|
Name |
Accession |
Description |
Interval |
E-value |
| Cnn_1N |
pfam07989 |
Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated ... |
61-129 |
6.49e-20 |
|
Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated proteins in Schizosaccharomyces pombe, Mto1 and Pcp1. Mto1 has been identified in association with spindle pole body and non-spindle pole body microtubules. The pericentrin homolog Pcp1 is also associated with the fungal centrosome or spindle pole body (SPB). Members of this family have been named centrosomins, and are an essential mitotic centrosome component required for assembly of all other known pericentriolar matrix proteins in order to achieve microtubule-organizing activity in fission yeast. Cnn_1N is a short conserved motif towards the N-terminus. Motif 1 is found to be necessary for proper recruitment of gamma-tubulin, D-TACC (the homolog of vertebrate transforming acidic coiled-coil proteins [TACC]), and Minispindles (Msps) to embryonic centrosomes but is not required for assembly of other centrosome components including Aurora A kinase and CP60 in Drosophila.
Pssm-ID: 462333 [Multi-domain] Cd Length: 69 Bit Score: 85.27 E-value: 6.49e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58535453 61 KDFENQITELKKENFNLKLRIYFLEERMQQEFHGPTEHIYKTNIELKVEVESLKRELQEREQLLIKASK 129
Cdd:pfam07989 1 REQEKQIDKLKKENFNLKLKIHFLEERLEKLAPEQIEEALKENIELKVELETLQRELKKLKKLLREAEK 69
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
146-458 |
5.00e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.05 E-value: 5.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 146 KEDARKK---VQQ----VEDL---LTKRILLLEKDvtAAQAELEKAFAgtetEKALRLRLESKLSEMKKMHEGDLAMALV 215
Cdd:COG1196 174 KEEAERKleaTEEnlerLEDIlgeLERQLEPLERQ--AEKAERYRELK----EELKELEAELLLLKLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 216 LDEKDRLIEELKLSLKSKEALIQCLKEEKSQmacpdENVSSGELRglcaapreEKERETEAAQMEHQKERNSFEERIQAL 295
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEE-----LELELEEAQ--------AEEYELLAELARLEQDIARLEERRREL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 296 EEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETALsg 375
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL-- 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 376 KEALSAALRSQNLTKSTENHRLRRSikKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREK 455
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLE--RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
...
gi 58535453 456 AME 458
Cdd:COG1196 471 EAA 473
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
64-630 |
1.56e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 76.31 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 64 ENQITELKKENFN-LKLRIYFLEERMQQ-------EFHGPTEHIYKTNIE---LKVEVESLKRELQEREQLLIKASKAVE 132
Cdd:pfam15921 244 EDQLEALKSESQNkIELLLQQHQDRIEQlisehevEITGLTEKASSARSQansIQSQLEIIQEQARNQNSMYMRQLSDLE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 133 SLAEAGGSEIQRVKEDARKKVQQVEdlltKRILLLEKDVTAAQAE--------------LEKAFAGT-ETEKALRLRLES 197
Cdd:pfam15921 324 STVSQLRSELREAKRMYEDKIEELE----KQLVLANSELTEARTErdqfsqesgnlddqLQKLLADLhKREKELSLEKEQ 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 198 KlsemKKMHEGDLAMALVLDEKDRLIEELKLSLKSKEALIQCLKEE-KSQMacpdenvssgelrglcaapreekERETEA 276
Cdd:pfam15921 400 N----KRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEcQGQM-----------------------ERQMAA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 277 AQMEHQ--KERNSFEERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLsaafaKAREA 354
Cdd:pfam15921 453 IQGKNEslEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKL-----RSRVD 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 355 LQKAQTQEFQGSEDYetaLSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSD-------LQQERERLEKDLEEAHR 427
Cdd:pfam15921 528 LKLQELQHLKNEGDH---LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQhgrtagaMQVEKAQLEKEINDRRL 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 428 E-------KSKGDCTIRDLRNEVE-------KLRNEVNEREKAME----------NRYKSLLSESNKKLHNQEQVIKHL- 482
Cdd:pfam15921 605 ElqefkilKDKKDAKIRELEARVSdlelekvKLVNAGSERLRAVKdikqerdqllNEVKTSRNELNSLSEDYEVLKRNFr 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 483 -----TESTNQKDVLLQKFNEKDLEVIQQNCYLMAAED-----LELRSEGLITEKCSSQQPPGSKTIFSKEKKQSSDYEE 552
Cdd:pfam15921 685 nkseeMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDghamkVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEK 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 553 liQVLKKEQDIYTHLVKSLQESDsiNNLQAELNKIFALRKQLEQDVLSYQNLRKTLEEQISE----IRRREEESFSLYSD 628
Cdd:pfam15921 765 --HFLKEEKNKLSQELSTVATEK--NKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAEcqdiIQRQEQESVRLKLQ 840
|
..
gi 58535453 629 QT 630
Cdd:pfam15921 841 HT 842
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
104-452 |
1.91e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 76.25 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 104 IELKVEVESLKRELQEREQLLIKASKAVESLAEaggsEIQRVKEDARKKVQQVEDLltkrilllEKDVTAAQAELEKAFA 183
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRK----ELEELEEELEQLRKELEEL--------SRQISALRKDLARLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 184 GTETEKALRLRLESKLSEMKKMHEGDLAMalvLDEKDRLIEELKLSLKSKEALIQCLKEEKSQMacpdenvssgelrglc 263
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEER---LEEAEEELAEAEAEIEELEAQIEQLKEELKAL---------------- 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 264 aaprEEKERETEAAQMEHQKERNSFEERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEK 343
Cdd:TIGR02168 802 ----REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 344 LSAAFAKAREALQKAQTQEFQGSEDYETALSGKEALSAALRSQNltksTENHRLRRSIKKITQELSDLQQE-RERLEKDL 422
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR----EKLAQLELRLEGLEVRIDNLQERlSEEYSLTL 953
|
330 340 350
....*....|....*....|....*....|
gi 58535453 423 EEAHREKSKGDCTIRDLRNEVEKLRNEVNE 452
Cdd:TIGR02168 954 EEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
147-500 |
1.44e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.17 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 147 EDARKKVQQVEDLLTKrillLEKDVTAAQAELEKAfagtetEKALRLRLESKlsemkkmhegDLAMALVLDEKDRLIEEL 226
Cdd:TIGR02168 182 ERTRENLDRLEDILNE----LERQLKSLERQAEKA------ERYKELKAELR----------ELELALLVLRLEELREEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 227 KLSLKSKEALIQCLKEEKSQMACPDENVSsgELRgLCAAPREEKERETEAAQMEHQKERNSFEERIQALEEDLREKEREI 306
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLE--ELR-LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 307 ATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEfqgsEDYETALSGKEALSAALRSQ 386
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL----EELEEQLETLRSKVAQLELQ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 387 NLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCtirdlrNEVEKLRNEVNEREKAMENRYKSLLS 466
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL------EELEEELEELQEELERLEEALEELRE 468
|
330 340 350
....*....|....*....|....*....|....
gi 58535453 467 ESNKKLHNQEQVIKHLTESTNQKDVLLQKFNEKD 500
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
62-671 |
9.99e-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: 70.47 E-value: 9.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 62 DFENQITELKKENFNLKLRIYFLEERMQQEFHGPTEHIYKTNI------ELKVEVESLKRELQEREQLLIKASKAVESLA 135
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEleekleELKEELESLEAELEELEAELEELESRLEELE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 136 EaggsEIQRVKEDARKKVQQVEdLLTKRILLLEKDVTAAQAELEKAFAgtETEKALRLRLESKLSEMKKMHEGDLAMALV 215
Cdd:TIGR02168 379 E----QLETLRSKVAQLELQIA-SLNNEIERLEARLERLEDRRERLQQ--EIEELLKKLEEAELKELQAELEELEEELEE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 216 LDEK-DRLIEELKLSLKSKEALIQCLKEEKSQmacpdENVSSGELRGLCAAPRE-EKERETEAAQMEHQKERN------- 286
Cdd:TIGR02168 452 LQEElERLEEALEELREELEEAEQALDAAERE-----LAQLQARLDSLERLQENlEGFSEGVKALLKNQSGLSgilgvls 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 287 ---SFEE------------RIQALE-EDLREKEREIATEKKNSLKR----------DKAIQGLTMALKSKEKKVEELNSE 340
Cdd:TIGR02168 527 eliSVDEgyeaaieaalggRLQAVVvENLNAAKKAIAFLKQNELGRvtflpldsikGTEIQGNDREILKNIEGFLGVAKD 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 341 IEKLSAAFAKAREAL--------QKAQTQEFQGSEDYETAL-----------------SGKEALSAALRSQNLTKSTEN- 394
Cdd:TIGR02168 607 LVKFDPKLRKALSYLlggvlvvdDLDNALELAKKLRPGYRIvtldgdlvrpggvitggSAKTNSSILERRREIEELEEKi 686
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 395 HRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHN 474
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 475 QEQVIKHLTESTNQKDVLLQkfNEKDLEVIQQNCYLMAAEDLELRSE-----GLITEKCSSQQppGSKTIFSKEKKQSSD 549
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEE--LEAQIEQLKEELKALREALDELRAEltllnEEAANLRERLE--SLERRIAATERRLED 842
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 550 YEELIQVLKKEQDIYTHLVKSLQEsdSINNLQAELNKIFALRKQLEQDVLSyqnLRKTLEEQISEIRRREEESfslySDQ 629
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEE--LIEELESELEALLNERASLEEALAL---LRSELEELSEELRELESKR----SEL 913
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 58535453 630 TSYLSICLEENNRFQVEhfsQEELKKKVSDLIQLVKELYTDN 671
Cdd:TIGR02168 914 RRELEELREKLAQLELR---LEGLEVRIDNLQERLSEEYSLT 952
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
216-623 |
1.56e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 216 LDEKDRLIEELKLSLKSKEALIQCLKEEKSQMAcpdenvssGELRGLCAAPrEEKERETEAAQMEHQKernsFEERIQAL 295
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELE--------EELEQLRKEL-EELSRQISALRKDLAR----LEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 296 EEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETALSG 375
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 376 KEALSAALRS-----QNLTKSTEnhRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEV 450
Cdd:TIGR02168 826 LESLERRIAAterrlEDLEEQIE--ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 451 NE-REKAMENRYKslLSESNKKLHnqeQVIKHLTESTNQKDVLLQKFNEKdleviqqncYLMAAEDLELRSEGLitekcs 529
Cdd:TIGR02168 904 RElESKRSELRRE--LEELREKLA---QLELRLEGLEVRIDNLQERLSEE---------YSLTLEEAEALENKI------ 963
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 530 sqqppgsktifskEKKQSSDYEELIQVLKKEQDIYTHLVKSLQESDSINNLQAELNKifalrkQLEqDVLSyqnLRKTLE 609
Cdd:TIGR02168 964 -------------EDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTA------QKE-DLTE---AKETLE 1020
|
410
....*....|....
gi 58535453 610 EQISEIRRREEESF 623
Cdd:TIGR02168 1021 EAIEEIDREARERF 1034
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
105-425 |
2.80e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 105 ELKVEVESLKRELQEREQLLIKASKAVEsLAEAGGSEIQRVKEDARKKV---QQVEDLLTKRILLLEKDVTAAQAELEKA 181
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELA-ELEAELEELRLELEELELELeeaQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 182 fagTETEKALRLRLESKLSEMKKMHEgdlAMALVLDEKDRLIEELKLSLKSKEALIQCLKEEKSQMACPDENVSSgelrg 261
Cdd:COG1196 315 ---EERLEELEEELAELEEELEELEE---ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE----- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 262 lcaapREEKERETEAAQMEHQKERNSFEERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEI 341
Cdd:COG1196 384 -----LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 342 EKLSAAFAKAREALQKAQTQEFQGSEDYETALSGKEALSAALRSQN-LTKSTENHRLRRSIKKITQELSDLQQERERLEK 420
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA 538
|
....*
gi 58535453 421 DLEEA 425
Cdd:COG1196 539 ALEAA 543
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
137-455 |
2.91e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.94 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 137 AGGSEIQRVKEDARKKVQQVEDLLtKRILLLEKDVTAAQAELEKAFAGTETEKALRLRLES-----KLSEMKKMHEGDLA 211
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENI-ERLDLIIDEKRQQLERLRREREKAERYQALLKEKREyegyeLLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 212 MALVLDEKDRLIEELKLSLKSKEALIQCLKEEKSQMACPDENVSSGELRGL-------------CAAPREEKERETEAAQ 278
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVkekigeleaeiasLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 279 MEHQKernsFEERIQALEEDLREKEREIATEKKnslKRDKaiqgLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKA 358
Cdd:TIGR02169 322 ERLAK----LEAEIDKLLAEIEELEREIEEERK---RRDK----LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 359 QTQ-EFQGSEDYE--TALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCT 435
Cdd:TIGR02169 391 REKlEKLKREINElkRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
330 340
....*....|....*....|
gi 58535453 436 IRDLRNEVEKLRNEVNEREK 455
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQR 490
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
85-621 |
1.27e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.09 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 85 EERMQQEFHGPTEHIYKTNIELKVE----VESLKRELQEREQLLIKASKAVESLAEAGGSEIQRVKEDARKKVQQVEDLL 160
Cdd:PTZ00121 1149 EDAKRVEIARKAEDARKAEEARKAEdakkAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEA 1228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 161 TKRILLLEKDVTAAQ-AELEKAFAGTETEKALRLRLESKLSEMKKMHEGDLAMALVLDEKDRLIEELKLSLKSKEALIQC 239
Cdd:PTZ00121 1229 VKKAEEAKKDAEEAKkAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAK 1308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 240 LKEEKSQMACPDENVSSGELRGLCAAPR--EEKERETEAAQMEHQKERNSFEERIQALEEDlrEKEREIATEKKNSLKRD 317
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKkaEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA--EKKKEEAKKKADAAKKK 1386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 318 KAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEF-----QGSEDYETALSGKEALSAALRSQNLTKST 392
Cdd:PTZ00121 1387 AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKadeakKKAEEAKKADEAKKKAEEAKKAEEAKKKA 1466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 393 ENHRLRRSIKKITQE---LSDLQQERERLEKDLEEAHR---EKSKGDctirDLRNEVEKLRNEvnEREKAMENRYKSLLS 466
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEakkADEAKKKAEEAKKKADEAKKaaeAKKKAD----EAKKAEEAKKAD--EAKKAEEAKKADEAK 1540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 467 ESNKKLHNQEqvIKHLTESTNQKDVllQKFNEKDLEVIQQNCYLMAAEDLELRSEGLITEKCSSQQPpgSKTIFSKEKKQ 546
Cdd:PTZ00121 1541 KAEEKKKADE--LKKAEELKKAEEK--KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE--EKKMKAEEAKK 1614
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58535453 547 SSDYEELIQVLKKEQDIYTHLVKSLQESDSinnlqaELNKIFALRKQLEQDVLSYQNLRKTLEE---QISEIRRREEE 621
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAE------EKKKAEELKKAEEENKIKAAEEAKKAEEdkkKAEEAKKAEED 1686
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
264-470 |
1.28e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.56 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 264 AAPREEKERETEAAQ---MEHQKERNSFEERIQALEEDLREKEREIAtekknslKRDKAIQGLTMALKSKEKKVEELNSE 340
Cdd:COG4942 19 ADAAAEAEAELEQLQqeiAELEKELAALKKEEKALLKQLAALERRIA-------ALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 341 IEKLSAAFAKAREALQK-AQTQEFQGSEDYETALSGKEALSAALRSQNLTKSTENHR------LRRSIKKITQELSDLQQ 413
Cdd:COG4942 92 IAELRAELEAQKEELAElLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARreqaeeLRADLAELAALRAELEA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 58535453 414 ERERLEKDLEEAHREKSKgdctIRDLRNEVEKLRNEVNEREKAMENRYKSLLSESNK 470
Cdd:COG4942 172 ERAELEALLAELEEERAA----LEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
290-601 |
2.70e-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: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 290 ERIQALEEDLREKEREIATEKKNSLKRDKA-----IQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQ 364
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEeleaeLEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 365 GSEDYETALSGKEAL---SAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREkskgdctIRDLRN 441
Cdd:COG1196 293 LLAELARLEQDIARLeerRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE-------LAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 442 EVEKLRNEVNEREKAMENRYKSLLSESNKKLhNQEQVIKHLTESTNQKDVLLQKFNEKDLEVIQQncylmAAEDLELRSE 521
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEA-----LAELEEEEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 522 GLITEKcssqqppgsktifSKEKKQSSDYEELIQVLKKEQDIYTHLVKSLQESDSINNLQAELNKIFALRKQLEQDVLSY 601
Cdd:COG1196 440 EEEALE-------------EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
59-621 |
8.58e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.93 E-value: 8.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 59 NMKDFENQITELKKENFNLKLRIYFLEERMQQefhgpTEHIYKTNIELKVEVESLKRELQEREQLLIKASKAVESLAEag 138
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIKR-----TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEK-- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 139 gsEIQRVKEDARKKVQqvedlLTKRILLLEKDVTAaqaelekafagtetekalrlrLESKLSEMKKMHEGDLAMALVLDE 218
Cdd:PRK03918 229 --EVKELEELKEEIEE-----LEKELESLEGSKRK---------------------LEEKIRELEERIEELKKEIEELEE 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 219 KDRLIEELKLSLKSKEALIQCLKEEKSQMACPDENVS--SGELRGLCA--APREEKERETEaaqmEHQKERNSFEERIQA 294
Cdd:PRK03918 281 KVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSrlEEEINGIEEriKELEEKEERLE----ELKKKLKELEKRLEE 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 295 LEEDLREKEReiATEKKNSLKRDKA------IQGLTMALKSKEKKVEELNSEIEKLSAAFA--KAREALQKAQTQEFQGS 366
Cdd:PRK03918 357 LEERHELYEE--AKAKKEELERLKKrltgltPEKLEKELEELEKAKEEIEEEISKITARIGelKKEIKELKKAIEELKKA 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 367 EDyETALSGKEaLSAALRSQNLTKST-ENHRLRRSIKKITQELSDLQQERERLEKDLEEAHR---EKSKGDcTIRDLRNE 442
Cdd:PRK03918 435 KG-KCPVCGRE-LTEEHRKELLEEYTaELKRIEKELKEIEEKERKLRKELRELEKVLKKESElikLKELAE-QLKELEEK 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 443 VEKLRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFNEKDLEVIQQNCYLmaaEDLELRSEG 522
Cdd:PRK03918 512 LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL---EELGFESVE 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 523 LITEKCSSQQPPGSKtiFSKEKKQSSDYEELIQVLKKEQDiythlvkslQESDSINNLQAELNKIFALRKQLEQ-----D 597
Cdd:PRK03918 589 ELEERLKELEPFYNE--YLELKDAEKELEREEKELKKLEE---------ELDKAFEELAETEKRLEELRKELEElekkyS 657
|
570 580
....*....|....*....|....
