|
Name |
Accession |
Description |
Interval |
E-value |
| Cnn_1N |
pfam07989 |
Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated ... |
143-210 |
3.30e-17 |
|
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: 76.79 E-value: 3.30e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392194 143 RDFEKHLNDLKKENFSLKLRIYFLEERMQQKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTW 210
Cdd:pfam07989 1 REQEKQIDKLKKENFNLKLKIHFLEERLEKLAPEQIEEALKENIELKVELETLQRELKKLKKLLREAE 68
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
140-816 |
9.62e-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: 72.78 E-value: 9.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 140 QALRDFEKHLNDLKKENFSLKLRIYFLE-ERMQQKYEASREDIYKRNIELkVEVESLKRELQDKKQHLDKTWADVENLNS 218
Cdd:TIGR02168 220 AELRELELALLVLRLEELREELEELQEElKEAEEELEELTAELQELEEKL-EELRLEVSELEEEIEELQKELYALANEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 219 QNEAELRRQFEERQQ------ETEHVYELLENKIQLLQEESRL-------AKNEAARMAALVEAEKECNLELSEKLKGVT 285
Cdd:TIGR02168 299 RLEQQKQILRERLANlerqleELEAQLEELESKLDELAEELAEleekleeLKEELESLEAELEELEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 286 KNWEDVPGDQvkpDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEPTSMEVQPMTEELLKQQklnshE 365
Cdd:TIGR02168 379 EQLETLRSKV---AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEL-----E 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 366 TTITQQSVSDSHLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRER------------E 433
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlseliS 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 434 TEELYQ--------------VIEGQNDTMAKLrEMLHQSQLGQLHSSEGTS----------------------------- 470
Cdd:TIGR02168 531 VDEGYEaaieaalggrlqavVVENLNAAKKAI-AFLKQNELGRVTFLPLDSikgteiqgndreilkniegflgvakdlvk 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 471 -PAQQQVALLDLQSALFCSQ-----LEIQKLQR----------------------------VVRQKERQLADAKQCVQFV 516
Cdd:TIGR02168 610 fDPKLRKALSYLLGGVLVVDdldnaLELAKKLRpgyrivtldgdlvrpggvitggsaktnsSILERRREIEELEEKIEEL 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 517 EAAAHESEQQkeaswkhnqelRKALQQLQEELQNKSQQLRAWEAEKYNEI----------RTQEQNIQHLNHSLSHK-EQ 585
Cdd:TIGR02168 690 EEKIAELEKA-----------LAELRKELEELEEELEQLRKELEELSRQIsalrkdlarlEAEVEQLEERIAQLSKElTE 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 586 LLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDkavaLERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLS 665
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ----LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 666 SNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQlqtsLHDRNKEVEDLSATLlcklgpg 745
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA----LALLRSELEELSEEL------- 903
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2056392194 746 qsEIAEELCQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMERNSELQA 816
Cdd:TIGR02168 904 --RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR 972
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
197-724 |
2.15e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 197 RELQDKKQHLDKTWADVENLNSQNEAELrRQFEERQQETEHVYELLENKIQLLQEESRLAKNEAARMAALVEAEKECNLE 276
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAEL-AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 277 LSEKLKGVTKNWEDVP----GDQVKPDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEPTSMEVQPMT 352
Cdd:COG1196 314 LEERLEELEEELAELEeeleELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 353 EELLKQQKLNSHETTITQQSVSDSHLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRER 432
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 433 ETEELYQVIEGQNDTMAKLREMLHQSQLGQLHSSEGTSPAQ---------QQVALLDLQSALFCSQLEIQKLQRVVRQKE 503
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALllaglrglaGAVAVLIGVEAAYEAALEAALAAALQNIVV 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 504 RQLADAKQCVQFV--EAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLS 581
Cdd:COG1196 554 EDDEVAAAAIEYLkaAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 582 HKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLR 661
Cdd:COG1196 634 AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAE 713
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2056392194 662 DVLSSNEATMQSMESLLRAKG--LEVEQLSTTCQNLQWLKEEMETKFSRwqKEQESIIQQLQTSL 724
Cdd:COG1196 714 EERLEEELEEEALEEQLEAEReeLLEELLEEEELLEEEALEELPEPPDL--EELERELERLEREI 776
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
489-994 |
1.57e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 489 QLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAEKYNEIRT 568
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 569 QEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKFSAL---EEKEKELRQ 645
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALraaAELAAQLEE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 646 LRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQTSLH 725
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 726 DRNKEVEDLSATLLCK---LGPGQSEIAEELCQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEK 802
Cdd:COG1196 485 ELAEAAARLLLLLEAEadyEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIE 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 803 L------------------VQALMERNSELQALRQYLGGRDSLMSQAPISNQQAEVTPTGRLGKQTDQGSMQIPSRDDST 864
Cdd:COG1196 565 YlkaakagratflpldkirARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAG 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 865 SLTAKEDVSIPRSTLGDLDTVAGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAA-DMESLTRNIQI 943
Cdd:COG1196 645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAeEERLEEELEEE 724
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2056392194 944 KEDLIKDLQMQLVDPEDIPAMERLTQEVLLLREKVASVESQGQEISGNRRQ 994
Cdd:COG1196 725 ALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
307-1016 |
1.93e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 307 QRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEpTSMEVQPMTEELLKQQK-LNSH-------ETTITQQSVSDSHL 378
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEE-LRLEVSELEEEIEELQKeLYALaneisrlEQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 379 ----AELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREM 454
Cdd:TIGR02168 315 erqlEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 455 L--HQSQLGQLhSSEGTSPAQQQVALLDLQSALFCSQLE--IQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEAS 530
Cdd:TIGR02168 395 IasLNNEIERL-EARLERLEDRRERLQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEALEELREELEEA 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 531 WKHNQELR----------KALQQLQEELQNKSQQLRAWEAEKyneiRTQEQNIQHLNHSLSHKEQLLQEFRELLQYR--- 597
Cdd:TIGR02168 474 EQALDAAErelaqlqarlDSLERLQENLEGFSEGVKALLKNQ----SGLSGILGVLSELISVDEGYEAAIEAALGGRlqa 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 598 ---DNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLRLA--VRERDHDLERLRDVLSSNEATMQ 672
Cdd:TIGR02168 550 vvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAkdLVKFDPKLRKALSYLLGGVLVVD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 673 SMESLLR-AKGLEVEQLSTTCQNLQWLKEEMETKFSRWQ-----------KEQESIIQQLQTSLHDRNKEVEDLSATLlc 740
Cdd:TIGR02168 630 DLDNALElAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTnssilerrreiEELEEKIEELEEKIAELEKALAELRKEL-- 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 741 klgpgqSEIAEELCQRLQRKERMLQDlLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMERNSELQALRQY 820
Cdd:TIGR02168 708 ------EELEEELEQLRKELEELSRQ-ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 821 LGGRDSLMSQAP------------ISNQQAEVTPTGRLGKQTDQGSMQIPSRDDSTSLTAKEDVSIPRSTLGDLdtvAGL 888
Cdd:TIGR02168 781 EAEIEELEAQIEqlkeelkalreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI---ESL 857
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 889 EKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAADMESLTRNIQIKEDLIKDLQMQLVDPEDipAMERLT 968
Cdd:TIGR02168 858 AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL--RLEGLE 935
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 2056392194 969 QEVLLLREKVASVESQGQEISGNRRQQLLLMLEGLVDERSRLNEALQA 1016
Cdd:TIGR02168 936 VRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
213-818 |
5.75e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.92 E-value: 5.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 213 VENLNSQNEAELRRQfEERQQETEHVYELLENKIQLLQEESRLAKNEAARMA----ALVEAEKECNLELSEKLKGVTKNW 288
Cdd:TIGR02168 202 LKSLERQAEKAERYK-ELKAELRELELALLVLRLEELREELEELQEELKEAEeeleELTAELQELEEKLEELRLEVSELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 289 EDVPGDQVKPDQYTEALAQRDKRIEELNQSLAA----QERLVEQLSREKQQLLHLLEEPTSMEVQpmTEELLKQQKLNSH 364
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANlerqLEELEAQLEELESKLDELAEELAELEEK--LEELKEELESLEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 365 EttitqqsvsdshLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQ 444
Cdd:TIGR02168 359 E------------LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 445 NDTMAKLREMLHQSQLGQLHSSEgtspAQQQVALLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEA--AAHE 522
Cdd:TIGR02168 427 LKKLEEAELKELQAELEELEEEL----EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERlqENLE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 523 SEQQKEASWKHNQELRKALQQ-------------------LQEELQ-----NKSQQLRAWEAEKYNEI------------ 566
Cdd:TIGR02168 503 GFSEGVKALLKNQSGLSGILGvlselisvdegyeaaieaaLGGRLQavvveNLNAAKKAIAFLKQNELgrvtflpldsik 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 567 --------RTQEQNIQHLNHSLSHKEQLLQEFRELLQYR-------DNSD------KTLEANEML--------------- 610
Cdd:TIGR02168 583 gteiqgndREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvDDLDnalelaKKLRPGYRIvtldgdlvrpggvit 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 611 ----------------LEKLRQRI---HDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATM 671
Cdd:TIGR02168 663 ggsaktnssilerrreIEELEEKIeelEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 672 QSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQTSLHDRNKEVEDLSA-----TLLCKLGPGQ 746
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraelTLLNEEAANL 822
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2056392194 747 SEIAEELCQRLQRKERMLQDlLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMERNSELQALR 818
Cdd:TIGR02168 823 RERLESLERRIAATERRLED-LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
536-806 |
2.00e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.01 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 536 ELRKALQQLQEE---------LQNKSQQLRAWEaeKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDnsdKTLEA 606
Cdd:TIGR02169 195 EKRQQLERLRRErekaeryqaLLKEKREYEGYE--LLKEKEALERQKEAIERQLASLEEELEKLTEEISELE---KRLEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 607 NEMLLEKLRQRIHDKAVALERAIDEKfsaLEEKEKELRQLRLAVRERDHDLERLrdvlssnEATMQSMESLLRAKGLEVE 686
Cdd:TIGR02169 270 IEQLLEELNKKIKDLGEEEQLRVKEK---IGELEAEIASLERSIAEKERELEDA-------EERLAKLEAEIDKLLAEIE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 687 QLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQtSLHDRNKEVEDLSATLLCKLGPGQSEIAEelcqrLQRKERMLQD 766
Cdd:TIGR02169 340 ELEREIEEERKRRDKLTEEYAELKEELEDLRAELE-EVDKEFAETRDELKDYREKLEKLKREINE-----LKRELDRLQE 413
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2056392194 767 LLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQA 806
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
146-647 |
8.72e-09 |
|
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: 59.65 E-value: 8.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 146 EKHLNDLKKENFSLKLRIYFLEERMQQ--KYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTWADVENLNSQNEaE 223
Cdd:TIGR04523 186 QKNIDKIKNKLLKLELLLSNLKKKIQKnkSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN-K 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 224 LRRQFEERQQETEHVYELLENKIQLLQEesrlAKNEaarmaaLVEAEKECNLELSEKLKGVTKNWEDvpgdqvKPDQYTE 303
Cdd:TIGR04523 265 IKKQLSEKQKELEQNNKKIKELEKQLNQ----LKSE------ISDLNNQKEQDWNKELKSELKNQEK------KLEEIQN 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 304 ALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEPTSmEVQPMTEEllKQQKLNSHETTITQQSvsdshlaELQE 383
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQN-EIEKLKKE--NQSYKQEIKNLESQIN-------DLES 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 384 KIQQTEATNKILQEKlnemsyelkcaqessqkqdgtIQNLKETLKSRERETEELYQVIEGQNDTMAKLREMLHQSQLGQL 463
Cdd:TIGR04523 399 KIQNQEKLNQQKDEQ---------------------IKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 464 HSSEGTSPAQQQVALLdlqsalfcsQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKeaswkhnqelrKALQQ 543
Cdd:TIGR04523 458 NLDNTRESLETQLKVL---------SRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV-----------KDLTK 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 544 LQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSH---KEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRiHD 620
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQK-EK 596
|
490 500
....*....|....*....|....*..
