|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
446-729 |
4.00e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 76.63 E-value: 4.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 446 TRQNIAQ-REEISILGATLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQ 524
Cdd:TIGR02168 675 RRREIEElEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 525 DISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILK 604
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 605 SEESENRQIMEQLRKANEDAENwenkarqteaenntLKLELITAEAEGNRLKEKVDALNREVEQMENELDSARSEIELLR 684
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIES--------------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1039728160 685 SQMTNERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHL 729
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
335-681 |
9.63e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.48 E-value: 9.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 335 NEKAHLEQRIEELECTVHNLDDERMEQMANMTLMKETITTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDL 414
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 415 SDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGATLNDLAKEKECLQACLDKKSENIASLGESLAMK 494
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 495 EKTISGMKNIIAEMEQASRQSTEALIMCEQDISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKK 574
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 575 LNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQL-RKANEDAENWENKARQTEAENNTLKLELITAEAEGN 653
Cdd:TIGR02168 917 LEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALeNKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYE 996
|
330 340
....*....|....*....|....*...
gi 1039728160 654 RLKEKVDALNREVEqmenELDSARSEIE 681
Cdd:TIGR02168 997 ELKERYDFLTAQKE----DLTEAKETLE 1020
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
310-781 |
3.67e-12 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 70.53 E-value: 3.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 310 TDLRRMTTERDSL---RERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMANMTLMKETITTVEKEMKSLArka 386
Cdd:pfam15921 117 TKLQEMQMERDAMadiRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIL--- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 387 MDTESELGRQKAENNSLRLL-YENTEKDLSDTQRHLAKK---------KYELQL------TQEKIMCLDEKIDNFTRQNI 450
Cdd:pfam15921 194 VDFEEASGKKIYEHDSMSTMhFRSLGSAISKILRELDTEisylkgrifPVEDQLealkseSQNKIELLLQQHQDRIEQLI 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 451 AQRE-EISILGATLNDLAKEKECLQACLDKKSENIASLGeslAMKEKTISGMKNIIAEMEQASRqstEALIMCEQDISRM 529
Cdd:pfam15921 274 SEHEvEITGLTEKASSARSQANSIQSQLEIIQEQARNQN---SMYMRQLSDLESTVSQLRSELR---EAKRMYEDKIEEL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 530 RRQLDETNDELGQIARERDILAHENDNLQEQFAKV------KQENQALSKKLN------DTHNELS--DIKQKVQDTNLE 595
Cdd:pfam15921 348 EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLladlhkREKELSLEKEQNkrlwdrDTGNSITidHLRRELDDRNME 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 596 VNKLKNILKSEESENRQIMEQ----LRKANEDAENWENKARQTEAENNTLK--LELITAEAEGNRLKEK-VDALNREVEQ 668
Cdd:pfam15921 428 VQRLEALLKAMKSECQGQMERqmaaIQGKNESLEKVSSLTAQLESTKEMLRkvVEELTAKKMTLESSERtVSDLTASLQE 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 669 MENELDSARSEIELLRSQ----------MTNERISMQNL----EALLVANRDKEYQSQIALQEKESEIQLLKEH------ 728
Cdd:pfam15921 508 KERAIEATNAEITKLRSRvdlklqelqhLKNEGDHLRNVqtecEALKLQMAEKDKVIEILRQQIENMTQLVGQHgrtaga 587
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039728160 729 ----------------LCLAENKMAIQSRDvAQFRNVVTQLeADLDITKRQLGTERFERERAVQELRRQ 781
Cdd:pfam15921 588 mqvekaqlekeindrrLELQEFKILKDKKD-AKIRELEARV-SDLELEKVKLVNAGSERLRAVKDIKQE 654
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
274-602 |
8.30e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 8.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 274 EIARLRREMmksckspksTTAHAILRRVETERDVAFTDLRRMTTERDSLR---ERLKIAQETAFNEKAHLEQRIEELECT 350
Cdd:TIGR02168 678 EIEELEEKI---------EELEEKIAELEKALAELRKELEELEEELEQLRkelEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 351 VHNLDDERMEQMANMTLMKETITTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQL 430
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 431 TQEKIMCLDEKIDNFTRQNIAQREEISILGATLNDLAKEKECLQACLDKKSENIASLGESLAMKEKtisgmkniiaEMEQ 510
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS----------ELEE 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 511 ASRQSTEAlimcEQDISRMRRQLDETNDELGQIARERDILAHENDNLQEQFA-KVKQENQALSKKLNDTHNELSDIKQKV 589
Cdd:TIGR02168 899 LSEELREL----ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEEEARRRL 974
|
330
....*....|...