gi 58535453 598 VLSYQNLRKTLEEQISEIRRREEE 621
Cdd:PRK03918 658 EEEYEELREEYLELSRELAGLRAE 681
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
59-616 |
1.41e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.54 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 59 NMKDFENQITELKKENFNLKLRIYFLEERMQQ---EFHGPTEHIYKTNIE---LKVEVESLKREL----QEREQLLIKAS 128
Cdd:TIGR02168 352 ELESLEAELEELEAELEELESRLEELEEQLETlrsKVAQLELQIASLNNEierLEARLERLEDRRerlqQEIEELLKKLE 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 129 KAVESLAEAGGSEIQRVKEDARKK---VQQVEDLLTKRILLLEKDVTAAQAELEKAFAGTETEKALRLRLESK----LSE 201
Cdd:TIGR02168 432 EAELKELQAELEELEEELEELQEElerLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFsegvKAL 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 202 MKKMHEGDLAMALVL-----DEKDRLIEELKL----------SLKSKEALIQCLKEEKSQMA--CPDENVSSGELRGLCA 264
Cdd:TIGR02168 512 LKNQSGLSGILGVLSelisvDEGYEAAIEAALggrlqavvveNLNAAKKAIAFLKQNELGRVtfLPLDSIKGTEIQGNDR 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 265 APREEKERETEAAqMEHQKERNSFE-------------ERIQALEEDLREKERE--IATEKKNSLKRDKAIQG----LTM 325
Cdd:TIGR02168 592 EILKNIEGFLGVA-KDLVKFDPKLRkalsyllggvlvvDDLDNALELAKKLRPGyrIVTLDGDLVRPGGVITGgsakTNS 670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 326 ALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETALSGKEALSAALRSQNLTKStenhRLRRSIKKIT 405
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA----RLEAEVEQLE 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 406 QELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMEN---RYKSL---LSESNKKLHNQEQVI 479
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlreALDELraeLTLLNEEAANLRERL 826
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 480 KHLTESTNQKdvllqkfnEKDLEVIQQNcylmaAEDLELRSEGLITEKCSSQQPPgsKTIFSKEKKQSSDYEELIQVLKK 559
Cdd:TIGR02168 827 ESLERRIAAT--------ERRLEDLEEQ-----IEELSEDIESLAAEIEELEELI--EELESELEALLNERASLEEALAL 891
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 58535453 560 EQDIYTHLVKSLQESDsiNNLQAELNKIFALRKQLEQDVLSYQNLRKTLEEQISEIR 616
Cdd:TIGR02168 892 LRSELEELSEELRELE--SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
59-484 |
4.11e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 59 NMKDFENQITELKKENFNLKLRIYFLEERMQQ-EFHGPTEHIYKTNIELKVEVESLKRELQEREQLLIKASKAVESLAEA 137
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELEEKVKElKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 138 GGSEIQRVKEDARKKVQQVEDL--LTKRILLLEkDVTAAQAELE---KAFAGTETEKalrlrLESKLSEMKKMHEgdlAM 212
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLeeLEERHELYE-EAKAKKEELErlkKRLTGLTPEK-----LEKELEELEKAKE---EI 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 213 ALVLDEKDRLIEELKLSLKSKEALIQCLKEEKSQmaCPdenvssgelrgLCAAPREEKERETEAAqmEHQKERNSFEERI 292
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEELKKAKGK--CP-----------VCGRELTEEHRKELLE--EYTAELKRIEKEL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 293 QALEEDLREKEREIATEKKNSLKRDKAIQGLTMA--LKSKEKKVEELNSE-IEKLSAAFAKAREALQKAQTQ------EF 363
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKKESELIKLKELAeqLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEikslkkEL 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 364 QGSEDYEtalSGKEALSAALRSQNLTKSTENHRLRR------------------------SIKKITQELSDLQQERERLE 419
Cdd:PRK03918 549 EKLEELK---KKLAELEKKLDELEEELAELLKELEElgfesveeleerlkelepfyneylELKDAEKELEREEKELKKLE 625
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58535453 420 KDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNERE-KAMENRYKSLLSESNKKLHNQEQVIKHLTE 484
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREE 691
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
97-681 |
1.49e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 97 EHIYKTNIELKVEVESLKRELQEreqlLIKASKAVESLAEAGGSEIQRVKEDARKkvqqvedlLTKRILLLEKDVTAAQA 176
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEK----FIKRTENIEELIKEKEKELEEVLREINE--------ISSELPELREELEKLEK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 177 ELEKAFAGTETEKALRLRLESKLSEMKKMHEgdlamalVLDEKDRLIEELKLSLKSKEALIQCLKEEKsqmacpdenvss 256
Cdd:PRK03918 229 EVKELEELKEEIEELEKELESLEGSKRKLEE-------KIRELEERIEELKKEIEELEEKVKELKELK------------ 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 257 gelrglcaaPREEKERETEAAQMEHQKERNSFEERIQALEEDLREKEREI--ATEKKNSLKRdkaiqgltmaLKSKEKKV 334
Cdd:PRK03918 290 ---------EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIkeLEEKEERLEE----------LKKKLKEL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 335 EELNSEIEKLSAAFAKAREALQKAqtqefqgsEDYETALSGKEALSAALRSQNLTKSTEnhRLRRSIKKITQELSDLQQE 414
Cdd:PRK03918 351 EKRLEELEERHELYEEAKAKKEEL--------ERLKKRLTGLTPEKLEKELEELEKAKE--EIEEEISKITARIGELKKE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 415 RERLEKDLEEAhrEKSKGDCTI--RDLRNE-----VEKLRNEVNEREKAMEnRYKSLLSESNKKLHNQEQVIKHLTESTN 487
Cdd:PRK03918 421 IKELKKAIEEL--KKAKGKCPVcgRELTEEhrkelLEEYTAELKRIEKELK-EIEEKERKLRKELRELEKVLKKESELIK 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 488 QKDVL---------LQKFNEKDLEVIQQNCYLMAAEDLELRSEGLITEKCSSQQPPGSKTIFSKEKKQSSDYEELIQVLK 558
Cdd:PRK03918 498 LKELAeqlkeleekLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLK 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 559 KEQDIYTHLVKSLQEsdSINNLQAELNKIFALrKQLEQDVLSYQNLRKTLEEQISEIRRREEESFSLYSDQTSYLSiclE 638
Cdd:PRK03918 578 ELEELGFESVEELEE--RLKELEPFYNEYLEL-KDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE---E 651
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 58535453 639 ENNRFQVEHFSQ-----EELKKKVSDLIQLVKELYTDNQHLKKTIFDL 681
Cdd:PRK03918 652 LEKKYSEEEYEElreeyLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
268-523 |
1.81e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 268 EEKERETEAAQMEHQKERNSFEERIQALEEDL-------REKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSE 340
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLeelrlevSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 341 IEKLSAAF---------AKAREALQKAQTQEFQGS-EDYETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSD 410
Cdd:TIGR02168 318 LEELEAQLeeleskldeLAEELAELEEKLEELKEElESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 411 LQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMENRyksllsESNKKLHNQEQVIKHLTESTNQKD 490
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEE------ELEELQEELERLEEALEELREELE 471
|
250 260 270
....*....|....*....|....*....|...
gi 58535453 491 VLLQKFNEKDLEVIQQNCYLMAAEDLELRSEGL 523
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQENLEGF 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
218-562 |
2.53e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 218 EKDRLiEELKLSLKSKEALIQCLKEEKSQMacpdENVSSGELRGLCAAPREEKERETEAAQMEhqKERNSFEERIQALEE 297
Cdd:TIGR02169 672 EPAEL-QRLRERLEGLKRELSSLQSELRRI----ENRLDELSQELSDASRKIGEIEKEIEQLE--QEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 298 DLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEEL-----NSEIEKLSAAFAKAREALQKAQTQefqgSEDYETA 372
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEAR----LREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 373 LSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREkskgdctIRDLRNEVEKLRNEVNE 452
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA-------LRDLESRLGDLKKERDE 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 453 REK---AMENRYKSLLSESNKKLHNQEQvikhLTESTNQKDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEGlITEKCS 529
Cdd:TIGR02169 894 LEAqlrELERKIEELEAQIEKKRKRLSE----LKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQR-VEEEIR 968
|
330 340 350
....*....|....*....|....*....|....*
gi 58535453 530 SQQPPGSKTI--FSKEKKQSSDYEELIQVLKKEQD 562
Cdd:TIGR02169 969 ALEPVNMLAIqeYEEVLKRLDELKEKRAKLEEERK 1003
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
141-429 |
4.83e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 58.21 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 141 EIQRVKEDARKKVQQVEdlltkRILLLEKDVTAAQAELEKAFA--------GTETEKAL-RLRLESKLSEMKKMHEGDLA 211
Cdd:pfam17380 297 EQERLRQEKEEKAREVE-----RRRKLEEAEKARQAEMDRQAAiyaeqermAMERERELeRIRQEERKRELERIRQEEIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 212 MALV-LDEKDRLIEE-----------------LKLSLKSKEALIQCLKEEKSQMACPDENVSSGELRGLcaapREEKERE 273
Cdd:pfam17380 372 MEISrMRELERLQMErqqknervrqeleaarkVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRL----EEERARE 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 274 TEAAQMEHQkERNSFEERIQALEEDLREKEREIATEKKnslKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKARE 353
Cdd:pfam17380 448 MERVRLEEQ-ERQQQVERLRQQEEERKRKKLELEKEKR---DRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEME 523
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58535453 354 ALQKAQTQEFQGSEDYETALSGKEAlsaalrsqnltksTENHRLRRSIKKITQELSDL---QQERERLEKDLEEAHREK 429
Cdd:pfam17380 524 ERQKAIYEEERRREAEEERRKQQEM-------------EERRRIQEQMRKATEERSRLeamEREREMMRQIVESEKARA 589
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
116-680 |
6.70e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 57.75 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 116 ELQEREQLLIKASKAVESLAEAGGSEIQRVKEDARKKVQQVEDLL---------TKRILLLEKDVTAAQAELEKA--FAG 184
Cdd:TIGR00606 416 DLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIkelqqlegsSDRILELDQELRKAERELSKAekNSL 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 185 TETEKALRLRLES-KLSEMKKMHEGDLAMALVLDEKDRLIEELKLSlKSKEALIQCLKEEKSQmacpdenvSSGELRGLC 263
Cdd:TIGR00606 496 TETLKKEVKSLQNeKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLT-KDKMDKDEQIRKIKSR--------HSDELTSLL 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 264 AAPREEKEREteaaqmehqKERNSFEERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEiEK 343
Cdd:TIGR00606 567 GYFPNKKQLE---------DWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QD 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 344 LSAAFAKAREALQKAQTQefqgsedyETALSGKEALSAALRSQNLTKSTE----NHRLRRSIKKITQELSDLQQERERLE 419
Cdd:TIGR00606 637 EESDLERLKEEIEKSSKQ--------RAMLAGATAVYSQFITQLTDENQSccpvCQRVFQTEAELQEFISDLQSKLRLAP 708
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 420 KDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAmenrykslLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFNEK 499
Cdd:TIGR00606 709 DKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKE--------IPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPE 780
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 500 ---------DLEVIQQncYLMAAEDLELRSEGLITEkcsSQQPPGSKTIFSKEKKQSSDYEELIQVLKKEQDiythLVKS 570
Cdd:TIGR00606 781 eesakvcltDVTIMER--FQMELKDVERKIAQQAAK---LQGSDLDRTVQQVNQEKQEKQHELDTVVSKIEL----NRKL 851
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 571 LQE-SDSINNLQAELNKIFALRKQLEQDVLSYQNLRKTLEEQISEIRRREEEsFSLYSDQTSYLSICLEENNRFQVEHFS 649
Cdd:TIGR00606 852 IQDqQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIRE-IKDAKEQDSPLETFLEKDQQEKEELIS 930
|
570 580 590
....*....|....*....|....*....|..