gi 2056392194 621 KAVALERAIDEKFSALEEKEKELRQLR 647
Cdd:TIGR04523 597 EKKDLIKEIEEKEKKISSLEKELEKAK 623
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
427-1069 |
1.10e-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: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 427 LKSRERETEELYQVIEGQNDTMAKLREMLHQSQLGQLHSSEGTSPAQQQVAllDLQSALFCSQLEIQKLQRVVRQKERQL 506
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE--ELQKELYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 507 ADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAE--------------------KYNEI 566
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEleelesrleeleeqletlrsKVAQL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 567 RTQEQNIQ--------HLNHSLSHKEQLLQEFRELLQYRDNSDktLEANEMLLEKLRQRIHDKAVALERAIdekfSALEE 638
Cdd:TIGR02168 392 ELQIASLNneierleaRLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLE----EALEE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 639 KEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKfSRWQKEQESIIQ 718
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVD-EGYEAAIEAALG 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 719 QLQTSLHDRNKEVEDLSATLLCKLGPGQSEIAEElcqrlqrkermlqDLLSDRNKQVLEHEM--EIQGLLQSVSTREqES 796
Cdd:TIGR02168 545 GRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPL-------------DSIKGTEIQGNDREIlkNIEGFLGVAKDLV-KF 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 797 QAAAEKLVQALMERNSELQALRQYLGGRDSLMSQAPISNQQAE-VTPTGRLGKQTDQGSMQIPSRdDSTSLTAKEDVSIP 875
Cdd:TIGR02168 611 DPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDlVRPGGVITGGSAKTNSSILER-RREIEELEEKIEEL 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 876 RSTLGDLDT-VAGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAADMESLTRNIQIKEDLIKDLQMQ 954
Cdd:TIGR02168 690 EEKIAELEKaLAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEER 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 955 LvdpedipamERLTQEVLLLREKVASVESQGQEISgNRRQQLLLMLEGLVDERSRLNEALQAERQLYSSLVKFHAhpESS 1034
Cdd:TIGR02168 770 L---------EEAEEELAEAEAEIEELEAQIEQLK-EELKALREALDELRAELTLLNEEAANLRERLESLERRIA--ATE 837
|
650 660 670
....*....|....*....|....*....|....*
gi 2056392194 1035 ERDRTLQVELEGAQVLRSRLEEVLGRSLERLNRLE 1069
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
153-839 |
6.56e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 56.90 E-value: 6.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 153 KKENFSLKLRIYFLEERMQQKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTWADVENLNSQNEAELRRQFEERQ 232
Cdd:TIGR00618 186 FAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 233 QETEHVYELLENKIQLLQEESRLAKnEAARMAALVEAEKECNLELSEKLKGVtknwedvpgdQVKPDQYTEALAQRDKRI 312
Cdd:TIGR00618 266 RARIEELRAQEAVLEETQERINRAR-KAAPLAAHIKAVTQIEQQAQRIHTEL----------QSKMRSRAKLLMKRAAHV 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 313 EElNQSLAAQERLVEQLSREKQQLLHLLEEPTSMEVQ-----PMTEELLKQQKLNSHETTITQQSVSD-SHLAELQEKIQ 386
Cdd:TIGR00618 335 KQ-QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIscqqhTLTQHIHTLQQQKTTLTQKLQSLCKElDILQREQATID 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 387 QTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQviegqndtmaKLREMLHQSQLGQLHSS 466
Cdd:TIGR00618 414 TRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ----------SLKEREQQLQTKEQIHL 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 467 EGTSPAQQQVALLdlqsalfcsqLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQE 546
Cdd:TIGR00618 484 QETRKKAVVLARL----------LELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTS 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 547 ELqNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDN-SDKTLEANEMLLEKLRQRIHDKAVAL 625
Cdd:TIGR00618 554 ER-KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEaEDMLACEQHALLRKLQPEQDLQDVRL 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 626 ERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRD----VLSSNEATMQSMESLLRAKGLEVEQLStTCQNLQWLKEE 701
Cdd:TIGR00618 633 HLQQCSQELALKLTALHALQLTLTQERVREHALSIRVlpkeLLASRQLALQKMQSEKEQLTYWKEMLA-QCQTLLRELET 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 702 METKFSRWQKEQESIIQQLQTSLHDRN-------KEVEDLSATLLCKLGPGQSEIAEELCQRLQR--KERMLQDLLSDRN 772
Cdd:TIGR00618 712 HIEEYDREFNEIENASSSLGSDLAAREdalnqslKELMHQARTVLKARTEAHFNNNEEVTAALQTgaELSHLAAEIQFFN 791
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2056392194 773 KQVLEHEMEIQGLLQSVSTR----EQESQAAAEKLVQALMERNSELQALRQYLGGRDSLMSQAPISNQQAE 839
Cdd:TIGR00618 792 RLREEDTHLLKTLEAEIGQEipsdEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA 862
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
525-1096 |
1.68e-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: 55.83 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 525 QQKEASWKHNQELRKALQQLQEELQNKSQ-------QLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYR 597
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQeleekleELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 598 DNSDKTLEANEMLLEKLRQRIHDKAVALERAIDE---KFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSM 674
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEElkeELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 675 ESLLRAK----GLEVEQLSTTCQNLQWLKEEMETKFSRWQ-KEQESIIQQLQTSLHDRNKEVEDLSATLlcKLGPGQSEI 749
Cdd:TIGR02168 395 IASLNNEierlEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEAL--EELREELEE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 750 AEEL-------CQRLQRKERMLQDLL------SDRNKQVLEHEMEIQGLLQSVSTR-------EQESQAAAEKLVQALME 809
Cdd:TIGR02168 473 AEQAldaaereLAQLQARLDSLERLQenlegfSEGVKALLKNQSGLSGILGVLSELisvdegyEAAIEAALGGRLQAVVV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 810 RNSE-----LQALRQYLGGRDSLMsqAPISNQQAEVTPTGRLGKQTDQGSMQIPSRDDSTSLTAKEDVSiprSTLGDLDT 884
Cdd:TIGR02168 553 ENLNaakkaIAFLKQNELGRVTFL--PLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS---YLLGGVLV 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 885 VAGLEKELSNAKEELE----------------LMAKKERESQMELSALQSMMAVQEEELQVQAADMESLTRNIQIKEDLI 948
Cdd:TIGR02168 628 VDDLDNALELAKKLRPgyrivtldgdlvrpggVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKEL 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 949 KDLQMQLVDPEDIPamERLTQEVLLLREKVASVESQGQEISgNRRQQLLLMLEGLVDERSRLNEALQAERQLYSSLVKfh 1028
Cdd:TIGR02168 708 EELEEELEQLRKEL--EELSRQISALRKDLARLEAEVEQLE-ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA-- 782
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392194 1029 ahpESSERDRTLQVELEGAQVLRSRLEEVLGRsLERLNRLETLAAIGGAAAGDDTEDTSTEFTDSIEE 1096
Cdd:TIGR02168 783 ---EIEELEAQIEQLKEELKALREALDELRAE-LTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
376-661 |
3.98e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 376 SHLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREML 455
Cdd:TIGR02169 695 SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 456 H--QSQLGQLHSSEGTSPAQQQVALL---------------DLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEA 518
Cdd:TIGR02169 775 HklEEALNDLEARLSHSRIPEIQAELskleeevsriearlrEIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 519 AAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAekynEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRD 598
Cdd:TIGR02169 855 EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA----QLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 599 NSDKTLE----------ANEMLLEKLRQRIHDKAVALE-------RAIDE------KFSALEEKEKELRQLRLAVRERDH 655
Cdd:TIGR02169 931 EELSEIEdpkgedeeipEEELSLEDVQAELQRVEEEIRalepvnmLAIQEyeevlkRLDELKEKRAKLEEERKAILERIE 1010
|
....*.