gi 1039728160 590 QDTNLEVNKLKNI 602
Cdd:TIGR02168 975 KRLENKIKELGPV 987
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
455-748 |
1.98e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 455 EISILGATLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQDISRMRRQLd 534
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 535 etndelgQIARERDilahenDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIM 614
Cdd:TIGR02168 305 -------QILRERL------ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 615 EQLRKANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQMENELDSArsEIELLRSQMTNERISM 694
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEEL 449
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1039728160 695 QNLEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRN 748
Cdd:TIGR02168 450 EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
525-779 |
1.98e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 525 DISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILK 604
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 605 SEESENRQIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQMENELDSARSEIELLR 684
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 685 SQMTNERISMQNLEAL---LVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRdVAQFRNVVTQLEAdLDITK 761
Cdd:TIGR02168 393 LQIASLNNEIERLEARlerLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEEL-QEELERLEEALEE-LREEL 470
|
250
....*....|....*...
gi 1039728160 762 RQLGTERFERERAVQELR 779
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQ 488
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
526-781 |
3.89e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 526 ISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNEL----SDIKQKVQDTNLEVNKLKN 601
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 602 I---LKSEESENRQIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQMENELDSARS 678
Cdd:COG1196 314 LeerLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 679 EIELLRSQMTNERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLD 758
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250 260
....*....|....*....|...
gi 1039728160 759 ITKRQLGTERFERERAVQELRRQ 781
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLL 496
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
455-727 |
4.24e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 4.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 455 EISILGATLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQAS-------RQSTEALIMCEQDIS 527
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELeeaqaeeYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 528 RMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDtnlEVNKLKNILKSEE 607
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE---AEAELAEAEEELE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 608 SENRQIMEQLRKANEDaenwENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQMENELDSARSEIELLRSQM 687
Cdd:COG1196 383 ELAEELLEALRAAAEL----AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1039728160 688 TNERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKE 727
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
49-782 |
1.07e-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: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 49 QLEQEVRTQDRFISTLKLQIEDLKQTNHDLEEYVRKLLDSKEAVSTQVDDLANHNEHLCKELIKLDQLAEKLQkeknfvv 128
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE------- 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 129 dtadKELEEAKIELICQQNNITVLEDTIQRLKSIILETEKAQntspsrldsfvktleadrdyykTEAQNLRKMMRNRSKS 208
Cdd:TIGR02168 323 ----AQLEELESKLDELAEELAELEEKLEELKEELESLEAEL----------------------EELEAELEELESRLEE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 209 PRRPSPTSRAAncdvelLKSTARDREELKCMLEKYERHLAEIQGNVKVLTSERdktfllyEQAQEEIARLRREmmkscks 288
Cdd:TIGR02168 377 LEEQLETLRSK------VAQLELQIASLNNEIERLEARLERLEDRRERLQQEI-------EELLKKLEEAELK------- 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 289 pkstTAHAILRRVETERDVAFTDLRRMTTERDSLRERLKIAQE---TAFNEKAHLEQRIEELECTVHNLDDERmEQMANM 365
Cdd:TIGR02168 437 ----ELQAELEELEEELEELQEELERLEEALEELREELEEAEQaldAAERELAQLQARLDSLERLQENLEGFS-EGVKAL 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 366 TLMKETITTVEKEMKSLARkaMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNF 445
Cdd:TIGR02168 512 LKNQSGLSGILGVLSELIS--VDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGN 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 446 TRQniaQREEISILGATLNDLAKEKECLQACLDKKSENIA---SLGESLAMKEKTISGMKNIIAEMEQASRQ-------- 514
Cdd:TIGR02168 590 DRE---ILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLvvdDLDNALELAKKLRPGYRIVTLDGDLVRPGgvitggsa 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 515 STEALIMC-EQDISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQ--- 590
Cdd:TIGR02168 667 KTNSSILErRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqle 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 591 ----DTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREV 666
Cdd:TIGR02168 747 eriaQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 667 EQMENELDSARSEIELLRSQMTNERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQF 746
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
730 740 750
....*....|....*....|....*....|....*.
gi 1039728160 747 RNVVTQLEADLDITKRQLGTERFERERAVQELRRQN 782
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
539-781 |
1.40e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 539 ELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLR 618
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 619 KANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQMENELDSARSEIELLRSQMTNERISMQNLE 698
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 699 ALLVANRDKEYQSQIALQEKESEIQLLKEHlcLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERAVQEL 778
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLER--LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
...
gi 1039728160 779 RRQ 781
Cdd:COG1196 464 LLA 466
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
523-781 |
3.79e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 523 EQDISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNI 602
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 603 LKSEESENRQIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQMENELDSARSEIEL 682
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 683 LRSQMTNERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKR 762
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
250
....*....|....*....
gi 1039728160 763 QLGTERfERERAVQELRRQ 781
Cdd:COG1196 485 ELAEAA-ARLLLLLEAEAD 502
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
418-741 |
2.30e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 418 QRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGATLNDLAKEKECLQACLDKKSENIASLGESLAMKEKT 497
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 498 ISGMKNIIAEMEQASRQSTEALIMCEQDISR-----MRRQLDETNDELGQI-ARERDILAHENDNLQEQfAKVKQENQAL 571
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDLEARLSHsripeIQAELSKLEEEVSRIeARLREIEQKLNRLTLEK-EYLEKEIQEL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 572 SKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAE 651
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 652 GNRLKEKVDALNREVEQMENELDSARSEIELLRSqmtnERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKE---- 727
Cdd:TIGR02169 919 LSELKAKLEALEEELSEIEDPKGEDEEIPEEELS----LEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDElkek 994
|
330
....*....|....