gi 58535453 650 -QEELKKKVSDLIQLVKELYTDNQHLKKTIFD 680
Cdd:TIGR00606 931 sKETSNKKAQDKVNDIKEKVKNIHGYMKDIEN 962
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
56-474 |
2.06e-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: 56.22 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 56 RARNMKDFENQITELKKENFNLKLRIYFLE---ERMQQEFHGPTEHIYKTNIELKVEVESLKRELQEREQLL-------- 124
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRkelEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEeriaqlsk 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 125 -IKASKAVESLAEAGGSEIQRVKEDARKKVQQVEDLLTK---RILLLEKDVTAAQAELekafagtETEKALRLRLESKLS 200
Cdd:TIGR02168 755 eLTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDELRAEL-------TLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 201 EMKKMHEgdlamalvldEKDRLIEELKLSLKSKEALIQCLKEEKSQmacpdenvssgelrglCAAPREEKERETEaaqmE 280
Cdd:TIGR02168 828 SLERRIA----------ATERRLEDLEEQIEELSEDIESLAAEIEE----------------LEELIEELESELE----A 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 281 HQKERNSFEERIQALEEDLREKEREIatekknslkrdkaiqgltmalKSKEKKVEELNSEIEKLSAAFAKAREALQKAQT 360
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEEL---------------------RELESKRSELRRELEELREKLAQLELRLEGLEV 936
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 361 --QEFQG--SEDYETALSGKEALSAALrsqnltkSTENHRLRRSIKKITQELSDL-----------QQERERLEKDLEEa 425
Cdd:TIGR02168 937 riDNLQErlSEEYSLTLEEAEALENKI-------EDDEEEARRRLKRLENKIKELgpvnlaaieeyEELKERYDFLTAQ- 1008
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 58535453 426 hrekskgdctIRDLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHN 474
Cdd:TIGR02168 1009 ----------KEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQR 1047
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
268-458 |
3.66e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 268 EEKERETEAAQMEHQKERNSFEERIQALEEDLrekerEIATEKKNSLKrdKAIQGLTMALKSKEKKVEELNSEIEKLSAA 347
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAEL-----EELNEEYNELQ--AELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 348 FAKAREALQKAQTQ-----EFQGSEDYETALSGKEALSAALRSQNltksTENHRLRRSIKKITQELSDLQQERERLEKDL 422
Cdd:COG3883 88 LGERARALYRSGGSvsyldVLLGSESFSDFLDRLSALSKIADADA----DLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 58535453 423 EEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAME 458
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
64-586 |
4.46e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.03 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 64 ENQITELKKENFNLKLRIYFLEERMQQ--EFHGPTEHIYKTNIELKVEVESLKRELQEREQLLIKASKAVESLAEaggsE 141
Cdd:TIGR04523 186 QKNIDKIKNKLLKLELLLSNLKKKIQKnkSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKD----E 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 142 IQRVKEDARKKVQQVEDLlTKRILLLEKDVTaaqaelekafagtetekalrlRLESKLSEMKKMHEGDLAMAL--VLDEK 219
Cdd:TIGR04523 262 QNKIKKQLSEKQKELEQN-NKKIKELEKQLN---------------------QLKSEISDLNNQKEQDWNKELksELKNQ 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 220 DRLIEELKLSLKSKEALIQCLKEEKSQMACPDENVSSGELRglcaAPREEKERETEAAQMEhqKERNSFEERIQALEEDL 299
Cdd:TIGR04523 320 EKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSE----KQRELEEKQNEIEKLK--KENQSYKQEIKNLESQI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 300 REKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKlsaafakarealQKAQTQEFQgSEDYETALSGKEaL 379
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK------------NNSEIKDLT-NQDSVKELIIKN-L 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 380 SAALRSQNLTKSTenhrLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDL-------RNEVEKLRNEVNE 452
Cdd:TIGR04523 460 DNTRESLETQLKV----LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLtkkisslKEKIEKLESEKKE 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 453 REKAMENRYKSLLS-ESNKKLHNQEQVI----KHLTESTNQKDVLLQKFNEKDLEVIQQncylmAAEDLELRSEGLITEK 527
Cdd:TIGR04523 536 KESKISDLEDELNKdDFELKKENLEKEIdeknKEIEELKQTQKSLKKKQEEKQELIDQK-----EKEKKDLIKEIEEKEK 610
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 528 CSSQQppgsKTIFSKEKKQSSDYEELIQVLKKEQDIYTHLVKSLQES-DSINNLQAELNK 586
Cdd:TIGR04523 611 KISSL----EKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETiKEIRNKWPEIIK 666
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
210-431 |
7.57e-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: 53.61 E-value: 7.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 210 LAMALVLDEKDRLIEELKLSLKSKEALIQCLKEEKSQMAcpdenvssGELRGLcaaprEEKERETEAAQMEHQKERNSFE 289
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALL--------KQLAAL-----ERRIAALARRIRALEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 290 ERIQALEEDLREKEREIATEKKNSLKRDKAIQ------GLTMALKSKE--------KKVEELNSEIEKLSAAFAKAREAL 355
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAELLRALYrlgrqpPLALLLSPEDfldavrrlQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58535453 356 QKAQTQEFQGSEDYETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSK 431
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
267-471 |
8.05e-07 |
|
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: 53.97 E-value: 8.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 267 REEKERETE----------AAQMEHQKERNSFEERIQALEEDLREKEREIATEKKNSLKRDKAiQGLTMALkSKEKKVEE 336
Cdd:pfam17380 305 KEEKAREVErrrkleeaekARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQ-EEIAMEI-SRMRELER 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 337 LNSEIEKLSAafaKAREALQKAQTQEFQGSEDYETALSGKEALSAALRSQNLTKSTENHRLR----RSIKKITQELSDLQ 412
Cdd:pfam17380 383 LQMERQQKNE---RVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEeeraREMERVRLEEQERQ 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 58535453 413 QERERLEKDLEEAHREKSKGDCTIRDlRNEVEKLRNEVNEREkaMENRYKSLLSESNKK 471
Cdd:pfam17380 460 QQVERLRQQEEERKRKKLELEKEKRD-RKRAEEQRRKILEKE--LEERKQAMIEEERKR 515
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
142-458 |
1.45e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 142 IQRVKEDARKKVQQVEDL--------LTKRILLLEKDVTAAQAELEKAFAGTETEKALRLRLESKLSEMKKMHE------ 207
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQieekeekdLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREeletle 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 208 ---GDLAMALVLDEKDRliEELKLSLKSKEALIQCLKEEKSQMAcPDENVSSGELRGLcAAPREEKERETEAAQMEHQKE 284
Cdd:PRK02224 258 aeiEDLRETIAETERER--EELAEEVRDLRERLEELEEERDDLL-AEAGLDDADAEAV-EARREELEDRDEELRDRLEEC 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 285 RNS---FEERIQALEEDLREKEREiATEKKNSLKR-DKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQT 360
Cdd:PRK02224 334 RVAaqaHNEEAESLREDADDLEER-AEELREEAAElESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAED 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 361 QEFQGSEDYEtALSGKEA-LSAALRS---------------------QNLTKSTENHRL---RRSIKKITQELSDLQQER 415
Cdd:PRK02224 413 FLEELREERD-ELREREAeLEATLRTarerveeaealleagkcpecgQPVEGSPHVETIeedRERVEELEAELEDLEEEV 491
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 58535453 416 ERLEKDLEEAH--REKSKGDCTIRDLRNEVEKL----RNEVNEREKAME 458
Cdd:PRK02224 492 EEVEERLERAEdlVEAEDRIERLEERREDLEELiaerRETIEEKRERAE 540
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
119-403 |
2.35e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 119 EREQLLIKASKAVESLAEAggSEIQRVKEDARKKVQQVEDLLtkrilllekdvtAAQAELEKAFAGTETEKALRLRLESK 198
Cdd:COG4913 219 EEPDTFEAADALVEHFDDL--ERAHEALEDAREQIELLEPIR------------ELAERYAAARERLAELEYLRAALRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 199 LSEMKkmhegdlamalvLDEKDRLIEELKLSLKSKEALIQCLKEEKSQMacpdenvssgelrglcaaprEEKERETEAAQ 278
Cdd:COG4913 285 FAQRR------------LELLEAELEELRAELARLEAELERLEARLDAL--------------------REELDELEAQI 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 279 MEHQKERnsfeerIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKA 358
Cdd:COG4913 333 RGNGGDR------LEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA 406
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 58535453 359 QTQEFQGSEDYETALSGKEALSAALRSQNLTKSTENHRLRRSIKK 403
Cdd:COG4913 407 LAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAE 451
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
84-423 |
2.35e-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: 52.76 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 84 LEERMQQEFHGPTEHIYKTNIELKVEVESLKRELQEREQLLIKASKAVESLAE--AGGSEIQRVKEDARKKVQQVEdllt 161
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEleEDLSSLEQEIENVKSELKELE---- 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 162 KRILLLEKDVTAAQAELEKafagtetekalrlrLESKLSEMKkmhegdlamalvLDEKDRLIEELKLSLKSKEALIQCLK 241
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALND--------------LEARLSHSR------------IPEIQAELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 242 EEksqmacpdENVSSGELRGLcaapreEKERETEAAQMEHQKER-NSFEERIQALEEDLREKEREIAtEKKNslkrdkai 320
Cdd:TIGR02169 819 QK--------LNRLTLEKEYL------EKEIQELQEQRIDLKEQiKSIEKEIENLNGKKEELEEELE-ELEA-------- 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 321 qgltmALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETALSGKEALsaalrSQNLTKSTENHRLRRS 400
Cdd:TIGR02169 876 -----ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL-----EEELSEIEDPKGEDEE 945
|
330 340
....*....|....*....|...
gi 58535453 401 IKKITQELSDLQQERERLEKDLE 423
Cdd:TIGR02169 946 IPEEELSLEDVQAELQRVEEEIR 968
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
87-676 |
3.04e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.42 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 87 RMQQEFHGPTEHIYKTNIELKVEVESLKRELQEREQLLIKASKAVESLAeaggSEIQRVKEDARKKVQQVEDLL-----T 161
Cdd:pfam05483 78 RLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQ----FENEKVSLKLEEEIQENKDLIkennaT 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 162 KRILLLEKDVTAAQAELEKAFAGTETE-KALRLRLESKLSEMKKMHEGDLAMAlvldEKDRLieELKLSLKSKEALIQCL 240
Cdd:pfam05483 154 RHLCNLLKETCARSAEKTKKYEYEREEtRQVYMDLNNNIEKMILAFEELRVQA----ENARL--EMHFKLKEDHEKIQHL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 241 KEEKSQMACPDENVSSgeLRGLCAAPREEKERETEAAQMEHQKERNSFEERIQALEEDLREkereiATEKKNSLKrdkai 320
Cdd:pfam05483 228 EEEYKKEINDKEKQVS--LLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKE-----LIEKKDHLT----- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 321 qgltmalkskeKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETALsgkEALSAALRSQNLTKStenhRLRRS 400
Cdd:pfam05483 296 -----------KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQM---EELNKAKAAHSFVVT----EFEAT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 401 IKKITQELSDLQQERERLEKDLEEAHREKSKGDctirdlrNEVEKLRNEVNEREKAMEnRYKSLLSESNKKLHNQEQVIK 480
Cdd:pfam05483 358 TCSLEELLRTEQQRLEKNEDQLKIITMELQKKS-------SELEEMTKFKNNKEVELE-ELKKILAEDEKLLDEKKQFEK 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 481 HLTE--STNQKDVLLQKFNEK---DLEV------IQQNCYLMAAEDL--ELRSEGLITEKCSSQqppgSKTIFSKEKKQS 547
Cdd:pfam05483 430 IAEElkGKEQELIFLLQAREKeihDLEIqltaikTSEEHYLKEVEDLktELEKEKLKNIELTAH----CDKLLLENKELT 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 548 SDYEELIQVLKKEQDIYTHLVKslQESDSINNLQAELNKIFALRKQLEqdvlsyqNLRKTLEEQISEIRRREEESfslYS 627
Cdd:pfam05483 506 QEASDMTLELKKHQEDIINCKK--QEERMLKQIENLEEKEMNLRDELE-------SVREEFIQKGDEVKCKLDKS---EE 573
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 58535453 628 DQTSYLSICLEENNRFQVEHFSQEELKKKVSDLIQLVKELYTDNQHLKK 676
Cdd:pfam05483 574 NARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
290-616 |
4.26e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 290 ERIQALEEDLREKEREIatekknslkrdkaiqgLTMALKSKEKKVEELNSEIEKlsaafakarealqkAQTQEfqgsEDY 369
Cdd:TIGR02168 213 ERYKELKAELRELELAL----------------LVLRLEELREELEELQEELKE--------------AEEEL----EEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 370 ETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNE 449
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 450 VNEREKAME------NRYKSLLSESNKKLHNQEQVIKHL-TESTNQKDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEG 522
Cdd:TIGR02168 339 LAELEEKLEelkeelESLEAELEELEAELEELESRLEELeEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 523 LITEKCSSQQPPGSKtifsKEKKQSSDYEELIQVLKKEQDIYTHLVKSLQEsdsinnLQAELNKIFALRKQLEQDVLSYQ 602
Cdd:TIGR02168 419 LQQEIEELLKKLEEA----ELKELQAELEELEEELEELQEELERLEEALEE------LREELEEAEQALDAAERELAQLQ 488
|
330
....*....|....