gi 2056392194 656 DLERLR 661
Cdd:TIGR02169 1011 EYEKKK 1016
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
143-739 |
8.76e-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: 53.10 E-value: 8.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 143 RDFEKHLNDLKKENFSLKLRIYFLEERMQQKYEASREDIYKRNIeLKVEVESLKRELQDKKQHLDKTWADVENLNSQ--- 219
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKI-LEQQIKDLNDKLKKNKDKINKLNSDLSKINSEikn 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 220 -------NEAELRRQFEERQQETEHVYELLeNKIQLLQEESRLAKNEAARMAALVEAEKECNLELSEKLKGVTKNWEDVP 292
Cdd:TIGR04523 115 dkeqknkLEVELNKLEKQKKENKKNIDKFL-TEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 293 GDQVKPDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEptsmevqpmteellKQQKLNSHETTITQQS 372
Cdd:TIGR04523 194 NKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINE--------------KTTEISNTQTQLNQLK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 373 VSDSH-LAELQEKIQQTEATNKILQEKLNEMS-YELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAK 450
Cdd:TIGR04523 260 DEQNKiKKQLSEKQKELEQNNKKIKELEKQLNqLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQ 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 451 LREmlhqsQLGQLHSSegtspaqqqvaLLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEAS 530
Cdd:TIGR04523 340 LNE-----QISQLKKE-----------LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQ 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 531 WKHNQELRKALQQLQEELQNKSQQ---LRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEAN 607
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEierLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 608 emlLEKLRQRIHDKAVALERAIDEKfSALEEKEKELRQLRLAVRERDHDLE----RLRDVLSSNEATMQSMESLLRAKGL 683
Cdd:TIGR04523 484 ---LEQKQKELKSKEKELKKLNEEK-KELEEKVKDLTKKISSLKEKIEKLEsekkEKESKISDLEDELNKDDFELKKENL 559
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 2056392194 684 EvEQLSTTCQNLQWLKEEmETKFSRWQKEQESIIQQLQTSLHDRNKEVEDLSATLL 739
Cdd:TIGR04523 560 E-KEIDEKNKEIEELKQT-QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS 613
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
170-975 |
1.74e-06 |
|
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: 52.43 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 170 MQQKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTwADVENLNSQNEAELRRQFEERQQETEHVYELLENKI--- 246
Cdd:pfam15921 90 LQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAM-ADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLeds 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 247 --QLLQEESRLAKNEAARM---AALVEAEKECNLELSEKLKGVTKNWEDVpGDQVkpdqyTEALAQRDKRIEELNQSLAA 321
Cdd:pfam15921 169 ntQIEQLRKMMLSHEGVLQeirSILVDFEEASGKKIYEHDSMSTMHFRSL-GSAI-----SKILRELDTEISYLKGRIFP 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 322 QERLVEQLSREKQQLLhlleeptsmevqpmteELLKQQKLNSHETTITQQSVsdsHLAELQEKIQQTEATNKILQEKLNE 401
Cdd:pfam15921 243 VEDQLEALKSESQNKI----------------ELLLQQHQDRIEQLISEHEV---EITGLTEKASSARSQANSIQSQLEI 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 402 MSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQviegqndtmAKLREMLHQSQLGQLHSSEGTSPAQQqvalLDL 481
Cdd:pfam15921 304 IQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYE---------DKIEELEKQLVLANSELTEARTERDQ----FSQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 482 QSALFCSQLeiQKLQRVVRQKERQLAdakqcvqfveaaaHESEQQKEAsWKHN-------QELRKALQQLQEELQNKSQQ 554
Cdd:pfam15921 371 ESGNLDDQL--QKLLADLHKREKELS-------------LEKEQNKRL-WDRDtgnsitiDHLRRELDDRNMEVQRLEAL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 555 LRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALEraidEKFS 634
Cdd:pfam15921 435 LKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ----EKER 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 635 ALEEKEKELRQLRLAVRERDHDLERLR---DVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQK 711
Cdd:pfam15921 511 AIEATNAEITKLRSRVDLKLQELQHLKnegDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQV 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 712 EQesiiQQLQTSLHDRNKEVEDLSatLLCKLGPGQSEIAEELCQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVST 791
Cdd:pfam15921 591 EK----AQLEKEINDRRLELQEFK--ILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKT 664
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 792 REQESQAAAEKLvqALMERNSELQALRQYLGGRDSLMSQAPISNQQAEVTPTGRLGKQTDQGSMQIpsrddstSLTAKED 871
Cdd:pfam15921 665 SRNELNSLSEDY--EVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKV-------AMGMQKQ 735
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 872 VSIPRSTLGDLDT-VAGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAADMESLTRNIQIKEDLIKD 950
Cdd:pfam15921 736 ITAKRGQIDALQSkIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDK 815
|
810 820
....*....|....*....|....*
gi 2056392194 951 LQMQLVDPEDIpaMERLTQEVLLLR 975
Cdd:pfam15921 816 ASLQFAECQDI--IQRQEQESVRLK 838
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
169-679 |
1.89e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.28 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 169 RMQQKYEASREDIYKRNIELKVEVESL---KRELQDKKQHLDKTWADVENLNSQNEAELRRQFEERQQETEhvyelLENK 245
Cdd:TIGR00618 358 RDAHEVATSIREISCQQHTLTQHIHTLqqqKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAH-----AKKQ 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 246 IQLLQEESRLAKNEAARMAALVEAEKECNLELSEKLKGVTKNWEDVpgdQVKPDQYTEALAQRDKRIEELnqslAAQERL 325
Cdd:TIGR00618 433 QELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK---EQIHLQETRKKAVVLARLLEL----QEEPCP 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 326 VEQLSREKQQLLHLLEEPTSMEVQPMTEELLKQQKLNSHETTITQQSVSDSHLAELQEKIQQTEATNKILQEKLNEMSYE 405
Cdd:TIGR00618 506 LCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKED 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 406 L-KCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDtmakLREMLHQSQLGQLHSSEGTSPAQQQVALL---DL 481
Cdd:TIGR00618 586 IpNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDL----QDVRLHLQQCSQELALKLTALHALQLTLTqerVR 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 482 QSALFCSQLEIQKLQRVVRQ------KERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNK---- 551
Cdd:TIGR00618 662 EHALSIRVLPKELLASRQLAlqkmqsEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARedal 741
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 552 SQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALEraiDE 631
Cdd:TIGR00618 742 NQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDE---DI 818
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2056392194 632 KFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLR 679
Cdd:TIGR00618 819 LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQ 866
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
378-592 |
4.11e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 378 LAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREMLhQ 457
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL-A 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 458 SQLGQLHSSEGTSPAQQQVALLDLQSALFCSQLeIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQEL 537
Cdd:COG4942 108 ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2056392194 538 RKALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRE 592
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
167-653 |
5.18e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 167 EERMQQKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTWADVENLNSQNEAELRRQFEERQQETEHVYELLE-NK 245
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkKK 1392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 246 IQLLQEESRLAKNEAARMAALVEAEKECNlELSEKLKGVTKNWE-DVPGDQVKPDQYTEALAQRDKRIEELNQSlAAQER 324
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKKKADEaKKKAEEAKKADEAKKKAEEAKKAEEAKKK-AEEAK 1470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 325 LVEQLSREKQQLLHLLE-EPTSMEVQPMTEELLK--QQKLNSHETTITQQSVSDSHLAELQEKIQQTEATNKILQEKLNE 401
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEaKKKAEEAKKKADEAKKaaEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE 1550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 402 M--SYELKCAQESSQKQDGtiQNLKETLKSRERETEELYQVIEGQNDTMAKLREMLHQSQLGQLHSSEGTSPAQQQVALL 479
Cdd:PTZ00121 1551 LkkAEELKKAEEKKKAEEA--KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA 1628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 480 DlQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEA--SWKHNQELRKALQQL--QEELQNKSQQL 555
Cdd:PTZ00121 1629 E-EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALkkEAEEAKKAEEL 1707
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 556 RAWEAEkynEIRTQEQNIQHLNHSLSHKEQLLQEFREllqyRDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKFSA 635
Cdd:PTZ00121 1708 KKKEAE---EKKKAEELKKAEEENKIKAEEAKKEAEE----DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
490
....*....|....*...