gi 1039728160 728 HLCLAENKMAIQSR 741
Cdd:TIGR02169 995 RAKLEEERKAILER 1008
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
111-772 |
4.36e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 111 IKLDQLaEKLQKEKNFVVDTADKELEEAKIELICQQNNITVLEDTIQRLKSIILETEKAQNTSPSRLDSFVKTLEADRDY 190
Cdd:TIGR02169 195 EKRQQL-ERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 191 YKTEAQNLRKMMRNRSKSPRRPsptsraancdvelLKSTARDREELKCMLEKYERHLAEIQGNVKVLTSERDKTFLLYEQ 270
Cdd:TIGR02169 274 LEELNKKIKDLGEEEQLRVKEK-------------IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 271 AQEEIA--RLRREMMKSCKSPKSTTAHAILRRVEtERDVAFTDLRRmttERDSLRERLkiaqETAFNEKAHLEQRIEELE 348
Cdd:TIGR02169 341 LEREIEeeRKRRDKLTEEYAELKEELEDLRAELE-EVDKEFAETRD---ELKDYREKL----EKLKREINELKRELDRLQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 349 CTVHNLDDERMEQMANMTLMKETITTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYEL 428
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 429 QLTQEKIMCLDEKIDNFTRQNIAQREEISILGATLNDLAKEKECLQACL------------------------------- 477
Cdd:TIGR02169 493 AEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIevaagnrlnnvvveddavakeaiellkrrka 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 478 ------------------------------------DKKSENIAS--LGESLAMKE------------------------ 495
Cdd:TIGR02169 573 gratflplnkmrderrdlsilsedgvigfavdlvefDPKYEPAFKyvFGDTLVVEDieaarrlmgkyrmvtlegelfeks 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 496 --------KTISGMKNIIAEMEQASRQSTE------ALIMCEQDISRMRRQLDETNDEL-------GQIARERDILAHEN 554
Cdd:TIGR02169 653 gamtggsrAPRGGILFSRSEPAELQRLRERleglkrELSSLQSELRRIENRLDELSQELsdasrkiGEIEKEIEQLEQEE 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 555 DNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEE-----SENRQIMEQLRKANEDAENWEN 629
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEarlshSRIPEIQAELSKLEEEVSRIEA 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 630 KARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQMENELDSARSEIELLRSQMTNERISMQNLEALL------VA 703
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLgdlkkeRD 892
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039728160 704 NRDKEY-QSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQL----EADLDITKRQLGTERFERE 772
Cdd:TIGR02169 893 ELEAQLrELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDeeipEEELSLEDVQAELQRVEEE 966
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
505-780 |
6.23e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 505 IAEMEQASRQSTEALIMCEQDISRMRRQLDETNDELGQIARERDiLAHENDNLQEQfaKVKQENQALSKKLNDTHNELSD 584
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERE-KAERYQALLKE--KREYEGYELLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 585 IKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAEnwenkaRQTEAENNTLKLELITAEAEGNRLKEKVDALNR 664
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIK------DLGEEEQLRVKEKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 665 EVEQMENELDSARSEIELLRSQMTnerismqnleallvaNRDKEYQSQIALQEK-ESEIQLLKEHLCLAENKMAIQSRDV 743
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIE---------------ELEREIEEERKRRDKlTEEYAELKEELEDLRAELEEVDKEF 380
|
250 260 270
....*....|....*....|....*....|....*..
gi 1039728160 744 AQFRNVVTQLEADLDITKRQLGTERFERERAVQELRR 780
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
524-773 |
6.80e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 524 QDISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNIL 603
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 604 KSEEsenRQIMEQLRKAnedaenwenkarQTEAENNTLKLeLITAE--AEGNRLKEKVDALNREVEQMENELDSARSEIE 681
Cdd:COG4942 100 EAQK---EELAELLRAL------------YRLGRQPPLAL-LLSPEdfLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 682 LLRSQMTNERismQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITK 761
Cdd:COG4942 164 ALRAELEAER---AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
250
....*....|..
