 AVAQVLEQ-----DQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMREEEsQRLSW 646
Cdd:TIGR02168 387 KVAQLELQiaslnNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE-EALEE 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 647 LRAQVQSSTQA------DEDQIRAEQeASLQKLREELESQQKAERASLEQKNR--QMLEQLKEEIEASEKSEqAALNAAK 718
Cdd:TIGR02168 466 LREELEEAEQAldaaerELAQLQARL-DSLERLQENLEGFSEGVKALLKNQSGlsGILGVLSELISVDEGYE-AAIEAAL 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 719 EKALQQLREQLEGERKEAVATLEKEHS-----AELERLC-SSLEAKHRE------------------------------- 761
Cdd:TIGR02168 544 GGRLQAVVVENLNAAKKAIAFLKQNELgrvtfLPLDSIKgTEIQGNDREilkniegflgvakdlvkfdpklrkalsyllg 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 762 ---VVSSLQ------KKIQE------------------------------AQQKEEAQLQKCLGQVEHRVHQKSYHVAGY 802
Cdd:TIGR02168 624 gvlVVDDLDnalelaKKLRPgyrivtldgdlvrpggvitggsaktnssilERRREIEELEEKIEELEEKIAELEKALAEL 703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 803 EHELSSLLREKRQevegeherrLDKMKEEHQQVMAKAREQYEAEERKQRAellghLTGELERLQRAHErELETVRQEQHK 882
Cdd:TIGR02168 704 RKELEELEEELEQ---------LRKELEELSRQISALRKDLARLEAEVEQ-----LEERIAQLSKELT-ELEAEIEELEE 768
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 883 RLEDLRRRHREQERKLQDLELDLETRAKDVKA-RLALLEVQEEtARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEH 961
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKAlREALDELRAE-LTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 578822059 962 THLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLREV 1020
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
563-936 |
1.66e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.85 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 563 EAALKAMEEAVAQVleQDQRHLLESKQEKMQQLREKLcqeeeeeiLRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQ 642
Cdd:TIGR02168 683 EEKIEELEEKIAEL--EKALAELRKELEELEEELEQL--------RKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 643 RLSWLRAQVQSSTQADEdqiraEQEASLQKLREElesqqkAERASLEQKNRQMLEQLKEEIEASeKSEQAALNAAKEKAl 722
Cdd:TIGR02168 753 SKELTELEAEIEELEER-----LEEAEEELAEAE------AEIEELEAQIEQLKEELKALREAL-DELRAELTLLNEEA- 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 723 QQLREQLEGERKEAVATlekehSAELERLCSSLEAKhREVVSSLQKKIQEAQQKEEAQlqkclgQVEHRVHQKSYHVAGY 802
Cdd:TIGR02168 820 ANLRERLESLERRIAAT-----ERRLEDLEEQIEEL-SEDIESLAAEIEELEELIEEL------ESELEALLNERASLEE 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 803 EHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKareQYEAEERKQRAELLghLTGELERLQRAHERELETVRQEQHK 882
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELRRELEELREK---LAQLELRLEGLEVR--IDNLQERLSEEYSLTLEEAEALENK 962
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 883 RLED---LRRRHREQERKLQDL---ELDLETRAKDVKARLALLEVQEETARREKQQLLDV 936
Cdd:TIGR02168 963 IEDDeeeARRRLKRLENKIKELgpvNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEA 1022
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
559-936 |
1.95e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 559 EQLSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKLcQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMRE 638
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL-AEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 639 EESQRLSW---LRAQVQSSTQADEDQIRAEQEASLQKLREELEsQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALN 715
Cdd:COG1196 525 AVAVLIGVeaaYEAALEAALAAALQNIVVEDDEVAAAAIEYLK-AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 716 AAKEKALQQLREQLEGERkEAVATLEKEHSAELERLCSSLEAKHREVvSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQK 795
Cdd:COG1196 604 VASDLREADARYYVLGDT-LLGRTLVAARLEAALRRAVTLAGRLREV-TLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 796 SyhvagyehELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELET 875
Cdd:COG1196 682 E--------ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAL 753
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578822059 876 VRQEQHKRLEDLRRRHREQERKLQDLE---LDLETRAKDVKARLALLEVQEETARREKQQLLDV 936
Cdd:COG1196 754 EELPEPPDLEELERELERLEREIEALGpvnLLAIEEYEELEERYDFLSEQREDLEEARETLEEA 817
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
585-1173 |
2.49e-10 |
|
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: 65.52 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 585 LESKQEKMQQLREKLCQeeeeeilrLHQQKEQSLSSLRERLQKAIEEEEARMReeesqrlswLRAQVQSSTQADEDQIRA 664
Cdd:pfam15921 115 LQTKLQEMQMERDAMAD--------IRRRESQSQEDLRNQLQNTVHELEAAKC---------LKEDMLEDSNTQIEQLRK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 665 ---EQEASLQKLR------EELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLrEQLEGERKE 735
Cdd:pfam15921 178 mmlSHEGVLQEIRsilvdfEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQL-EALKSESQN 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 736 AVATLEKEHSAELERLCSsleaKHREVVSSLQKKIQEAQQKEEAqLQKCLGQVEHRVHQKSYHVAGYEHELSSLLREKRQ 815
Cdd:pfam15921 257 KIELLLQQHQDRIEQLIS----EHEVEITGLTEKASSARSQANS-IQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 816 EVEGEHERRLDKMKEEHQQVMAKAREQYEAE-ERKQRAELLGHLTGELERL-QRAHERELE-TVRQEQHKRLEDlrrRHR 892
Cdd:pfam15921 332 ELREAKRMYEDKIEELEKQLVLANSELTEARtERDQFSQESGNLDDQLQKLlADLHKREKElSLEKEQNKRLWD---RDT 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 893 EQERKLQDLELDLETRAKDVKARLALLE-VQEETARREKQQLLDVQrqvalkseeatATHQQLEEAQKEHTHLLQSNQQL 971
Cdd:pfam15921 409 GNSITIDHLRRELDDRNMEVQRLEALLKaMKSECQGQMERQMAAIQ-----------GKNESLEKVSSLTAQLESTKEML 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 972 REILDELQARKLKLESQvdllqaqsqqlQKHFSSLEAEAQKKQHLLR----EVTVEENNASPHFEPDLHIEDLRKSLGTN 1047
Cdd:pfam15921 478 RKVVEELTAKKMTLESS-----------ERTVSDLTASLQEKERAIEatnaEITKLRSRVDLKLQELQHLKNEGDHLRNV 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1048 QTKEVSSSLSQSKEDLYLDSLSSH--NVWHLLSAEGvalRSAKEFLVQQTRsmrrrqtaLKAAQQHWRHELASAQEVA-K 1124
Cdd:pfam15921 547 QTECEALKLQMAEKDKVIEILRQQieNMTQLVGQHG---RTAGAMQVEKAQ--------LEKEINDRRLELQEFKILKdK 615
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 578822059 1125 DPPGIKALEDMRKNLEKETRHLDEMKSA-MRKGHNLLKKKEEKLNQLESS 1173
Cdd:pfam15921 616 KDAKIRELEARVSDLELEKVKLVNAGSErLRAVKDIKQERDQLLNEVKTS 665
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
558-978 |
2.68e-10 |
|
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: 65.38 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 558 PEQLSEAALKAMEEAVAQVLEQDQRHLLESKQ---EKMQQL--------REKLCQEEEEEILRLHQQKEQSL-SSLRERL 625
Cdd:TIGR00618 435 LQQRYAELCAAAITCTAQCEKLEKIHLQESAQslkEREQQLqtkeqihlQETRKKAVVLARLLELQEEPCPLcGSCIHPN 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 626 QKAIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEaSLQKLREELESQQKAERASLEQKNR--QMLEQLKEEI 703
Cdd:TIGR00618 515 PARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK-QRASLKEQMQEIQQSFSILTQCDNRskEDIPNLQNIT 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 704 EASEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEA-----QQKEE 778
Cdd:TIGR00618 594 VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHalsirVLPKE 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 779 --AQLQKCLGQVEHRVHQKSYHVAGYEHELSsLLREkrqevEGEHERRLDKMKEEHQQVMAKAREQYEAEE--------- 847
Cdd:TIGR00618 674 llASRQLALQKMQSEKEQLTYWKEMLAQCQT-LLRE-----LETHIEEYDREFNEIENASSSLGSDLAAREdalnqslke 747
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 848 -RKQRAELLGHLTGELERLQRAHERELETVRQEQHKRlEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETA 926
Cdd:TIGR00618 748 lMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLA-AEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETL 826
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 578822059 927 RREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDEL 978
Cdd:TIGR00618 827 VQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
706-1044 |
4.23e-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: 64.70 E-value: 4.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 706 SEKSEQAALNAAKEKA-LQQLREQLEGERKEAVATLEKEHSAELER--LCSSLEAKHREVvSSLQKKIQEAQQKEEAQLQ 782
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAeLQRLRERLEGLKRELSSLQSELRRIENRLdeLSQELSDASRKI-GEIEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 783 KcLGQVEHRVHQKSYHVAGYEHELSsllrekrqevegeherRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGEL 862
Cdd:TIGR02169 738 R-LEELEEDLSSLEQEIENVKSELK----------------ELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAEL 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 863 erlqraheRELETVRQEQHKRLEDLrrrhreqERKLQDLELDLEtrakdvkarLALLEVQEETARRE--KQQLLDVQRQV 940
Cdd:TIGR02169 801 --------SKLEEEVSRIEARLREI-------EQKLNRLTLEKE---------YLEKEIQELQEQRIdlKEQIKSIEKEI 856
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 941 ALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLREV 1020
Cdd:TIGR02169 857 ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
330 340
....*....|....*....|....
gi 578822059 1021 TVEENNASPHFEPDLHIEDLRKSL 1044
Cdd:TIGR02169 937 EDPKGEDEEIPEEELSLEDVQAEL 960
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
654-902 |
4.77e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.29 E-value: 4.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 654 STQADEDQIRAEQEASLQKLREELES-QQKAERASLEQKNRQMLEQLKEEIEASEK--SEQAALNAAKEKALQQLREQLE 730
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDLEEEVEEvEERLERAEDLVEAEDRIERLEERREDLEEliAERRETIEEKRERAEELRERAA 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 731 GERKEAVATLEKEHSAELErlcsslEAKHREVVSSLQKKIQEAQQKEEAqlqkcLGQVEHRVHQksyhVAGYEHELSSLl 810
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEE------AEEAREEVAELNSKLAELKERIES-----LERIRTLLAA----IADAEDEIERL- 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 811 REKR---QEVEGEHERRLDKMKEEHQQVMAKAREQY--EAEERKQRAE-LLGHLTGELERLqRAHERELET----VRQEQ 880
Cdd:PRK02224 612 REKRealAELNDERRERLAEKRERKRELEAEFDEARieEAREDKERAEeYLEQVEEKLDEL-REERDDLQAeigaVENEL 690
|
250 260
....*....|....*....|..
gi 578822059 881 hKRLEDLRRRHREQERKLQDLE 902
Cdd:PRK02224 691 -EELEELRERREALENRVEALE 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
819-1144 |
7.99e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.92 E-value: 7.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 819 GEHERRLDKMKEEHQQVMaKAREQYEAEERKQRAELLGHLT---GELERLQRAHER------ELETVRQEQHKRLEDLRR 889
Cdd:TIGR02168 196 NELERQLKSLERQAEKAE-RYKELKAELRELELALLVLRLEelrEELEELQEELKEaeeeleELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 890 RHREQERKLQDLEldleTRAKDVKARLALLEVQEETARREKQQLldvQRQVALKSEEATATHQQLEEAQKEHThllqsnq 969
Cdd:TIGR02168 275 EVSELEEEIEELQ----KELYALANEISRLEQQKQILRERLANL---ERQLEELEAQLEELESKLDELAEELA------- 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 970 QLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLREVTVEENNASPHFEP-DLHIEDLRKSLgtNQ 1048
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERlEARLERLEDRR--ER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1049 TKEVSSSLSQSKEDLYLDSLSSHNVwhLLSAEGVALRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELASAQEvakdppG 1128
Cdd:TIGR02168 419 LQQEIEELLKKLEEAELKELQAELE--ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA------R 490
|
330
....*....|....*.
gi 578822059 1129 IKALEDMRKNLEKETR 1144
Cdd:TIGR02168 491 LDSLERLQENLEGFSE 506
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
590-989 |
1.24e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 590 EKMQQLREKLcqEEEEEILRLHQQKEQSLSSLRERLQKAieeeeARMREEESQRLSWLRAQVQsstQADEDQIRAEQEAS 669
Cdd:COG4717 71 KELKELEEEL--KEAEEKEEEYAELQEELEELEEELEEL-----EAELEELREELEKLEKLLQ---LLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 670 LQKLREELES--QQKAERASLEQKNRQMLEQLkEEIEASEKSEQAALNAAKEKALQQLREQLEgERKEAVATLEKEhSAE 747
Cdd:COG4717 141 LAELPERLEEleERLEELRELEEELEELEAEL-AELQEELEELLEQLSLATEEELQDLAEELE-ELQQRLAELEEE-LEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 748 LERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQV------EHRVHQKSYHVAGYEHELSSLLREKRQEVEGEH 821
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALlallglGGSLLSLILTIAGVLFLVLGLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 822 ERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKlqdl 901
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA---- 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 902 ELDLETRAKDVKARLALLE-VQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQA 980
Cdd:COG4717 374 ALLAEAGVEDEEELRAALEqAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELRE 453
|
....*....