gi 2056392194 636 LEEKEKELRQLRLAVRER 653
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEVDK 1798
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
168-691 |
6.00e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 168 ERMQQKYEASREDIyKRNIELKVEVESLKReLQDKKQHLDKTWADVENLNSQNE-AELRRQ--------FEERQQETEHv 238
Cdd:PRK02224 179 ERVLSDQRGSLDQL-KAQIEEKEEKDLHER-LNGLESELAELDEEIERYEEQREqARETRDeadevleeHEERREELET- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 239 yelLENKIQLLQEESRLAKNEAARMAALVEAEKECNLELSEKLKGVTKNWEDVPGDQVKPDQYTEALAQRDKRIEE-LNQ 317
Cdd:PRK02224 256 ---LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDrLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 318 SLAAQERLVEQLSREKQQLLHLLEEPTSMEVQPMTEELLKQQKLNSHETTITQQSVSDSHLAELQEKIQQTEATNKILQE 397
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAED 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 398 KLNEMSYELKCAQESSQKQDGTIQNLKETLKSRER--------------ETEELYQVIEGQNDTMAKLREMLHQSQLGQ- 462
Cdd:PRK02224 413 FLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVe 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 463 -----LHSSEGTSPAQQQVALLDLQSALFCSQLEIQKlqRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQEL 537
Cdd:PRK02224 493 eveerLERAEDLVEAEDRIERLEERREDLEELIAERR--ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEA 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 538 RKALQQLQEELQNKSQQLRAWE--AEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEA--NEMLLEK 613
Cdd:PRK02224 571 REEVAELNSKLAELKERIESLEriRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAefDEARIEE 650
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392194 614 LRQRiHDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRakglEVEQLSTT 691
Cdd:PRK02224 651 ARED-KERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEALEALYD----EAEELESM 723
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
229-561 |
6.25e-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: 50.45 E-value: 6.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 229 EERQQETEHVYELLENKIQLLQEEsrlaKNEAARMAALVEAEKEcnLELSEKLKGVTKNWEDVPGDQVKPDQYTEALAQR 308
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKRE--YEGYELLKEKEALERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 309 DKRIEELNQSLAAQERLVEQLSREkqqllhlleeptsmeVQPMTEELLKQQKLNSHETTITQQSVSDShLAELQEKIQQT 388
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELNKK---------------IKDLGEEEQLRVKEKIGELEAEIASLERS-IAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 389 EATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREMLhqsqlgqlhsseg 468
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL------------- 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 469 tspAQQQVALLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKE--------ASWKHNQ----- 535
Cdd:TIGR02169 388 ---KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEdkaleikkQEWKLEQlaadl 464
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2056392194 536 ---------------ELRKALQQLQEELQNKSQQLRAWEAE 561
Cdd:TIGR02169 465 skyeqelydlkeeydRVEKELSKLQRELAEAEAQARASEER 505
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
142-716 |
9.99e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 9.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 142 LRDFEKHLNDLKKENFSLKLRIYFLEermqqKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTWADVENLnsqne 221
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLE-----KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKL----- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 222 aelrrqfEERQQETEHVYELLEN-KIQLLQEESRLAKNEaarmAALVEAEKECNlELSEKLKGVTKNWEDVPGDQVKPDQ 300
Cdd:PRK03918 227 -------EKEVKELEELKEEIEElEKELESLEGSKRKLE----EKIRELEERIE-ELKKEIEELEEKVKELKELKEKAEE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 301 YTEALAQRDKRIEELNQSlaaqERLVEQLSREKQQLLHLLEEPTSMEVQpmTEELLKQQKLNSHETTITQQSVSDSHLA- 379
Cdd:PRK03918 295 YIKLSEFYEEYLDELREI----EKRLSRLEEEINGIEERIKELEEKEER--LEELKKKLKELEKRLEELEERHELYEEAk 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 380 ELQEKIQQTEATNKILQ-EKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREML--- 455
Cdd:PRK03918 369 AKKEELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELtee 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 456 HQSQLGQLHSSEGTSPAQQQVALLDLQSALFCSQLEIQKlqrvVRQKERQLADAKQCVQFVEAAAHESE----QQKEASW 531
Cdd:PRK03918 449 HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEK----VLKKESELIKLKELAEQLKELEEKLKkynlEELEKKA 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 532 KHNQELRKALQQLQEELQN------KSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHK-----EQLLQEFRELLQYRD-- 598
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEIKSlkkeleKLEELKKKLAELEKKLDELEEELAELLKELEELgfesvEELEERLKELEPFYNey 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 599 ----NSDKTLEANEMLLEKLRqrihDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHdlERLRDVLSSNEATMQSM 674
Cdd:PRK03918 605 lelkDAEKELEREEKELKKLE----EELDKAFEELAETEKRLEELRKELEELEKKYSEEEY--EELREEYLELSRELAGL 678
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 2056392194 675 ESllRAKGLEvEQLSTTCQNLQWLKEEMEtKFSRWQKEQESI 716
Cdd:PRK03918 679 RA--ELEELE-KRREEIKKTLEKLKEELE-EREKAKKELEKL 716
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
393-1018 |
2.97e-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: 48.53 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 393 KILQEKLNEMSYELKCAQEssQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREMLHQSQLGQLHSSEGTSpa 472
Cdd:TIGR02169 214 QALLKEKREYEGYELLKEK--EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ-- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 473 qqqvalLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKS 552
Cdd:TIGR02169 290 ------LRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 553 QQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDkavaLERAIDEK 632
Cdd:TIGR02169 364 EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAG----IEAKINEL 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 633 FSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLqwlkEEMETKFSRWQKE 712
Cdd:TIGR02169 440 EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARAS----EERVRGGRAVEEV 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 713 QESIIQQLQTSLHDRNKEVEDLSATLLCKLGP-------GQSEIAEELCQRLQRKE--RM----LQDLLSDRNKQVLEHE 779
Cdd:TIGR02169 516 LKASIQGVHGTVAQLGSVGERYATAIEVAAGNrlnnvvvEDDAVAKEAIELLKRRKagRAtflpLNKMRDERRDLSILSE 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 780 MEIQGLLQSVSTREQESQAAAEKLVQALMERNSeLQALRQYLGG------------RDSLMSQAPISNQQAEVTPTgRLG 847
Cdd:TIGR02169 596 DGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVED-IEAARRLMGKyrmvtlegelfeKSGAMTGGSRAPRGGILFSR-SEP 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 848 KQTDQGSMQIPSRDDSTSLTAKEDVSIPRSTLGDLDTVAGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEEL 927
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 928 QVQAADMESLTRNIQIKEDLIKDLQMQLVDPEDIPAMER---LTQEVLLLREKVASVESQGQEISG--NRRQQLLLMLEG 1002
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeIQAELSKLEEEVSRIEARLREIEQklNRLTLEKEYLEK 833
|
650
....*....|....*.
gi 2056392194 1003 LVDERSRLNEALQAER 1018
Cdd:TIGR02169 834 EIQELQEQRIDLKEQI 849
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
143-719 |
3.90e-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: 47.79 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 143 RDFEKHLNDLKKENFSLKLRIYFLEERMQQK---YEASREDIYKRNIELKVEVESLKrELQDKKQHLDKTWADVENLNSQ 219
Cdd:pfam05483 229 EEYKKEINDKEKQVSLLLIQITEKENKMKDLtflLEESRDKANQLEEKTKLQDENLK-ELIEKKDHLTKELEDIKMSLQR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 220 NEAELRRQFEERQQETEHVYELLENKIQLLQEesrlaKNEAARMAALVEAEKECNLELSEKLKGVTKNWEDVPGDQVKP- 298
Cdd:pfam05483 308 SMSTQKALEEDLQIATKTICQLTEEKEAQMEE-----LNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIi 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 299 -----------DQYTEALAQRDKRIEELNQSLAAQERLVEqlsrEKQQLLHLLEEPTSMEVQPMTEELLKQQKLNSHETT 367
Cdd:pfam05483 383 tmelqkksselEEMTKFKNNKEVELEELKKILAEDEKLLD----EKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQ 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 368 ITQQSVSDSH----LAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEG 443
Cdd:pfam05483 459 LTAIKTSEEHylkeVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEN 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 444 QNDTMAKLREMLHQSQLGQLHSSEGTspaqqqvalldlqsalfcsQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHES 523
Cdd:pfam05483 539 LEEKEMNLRDELESVREEFIQKGDEV-------------------KCKLDKSEENARSIEYEVLKKEKQMKILENKCNNL 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 524 EQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAEkyneirtqeqnIQHLNHSLSHKEQLLQEFRELLQYRDNSDKT 603
Cdd:pfam05483 600 KKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIK-----------VNKLELELASAKQKFEEIIDNYQKEIEDKKI 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 604 LEANEMLLEKLRQRIHDKAVALERAIDEK-------FSALEEKEKElrQLRLAVRERDHDLERLRDVLSSNEATMQSMES 676
Cdd:pfam05483 669 SEEKLLEEVEKAKAIADEAVKLQKEIDKRcqhkiaeMVALMEKHKH--QYDKIIEERDSELGLYKNKEQEQSSAKAALEI 746
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2056392194 677 LLraKGLEVEQLSTTCQnLQWLKEEMEtKFSRWQKEQESIIQQ 719
Cdd:pfam05483 747 EL--SNIKAELLSLKKQ-LEIEKEEKE-KLKMEAKENTAILKD 785
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
489-779 |
5.10e-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: 47.76 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 489 QLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWE-AEKYNEIR 567
Cdd:TIGR02169 722 EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELS 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 568 TQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLr 647
Cdd:TIGR02169 802 KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL- 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 648 lavRERDHDLERLRDVLSsneatmqsmesllrakglevEQLSTTCQNLQWLKEEMETKFSRwQKEQESIIQQLQtslhDR 727
Cdd:TIGR02169 881 ---ESRLGDLKKERDELE--------------------AQLRELERKIEELEAQIEKKRKR-LSELKAKLEALE----EE 932
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2056392194 728 NKEVEDLSATLLCKlgPGQSEIAEELCQRLQRKERMLQDLLSDRNKQVLEHE 779
Cdd:TIGR02169 933 LSEIEDPKGEDEEI--PEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYE 982
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
468-680 |
6.62e-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: 46.68 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 468 GTSPAQQQVALLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEE 547
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 548 LQNKSQQLRAWEAEKYNEIRTQEQNIQH-------LNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHD 620
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 621 KAVALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRA 680
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
488-664 |
1.76e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 488 SQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEEL-QNKSQQLRAWEAekynEI 566
Cdd:COG4913 272 AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrGNGGDRLEQLER----EI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 567 RTQEQNIQHLNHSLSHKEQLLQEF--------RELLQYRDNSDKTLEAnemlLEKLRQRIHDKAVALERAIDEKFSALEE 638
Cdd:COG4913 348 ERLERELEERERRRARLEALLAALglplpasaEEFAALRAEAAALLEA----LEEELEALEEALAEAEAALRDLRRELRE 423
|
170 180
....*....|....*....|....*.
gi 2056392194 639 KEKELRQLRLAVRERDHDLERLRDVL 664
Cdd:COG4913 424 LEAEIASLERRKSNIPARLLALRDAL 449
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
472-684 |
1.80e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 472 AQQQVALLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNK 551
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 552 SQQLRAWEAEKY--------------NEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQR 617
Cdd:COG4942 103 KEELAELLRALYrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392194 618 IHDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKGLE 684
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
306-684 |
1.94e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 306 AQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEE---------PTSMEVQPMTEELLKQQKLNSHETtitqqsvsds 376
Cdd:PRK04863 782 AAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAfsrfigshlAVAFEADPEAELRQLNRRRVELER---------- 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 377 HLAELQEKIQQTEATNKILQEKLNEMSyelKCAQESSQKQDgtiqnlkETLKSRERETEElyQVIEGQNdtmAKLREMLH 456
Cdd:PRK04863 852 ALADHESQEQQQRSQLEQAKEGLSALN---RLLPRLNLLAD-------ETLADRVEEIRE--QLDEAEE---AKRFVQQH 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 457 QSQLGQLhssegtspaQQQVALLDlqsalfCSQLEIQKLQRVVRQKERQLADAKQCV----QFVEAAAH----ESEQQKE 528
Cdd:PRK04863 917 GNALAQL---------EPIVSVLQ------SDPEQFEQLKQDYQQAQQTQRDAKQQAfaltEVVQRRAHfsyeDAAEMLA 981
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 529 ASWKHNQELRKALQQLQEELQNKSQQLRAWEAE--KYNEIRTQeqniqhLNHSLSHKEQLLQEFRELLQyrdnsDKTLEA 606
Cdd:PRK04863 982 KNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQlaQYNQVLAS------LKSSYDAKRQMLQELKQELQ-----DLGVPA 1050
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 607 NEMLLEKLRQRiHDKAVALERAIDEKFSALEEK----EKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKG 682
Cdd:PRK04863 1051 DSGAEERARAR-RDELHARLSANRSRRNQLEKQltfcEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNG 1129
|
..