gi 1039728160 762 RQLGTERFERER 773
Cdd:COG4942 241 ERTPAAGFAALK 252
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
73-720 |
8.12e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 56.28 E-value: 8.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 73 QTNHDLEEYVRKLLDSKEAVSTQVDDLANHNEHLCKELIKLDQLAEK-LQKEKNFVVDtadkeLEEAKIELICQQNNITV 151
Cdd:pfam15921 138 QSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGvLQEIRSILVD-----FEEASGKKIYEHDSMST 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 152 LEdtIQRLKSIILETEKAQNTSPSRLDSFVKTLEADRDYYKTEAQNLRKMMRNRSKS----------------PRRPSPT 215
Cdd:pfam15921 213 MH--FRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDrieqliseheveitglTEKASSA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 216 SRAANC---DVELLKSTARDREELkcmlekYERHLAEIQGNVKVLTSERDKTFLLYEQAQEEIARlrremmksckspKST 292
Cdd:pfam15921 291 RSQANSiqsQLEIIQEQARNQNSM------YMRQLSDLESTVSQLRSELREAKRMYEDKIEELEK------------QLV 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 293 TAHAILRRVETERDVAFTD-------LRRMTTERDSLRERLKIAQE--------------TAFNEKAHLEQR---IEELE 348
Cdd:pfam15921 353 LANSELTEARTERDQFSQEsgnlddqLQKLLADLHKREKELSLEKEqnkrlwdrdtgnsiTIDHLRRELDDRnmeVQRLE 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 349 CTVHNLDDERMEQMA-NMTLMKETITTVEKeMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYE 427
Cdd:pfam15921 433 ALLKAMKSECQGQMErQMAAIQGKNESLEK-VSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERA 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 428 LQLTQEKIMCLDEKIDnftrQNIAQREEISILGATLNDLAKEKECLQACLDKKS-------ENIASLGESLAMKEKTISG 500
Cdd:pfam15921 512 IEATNAEITKLRSRVD----LKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDkvieilrQQIENMTQLVGQHGRTAGA 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 501 MKNIIAEMEQA----SRQSTEALIMCEQDISRMRRQLDETND-----------------ELGQIARERDILAHENDNLQE 559
Cdd:pfam15921 588 MQVEKAQLEKEindrRLELQEFKILKDKKDAKIRELEARVSDlelekvklvnagserlrAVKDIKQERDQLLNEVKTSRN 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 560 QFAKVKQENQALSKKLNDTHNEL----SDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKARQTE 635
Cdd:pfam15921 668 ELNSLSEDYEVLKRNFRNKSEEMetttNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQ 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 636 AENNTLKLELITAEAEGNRLKEKVDALNREVEQMENELDSARSEIELLRSQMTNERISMQNLEALL--VANRDKEYQSQI 713
Cdd:pfam15921 748 SKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALdkASLQFAECQDII 827
|
....*..
gi 1039728160 714 ALQEKES 720
Cdd:pfam15921 828 QRQEQES 834
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
378-651 |
1.30e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 378 EMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEIS 457
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 458 ILGATLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQDISRMRRQLDETN 537
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 538 DELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKlkniLKSEESENRQIMEQL 617
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE----LEEEEEALLELLAEL 468
|
250 260 270
....*....|....*....|....*....|....
gi 1039728160 618 RKANEDAENWENKARQTEAENNTLKLELITAEAE 651
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
408-637 |
1.42e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 408 ENTEKDLSDTQRHLAKKKYELQLTQEKIMC-------LDEKIDNFTRQNIAQREEISILGATLNDLAKEKECLQACLDKK 480
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKAllkqlaaLERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 481 SENIASLgeslamkektisgmkniIAEMEQASRQSTEALIMCEQDISRMRRQLdetnDELGQIARERDILAHENDNLQEQ 560
Cdd:COG4942 103 KEELAEL-----------------LRALYRLGRQPPLALLLSPEDFLDAVRRL----QYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039728160 561 FAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKARQTEAE 637
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
342-755 |
1.64e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.03 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 342 QRIEELECTVHNLDDERMEQMANMTLMKETITTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHL 421
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 422 AKKKYELQLTQEKImcldEKIDNFTRQNIAQREEISILGATLNDLAKEKECLQACLDKKSENIASLGESlamKEKTISGM 501
Cdd:TIGR04523 197 LKLELLLSNLKKKI----QKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE---QNKIKKQL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 502 KNIIAEMEQASR---QSTEALIMCEQDISRMRRQ-----LDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSK 573
Cdd:TIGR04523 270 SEKQKELEQNNKkikELEKQLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 574 KLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAEGN 653
Cdd:TIGR04523 350 ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 654 RLKEKVDALNREVEQMENELDSARSEIELLRSQMTNERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAE 733
Cdd:TIGR04523 430 RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELE 509
|
410 420
....*....|....*....|..
gi 1039728160 734 NKMAIQSRDVAQFRNVVTQLEA 755
Cdd:TIGR04523 510 EKVKDLTKKISSLKEKIEKLES 531
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
269-619 |
4.08e-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: 53.92 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 269 EQAQEEIARLRREMmkSCKSPKSTTAHAILRRVETERDVAFTDLRRMTTERDSLRERLKIAQETAFN---EKAHLEQRIE 345
Cdd:TIGR02169 691 SSLQSELRRIENRL--DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvksELKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 346 ELECTVHNLddermeqmanmtlmketittvEKEMKSLarKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKK 425
Cdd:TIGR02169 769 ELEEDLHKL---------------------EEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 426 YELQLtqekimcLDEKIDNFTRQNIAQREEISILGATLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNII 505
Cdd:TIGR02169 826 LEKEY-------LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 506 AEMEQASRQSTEALIMCEQDISRMRRQLDETNDELGQIARE--RDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELS 583
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPkgEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAI 978
|
330 340 350
....*....|....*....|....*....|....*.