gi 58535453 603 NLRKTLEEQISEIR 616
Cdd:TIGR02168 489 ARLDSLERLQENLE 502
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
105-452 |
4.35e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 105 ELKVEVESLKRELQEREQLLiKASKAVESLAEAGGSEIQRVKEDARKKVQQVEDLLTKrillLEKDVTAAQAELEKAFAG 184
Cdd:PRK02224 430 ELEATLRTARERVEEAEALL-EAGKCPECGQPVEGSPHVETIEEDRERVEELEAELED----LEEEVEEVEERLERAEDL 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 185 TETEKalrlRLESKLSEMKKMHEgdlamalvldekdrLIEELKLSLKSKEALIQCLKEEKSQMACPDEnvssgELRGLCA 264
Cdd:PRK02224 505 VEAED----RIERLEERREDLEE--------------LIAERRETIEEKRERAEELRERAAELEAEAE-----EKREAAA 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 265 APREEKERETEAAQmEHQKERNSFEERIQALE----------------EDLREKEREIATekKNSLKRDKaiqgltmaLK 328
Cdd:PRK02224 562 EAEEEAEEAREEVA-ELNSKLAELKERIESLErirtllaaiadaedeiERLREKREALAE--LNDERRER--------LA 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 329 SKEKKVEELNSEIEklSAAFAKAREalQKAQTQEFQgsEDYETALSGKEALSAALrsQNLTKSTENhrlrrSIKkitqEL 408
Cdd:PRK02224 631 EKRERKRELEAEFD--EARIEEARE--DKERAEEYL--EQVEEKLDELREERDDL--QAEIGAVEN-----ELE----EL 693
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 58535453 409 SDLQQERERLE---KDLEEAHREKSKGDCTIRDLRNE-----VEKLRNEVNE 452
Cdd:PRK02224 694 EELRERREALEnrvEALEALYDEAEELESMYGDLRAElrqrnVETLERMLNE 745
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
105-623 |
6.54e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 6.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 105 ELKVEVESLKRELQEREQLLIKASKAVESLAEaggsEIQRVKEDARKKVQQVEDLLTKRILLLE--KDVTAAQAELEKAF 182
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELEL----ELEEAQAEEYELLAELARLEQDIARLEErrRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 183 AGTETEKALRLRLESKLSEMKKMHEGDLAMAL--VLDEKDRLIEELKLSLKSKEALIQCLKEEKSQMAcpDENVSSGELR 260
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEaeLAEAEEALLEAEAELAEAEEELEELAEELLEALR--AAAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 261 GLcaaprEEKERETEAAQMEHQKERNSFEERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSE 340
Cdd:COG1196 404 EL-----EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 341 IEKLSAAF--AKAREALQKAQTQEFQGSEDYETALSGK------------------------EALSAALRSQNLTKSTE- 393
Cdd:COG1196 479 LAELLEELaeAAARLLLLLEAEADYEGFLEGVKAALLLaglrglagavavligveaayeaalEAALAAALQNIVVEDDEv 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 394 -----NHRLRRSIKKITQELSDLQQERERLEKDLE-------------EAHREKSKGDCTIRDLRNEVEKLRNEVNEREK 455
Cdd:COG1196 559 aaaaiEYLKAAKAGRATFLPLDKIRARAALAAALArgaigaavdlvasDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 456 AMENRYKSLLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEGLITEKCSSQQPPG 535
Cdd:COG1196 639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 536 SKTIFSKEKKQSSDYEELIQVLKKE--QDIYTHLVKSLQESDSINNLQAELNKIFALRKQL---------EQDVLS--YQ 602
Cdd:COG1196 719 EELEEEALEEQLEAEREELLEELLEeeELLEEEALEELPEPPDLEELERELERLEREIEALgpvnllaieEYEELEerYD 798
|
570 580 590
....*....|....*....|....*....|.
gi 58535453 603 NL----------RKTLEEQISEIRRREEESF 623
Cdd:COG1196 799 FLseqredleeaRETLEEAIEEIDRETRERF 829
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
129-681 |
8.09e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.06 E-value: 8.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 129 KAVESLAEAGGSEIQRVKEDARKKVQQVEDL------LTKRILLLEKDVTAAQAELEKAFAGTETEKALRLRLESKLSEM 202
Cdd:PRK01156 172 KDVIDMLRAEISNIDYLEEKLKSSNLELENIkkqiadDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMK 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 203 KKMH------EGDLAMALVLDEKDRLIEELKLSL------KSKEALIQCLK-----EEKSQMacpdenvssgeLRGLCAA 265
Cdd:PRK01156 252 NRYEseiktaESDLSMELEKNNYYKELEERHMKIindpvyKNRNYINDYFKykndiENKKQI-----------LSNIDAE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 266 PREEKERETEAAQMehQKERNSFEERiQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEI-EKL 344
Cdd:PRK01156 321 INKYHAIIKKLSVL--QKDYNDYIKK-KSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFIsEIL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 345 SAAFAKArEALQKAQTQEFQGSEDYETALSGKEALSAALRsQNLTKSTENHRLRRS------------IKKITQELSDLQ 412
Cdd:PRK01156 398 KIQEIDP-DAIKKELNEINVKLQDISSKVSSLNQRIRALR-ENLDELSRNMEMLNGqsvcpvcgttlgEEKSNHIINHYN 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 413 QERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMENRYKSLLSEsnkkLHNQEQVIKHLTESTNQKDVL 492
Cdd:PRK01156 476 EKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARAD----LEDIKIKINELKDKHDKYEEI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 493 LQKFNEKDLeviqqncylmaaEDLELRSEGLIT--EKCSSQQPPGSKTIFSKEKKQSSDYEELIQVLKKE-QDIYTHLVK 569
Cdd:PRK01156 552 KNRYKSLKL------------EDLDSKRTSWLNalAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGfPDDKSYIDK 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 570 SLQE-SDSINNLQAELNKIFALRKQLEqdvlsyqnlrkTLEEQISEIRRREEESFSLYSDQTSYLSICLEENNRFQVEHF 648
Cdd:PRK01156 620 SIREiENEANNLNNKYNEIQENKILIE-----------KLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRK 688
|
570 580 590
....*....|....*....|....*....|...
gi 58535453 649 SQEELKKKVSDLIQLVKELYTDNQHLKKTIFDL 681
Cdd:PRK01156 689 ALDDAKANRARLESTIEILRTRINELSDRINDI 721
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
215-621 |
1.12e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 215 VLDEKDRLIEELKLSLKSKEA--LIQCLKEEKSQMACPDENVSSGELRGLCAAPREEKERETEAAQMEHQKERNSFEERI 292
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEEKEEkdLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 293 QALEEDLREKEREiatekKNSLKRdkAIQGLTMALKSKEKKVEELNSEIEKLSA---AFAKAREALQKAQTQEFQGSEDY 369
Cdd:PRK02224 261 EDLRETIAETERE-----REELAE--EVRDLRERLEELEEERDDLLAEAGLDDAdaeAVEARREELEDRDEELRDRLEEC 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 370 ETALSgkealsaalrsqnlTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNE 449
Cdd:PRK02224 334 RVAAQ--------------AHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 450 VNEREKAMEN--RYKSLLSESNKKLHNQEqvikhltestnqkdvllqkfneKDLEVIQQNCYLMAAEDLELRSEGliteK 527
Cdd:PRK02224 400 FGDAPVDLGNaeDFLEELREERDELRERE----------------------AELEATLRTARERVEEAEALLEAG----K 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 528 CSS--QQPPGSKTIFSKEkkqssDYEELIQVLKKEQDiythlvkslQESDSINNLQAELNKIFALRKqLEQDVLSYQNLR 605
Cdd:PRK02224 454 CPEcgQPVEGSPHVETIE-----EDRERVEELEAELE---------DLEEEVEEVEERLERAEDLVE-AEDRIERLEERR 518
|
410
....*....|....*.
gi 58535453 606 KTLEEQISEIRRREEE 621
Cdd:PRK02224 519 EDLEELIAERRETIEE 534
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
78-639 |
1.21e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.43 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 78 KLRIYFLEERMQQEFHGPTEHIYKTNIELKVEVESLKRELQEREQLLIKASKAVESLAEAGGSEIQRVkEDARKKVQQVE 157
Cdd:TIGR00606 190 TLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEI-EHNLSKIMKLD 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 158 DLLT---KRILLLEKDVTAAQAELEKAFAGTETE---------KALRLRLESKLSEMKKMHEGDLAMALVLDEKDRLIEE 225
Cdd:TIGR00606 269 NEIKalkSRKKQMEKDNSELELKMEKVFQGTDEQlndlyhnhqRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 226 L-KLSLKSKEALIQCLKEEKSQMacpdENVSSGELRGLCAAPREEKERETeaaQMEHQKERNSFEER-IQALEEDLREKE 303
Cdd:TIGR00606 349 QgRLQLQADRHQEHIRARDSLIQ----SLATRLELDGFERGPFSERQIKN---FHTLVIERQEDEAKtAAQLCADLQSKE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 304 ReIATEKKNSLKRDKAIQGLTMALKSK--EKKVEELNSEIEKLSAAFAKAREALQKaqTQEFQGSEDyETALSGKEALSA 381
Cdd:TIGR00606 422 R-LKQEQADEIRDEKKGLGRTIELKKEilEKKQEELKFVIKELQQLEGSSDRILEL--DQELRKAER-ELSKAEKNSLTE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 382 ALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLeKDLEEAHREKSKGDCTIRD---------------------LR 440
Cdd:TIGR00606 498 TLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTR-TQMEMLTKDKMDKDEQIRKiksrhsdeltsllgyfpnkkqLE 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 441 NEVEKLRNEVNErekaMENRykslLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFNEKDLEVIqqncylmAAEDLELRS 520
Cdd:TIGR00606 577 DWLHSKSKEINQ----TRDR----LAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVC-------GSQDEESDL 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 521 EGLIT--EKCSSQQPPGSktifskekKQSSDYEELIQVLKKEQDIYTHLVkslqesDSINNLQAELNKIFalrKQLEQDV 598
Cdd:TIGR00606 642 ERLKEeiEKSSKQRAMLA--------GATAVYSQFITQLTDENQSCCPVC------QRVFQTEAELQEFI---SDLQSKL 704
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 58535453 599 LSYQNLRKTLEEQISEIRRREEESFSLYSDQTSYLSICLEE 639
Cdd:TIGR00606 705 RLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKE 745
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
105-366 |
1.40e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 105 ELKVEVESLKRELQEREQLLIKASKAVESLAEaggsEIQRVkEDARKKVQQVEDLLTKRILLLEKDVTAAQAELEKAfag 184
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLK----QLAAL-ERRIAALARRIRALEQELAALEAELAELEKEIAEL--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 185 TETEKALRLRLESKLSEMKKMHEGDLAMALV----LDEKDRLIEELKLSLKSKEALIQCLKEEKSQMacpdenvssgelr 260
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLALLLspedFLDAVRRLQYLKYLAPARREQAEELRADLAEL------------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 261 glcaaprEEKERETEAAQMEHQKERNSFEERIQALEEDLREKEREIATEKKNSLKRDKAIQGLtmalkskEKKVEELNSE 340
Cdd:COG4942 163 -------AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL-------QQEAEELEAL 228
|
250 260
....*....|....*....|....*.
gi 58535453 341 IEKLSAAFAKAREALQKAQTQEFQGS 366
Cdd:COG4942 229 IARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
299-494 |
1.70e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 48.99 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 299 LREKEREIATEKKNSLKRD-KAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYEtalsgke 377
Cdd:pfam09787 20 LQSKEKLIASLKEGSGVEGlDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSR------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 378 alsaalrsQNLTKSTENHRLRRSIKKITQ-ELSDLQQERERLEkdlEEAHREKSKGDCTIRDLRNEVEKLRNEVNEreka 456
Cdd:pfam09787 93 --------EQLQELEEQLATERSARREAEaELERLQEELRYLE---EELRRSKATLQSRIKDREAEIEKLRNQLTS---- 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 58535453 457 menryKSLLSESNKKLhnqEQVIKHLTESTNQKDVLLQ 494
Cdd:pfam09787 158 -----KSQSSSSQSEL---ENRLHQLTETLIQKQTMLE 187
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
56-666 |
1.73e-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: 49.63 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 56 RARNMKDFENQITELKKENFNLKLRIYFLEERMQQefhgPTEHIYKTNIELK----------VEVESLKRELQEREQLLI 125
Cdd:TIGR04523 66 DEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINK----LNSDLSKINSEIKndkeqknkleVELNKLEKQKKENKKNID 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 126 KASKAVESLaEAGGSEIQRVKEDARKKVQQVEDLLTKrillLEKDVTAAQAELEKAfagteteKALRLRLESKLSEMKKm 205
Cdd:TIGR04523 142 KFLTEIKKK-EKELEKLNNKYNDLKKQKEELENELNL----LEKEKLNIQKNIDKI-------KNKLLKLELLLSNLKK- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 206 hegdlamalvLDEKDRLIEELKLSLKSKEALIQCLKEEKSQMACPDENVSSGELRGLCAAPREEKERETEAAqmEHQKER 285
Cdd:TIGR04523 209 ----------KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS--EKQKEL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 286 NSFEERIQALEEDLREKEREIatEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQtQEFQG 365
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEI--SDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLK-KELTN 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 366 SE----DYETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRN 441
Cdd:TIGR04523 354 SEsensEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKE 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 442 EVEKLRNEVNEREK---AMENRYKSLlsesNKKLHNQEQVIKHLTESTNQkdvllqkfNEKDLEVIQQNCYLMAAEDLEL 518
Cdd:TIGR04523 434 TIIKNNSEIKDLTNqdsVKELIIKNL----DNTRESLETQLKVLSRSINK--------IKQNLEQKQKELKSKEKELKKL 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 519 RSEGLITEKCSSQQPPGSKTIFSKEKKQSSDYEELIQVLKKEQD----IYTHLVKSLQEsDSINNLQAELNKIFALRKQL 594
Cdd:TIGR04523 502 NEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDelnkDDFELKKENLE-KEIDEKNKEIEELKQTQKSL 580
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 58535453 595 EQDVLSYQNLRKTLEEQISEIRRREEESFSLYSDQTSYLSICLEENNRFQVEHFSQEELKKKVSDLIQLVKE 666
Cdd:TIGR04523 581 KKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKE 652
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
78-666 |
2.01e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.72 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 78 KLRIYFLEERMQQEFHGPTEHIYKTNIElkvevESLKRELQEREQ----LLIKASKAveslaEAGGSEIQRVKEDARKKV 153
Cdd:pfam05483 201 ELRVQAENARLEMHFKLKEDHEKIQHLE-----EEYKKEINDKEKqvslLLIQITEK-----ENKMKDLTFLLEESRDKA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 154 QQVEDlltkRILLLEKDVtaaQAELEKAFAGTETEKALRLRLESKLSEMKKMHEgDLAMAL-----VLDEKDRLIEELKl 228
Cdd:pfam05483 271 NQLEE----KTKLQDENL---KELIEKKDHLTKELEDIKMSLQRSMSTQKALEE-DLQIATkticqLTEEKEAQMEELN- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 229 slKSKEALIQCLKEEKSQMACPDENVSSGELRglcaapREEKERETEAAQMEHQKERNSFEE--RIQALEEDLREKEREI 306
Cdd:pfam05483 342 --KAKAAHSFVVTEFEATTCSLEELLRTEQQR------LEKNEDQLKIITMELQKKSSELEEmtKFKNNKEVELEELKKI 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 307 ATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETALSGKEALSAALRSQ 386
Cdd:pfam05483 414 LAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAH 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 387 NLTKSTENhrlrrsiKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMENRYKSLLS 466
Cdd:pfam05483 494 CDKLLLEN-------KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKC 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 467 ESNKKLHNQEQVIKHLTESTNQKDVLLQKFN--EKDLEVIQQNCYLMAAEDLELRSEGLITEKCSSQQPPGSKTIFSKEK 544
Cdd:pfam05483 567 KLDKSEENARSIEYEVLKKEKQMKILENKCNnlKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELA 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 545 KQSSDYEELIQVLKK--------EQDIYTHLVKSLQESDSINNLQAELN-----KIFALRKQLEQDVLSYQNLRKTLEEQ 611
Cdd:pfam05483 647 SAKQKFEEIIDNYQKeiedkkisEEKLLEEVEKAKAIADEAVKLQKEIDkrcqhKIAEMVALMEKHKHQYDKIIEERDSE 726
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 58535453 612 ISEIRRREEESFSLYSDQTSYLSICLEE----NNRFQVEHFSQEELKKKVSDLIQLVKE 666
Cdd:pfam05483 727 LGLYKNKEQEQSSAKAALEIELSNIKAEllslKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
105-346 |
2.44e-05 |
|
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: 49.30 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 105 ELKVEVESLKRELQEREQLLIKASKAVESLaeaGGSEIQRVKEDARKkvqqvedlLTKRILLLEKDVTAAQAELEKAfag 184
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKIKDL---GEEEQLRVKEKIGE--------LEAEIASLERSIAEKERELEDA--- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 185 TETEKALRLRLESKLSEMKKMhEGDLAMALVldEKDRLIEELKLSLKSKEALIQCLKEEKSQMACPDENVSS-------- 256
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEEL-EREIEEERK--RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDyreklekl 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 257 ----GELRGLCAAPREEKERETEA-AQMEHQKER-----NSFEERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMA 326
Cdd:TIGR02169 398 kreiNELKRELDRLQEELQRLSEElADLNAAIAGieakiNELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
250 260
....*....|....*....|
gi 58535453 327 LKSKEKKVEELNSEIEKLSA 346
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEA 497
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
216-619 |
2.45e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.66 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 216 LDEKDRLIEELKLSLKSKEALIQCLKEEKSQMACPDENVSSGELRGLCAAPREEKERETEAAQMEHQKERNSFEERIQAL 295
Cdd:TIGR00606 718 LKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERF 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 296 EEDLREKEREIATE--KKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQ-GSEdyETA 372
Cdd:TIGR00606 798 QMELKDVERKIAQQaaKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNElKSE--KLQ 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 373 LSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQErerLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNE 452
Cdd:TIGR00606 876 IGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETF---LEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKN 952
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 453 REKAMENRYKSLLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFNekdleviqqncylmaaEDLELRSEGLITEKCSSQQ 532
Cdd:TIGR00606 953 IHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKIN----------------EDMRLMRQDIDTQKIQERW 1016
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 533 PPGSKTIFSKEKKQSSDYEELIQVLKK-EQDIYTHLVKSLQE-SDSINNLQAELNKIFALRKQLEQDVLSYQNLRKTLEE 610
Cdd:TIGR00606 1017 LQDNLTLRKRENELKEVEEELKQHLKEmGQMQVLQMKQEHQKlEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQF 1096
|
....*....