gi 2056392194 683 LE 684
Cdd:PRK04863 1130 VE 1131
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
300-669 |
2.32e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 300 QYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLE-EPTSMEVQPMTEELLK-QQKLNSHETTITQQSVSDSH 377
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQElEALEAELAELPERLEElEERLEELRELEEELEELEAE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 378 LAELQEKIQQTEATNKILQEK-LNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREMLH 456
Cdd:COG4717 172 LAELQEELEELLEQLSLATEEeLQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 457 QSQLGQLHS-----SEGTSPAQQQVALLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQK---- 527
Cdd:COG4717 252 LLIAAALLAllglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAlglp 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 528 -EASWKHNQELRKALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLnhslSHKEQLLQEFRELLQYRDNSDKTLEA 606
Cdd:COG4717 332 pDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGV----EDEEELRAALEQAEEYQELKEELEEL 407
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2056392194 607 NEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEA 669
Cdd:COG4717 408 EEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE 470
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
120-819 |
2.73e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 120 VPFVQTYSLRAFEKPPQVQTQALRDFEKHLNDLKKENFS---LKLRIYF-LEERMQQKYEASREDIYKRNIELKVEVESL 195
Cdd:PTZ00121 1018 IDFNQNFNIEKIEELTEYGNNDDVLKEKDIIDEDIDGNHegkAEAKAHVgQDEGLKPSYKDFDFDAKEDNRADEATEEAF 1097
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 196 KRELQDKKQHLDKTWADVENLNSQNEAELRRQFEE--RQQETEHVYELLENKIQLLQEESRLAKnEAARMAALVEAEKEC 273
Cdd:PTZ00121 1098 GKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEarKAEDARKAEEARKAEDAKRVEIARKAE-DARKAEEARKAEDAK 1176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 274 NLELSEKLKGVTKNWEDVPGDQVKPDQYTEAlAQRDKRIEELNQslAAQERLVEQLSREKqqllhlleeptsmEVQPMTE 353
Cdd:PTZ00121 1177 KAEAARKAEEVRKAEELRKAEDARKAEAARK-AEEERKAEEARK--AEDAKKAEAVKKAE-------------EAKKDAE 1240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 354 ELLKQQKLNSHETTITQQSVSDSHLAELQEKIQQTEATNKILQEKLNEMSY--------------ELKCAQESSQKQDGT 419
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKadeakkaeekkkadEAKKKAEEAKKADEA 1320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 420 IQNLKETLKSRE---RETEELYQVIEGQNDTMAKLREMLHQSQLGQLHSSEGTSPAQQQVALLDLQSALFCSQLEIQKLQ 496
Cdd:PTZ00121 1321 KKKAEEAKKKADaakKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 497 RVVRQKERQLADAKQCVQFVEAAAHESEQQKEASW--KHNQELRKAlqqlqEELQNKSQQLR-AWEAEKYNEIRTQEQNI 573
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEakKKAEEAKKA-----DEAKKKAEEAKkAEEAKKKAEEAKKADEA 1475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 574 QHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALERAiDEKFSALEEKEKELRQLRLAVR-- 651
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA-EEAKKADEAKKAEEKKKADELKka 1554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 652 ERDHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQTslhdRNKEV 731
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL----KKAEE 1630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 732 EDLSATLLCKLGPGQSEIAEELCQRLQ----RKERMLQDLLSDRNK-QVLEHEMEIQGLLQSVSTREQESQAAAEKLVQA 806
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEenkiKAAEEAKKAEEDKKKaEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
730
....*....|...
gi 2056392194 807 LMERNSELQALRQ 819
Cdd:PTZ00121 1711 EAEEKKKAEELKK 1723
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
302-602 |
3.80e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 302 TEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEPTSM------EVQPMTEELLK-QQKLNSHETTITQQSV- 373
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSElkeleaRIEELEEDLHKlEEALNDLEARLSHSRIp 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 374 -SDSHLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEgqnDTMAKLR 452
Cdd:TIGR02169 795 eIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE---ELEEELE 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 453 EmlHQSQLGQLHSSegtspaqqqvaLLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQK---EA 529
Cdd:TIGR02169 872 E--LEAALRDLESR-----------LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELseiED 938
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2056392194 530 SWKHNQELRKA---LQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDK 602
Cdd:TIGR02169 939 PKGEDEEIPEEelsLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
147-716 |
3.90e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.71 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 147 KHLNDLKKENFSLKLRIYFLEERMQQK---YEASREDIYKRNIELKVEVESLKRELQD-----KKQHLDKTWADVENLNS 218
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQENrkiIEAQRKAIQELQFENEKVSLKLEEEIQEnkdliKENNATRHLCNLLKETC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 219 QNEAELRRQFEERQQETEHVYELLENKIqllqeESRLAKNEAARMAAlveaeKECNLELSEKLKgvtknwEDVPGDQVKP 298
Cdd:pfam05483 165 ARSAEKTKKYEYEREETRQVYMDLNNNI-----EKMILAFEELRVQA-----ENARLEMHFKLK------EDHEKIQHLE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 299 DQYTEALAQRDKRIEELNQSLAAQERLVEQLS---REKQQLLHLLEEPTSMEVQPMTEELLKQQKLNshettitqqsvsd 375
Cdd:pfam05483 229 EEYKKEINDKEKQVSLLLIQITEKENKMKDLTfllEESRDKANQLEEKTKLQDENLKELIEKKDHLT------------- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 376 SHLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQdgtiqnLKETLKSRERETeelyQVIEGQNDTMAKLREML 455
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQ------MEELNKAKAAHS----FVVTEFEATTCSLEELL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 456 HQSQlGQLHSSEGtspaQQQVALLDLQSalfcSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWK--- 532
Cdd:pfam05483 366 RTEQ-QRLEKNED----QLKIITMELQK----KSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEElkg 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 533 HNQELRKALQQLQEELQNKSQQLRA------WEAEKYNEIRTQEQNIQHLNHSL-SHKEQLLQEFRELLQyrDNSDKTLE 605
Cdd:pfam05483 437 KEQELIFLLQAREKEIHDLEIQLTAiktseeHYLKEVEDLKTELEKEKLKNIELtAHCDKLLLENKELTQ--EASDMTLE 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 606 anemlLEKLRQRIHDKAVALERAIdEKFSALEEKEKELRQLRLAVRER-DHDLERLRDVLSSNEATMQSMESLLRAKGLE 684
Cdd:pfam05483 515 -----LKKHQEDIINCKKQEERML-KQIENLEEKEMNLRDELESVREEfIQKGDEVKCKLDKSEENARSIEYEVLKKEKQ 588
|
570 580 590
....*....|....*....|....*....|..
gi 2056392194 685 VEQLSTTCQNLQWLKEEMETKFSRWQKEQESI 716
Cdd:pfam05483 589 MKILENKCNNLKKQIENKNKNIEELHQENKAL 620
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
187-399 |
4.07e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 187 ELKVEVESLKRELQDKKQHLDKTWADVENLNSQneaelRRQFEERQQETEHVYELLENKIQLLQEESRLAKNEAARMAAL 266
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQ-----LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 267 VEAEKEcnlELSEKLKGVTKNWE----------DVPGDQVKPDQYTEALAQ-RDKRIEELNQSLAAQERLVEQLSREKQQ 335
Cdd:COG4942 99 LEAQKE---ELAELLRALYRLGRqpplalllspEDFLDAVRRLQYLKYLAPaRREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2056392194 336 LLHLLEEPTSMEVQPMTEELLKQQKLNSHETTITQQSVSdshLAELQEKIQQTEATNKILQEKL 399
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAE---LAELQQEAEELEALIARLEAEA 236
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
394-831 |
4.25e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 394 ILQEKLNEMSYEL-KCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREmlhqsqlgqlhssegtspA 472
Cdd:COG4717 46 MLLERLEKEADELfKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEE------------------L 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 473 QQQVALLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKS 552
Cdd:COG4717 108 EAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 553 QQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEK 632
Cdd:COG4717 188 LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 633 FSALEEKEKELRQLRLAVRErdHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLqWLKEEMETKFSRWQKE 712
Cdd:COG4717 268 LLSLILTIAGVLFLVLGLLA--LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAL-GLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 713 QESIIQQLQTSLHDRNKEV-----EDLSATLLCKLGPGQSEIAEELCQRLQRKERmLQDLLSDRNKQVLEHEMEIQGLLQ 787
Cdd:COG4717 345 RIEELQELLREAEELEEELqleelEQEIAALLAEAGVEDEEELRAALEQAEEYQE-LKEELEELEEQLEELLGELEELLE 423
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2056392194 788 SVStrEQESQAAAEKLVQALMERNSELQALRQYLGGRDSLMSQA 831
Cdd:COG4717 424 ALD--EEELEEELEELEEELEELEEELEELREELAELEAELEQL 465
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
374-562 |
4.42e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 374 SDSHLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAK-LR 452
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 453 EMLHQ----SQLGQLHSSEGTSPAQQQVALLDLQSALfcSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKE 528
Cdd:COG3883 94 ALYRSggsvSYLDVLLGSESFSDFLDRLSALSKIADA--DADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190
....*....|....*....|....*....|....