gi 1039728160 584 DIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRK 619
Cdd:TIGR02169 979 QEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
231-550 |
4.92e-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: 53.53 E-value: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 231 RDREELKCMLEKYERHLAEIQGNVKVLTSERDKTfLLYEQAQEEiarlRREMMKSCKSPKSTTAHAILRRVETERDVAFT 310
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKA-ERYQALLKE----KREYEGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 311 DLRRMTTERDSLRERLkiaqetafnekAHLEQRIEELECTVHNLDDERMEQM--------ANMTLMKETITTVEKEMKSL 382
Cdd:TIGR02169 252 ELEKLTEEISELEKRL-----------EEIEQLLEELNKKIKDLGEEEQLRVkekigeleAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 383 ARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGAT 462
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 463 LNDLAKEKECLQACLDKKSENIASLGESLAMKE----KTISGMKNIIAEMEQASR---QSTEALIMCEQDISRMRRQLDE 535
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEakinELEEEKEDKALEIKKQEWkleQLAADLSKYEQELYDLKEEYDR 480
|
330
....*....|....*
gi 1039728160 536 TNDELGQIARERDIL 550
Cdd:TIGR02169 481 VEKELSKLQRELAEA 495
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
593-714 |
7.50e-07 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 51.89 E-value: 7.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 593 NLEVNKLKNILKSEESENRQIMEQLrkANEDAEnwenkARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQMENE 672
Cdd:PRK09039 59 NSQIAELADLLSLERQGNQDLQDSV--ANLRAS-----LSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQV 131
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1039728160 673 LDSARSEIELLRSQMTNERISMQNLEALLVA--NRDKEYQSQIA 714
Cdd:PRK09039 132 SARALAQVELLNQQIAALRRQLAALEAALDAseKRDRESQAKIA 175
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
42-448 |
7.53e-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: 53.14 E-value: 7.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 42 GRNQNTFQLEQEVRTQDRFISTLKLQIEDLKQTNHDLEEYVRKLLDSKEAVSTQVDDLAnhnehlcKELIKLDQLAEKLQ 121
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR-------KDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 122 KEknfvVDTADKELEEAKIELICQQNNITVLEDTIQRLKSIILETEKAQNTSPSRLDSFVKTLEADRDYYKTEAQNLRKM 201
Cdd:TIGR02168 747 ER----IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 202 MRNRSKSPRRPSPTSRAANCDVELLKSTARDREELKCMLEKYERHLAEIQGNVKVLTSERDktfllyeQAQEEIARLRRE 281
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA-------SLEEALALLRSE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 282 MmksckspksttahailrrveterDVAFTDLRRMTTERDSLRERLKIAQEtafnEKAHLEQRIEELECTVHNLDDERMEQ 361
Cdd:TIGR02168 896 L-----------------------EELSEELRELESKRSELRRELEELRE----KLAQLELRLEGLEVRIDNLQERLSEE 948
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 362 mANMTLmkETITTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEK 441
Cdd:TIGR02168 949 -YSLTL--EEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEE 1025
|
....*..
gi 1039728160 442 IDNFTRQ 448
Cdd:TIGR02168 1026 IDREARE 1032
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
377-677 |
7.66e-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: 53.14 E-value: 7.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 377 KEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEI 456
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 457 SILGATLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQstealimceqdisrMRRQLDET 536
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE--------------LESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 537 NDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVnklkniLKSEESENRQIMEQ 616
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE------LQAELEELEEELEE 451
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039728160 617 LRKANEDAENWENKARQTEAENNTlklELITAEAEGNRLKEKVDALNREVEQMENELDSAR 677
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQ---ALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
364-764 |
7.95e-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: 52.72 E-value: 7.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 364 NMTLMKETITTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKID 443
Cdd:TIGR04523 62 NLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNID 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 444 NFTRQNIAQREEISILGATLNDLAKEKECLQACLD-------KKSENIASLGESLAMKEKTISGMKNI----------IA 506
Cdd:TIGR04523 142 KFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNllekeklNIQKNIDKIKNKLLKLELLLSNLKKKiqknkslesqIS 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 507 EMEQASRQSTEALIMCEQDISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIK 586
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLN 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 587 -QKVQDTNlevNKLKNILKSEESENRQIMEQLRKANEdaenwenKARQTEAENNTLKLELITAEAEGNRLKEKVDALNRE 665
Cdd:TIGR04523 302 nQKEQDWN---KELKSELKNQEKKLEEIQNQISQNNK-------IISQLNEQISQLKKELTNSESENSEKQRELEEKQNE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 666 VEQMENELDSARSEIELLRSQMTNERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQ 745
Cdd:TIGR04523 372 IEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV 451
|
410
....*....|....*....