gi 58535453 611 QISEIRRRE 619
Cdd:TIGR00606 1097 RDAEEKYRE 1105
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
282-622 |
3.45e-05 |
|
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: 48.70 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 282 QKERNSFEERIQALEEDLREKEREIA----TEKKNSlkrdKAIQGLtmalkskEKKVEELNSEIEKLSAAFAKAREALQK 357
Cdd:pfam06160 85 KKALDEIEELLDDIEEDIKQILEELDelleSEEKNR----EEVEEL-------KDKYRELRKTLLANRFSYGPAIDELEK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 358 AQTQEFQGSEDYETALSGKEALSAalRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHRE-KSKG---- 432
Cdd:pfam06160 154 QLAEIEEEFSQFEELTESGDYLEA--REVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREmEEEGyale 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 433 ----DCTIRDLRNEVEKLRN--------EVNEREKAMENR----YKSLLSESNKK---LHNQEQVIKHLTESTNQKDVLL 493
Cdd:pfam06160 232 hlnvDKEIQQLEEQLEENLAllenleldEAEEALEEIEERidqlYDLLEKEVDAKkyvEKNLPEIEDYLEHAEEQNKELK 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 494 qkfneKDLEVIQQNcYLMAAEDLElRSEGLITEKcssqqppgsktifskeKKQSSDYEELIQVLKKEQDIYTHLVKSLQE 573
Cdd:pfam06160 312 -----EELERVQQS-YTLNENELE-RVRGLEKQL----------------EELEKRYDEIVERLEEKEVAYSELQEELEE 368
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 58535453 574 S-DSINNLQAELNKIFALRKQLEQDVLSYQNLRKTLEEQISEIRRREEES 622
Cdd:pfam06160 369 IlEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEKS 418
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
101-612 |
3.73e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 101 KTNIELKVEVESLKRELQER---EQLLIKASKAVESLAEAGGSEIQRVKEDARKKVQQVEDLLTKRILLLEKDVTAAQAE 177
Cdd:PTZ00121 1463 KKKAEEAKKADEAKKKAEEAkkaDEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA 1542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 178 LEKAFAgTETEKALRLRL--ESKLSEMKKMHEGDLAMALVLDEKDRLIEELKLSLKSKEALI-------QCLKEEKSQMA 248
Cdd:PTZ00121 1543 EEKKKA-DELKKAEELKKaeEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEekkmkaeEAKKAEEAKIK 1621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 249 CPDENVSSGELRGLCAAPREEKERETEAAQMEHQKERNSFE-ERIQALEEDLREKEREIATEKKNslkrdkaiqgltmal 327
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKaAEEAKKAEEDKKKAEEAKKAEED--------------- 1686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 328 ksKEKKVEELNSEIEKlsaafAKAREALQKAQTQEFQGSEDYETAlsgkEALSAALRSQNLTKSTENHRLRRSIKKITQE 407
Cdd:PTZ00121 1687 --EKKAAEALKKEAEE-----AKKAEELKKKEAEEKKKAEELKKA----EEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 408 LSDLQQERERLEKDLEEAHREKSKgdCTIRDLRNEVEKLRNEVNEREKAMENRYKSLLsESNKKLHNQEQVIKHLTESTN 487
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKEKEA--VIEEELDEEDEKRRMEVDKKIKDIFDNFANII-EGGKEGNLVINDSKEMEDSAI 1832
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 488 QKDVLLQKFNEKDLEVIQQNCYLMAAEdlelrseglitekcsSQQPPGSKTIFSKEKKQSSDYEELIQvlkkEQDIYTHL 567
Cdd:PTZ00121 1833 KEVADSKNMQLEEADAFEKHKFNKNNE---------------NGEDGNKEADFNKEKDLKEDDEEEIE----EADEIEKI 1893
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 58535453 568 VKSLQESDSINNLQAELNKIFALRKqLEQDVLSYQNLRKTLEEQI 612
Cdd:PTZ00121 1894 DKDDIEREIPNNNMAGKNNDIIDDK-LDKDEYIKRDAEETREEII 1937
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
263-454 |
4.00e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.35 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 263 CAAPREEKERETEAAQMEHQKERNSFEERIQALEEDLREKEREIAtEKKNSLKRdkaiqgltmaLKSKEKKVEELNSEIE 342
Cdd:pfam07888 39 CLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVA-ELKEELRQ----------SREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 343 KLSAAFAKAREALQKAQtqefqgsEDYETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDL 422
Cdd:pfam07888 108 ASSEELSEEKDALLAQR-------AAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKL 180
|
170 180 190
....*....|....*....|....*....|..
gi 58535453 423 EEAHREkskgdctIRDLRNEVEKLRNEVNERE 454
Cdd:pfam07888 181 QQTEEE-------LRSLSKEFQELRNSLAQRD 205
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
110-464 |
4.06e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 110 VESLKRELQEREQLLIKASKAVESLAEAGGSEIQRVKEDARKKVQQVEDLLTKRILLlEKDVTAAQAELEKAFAGTETek 189
Cdd:PRK02224 312 VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAEL-ESELEEAREAVEDRREEIEE-- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 190 alrlrLESKLSEMKKMHE------GDLA--MALVLDEKDRLIE---ELKLSLKSKEALIQCLKEEKSQMACPDENVSSGE 258
Cdd:PRK02224 389 -----LEEEIEELRERFGdapvdlGNAEdfLEELREERDELREreaELEATLRTARERVEEAEALLEAGKCPECGQPVEG 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 259 LRGLCAAPREEKERETEAAQMEHQK-ERNSFEERIQALEeDLREKEREIAT--EKKNSLKRDKAIQGLTM-----ALKSK 330
Cdd:PRK02224 464 SPHVETIEEDRERVEELEAELEDLEeEVEEVEERLERAE-DLVEAEDRIERleERREDLEELIAERRETIeekreRAEEL 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 331 EKKVEELNSEIEKLSAAFAKAREALQKAQ-------------TQEFQGSEDYETALSGKEALSAAL-----RSQNLTKST 392
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEEAEEAReevaelnsklaelKERIESLERIRTLLAAIADAEDEIerlreKREALAELN 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 393 ENHR-----LRRSIKKITQE-----LSDLQQERERLEK-------DLEEAHREKSKGDCTIRDLRNEVEKLrNEVNEREK 455
Cdd:PRK02224 623 DERRerlaeKRERKRELEAEfdearIEEAREDKERAEEyleqveeKLDELREERDDLQAEIGAVENELEEL-EELRERRE 701
|
....*....
gi 58535453 456 AMENRYKSL 464
Cdd:PRK02224 702 ALENRVEAL 710
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
221-573 |
4.45e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.43 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 221 RLIEELKLSLKSKEALIQCLKEEKSQMACPDENVSSGELrglcAAPREEKERETEAAQMEHQKERNS-------FEERIQ 293
Cdd:pfam02463 123 ELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEIEEE----AAGSRLKRKKKEALKKLIEETENLaeliidlEELKLQ 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 294 ALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETA- 372
Cdd:pfam02463 199 ELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEe 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 373 ---------LSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEV 443
Cdd:pfam02463 279 kekklqeeeLKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 444 EKLRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIKHLTE-STNQKDVLLQKFNEKDLEVIQQNcyLMAAEDLELRSEG 522
Cdd:pfam02463 359 EELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELkSEEEKEAQLLLELARQLEDLLKE--EKKEELEILEEEE 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 58535453 523 LITEKCSSQQPPGSKTIFSKEKKQSSDYEELIQVLKKEQDIYTHLVKSLQE 573
Cdd:pfam02463 437 ESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLE 487
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
69-364 |
4.49e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 69 ELKKENFNLKLRIYFLE---------------ERMQQEFHGPTEHIYKTNIEL------KVEVESLKRELQEREQLLika 127
Cdd:TIGR02168 217 ELKAELRELELALLVLRleelreeleelqeelKEAEEELEELTAELQELEEKLeelrleVSELEEEIEELQKELYAL--- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 128 skaveslaeagGSEIQRVKEDARKKVQQVEDlltkrillLEKDVTAAQAELEKAFAGTETEKALRLRLESKLSEMKKMHE 207
Cdd:TIGR02168 294 -----------ANEISRLEQQKQILRERLAN--------LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 208 GDLAMalvLDEKDRLIEELKLSLKSKEALIQCLKEEKSQMacpdenvssgelrglcaapreEKERETEAAQMEHQKER-N 286
Cdd:TIGR02168 355 SLEAE---LEELEAELEELESRLEELEEQLETLRSKVAQL---------------------ELQIASLNNEIERLEARlE 410
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58535453 287 SFEERIQALEEDLREKEREIATEKKNSLKRDkaIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQ 364
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEEAELKELQAE--LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
283-464 |
4.87e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 283 KERNSFEERIQALEEDLREKEREIATEKKnslkrdkAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQe 362
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEA-------RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 363 fqgsEDYetalsgkEALSAALRSQNLTKSTENHRLRR---SIKKITQELSDLQQERERLEKDLEEAHREKskgDCTIRDL 439
Cdd:COG1579 89 ----KEY-------EALQKEIESLKRRISDLEDEILElmeRIEELEEELAELEAELAELEAELEEKKAEL---DEELAEL 154
|
170 180
....*....|....*....|....*
gi 58535453 440 RNEVEKLRNEVNEREKAMENRYKSL 464
Cdd:COG1579 155 EAELEELEAEREELAAKIPPELLAL 179
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
64-495 |
5.91e-05 |
|
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: 48.04 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 64 ENQITELKKENFNLKLRIYFLEERMQQEfhGPTEHIYKTNIELKVEVESLKRELQEREQLLIK-----ASKAVESLAEAG 138
Cdd:TIGR00618 448 TCTAQCEKLEKIHLQESAQSLKEREQQL--QTKEQIHLQETRKKAVVLARLLELQEEPCPLCGscihpNPARQDIDNPGP 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 139 GSEIQRVKEDARKKVQQVEDLLTKRILLLEKDVTAAQAELEKAFAGTETEKALRLRLESKLSEMKKMHEgdlamaLVLDE 218
Cdd:TIGR00618 526 LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITV------RLQDL 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 219 KDRLIEELKLSLKSKEALIQCLKEE--KSQMACPDENVSSGELRGLCAAPREE----KERETEAAQMEHQKERNSFEERi 292
Cdd:TIGR00618 600 TEKLSEAEDMLACEQHALLRKLQPEqdLQDVRLHLQQCSQELALKLTALHALQltltQERVREHALSIRVLPKELLASR- 678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 293 QALEEDLREKEREIATEKKnslkrdkAIQGLTMALKSKEKKVEELNSEIEKLSAAfakarealQKAQTQEFQGSEDYETA 372
Cdd:TIGR00618 679 QLALQKMQSEKEQLTYWKE-------MLAQCQTLLRELETHIEEYDREFNEIENA--------SSSLGSDLAAREDALNQ 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 373 LSGKEALSAALRSQNLTKSTENHRLRRSIKKIT-QELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVN 451
Cdd:TIGR00618 744 SLKELMHQARTVLKARTEAHFNNNEEVTAALQTgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQC 823
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 58535453 452 EREKAMENRYKSLLSESNKKLHNQEQVIKHLTESTNQKDVLLQK 495
Cdd:TIGR00618 824 ETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQE 867
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
64-456 |
6.01e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 64 ENQITELKKENFNLKLRIYFLEErmQQEFHGPTEHIYKTNIELK---VEVESLKRELQEREQLLIKASKAVESLAEAGGS 140
Cdd:COG4717 101 EEELEELEAELEELREELEKLEK--LLQLLPLYQELEALEAELAelpERLEELEERLEELRELEEELEELEAELAELQEE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 141 EIQRVKEDARKKVQQVEDL------LTKRILLLEKDVTAAQAELEKAFAGTE--TEKALRLRLESKLSEMKKMHEGdLAM 212
Cdd:COG4717 179 LEELLEQLSLATEEELQDLaeeleeLQQRLAELEEELEEAQEELEELEEELEqlENELEAAALEERLKEARLLLLI-AAA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 213 ALVLDEKDRLIEELKLSLKSKEALIQCLKEEKSQMACPDENVSSGELRGLCAAPREEKERETEAAQMEHQKERNSFEERI 292
Cdd:COG4717 258 LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 293 QALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKS--KEKKVEELNsEIEKLSAAFAKAREALQKAQTQEfqgsEDYE 370
Cdd:COG4717 338 ELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllAEAGVEDEE-ELRAALEQAEEYQELKEELEELE----EQLE 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 371 TALSGKEALSAALRSQNLTKstENHRLRRSIKKITQELSDLQQERERLEKDLEEAhreksKGDCTIRDLRNEVEKLRNEV 450
Cdd:COG4717 413 ELLGELEELLEALDEEELEE--ELEELEEELEELEEELEELREELAELEAELEQL-----EEDGELAELLQELEELKAEL 485
|
....*.