gi 2056392194 529 ASWKHNQELRKALQQLQEELQNKSQQLRAWEAEK 562
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
360-830 |
4.48e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 360 KLNSHETTITQqsvSDSHLAELQEKIQQTEATNKILQEKLNEmsYELKcaQESSQKQDGTIQNLKETLKSRERETEELYQ 439
Cdd:PRK02224 207 RLNGLESELAE---LDEEIERYEEQREQARETRDEADEVLEE--HEER--REELETLEAEIEDLRETIAETEREREELAE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 440 VIEGQNDTMAKLREMLHqsqlGQLHSSEGTSPAQQqvALLDLQSALfcsQLEIQKLQRVVRQKERQLADAKQCVQFVEAA 519
Cdd:PRK02224 280 EVRDLRERLEELEEERD----DLLAEAGLDDADAE--AVEARREEL---EDRDEELRDRLEECRVAAQAHNEEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 520 AHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAE------KYNEIRTQEQNIQHLNHSL-SHKEQLLQEFRE 592
Cdd:PRK02224 351 ADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEieelreRFGDAPVDLGNAEDFLEELrEERDELREREAE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 593 LLQYRDNSDKTLEANEMLLEKLR-----QRIHDKAVAleRAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDV---- 663
Cdd:PRK02224 431 LEATLRTARERVEEAEALLEAGKcpecgQPVEGSPHV--ETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLveae 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 664 --LSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQK---EQESIIQQLQTSLHDRNKEVEDLSATL 738
Cdd:PRK02224 509 drIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREaaaEAEEEAEEAREEVAELNSKLAELKERI 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 739 --LCKLGPGQSEIAE--ELCQRLQRKERMLQDL-------LSDRNKQVLEHEMEIQGllqsvsTREQESQAAAEKLVQAL 807
Cdd:PRK02224 589 esLERIRTLLAAIADaeDEIERLREKREALAELnderrerLAEKRERKRELEAEFDE------ARIEEAREDKERAEEYL 662
|
490 500
....*....|....*....|...
gi 2056392194 808 MERNSELQALRQylgGRDSLMSQ 830
Cdd:PRK02224 663 EQVEEKLDELRE---ERDDLQAE 682
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
195-696 |
4.59e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 195 LKRELQDKKQHLDKTWADVENLNSQNEAELRRQFEERQQETEHVYELLENKIQLLQEESRLAKNEAARMAALVEAEKECN 274
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 275 L-ELSEKLKGVTKNWEDVpgdqvkPDQYtEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEPTSMEVQPMTE 353
Cdd:COG4717 127 LlPLYQELEALEAELAEL------PERL-EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 354 ELLKQQKLnshettitqqsvsdshLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKET----LKS 429
Cdd:COG4717 200 ELEELQQR----------------LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallaLLG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 430 RERETEELYQVIEGQNDTMAKLREMLHQSQLGQLHSS-EGTSPAQQQVALLDLQSALFCSQLEIQKLQRVVrQKERQLAD 508
Cdd:COG4717 264 LGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLgKEAEELQALPALEELEEEELEELLAALGLPPDL-SPEELLEL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 509 AKQCVQFVEAAAHESEQQKEASWKHNQELRKALqqLQEELQNKSQQLRAWeAEKYNEIRTQEQNIQHLNHSLshkEQLLQ 588
Cdd:COG4717 343 LDRIEELQELLREAEELEEELQLEELEQEIAAL--LAEAGVEDEEELRAA-LEQAEEYQELKEELEELEEQL---EELLG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 589 EFRELLQYRDnsdktleanemlLEKLRQRIHDKAVALErAIDEKFSALEEKEKELRQlRLAVRERDHDLERLRDVLSSNE 668
Cdd:COG4717 417 ELEELLEALD------------EEELEEELEELEEELE-ELEEELEELREELAELEA-ELEQLEEDGELAELLQELEELK 482
|
490 500
....*....|....*....|....*...
gi 2056392194 669 ATMQSMESLLRAKGLEVEQLSTTCQNLQ 696
Cdd:COG4717 483 AELRELAEEWAALKLALELLEEAREEYR 510
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
583-837 |
5.76e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 583 KEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIhdkaVALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRD 662
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRI----AALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 663 VLSSNEATMQSMESLLRAK-GLEVEQLSTTCQNLQWLKEemetkFSRWQKEQESIIQQLQTSLHDRNKEVEDLSATLlck 741
Cdd:COG4942 105 ELAELLRALYRLGRQPPLAlLLSPEDFLDAVRRLQYLKY-----LAPARREQAEELRADLAELAALRAELEAERAEL--- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 742 lgpgqseiaEELCQRLQRKERMLQDLLSDRNKqvlehemeiqgLLQSVSTREQESQAAAEKLVQALMERNSELQALRQYL 821
Cdd:COG4942 177 ---------EALLAELEEERAALEALKAERQK-----------LLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
250
....*....|....*.
gi 2056392194 822 GGRDSLMSQAPISNQQ 837
Cdd:COG4942 237 AAAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
427-928 |
5.93e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 427 LKSRERETEELYQVIEGQND-----TMAKLREMLHQS---QLGQLHSSEGTSPAQQQVALLDLQSALFCSQLEIQKLQRV 498
Cdd:COG4717 14 FRDRTIEFSPGLNVIYGPNEagkstLLAFIRAMLLERlekEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 499 VRQKERQLADAKQCVQFVEAAAHESEQQKEAswKHNQELRKALQQLQEELQNKSQQLRAWEaEKYNEIRTQEQNIQHLNH 578
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKL--LQLLPLYQELEALEAELAELPERLEELE-ERLEELRELEEELEELEA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 579 SLSHKEQLLQEfrellQYRDNSDKTLEANEMLLEKLrQRIHDKAVALERAIDEKFSALEEKEKELRQLRlAVRERDHDLE 658
Cdd:COG4717 171 ELAELQEELEE-----LLEQLSLATEEELQDLAEEL-EELQQRLAELEEELEEAQEELEELEEELEQLE-NELEAAALEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 659 RLRDVLSSNEATmqSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQTSLHDRNKEvEDLSATL 738
Cdd:COG4717 244 RLKEARLLLLIA--AALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAL-EELEEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 739 LCKL-------GPGQSEIAEELCQRLQRKERMLQDLLSDRNK-QVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMER 810
Cdd:COG4717 321 LEELlaalglpPDLSPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQEL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 811 NSELQALRQYLGgrdslmSQAPISNQQAEVTPTGRLGKQTDQGSMQIPSRDDSTS--LTAKEDVSIPRSTLGDLDTVAGL 888
Cdd:COG4717 401 KEELEELEEQLE------ELLGELEELLEALDEEELEEELEELEEELEELEEELEelREELAELEAELEQLEEDGELAEL 474
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2056392194 889 EKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQ 928
Cdd:COG4717 475 LQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
166-439 |
6.72e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 166 LEERMQQKYEA--SREDIYKRNIELKVEVESLKRELQDKKQHLD-------------------KTWADVENLNSQNEAEL 224
Cdd:COG3096 363 LEEQEEVVEEAaeQLAEAEARLEAAEEEVDSLKSQLADYQQALDvqqtraiqyqqavqalekaRALCGLPDLTPENAEDY 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 225 RRQFEERQQETEHvyellenkiQLLQEESRLAKNEAARmaalveAEKECNLELSEKLKG--VTKNWEDVPGDQVKPDQYT 302
Cdd:COG3096 443 LAAFRAKEQQATE---------EVLELEQKLSVADAAR------RQFEKAYELVCKIAGevERSQAWQTARELLRRYRSQ 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 303 EALAQRDKRIE----ELNQSLAAQERLVEQLSREKQQLLHLLEEPTSMEVQPMTEELLKQQKLNSHETTITQQSVSDSHL 378
Cdd:COG3096 508 QALAQRLQQLRaqlaELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQL 587
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2056392194 379 AELQEKIQQTEATNKI---LQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQ 439
Cdd:COG3096 588 EQLRARIKELAARAPAwlaAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAA 651
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
888-1106 |
8.27e-04 |
|
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: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 888 LEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAADMESLTRNIQIKEDLIKDLQMQLVdpEDIPAMERL 967
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE--ELEEELAEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 968 TQEVLLLREKVASVESQGQEISgNRRQQLLLMLEGLVDERSRLNEALQAERQLYSSLVkfhahpessERDRTLQVELEGA 1047
Cdd:COG1196 329 EEELEELEEELEELEEELEEAE-EELEEAEAELAEAEEALLEAEAELAEAEEELEELA---------EELLEALRAAAEL 398
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392194 1048 QVLRSRLEEVLGRSLERLNRLETLAAIGGAAAGDDTEDTSTEFTDSIEEEAAHHSHQQL 1106
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
532-815 |
1.12e-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: 43.04 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 532 KHNQELRKALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQ---------------------HLNHSLSHKEQLLQEF 590
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKaleyyqlkekleleeeyllylDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 591 RELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEAT 670
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 671 MQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQTSLHD----RNKEVEDLSATLLCKLGPGQ 746
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLeserLSSAAKLKEEELELKSEEEK 405
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392194 747 SEiaeelcQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMERNSELQ 815
Cdd:pfam02463 406 EA------QLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELK 468
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
302-664 |
1.17e-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: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 302 TEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLlhlleeptsmevqpmTEELLKQQKLNSHETTITQQSVSDSHLAEL 381
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDAL---------------QERREALQRLAEYSWDEIDVASAEREIAEL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 382 QEKIQQTEATNKILQEkLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREMLHQSQLG 461
Cdd:COG4913 674 EAELERLDASSDDLAA-LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 462 QLHSSEGTSPAQQQVAlLDLQSalfcsqlEIQKLQRVVRQKERQLADAKQcvQFVEAAAHESeQQKEASWKHNQELRKAL 541
Cdd:COG4913 753 ERFAAALGDAVERELR-ENLEE-------RIDALRARLNRAEEELERAMR--AFNREWPAET-ADLDADLESLPEYLALL 821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 542 QQLQEE------------LQNKSQQLRAWEAEK-YNEIRTQEQNIQHLNHSLSHkeqllqefrelLQYRDNSDKTLEANE 608
Cdd:COG4913 822 DRLEEDglpeyeerfkelLNENSIEFVADLLSKlRRAIREIKERIDPLNDSLKR-----------IPFGPGRYLRLEARP 890
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2056392194 609 MLLE---KLRQRIHDkavALERAIDEKFSALEEKEKELRQL--RLAVRERDHDLERLRDVL 664
Cdd:COG4913 891 RPDPevrEFRQELRA---VTSGASLFDEELSEARFAALKRLieRLRSEEEESDRRWRARVL 948
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
495-714 |
1.41e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.81 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 495 LQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRaweaEKYNEIRTQEQNIQ 574
Cdd:pfam05557 11 LSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALR----EQAELNRLKKKYLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 575 HLNHSLSHKEQLL-----------QEFRELLQYRDNSDKTLEANEMLLEKLRQRiHDKAVALERAIDEKFSALEEKEKEL 643
Cdd:pfam05557 87 ALNKKLNEKESQLadarevisclkNELSELRRQIQRAELELQSTNSELEELQER-LDLLKAKASEAEQLRQNLEKQQSSL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 644 RQLRLAVRERDHDLERLRD------VLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEE---METKFSRWQKEQE 714