gi 1039728160 746 FRNVVTQLEADLDITKRQL 764
Cdd:TIGR04523 452 KELIIKNLDNTRESLETQL 470
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
110-683 |
1.90e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 110 LIKLDQLAEKLQKeknfvvdtADKELEEAKIELICQQNNITVLEDTIQRLKSIILETEKAQNTSPSRLDSFVK---TLEA 186
Cdd:COG1196 231 LLKLRELEAELEE--------LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAelaRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 187 DRDYYKTEAQNLRkmmrnrsksprrpsptsraancdvELLKSTARDREELKCMLEKYERHLAEIQGNVKVLTSERDKTFL 266
Cdd:COG1196 303 DIARLEERRRELE------------------------ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 267 LYEQAQEEIARLRREMmksckSPKSTTAHAILRRVETERDVAF------TDLRRMTTERDSLRERLKIAQETAFNEKAHL 340
Cdd:COG1196 359 ELAEAEEALLEAEAEL-----AEAEEELEELAEELLEALRAAAelaaqlEELEEAEEALLERLERLEEELEELEEALAEL 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 341 EQRIEELECTVHNLDDERMEQMANMTLMKETITTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRH 420
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 421 LAKKKYELQLTQEKIMCLDEKIDnftRQNIAQREEISILGATLNDLAKEKECLQAcLDKKSENIASLGESLAMKEKTISG 500
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAAY---EAALEAALAAALQNIVVEDDEVAAAAIEY-LKAAKAGRATFLPLDKIRARAALA 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 501 MKNIIAEMEQASRQSTEALIMCEQDISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHN 580
Cdd:COG1196 590 AALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 581 ELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENW-------ENKARQTEAENNTLKLELITAEAEGN 653
Cdd:COG1196 670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERleeeleeEALEEQLEAEREELLEELLEEEELLE 749
|
570 580 590
....*....|....*....|....*....|
gi 1039728160 654 RLKEKVDALNREVEQMENELDSARSEIELL 683
Cdd:COG1196 750 EEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
532-723 |
2.29e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 532 QLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKS------ 605
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 606 EESENRQIMEQLRKANEDAE---NWENKARQTEAENNTLKlELITAEAEGNRLKEKVDALNREVEQMENELDSARSEIEL 682
Cdd:COG3883 97 RSGGSVSYLDVLLGSESFSDfldRLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039728160 683 LRSQMTNERISMQNLEALLVANRDKEYQSQIALQEKESEIQ 723
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
569-781 |
3.84e-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: 50.15 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 569 QALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKARQTEAENNTLKLELITA 648
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 649 EAEGNRLKEKVDALNREVEQMENE-----LDSARSEIELLRSQMTNERISMQNLEALLVANRDKEyqsqiALQEKESEIQ 723
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQpplalLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA-----ELAALRAELE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039728160 724 LLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERAVQELRRQ 781
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
456-764 |
5.26e-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: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 456 ISILGATLNDLAKEKECL---QACLDKKSEniASLGESLAMKEKTISGMKNIIAEMEQAsrqstealimcEQDISRMRRQ 532
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAeryQALLKEKRE--YEGYELLKEKEALERQKEAIERQLASL-----------EEELEKLTEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 533 LDETNDELGQIARERDILAHENDNLQEQfakvkqENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQ 612
Cdd:TIGR02169 260 ISELEKRLEEIEQLLEELNKKIKDLGEE------EQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 613 IMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQMENELDSARSEI-----ELLRSQM 687
Cdd:TIGR02169 334 LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREInelkrELDRLQE 413
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039728160 688 TNERISMQ--NLEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQL 764
Cdd:TIGR02169 414 ELQRLSEElaDLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
523-712 |
7.78e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 7.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 523 EQDISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNI 602
Cdd:COG3883 29 QAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 603 LKSEE---------------SENRQIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAEgnrLKEKVDALNREVE 667
Cdd:COG3883 109 LGSESfsdfldrlsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE---LEAQQAEQEALLA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039728160 668 QMENELDSARSEIELLRSQMTNERISMQNLEALLVANRDKEYQSQ 712
Cdd:COG3883 186 QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
481-707 |
9.36e-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: 48.61 E-value: 9.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 481 SENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQDISRMRRQLDETNDELGQiarerdilahendnLQEQ 560
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA--------------LEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 561 FAKVKQENQALSKKLNDTHNELSDIKQKVQdTNLEVNKLKNILKSEESE------------NRQIMEQLRKANEDAENWE 628
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRALY-RLGRQPPLALLLSPEDFLdavrrlqylkylAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039728160 629 NKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQMENELDSARSEIELLRSQMTNERISMQNLEALLVANRDK 707
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
451-676 |
1.19e-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: 48.61 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 451 AQREEISILGATLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQDISRMR 530
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 531 RQLDETNDELGQIARER---------DILAHENDNLQ--EQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKL 599
Cdd:COG4942 97 AELEAQKEELAELLRALyrlgrqpplALLLSPEDFLDavRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039728160 600 KNiLKSEESENRQIMEQLRKANEDAenwenkARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQMENELDSA 676
Cdd:COG4942 177 EA-LLAELEEERAALEALKAERQKL------LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
524-703 |
1.33e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 524 QDISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLN--DTHNELSDIKQKVQDTNLEVNKLKN 601
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 602 ilksEESENRQIMEQLRKANEDAENWENKARQTEAENNTLKL-ELITAEAEGNRLKEKVDALNREVEQMENELDSARSEI 680
Cdd:COG4717 154 ----RLEELRELEEELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180
....*....|....*....|...