gi 578822059 981 RKLKLESQV 989
Cdd:COG4717 454 ELAELEAEL 462
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
563-978 |
2.34e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 563 EAALKAMEEAVAQVLE-QDQRHLLESKQEKMQQLREKLCQEEEE-EILRLHQQKEQSLSSLRERLQkaieeeearmreEE 640
Cdd:COG4717 77 EEELKEAEEKEEEYAElQEELEELEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELA------------EL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 641 SQRLSWLRAQVQSSTQADEDQIRAEQEasLQKLREELESQQKAERASLEQKNRQMLEQLkEEIEASEKSEQAALNAAKEK 720
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAE--LAELQEELEELLEQLSLATEEELQDLAEEL-EELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 721 aLQQLREQLEGERKEAVATLEKEHSAELERL-------------------------------------CSSLEAKHREVV 763
Cdd:COG4717 222 -LEELEEELEQLENELEAAALEERLKEARLLlliaaallallglggsllsliltiagvlflvlgllalLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 764 SSLQKKIQEAQQK---EEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKA- 839
Cdd:COG4717 301 GKEAEELQALPALeelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAg 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 840 ----------------REQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLEL 903
Cdd:COG4717 381 vedeeelraaleqaeeYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEA 460
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578822059 904 DLETRAKDvkARLALLEVQEETARREKQQLldVQRQVALKseeatATHQQLEEAQKEHTHLLQS--NQQLREILDEL 978
Cdd:COG4717 461 ELEQLEED--GELAELLQELEELKAELREL--AEEWAALK-----LALELLEEAREEYREERLPpvLERASEYFSRL 528
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
559-1181 |
4.09e-09 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 61.53 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 559 EQLSEAALKAMEEAVAQVLEQDQRHLLEsKQEKMQQLREKLCQ--EEEEEILRLHQQKEQsLSSLRERLQKAIEEEEARM 636
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELK-LQELKLKEQAKKALeyYQLKEKLELEEEYLL-YLDYLKLNEERIDLLQELL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 637 REEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQM------LEQLKEEIEASEKSE 710
Cdd:pfam02463 247 RDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLerrkvdDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 711 QAALNAAKEKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQkCLGQVEH 790
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE-LKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 791 RVHQKSYHVAGYEHELSSLLREKRQEVEGEhERRLDKMKEEHQQVMAKAREQYEAEERKQRAEllghltgELERLQRAHE 870
Cdd:pfam02463 406 EAQLLLELARQLEDLLKEEKKEELEILEEE-EESIELKQGKLTEEKEELEKQELKLLKDELEL-------KKSEDLLKET 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 871 RELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALkSEEATAT 950
Cdd:pfam02463 478 QLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV-IVEVSAT 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 951 HQQLEEAQKEHTHLLQSNQqlreILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLREVTVEENNASPH 1030
Cdd:pfam02463 557 ADEVEERQKLVRALTELPL----GARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDT 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1031 FEPDLHIEDLRKSLGTNQTKEVSSSLSQSKEDLYLDSLSshnvwhLLSAEGVALRSAKEFLVQQTRSMRRRQTALKAAQQ 1110
Cdd:pfam02463 633 ELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSEL------TKELLEIQELQEKAESELAKEEILRRQLEIKKKEQ 706
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578822059 1111 HWRHELASAQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSLWEEASDE 1181
Cdd:pfam02463 707 REKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELA 777
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
607-935 |
8.75e-09 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 60.37 E-value: 8.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 607 ILRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERA 686
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 687 SLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQlreQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSL 766
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEK---KLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 767 QKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYE-A 845
Cdd:pfam02463 321 KEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELElK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 846 EERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEET 925
Cdd:pfam02463 401 SEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480
|
330
....*....|
gi 578822059 926 ARREKQQLLD 935
Cdd:pfam02463 481 KLQEQLELLL 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
560-935 |
1.21e-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: 60.08 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 560 QLSEAALKAMEEAVAQVLE--QDQRHLLESKQEKMQQLREKLCQEEeeeilrlhQQKEQSLSSLRERLQKAieeeeARMR 637
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEglKRELSSLQSELRRIENRLDELSQEL--------SDASRKIGEIEKEIEQL-----EQEE 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 638 EEESQRLSWLRAQVQSSTQADEDQIR---------AEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIeaSEK 708
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQEIENVKSelkeleariEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEV--SRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 709 SEQAALNAAKEKALQQLREQLEGERKEAVATLEkehsaelerlcssleakhrevvsSLQKKIQEAQQKEEAqLQKCLGQV 788
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRI-----------------------DLKEQIKSIEKEIEN-LNGKKEEL 866
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 789 EHRVHQKSYHVAGYEHELSSLLREKRqevegEHERRLDKMKEEHQQvmAKAREQYEAEERKQRAELLGHLTGELERLQRA 868
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKKERD-----ELEAQLRELERKIEE--LEAQIEKKRKRLSELKAKLEALEEELSEIEDP 939
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578822059 869 HERELETVRQEQhkRLEDLRRRHREQERKLQDLElDLETRA----KDVKARLALLEVQEETARREKQQLLD 935
Cdd:TIGR02169 940 KGEDEEIPEEEL--SLEDVQAELQRVEEEIRALE-PVNMLAiqeyEEVLKRLDELKEKRAKLEEERKAILE 1007
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
665-1024 |
3.44e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 665 EQEASLQKLREELESQQK--AERASLEQKNRQMLEQLKE---EIEASEKSEQAALNA-AKEKALQQLREQLEGERKEAVa 738
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEEriKELEEKEERLEELKKKLKElekRLEELEERHELYEEAkAKKEELERLKKRLTGLTPEKL- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 739 tleKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEA--QLQKCLGQV-----EHRVHQKSYHVAGYEHELSSLLR 811
Cdd:PRK03918 390 ---EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAieELKKAKGKCpvcgrELTEEHRKELLEEYTAELKRIEK 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 812 EKRqevegEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRaheRELEtvrqEQHKRLEDLRRRH 891
Cdd:PRK03918 467 ELK-----EIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNL---EELE----KKAEEYEKLKEKL 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 892 REQERKLQDLELDLEtRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKS-EEATATHQQLEEAQKEHTHLLQSNQQ 970
Cdd:PRK03918 535 IKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELEELGFESvEELEERLKELEPFYNEYLELKDAEKE 613
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 578822059 971 LREILDELQarklKLESQVDLLQAQSQQLQKHFSSLEAEAQKkqhLLREVTVEE 1024
Cdd:PRK03918 614 LEREEKELK----KLEEELDKAFEELAETEKRLEELRKELEE---LEKKYSEEE 660
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
646-960 |
6.81e-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: 57.39 E-value: 6.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 646 WLRAQVQSSTQADEDQIRAeQEASLQKLREELESQQKAERASLEQKNrQMLEQLKEEIEASEKSEQAALnaaKEKALQQL 725
Cdd:TIGR02169 226 YELLKEKEALERQKEAIER-QLASLEEELEKLTEEISELEKRLEEIE-QLLEELNKKIKDLGEEEQLRV---KEKIGELE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 726 REQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEaQQKEEAQLQKCLGQVEHRVHQKSYHVAgyehE 805
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEE-ERKRRDKLTEEYAELKEELEDLRAELE----E 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 806 LSSLLREKRQEVEgEHERRLDKMKEEHQQVmaKAREQYEAEERKQRAELLGHLTGELERLQRAHeRELETvrqeqhkRLE 885
Cdd:TIGR02169 376 VDKEFAETRDELK-DYREKLEKLKREINEL--KRELDRLQEELQRLSEELADLNAAIAGIEAKI-NELEE-------EKE 444
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578822059 886 DLRRRHREQERKLQDLELDLEtrakdvKARLALLEVQEETARREKQqlldvQRQVALKSEEATATHQQLEEAQKE 960
Cdd:TIGR02169 445 DKALEIKKQEWKLEQLAADLS------KYEQELYDLKEEYDRVEKE-----LSKLQRELAEAEAQARASEERVRG 508
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
680-973 |
9.27e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 55.70 E-value: 9.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 680 QQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEgerkeavatlEKEHSAELERLcssLEAKH 759
Cdd:pfam13868 33 RIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIE----------EREQKRQEEYE---EKLQE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 760 REVVSSLQKKIQEAQQKEEAQLQKclgqvehRVHQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKA 839
Cdd:pfam13868 100 REQMDEIVERIQEEDQAEAEEKLE-------KQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEERE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 840 REQYEAEERKQR-AELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDlETRAKDVKARLAL 918
Cdd:pfam13868 173 AEREEIEEEKEReIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQ-QAREEQIELKERR 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 578822059 919 LEVQEETARREKQQLLDVQR-QVALKSEEATATHQQLEEAQKEHTHLLQSNQQLRE 973
Cdd:pfam13868 252 LAEEAEREEEEFERMLRKQAeDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRA 307
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
653-1171 |
1.04e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 653 SSTQADEDQIRAEQEASLQKLRE--ELESQQKAERASLE--QKNRQMLEQLKEEIEASEKSEQAALNAAK--EKALQQLR 726
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREinEISSELPELREELEklEKEVKELEELKEEIEELEKELESLEGSKRklEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 727 EQLEGERKE-------------------AVATLEKEHSAELERL--CSSLEAKHREVVSSLQKKIQEAQQKEE--AQLQK 783
Cdd:PRK03918 266 ERIEELKKEieeleekvkelkelkekaeEYIKLSEFYEEYLDELreIEKRLSRLEEEINGIEERIKELEEKEErlEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 784 CLGQVEHRVHQKSYHVAGYEhELSSLLREKRQEVEGEHERRLDKMKEEHQQVmAKAREQYEAEERKQRAELlGHLTGELE 863
Cdd:PRK03918 346 KLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEKLEKELEEL-EKAKEEIEEEISKITARI-GELKKEIK 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 864 RLQRAHErELETVRQ---------EQHKRLEDLRRRHREQERKLQDLElDLETRAKDVKARLALLEVQeetarREKQQLL 934
Cdd:PRK03918 423 ELKKAIE-ELKKAKGkcpvcgrelTEEHRKELLEEYTAELKRIEKELK-EIEEKERKLRKELRELEKV-----LKKESEL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 935 DVQRQVA--LKSEEATATHQQLEEAQKEHTHLlqsnQQLREILDELQARKLKLESQVdllqaqsqqlqkhfSSLEAEAQK 1012
Cdd:PRK03918 496 IKLKELAeqLKELEEKLKKYNLEELEKKAEEY----EKLKEKLIKLKGEIKSLKKEL--------------EKLEELKKK 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1013 KQHLLREV-TVEENNASphfepdlhIEDLRKSLGTNQTKEVSSSLsQSKEDLYLDSLSSHNVWHLLSAEGVALRSAKEFL 1091
Cdd:PRK03918 558 LAELEKKLdELEEELAE--------LLKELEELGFESVEELEERL-KELEPFYNEYLELKDAEKELEREEKELKKLEEEL 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1092 VQ----------QTRSMRRRQTALKAAQQHWRHE------LASAQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSAMRK 1155
Cdd:PRK03918 629 DKafeelaetekRLEELRKELEELEKKYSEEEYEelreeyLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREK 708
|
570
....*....|....*.
gi 578822059 1156 GHNLLKKKEEKLNQLE 1171
Cdd:PRK03918 709 AKKELEKLEKALERVE 724
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
869-1186 |
1.31e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 869 HERELETVR-----QEQHKRLEDLRRrhrEQERKLQDLEL---------DLETRAKDVKARLALLEVQEETARRE--KQQ 932
Cdd:TIGR02168 171 KERRKETERklertRENLDRLEDILN---ELERQLKSLERqaekaerykELKAELRELELALLVLRLEELREELEelQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 933 LLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQK 1012
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1013 KQHLLREVTVEENNASPHFEPDL-HIEDLRKSLGT-NQTKEVSSSLSQSKEDLYLDslsshnvwhlLSAEGVALRSAKEF 1090
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKeELESLEAELEElEAELEELESRLEELEEQLET----------LRSKVAQLELQIAS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1091 LVQQTRSMRRRQTALKAAQQHWRHELASAQEVAKDPpgikALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQL 1170
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA----ELKELQAELEELEEELEELQEELERLEEALEELREELEEA 473
|
330
....*....|....*.
gi 578822059 1171 ESSLWEEASDEGTLGG 1186
Cdd:TIGR02168 474 EQALDAAERELAQLQA 489
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
711-949 |
1.52e-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: 55.54 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 711 QAALNAAKEKALQQLREQLEgERKEAVATLEKEHSAELERLcssleAKHREVVSSLQKKIQEAQQkEEAQLQKCLGQVEH 790
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIA-ELEKELAALKKEEKALLKQL-----AALERRIAALARRIRALEQ-ELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 791 RVHQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRahe 870
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA--- 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578822059 871 rELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATA 949
Cdd:COG4942 168 -ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
571-933 |
2.92e-07 |
|
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: 55.11 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 571 EAVAQVLEQDQRHLLESKQekMQQLREKLcqeeeeeilrlhQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLRAQ 650
Cdd:pfam05483 408 EELKKILAEDEKLLDEKKQ--FEKIAEEL------------KGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEV 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 651 VQSSTQADEDQIR-AEQEASLQKLR-EELESQQKAERASLEQKNRQ------------MLEQLkEEIEASEKSEQAALNA 716
Cdd:pfam05483 474 EDLKTELEKEKLKnIELTAHCDKLLlENKELTQEASDMTLELKKHQediinckkqeerMLKQI-ENLEEKEMNLRDELES 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 717 AKEKALQQ-------LREQLEGERKEAVATLEKEHSAE-LERLCSSLeakhREVVSSLQKKIQEAQQKEEAQLQKC---- 784
Cdd:pfam05483 553 VREEFIQKgdevkckLDKSEENARSIEYEVLKKEKQMKiLENKCNNL----KKQIENKNKNIEELHQENKALKKKGsaen 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 785 --LGQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEGE---HERRLDKMKEEHQQVMAKAREQYEAEERKQraellgHLT 859
Cdd:pfam05483 629 kqLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKkisEEKLLEEVEKAKAIADEAVKLQKEIDKRCQ------HKI 702
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578822059 860 GELERLQRAHERELETVRQEQHKRLEDLRRRHREQerklQDLELDLETRAKDVKARLALLEVQEETARREKQQL 933
Cdd:pfam05483 703 AEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQ----SSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKL 772
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
667-901 |
4.27e-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: 54.96 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 667 EASLQKLRE---ELESQQKAERASlEQKNRQMLEQLKEEIEASEK-SEQAALNAAKEKA--LQQLREQLEgERKEAVATL 740
Cdd:COG3096 835 EAELAALRQrrsELERELAQHRAQ-EQQLRQQLDQLKEQLQLLNKlLPQANLLADETLAdrLEELREELD-AAQEAQAFI 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 741 EK--EHSAELERLCSSLEAKhREVVSSLQKKIQEAQQKEEAQLQKC--LGQVEHRVHQKSYHVA----GYEHELSSLLRE 812
Cdd:COG3096 913 QQhgKALAQLEPLVAVLQSD-PEQFEQLQADYLQAKEQQRRLKQQIfaLSEVVQRRPHFSYEDAvgllGENSDLNEKLRA 991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 813 KRQEVEGEHERRLDKMK------EEHQQVMAKAREQYEAeerkqRAELLGHLTGELERL---------QRAHER------ 871
Cdd:COG3096 992 RLEQAEEARREAREQLRqaqaqySQYNQVLASLKSSRDA-----KQQTLQELEQELEELgvqadaeaeERARIRrdelhe 1066
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 578822059 872 ----------ELETVRQEQHKRLEDLRRRHREQERKLQDL 901
Cdd:COG3096 1067 elsqnrsrrsQLEKQLTRCEAEMDSLQKRLRKAERDYKQE 1106
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
566-1185 |
5.15e-07 |
|
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: 54.67 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 566 LKAMEEAVAQVLE-QDQRHLLESKQEKMQQLREKLCQEEEE----------EILRLHQQKEQSLSSLRERLQKAIEEEEA 634
Cdd:TIGR00606 254 LKEIEHNLSKIMKlDNEIKALKSRKKQMEKDNSELELKMEKvfqgtdeqlnDLYHNHQRTVREKERELVDCQRELEKLNK 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 635 RMREEESQRLSWLRAQVQSSTQAD--EDQIRAEQEASLQ-KLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQ 711
Cdd:TIGR00606 334 ERRLLNQEKTELLVEQGRLQLQADrhQEHIRARDSLIQSlATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 712 AALNAAKEKALQQLREQLEGERKEAVATLEKEhSAELERLCSSL-----EAKHREVVSSLQKKIQEAQQKEEAQLQKClg 786
Cdd:TIGR00606 414 CADLQSKERLKQEQADEIRDEKKGLGRTIELK-KEILEKKQEELkfvikELQQLEGSSDRILELDQELRKAERELSKA-- 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 787 QVEHRVHQKSYHVAGYEHELSSLLREKRQEVEGEHErrLDKMKEEHQQVMAKAREQYEAEER------KQRAELLGHL-- 858
Cdd:TIGR00606 491 EKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQ--LNHHTTTRTQMEMLTKDKMDKDEQirkiksRHSDELTSLLgy 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 859 ---TGELERLQRAHERELETVR------QEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARlallEVQEETARRE 929
Cdd:TIGR00606 569 fpnKKQLEDWLHSKSKEINQTRdrlaklNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS----QDEESDLERL 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 930 KQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAE 1009
Cdd:TIGR00606 645 KEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKR 724
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1010 aqkKQHLLREVTVEENnasphfEPDLHIEDLRKSlgTNQTKEVSSSLSQSKEDLYLDSlsshnvwHLLSAEGVALRSAKE 1089
Cdd:TIGR00606 725 ---RDEMLGLAPGRQS------IIDLKEKEIPEL--RNKLQKVNRDIQRLKNDIEEQE-------TLLGTIMPEEESAKV 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1090 FLVQQTrSMRRRQTALKAAQQHWRHELASAQEVAKDppgiKALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQ 1169
Cdd:TIGR00606 787 CLTDVT-IMERFQMELKDVERKIAQQAAKLQGSDLD----RTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQH 861
|
650
....*....|....*.
gi 578822059 1170 LESSLWEEASDEGTLG 1185
Cdd:TIGR00606 862 LKSKTNELKSEKLQIG 877
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
801-1149 |
5.55e-07 |
|
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: 54.30 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 801 GYEHELSSLLREKRqEVEGEHERRLDKMKEEHQQV--MAKAREQYEAEERKQRAELlghltGELERLQRAHERELETVRQ 878
Cdd:TIGR02169 685 GLKRELSSLQSELR-RIENRLDELSQELSDASRKIgeIEKEIEQLEQEEEKLKERL-----EELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 879 EqhkrLEDLRRRHREQERKLQDLELDLEtrakDVKARLALLEVQEETARREKQQLlDVQRQVAlkseeatathqQLEEAQ 958
Cdd:TIGR02169 759 E----LKELEARIEELEEDLHKLEEALN----DLEARLSHSRIPEIQAELSKLEE-EVSRIEA-----------RLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 959 KEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLREVTVEennasphfepdlhIE 1038
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR-------------LG 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1039 DLRKslgtnQTKEVSSSLSQSKEdlyldslsshnvwhllsaegvALRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELAS 1118
Cdd:TIGR02169 886 DLKK-----ERDELEAQLRELER---------------------KIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDP 939
|
330 340 350
....*....|....*....|....*....|.
gi 578822059 1119 AQEVAKDPPGIKALEDMRKNLEKETRHLDEM 1149
Cdd:TIGR02169 940 KGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
821-990 |
5.67e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 5.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 821 HERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELEtvRQEQHKRLEDLRRRHREQERKLQD 900
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE--KLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 901 LEldleTRAKDVKARLALLEVQEETARREKQQLLDVQRQVA-LKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQ 979
Cdd:COG4717 144 LP----ERLEELEERLEELRELEEELEELEAELAELQEELEeLLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170
....*....|.
gi 578822059 980 ARKLKLESQVD 990
Cdd:COG4717 220 EELEELEEELE 230
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
643-988 |
7.99e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 7.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 643 RLSWLRAQVQSSTQADEDQIRAEQEASLQKLREEL---ESQQKAERASLEQKN---------RQMLEQLKEEIEASEKSE 710
Cdd:PRK02224 188 SLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIeryEEQREQARETRDEADevleeheerREELETLEAEIEDLRETI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 711 qaalnAAKEKALQQLREQLEgERKEAVATLEKEHSAELERlcSSLEAKHREVVSSLqkkiQEAQQKEEAQLQKCLGQVEH 790
Cdd:PRK02224 268 -----AETEREREELAEEVR-DLRERLEELEEERDDLLAE--AGLDDADAEAVEAR----REELEDRDEELRDRLEECRV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 791 RVHQKSYHVAGYEHELSSL------LREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEER-----KQRAELLGHLT 859
Cdd:PRK02224 336 AAQAHNEEAESLREDADDLeeraeeLREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapVDLGNAEDFLE 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 860 GELERLQRAHER--ELETVRQEQHKRLEDLRR------------------------RHREQERKLQDLELDLETRAKDVK 913
Cdd:PRK02224 416 ELREERDELREReaELEATLRTARERVEEAEAlleagkcpecgqpvegsphvetieEDRERVEELEAELEDLEEEVEEVE 495
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578822059 914 ARLALLEVQEETARR---EKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREildelQARKLKLESQ 988
Cdd:PRK02224 496 ERLERAEDLVEAEDRierLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKRE-----AAAEAEEEAE 568
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
576-946 |
8.66e-07 |
|
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: 8.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 576 VLEQDQRHLLESKQEKMQQLREKLcQEEEEEILRLHQQKEQsLSSLRERLQKAIEEEEARMREEESQR-LSWLRAQVQSS 654
Cdd:COG4913 603 VLGFDNRAKLAALEAELAELEEEL-AEAEERLEALEAELDA-LQERREALQRLAEYSWDEIDVASAEReIAELEAELERL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 655 TQADED-----QIRAEQEASLQKLREELEsQQKAERASLEQKnrqmLEQLKEEIEASekseQAALNAAKEKALQQLREQL 729
Cdd:COG4913 681 DASSDDlaaleEQLEELEAELEELEEELD-ELKGEIGRLEKE----LEQAEEELDEL----QDRLEAAEDLARLELRALL 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 730 EGERKEA-VATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQkclgqvEHRVHQKSYHvaGYEHELSS 808
Cdd:COG4913 752 EERFAAAlGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETA------DLDADLESLP--EYLALLDR 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 809 LLREKRQEVEGEHERRLDKMKEEH----QQVMAKAREqyEAEERkqraelLGHLTGELERLQRAHERELE-TVRQEQHKR 883
Cdd:COG4913 824 LEEDGLPEYEERFKELLNENSIEFvadlLSKLRRAIR--EIKER------IDPLNDSLKRIPFGPGRYLRlEARPRPDPE 895
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578822059 884 LEDLRRRHREQERKLQDLELDL-ETRAKDVKARLALLEVQE-ETARREKQQLLDVQRQVALKSEE 946
Cdd:COG4913 896 VREFRQELRAVTSGASLFDEELsEARFAALKRLIERLRSEEeESDRRWRARVLDVRNHLEFDAEE 960
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
453-777 |
9.35e-07 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 53.61 E-value: 9.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 453 ERAQSPPRSLATEEEPPQGPEGQPEWKEAEELGEDSAASLSLQLSLQREQAPSppAACEKGKEQHSQAEELgpgQEEAED 532
Cdd:pfam09731 76 TGESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEK--ALEEVLKEAISKAESA---TAVAKE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 533 PEEKVAVSPTPPVSPEVRSTEPVAPPEQLSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQ 612
Cdd:pfam09731 151 AKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDN 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 613 -----QKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLRAQVQ---SSTQADEDQIRAEQEASLQKLREELESQQKAE 684
Cdd:pfam09731 231 veekvEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKednLLSNDDLNSLIAHAHREIDQLSKKLAELKKRE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 685 RASLEQKnrqmLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVS 764
Cdd:pfam09731 311 EKHIERA----LEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLV 386
|
330
....*....|...