gi 58535453 451 NEREKA 456
Cdd:COG4717 486 RELAEE 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
401-621 |
6.41e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 401 IKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAmenrykslLSESNKKLHNQEQVIK 480
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE--------EYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 481 HLTESTNQKDVLLQKfNEKDLEVIQQNCYLMAAEDLELRSEGL-ITEKCSSQQppgsKTIFSKEKKQSSDYEELIQVLKK 559
Cdd:COG1196 306 RLEERRRELEERLEE-LEEELAELEEELEELEEELEELEEELEeAEEELEEAE----AELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58535453 560 EQDIYTHLVKSLQES----DSINNLQAELNKIFALRKQLEQDVLSYQNLRKTLEEQISEIRRREEE 621
Cdd:COG1196 381 LEELAEELLEALRAAaelaAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
326-502 |
6.49e-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: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 326 ALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQ--EFQGSEDYETALSGKEALSAALRSqnltKSTENHRLRRS--- 400
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERreALQRLAEYSWDEIDVASAEREIAE----LEAELERLDASsdd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 401 IKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIK 480
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERE 766
|
170 180
....*....|....*....|....
gi 58535453 481 HLTESTNQKDVLLQKFN--EKDLE 502
Cdd:COG4913 767 LRENLEERIDALRARLNraEEELE 790
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
106-484 |
8.91e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.48 E-value: 8.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 106 LKVEVESLKRELQEREQLLIKASKAVESLaeagGSEIQRVKEDARKKVQQVEDLLTkRILLLEKDVTAAQAELEKAFAGT 185
Cdd:pfam01576 438 LQSELESVSSLLNEAEGKNIKLSKDVSSL----ESQLQDTQELLQEETRQKLNLST-RLRQLEDERNSLQEQLEEEEEAK 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 186 ETEKALRLRLESKLSEMKKMHEGDLAMALVLDE-KDRL---IEELKLSLKSKEALIQCLKEEKS--QMACPDENVSSGEL 259
Cdd:pfam01576 513 RNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEgKKRLqreLEALTQQLEEKAAAYDKLEKTKNrlQQELDDLLVDLDHQ 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 260 RGLCAApREEKERETEAAQMEHQKERNSFEERIQALEEDLREKER---------EIATEKKNSLKRDKAIQGLTMA--LK 328
Cdd:pfam01576 593 RQLVSN-LEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETralslaralEEALEAKEELERTNKQLRAEMEdlVS 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 329 SKE---KKVEELNSEIEKLSAAFAKAREALQKAQtQEFQGSED---------------YETALSGKEALSAALRSQ---- 386
Cdd:pfam01576 672 SKDdvgKNVHELERSKRALEQQVEEMKTQLEELE-DELQATEDaklrlevnmqalkaqFERDLQARDEQGEEKRRQlvkq 750
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 387 --NLTKSTENHRLRRSI-----KKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRnevNEREKAMen 459
Cdd:pfam01576 751 vrELEAELEDERKQRAQavaakKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEAR---ASRDEIL-- 825
|
410 420
....*....|....*....|....*
gi 58535453 460 rykSLLSESNKKLHNQEQVIKHLTE 484
Cdd:pfam01576 826 ---AQSKESEKKLKNLEAELLQLQE 847
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
141-449 |
9.86e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.48 E-value: 9.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 141 EIQRVKEDARKKVQQVEDLLTKRILLL-EKDVTAAQAELEKAFAGTETEKALRL-----RLESKLSEMK-KMHEGDLAMA 213
Cdd:pfam01576 13 ELQKVKERQQKAESELKELEKKHQQLCeEKNALQEQLQAETELCAEAEEMRARLaarkqELEEILHELEsRLEEEEERSQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 214 LVLDEKDRL---IEELKLSLKSKEALIQCLKEEKSqmacpdenVSSGELRGLcaaprEEKERETEAAQMEHQKERNSFEE 290
Cdd:pfam01576 93 QLQNEKKKMqqhIQDLEEQLDEEEAARQKLQLEKV--------TTEAKIKKL-----EEDILLLEDQNSKLSKERKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 291 RIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQefqgSEDYE 370
Cdd:pfam01576 160 RISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQ----IAELR 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58535453 371 TALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERlekdlEEAHREKSKGDCtiRDLRNEVEKLRNE 449
Cdd:pfam01576 236 AQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLES-----ERAARNKAEKQR--RDLGEELEALKTE 307
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
118-506 |
1.04e-04 |
|
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: 47.26 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 118 QEREQLLIKASKAVESLAEAGGSEIQRVKEDARKKVQQVE----DLLTKRILLLEKDVTAAQAELEKAFAGTETEKALRL 193
Cdd:COG5185 170 QELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKEsetgNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLA 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 194 RLESKLSEMKKmhegdlamalvldekdrLIEELKLS-LKSKEALIQCLKEEKSQMACPDENVSSgELRGLCAAPREEKER 272
Cdd:COG5185 250 QTSDKLEKLVE-----------------QNTDLRLEkLGENAESSKRLNENANNLIKQFENTKE-KIAEYTKSIDIKKAT 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 273 ETEAAQMEHQKERNSFEERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALkSKEKKVEELNSEIEKLSAAFAKAR 352
Cdd:COG5185 312 ESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENI-VGEVELSKSSEELDSFKDTIESTK 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 353 EAL-QKAQTQEFQGSEdyetalsGKEALSAALRSQnltkSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHRE--- 428
Cdd:COG5185 391 ESLdEIPQNQRGYAQE-------ILATLEDTLKAA----DRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREade 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 429 --KSKGDCTIRDLRNEVEKLRNEVNEREKAMENRYKSLLSE-------SNKKLHNQEQVIKHLTESTNQKDVLLQKFNEK 499
Cdd:COG5185 460 esQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATleklrakLERQLEGVRSKLDQVAESLKDFMRARGYAHIL 539
|
....*..
gi 58535453 500 DLEVIQQ 506
Cdd:COG5185 540 ALENLIP 546
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
256-449 |
1.09e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 256 SGELRGLCAAPREEKERETEAAQmEHQKERNSFEERIQALEEDLREKEREIAtEKKNSLKRDKAIQGLTMALKSKEKKVE 335
Cdd:COG4717 62 QGRKPELNLKELKELEEELKEAE-EKEEEYAELQEELEELEEELEELEAELE-ELREELEKLEKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 336 ELNSEIEKLSAAFAKAREaLQKAQTQEFQGSEDYETAlsgKEALSAALRSQNLTKstenhrlRRSIKKITQELSDLQQER 415
Cdd:COG4717 140 ELAELPERLEELEERLEE-LRELEEELEELEAELAEL---QEELEELLEQLSLAT-------EEELQDLAEELEELQQRL 208
|
170 180 190
....*....|....*....|....*....|....
gi 58535453 416 ERLEKDLEEAHREkskgdctIRDLRNEVEKLRNE 449
Cdd:COG4717 209 AELEEELEEAQEE-------LEELEEELEQLENE 235
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
412-676 |
1.43e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.89 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 412 QQERERLEKDLEEAHREKSKgdctIRDLRNEVEKLRNEVNEREKAMENRYKSL---LSESNKKLHNQEQVIKHLTESTNQ 488
Cdd:pfam02463 169 RKKKEALKKLIEETENLAEL----IIDLEELKLQELKLKEQAKKALEYYQLKEkleLEEEYLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 489 KDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEglitEKCSSQQPPGSKTIFSKEKKQSSDYEELIQVLKKEQDIYTHLV 568
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEE----EKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 569 KSLQesdsinNLQAELNKIFALRKQLEQDVLSYQNLRKTLEEQISEIRRREEESFSLYSDQTSYLSICLEENNRFQVEHF 648
Cdd:pfam02463 321 KEKK------KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
250 260
....*....|....*....|....*...
gi 58535453 649 SQEELKKKVSDLIQLVKELYTDNQHLKK 676
Cdd:pfam02463 395 EELELKSEEEKEAQLLLELARQLEDLLK 422
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
332-472 |
1.82e-04 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 44.15 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 332 KKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETALSGK-----EALSAALRSQN------LTKSTENHRLRRS 400
Cdd:pfam08614 14 DRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLlaqlrEELAELYRSRGelaqrlVDLNEELQELEKK 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58535453 401 IKKITQELSDLQQERERLE---KDLEEAHREKSKGdctIRDLRNEVEKLRNEVNEREKAMENrykslLSESNKKL 472
Cdd:pfam08614 94 LREDERRLAALEAERAQLEeklKDREEELREKRKL---NQDLQDELVALQLQLNMAEEKLRK-----LEKENREL 160
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
66-667 |
1.87e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.50 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 66 QITELKKENFNLKLRIYFLEERM---QQEFHGPTEHIYKTNIELKVEVESLKRELQEREqlLIKASKAVESLAEAGGSEI 142
Cdd:pfam02463 217 EKLELEEEYLLYLDYLKLNEERIdllQELLRDEQEEIESSKQEIEKEEEKLAQVLKENK--EEEKEKKLQEEELKLLAKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 143 QRVKEDARKKVQQVEDLLTKRILLLEKDVTAAQAELEKAFAGTETEKALRLRLESKLSEMKKMHEgdlAMALVLDEKDRL 222
Cdd:pfam02463 295 EEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE---ELEKLQEKLEQL 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 223 IEELKLSLKSKEALIQCLKEEKSQMACPDENVSSGELRGLCAAPREE----KERETEAAQMEHQKERNSFEERIQALEED 298
Cdd:pfam02463 372 EEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEdllkEEKKEELEILEEEEESIELKQGKLTEEKE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 299 LREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEI-EKLSAAFAKAREALQKAQ-----------TQEFQGS 366
Cdd:pfam02463 452 ELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKlEERSQKESKARSGLKVLLalikdgvggriISAHGRL 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 367 EDYETALSG-KEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEK 445
Cdd:pfam02463 532 GDLGVAVENyKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 446 -----------LRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFNEKDLEVIQQNCYLMAAE 514
Cdd:pfam02463 612 tleadeddkraKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAK 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 515 DLELRSEGLITEKCSSQQPPGSKTIFSKEKKQSSDYEELIQVLKKEQDIYTHLVKSLQESDSINNLQAELNKIFALRKQL 594
Cdd:pfam02463 692 EEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSL 771
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 58535453 595 EQ----DVLSYQNLRKTLEEQISEIRRREEESFSLYSDQTSYLSICLEENNRFQVEHFSQEELKKKVSDLIQLVKEL 667
Cdd:pfam02463 772 KEkelaEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKL 848
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
126-386 |
1.99e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 126 KASKAVESLAEAggsEIQRVKEDARKKVQQVEDLLTKRILLLEKDVTAAQAELEkafagtetekalRLRLESKLSEMKKm 205
Cdd:COG3206 149 LAAAVANALAEA---YLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALE------------EFRQKNGLVDLSE- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 206 hEGDLAMALvLDEKDRLIEELKLSLKSKEALIQCLKEEKSQmacpdenvSSGELRGLCAAPREEKERETEA-AQMEHQKE 284
Cdd:COG3206 213 -EAKLLLQQ-LSELESQLAEARAELAEAEARLAALRAQLGS--------GPDALPELLQSPVIQQLRAQLAeLEAELAEL 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 285 RNSFEE---RIQALEEDLREKEREIATEKKNSL-KRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQT 360
Cdd:COG3206 283 SARYTPnhpDVIALRAQIAALRAQLQQEAQRILaSLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEV 362
|
250 260
....*....|....*....|....*.
gi 58535453 361 QEfqgsEDYETALSGKEALSAALRSQ 386
Cdd:COG3206 363 AR----ELYESLLQRLEEARLAEALT 384
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
265-357 |
2.05e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 265 APREEKERETEA------AQMEHQKERNSFEERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELN 338
Cdd:PRK12704 51 AEAIKKEALLEAkeeihkLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKE 130
|
90
....*....|....*....
gi 58535453 339 SEIEKLSaafAKAREALQK 357
Cdd:PRK12704 131 EELEELI---EEQLQELER 146
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
268-430 |
2.34e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 268 EEKERETEAAQMEHQKERNSFEERIQALEEDLREKEREIA---TEKKNSLKRDkaIQGLTMALKSKEKKVEELNSEIEKL 344
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRgngGDRLEQLERE--IERLERELEERERRRARLEALLAAL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 345 SAAFAKAREALQKAQTQefqgsedyetALSGKEALSAALrsqnltkstenHRLRRSIKKITQELSDLQQERERLEKDLEE 424
Cdd:COG4913 372 GLPLPASAEEFAALRAE----------AAALLEALEEEL-----------EALEEALAEAEAALRDLRRELRELEAEIAS 430
|
....*.
gi 58535453 425 AHREKS 430
Cdd:COG4913 431 LERRKS 436
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
257-452 |
2.49e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 257 GELRGLCAAPREEKERETEAAQMEH-------QKERNSFEERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKS 329
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAalrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 330 KE-KKVEELNSEIEKLSAAFAKAREALQKaqtqefqgsedyetalsgkeaLSAALRSQNLTKSTENHRLRRSIKKITQEL 408
Cdd:COG4913 335 NGgDRLEQLEREIERLERELEERERRRAR---------------------LEALLAALGLPLPASAEEFAALRAEAAALL 393
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 58535453 409 SDLQQERERLEKDLEEAHREKskgdctiRDLRNEVEKLRNEVNE 452
Cdd:COG4913 394 EALEEELEALEEALAEAEAAL-------RDLRRELRELEAEIAS 430
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
327-599 |
2.49e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 327 LKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETALSGKEALSAALRSqnltKSTENHRLRRSIKKITQ 406
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES----LQEEAEELQEELEELQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 407 ELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQ--EQVIKHLTE 484
Cdd:COG4372 123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEanRNAEKEEEL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 485 STNQKDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEGLITEKCSSQQPPGSKTIFSKEKKQSSDYEELIQVLKKEQDIY 564
Cdd:COG4372 203 AEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAA 282
|
250 260 270
....*....|....*....|....*....|....*
gi 58535453 565 THLVKSLQESDSINNLQAELNKIFALRKQLEQDVL 599
Cdd:COG4372 283 LELEALEEAALELKLLALLLNLAALSLIGALEDAL 317
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
320-482 |
3.76e-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: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 320 IQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQefqgSEDYETALSGKEALSAALRsQNLTKSTE---NHR 396
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE----LEDLEKEIKRLELEIEEVE-ARIKKYEEqlgNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 397 LRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQE 476
Cdd:COG1579 87 NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*.
gi 58535453 477 QVIKHL 482
Cdd:COG1579 167 ELAAKI 172
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
287-448 |
4.08e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.23 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 287 SFEERIQALEEDLREKEREiaTEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALqkaqtqefqgs 366
Cdd:COG2433 377 SIEEALEELIEKELPEEEP--EAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERI----------- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 367 EDYETALSgkealsaalrsqnLTKSTENHRLRRSikkitQELSDLQQERERLEKDLEEAHREkskgdctIRDLRNEVEKL 446
Cdd:COG2433 444 ERLERELS-------------EARSEERREIRKD-----REISRLDREIERLERELEEERER-------IEELKRKLERL 498
|
..