gi 1039728160 681 ELLRSQMTNERISMQNLEALLVA 703
Cdd:COG4717 230 EQLENELEAAALEERLKEARLLL 252
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
266-787 |
1.34e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 266 LLYEQAQEEIARLRREMMKSckspksTTAHAILRRVETERDVAFTDLRRMTTERDSLRERLKIAQETAFNEKAHLEQRIE 345
Cdd:TIGR02168 232 LRLEELREELEELQEELKEA------EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 346 ELECTVHNLDDE--------------RMEQMANMTLMKETITTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTE 411
Cdd:TIGR02168 306 ILRERLANLERQleeleaqleeleskLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 412 KDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISI-----LGATLNDLAKEKECLQACLDKKSENIAS 486
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelkeLQAELEELEEELEELQEELERLEEALEE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 487 LGESLAMKEKTISGMKNIIAEMeQASRQSTEALIMCEQDISRMRRQLDETNDELGQI----------------ARERDIL 550
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQL-QARLDSLERLQENLEGFSEGVKALLKNQSGLSGIlgvlselisvdegyeaAIEAALG 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 551 AHENDNLQEQFAKVKQENQALSKKLNDTHN--ELSDIK-QKVQDTNLEVNKLKNILKSEESENRQIMEQLRKA------- 620
Cdd:TIGR02168 545 GRLQAVVVENLNAAKKAIAFLKQNELGRVTflPLDSIKgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAlsyllgg 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 621 ---NEDAENWENKARQTEAENN--TLKLELIT--------------------------------AEAEGNRLKEKVDALN 663
Cdd:TIGR02168 625 vlvVDDLDNALELAKKLRPGYRivTLDGDLVRpggvitggsaktnssilerrreieeleekieeLEEKIAELEKALAELR 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 664 REVEQMENELDSARSEIELLRSQMTNERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKE-------HLCLAENKM 736
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEErleeaeeELAEAEAEI 784
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1039728160 737 AIQSRDVAQFRNVVTQLEADLDITKRQLGTERfeRERAVQELRRQNYSSNA 787
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAELTLLN--EEAANLRERLESLERRI 833
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
411-640 |
1.72e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 411 EKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGATLNDLAKEKECLQACLDKKSENIASLGES 490
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 491 LAMKEKTISGMKNIIaemeqaSRQSTEALImceQDISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQA 570
Cdd:COG3883 95 LYRSGGSVSYLDVLL------GSESFSDFL---DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 571 LSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKARQTEAENNT 640
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
231-781 |
2.15e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 231 RDREELKCMLEKYERHLAEIQGNVKVLTSERDKTFLLYEQAQEEIARLRREmmksckspksttahaiLRRVETERDVAFT 310
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE----------------LEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 311 DLRRMTTERDSLRERLKIAQEtafnEKAHLEQRIEELECTVHNLDDERMEQMANMTLMKETITTVEKEMKSLARKAMDTE 390
Cdd:COG1196 289 EEYELLAELARLEQDIARLEE----RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 391 SELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGATLNDLAKEK 470
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 471 ECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMcEQDISRMRRQLDETNDELGQIARERDIL 550
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL-LLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 551 AHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQD----------TNLEVNKLKNILKSEESENRQIMEQLRKA 620
Cdd:COG1196 524 GAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEylkaakagraTFLPLDKIRARAALAAALARGAIGAAVDL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 621 NEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQMENELDSARSEIELLRSQMTNE----RISMQN 696
Cdd:COG1196 604 VASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAlleaEAELEE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 697 LEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERAVQ 776
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
....*
gi 1039728160 777 ELRRQ 781
Cdd:COG1196 764 ELERE 768
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
50-782 |
2.16e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.43 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 50 LEQEVRTQDRFISTLKLQIEDLKQTNHDLEEYVRKLLDSKEAVSTQVDDLANHNEHLckelikldQLAEKLQKEKNFVVD 129
Cdd:pfam02463 267 LAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK--------KKAEKELKKEKEEIE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 130 TADKELEEAKIelicqqnnitvledTIQRLKSIILETEKAQNTSPSRLDSFVKTLEADRDYYKTEAQNLRKMMRNRSKSP 209
Cdd:pfam02463 339 ELEKELKELEI--------------KREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 210 RRPSPTSRAANCDVELLKSTARDREELKCMLEKYERHLAEIQGNVKVLTSERDKTFLLYEQAQEEIARLRREmmKSCKSP 289
Cdd:pfam02463 405 KEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKE--TQLVKL 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 290 KSTTAHAILRRVETERDVAFTDLRRMTTERDSLRERLKIAQETAFNEKAHLEQRIEELE----CTVHNLDDERMEQMANM 365
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYkvaiSTAVIVEVSATADEVEE 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 366 TLMKETITTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENtEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNF 445
Cdd:pfam02463 563 RQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLA-QLDKATLEADEDDKRAKVVEGILKDTELTKLKESA 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 446 TRQNIAQREEISILGATLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQD 525
Cdd:pfam02463 642 KAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEE 721
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 526 ISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQdtNLEVNKLKNILKS 605
Cdd:pfam02463 722 LLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKL--KVEEEKEEKLKAQ 799
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 606 EESENRQIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQMENELDSARSEIELLRS 685
Cdd:pfam02463 800 EEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEEL 879
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 686 QMTNERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLG 765
Cdd:pfam02463 880 EEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEE 959
|
730
....*....|....*..