gi 578822059 765 SLQKKIQEAQQKE 777
Cdd:pfam09731 387 EQEIELQREFLQD 399
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
684-980 |
9.55e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 684 ERAS--------LEQKNRQMLEQLKEEIEASEKSE-QAALNAAkEKALQQLREQL---EGERKEAVATLEK------EHS 745
Cdd:PRK02224 169 ERASdarlgverVLSDQRGSLDQLKAQIEEKEEKDlHERLNGL-ESELAELDEEIeryEEQREQARETRDEadevleEHE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 746 AELERLcSSLEAKHREvvssLQKKIQEAQQKEEaqlqkclgqvehrvhqksyhvagyehELSSLLREKRQEVEGEHERRL 825
Cdd:PRK02224 248 ERREEL-ETLEAEIED----LRETIAETERERE--------------------------ELAEEVRDLRERLEELEEERD 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 826 DKMKEehqqvmaKAREQYEAEERKQRAEllghltgELERLQRAHERELETVRQEQhkrledlrRRHREQERKLQDLELDL 905
Cdd:PRK02224 297 DLLAE-------AGLDDADAEAVEARRE-------ELEDRDEELRDRLEECRVAA--------QAHNEEAESLREDADDL 354
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578822059 906 ETRAKDVKARLALLEVQEETARRE----KQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQA 980
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAvedrREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEA 433
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
644-879 |
9.63e-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: 52.84 E-value: 9.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 644 LSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQknrqmLEQLKEEIEASEK------SEQAALNA- 716
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ-----LAALERRIAALARriraleQELAALEAe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 717 -----AKEKALQQLREQLEGERKEAVATLEKEHSA-ELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEH 790
Cdd:COG4942 85 laeleKEIAELRAELEAQKEELAELLRALYRLGRQpPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 791 RVHQKSYHVAgyehELSSLLREKRQEvegehERRLDKMKEEHQQVMAKAREQYEAEErkQRAELLGHLTGELERLQRAHE 870
Cdd:COG4942 165 LRAELEAERA----ELEALLAELEEE-----RAALEALKAERQKLLARLEKELAELA--AELAELQQEAEELEALIARLE 233
|
....*....
gi 578822059 871 RELETVRQE 879
Cdd:COG4942 234 AEAAAAAER 242
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
561-749 |
1.07e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.24 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 561 LSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKlcqeeeeeILRLHQQKEQSLSSLRERLQkaieeeearmreee 640
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEE--------IHKLRNEFEKELRERRNELQ-------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 641 sqrlswlraQVQSSTQADEDQIRAEQEaSLQKLREELESQQKaeraSLEQKNRQmLEQLKEEIEASEKSEQAAL----NA 716
Cdd:PRK12704 86 ---------KLEKRLLQKEENLDRKLE-LLEKREEELEKKEK----ELEQKQQE-LEKKEEELEELIEEQLQELerisGL 150
|
170 180 190
....*....|....*....|....*....|....*
gi 578822059 717 AKEKALQQLREQLEGE-RKEAVATL-EKEHSAELE 749
Cdd:PRK12704 151 TAEEAKEILLEKVEEEaRHEAAVLIkEIEEEAKEE 185
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
563-1179 |
1.57e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 563 EAALKAMEEAVAQVLEQ--DQRHLLESKQEKMQQLREKLCQEEEEEILRLhQQKEQSLSSLRERLQKAIEEEEarmreee 640
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEisELEKRLEEIEQLLEELNKKIKDLGEEEQLRV-KEKIGELEAEIASLERSIAEKE------- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 641 sQRLSWLRAQVQsstQADEDqiRAEQEASLQKLREELESQQKaERASLE---QKNRQMLEQLKEEIEASEKSEQAA---L 714
Cdd:TIGR02169 315 -RELEDAEERLA---KLEAE--IDKLLAEIEELEREIEEERK-RRDKLTeeyAELKEELEDLRAELEEVDKEFAETrdeL 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 715 NAAKEK--ALQQLREQLEGERKEAVATLEKEHS--AELERLCSSLEAKHREVVS---SLQKKIQEAQQKEEaQLQKCLGQ 787
Cdd:TIGR02169 388 KDYREKleKLKREINELKRELDRLQEELQRLSEelADLNAAIAGIEAKINELEEekeDKALEIKKQEWKLE-QLAADLSK 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 788 VEHRVHQKSYHVAGYEHELSSLLRE-------KRQEVEGEHERR-------------------LDKMKEEHQ-------- 833
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRElaeaeaqARASEERVRGGRaveevlkasiqgvhgtvaqLGSVGERYAtaievaag 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 834 ----------QVMAKAREQYEAEERKQRAELL-------GHLTGELERLQRAHERELETVRQEQHKR------------L 884
Cdd:TIGR02169 547 nrlnnvvvedDAVAKEAIELLKRRKAGRATFLplnkmrdERRDLSILSEDGVIGFAVDLVEFDPKYEpafkyvfgdtlvV 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 885 EDLR--RRHREQERkLQDLELDL-----------------ETRAKDVKARLALLEVQEETARREKQQLLD----VQRQVA 941
Cdd:TIGR02169 627 EDIEaaRRLMGKYR-MVTLEGELfeksgamtggsraprggILFSRSEPAELQRLRERLEGLKRELSSLQSelrrIENRLD 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 942 LKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLREVt 1021
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL- 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1022 veENNASPHFEPDL--HIEDLRKSLGTNQtkEVSSSLSQSKEDLYLDSLSshnvwhllsaegvaLRSAKEFLVQQTRSMR 1099
Cdd:TIGR02169 785 --EARLSHSRIPEIqaELSKLEEEVSRIE--ARLREIEQKLNRLTLEKEY--------------LEKEIQELQEQRIDLK 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1100 RRQTALKAAQQHWRHELAS-AQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSLWEEA 1178
Cdd:TIGR02169 847 EQIKSIEKEIENLNGKKEElEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
.
gi 578822059 1179 S 1179
Cdd:TIGR02169 927 E 927
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
574-916 |
1.73e-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: 51.84 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 574 AQVLEQDQRHLLESKQEK-----MQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLR 648
Cdd:pfam13868 26 AQIAEKKRIKAEEKEEERrldemMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 649 AQVQssTQADEDQIRAEQEASLQKLREELEsQQKAERASLEQKNRQMLEQL----------KEEIEASEKSEQAALNAAK 718
Cdd:pfam13868 106 IVER--IQEEDQAEAEEKLEKQRQLREEID-EFNEEQAEWKELEKEEEREEderileylkeKAEREEEREAEREEIEEEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 719 EKALQQLREQLEGERKEavatLEKEHSAELERLCSSLEAKHRevvsslQKKIQEAQQKEEAQLQKCLGQVEHRVHqksyh 798
Cdd:pfam13868 183 EREIARLRAQQEKAQDE----KAERDELRAKLYQEEQERKER------QKEREEAEKKARQRQELQQAREEQIEL----- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 799 vagyehelssllREKRQEVEGEHERRLDKMKEEHQQVMAKaREQYEAEERKQRaellghltgelerlQRAHERELETVRQ 878
Cdd:pfam13868 248 ------------KERRLAEEAEREEEEFERMLRKQAEDEE-IEQEEAEKRRMK--------------RLEHRRELEKQIE 300
|
330 340 350
....*....|....*....|....*....|....*...
gi 578822059 879 EQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARL 916
Cdd:pfam13868 301 EREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
664-853 |
1.99e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.09 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 664 AEQEASLQKLREELESQQKAERASLEQKnrQMLEQLKEEIEAsEKSEQAALNAAKEKALQQLREQLEgERKEAvatLEKE 743
Cdd:PRK12704 36 AEEEAKRILEEAKKEAEAIKKEALLEAK--EEIHKLRNEFEK-ELRERRNELQKLEKRLLQKEENLD-RKLEL---LEKR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 744 hSAELERLCSSLEAKHREvvssLQKKIQEAQQKEEAQLQKCLgqvehrvhqksyHVAGYEHElssllrEKRQEVegeher 823
Cdd:PRK12704 109 -EEELEKKEKELEQKQQE----LEKKEEELEELIEEQLQELE------------RISGLTAE------EAKEIL------ 159
|
170 180 190
....*....|....*....|....*....|
gi 578822059 824 rLDKMKEEHQQVMAKAREQYEaEERKQRAE 853
Cdd:PRK12704 160 -LEKVEEEARHEAAVLIKEIE-EEAKEEAD 187
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
559-1177 |
2.36e-06 |
|
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: 52.28 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 559 EQLSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMRE 638
Cdd:pfam02463 287 ELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 639 EESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAAL---- 714
Cdd:pfam02463 367 KLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKqgkl 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 715 ----NAAKEKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQK---CLGQ 787
Cdd:pfam02463 447 teekEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGvggRIIS 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 788 VEHRVHQKSYHVAGYEHELSSL-----LREKRQEVEGEHERR---------------LDKMKEEHQQVMAKAREQYEAEE 847
Cdd:pfam02463 527 AHGRLGDLGVAVENYKVAISTAvivevSATADEVEERQKLVRaltelplgarklrllIPKLKLPLKSIAVLEIDPILNLA 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 848 RKQRAELLGHLTGELERLQRAHERE-LETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEetA 926
Cdd:pfam02463 607 QLDKATLEADEDDKRAKVVEGILKDtELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQE--K 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 927 RREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQvDLLQAQSQQLQKHFSSL 1006
Cdd:pfam02463 685 AESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKID-EEEEEEEKSRLKKEEKE 763
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1007 EAEAQKKQHLLREVTVEENNASPHFEPDLHIEDLRKSLG-TNQTKEVSSSLSQSKEDLYLDSLSSH---NVWHLLSAEGV 1082
Cdd:pfam02463 764 EEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEElRALEEELKEEAELLEEEQLLIEQEEKikeEELEELALELK 843
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1083 ALRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELASAQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSAMRKGHNLLKK 1162
Cdd:pfam02463 844 EEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERI 923
|
650
....*....|....*
gi 578822059 1163 KEEKLNQLESSLWEE 1177
Cdd:pfam02463 924 KEEAEILLKYEEEPE 938
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
700-1178 |
3.11e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 700 KEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKEHSAElerlcsslEAKHREVVsslqKKIQEAQQKEEA 779
Cdd:PTZ00121 1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAE--------EARKAEDA----RKAEEARKAEDA 1151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 780 QLQKCLGQVEHRVHQKSYHVAgyehELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAEllghlt 859
Cdd:PTZ00121 1152 KRVEIARKAEDARKAEEARKA----EDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAE------ 1221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 860 gelerlqraHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQ 939
Cdd:PTZ00121 1222 ---------DAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA 1292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 940 VALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLRE 1019
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK 1372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1020 VTVEENNASphfEPDLHIEDLRKSlgtNQTKEVSSSLSQSKEDLYLDSLSSHNVwHLLSAEGVALRSAKEfLVQQTRSMR 1099
Cdd:PTZ00121 1373 KEEAKKKAD---AAKKKAEEKKKA---DEAKKKAEEDKKKADELKKAAAAKKKA-DEAKKKAEEKKKADE-AKKKAEEAK 1444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1100 RRQTALKAAQqhwrhELASAQEVAKDPPGIKALEDMRKNLEkETRHLDEMK----SAMRKGHNLLKKKEEKLNQLESSLW 1175
Cdd:PTZ00121 1445 KADEAKKKAE-----EAKKAEEAKKKAEEAKKADEAKKKAE-EAKKADEAKkkaeEAKKKADEAKKAAEAKKKADEAKKA 1518
|
...
gi 578822059 1176 EEA 1178
Cdd:PTZ00121 1519 EEA 1521
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
581-783 |
3.13e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 581 QRHLLESKQEKMQQLREKLcqEEEEEILRLHQQKEQSLSSLRERLQKAIEeEEARMREEESQRLSWLRAQVQsSTQADED 660
Cdd:COG4942 18 QADAAAEAEAELEQLQQEI--AELEKELAALKKEEKALLKQLAALERRIA-ALARRIRALEQELAALEAELA-ELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 661 QIRAEQEASLQKLREELESQQKAERASLEQ------------KNRQMLEQLKEEIEaseksEQAALNAAKEKALQQLREQ 728
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLAlllspedfldavRRLQYLKYLAPARR-----EQAEELRADLAELAALRAE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 578822059 729 LEGERKEaVATLEKEHSAELERLcSSLEAKHREVVSSLQKKIQEAQQKEEAQLQK 783
Cdd:COG4942 169 LEAERAE-LEALLAELEEERAAL-EALKAERQKLLARLEKELAELAAELAELQQE 221
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
563-1028 |
3.48e-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: 51.71 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 563 EAALKAMEEAVAQVLEQDQRHLLESKQekmqqLREKLCQEEEEeiLRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQ 642
Cdd:pfam01576 130 EAKIKKLEEDILLLEDQNSKLSKERKL-----LEERISEFTSN--LAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 643 RLSWLRAQVQSSTQADE--DQIR------AEQEASLQKLREELES------QQKAERASLEQKNRQMLEQLKEEIEASEk 708
Cdd:pfam01576 203 RQELEKAKRKLEGESTDlqEQIAelqaqiAELRAQLAKKEEELQAalarleEETAQKNNALKKIRELEAQISELQEDLE- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 709 SEQAALNAAkEKALQQLREQLEGERKEAVATL-----EKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQK 783
Cdd:pfam01576 282 SERAARNKA-EKQRRDLGEELEALKTELEDTLdttaaQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 784 CLGQVEHRVHQKS---YHVAGYEHELSSLLREKR--QEVEGEHERRLDKMKEEHQQVMAKAREQyeAEERKQRAELLGHL 858
Cdd:pfam01576 361 LTEQLEQAKRNKAnleKAKQALESENAELQAELRtlQQAKQDSEHKRKKLEGQLQELQARLSES--ERQRAELAEKLSKL 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 859 TGELERLQRAHErELETVRQEQHKRLEDLrrrhreqERKLQDLE--LDLETRAK------------DVKARLALLEVQEE 924
Cdd:pfam01576 439 QSELESVSSLLN-EAEGKNIKLSKDVSSL-------ESQLQDTQelLQEETRQKlnlstrlrqledERNSLQEQLEEEEE 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 925 TARREKQQLLDVQRQVA---LKSEEATATHQQLEEAQKEHTHLLQS-NQQLRE---ILDELQARKLKLESQVDLLQAQSQ 997
Cdd:pfam01576 511 AKRNVERQLSTLQAQLSdmkKKLEEDAGTLEALEEGKKRLQRELEAlTQQLEEkaaAYDKLEKTKNRLQQELDDLLVDLD 590
|
490 500 510
....*....|....*....|....*....|.
gi 578822059 998 QLQKHFSSLEaeaqKKQHLLREVTVEENNAS 1028
Cdd:pfam01576 591 HQRQLVSNLE----KKQKKFDQMLAEEKAIS 617
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
648-1008 |
4.35e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.49 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 648 RAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERAsLE---QKNRQMLEQLKEEIEASEKSE--QAALNAAKEKAL 722
Cdd:COG3096 286 RALELRRELFGARRQLAEEQYRLVEMARELEELSARESD-LEqdyQAASDHLNLVQTALRQQEKIEryQEDLEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 723 QQ--LREQLEGERKEAVATLEkEHSAELERLCSSLeAKHREVVSSLQKKIQEAQQKEEAqlqkcLGQVEHRVHQKSYHVA 800
Cdd:COG3096 365 EQeeVVEEAAEQLAEAEARLE-AAEEEVDSLKSQL-ADYQQALDVQQTRAIQYQQAVQA-----LEKARALCGLPDLTPE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 801 GYEHELSSLlREKRQEVegeHERRLDKmkEEHQQVMAKAREQYEaeerkQRAELLGHLTGELERLQrAHERELETVR--- 877
Cdd:COG3096 438 NAEDYLAAF-RAKEQQA---TEEVLEL--EQKLSVADAARRQFE-----KAYELVCKIAGEVERSQ-AWQTARELLRryr 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 878 --QEQHKRLEDLRRRHREQERKL---QDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQ 952
Cdd:COG3096 506 sqQALAQRLQQLRAQLAELEQRLrqqQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQ 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 953 QLEEAQKEHTHL------------------------LQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEA 1008
Cdd:COG3096 586 QLEQLRARIKELaarapawlaaqdalerlreqsgeaLADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQ 665
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
766-1173 |
4.58e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 766 LQKKIQEAQQKEE--AQLQKCLGQVEHRVHQKSYHVAGYEHELSSLLREKRQ----EVEGEHERRLDKMKEEHQQVMAKA 839
Cdd:COG4717 76 LEEELKEAEEKEEeyAELQEELEELEEELEELEAELEELREELEKLEKLLQLlplyQELEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 840 REQYEAEERKQRAEllghltGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLET---RAKDVKARL 916
Cdd:COG4717 156 EELRELEEELEELE------AELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEaqeELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 917 ALLEVQEETArREKQQLLDVQRQVALKSE--EATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQvdllqa 994
Cdd:COG4717 230 EQLENELEAA-ALEERLKEARLLLLIAAAllALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK------ 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 995 qsqqlqkhfSSLEAEAQKKQHLLREVTVEENNASPHFEPDLHIEDLRKSLGT-NQTKEVSSSLSQSKEDLYLDSLSSHNV 1073
Cdd:COG4717 303 ---------EAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRiEELQELLREAEELEEELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1074 wHLLSAEGVALRSAKEFLVQQTrsmrRRQTALKAAQQHWRHELASAQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSAM 1153
Cdd:COG4717 374 -ALLAEAGVEDEEELRAALEQA----EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEEL 448
|
410 420
....*....|....*....|
gi 578822059 1154 RKGHNLLKKKEEKLNQLESS 1173
Cdd:COG4717 449 EELREELAELEAELEQLEED 468
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
59-89 |
4.98e-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: 4.98e-06
10 20 30
....*....|....*....|....*....|.