Cdd:pfam05557 166 AEAEQRIKELEFEIQSQEQdseivkNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEvedLKRKLEREEKYRE 245
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
172-835 |
1.53e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 172 QKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTWADVENLNSQNEAELRRQFEE---RQQETEHVYELLENKIQL 248
Cdd:PTZ00121 1176 KKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEakkDAEEAKKAEEERNNEEIR 1255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 249 LQEESRLAknEAARMAALVEAEKECNLELSEKLKGVTKNWEDVPGDQVKPDQYTEALAQRDKRIEELNQSLAAQERLVEQ 328
Cdd:PTZ00121 1256 KFEEARMA--HFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA 1333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 329 LSREKQQLLHLLEEPTSMEVQPMTEELLKQQKLNSHETTITQQSVSDSHLAELQEKIQQTEATNKILQEKlNEMSYELKC 408
Cdd:PTZ00121 1334 AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED-KKKADELKK 1412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 409 AQESSQKQDGTIQNLKETLKSRE---------------------RETEELYQVIE---------GQNDTMAKLREMLHQS 458
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKADEakkkaeeakkadeakkkaeeaKKAEEAKKKAEeakkadeakKKAEEAKKADEAKKKA 1492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 459 QLGQLHSSEGTSPAQQQVALLDLQSALfcsqlEIQKLQRVVRQKERQLADAKQCVQFVEAAaheSEQQKEASWKHNQELR 538
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAE-----EAKKADEAKKAEEAKKADEAKKAEEKKKA---DELKKAEELKKAEEKK 1564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 539 KALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQL---------LQEFRELLQYRDNSDKTLEANEM 609
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkaeeakikAEELKKAEEEKKKVEQLKKKEAE 1644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 610 LLEKLRQRIHDKAVALERAIDEKFSALEEKEK--ELRQLRLAVRERDHDLER-LRDVLSSNEATMQSMESLLRAKGLEVE 686
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKaeEAKKAEEDEKKAAEALKKeAEEAKKAEELKKKEAEEKKKAEELKKA 1724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 687 QLSTTCQNLQWLKEEMETKF----SRWQKEQESIIQQLQTSLHDRNKEVEDLSATLLcklgpgQSEIAEELCQRLQRKER 762
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKkaeeAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI------EEELDEEDEKRRMEVDK 1798
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2056392194 763 MLQDLLSdrNKQVLEhEMEIQGLLQSVSTREQESQAAAEKLVQALMERNsELQALRQYLGGRDSLMSQAPISN 835
Cdd:PTZ00121 1799 KIKDIFD--NFANII-EGGKEGNLVINDSKEMEDSAIKEVADSKNMQLE-EADAFEKHKFNKNNENGEDGNKE 1867
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
171-819 |
1.78e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 171 QQKYEASREDIYKRNIELKvEVESLKRELQDKKQHLDKTWADV-----ENLNS--QNEAELRRQFEERQQETEHVYELLE 243
Cdd:TIGR00606 254 LKEIEHNLSKIMKLDNEIK-ALKSRKKQMEKDNSELELKMEKVfqgtdEQLNDlyHNHQRTVREKERELVDCQRELEKLN 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 244 NKIQLLQEESRLAKNEAARMAALVEAEKECNLE-----LSEKLKGVTKNWEDVPGDQVKPDQYTEALAQRDKRIEELNQS 318
Cdd:TIGR00606 333 KERRLLNQEKTELLVEQGRLQLQADRHQEHIRArdsliQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 319 LAAQERLVEQLSREKQQLLHLLEEPTSMEVQPMTEELLKQQKLNSHETTITQQSVSDS-HLAELQEKIQQTEATNKILQE 397
Cdd:TIGR00606 413 LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSdRILELDQELRKAERELSKAEK 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 398 KLNE--MSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREMlhqSQLGQLHSSEGTSPAQQQ 475
Cdd:TIGR00606 493 NSLTetLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQI---RKIKSRHSDELTSLLGYF 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 476 VALLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQkEASWKHN-------QELRKALQQLQEEL 548
Cdd:TIGR00606 570 PNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQ-LSSYEDKlfdvcgsQDEESDLERLKEEI 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 549 QNKSQQLRAWEAEK------YNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKT-LEANEMLLEKLRQRIHDK 621
Cdd:TIGR00606 649 EKSSKQRAMLAGATavysqfITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDkLKSTESELKKKEKRRDEM 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 622 AVALERaideKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQS-MESLLRAKGLEVEqlSTTCQNLQWLKE 700
Cdd:TIGR00606 729 LGLAPG----RQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTiMPEEESAKVCLTD--VTIMERFQMELK 802
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 701 EMETKFSRWQKEQESIiqQLQTSLHDRNKEVEDlsatllcklgpgqseiAEELCQRLQRKERMLQDLLSDRNKQVLEHEM 780
Cdd:TIGR00606 803 DVERKIAQQAAKLQGS--DLDRTVQQVNQEKQE----------------KQHELDTVVSKIELNRKLIQDQQEQIQHLKS 864
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 2056392194 781 EIQGLLQ---SVSTREQESQAAAEKLVQALMERNSELQALRQ 819
Cdd:TIGR00606 865 KTNELKSeklQIGTNLQRRQQFEEQLVELSTEVQSLIREIKD 906
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
299-567 |
2.17e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 299 DQYTEALAQRDKRIEELNQSLAAQERLVEQLsREKQQLLHLleeptSMEVQPMTEELlkqqklnsheTTITQQsvsdshL 378
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALEEF-RQKNGLVDL-----SEEAKLLLQQL----------SELESQ------L 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 379 AELQEKIQQTEATNKILQEKLNEMSYELkcaqeSSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREmlhqs 458
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDAL-----PELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRA----- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 459 qlgQLHSSEGTSPAQQQVALLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQcvQFVEAAAHESEQQkeaswkhnqelr 538
Cdd:COG3206 299 ---QIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPE--LEAELRRLEREVE------------ 361
|
250 260
....*....|....*....|....*....
gi 2056392194 539 kALQQLQEELQNKSQQLRAWEAEKYNEIR 567
Cdd:COG3206 362 -VARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
146-631 |
3.29e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 146 EKHLNDLKKENFSLKLRIYFLEERMQQKYEASR--EDIYKRNIELK------VEVESLKRELQDKKQHLDKTWADVENLN 217
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEelEEKVKELKELKekaeeyIKLSEFYEEYLDELREIEKRLSRLEEEI 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 218 SQNEAELR---------RQFEERQQETEHVYELLENKIQLLQEESRLAKNEAARMAALVEAEKEcnlELSEKLKGVTKNW 288
Cdd:PRK03918 324 NGIEERIKeleekeerlEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPE---KLEKELEELEKAK 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 289 EDVpgdQVKPDQYTEALAQRDKRIEELNQSLAA-------------------QERLVEQLSREKQQLLHLLEEPTSMEVQ 349
Cdd:PRK03918 401 EEI---EEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERK 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 350 PMTEELLKQQKLNSHETTITQQSVSDsHLAELQEKiqqteaTNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKS 429
Cdd:PRK03918 478 LRKELRELEKVLKKESELIKLKELAE-QLKELEEK------LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 430 RERETEELYQVIEGQNDTMAKLREMLHQ-SQLG-------QLHSSEGTSPAQQQVALLDLQSALFCSQLEIQKLQRVVRQ 501
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEELAELLKElEELGfesveelEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDK 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 502 KERQLADAKQCVQfvEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEaekyNEIRTQEQNIQHLNHSLS 581
Cdd:PRK03918 631 AFEELAETEKRLE--ELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELE----KRREEIKKTLEKLKEELE 704
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2056392194 582 HKEQLLQEFRELlqyrdnsDKTLEANEMLLEKLRQRihdKAVALERAIDE 631
Cdd:PRK03918 705 EREKAKKELEKL-------EKALERVEELREKVKKY---KALLKERALSK 744
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
514-797 |
3.47e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 514 QFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNksqqlraweAEK----YNEIRTQEqnIQHLNHSLSHKEQLLQE 589
Cdd:PLN02939 103 QRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQN---------AEKnillLNQARLQA--LEDLEKILTEKEALQGK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 590 FREL---LQYRDNSDKT-------LEANEMLLEKLRQRIHDKAV---ALERAIDEKFSALEEKEKELRQLRLAVR----- 651
Cdd:PLN02939 172 INILemrLSETDARIKLaaqekihVEILEEQLEKLRNELLIRGAtegLCVHSLSKELDVLKEENMLLKDDIQFLKaelie 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 652 -----ERDHDLERLRDVLssnEATMQSMESLLRAKGLEVEQLSTTCQNLQWLK-EEMETKFSRWQKEQESIIQQLQTSlH 725
Cdd:PLN02939 252 vaeteERVFKLEKERSLL---DASLRELESKFIVAQEDVSKLSPLQYDCWWEKvENLQDLLDRATNQVEKAALVLDQN-Q 327
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2056392194 726 DRNKEVEDLSATLL-CKLGPGQSEIAEELCQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVSTREQESQ 797
Cdd:PLN02939 328 DLRDKVDKLEASLKeANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEESK 400
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
168-819 |
3.86e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 168 ERMQQKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTWADVENLNSQNEAELRRQFEERQQETEHVYELLENKIQ 247
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAE 1191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 248 LLQEESRLAKNEAARMAALVEAEKECNLELSEKLKGVTKNWEDVPGDQVKPDQYTEALAQRDKRIEELNQSLAAQERLVE 327
Cdd:PTZ00121 1192 ELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAA 1271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 328 QLSREKQQllhlLEEPTSMEVQPMTEELLKQQKLNSHEtTITQQSVSDSHLAELQEKIQQTEATNKILQEKLNEMSYELK 407
Cdd:PTZ00121 1272 IKAEEARK----ADELKKAEEKKKADEAKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE 1346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 408 CAQESSQKQDGTIQNLKETLKSRERETEELYQviegQNDTMAKLREMLHQSQLGQLHSSEGTSPAQQqvalLDLQSALFC 487
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK----KADAAKKKAEEKKKADEAKKKAEEDKKKADE----LKKAAAAKK 1418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 488 SQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQK-EASWKHNQELRKAlqqlqEELQNKSQqlrawEAEKYNEI 566
Cdd:PTZ00121 1419 KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKaEEAKKKAEEAKKA-----DEAKKKAE-----EAKKADEA 1488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 567 RTQEQNIQHLNHSLSHKEQLLQEFRELLQYRD--NSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKeLR 644
Cdd:PTZ00121 1489 KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEakKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK-AE 1567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 645 QLRLAVRERDHDLERLRDVLSSNEATMQS-MESLLRAKGLEVEQLSTtcqnlqwlKEEMETKFSRWQKEQE--SIIQQLQ 721
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEvMKLYEEEKKMKAEEAKK--------AEEAKIKAEELKKAEEekKKVEQLK 1639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 722 TSLHDRNKEVEDLSatllcKLGPGQSEIAEELCQRLQRKERMLQDLLSD-----RNKQVLEHEMEIQGLLQSVSTREQES 796
Cdd:PTZ00121 1640 KKEAEEKKKAEELK-----KAEEENKIKAAEEAKKAEEDKKKAEEAKKAeedekKAAEALKKEAEEAKKAEELKKKEAEE 1714
|
650 660
....*....|....*....|...