gi 58535453 447 RN 448
Cdd:COG2433 499 KE 500
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
270-383 |
4.22e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.32 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 270 KERETEAAQMEHQKERnsFEERIQALEedlREK-EREIATEKKNSLKRDKAIQGLTMAL-KSKEKKVEELNSEIEKLSA- 346
Cdd:PRK05035 439 RAIEQEKKKAEEAKAR--FEARQARLE---REKaAREARHKKAAEARAAKDKDAVAAALaRVKAKKAAATQPIVIKAGAr 513
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 58535453 347 ----AFAKAREALQKAQTQEFQGSEDYETALSGKEALSAAL 383
Cdd:PRK05035 514 pdnsAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAI 554
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
40-596 |
4.27e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.20 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 40 GNGLLPNVSEETVSptRARNMKDFENQITEL-----KKENFNLKLRIYfLEERMQQEFHGPTEHIYKTNIELK-VEVESL 113
Cdd:pfam10174 169 SKGLPKKSGEEDWE--RTRRIAEAEMQLGHLevlldQKEKENIHLREE-LHRRNQLQPDPAKTKALQTVIEMKdTKISSL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 114 KRELQEREQLL-----------------IKASKAVESLAEAGGSEIQRVKEDARKKVQQVEDLLTK-------------R 163
Cdd:pfam10174 246 ERNIRDLEDEVqmlktngllhtedreeeIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKletltnqnsdckqH 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 164 ILLLEKDVTAAqaELEKAFAGTETEkALRLRLESKLSemkkmhegdlamalVLDEKDRLIEELKlslkskealiqclkEE 243
Cdd:pfam10174 326 IEVLKESLTAK--EQRAAILQTEVD-ALRLRLEEKES--------------FLNKKTKQLQDLT--------------EE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 244 KSQMAcpdenvssGELRGLcaapreekereteaAQMEHQKER--NSFEERIQALEEDLREKEREIATEKK-------NSL 314
Cdd:pfam10174 375 KSTLA--------GEIRDL--------------KDMLDVKERkiNVLQKKIENLQEQLRDKDKQLAGLKErvkslqtDSS 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 315 KRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREAL--------QKAQTQEFQGSEDYETALSGKEALSaALRSQ 386
Cdd:pfam10174 433 NTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLkkenkdlkEKVSALQPELTEKESSLIDLKEHAS-SLASS 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 387 NLTKSTENHRLRRSIKKITQELSDLQQERERLEkDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMEnRYKSLLS 466
Cdd:pfam10174 512 GLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH-NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVE-RLLGILR 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 467 ESNKKLHNQEQVIKHLtESTNQKDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEGLITEKCSSQQPPGSKTIFSKEKKQ 546
Cdd:pfam10174 590 EVENEKNDKDKKIAEL-ESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTR 668
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 58535453 547 ssdyeeliQVLKKEQDIYTHLVKSLQESDSI-NNLQAElnkifaLRKQLEQ 596
Cdd:pfam10174 669 --------QELDATKARLSSTQQSLAEKDGHlTNLRAE------RRKQLEE 705
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
268-507 |
4.77e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.43 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 268 EEKERETEAAQMEHQKERNSFEERIQALEEDLREKERE---IATEKKNSLKRDKAIQGLTMAlkskekkVEELNSEIEKL 344
Cdd:TIGR01612 1540 AKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEkfrIEDDAAKNDKSNKAAIDIQLS-------LENFENKFLKI 1612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 345 SAAFAKAREALQKAQTQEfqgsedyetalsgKEALSAALRSQNlTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEE 424
Cdd:TIGR01612 1613 SDIKKKINDCLKETESIE-------------KKISSFSIDSQD-TELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDE 1678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 425 ahrekskgdctirdLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIKHLTESTNQKdvLLQKFNEKDLEVI 504
Cdd:TIGR01612 1679 --------------LDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKEEIESIKELIEPTIEN--LISSFNTNDLEGI 1742
|
...
gi 58535453 505 QQN 507
Cdd:TIGR01612 1743 DPN 1745
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
86-337 |
6.10e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.81 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 86 ERMQQEFHGPTEHIYKTNIELKVEVESLKRELQEREQLLIKASKAVESLAEAGGS----------EIQRVKEDARK---- 151
Cdd:pfam10174 460 EREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKkdsklksleiAVEQKKEECSKlenq 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 152 --KVQQVEDL------LTKRILLLEKDV-------TAAQAELEK---AFAGTETEKALRlrlESKLSEMKKMHEGDLAMA 213
Cdd:pfam10174 540 lkKAHNAEEAvrtnpeINDRIRLLEQEVarykeesGKAQAEVERllgILREVENEKNDK---DKKIAELESLTLRQMKEQ 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 214 LVLDEKDRLIEELKLSlKSKEALIQCLKEEKSQMACPDENVSSgELRGLCAAPREE----KERETEAAQMEHQKER---N 286
Cdd:pfam10174 617 NKKVANIKHGQQEMKK-KGAQLLEEARRREDNLADNSQQLQLE-ELMGALEKTRQEldatKARLSSTQQSLAEKDGhltN 694
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58535453 287 SFEERIQALEEDLR-----------EKEREIATEKKNSLKRDKAiQGLTMALK-SKEKKVEEL 337
Cdd:pfam10174 695 LRAERRKQLEEILEmkqeallaaisEKDANIALLELSSSKKKKT-QEEVMALKrEKDRLVHQL 756
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
331-618 |
7.20e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 331 EKKVEELNSEIEKLSAAFAKAREALQKAQTQefqgsedyetalsgKEALSAalRSQNLTKSTENHRLRRSIKKITQELSD 410
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAE--------------LDALQE--RREALQRLAEYSWDEIDVASAEREIAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 411 LQQERERLEK---DLEEAHREKSKgdctIRDLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIKhltestN 487
Cdd:COG4913 673 LEAELERLDAssdDLAALEEQLEE----LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED------L 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 488 QKDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEGLitekcssqqppgsktifskEKKQSSDYEELIQVLKKEQDIYTHL 567
Cdd:COG4913 743 ARLELRALLEERFAAALGDAVERELRENLEERIDAL-------------------RARLNRAEEELERAMRAFNREWPAE 803
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58535453 568 VKSLQES-DSINNLQAELNKI-----------F--ALRKQLEQDVLsyqNLRKTLEEQISEIRRR 618
Cdd:COG4913 804 TADLDADlESLPEYLALLDRLeedglpeyeerFkeLLNENSIEFVA---DLLSKLRRAIREIKER 865
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1359-1573 |
1.42e-03 |
|
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: 43.57 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 1359 LSDYETSEKSFfsRDQKQDNETEKTSVMVNSFSQDLLMEHIQEIRTLRKRLEESIKT-NEKLRKQLERQGSEfVQGSTSI 1437
Cdd:pfam15921 383 LADLHKREKEL--SLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAmKSECQGQMERQMAA-IQGKNES 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 1438 FASGSELHSSLTSEIHFLRKQNQALNAmlikgsrdKQKENDKLRESLSRKTVSLEHLQReyaSVKEENERLQKEGSEKER 1517
Cdd:pfam15921 460 LEKVSSLTAQLESTKEMLRKVVEELTA--------KKMTLESSERTVSDLTASLQEKER---AIEATNAEITKLRSRVDL 528
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 58535453 1518 HNQQLiQEVRCSGQELSRVQEEVKLRQQLLSQNDKLLQSLRVELKAYEKLDEEHRR 1573
Cdd:pfam15921 529 KLQEL-QHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGR 583
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1392-1576 |
1.43e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 1392 QDLLMEHIQEIRTLRKRLEESIKTNEKLRKQLERQGSEFVQGSTSIfasgselhSSLTSEIHFLRKQNQALNAMLIKGSR 1471
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL--------ARLEQDIARLEERRRELEERLEELEE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 1472 DKQ---KENDKLRESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQEVRcsgQELSRVQEEVKLRQQLLS 1548
Cdd:COG1196 324 ELAeleEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE---ELAEELLEALRAAAELAA 400
|
170 180
....*....|....*....|....*...
gi 58535453 1549 QNDKLLQSLRVELKAYEKLDEEHRRLRD 1576
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEE 428
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
273-665 |
1.44e-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: 43.81 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 273 ETEAAQMEHQKERNSFEERIQALEEDLREKER--EIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAK 350
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGSRLKRKKKEAlkKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 351 AREALQKAQTQEFQGSEDYETALSGKEALSAALRSQNLTKSTE-NHRLRRSIKKITQELSDLQQERERLEKDLEEAHREK 429
Cdd:pfam02463 223 EEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEkLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSEL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 430 SKGDCTIRDLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIKHLTESTNQKDvLLQKFNEKDLEVIQQNCY 509
Cdd:pfam02463 303 LKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEK-LQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 510 LMAAEDLELRSEGLITEKcssqqppgsktifsKEKKQSSDyEELIQVLKKEQDIYTHLVKSLQESDSINNLQAELNKIFA 589
Cdd:pfam02463 382 ESERLSSAAKLKEEELEL--------------KSEEEKEA-QLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKL 446
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58535453 590 LRKQLEQDVLSYQNLRKTLEEQISEIRRREEESFSLYSDQTSYLSICLEENNRFQvEHFSQEELKKKVSDLIQLVK 665
Cdd:pfam02463 447 TEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQK-ESKARSGLKVLLALIKDGVG 521
|
|
| ALIX_LYPXL_bnd |
pfam13949 |
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ... |
335-488 |
1.63e-03 |
|
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.
Pssm-ID: 464053 [Multi-domain] Cd Length: 294 Bit Score: 42.61 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 335 EELNSEIEKLSAAFAKAREALQKAQtQEFQGSEDYETALSG-KEALSAALRSQNLTKSTEN-HRLRRSIKKITQELSDLQ 412
Cdd:pfam13949 75 ATLRAEIRKYREILEQASESDSQVR-SKFREHEEDLELLSGpDEDLEAFLPSSRRAKNSPSvEEQVAKLRELLNKLNELK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 413 QERERLEKDLeeahREKSKGDctirDLRNEV--EKLRNEVNEREKAMENR----YKSLLSESNKKLHNQEQVIKHLTEST 486
Cdd:pfam13949 154 REREQLLKDL----KEKARND----DISPKLllEKARLIAPNQEEQLFEEelekYDPLQNRLEQNLHKQEELLKEITEAN 225
|
..
gi 58535453 487 NQ 488
Cdd:pfam13949 226 NE 227
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
189-347 |
1.65e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 189 KALRlRLESKLSE-MKKMHEG---DLAMALVLDEK--DRLIEELKLSLKSKEaliqclkEEKSQMACPDENVSSGELRGL 262
Cdd:COG2433 343 KAYD-AYKNKFERvEKKVPPDvdrDEVKARVIRGLsiEEALEELIEKELPEE-------EPEAEREKEHEERELTEEEEE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 263 CAAPREEKER-ETEAAQMEHQKERNsfEERIQALEEDLREKEREIATEKKNS---LKRDKAIQGLTMALKSKEKKVEELN 338
Cdd:COG2433 415 IRRLEEQVERlEAEVEELEAELEEK--DERIERLERELSEARSEERREIRKDreiSRLDREIERLERELEEERERIEELK 492
|
....*....
gi 58535453 339 SEIEKLSAA 347
Cdd:COG2433 493 RKLERLKEL 501
|
|
| V_Alix_like |
cd08915 |
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ... |
289-497 |
1.89e-03 |
|
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains the V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Bro1, and Rim20 all interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. The Alix V-domain contains a binding site, partially conserved in this superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Members of this superfamily have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members, including Alix, HD-PTP, and Bro1, also have a proline-rich region (PRR), which binds multiple partners in Alix, including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2. The C-terminal portion (V-domain and PRR) of Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes; it interacts with a YPxL motif in Doa4s catalytic domain to stimulate its deubiquitination activity. Rim20 may bind the ESCRT-III subunit Snf7, bringing the protease Rim13 (a YPxL-containing transcription factor) into proximity with Rim101, and promoting the proteolytic activation of Rim101. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate often absent in human kidney, breast, lung, and cervical tumors. HD-PTP has a C-terminal catalytically inactive tyrosine phosphatase domain.
Pssm-ID: 185746 [Multi-domain] Cd Length: 342 Bit Score: 42.71 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 289 EERIQALEEDLREKEREIatekknslKRDKAIQGLTMA-LKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSE 367
Cdd:cd08915 90 EELLQECEELLEEEAAED--------DQLRAKFGTLRWrRPSSDEAAKELYEKVTKLRGYLEQASNSDNEVLQCYESIDP 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 368 DYETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEeahrEKSKGDCTIRDLRNEVEKLR 447
Cdd:cd08915 162 NLVLLCGGYKELKAFIPSPYPALDPEVSEVVSSLRPLLNEVSELEKERERFISELE----IKSRNNDILPKLITEYKKNG 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 58535453 448 NEVNER--EKAMENrYKSLLSESNKKLHNQEQVIKHLTEStNQKDVLLQKFN 497
Cdd:cd08915 238 TTEFEDlfEEHLKK-FDKDLTYVEKTKKKQIELIKEIDAA-NQEFSQVKNSN 287
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1395-1576 |
1.98e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 1395 LMEHIQEIRTLRKRLEESIKTNEKLRKQLERQGSEFVQGSTSIFASGSELhSSLTSEIHFLRKQNQALNAMLikgsRDKQ 1474
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI-EELEAQIEQLKEELKALREAL----DELR 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 1475 KENDKLRESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQEVRCSGQELSRVQEEVKLRQQLLSQNDKLL 1554
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
170 180
....*....|....*....|..
gi 58535453 1555 QSLRvelKAYEKLDEEHRRLRD 1576
Cdd:TIGR02168 890 ALLR---SELEELSEELRELES 908
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1399-1576 |
2.18e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 1399 IQEIRTLRKRLEESIKTNEKLRKQLERQGSEFVQGSTSIFASGSELHSSLTSEIHFLRKQNQALNAM---LIKGSRDKQK 1475
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAeaeLAEAEEELEE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 1476 ENDKLRESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQEVRCSGQELSRVQEEVKLRQQLLSQNDKLLQ 1555
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
170 180
....*....|....*....|.