gi 578822059 59 PGEWKPCQDITGDIYYFNFANGQSMWDHPCD 89
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
822-987 |
6.13e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.55 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 822 ERRLDKMKEEHQQVMAKAREqyEAEERKQRAELlghltgelerlqrahereleTVRQEQHKRLEDLRRRHREQERKLQDL 901
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKK--EAEAIKKEALL--------------------EAKEEIHKLRNEFEKELRERRNELQKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 902 EldletraKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHthllqsNQQLREI--LDELQ 979
Cdd:PRK12704 88 E-------KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQ------LQELERIsgLTAEE 154
|
....*...
gi 578822059 980 ARKLKLES 987
Cdd:PRK12704 155 AKEILLEK 162
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
422-989 |
6.31e-06 |
|
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: 51.12 E-value: 6.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 422 DKDDSQSSQDELQSKQSKGLEERLspplphEERAQSPPRSLAT-EEEPPQGPEGQPEWKEAEELGEDSAASLSLQLSLQR 500
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCT------PCMPDTYHERKQVlEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQ 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 501 EQapsppaacekgKEQHSQAEELGPGQEEAEDPEEKVAVSP-TPPVSPEVRSTEPVAPPEQLSEAALKAMEEAVAQVLEQ 579
Cdd:TIGR00618 261 LL-----------KQLRARIEELRAQEAVLEETQERINRARkAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 580 DQRHL-----LESKQEKMQQL-----------------REKLCQEEEEE--ILRLHQQKE------QSLSSLRERLQK-- 627
Cdd:TIGR00618 330 RAAHVkqqssIEEQRRLLQTLhsqeihirdahevatsiREISCQQHTLTqhIHTLQQQKTtltqklQSLCKELDILQReq 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 628 -------------AIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELE--------SQQKAERA 686
Cdd:TIGR00618 410 atidtrtsafrdlQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQqlqtkeqiHLQETRKK 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 687 SLEQKNRQMLEQLKEEIEASEKSEQAALNAAKE-KALQQLREQLEGERK---EAVATLEKEHSAELERLCSSLEAKHREV 762
Cdd:TIGR00618 490 AVVLARLLELQEEPCPLCGSCIHPNPARQDIDNpGPLTRRMQRGEQTYAqleTSEEDVYHQLTSERKQRASLKEQMQEIQ 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 763 VSSLQKKIQEAQQKEEAQ-LQKCLGQVEHRVHQKSyhvagyEHELSSLLREKRQEVEGEHERRL--------DKMKEEHQ 833
Cdd:TIGR00618 570 QSFSILTQCDNRSKEDIPnLQNITVRLQDLTEKLS------EAEDMLACEQHALLRKLQPEQDLqdvrlhlqQCSQELAL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 834 QVMAKAREQYEAEERKQRAELLGHLTGELERLQR--AHERELE-----------------TVRQEQHKRLEDLRRRHREQ 894
Cdd:TIGR00618 644 KLTALHALQLTLTQERVREHALSIRVLPKELLASrqLALQKMQsekeqltywkemlaqcqTLLRELETHIEEYDREFNEI 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 895 ERKLQDLELDLETRAKdvkarlALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQkehtHLLQSNQQLREI 974
Cdd:TIGR00618 724 ENASSSLGSDLAARED------ALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELS----HLAAEIQFFNRL 793
|
650
....*....|....*
gi 578822059 975 LDELQARKLKLESQV 989
Cdd:TIGR00618 794 REEDTHLLKTLEAEI 808
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
649-847 |
6.37e-06 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 50.64 E-value: 6.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 649 AQVQSSTQADEDQIRAEQEAslQKLREELESQQKAERasleQKNRQMLEQLKEEIEASEKSEQAALNaaKEKALQQLREQ 728
Cdd:PRK00106 62 AKRESKALKKELLLEAKEEA--RKYREEIEQEFKSER----QELKQIESRLTERATSLDRKDENLSS--KEKTLESKEQS 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 729 LE------GERKEAVATLEKEHSAELERLCSSLEAKHREVVsslqkkiqeaqqkeeaqlqkcLGQVEHRVhqksyhvagy 802
Cdd:PRK00106 134 LTdkskhiDEREEQVEKLEEQKKAELERVAALSQAEAREII---------------------LAETENKL---------- 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 578822059 803 EHELSSLLREKRQEVegehERRLDKM-KEEHQQVMAKAREQYEAEE 847
Cdd:PRK00106 183 THEIATRIREAEREV----KDRSDKMaKDLLAQAMQRLAGEYVTEQ 224
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
799-977 |
6.62e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.55 E-value: 6.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 799 VAGYEHELSSLLREKRQEVEGEHERRLDKMKEEhqqvMAKAREQYEAEERKQRAELlghltGELERLQRAHERELEtvrq 878
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIKKEALLEAKEE----IHKLRNEFEKELRERRNEL-----QKLEKRLLQKEENLD---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 879 eqhKRLEDLRRRhreqERKLQDLELDLETRAKDVKARlallevQEETARREKQQLLDVQRQVALKSEEATAthQQLEEAQ 958
Cdd:PRK12704 100 ---RKLELLEKR----EEELEKKEKELEQKQQELEKK------EEELEELIEEQLQELERISGLTAEEAKE--ILLEKVE 164
|
170
....*....|....*....
gi 578822059 959 KEHTHllQSNQQLREILDE 977
Cdd:PRK12704 165 EEARH--EAAVLIKEIEEE 181
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
667-990 |
7.27e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 667 EASLQKLREELESQQKAERASLEQK--NRQMLEQLKEEIEaSEKSE----QAALNAAKEKALQQlreqlegerKEAVATL 740
Cdd:PRK04863 354 QADLEELEERLEEQNEVVEEADEQQeeNEARAEAAEEEVD-ELKSQladyQQALDVQQTRAIQY---------QQAVQAL 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 741 EKehsaeLERLC--SSLEAKhrevvsSLQKKIQEAQQKEEAQLQKCLgQVEHRVHQKSYHVAGYEHELSSLLRekrqeVE 818
Cdd:PRK04863 424 ER-----AKQLCglPDLTAD------NAEDWLEEFQAKEQEATEELL-SLEQKLSVAQAAHSQFEQAYQLVRK-----IA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 819 GEHERrldkmKEEHQQVMAKAREqyeAEERKQRAELLGHLTGELERLQRahereletvRQEQHKRLEDLRR-------RH 891
Cdd:PRK04863 487 GEVSR-----SEAWDVARELLRR---LREQRHLAEQLQQLRMRLSELEQ---------RLRQQQRAERLLAefckrlgKN 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 892 REQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQL-LDVQR-----------QVAL-----KSEEATATHQQL 954
Cdd:PRK04863 550 LDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLqARIQRlaarapawlaaQDALarlreQSGEEFEDSQDV 629
|
330 340 350
....*....|....*....|....*....|....*.
gi 578822059 955 EEAQKEHTHLLQSNQQLReilDELQARKLKLESQVD 990
Cdd:PRK04863 630 TEYMQQLLERERELTVER---DELAARKQALDEEIE 662
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
664-914 |
8.90e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 8.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 664 AEQEASLQKLREELeSQQKAERASLEQKNRQM---LEQLKEEIEASEKSE-QAAL--NAAKEKALQQLREQLEgERKEAV 737
Cdd:PRK04863 833 ADPEAELRQLNRRR-VELERALADHESQEQQQrsqLEQAKEGLSALNRLLpRLNLlaDETLADRVEEIREQLD-EAEEAK 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 738 ATLEK--EHSAELERLCSSLEAKHREVvSSLQKKIQEAQQKEEAQLQKC--LGQVEHRVHQKSYHVA----GYEHELSSL 809
Cdd:PRK04863 911 RFVQQhgNALAQLEPIVSVLQSDPEQF-EQLKQDYQQAQQTQRDAKQQAfaLTEVVQRRAHFSYEDAaemlAKNSDLNEK 989
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 810 LREKRQEVEGEherrLDKMKEEHQQ----------VMAKAREQYEA-----EERKQRAELLG-HLTGELERLQRAHEREL 873
Cdd:PRK04863 990 LRQRLEQAEQE----RTRAREQLRQaqaqlaqynqVLASLKSSYDAkrqmlQELKQELQDLGvPADSGAEERARARRDEL 1065
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 578822059 874 etvrqeqHKRLEDLRRRHREQERKLQDLELDLETRAKDVKA 914
Cdd:PRK04863 1066 -------HARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRK 1099
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
810-1013 |
9.47e-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: 49.76 E-value: 9.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 810 LREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEER-KQRAELLGHLTGELERLQR---AHERELETVRQEQHKRLE 885
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiAALARRIRALEQELAALEAelaELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 886 DLRRRHREQERKLQDLELDLETRAKDVKA---RLALL----EVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQ 958
Cdd:COG4942 105 ELAELLRALYRLGRQPPLALLLSPEDFLDavrRLQYLkylaPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 578822059 959 KEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKK 1013
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
566-936 |
9.56e-06 |
|
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: 50.61 E-value: 9.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 566 LKAMEEAVAQ------VLEQDQRHLLESKQEKMQQLREKLCQ-----EEEEEILRLHQQKEQSLSSLRERLQKAIEEEEA 634
Cdd:pfam12128 310 LSAADAAVAKdrseleALEDQHGAFLDADIETAAADQEQLPSwqselENLEERLKALTGKHQDVTAKYNRRRSKIKEQNN 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 635 RMREEESQRLSWLR-------AQVQSSTQADEDQIRAEQEASLQKLREE-LESQQKAERASLEQKNRQMLEQLKEEIEAS 706
Cdd:pfam12128 390 RDIAGIKDKLAKIReardrqlAVAEDDLQALESELREQLEAGKLEFNEEeYRLKSRLGELKLRLNQATATPELLLQLENF 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 707 E------KSEQAALNAAKEkALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHreVVSSLQKKIQEAQQKEEAQ 780
Cdd:pfam12128 470 DerieraREEQEAANAEVE-RLQSELRQARKRRDQASEALRQASRRLEERQSALDELEL--QLFPQAGTLLHFLRKEAPD 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 781 LQKCLGQVE-----HRVHQKSYHVAGYEHELSSL----LREKRQEV------EGEHERRLDKMKEEHQQVMAKAREQYEA 845
Cdd:pfam12128 547 WEQSIGKVIspellHRTDLDPEVWDGSVGGELNLygvkLDLKRIDVpewaasEEELRERLDKAEEALQSAREKQAAAEEQ 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 846 eerkqraelLGHLTGELERLQRAHERELETV--------------RQEQHKRLEDLRRRHREQERKLQDLELDLETRAKD 911
Cdd:pfam12128 627 ---------LVQANGELEKASREETFARTALknarldlrrlfdekQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKK 697
|
410 420
....*....|....*....|....*
gi 578822059 912 VKARLALLEVQEETARREKQQLLDV 936
Cdd:pfam12128 698 HQAWLEEQKEQKREARTEKQAYWQV 722
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
661-777 |
9.59e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.21 E-value: 9.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 661 QIRAEQEA-SLQKLREELESQQKaeraSLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVAT 739
Cdd:PRK00409 529 ERELEQKAeEAEALLKEAEKLKE----ELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASV 604
|
90 100 110
....*....|....*....|....*....|....*...
gi 578822059 740 LEKEHSAELERLCSSLEAKHREvvsslqKKIQEAQQKE 777
Cdd:PRK00409 605 KAHELIEARKRLNKANEKKEKK------KKKQKEKQEE 636
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
660-786 |
1.12e-05 |
|
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: 48.14 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 660 DQIRAEQEASLQKLREELEsQQKAERASLEQKnrqmLEQLKEEIEASEKSEQAALNAAKE----KALQQlREQLEG--ER 733
Cdd:pfam04012 28 EQAIRDMQSELVKARQALA-QTIARQKQLERR----LEQQTEQAKKLEEKAQAALTKGNEelarEALAE-KKSLEKqaEA 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 578822059 734 KEAVATLEKEHSAELERLCSSLEAKHREVVSSLQK-KIQEAQQKEEAQLQKCLG 786
Cdd:pfam04012 102 LETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLlKARLKAAKAQEAVQTSLG 155
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
58-87 |
1.23e-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: 1.23e-05
10 20 30
....*....|....*....|....*....|
gi 578822059 58 LPGEWKPCQDITGDIYYFNFANGQSMWDHP 87
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
761-1177 |
1.29e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 761 EVVSSLQKKIQEAQQ--KEEAQLQKCLGQVEHRVHQKSYHVagyeHELSSLLREKRQEVEGEHER--RLDKMKEEhqqvM 836
Cdd:PRK03918 169 EVIKEIKRRIERLEKfiKRTENIEELIKEKEKELEEVLREI----NEISSELPELREELEKLEKEvkELEELKEE----I 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 837 AKAREQYEAEERKQRA--ELLGHLTGELERLqRAHERELETVRQE---------QHKRLEDLRRRHREQERKLQDLELDL 905
Cdd:PRK03918 241 EELEKELESLEGSKRKleEKIRELEERIEEL-KKEIEELEEKVKElkelkekaeEYIKLSEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 906 ETRAKDVKARLALLEVQEETARREKQQLLDVQRQV------ALKSEEATATHQQLEEAQKEHTHLlqSNQQLREILDELQ 979
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKELEKRLeeleerHELYEEAKAKKEELERLKKRLTGL--TPEKLEKELEELE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 980 ARKLKLESQVDLLQAQSQQLQKHFSSLEA------EAQKKQHLLREVTVEENNASPHFEPDLHIEDLRKSLgtnqtKEVS 1053
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKKaieelkKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKEL-----KEIE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1054 SSLSQSKEDLyldslsshnvwhllsaegvalRSAKEFLVQQTRSMRRRQTA--LKAAQQHWR-HELASAQEVAKDPPGIK 1130
Cdd:PRK03918 473 EKERKLRKEL---------------------RELEKVLKKESELIKLKELAeqLKELEEKLKkYNLEELEKKAEEYEKLK 531
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 578822059 1131 ----ALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSLWEE 1177
Cdd:PRK03918 532 ekliKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
654-944 |
1.33e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 49.57 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 654 STQADEDQI-RAEQEASLQKLREELESQQKAERASLEQKNRQMLEQL------KEEIEASEKSEQAA---------LNAA 717
Cdd:COG5185 310 ATESLEEQLaAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLeaikeeIENIVGEVELSKSSeeldsfkdtIEST 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 718 KEKALQQLREQlEGERKEAVATLE---KEHSAELERLCSSLEAKHREVvsslqkkiqEAQQKEEAQLQKCLGQVEHRVhq 794
Cdd:COG5185 390 KESLDEIPQNQ-RGYAQEILATLEdtlKAADRQIEELQRQIEQATSSN---------EEVSKLLNELISELNKVMREA-- 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 795 ksyhvagyEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREqyeaeerkqraellghLTGELERLQRAHERELE 874
Cdd:COG5185 458 --------DEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVST----------------LKATLEKLRAKLERQLE 513
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578822059 875 TVRQEQHKRLEDLRRRHREQErklQDLELDLETRAKDVKARLALLE--VQEETARREKQQLLDVQRQVALKS 944
Cdd:COG5185 514 GVRSKLDQVAESLKDFMRARG---YAHILALENLIPASELIQASNAktDGQAANLRTAVIDELTQYLSTIES 582
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
235-582 |
1.93e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 49.40 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 235 SQPEEKKDVSLDSDAAGPPTPCKPSSPGADSSLSSAvgkgRQGSGARPGLPEKEENEKSEPKicRNLVTPKADPTGSEPA 314
Cdd:PHA03307 45 SDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAP----ANESRSTPTWSLSTLAPASPAR--EGSPTPPGPSSPDPPP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 315 KASEKEAPEDTVDAGEEGSRREEAAKEPKKKASALEEGSSDASQEleiSEHMKEPQLSDSIASDPKSFHGL-----DFGF 389
Cdd:PHA03307 119 PTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVA---SDAASSRQAALPLSSPEETARAPssppaEPPP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 390 RSRISEHLLDVDVLSPVLGGACRQAQQPLGIEDKDDSQSSQDELQSKQSKGLEE--RLSPPLPHEERAQSPPRSLATEEE 467
Cdd:PHA03307 196 STPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWgpENECPLPRPAPITLPTRIWEASGW 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 468 PPQGPEGQPEWKEAEELGEDSAAS--------LSLQLSLQREQAPSPPAACEKGKEQHSQAEELG--PGQEEAEDPEEKV 537
Cdd:PHA03307 276 NGPSSRPGPASSSSSPRERSPSPSpsspgsgpAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAvsPGPSPSRSPSPSR 355
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 578822059 538 AVSPTPPVSPEVRSTEPVAPPEQLSEAALKAMEEAVAQVLEQDQR 582
Cdd:PHA03307 356 PPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARR 400
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
532-820 |
2.05e-05 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 49.08 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 532 DPEEKVAVSPTPPVSPEVRSTEPVAP--PEQLSEA----------ALKAMEEAVAQVLEQDQRHLLESK--QEKMQQLRE 597
Cdd:PLN03229 414 DPERKVNMKKREAVKTPVRELEGEVEklKEQILKAkessskpselALNEMIEKLKKEIDLEYTEAVIAMglQERLENLRE 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 598 KLCQEEEE----------EILRLHQQKEQSLS------SLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQADEDq 661
Cdd:PLN03229 494 EFSKANSQdqlmhpvlmeKIEKLKDEFNKRLSrapnylSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMD- 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 662 iRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASE----KSEQAALNAAKEKALQQLREQLEGERKEAV 737
Cdd:PLN03229 573 -RPEIKEKMEALKAEVASSGASSGDELDDDLKEKVEKMKKEIELELagvlKSMGLEVIGVTKKNKDTAEQTPPPNLQEKI 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 738 ATLEKEHSAELERLCSSLEAKHRevVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGyehelSSLLREKRQEV 817
Cdd:PLN03229 652 ESLNEEINKKIERVIRSSDLKSK--IELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEALN-----SSELKEKFEEL 724
|
...