gi 2056392194 797 QAAAEKLVQALMERNSELQALRQ 819
Cdd:PTZ00121 1715 KKKAEELKKAEEENKIKAEEAKK 1737
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
170-422 |
4.58e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 40.99 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 170 MQQKYEASREDIYKRNIE-------LKVEVESLKRE-------------LQDKKQHLDKTWADVENLNSQNEAE-LRRQF 228
Cdd:PLN03229 484 LQERLENLREEFSKANSQdqlmhpvLMEKIEKLKDEfnkrlsrapnylsLKYKLDMLNEFSRAKALSEKKSKAEkLKAEI 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 229 EERQQETEHVYELLEnKIQLLQEEsrLAKNEAARMAAL--------VEAEKECNLELSEKLKGVTKNWEDVPGDQVKPDQ 300
Cdd:PLN03229 564 NKKFKEVMDRPEIKE-KMEALKAE--VASSGASSGDELdddlkekvEKMKKEIELELAGVLKSMGLEVIGVTKKNKDTAE 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 301 YTEALAQRDKrIEELNqslaaqerlvEQLSREKQQLLHlleeptSMEVQPMTEELlkqqKLNSHETTITQQSVSDSHLAE 380
Cdd:PLN03229 641 QTPPPNLQEK-IESLN----------EEINKKIERVIR------SSDLKSKIELL----KLEVAKASKTPDVTEKEKIEA 699
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2056392194 381 LQEKIQQ--TEATNKI-LQEKLNEMSYELKCAQESSQKQDGTIQN 422
Cdd:PLN03229 700 LEQQIKQkiAEALNSSeLKEKFEELEAELAAARETAAESNGSLKN 744
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
505-821 |
6.25e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 505 QLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQlraweaekyneIRTQEQNIQHLNHSLSHKE 584
Cdd:PRK11281 25 AFARAASNGDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDK-----------IDRQKEETEQLKQQLAQAP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 585 QLLQEF-RELLQYRDNSDKTLEANemlLEKLRQRihdkavALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDV 663
Cdd:PRK11281 94 AKLRQAqAELEALKDDNDEETRET---LSTLSLR------QLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 664 LSSNEATMQSMESLLRAKGLEVEQLSTTCQNLqwlkeemetkfsrWQKEQESIiqQLQTSLhdRNKEVEdlSATLLCKLG 743
Cdd:PRK11281 165 LYANSQRLQQIRNLLKGGKVGGKALRPSQRVL-------------LQAEQALL--NAQNDL--QRKSLE--GNTQLQDLL 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392194 744 PGQSEIAEELCQRLQRKERMLQDLLSDRNKQVLEHEMeiqgllQSVSTREQESQAAAEKLVQALMERNSELQalrQYL 821
Cdd:PRK11281 226 QKQRDYLTARIQRLEHQLQLLQEAINSKRLTLSEKTV------QEAQSQDEAARIQANPLVAQELEINLQLS---QRL 294
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
602-1056 |
6.40e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 602 KTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAK 681
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 682 GLEVEqlsttcqnLQWLKEEMETKFSRWQKEQESI--IQQLQTSLHDRNKEVEDLSATLLCKLGPGQSEIAEELcQRLQR 759
Cdd:COG4717 129 PLYQE--------LEALEAELAELPERLEELEERLeeLRELEEELEELEAELAELQEELEELLEQLSLATEEEL-QDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 760 KERMLQDLLSDRNKQVLEHEMEIQGLlqsvstREQESQAAAEKLVQALMERNSELQALRQYLGGRDSLMSQAPISNQQAE 839
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEEL------EEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 840 VTPTGRLGKQTDQGSMQIPSRDDSTSLTAKEDVSIPRSTLGDLDtvaglEKELSNAKEELELMAKKERESQMELSAlqsm 919
Cdd:COG4717 274 TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELE-----EEELEELLAALGLPPDLSPEELLELLD---- 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 920 mavQEEELQVQAADMESLTRNIQIK--EDLIKDL--QMQLVDPEDIPAMERLTQEVLLLREKVASVESQGQEISGNRRQQ 995
Cdd:COG4717 345 ---RIEELQELLREAEELEEELQLEelEQEIAALlaEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEL 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2056392194 996 L-LLMLEGLVDERSRLNEALQAER----QLYSSLVKFHAHPESSERDRTLQVELEGAQVLRSRLEE 1056
Cdd:COG4717 422 LeALDEEELEEELEELEEELEELEeeleELREELAELEAELEQLEEDGELAELLQELEELKAELRE 487
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
493-714 |
6.50e-03 |
|
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: 40.13 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 493 QKLQRVVRQKERQLADAKqcvqfvEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAEkyneirTQEQN 572
Cdd:pfam09787 14 QKAARILQSKEKLIASLK------EGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTE------LQELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 573 IQHLNHSLSHKEQLlQEFRELLQYRDNSDKTLEANemlLEKLRQRIHdkavaleraidekfSALEEKEKELRQLRLAVRE 652
Cdd:pfam09787 82 AQQQEEAESSREQL-QELEEQLATERSARREAEAE---LERLQEELR--------------YLEEELRRSKATLQSRIKD 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2056392194 653 RDHDLERLRDVL---SSNEATMQSMESLLR-------AKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQE 714
Cdd:pfam09787 144 REAEIEKLRNQLtskSQSSSSQSELENRLHqltetliQKQTMLEALSTEKNSLVLQLERMEQQIKELQGEGS 215
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
142-437 |
7.79e-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: 40.44 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 142 LRDFEKHLNDLKKENFSLKLRIYFLEERMQQKyEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTWADVENLNSQNE 221
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSDA-SRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 222 ------AELRRQFEERQQETEHVY-ELLENKIQLLQEESRLAKNEAARM-AALVEAEKECNLELSEKlkgvTKNWEDVPG 293
Cdd:TIGR02169 762 eleariEELEEDLHKLEEALNDLEaRLSHSRIPEIQAELSKLEEEVSRIeARLREIEQKLNRLTLEK----EYLEKEIQE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 294 DQVKPDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEpTSMEVQPMTEELLK-QQKLNSHETTITQQs 372
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD-LKKERDELEAQLRElERKIEELEAQIEKK- 915
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2056392194 373 vsDSHLAELQEKIQQTEATNKILQEKLNEMSYELKCaqessqkqDGTIQNLKETLKSRERETEEL 437
Cdd:TIGR02169 916 --RKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE--------ELSLEDVQAELQRVEEEIRAL 970
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
626-998 |
9.39e-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: 40.05 E-value: 9.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 626 ERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDvlssneatmqSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETK 705
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRR----------EREKAERYQALLKEKREYEGYELLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 706 FSRWQKEQESI---IQQLQTSLHDRNKEVEDLSATLlcklgpgqSEIAEELcqrlqrkERMLQDLLSDRNKQVLEHEMEI 782
Cdd:TIGR02169 239 KEAIERQLASLeeeLEKLTEEISELEKRLEEIEQLL--------EELNKKI-------KDLGEEEQLRVKEKIGELEAEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 783 QGLLQSVSTREQESQAAAEKLVQALMERNSELQALRQylggrdslmSQAPISNQQAEVTPTGRLGKQTDQGSMQIPSR-- 860
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE---------LEREIEEERKRRDKLTEEYAELKEELEDLRAEle 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 861 -DDSTSLTAKEDVSIPRSTLGDL-DTVAGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAADMESLT 938
Cdd:TIGR02169 375 eVDKEFAETRDELKDYREKLEKLkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE 454
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2056392194 939 RNI-QIKEDLIKDLQMQLVDPEDIPAME-RLTQEVLLLREKVASVESQGQEISGNRRQQLLL 998
Cdd:TIGR02169 455 WKLeQLAADLSKYEQELYDLKEEYDRVEkELSKLQRELAEAEAQARASEERVRGGRAVEEVL 516
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
611-802 |
9.84e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 611 LEKLRQRIHDKAVALERAIDEKFSALEEKEKE------------LRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLL 678
Cdd:PRK02224 164 LEEYRERASDARLGVERVLSDQRGSLDQLKAQieekeekdlherLNGLESELAELDEEIERYEEQREQARETRDEADEVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392194 679 ---RAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEqesiIQQLQTSLHDRNKEVEDLSATllCKLGPGQSEIAEELCQ 755
Cdd:PRK02224 244 eehEERREELETLEAEIEDLRETIAETEREREELAEE----VRDLRERLEELEEERDDLLAE--AGLDDADAEAVEARRE 317
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2056392194 756 RLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEK 802
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREE 364
|
|
| |