gi 58535453 1556 SLRVELKAYEKLDEEHRRLRD 1576
Cdd:COG1196 464 LLAELLEEAALLEAALAELLE 484
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
110-419 |
2.60e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 110 VESLKRELQEREQLLIKASKAVESLAEAGgSEIQRVKEDARKKVQQVEDLLtkRILLLEKDVTAAQAELEKAFAGTETEK 189
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAEL-DALQERREALQRLAEYSWDEI--DVASAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 190 ALRLRLESKLSEMKKMHEgdlamalVLDEKDRLIEELKLSLKSKEALIQCLKEEKSQMACPDENVSSGELrglcaapreE 269
Cdd:COG4913 689 ALEEQLEELEAELEELEE-------ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL---------E 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 270 KERETEAAQMEHQKERNSFEERIQALEEDLREKEREIaTEKKNSLKRD--KAIQGLTMALKSKEKKVEELNS-EIEKLSA 346
Cdd:COG4913 753 ERFAAALGDAVERELRENLEERIDALRARLNRAEEEL-ERAMRAFNREwpAETADLDADLESLPEYLALLDRlEEDGLPE 831
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58535453 347 AFAKAREALQKAQTQEFqgsedyeTALsgkealsaalrsqnltksteNHRLRRSIKKITQELSDLQQERERLE 419
Cdd:COG4913 832 YEERFKELLNENSIEFV-------ADL--------------------LSKLRRAIREIKERIDPLNDSLKRIP 877
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
61-507 |
3.08e-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: 42.65 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 61 KDFENQITELKKENFNLKLRIYFLEERMQQEFHGPTEHIYKTNIELKVEVESLKRELQEREQLLIKASKAVESLAEAGGS 140
Cdd:pfam02463 574 PLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVS 653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 141 EIQrvKEDARKKVQQVEDLLTKRILLLEKDVTAAQAELEKAFAGTETEKALRLRLESKLSEMKKMHEGDLAMALVLDEKD 220
Cdd:pfam02463 654 LEE--GLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQ 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 221 RLIEELKLSLKSKEALIQCLKEEKSQmacpdenvssgelrglcaapreEKERETEAAQMEHQKERNSFEERIQALEEDLR 300
Cdd:pfam02463 732 DKINEELKLLKQKIDEEEEEEEKSRL----------------------KKEEKEEEKSELSLKEKELAEEREKTEKLKVE 789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 301 EKEREIATEKKNSLKRDKAiqgltmALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSE--DYETALSGKEA 378
Cdd:pfam02463 790 EEKEEKLKAQEEELRALEE------ELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKlaEEELERLEEEI 863
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 379 LSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAME 458
Cdd:pfam02463 864 TKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE 943
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 58535453 459 NRYKSLLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFNEKDLEVIQQN 507
Cdd:pfam02463 944 EADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNK 992
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1400-1549 |
3.09e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 1400 QEIRTLRKRLEESIKTNEKLRKQLERQGSEFVQGSTSIFASGSE------LHSS----LTSEIHFLRKQNQALNAmLIKG 1469
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQpplallLSPEdfldAVRRLQYLKYLAPARRE-QAEE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 1470 SRDKQKENDKLRESLSRKTVSLEHLQREyasVKEENERLQKEGSEKERHNQQLIQEVRCSGQELSRVQEEVKLRQQLLSQ 1549
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAE---LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
282-364 |
4.12e-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: 40.20 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 282 QKERNSFEERIQALEEDLREKEREIATEKKNsLKRDKAiqglTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQ 361
Cdd:COG2825 42 KAAQKKLEKEFKKRQAELQKLEKELQALQEK-LQKEAA----TLSEEERQKKERELQKKQQELQRKQQEAQQDLQKRQQE 116
|
...
gi 58535453 362 EFQ 364
Cdd:COG2825 117 LLQ 119
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
105-431 |
4.52e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 105 ELKVEVESLKRELQEREQLLIKASKAVESLAEAGGSEIQRVKEDARKKVQQVEDLLTKrilllEKDVTAAQAELekafag 184
Cdd:pfam07888 45 ELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEK-----YKELSASSEEL------ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 185 TETEKALRLRLESKLSEMKKMHEGDLAMALVLDEKDRLIEELKLSLKSKEALIQCLKEEKSQMACPDEnVSSGELRGLCA 264
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQ-QTEEELRSLSK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 265 APREEK----ERETEAAQMEhqkernsfeERIQALEEDLREKEREIAtEKKNSLKRDKAIQGLtmaLKSKEKKVEELNSE 340
Cdd:pfam07888 193 EFQELRnslaQRDTQVLQLQ---------DTITTLTQKLTTAHRKEA-ENEALLEELRSLQER---LNASERKVEGLGEE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 341 IEKLSAAFAKAREALQKAQTQEFQgsedyetaLSGKEA-LSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLE 419
Cdd:pfam07888 260 LSSMAAQRDRTQAELHQARLQAAQ--------LTLQLAdASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLE 331
|
330
....*....|..
gi 58535453 420 KDLEEAHREKSK 431
Cdd:pfam07888 332 ERLQEERMEREK 343
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
232-458 |
4.89e-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: 41.65 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 232 SKEALIQcLKEEKSQMacpdenvssgELRGLCAAPREEKERETEAAQMEHQKERN-SFEERIQALEEDLREKEREIATEK 310
Cdd:pfam05557 7 SKARLSQ-LQNEKKQM----------ELEHKRARIELEKKASALKRQLDRESDRNqELQKRIRLLEKREAEAEEALREQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 311 KNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQT---------QEFQGSED-YETALSGKEALS 380
Cdd:pfam05557 76 ELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELelqstnselEELQERLDlLKAKASEAEQLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 381 AALRSQNLTKSTENHRLRRSIKKITQ------ELSDLQQERER---LEKDLEEAHREKSKGDCTIRD---LRNEVEKLRN 448
Cdd:pfam05557 156 QNLEKQQSSLAEAEQRIKELEFEIQSqeqdseIVKNSKSELARipeLEKELERLREHNKHLNENIENkllLKEEVEDLKR 235
|
250
....*....|
gi 58535453 449 EVNEREKAME 458
Cdd:pfam05557 236 KLEREEKYRE 245
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
377-494 |
5.54e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 377 EAlSAALRSQNLTKSTEnhrlrrsIKKITQELSDLQQERERLEKDLEEAHREKskgdctIRDLRNEVEKLRNEVN----- 451
Cdd:COG0542 397 EA-AARVRMEIDSKPEE-------LDELERRLEQLEIEKEALKKEQDEASFER------LAELRDELAELEEELEalkar 462
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 58535453 452 -EREKAMENRYKSL---LSESNKKLHNQEQVIKHLTESTNQKDVLLQ 494
Cdd:COG0542 463 wEAEKELIEEIQELkeeLEQRYGKIPELEKELAELEEELAELAPLLR 509
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
378-618 |
5.97e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 378 ALSAALRSQNLTKSTEN--HRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREK 455
Cdd:COG4942 11 LALAAAAQADAAAEAEAelEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 456 AMEnryksllsESNKKLHNQEQVIKHLTES---TNQKDVLLQKFNEKDLEVIQQNCYLMA--AEDLELRSEGLITEKcss 530
Cdd:COG4942 91 EIA--------ELRAELEAQKEELAELLRAlyrLGRQPPLALLLSPEDFLDAVRRLQYLKylAPARREQAEELRADL--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 531 qqppgsKTIFSKEKKQSSDYEELIQVLKKEQDIYTHLVKSLQESDS-INNLQAELNKIFALRKQLEQDVLSYQNLRKTLE 609
Cdd:COG4942 160 ------AELAALRAELEAERAELEALLAELEEERAALEALKAERQKlLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
....*....
gi 58535453 610 EQISEIRRR 618
Cdd:COG4942 234 AEAAAAAER 242
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
267-350 |
6.18e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 40.77 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 267 REEKERETEAAQMEHQKERNSFEERIQALEEDLREKEREIATEK-----KNSLKR--DKAIQGLTMALKSKEKKVEELNS 339
Cdd:PRK06669 87 TDEASSIIEKLQMQIEREQEEWEEELERLIEEAKAEGYEEGYEKgreegLEEVREliEQLNKIIEKLIKKREEILESSEE 166
|
90
....*....|.
gi 58535453 340 EIEKLSAAFAK 350
Cdd:PRK06669 167 EIVELALDIAK 177
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
325-666 |
6.53e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.49 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 325 MALKSKEKKveELNSEIEKLSAAFAKAREAlqKAQTQEFQGSEDYETALSGKEALSAALRSQNLTKSTENhrLRRSIKKI 404
Cdd:TIGR00618 158 LKAKSKEKK--ELLMNLFPLDQYTQLALME--FAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQV--LEKELKHL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 405 TQELSDLQQERERLEKdLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMENRYKS-----LLSESNKKLHNQEQVI 479
Cdd:TIGR00618 232 REALQQTQQSHAYLTQ-KREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRArkaapLAAHIKAVTQIEQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 480 KHLTESTNQKDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEGLITEKCSSQQPPGSKTIFSKEKkqssdyeELIQVLKK 559
Cdd:TIGR00618 311 RIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQH-------TLTQHIHT 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 560 EQDIYTHLVKSLQESDSI-NNLQAELNKIFALrkQLEQDVLSYQNLRKTLEEQISEIRRREEESFSLYSDQtsylsiCLE 638
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKElDILQREQATIDTR--TSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQ------CEK 455
|
330 340
....*....|....*....|....*....
gi 58535453 639 ENNRFQVEHF-SQEELKKKVSDLIQLVKE 666
Cdd:TIGR00618 456 LEKIHLQESAqSLKEREQQLQTKEQIHLQ 484
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
282-622 |
7.09e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 282 QKERNSFEERIQALEEDLREKEREIATEKKNSLKRDKAIQGLtmalkskEKKVEELNSEIEKLSAAFAKAREALQK---- 357
Cdd:PRK04778 104 KHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQL-------KDLYRELRKSLLANRFSFGPALDELEKqlen 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 358 -----AQTQEFQGSEDYETAlsgKEALSAAlrsqnltkSTENHRLRRSIKKITQELSDLQQE-RERLEkDLEEAHRE-KS 430
Cdd:PRK04778 177 leeefSQFVELTESGDYVEA---REILDQL--------EEELAALEQIMEEIPELLKELQTElPDQLQ-ELKAGYRElVE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 431 KG--------DCTIRDLRNEVEKLRN--------EVNEREKAMENR----YKSLLSE---SNKKLHNQEQVIKHLTESTN 487
Cdd:PRK04778 245 EGyhldhldiEKEIQDLKEQIDENLAlleeldldEAEEKNEEIQERidqlYDILEREvkaRKYVEKNSDTLPDFLEHAKE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 488 QKDVLLQKfnekdLEVIQQNcYLMAAEDLELrseglitekcssqqppgSKTIFSKEKKQSSDYEELIQVLKKEQDIYTHL 567
Cdd:PRK04778 325 QNKELKEE-----IDRVKQS-YTLNESELES-----------------VRQLEKQLESLEKQYDEITERIAEQEIAYSEL 381
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 58535453 568 VKSLQES----DSINNLQAELNKifALrKQLEQDVLSYQNLRKTLEEQISEIRRREEES 622
Cdd:PRK04778 382 QEELEEIlkqlEEIEKEQEKLSE--ML-QGLRKDELEAREKLERYRNKLHEIKRYLEKS 437
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
55-499 |
7.21e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 55 TRARNMKDFENQITELKKENFNLKLRIYfleermqqefhgptehiyktniELKVEVESLKRELQEREQllikaskavesL 134
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIK----------------------NLESQINDLESKIQNQEK-----------L 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 135 AEAGGSEIQRVKEDARKKVQQVEDLLTKRILLLE--KDVTAAQAELEKAFagtETEKALRLRLESKLSEMKKMHEgdlam 212
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSeiKDLTNQDSVKELII---KNLDNTRESLETQLKVLSRSIN----- 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 213 alvldEKDRLIEELKLSLKSKEALIQCLKEEKSQMacpDENVSsgelrglcaapreekereteaaqmEHQKERNSFEERI 292
Cdd:TIGR04523 479 -----KIKQNLEQKQKELKSKEKELKKLNEEKKEL---EEKVK------------------------DLTKKISSLKEKI 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 293 QALEEDLREKEREIAT--EKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFqgseDYE 370
Cdd:TIGR04523 527 EKLESEKKEKESKISDleDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKK----DLI 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 371 TALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEV 450
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELM 682
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 58535453 451 NEREKAMENRYK---------SLLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFNEK 499
Cdd:TIGR04523 683 KDWLKELSLHYKkyitrmiriKDLPKLEEKYKEIEKELKKLDEFSKELENIIKNFNKK 740
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
402-624 |
7.84e-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: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 402 KKITQELSDLQQERERLEK---DLEEAHREKSKGDCTIRDLRNEVEKLRnevNEREKAMenRYKSLLSESNK-----KLH 473
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKaleELEEVEENIERLDLIIDEKRQQLERLR---REREKAE--RYQALLKEKREyegyeLLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 474 NQEQVIKHLTESTNQKDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEGLITEKCSSQQPPGSKTIFSKEKKQSSdYEEL 553
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAS-LERS 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58535453 554 IQVLKKEQdiythlvKSLQEsdSINNLQAELNKIFALRKQLEQDVLSYQNLRKTLEEQISEIRRREEESFS 624
Cdd:TIGR02169 310 IAEKEREL-------EDAEE--RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA 371
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1400-1576 |
9.55e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 9.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 1400 QEIRTLRKRLEESIKTNEKLRKQLERQGSEFVQGSTSIFASGSELHSSLTSEIHFLRKQNQalnamLIKGSRDKQKENDK 1479
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR-----LEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 1480 LRESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQEVRCSGQELSRVQEEV-KLRQQLLSQNDKLLQSLR 1558
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELaEAEEELEELAEELLEALR 393
|
170
....*....|....*...
gi 58535453 1559 VELKAYEKLDEEHRRLRD 1576
Cdd:COG1196 394 AAAELAAQLEELEEAEEA 411
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
282-364 |
9.58e-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: 38.33 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 282 QKERNSFEERIQALEEDLREKEREIATEKKNsLKRDKAiqglTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQ 361
Cdd:smart00935 17 KAAQKQLEKEFKKRQAELEKLEKELQKLKEK-LQKDAA----TLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQE 91
|
...
gi 58535453 362 EFQ 364
Cdd:smart00935 92 ELQ 94
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
115-358 |
9.87e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 115 RELQEREQLLIKASKAVESLA--EAGGSEIQRVKEDARKKVQQVEDL----LTKRILLLEKDVTAAQAELEKAfagtete 188
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEpiRELAERYAAARERLAELEYLRAALrlwfAQRRLELLEAELEELRAELARL------- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 189 KALRLRLESKLSEMKKMHEGdlAMALVLDEKDRLIEELKLSLKSKEALiqclKEEKSQmacpdenvSSGELRGLCAA--- 265
Cdd:COG4913 308 EAELERLEARLDALREELDE--LEAQIRGNGGDRLEQLEREIERLERE----LEERER--------RRARLEALLAAlgl 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 266 PREEKERETEAAQMEHQKERNSFEERIQALEEDLREKEREIATEKKnslkrdkaiqgltmALKSKEKKVEELNSEIEKLS 345
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR--------------ELRELEAEIASLERRKSNIP 439
|
250
....*....|...
gi 58535453 346 AAFAKAREALQKA 358
Cdd:COG4913 440 ARLLALRDALAEA 452
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
284-459 |
9.96e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 284 ERNSFEERI---QALEEDLREKEREIATEKKNslKRDKA---IQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQK 357
Cdd:PHA02562 189 KIDHIQQQIktyNKNIEEQRKKNGENIARKQN--KYDELveeAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58535453 358 AQTQEFQGSEDYETALSGKEALSAalrSQNLtkSTENHRL---RRSIKKITQELSDLQQERERLEKDLEEAhREKSKgdc 434
Cdd:PHA02562 267 IKSKIEQFQKVIKMYEKGGVCPTC---TQQI--SEGPDRItkiKDKLKELQHSLEKLDTAIDELEEIMDEF-NEQSK--- 337
|
170 180 190
....*....|....*....|....*....|..
gi 58535453 435 TIRDLRNEVEK-------LRNEVNEREKAMEN 459
Cdd:PHA02562 338 KLLELKNKISTnkqslitLVDKAKKVKAAIEE 369
|
|
| |