gi 578822059 818 EGE 820
Cdd:PLN03229 725 EAE 727
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
649-780 |
2.81e-05 |
|
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: 47.92 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 649 AQVQSSTQADEDQIRAEQEAslQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQ 728
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQER--QKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAK 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 578822059 729 LEGERK-------EAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQ 780
Cdd:TIGR02794 128 QAAEAKakaeaeaERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAE 186
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
767-1019 |
2.94e-05 |
|
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: 48.58 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 767 QKKIQEAQQKEEAQLQKclgqvEHRVHQKSYHVAgYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKARE--QYE 844
Cdd:pfam17380 281 QKAVSERQQQEKFEKME-----QERLRQEKEEKA-REVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMEREREleRIR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 845 AEERKQRAELLGH--------LTGELERLQRAHERELETVRQE-----QHKRLEDLRRRHREQERKLQDleldlETRAKD 911
Cdd:pfam17380 355 QEERKRELERIRQeeiameisRMRELERLQMERQQKNERVRQEleaarKVKILEEERQRKIQQQKVEME-----QIRAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 912 VKARLALLEVQEETARREKQQLldvqRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELqaRKLKLESQVDL 991
Cdd:pfam17380 430 EEARQREVRRLEEERAREMERV----RLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQ--RRKILEKELEE 503
|
250 260
....*....|....*....|....*...
gi 578822059 992 LQAQSQQLQKHFSSLEAEAQKKQHLLRE 1019
Cdd:pfam17380 504 RKQAMIEEERKRKLLEKEMEERQKAIYE 531
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
644-1012 |
2.95e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.90 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 644 LSWLRAQ-VQSSTQADEDQIRAE-QEASLQKlreeleSQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAakEKA 721
Cdd:PRK10929 9 MAWLLSWgAYAATAPDEKQITQElEQAKAAK------TPAQAEIVEALQSALNWLEERKGSLERAKQYQQVIDNF--PKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 722 LQQLREQLEGERKE--------AVATLEKE------HSAELERLCSSLEAKHREVVSSLQkkiQEAQQKEEAqlQKCLGQ 787
Cdd:PRK10929 81 SAELRQQLNNERDEprsvppnmSTDALEQEilqvssQLLEKSRQAQQEQDRAREISDSLS---QLPQQQTEA--RRQLNE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 788 VEHRVH-------------------QKSYHVAGY-EHELSSLLREKRQEVEgehERRLDKMKEEHQQVMAK--------- 838
Cdd:PRK10929 156 IERRLQtlgtpntplaqaqltalqaESAALKALVdELELAQLSANNRQELA---RLRSELAKKRSQQLDAYlqalrnqln 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 839 AREQYEAEERKQRAELLGHLTGEL-----ERLQRahERELETVRQEQHKRLEDLRRRHReqerklqdleldlETRAKDVK 913
Cdd:PRK10929 233 SQRQREAERALESTELLAEQSGDLpksivAQFKI--NRELSQALNQQAQRMDLIASQQR-------------QAASQTLQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 914 ARLALlevqeeTARREKQQLLDVQRQV--ALKSEEAtathqQLEEAQKEhthllqsnQQLREILDELQARKLKLESQVDL 991
Cdd:PRK10929 298 VRQAL------NTLREQSQWLGVSNALgeALRAQVA-----RLPEMPKP--------QQLDTEMAQLRVQRLRYEDLLNK 358
|
410 420
....*....|....*....|.
gi 578822059 992 LQAQSQQLQKHFSSLEAEAQK 1012
Cdd:PRK10929 359 QPQLRQIRQADGQPLTAEQNR 379
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
847-1127 |
3.02e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 847 ERKQRAELLGHLTGELERLQRAHErELETVRqEQHKRLEDLRRRHREQERKLQDLEL--DLETRAKDVKA--RLALLEVQ 922
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHE-ALEDAR-EQIELLEPIRELAERYAAARERLAEleYLRAALRLWFAqrRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 923 EETARREKQQLldvQRQVALKSEEATATHQQLEEAQKEHthLLQSNQQLREILDELQARKLKLESQvdllqaqsqqlqkh 1002
Cdd:COG4913 297 LEELRAELARL---EAELERLEARLDALREELDELEAQI--RGNGGDRLEQLEREIERLERELEER-------------- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1003 fsslEAEAQKKQHLLREVtveennaspHFEPDLHIEDLRKSLgtNQTKEVSSSLSQSKEDLyldslssHNVWHLLSAEGV 1082
Cdd:COG4913 358 ----ERRRARLEALLAAL---------GLPLPASAEEFAALR--AEAAALLEALEEELEAL-------EEALAEAEAALR 415
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 578822059 1083 ALRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELASAQEVAKDPP 1127
Cdd:COG4913 416 DLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAEL 460
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
57-87 |
3.04e-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: 3.04e-05
10 20 30
....*....|....*....|....*....|.
gi 578822059 57 PLPGEWKPCQDITGDIYYFNFANGQSMWDHP 87
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKP 31
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
559-974 |
4.01e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.98 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 559 EQLSEAALKAMEEAVAQVLEQD-----QRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEE 633
Cdd:COG5278 113 EALIDQWLAELEQVIALRRAGGleaalALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 634 ARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAA 713
Cdd:COG5278 193 LLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 714 LNAAKEKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKclgQVEHRVH 793
Cdd:COG5278 273 LLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAA---ALALLAA 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 794 QKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHEREL 873
Cdd:COG5278 350 LLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALA 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 874 ETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQ 953
Cdd:COG5278 430 EALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALL 509
|
410 420
....*....|....*....|.
gi 578822059 954 LEEAQKEHTHLLQSNQQLREI 974
Cdd:COG5278 510 LAAAEAALAAALAAALASAEL 530
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
648-783 |
4.55e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.49 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 648 RAQVQSSTQADEDQIR--AEQEASLQKLREELESQQKAERAslEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKAlqql 725
Cdd:PRK09510 80 QRKKKEQQQAEELQQKqaAEQERLKQLEKERLAAQEQKKQA--EEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEA---- 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 578822059 726 rEQLEGERKEAVATLEKEHSAELERLCSSlEAKHREVVSSLQKKIQEAQQKEEAQLQK 783
Cdd:PRK09510 154 -KRAAAAAKKAAAEAKKKAEAEAAKKAAA-EAKKKAEAEAAAKAAAEAKKKAEAEAKK 209
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
810-981 |
4.77e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 810 LREKRQEVEGEH---ERRLDKMKEEHQQvMAKAREQYEAEERKQRAEL--------LGHLTGELERLQRAHE--RELETV 876
Cdd:COG4913 615 LEAELAELEEELaeaEERLEALEAELDA-LQERREALQRLAEYSWDEIdvasaereIAELEAELERLDASSDdlAALEEQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 877 RQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEE 956
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE 773
|
170 180
....*....|....*....|....*.
gi 578822059 957 AQ-KEHTHLLQSNQQLREILDELQAR 981
Cdd:COG4913 774 RIdALRARLNRAEEELERAMRAFNRE 799
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
660-853 |
5.14e-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: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 660 DQIRAEQEASLQ--KLREELESQQKAERASLEQK----NRQMLEQLKEEIEASEKSEQAALNAAKEKAL----QQLREQL 729
Cdd:NF012221 1532 DNVVATSESSQQadAVSKHAKQDDAAQNALADKEraeaDRQRLEQEKQQQLAAISGSQSQLESTDQNALetngQAQRDAI 1611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 730 EGERKEAVATLEK------------EHSAEL---------ERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQkclgQV 788
Cdd:NF012221 1612 LEESRAVTKELTTlaqgldaldsqaTYAGESgdqwrnpfaGGLLDRVQEQLDDAKKISGKQLADAKQRHVDNQQ----KV 1687
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578822059 789 EHRVHQKSYHVA-GYEHELSSLLREKRQEVEGEhERRLDKMKEEHQQVMAKAREQYEAEERKQRAE 853
Cdd:NF012221 1688 KDAVAKSEAGVAqGEQNQANAEQDIDDAKADAE-KRKDDALAKQNEAQQAESDANAAANDAQSRGE 1752
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
563-824 |
5.16e-05 |
|
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: 47.81 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 563 EAALKAMEEAVAQVLEQD-QRHLLESKQEKMQQLREKLCQEEEEEIL---RLHQQKEQSLSSLRERL-----QKAIEEEE 633
Cdd:pfam17380 332 QAAIYAEQERMAMERERElERIRQEERKRELERIRQEEIAMEISRMReleRLQMERQQKNERVRQELeaarkVKILEEER 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 634 ARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLR-EELESQQKAE--RASLEQKNRQMLEQLKEEIEASEKSE 710
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRlEEQERQQQVErlRQQEEERKRKKLELEKEKRDRKRAEE 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 711 QAALNAAKEKALQQlREQLEGERKEAVatLEKEhsaelerlcssLEAKHREVVSSLQKKIQEAQQKEEAQLQKclgqvEH 790
Cdd:pfam17380 492 QRRKILEKELEERK-QAMIEEERKRKL--LEKE-----------MEERQKAIYEEERRREAEEERRKQQEMEE-----RR 552
|
250 260 270
....*....|....*....|....*....|....*..
gi 578822059 791 RVHQKSYHVAGYEHELSSLLREK---RQEVEGEHERR 824
Cdd:pfam17380 553 RIQEQMRKATEERSRLEAMERERemmRQIVESEKARA 589
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
577-989 |
5.16e-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: 47.71 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 577 LEQDQRHLLESKQEKMQQLREKlcqeeeEEILRLHQQKEQSLSSLRERLQKAIEEEEARMREEeSQRLSWLRAQVQSSTQ 656
Cdd:TIGR04523 223 LKKQNNQLKDNIEKKQQEINEK------TTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN-NKKIKELEKQLNQLKS 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 657 ADEDQIRAEQEASLQKLREELESQQKAERASLEQ--KNRQMLEQLKEEIEASEKSEQAalnaaKEKALQQLREQLEgERK 734
Cdd:TIGR04523 296 EISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQisQNNKIISQLNEQISQLKKELTN-----SESENSEKQRELE-EKQ 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 735 EAVATLEKEHSAELERLcSSLEAKHREVVSSLQKKIQEAQQKEE--AQLQKCLGQVEHRVHQKSYHVAGYEHELSSLlRE 812
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEI-KNLESQINDLESKIQNQEKLNQQKDEqiKKLQQEKELLEKEIERLKETIIKNNSEIKDL-TN 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 813 KRQEVEGEHERrLDKMKEEHQQVMAKAREQYEAEER--KQRAELLGHLTGELERLQRaHERELE------TVRQEQHK-R 883
Cdd:TIGR04523 448 QDSVKELIIKN-LDNTRESLETQLKVLSRSINKIKQnlEQKQKELKSKEKELKKLNE-EKKELEekvkdlTKKISSLKeK 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 884 LEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQE---------------ETARREKQQLL--------DVQRQV 940
Cdd:TIGR04523 526 IEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEknkeieelkqtqkslKKKQEEKQELIdqkekekkDLIKEI 605
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 578822059 941 ALKSEEATATHQQLEEAQKEhthllqsNQQLREILDELQARKLKLESQV 989
Cdd:TIGR04523 606 EEKEKKISSLEKELEKAKKE-------NEKLSSIIKNIKSKKNKLKQEV 647
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
695-946 |
6.31e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 46.95 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 695 MLEQLKEEIEASEKSEQAALNAAKEK-ALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEA 773
Cdd:pfam15558 13 MLARHKEEQRMRELQQQAALAWEELRrRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 774 QQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSLLREKrqevegehERRLDKMKEEHQQVMAKAREQyeAEERKQRAE 853
Cdd:pfam15558 93 ESRWREQAEDQENQRQEKLERARQEAEQRKQCQEQRLKEK--------EEELQALREQNSLQLQERLEE--ACHKRQLKE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 854 LLGHLTGELERLQraherelETVRQEQHKRLEDLRRRHREQERKLqDLELDLeTRAKDVKARLALLEVQE--ETARREKQ 931
Cdd:pfam15558 163 REEQKKVQENNLS-------ELLNHQARKVLVDCQAKAEELLRRL-SLEQSL-QRSQENYEQLVEERHRElrEKAQKEEE 233
|
250
....*....|....*
gi 578822059 932 QLLDVQRQVALKSEE 946
Cdd:pfam15558 234 QFQRAKWRAEEKEEE 248
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
564-776 |
9.54e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 46.61 E-value: 9.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 564 AALKAMEEAVAQVLEQdqrhlLESKQEKMQQLrEKLCQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMRE----- 638
Cdd:PRK11637 75 AQLKKQEEAISQASRK-----LRETQNTLNQL-NKQIDELNASIAKLEQQQAAQERLLAAQLDAAFRQGEHTGLQlilsg 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 639 EESQRLSWLRAQVQSSTQADEDQIraeqeASLQKLREELeSQQKAErasLEQKNRQMLEQLKEEIEASEKSEQA------ 712
Cdd:PRK11637 149 EESQRGERILAYFGYLNQARQETI-----AELKQTREEL-AAQKAE---LEEKQSQQKTLLYEQQAQQQKLEQArnerkk 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578822059 713 ---ALNAAKEKALQQLRE--QLEGERKEAVATLEKEHSAELERlcsslEAKHREVVsslQKKIQEAQQK 776
Cdd:PRK11637 220 tltGLESSLQKDQQQLSElrANESRLRDSIARAEREAKARAER-----EAREAARV---RDKQKQAKRK 280
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
581-1021 |
1.05e-04 |
|
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: 47.09 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 581 QRHLLESKQEKMQQLREKLCQEEEE--EILRLHQQKEQSLSSLRERLQKAIE--------------------------EE 632
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESElkELEKKHQQLCEEKNALQEQLQAETElcaeaeemrarlaarkqeleeilhelES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 633 EARMREEESQRLSWLRAQVQSSTQADEDQIrAEQEASLQKLREE---LESQQKAERASL----EQKNRQMLEQLKEEIEA 705
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQL-DEEEAARQKLQLEkvtTEAKIKKLEEDIllleDQNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 706 SEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKEHSA--ELERLCSSLEAKH---REVVSSLQKKIQEAQ---QKE 777
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGrqELEKAKRKLEGEStdlQEQIAELQAQIAELRaqlAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 778 EAQLQKCLGQVEHRVHQKSyHVAGYEHELSSLLREKRQEVEGEHERR-------------LDKMKEEHQQVMAKAREQYE 844
Cdd:pfam01576 242 EEELQAALARLEEETAQKN-NALKKIRELEAQISELQEDLESERAARnkaekqrrdlgeeLEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 845 AeeRKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLEldletrakdvKARLALlevqeE 924
Cdd:pfam01576 321 L--RSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLE----------KAKQAL-----E 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 925 TARREKQQLLDVQRQVALKSEEA-TATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHF 1003
Cdd:pfam01576 384 SENAELQAELRTLQQAKQDSEHKrKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDV 463
|
490
....*....|....*...
gi 578822059 1004 SSLEAEAQKKQHLLREVT 1021
Cdd:pfam01576 464 SSLESQLQDTQELLQEET 481
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
722-1099 |
1.08e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.02 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 722 LQQLREQLEGERKEAVATLEKEHSAELERLCS--------------SLEAKHREVVSSLQ--KKIQEAQQKEEAQLQ--- 782
Cdd:pfam05483 50 LEQVANSGDCHYQEGLKDSDFENSEGLSRLYSklykeaekikkwkvSIEAELKQKENKLQenRKIIEAQRKAIQELQfen 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 783 -KCLGQVEHRVHQKSYHVA--GYEHELSSLLRE---------KRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQ 850
Cdd:pfam05483 130 eKVSLKLEEEIQENKDLIKenNATRHLCNLLKEtcarsaektKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 851 RAELLGHLTGELERLQRAhERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARR-- 928
Cdd:pfam05483 210 RLEMHFKLKEDHEKIQHL-EEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKEli 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 929 EKQQLL---------DVQRQVALKS--EE----ATATHQQL---EEAQKEHTHLLQSNQQLreILDELQARKLKLESQVD 990
Cdd:pfam05483 289 EKKDHLtkeledikmSLQRSMSTQKalEEdlqiATKTICQLteeKEAQMEELNKAKAAHSF--VVTEFEATTCSLEELLR 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 991 LLQAQSQQLQKHFSSLEAEAQKKQHLLREVTVEENNAsphfepDLHIEDLRKSLGTNQT--------KEVSSSLSQSKED 1062
Cdd:pfam05483 367 TEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNK------EVELEELKKILAEDEKlldekkqfEKIAEELKGKEQE 440
|
410 420 430
....*....|....*....|....*....|....*..
gi 578822059 1063 LYLDSLSSHNVWHLLSAEGVALRSAKEFLVQQTRSMR 1099
Cdd:pfam05483 441 LIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLK 477
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
665-898 |
1.08e-04 |
|
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: 45.04 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 665 EQEASLQKLREelesQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAAlnaakeKALQQLREQLEGERKEAVATLEK-E 743
Cdd:pfam15665 11 EHEAEIQALKE----AHEEEIQQILAETREKILQYKSKIGEELDLKRRI------QTLEESLEQHERMKRQALTEFEQyK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 744 HSAELERLCssLEAKHREVVSSLQKKIQEAQQKEEAQLQKclgqvehrvhqksyhvagyehelsslLREKRQEVEGEHER 823
Cdd:pfam15665 81 RRVEERELK--AEAEHRQRVVELSREVEEAKRAFEEKLES--------------------------FEQLQAQFEQEKRK 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578822059 824 RLDKMKEEHQQVMAKAREQYEAEERKqraellghLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKL 898
Cdd:pfam15665 133 ALEELRAKHRQEIQELLTTQRAQSAS--------SLAEQEKLEELHKAELESLRKEVEDLRKEKKKLAEEYEQKL 199
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
736-981 |
1.24e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 736 AVATLEKEHSAELERLCSSLEAKhrevvsslqKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSLlrEKRQ 815
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAEL---------EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL--EAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 816 EVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAheRELETVRQEQHKRLEDLRRrhreqe 895
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRL--QYLKYLAPARREQAEELRA------ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 896 rKLQDLElDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEeatathQQLEEAQKEHTHLLQSNQQLREIL 975
Cdd:COG4942 158 -DLAELA-ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE------KELAELAAELAELQQEAEELEALI 229
|
....*.
gi 578822059 976 DELQAR 981
Cdd:COG4942 230 ARLEAE 235
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
833-962 |
1.55e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.36 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 833 QQVMAKAREQYEAEERK-----QRAEllghltgELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLEt 907
Cdd:PRK00409 501 ENIIEEAKKLIGEDKEKlneliASLE-------ELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAE- 572
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 578822059 908 rakdVKARLALLEVQEETARREKQ-QLLDVQRQVALKSEEATATHQQLEEAQKEHT 962
Cdd:PRK00409 573 ----KEAQQAIKEAKKEADEIIKElRQLQKGGYASVKAHELIEARKRLNKANEKKE 624
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
676-973 |
1.92e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.87 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 676 ELESQQKAERASLEQKNRQMlEQLKEEIEASEKSEQAALNAAKE---------KALQQLREQLEGERKEA---------- 736
Cdd:pfam05483 272 QLEEKTKLQDENLKELIEKK-DHLTKELEDIKMSLQRSMSTQKAleedlqiatKTICQLTEEKEAQMEELnkakaahsfv 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 737 -------VATLEKEHSAELERLCSSlEAKHREVVSSLQKKIQEAQQK---------EEAQLQKCLGQVEHRVHQK----- 795
Cdd:pfam05483 351 vtefeatTCSLEELLRTEQQRLEKN-EDQLKIITMELQKKSSELEEMtkfknnkevELEELKKILAEDEKLLDEKkqfek 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 796 -SYHVAGYEHELSSLLREKRQEVEG-EHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGH----LTGELERLQRAH 869
Cdd:pfam05483 430 iAEELKGKEQELIFLLQAREKEIHDlEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHcdklLLENKELTQEAS 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 870 ERELETVRQEQH------------KRLEDLRRRHREQERKLQDLELDLETRAKDVKARLallEVQEETARREKQQLLDVQ 937
Cdd:pfam05483 510 DMTLELKKHQEDiinckkqeermlKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKL---DKSEENARSIEYEVLKKE 586
|
330 340 350
....*....|....*....|....*....|....*.
gi 578822059 938 RQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLRE 973
Cdd:pfam05483 587 KQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
642-981 |
1.96e-04 |
|
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: 45.66 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 642 QRLSWLRAQVQSSTQADEDQIRAEQEA-SLQKLREELESQ---QKAERASLEQKNRQMLEQLKEEIEASE--KSEQAALN 715
Cdd:pfam07888 42 ERAELLQAQEAANRQREKEKERYKRDReQWERQRRELESRvaeLKEELRQSREKHEELEEKYKELSASSEelSEEKDALL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 716 AAKEKALQQLREQLEGERKEAVATLEKEhsAELERLCSSLEAKHREVV------SSLQKKIQEAQQkEEAQLQKCLGQVE 789
Cdd:pfam07888 122 AQRAAHEARIRELEEDIKTLTQRVLERE--TELERMKERAKKAGAQRKeeeaerKQLQAKLQQTEE-ELRSLSKEFQELR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 790 HRVHQKSYHVAGYEHELSSLlrekrQEVEGEHERRLDKMKEEHQQvMAKAREQYEAEERKqrAELLGHLTGELERLQRAH 869
Cdd:pfam07888 199 NSLAQRDTQVLQLQDTITTL-----TQKLTTAHRKEAENEALLEE-LRSLQERLNASERK--VEGLGEELSSMAAQRDRT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 870 ERELETVRQEQHK---RLEDLRRRHRE------QERK--LQDLELDLETRAKDVKARLALLE-VQEETARREKQQL---- 933
Cdd:pfam07888 271 QAELHQARLQAAQltlQLADASLALREgrarwaQEREtlQQSAEADKDRIEKLSAELQRLEErLQEERMEREKLEVelgr 350
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 578822059 934 -LDVQR-QVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQAR 981
Cdd:pfam07888 351 eKDCNRvQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQR 400
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
656-728 |
2.45e-04 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 42.85 E-value: 2.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578822059 656 QADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQ 728
Cdd:COG0711 47 KEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAE 119
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
835-988 |
2.55e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 835 VMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRqeqhKRLEDLRRRHREQERKLQDLELDLET---RAKD 911
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALE----ARLEAAKTELEDLEKEIKRLELEIEEveaRIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 912 VKARLAL---------LEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEH-THLLQSNQQLREILDELQAR 981
Cdd:COG1579 78 YEEQLGNvrnnkeyeaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELeAELEEKKAELDEELAELEAE 157
|
....*..
gi 578822059 982 KLKLESQ 988
Cdd:COG1579 158 LEELEAE 164
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
811-983 |
2.59e-04 |
|
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: 44.91 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 811 REKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRR 890
Cdd:pfam13868 31 KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 891 HREQERKLQDLELD----LETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHT---- 962
Cdd:pfam13868 111 QEEDQAEAEEKLEKqrqlREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIarlr 190
|
170 180
....*....|....*....|.
gi 578822059 963 HLLQSNQQLREILDELQARKL 983
Cdd:pfam13868 191 AQQEKAQDEKAERDELRAKLY 211
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
662-889 |
2.98e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 662 IRAEQEASLQKLREELESQQkaerASLEQKNRQMLEQLKEEIEASEksEQAALNAAKEKALQQLREQLEGERKEavatlE 741
Cdd:COG4717 43 IRAMLLERLEKEADELFKPQ----GRKPELNLKELKELEEELKEAE--EKEEEYAELQEELEELEEELEELEAE-----L 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 742 KEHSAELERLcssleakhrEVVSSLQKKIQEAQQKEE--AQLQKCLGQVEHRVHQksyhVAGYEHELSSlLREKRQEVEG 819
Cdd:COG4717 112 EELREELEKL---------EKLLQLLPLYQELEALEAelAELPERLEELEERLEE----LRELEEELEE-LEAELAELQE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578822059 820 EHERRLDKMKEEHQQVMAKAREQYEA--EERKQRAELLGHLTGELERLQRAHER-ELETVRQEQHKRLEDLRR 889
Cdd:COG4717 178 ELEELLEQLSLATEEELQDLAEELEElqQRLAELEEELEEAQEELEELEEELEQlENELEAAALEERLKEARL 250
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
572-1007 |
3.01e-04 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 45.34 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 572 AVAQVLEQDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLRAQV 651
Cdd:COG4995 12 ALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALALALLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 652 QSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAkEKALQQLREQLEG 731
Cdd:COG4995 92 AALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAA-AAAAAAALLALAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 732 ERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSLLR 811
Cdd:COG4995 171 ALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAAAAL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 812 EKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRH 891
Cdd:COG4995 251 AAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLLAAL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 892 REQERKLQDLELDLETRAkdvkARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQL 971
Cdd:COG4995 331 ALLALLLLLAAAALLAAA----LAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAA 406
|
410 420 430
....*....|....*....|....*....|....*.
gi 578822059 972 REILDELQARKLKLESQVDLLQAQSQQLQKHFSSLE 1007
Cdd:COG4995 407 QLLRLLLAALALLLALAAYAAARLALLALIEYIILP 442
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
650-982 |
3.27e-04 |
|
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: 45.23 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 650 QVQSSTQADEDQIRAEQEASLQKLREELESqqkaeraslEQKNRQMLEQLKEEIEASEKsEQAALNAAKEKALQQLREQL 729
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELDELLES---------EEKNREEVEELKDKYRELRK-TLLANRFSYGPAIDELEKQL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 730 EgerkeavaTLEKEHSaELERLCSS---LEAkhREVVSSLQKKIQEAQQKEE------AQLQKCL-GQVEhrvhqksyhv 799
Cdd:pfam06160 156 A--------EIEEEFS-QFEELTESgdyLEA--REVLEKLEEETDALEELMEdipplyEELKTELpDQLE---------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 800 agyehELSSLLRE-KRQEVEGEH---ERRLDKMKEEHQQVMAkareQYEAEERKQRAELLGHLTGELERLQRAHERELET 875
Cdd:pfam06160 215 -----ELKEGYREmEEEGYALEHlnvDKEIQQLEEQLEENLA----LLENLELDEAEEALEEIEERIDQLYDLLEKEVDA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 876 vRQEQHKRLEDLRRRHREQERKLQDLELDLETrakdVKARLALLEVQEETARREKQQLLDVQRQVAL---KSEEATATH- 951
Cdd:pfam06160 286 -KKYVEKNLPEIEDYLEHAEEQNKELKEELER----VQQSYTLNENELERVRGLEKQLEELEKRYDEiveRLEEKEVAYs 360
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 578822059 952 ----------QQLEEAQKEHTHLLQSNQQLREilDELQARK 982
Cdd:pfam06160 361 elqeeleeilEQLEEIEEEQEEFKESLQSLRK--DELEARE 399
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
659-931 |
4.69e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 44.75 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 659 EDQIRAEQEASLQKLREELESQQKAERASLEQKN-------RQMLEQLKEEIEASEKSEQAALNAAK-----EKALQQLR 726
Cdd:pfam09731 181 TDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLdaapetpPKLPEHLDNVEEKVEKAQSLAKLVDQykelvASERIVFQ 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 727 EQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVvSSLQKKIQEAQQKEEAQLQKCLGQVEHrvhqksyhvagyehEL 806
Cdd:pfam09731 261 QELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREI-DQLSKKLAELKKREEKHIERALEKQKE--------------EL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 807 SSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEerkqraellghLTGELERLQRAHERELETVRQEQHkrlED 886
Cdd:pfam09731 326 DKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEK-----------LRTELERQAEAHEEHLKDVLVEQE---IE 391
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 578822059 887 LRRRHR-------EQERKLQDLELD-LETRAKDVKARLALLEVQEETARREKQ 931
Cdd:pfam09731 392 LQREFLqdikekvEEERAGRLLKLNeLLANLKGLEKATSSHSEVEDENRKAQQ 444
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
677-958 |
4.74e-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: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 677 LESQQKAERASLEQKNRQMLEQLKEeieASEKSEQAalnaakEKALQQLREQlegerkEAVATLEKEHSAELERLcSSLE 756
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPE---LRKELEEA------EAALEEFRQK------NGLVDLSEEAKLLLQQL-SELE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 757 AKHREvvssLQKKIQEAQQKEEaQLQKCLGQVEHRVHQKSyhvagyEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVM 836
Cdd:COG3206 226 SQLAE----ARAELAEAEARLA-ALRAQLGSGPDALPELL------QSPVIQQLRAQLAELEAELAELSARYTPNHPDVI 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 837 AKareqyeaeeRKQRAELLGHLTGELERLQRAHERELETVRQeqhkRLEDLRRRHREQERKLQDLeldletrakdvkarl 916
Cdd:COG3206 295 AL---------RAQIAALRAQLQQEAQRILASLEAELEALQA----REASLQAQLAQLEARLAEL--------------- 346
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 578822059 917 allevqeetaRREKQQLLDVQRQVALKSEEATATHQQLEEAQ 958
Cdd:COG3206 347 ----------PELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
653-853 |
5.27e-04 |
|
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: 44.56 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 653 SSTQADEDQIRAEQeASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGE 732
Cdd:pfam15709 329 EQEKASRDRLRAER-AEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 733 RKEAVatlekEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKclgqvehrvhqksyhvagYEHELSSLLRE 812
Cdd:pfam15709 408 RKQRL-----QLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQR------------------QKELEMQLAEE 464
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 578822059 813 KRQEVEGEHERRLDKMKEEHQqvmAKAREQYEAEERKQRAE 853
Cdd:pfam15709 465 QKRLMEMAEEERLEYQRQKQE---AEEKARLEAEERRQKEE 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
559-878 |
5.98e-04 |
|
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: 44.66 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 559 EQLSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKAieEEEARMRE 638
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA--EEELAEAE 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 639 EESQRLSWLRAQVQSSTQADEDQIRAEQEA------SLQKLREELESQQKAERAS------LEQKNRQMLEQLkEEIEAS 706
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALREALDELRAEltllneEAANLRERLESLERRIAATerrledLEEQIEELSEDI-ESLAAE 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 707 EKSEQAALNAAKE--KALQQLREQLEGERKEAVATLEK------EHSAELERLCSSLEAKhREVVSSLQKKIQEAQQKEE 778
Cdd:TIGR02168 861 IEELEELIEELESelEALLNERASLEEALALLRSELEElseelrELESKRSELRRELEEL-REKLAQLELRLEGLEVRID 939
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 779 AQLQKC--LGQVEHRVHQKSYhvagyehelssllrEKRQEVEGEHERRLDKMKEEHQQ---VMAKAREQYEAEErkqraE 853
Cdd:TIGR02168 940 NLQERLseEYSLTLEEAEALE--------------NKIEDDEEEARRRLKRLENKIKElgpVNLAAIEEYEELK-----E 1000
|
330 340
....*....|....*....|....*
gi 578822059 854 LLGHLTGELERLQRAHERELETVRQ 878
Cdd:TIGR02168 1001 RYDFLTAQKEDLTEAKETLEEAIEE 1025
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
642-1012 |
6.68e-04 |
|
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: 44.34 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 642 QRLSWLRAQVQSSTQADEDQiraeQEASLQKLREELE--SQQKAERASLEQKNRQMLEQL---KEEIEASEK--SEQAAL 714
Cdd:pfam15921 429 QRLEALLKAMKSECQGQMER----QMAAIQGKNESLEkvSSLTAQLESTKEMLRKVVEELtakKMTLESSERtvSDLTAS 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 715 NAAKEKALQQLREQLEGERKEAVATL--------EKEHSAELERLCSSLE---AKHREVVSSLQKKIQE----------- 772
Cdd:pfam15921 505 LQEKERAIEATNAEITKLRSRVDLKLqelqhlknEGDHLRNVQTECEALKlqmAEKDKVIEILRQQIENmtqlvgqhgrt 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 773 --AQQKEEAQLQKCLGqvEHRVHQKSYHVagyehelsslLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEA--EER 848
Cdd:pfam15921 585 agAMQVEKAQLEKEIN--DRRLELQEFKI----------LKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAvkDIK 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 849 KQRAELLGHLtgelerlqRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARR 928
Cdd:pfam15921 653 QERDQLLNEV--------KTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGH 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 929 EKQQLLDVQRQVALKSEEATATH---QQLEE----AQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQK 1001
Cdd:pfam15921 725 AMKVAMGMQKQITAKRGQIDALQskiQFLEEamtnANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKE 804
|
410
....*....|.
gi 578822059 1002 HFSSLEAEAQK 1012
Cdd:pfam15921 805 KVANMEVALDK 815
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
612-1169 |
7.67e-04 |
|
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: 44.01 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 612 QQKEQSLSSLRERLQKAieeeearmrEEESQRLSWLRAQVQSSTQADEDQIRAEQeaslqklreELESQQKAERASLEQK 691
Cdd:pfam01576 8 QAKEEELQKVKERQQKA---------ESELKELEKKHQQLCEEKNALQEQLQAET---------ELCAEAEEMRARLAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 692 nRQMLEQLKEEIEA--SEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKEHsaeLERLcsSLEAKhrevvsslQKK 769
Cdd:pfam01576 70 -KQELEEILHELESrlEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQ---LEKV--TTEAK--------IKK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 770 IQEAQQKEEAQ---LQKCLGQVEHRVHQKSYHVAGYEHELSSL--LREKRQEVEGEHERRLDKmKEEHQQVMAKAREQYE 844
Cdd:pfam01576 136 LEEDILLLEDQnskLSKERKLLEERISEFTSNLAEEEEKAKSLskLKNKHEAMISDLEERLKK-EEKGRQELEKAKRKLE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 845 AEE----------RKQRAELLGHLTGELERLQRAHEReletVRQEQHKRLEDLrRRHREQERKLQDLELDLET----RAK 910
Cdd:pfam01576 215 GEStdlqeqiaelQAQIAELRAQLAKKEEELQAALAR----LEEETAQKNNAL-KKIRELEAQISELQEDLESeraaRNK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 911 DVKARLALLE-----------------VQEETARREKQQLLDVQRQValkSEEATATHQQLEEAQKEHThllQSNQQLRE 973
Cdd:pfam01576 290 AEKQRRDLGEelealkteledtldttaAQQELRSKREQEVTELKKAL---EEETRSHEAQLQEMRQKHT---QALEELTE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 974 ILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLR--EVTVEENNASpHFEPDLHIEDLRKSLGTNQTK- 1050
Cdd:pfam01576 364 QLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKklEGQLQELQAR-LSESERQRAELAEKLSKLQSEl 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1051 -EVSSSLSQSKEDLY-----LDSLSSHnvwhllsaegvaLRSAKEFLVQQTR-----SMRRRQTALKAA--QQHWRHELA 1117
Cdd:pfam01576 443 eSVSSLLNEAEGKNIklskdVSSLESQ------------LQDTQELLQEETRqklnlSTRLRQLEDERNslQEQLEEEEE 510
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 578822059 1118 SAQEVAKDPPGIKA-LEDMRKNLEKETRHLDEMKSAMRKghnlLKKKEEKLNQ 1169
Cdd:pfam01576 511 AKRNVERQLSTLQAqLSDMKKKLEEDAGTLEALEEGKKR----LQRELEALTQ 559
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
806-949 |
8.48e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.71 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 806 LSSLLREKRQEV-EGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRaellghltgELERLQRAH-ERELETVRQEQHKR 883
Cdd:COG2268 186 LDALGRRKIAEIiRDARIAEAEAERETEIAIAQANREAEEAELEQER---------EIETARIAEaEAELAKKKAEERRE 256
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578822059 884 LEDLRRR-----HREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLL--DVQRQVALKSEEATA 949
Cdd:COG2268 257 AETARAEaeaayEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKpaEAEKQAAEAEAEAEA 329
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
660-779 |
8.84e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.50 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 660 DQIRAEQEASLQKLREELeSQQKAERASLEQKnrqmLEQLKEEIEASEKSEQAALNAAKE----KALQQlREQLEGERKE 735
Cdd:COG1842 29 DQAIRDMEEDLVEARQAL-AQVIANQKRLERQ----LEELEAEAEKWEEKARLALEKGREdlarEALER-KAELEAQAEA 102
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 578822059 736 AVATLEkEHSAELERLcssleakhREVVSSLQKKIQEAQQKEEA 779
Cdd:COG1842 103 LEAQLA-QLEEQVEKL--------KEALRQLESKLEELKAKKDT 137
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
663-1059 |
9.03e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 43.74 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 663 RAEQEASLQKLREEL--ESQQKAERASLEQKNRQMLEQLKEEIEAS-EKSEQAALNAAKEKALQQLREQLEGERKEAVAT 739
Cdd:COG5278 85 RAEIDELLAELRSLTadNPEQQARLDELEALIDQWLAELEQVIALRrAGGLEAALALVRSGEGKALMDEIRARLLLLALA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 740 LEKEHSAELERLcsSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEG 819
Cdd:COG5278 165 LAALLLAAAALL--LLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALAL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 820 EHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQ 899
Cdd:COG5278 243 ALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 900 DLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQ 979
Cdd:COG5278 323 AALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAA 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 980 ARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLREVTVEENNASPHFEPDLHIEDLRKSLGTNQTKEVSSSLSQS 1059
Cdd:COG5278 403 AAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAA 482
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
580-1019 |
1.11e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 580 DQRHLLESKQEKMQQLREklcqeeeeeiLRLHQQKEQSLSSLRERLQKaieeeearmreeesqrlswlRAQVQSSTQADE 659
Cdd:PRK04863 507 EQRHLAEQLQQLRMRLSE----------LEQRLRQQQRAERLLAEFCK--------------------RLGKNLDDEDEL 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 660 DQIRAEQEASLQKLREELESQqkAERASLEqknRQMLEQLKEEIEASEKSEQAALNAakEKALQQLREQLEGERKEAVA- 738
Cdd:PRK04863 557 EQLQEELEARLESLSESVSEA--RERRMAL---RQQLEQLQARIQRLAARAPAWLAA--QDALARLREQSGEEFEDSQDv 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 739 ------TLEKEHSAELERlcSSLEAKHRevvsSLQKKIQEAQQKEEAQLQKCLGQVEH-------------RVHQKSYHV 799
Cdd:PRK04863 630 teymqqLLERERELTVER--DELAARKQ----ALDEEIERLSQPGGSEDPRLNALAERfggvllseiyddvSLEDAPYFS 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 800 AGY--------------------------------EHELSSLlREKRQEVE----------GEHERRLDKMKEeHQQVMA 837
Cdd:PRK04863 704 ALYgparhaivvpdlsdaaeqlagledcpedlyliEGDPDSF-DDSVFSVEelekavvvkiADRQWRYSRFPE-VPLFGR 781
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 838 KAREQYEAE---ERKQRAELLGHLTGELERLQRAHERELETVRQ--------EQHKRLEDLRRRHREQERKLQDLE---L 903
Cdd:PRK04863 782 AAREKRIEQlraEREELAERYATLSFDVQKLQRLHQAFSRFIGShlavafeaDPEAELRQLNRRRVELERALADHEsqeQ 861
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 904 DLETRAKDVKARLALL--------------------EVQEETARRE---------------------------------- 929
Cdd:PRK04863 862 QQRSQLEQAKEGLSALnrllprlnlladetladrveEIREQLDEAEeakrfvqqhgnalaqlepivsvlqsdpeqfeqlk 941
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 930 ------KQQLLDVQRQV-ALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKH 1002
Cdd:PRK04863 942 qdyqqaQQTQRDAKQQAfALTEVVQRRAHFSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQV 1021
|
570
....*....|....*..
gi 578822059 1003 FSSLEAEAQKKQHLLRE 1019
Cdd:PRK04863 1022 LASLKSSYDAKRQMLQE 1038
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
846-1053 |
1.20e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 846 EERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEET 925
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 926 ARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSS 1005
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578822059 1006 LEAEAQ-----KKQHLLREVTVEENNASPHFEPDLHIEDLRKSLGTNQTKEVS 1053
Cdd:COG4372 169 LEQELQalseaEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELL 221
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
766-937 |
1.23e-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: 42.56 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 766 LQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAG----YEHELSSLLRE-------------------KRQEVEGEHE 822
Cdd:cd16269 107 CKQNEEASSKRCQALLQELSAPLEEKISQGSYSVPGgyqlYLEDREKLVEKyrqvprkgvkaeevlqeflQSKEAEAEAI 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 823 RRLDKMKEEHQQVMAKAREQYEAEErkQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLE 902
Cdd:cd16269 187 LQADQALTEKEKEIEAERAKAEAAE--QERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESK 264
|
170 180 190
....*....|....*....|....*....|....*
gi 578822059 903 LDLETRakdvkarlALLEVQEETARREKQQLLDVQ 937
Cdd:cd16269 265 LKEQEA--------LLEEGFKEQAELLQEEIRSLK 291
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
806-987 |
1.49e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 806 LSSLLREKRQEVEgEHERRLDKMKEEHQQVMAKAREQYEAEE----RKQRAELLGHLTgELERLQRAHERELETVRQE-- 879
Cdd:COG3206 180 LEEQLPELRKELE-EAEAALEEFRQKNGLVDLSEEAKLLLQQlselESQLAEARAELA-EAEARLAALRAQLGSGPDAlp 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 880 ---QHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLL-DVQRQVALKSEEATATHQQLE 955
Cdd:COG3206 258 ellQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILaSLEAELEALQAREASLQAQLA 337
|
170 180 190
....*....|....*....|....*....|..
gi 578822059 956 EAQKEHTHLLQSNQQLREILDELQARKLKLES 987
Cdd:COG3206 338 QLEARLAELPELEAELRRLEREVEVARELYES 369
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
753-933 |
1.70e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 753 SSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHqksyhvagyehelssllrEKRQEVEGEHERRLDKMKEEH 832
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIH------------------KLRNEFEKELRERRNELQKLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 833 QQVMAKareqyeaEER-KQRAELLGHLTGELErlqrAHERELETVRQEQHKRLEDLRRRHREQERKLQDL-ELDLEtrak 910
Cdd:PRK12704 89 KRLLQK-------EENlDRKLELLEKREEELE----KKEKELEQKQQELEKKEEELEELIEEQLQELERIsGLTAE---- 153
|
170 180
....*....|....*....|...
gi 578822059 911 dvKARLALLEVQEETARREKQQL 933
Cdd:PRK12704 154 --EAKEILLEKVEEEARHEAAVL 174
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
647-990 |
1.73e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 647 LRAQVQSStqadEDQIRAEQEAsLQKLREELEsQQKAERASLEQKNRQMLEQLKEEIEA---SEKSEQAalnaakEKALQ 723
Cdd:PRK04863 291 LRRELYTS----RRQLAAEQYR-LVEMARELA-ELNEAESDLEQDYQAASDHLNLVQTAlrqQEKIERY------QADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 724 QLREQLEgERKEAVAtLEKEHSAELERLCSSLEakhrEVVSSLQKKIQEAQQKEEAQlQKCLGQVEHRVH-----QKSYH 798
Cdd:PRK04863 359 ELEERLE-EQNEVVE-EADEQQEENEARAEAAE----EEVDELKSQLADYQQALDVQ-QTRAIQYQQAVQaleraKQLCG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 799 VAGYEHE-LSSLLREKRQEVEGEHERRLDKmkeEHQQVMAK-AREQYEaeerkQRAELLGHLTGELERlQRAHERELETV 876
Cdd:PRK04863 432 LPDLTADnAEDWLEEFQAKEQEATEELLSL---EQKLSVAQaAHSQFE-----QAYQLVRKIAGEVSR-SEAWDVARELL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 877 RQ-EQHK----RLEDLRRRHREQERKLQdLELDLETRAKDVKARLAL-----LEVQEETARREkQQLLDVQRQVALKSEE 946
Cdd:PRK04863 503 RRlREQRhlaeQLQQLRMRLSELEQRLR-QQQRAERLLAEFCKRLGKnlddeDELEQLQEELE-ARLESLSESVSEARER 580
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 578822059 947 ATATHQQLEEaqkehthllqsnqqlreildelqarklkLESQVD 990
Cdd:PRK04863 581 RMALRQQLEQ----------------------------LQARIQ 596
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
676-982 |
1.74e-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: 42.82 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 676 ELESQQKAERASLEQKNRQMLEqLKEEIeASEKSEQAALnaakEKALQQLREQLEGERKEAVA-TLEKEHSAELERL--- 751
Cdd:pfam07111 321 QLKAQDLEHRDSVKQLRGQVAE-LQEQV-TSQSQEQAIL----QRALQDKAAEVEVERMSAKGlQMELSRAQEARRRqqq 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 752 -CSSLEAKHREVVSSLqKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYeHELSSLLREK------RQE-------- 816
Cdd:pfam07111 395 qTASAEEQLKFVVNAM-SSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKV-HTIKGLMARKvalaqlRQEscpppppa 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 817 --VEGEHERRLDKMKEEH--------------QQVMAKAREQYEAEeRKQRAELLGHLTGELERLQRAHE---RELETVR 877
Cdd:pfam07111 473 ppVDADLSLELEQLREERnrldaelqlsahliQQEVGRAREQGEAE-RQQLSEVAQQLEQELQRAQESLAsvgQQLEVAR 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 878 QEQHKRLED---LRRRHREQE----RKLQDLELDLETRAKDvkaRLALLEVQEETARREKQQLLDVQRQVALKSEEATAT 950
Cdd:pfam07111 552 QGQQESTEEaasLRQELTQQQeiygQALQEKVAEVETRLRE---QLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKER 628
|
330 340 350
....*....|....*....|....*....|..
gi 578822059 951 HQQLEEAQKEHTHllQSNQQLREILDELQARK 982
Cdd:pfam07111 629 NQELRRLQDEARK--EEGQRLARRVQELERDK 658
|
|
| Ax_dynein_light |
pfam10211 |
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ... |
660-731 |
1.78e-03 |
|
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: 41.02 E-value: 1.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578822059 660 DQIRAEQEASLQKLREELESQQKaERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKeKALQQLREQLEG 731
Cdd:pfam10211 118 EQGKAELEKKIADLEEEKEELEK-QVAELKAKCEAIEKREEERRQAEEKKHAEEIAFLK-KTNQQLKAQLER 187
|
|
| PRK14971 |
PRK14971 |
DNA polymerase III subunit gamma/tau; |
423-677 |
1.88e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237874 [Multi-domain] Cd Length: 614 Bit Score: 42.84 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 423 KDDSQSSQDELQSKQSKGLEERLSPPLPHEERAQSP-PRSLATEEEPPQGPEGQPEWKEAEELGEDSAASLSLQLSLQRE 501
Cdd:PRK14971 365 KGDDASGGRGPKQHIKPVFTQPAAAPQPSAAAAASPsPSQSSAAAQPSAPQSATQPAGTPPTVSVDPPAAVPVNPPSTAP 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 502 QAPSPPAACEKGKEQHSQAEELGPG-----QEEAEDPEEKVAVSPTPPvspevrstepvaPPEQLSEAALKAMEEAVAQV 576
Cdd:PRK14971 445 QAVRPAQFKEEKKIPVSKVSSLGPStlrpiQEKAEQATGNIKEAPTGT------------QKEIFTEEDLQYYWQEFAGT 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 577 LEQDQRHLleskQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQ 656
Cdd:PRK14971 513 RPQEEKAL----KETMINCRPKLLNGTTFEVAVDNELQEKELTNLIPDLLGFLRGRLKNSKITMTVRVSEPTEVNRAYSS 588
|
250 260
....*....|....*....|.
gi 578822059 657 ADEDQIRAEQEASLQKLREEL 677
Cdd:PRK14971 589 VEKFQYLAQKNPALLELREEL 609
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
671-773 |
1.90e-03 |
|
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: 40.59 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 671 QKLREELESQQKAERASLEQKNRQmLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAvatlEKEhsaeler 750
Cdd:COG2825 42 KAAQKKLEKEFKKRQAELQKLEKE-LQALQEKLQKEAATLSEEERQKKERELQKKQQELQRKQQEA----QQD------- 109
|
90 100
....*....|....*....|...
gi 578822059 751 lcssLEAKHREVVSSLQKKIQEA 773
Cdd:COG2825 110 ----LQKRQQELLQPILEKIQKA 128
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
805-933 |
2.04e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 805 ELSSLLREKRQEVEgEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHErELETVRQEQHKRL 884
Cdd:COG1579 42 ALEARLEAAKTELE-DLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIESLKRRIS-DLEDEILELMERI 119
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 578822059 885 EDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQL 933
Cdd:COG1579 120 EELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| PRK11091 |
PRK11091 |
aerobic respiration control sensor protein ArcB; Provisional |
871-944 |
2.08e-03 |
|
aerobic respiration control sensor protein ArcB; Provisional
Pssm-ID: 236842 [Multi-domain] Cd Length: 779 Bit Score: 42.62 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 871 RELETVRQEQHK---RLEDLRRRHREQERKLQD----LELDLETRAKDVKARLALL-EVQEETARREKQQLLDVQRQVAL 942
Cdd:PRK11091 78 EQLEESRQRLSRlvaKLEEMRERDLELNVQLKDniaqLNQEIAEREKAEEARQEAFeQLKNEIKEREETQIELEQQSSLL 157
|
..
gi 578822059 943 KS 944
Cdd:PRK11091 158 RS 159
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
651-780 |
2.12e-03 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 42.40 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 651 VQSSTQADEDQI-RAEQEASL-----QKLREELESQQKAEraSLEQKNRQMLEQLKEEIEASEKSEQaalnaakEKALQQ 724
Cdd:PRK00290 494 ITASSGLSDEEIeRMVKDAEAnaeedKKRKELVEARNQAD--SLIYQTEKTLKELGDKVPADEKEKI-------EAAIKE 564
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 578822059 725 LREQLEGERKEAVatleKEHSAELErlcssleakhrEVVSSLQKKIQEAQQKEEAQ 780
Cdd:PRK00290 565 LKEALKGEDKEAI----KAKTEELT-----------QASQKLGEAMYQQAQAAQGA 605
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
563-750 |
2.15e-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: 42.63 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 563 EAALKAMEEAVAQVleqdqrhlleSKQEKMQQLREKLCQeeeeeiLRLHQQKEQSLSSLRERLQKAieeeearmreeeSQ 642
Cdd:COG3096 475 EKAYELVCKIAGEV----------ERSQAWQTARELLRR------YRSQQALAQRLQQLRAQLAEL------------EQ 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 643 RLswlRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKN----------RQMLEQLKEEIEASEKSEQA 712
Cdd:COG3096 527 RL---RQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAaeaveqrselRQQLEQLRARIKELAARAPA 603
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 578822059 713 ALNAAkeKALQQLREQLEGERKEAVA-------TLEKEHSAELER 750
Cdd:COG3096 604 WLAAQ--DALERLREQSGEALADSQEvtaamqqLLEREREATVER 646
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
686-779 |
2.42e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 686 ASLEQKNRQmLEQLKEEIEASEKsEQAALNAAKEKALQQLREQLEGERKEAVA--TLEKEHSAELERLCSSLEAKHrEVV 763
Cdd:COG0542 411 EELDELERR-LEQLEIEKEALKK-EQDEASFERLAELRDELAELEEELEALKArwEAEKELIEEIQELKEELEQRY-GKI 487
|
90
....*....|....*.
gi 578822059 764 SSLQKKIQEAQQKEEA 779
Cdd:COG0542 488 PELEKELAELEEELAE 503
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
657-932 |
2.48e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.16 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 657 ADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALN---AAKEKALQQLREQLEGER 733
Cdd:pfam02029 8 ARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDrtaKREERRQKRLQEALERQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 734 KEAVATLEKEHSAELERL------CSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELS 807
Cdd:pfam02029 88 EFDPTIADEKESVAERKEnneeeeNSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 808 SLLRE--KRQEVEGEHERRLDKMKEEHQQVMAkaREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQH---- 881
Cdd:pfam02029 168 EVPTEnfAKEEVKDEKIKKEKKVKYESKVFLD--QKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEvfle 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578822059 882 --KRLEDLRRRHREQER--------KLQDLELDLETRAKDVKARLALLEVQEETARREKQQ 932
Cdd:pfam02029 246 aeQKLEELRRRRQEKESeefeklrqKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAE 306
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
862-1026 |
2.49e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 862 LERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLE-----LDLETRAKDVKARLALLEVQEETARRE------- 929
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRqknglVDLSEEAKLLLQQLSELESQLAEARAElaeaear 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 930 ---------------------------KQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQS-NQQLREILDELQAR 981
Cdd:COG3206 242 laalraqlgsgpdalpellqspviqqlRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILASLEAE 321
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 578822059 982 KLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLREVTVEENN 1026
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVAREL 366
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
660-948 |
2.54e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.83 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 660 DQIRA--EQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKsEQAALNAAKEKA---LQQLREQLE---G 731
Cdd:pfam00038 18 DKVRFleQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTV-ERARLQLELDNLrlaAEDFRQKYEdelN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 732 ERKEA---VATLEKE-HSAELERLcssleakhrevvsSLQKKIQEAQqkEEAQLQKCLGQVEHRvhqksyhvagyehELS 807
Cdd:pfam00038 97 LRTSAendLVGLRKDlDEATLARV-------------DLEAKIESLK--EELAFLKKNHEEEVR-------------ELQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 808 SLLREKRQEVEGEHERRLDKmkeehQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKrLEDL 887
Cdd:pfam00038 149 AQVSDTQVNVEMDAARKLDL-----TSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEE-ITEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 888 RRR----------HREQ----ERKLQDLELDLETRAKDVKARLALLEVQ-----EETAR--REKQQLLDVqrQVALKSEE 946
Cdd:pfam00038 223 RRTiqsleielqsLKKQkaslERQLAETEERYELQLADYQELISELEAElqetrQEMARqlREYQELLNV--KLALDIEI 300
|
..
gi 578822059 947 AT 948
Cdd:pfam00038 301 AT 302
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
802-960 |
2.89e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 802 YEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAEllghLTGELERLQRAHEreletVRQEQH 881
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREE----LQREEERLVQKEE-----QLDARA 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578822059 882 KRLEDLRRRHREQERKLQDLELDLETRAKDVKARlaLLEVQEETARREKQQLLDvQRQVALKSEEATATHQQLEEAQKE 960
Cdd:PRK12705 98 EKLDNLENQLEEREKALSARELELEELEKQLDNE--LYRVAGLTPEQARKLLLK-LLDAELEEEKAQRVKKIEEEADLE 173
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
563-978 |
3.19e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 563 EAALKAMEEAVAQV------LEQDQRHL-LESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEAR 635
Cdd:COG4913 238 ERAHEALEDAREQIellepiRELAERYAaARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 636 MREEESQRLSwLRAQVQSSTQADEDQIRAEQEAsLQKLREELES-----QQKAERASLE--------QKNRQMLEQLKEE 702
Cdd:COG4913 318 LDALREELDE-LEAQIRGNGGDRLEQLEREIER-LERELEERERrrarlEALLAALGLPlpasaeefAALRAEAAALLEA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 703 IEASEKSEQAALNAAkEKALQQLREQLEGERKEaVATLEK------EHSAEL-ERLCSSLEAKHREV--------VSSLQ 767
Cdd:COG4913 396 LEEELEALEEALAEA-EAALRDLRRELRELEAE-IASLERrksnipARLLALrDALAEALGLDEAELpfvgelieVRPEE 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 768 KKIQEAQQK-----------EEAQLQKCLGQVE----------HRVHQKSYHVAGYEHELSSLLRE-------KRQEVEG 819
Cdd:COG4913 474 ERWRGAIERvlggfaltllvPPEHYAAALRWVNrlhlrgrlvyERVRTGLPDPERPRLDPDSLAGKldfkphpFRAWLEA 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 820 EHERRLDKMKEEHQQVMAKAR----------EQYEAEERKQR-------------AELLGHLTGELERLQRAHE------ 870
Cdd:COG4913 554 ELGRRFDYVCVDSPEELRRHPraitragqvkGNGTRHEKDDRrrirsryvlgfdnRAKLAALEAELAELEEELAeaeerl 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 871 RELETVRQEQHKRLEDLRR---------RHREQERKLQDLELDLEtRAKDVKARLALLEVQEETARRE----KQQLLDVQ 937
Cdd:COG4913 634 EALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELE-RLDASSDDLAALEEQLEELEAEleelEEELDELK 712
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 578822059 938 RQVALKSEEATATHQQLEEAQKEHTHLLQ-SNQQLREILDEL 978
Cdd:COG4913 713 GEIGRLEKELEQAEEELDELQDRLEAAEDlARLELRALLEER 754
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
577-1181 |
3.35e-03 |
|
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: 42.27 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 577 LEQDQRHLLESKQEKMQQLREKLCQEEEEEILRL-HQQKEQSLSSLRERLQKA-IEEEEARMREEESQRLSWLRAQVQSS 654
Cdd:pfam02463 234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLaQVLKENKEEEKEKKLQEEeLKLLAKEEEELKSELLKLERRKVDDE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 655 TQADEDQIRAEQEASLQKLREELESQQKAERASLEqknRQMLEQLKEEIEASEKSEQAALNAAKEKALQQL-REQLEGER 733
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELE---IKREAEEEEEEELEKLQEKLEQLEEELLAKKKLeSERLSSAA 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 734 KEAVATLEKEHSAELERlcsSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSLLREK 813
Cdd:pfam02463 391 KLKEEELELKSEEEKEA---QLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 814 RQE-----------VEGEHERRLDKMKEEHQQVMA-KAREQYEAEERKQRAELLGHLTGELERLQRAHERE--------- 872
Cdd:pfam02463 468 KKSedllketqlvkLQEQLELLLSRQKLEERSQKEsKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVenykvaist 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 873 LETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQE--ETARREKQQLLDVQRQVALKSEEATAT 950
Cdd:pfam02463 548 AVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEidPILNLAQLDKATLEADEDDKRAKVVEG 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 951 HQQLEEAQKEHTHLLQSNQQLREI--LDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKQHLLREVTVEENNAS 1028
Cdd:pfam02463 628 ILKDTELTKLKESAKAKESGLRKGvsLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQR 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1029 PHFEP-DLHIEDLRKSLGTNQTKEVSSSLSQSKEDLYLDSLSSHNVWHLLSA-EGVALRSAKEFLVQQTRSMRRRQTALK 1106
Cdd:pfam02463 708 EKEELkKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKeEKEEEKSELSLKEKELAEEREKTEKLK 787
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578822059 1107 AAQQHWRHELASAQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSLWEEASDE 1181
Cdd:pfam02463 788 VEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEE 862
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
655-935 |
3.66e-03 |
|
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: 41.55 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 655 TQADEDQIRAEQEASLQKLREELESQQKAERasleqKNRQMLEQLKEEIEASEKSEQAALNAAKEkaLQQLREQLEGERK 734
Cdd:pfam05667 217 AAAQEWEEEWNSQGLASRLTPEEYRKRKRTK-----LLKRIAEQLRSAALAGTEATSGASRSAQD--LAELLSSFSGSST 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 735 EAVATLEKEHSAELERLCSSLEAKHREVVSSLQKK----IQEAQQKEEAQLQKCLGQVEHRVHQksyhvagYEHELSSLL 810
Cdd:pfam05667 290 TDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVEteeeLQQQREEELEELQEQLEDLESSIQE-------LEKEIKKLE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 811 REKRQ-EVEGEHERRLDKMKEEHQQVMAKAREQY-EAEER--------KQRAELLGHLTGELERLQRAHERELETVRQEQ 880
Cdd:pfam05667 363 SSIKQvEEELEELKEQNEELEKQYKVKKKTLDLLpDAEENiaklqalvDASAQRLVELAGQWEKHRVPLIEEYRALKEAK 442
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 578822059 881 HKRLEdlrrrhrEQERKLQDLEldlETRAKdvkarlaLLEVQEETARRE--KQQLLD 935
Cdd:pfam05667 443 SNKED-------ESQRKLEEIK---ELREK-------IKEVAEEAKQKEelYKQLVA 482
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
671-776 |
3.74e-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: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 671 QKLREELESQQKAERASLEQKNRQmLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKehsaeler 750
Cdd:smart00935 17 KAAQKQLEKEFKKRQAELEKLEKE-LQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQK-------- 87
|
90 100
....*....|....*....|....*.
gi 578822059 751 lcssleaKHREVVSSLQKKIQEAQQK 776
Cdd:smart00935 88 -------RQQEELQKILDKINKAIKE 106
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
833-983 |
4.07e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 833 QQVMAKAREQYEAEERKQR-------AELLGHLTgelERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLE--- 902
Cdd:COG2433 353 ERVEKKVPPDVDRDEVKARvirglsiEEALEELI---EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEaev 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 903 LDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARK 982
Cdd:COG2433 430 EELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGE 509
|
.
gi 578822059 983 L 983
Cdd:COG2433 510 L 510
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
807-927 |
4.65e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.48 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 807 SSLLREKRQEVEgeherRLDKMKEEHQQvmAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQE-QHKRLE 885
Cdd:PRK11448 141 ENLLHALQQEVL-----TLKQQLELQAR--EKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKaAETSQE 213
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 578822059 886 DLRRRHREQERKLQDLELD-LETRAK-DVKARLALLEVQEETAR 927
Cdd:PRK11448 214 RKQKRKEITDQAAKRLELSeEETRILiDQQLRKAGWEADSKTLR 257
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
697-783 |
5.12e-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: 38.72 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 697 EQLKEEIEASEKSEQAALNAaKEKALQQLREQLEGERkeavATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQK 776
Cdd:smart00935 17 KAAQKQLEKEFKKRQAELEK-LEKELQKLKEKLQKDA----ATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQE 91
|
....*..
gi 578822059 777 EEAQLQK 783
Cdd:smart00935 92 ELQKILD 98
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
580-939 |
5.22e-03 |
|
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: 41.35 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 580 DQRHLLESKQEKMQQLREKLcqeeeEEILRLHQQKEQSLSSLRERLQKaieeeearmreeesqrlswlrAQVQSSTQ--- 656
Cdd:pfam10174 384 DLKDMLDVKERKINVLQKKI-----ENLQEQLRDKDKQLAGLKERVKS---------------------LQTDSSNTdta 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 657 -ADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQmLEQLKEEIEAS--EKSEQ-AALNAAKEKA----------- 721
Cdd:pfam10174 438 lTTLEEALSEKERIIERLKEQREREDRERLEELESLKKE-NKDLKEKVSALqpELTEKeSSLIDLKEHAsslassglkkd 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 722 --LQQLREQLEGERKEAVAT---LEKEHSAEL-ERLCSSLEAKHREVVSSLQKKIQEAQ--QKEEAQLQKCLGQVEHRVH 793
Cdd:pfam10174 517 skLKSLEIAVEQKKEECSKLenqLKKAHNAEEaVRTNPEINDRIRLLEQEVARYKEESGkaQAEVERLLGILREVENEKN 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 794 QKSYHVAgyEHELSSLLREKRQEVEGEHERRLDK-MKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQR---AH 869
Cdd:pfam10174 597 DKDKKIA--ELESLTLRQMKEQNKKVANIKHGQQeMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQeldAT 674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 870 ERELETVRQEQHKR---LEDLRRRHREQ-ERKLQDLELDLETRAKDVKARLALLEV--------QEETA--RREKQQLLD 935
Cdd:pfam10174 675 KARLSSTQQSLAEKdghLTNLRAERRKQlEEILEMKQEALLAAISEKDANIALLELssskkkktQEEVMalKREKDRLVH 754
|
....
gi 578822059 936 VQRQ 939
Cdd:pfam10174 755 QLKQ 758
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
663-990 |
5.23e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 663 RAEQEASLQKL--REELESQQKAERASLEQ---------KNRQMLEQLKEEIEASE---KSEQAALNAAKEKALQQLREQ 728
Cdd:PRK11281 38 EADVQAQLDALnkQKLLEAEDKLVQQDLEQtlalldkidRQKEETEQLKQQLAQAPaklRQAQAELEALKDDNDEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 729 LEgerKEAVATLEK---EHSAELERLCSSLEAKHREVVSS------LQKKIQEAQQkeeaQLQkclgqvehrvhqksyhv 799
Cdd:PRK11281 118 LS---TLSLRQLESrlaQTLDQLQNAQNDLAEYNSQLVSLqtqperAQAALYANSQ----RLQ----------------- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 800 agyehELSSLLreKRQEVEGEHERRLDKMKEEHQQVMAKAREQYeaeerkQRAELLGH--LTgELERLQraheRELETVR 877
Cdd:PRK11281 174 -----QIRNLL--KGGKVGGKALRPSQRVLLQAEQALLNAQNDL------QRKSLEGNtqLQ-DLLQKQ----RDYLTAR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 878 QEQhkrledlrrrhreQERKLQDL-ELDLETRAKDVKARLALLEVQEETARREKQQLldvqrqVALKSEEATATHQQLEE 956
Cdd:PRK11281 236 IQR-------------LEHQLQLLqEAINSKRLTLSEKTVQEAQSQDEAARIQANPL------VAQELEINLQLSQRLLK 296
|
330 340 350
....*....|....*....|....*....|....
gi 578822059 957 AQKEHTHLLQSNQQLREILDELQARKLKLESQVD 990
Cdd:PRK11281 297 ATEKLNTLTQQNLRVKNWLDRLTQSERNIKEQIS 330
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
863-983 |
5.65e-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: 40.74 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 863 ERLQRAHERELETVRQEQHkrLEDLRRRHREQERKLQDLELDLETRAKDVKA-RLALLEVQEETARREKQQLLDVQRQVA 941
Cdd:pfam07767 199 ELLQKAVEAEKKRLKEEEK--LERVLEKIAESAATAEAREEKRKTKAQRNKEkRRKEEEREAKEEKALKKKLAQLERLKE 276
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 578822059 942 LKSEEAtathQQLEEAQKEHTHLLQSNQQLREILDELQARKL 983
Cdd:pfam07767 277 IAKEIA----EKEKEREEKAEARKREKRKKKKEEKKLRPRKL 314
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
474-762 |
6.04e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 474 GQPEWKEAEELgEDSAASLSlQLSLQREQAPSPPAACEKGKEQhsQAEELGPGQEEAEDPEEKVAVSPTPPVSPEVRSTE 553
Cdd:TIGR02169 729 EQEEEKLKERL-EELEEDLS-SLEQEIENVKSELKELEARIEE--LEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLE 804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 554 pvappEQLS--EAALKAMEEAVaQVLEQDQRHLLESKQEKMQQLRE------KLCQEEEEEILRL---------HQQKEQ 616
Cdd:TIGR02169 805 -----EEVSriEARLREIEQKL-NRLTLEKEYLEKEIQELQEQRIDlkeqikSIEKEIENLNGKKeeleeeleeLEAALR 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 617 SLSSLRERLQKAIEEEEARMREEEsQRLSWLRAQVQsstqaDEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQM- 695
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELE-RKIEELEAQIE-----KKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELs 952
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578822059 696 LEQLKEEIEASEKsEQAALNAAKEKALQQLREQLE--GERKEAVATLEKEHSAELERLcSSLEAKHREV 762
Cdd:TIGR02169 953 LEDVQAELQRVEE-EIRALEPVNMLAIQEYEEVLKrlDELKEKRAKLEEERKAILERI-EEYEKKKREV 1019
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
862-1035 |
6.59e-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: 39.91 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 862 LERLQRAHER--ELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQrq 939
Cdd:COG1579 9 LLDLQELDSEldRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 940 valKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSSLEAEAQKKqhlLRE 1019
Cdd:COG1579 87 ---NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE---LEE 160
|
170
....*....|....*.
gi 578822059 1020 VTVEENNASPHFEPDL 1035
Cdd:COG1579 161 LEAEREELAAKIPPEL 176
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
659-783 |
7.01e-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: 39.91 E-value: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 659 EDQIRAEQEA--SLQKLREELESQQKAERASLEQKNRQM--------LEQLKEEIEASEKSEQAAlnaakEKALQQLREQ 728
Cdd:COG1579 44 EARLEAAKTEleDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnnkeYEALQKEIESLKRRISDL-----EDEILELMER 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 578822059 729 LEgERKEAVATLEKEHsAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQK 783
Cdd:COG1579 119 IE-ELEEELAELEAEL-AELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| 4HB_MCP_1 |
pfam12729 |
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ... |
657-742 |
7.44e-03 |
|
Four helix bundle sensory module for signal transduction; This family is a four helix bundle that operates as a ubiquitous sensory module in prokaryotic signal-transduction. The 4HB_MCP is always found between two predicted transmembrane helices indicating that it detects only extracellular signals. In many cases the domain is associated with a cytoplasmic HAMP domain suggesting that most proteins carrying the bundle might share the mechanism of transmembrane signalling which is well-characterized in E coli chemoreceptors. This domain recognizes citrate and TCA cycle intermediates, cis-aconitate, boric acid, Phenanthrene, pyrene and benzopyrene (Matilla et el., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 432749 [Multi-domain] Cd Length: 181 Bit Score: 39.16 E-value: 7.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 657 ADEDQIRAEQEASLQKLREELESQQKA-ERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAK----EKALQQLREQLEG 731
Cdd:pfam12729 71 TTDPAERDELLKDIEELRAEIDKLLEKyEKTILTDEEKKLFAEFKENLNAYRAVRNKVLELAKagnkDEAYQLYKTEGRP 150
|
90
....*....|.
gi 578822059 732 ERKEAVATLEK 742
Cdd:pfam12729 151 AREAMIEALEE 161
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
647-793 |
8.49e-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: 39.96 E-value: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 647 LRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQM-LEQLKEEIEASEKseqaaLNAAKEKALQQL 725
Cdd:pfam17060 106 LKEDVKSSPRSEADSLGTPIKVDLLRNLKPQESPETPRRINRKYKSLELrVESMKDELEFKDE-----TIMEKDRELTEL 180
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578822059 726 REQLeGERKEAVATLEKEHS-----AELERLCSSLEA-KHREVVSSLQKKIQEaQQKEEAQLQKCLGQVEHRVH 793
Cdd:pfam17060 181 TSTI-SKLKDKYDFLSREFEfykqhHEHGGNNSIKTAtKHEFIISELKRKLQE-QNRLIRILQEQIQFDPGALH 252
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
806-979 |
8.83e-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: 40.49 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 806 LSSLLREKRQEvEGEHERRLDKMKEEhqqvmAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVR--QEQHKR 883
Cdd:pfam05557 11 LSQLQNEKKQM-ELEHKRARIELEKK-----ASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElnRLKKKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 884 LEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTH 963
Cdd:pfam05557 85 LEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSS 164
|
170
....*....|....*.
gi 578822059 964 LLQSNQQLREILDELQ 979
Cdd:pfam05557 165 LAEAEQRIKELEFEIQ 180
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
644-1170 |
8.99e-03 |
|
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: 40.58 E-value: 8.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 644 LSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQqkaerasLEQKNRQMLeQLKEEIEaseKSEQAALNAAKEKALQ 723
Cdd:pfam10174 164 LEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVL-------LDQKEKENI-HLREELH---RRNQLQPDPAKTKALQ 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 724 QLREQLE---GERKEAVATLEKE-----HSAELERLCSSLEAKHREVVSSLQK----KIQEAQQ---KEEAQLQKCLGQV 788
Cdd:pfam10174 233 TVIEMKDtkiSSLERNIRDLEDEvqmlkTNGLLHTEDREEEIKQMEVYKSHSKfmknKIDQLKQelsKKESELLALQTKL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 789 EHRVHQKS---YHVAGYEHELSSllREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEaeerkQRAELLGHLTGELERL 865
Cdd:pfam10174 313 ETLTNQNSdckQHIEVLKESLTA--KEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQ-----DLTEEKSTLAGEIRDL 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 866 QR---AHERELETVrqeqHKRLEDLRRRHREQERKLQDLE---LDLETRAKDVKARLALLE------------VQEETAR 927
Cdd:pfam10174 386 KDmldVKERKINVL----QKKIENLQEQLRDKDKQLAGLKervKSLQTDSSNTDTALTTLEealsekeriierLKEQRER 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 928 --REKQQLLDVQRQvALKSEEATATHQQLEEAQKEhthllQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSS 1005
Cdd:pfam10174 462 edRERLEELESLKK-ENKDLKEKVSALQPELTEKE-----SSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSK 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1006 LEAEAQKKQHLLREVTVEEnnasphfEPDLHIEDLRKSLGTNQTKevsSSLSQSKEDLYLDSLSSHNVWHLLSAEGVAlr 1085
Cdd:pfam10174 536 LENQLKKAHNAEEAVRTNP-------EINDRIRLLEQEVARYKEE---SGKAQAEVERLLGILREVENEKNDKDKKIA-- 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578822059 1086 SAKEFLVQQTRSMRRRQTALKAAQQHWRHELAS-------AQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSAMRKGHN 1158
Cdd:pfam10174 604 ELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQlleearrREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQ 683
|
570
....*....|..
gi 578822059 1159 LLKKKEEKLNQL 1170
Cdd:pfam10174 684 SLAEKDGHLTNL 695
|
|
| |