gi 1039728160 766 TERFERERAVQELRRQN 782
Cdd:pfam02463 960 ERNKRLLLAKEELGKVN 976
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
532-768 |
4.00e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 532 QLDETNDELGQIARERDILAHENDNLQ--EQFAKVKQENQALSKKLNDTHNELSDIKQkvqdtnlEVNKLKNILKSEESE 609
Cdd:PRK11281 44 QLDALNKQKLLEAEDKLVQQDLEQTLAllDKIDRQKEETEQLKQQLAQAPAKLRQAQA-------ELEALKDDNDEETRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 610 N------RQIMEQLRKANEDAENWENkarqTEAENNTLkleLITAEAEGNRLKEKVDALNREVEQMENELDSAR------ 677
Cdd:PRK11281 117 TlstlslRQLESRLAQTLDQLQNAQN----DLAEYNSQ---LVSLQTQPERAQAALYANSQRLQQIRNLLKGGKvggkal 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 678 ---------SEIELLRSQMTNERISMQN---LEALLVANRDkEYQSQIALQEKesEIQLLKE-----HLCLAENKM--AI 738
Cdd:PRK11281 190 rpsqrvllqAEQALLNAQNDLQRKSLEGntqLQDLLQKQRD-YLTARIQRLEH--QLQLLQEainskRLTLSEKTVqeAQ 266
|
250 260 270
....*....|....*....|....*....|....
gi 1039728160 739 QSRDVAQFRN---VVTQLEADLDITKRQLG-TER 768
Cdd:PRK11281 267 SQDEAARIQAnplVAQELEINLQLSQRLLKaTEK 300
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
108-781 |
5.86e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.96 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 108 KELIKLDQLAEKLQKEKnfvvdtadKELEEAKIELICQQNNITVLEDTIQRlKSIILETEKAQNTSPSRLDSFVKTLEAD 187
Cdd:TIGR00606 319 RELVDCQRELEKLNKER--------RLLNQEKTELLVEQGRLQLQADRHQE-HIRARDSLIQSLATRLELDGFERGPFSE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 188 RdyyktEAQNLRKMMRNRSKSPRRpsptsraancdvellkSTARDREELKCMLEKYERHLAEIQGNVKVLTSERDKTFLL 267
Cdd:TIGR00606 390 R-----QIKNFHTLVIERQEDEAK----------------TAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEI 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 268 YEQAQEEIARLRREMMKSCKSPKSttahaiLRRVETERDVAFTDLRRMttERDSLRERLKIAQETAFNEKAHLEQRIEEL 347
Cdd:TIGR00606 449 LEKKQEELKFVIKELQQLEGSSDR------ILELDQELRKAERELSKA--EKNSLTETLKKEVKSLQNEKADLDRKLRKL 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 348 ectvhnldDERMEQmanmtlmKETITTVEKEMKSLARKAMDTESELGRQKAENNSL---RLLYENTEKDLSDTqrhLAKK 424
Cdd:TIGR00606 521 --------DQEMEQ-------LNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDEltsLLGYFPNKKQLEDW---LHSK 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 425 KYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGATLNDLAKE--KECLQACLDKKSENIASLGESLAMKEKTISGMK 502
Cdd:TIGR00606 583 SKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfDVCGSQDEESDLERLKEEIEKSSKQRAMLAGAT 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 503 NIIAE-MEQASRQSTEALIMCEQDIsRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQAL----SKKLND 577
Cdd:TIGR00606 663 AVYSQfITQLTDENQSCCPVCQRVF-QTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLapgrQSIIDL 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 578 THNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKAR-QTEAENNTLKLELITAEAEGNRLK 656
Cdd:TIGR00606 742 KEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERfQMELKDVERKIAQQAAKLQGSDLD 821
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 657 EKVDALNREVEQMENELDSARSEIELLRSQMTNERISMQNLEALLVANRDKEYQSQIALQEKeseiQLLKEHLCLAENKM 736
Cdd:TIGR00606 822 RTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRR----QQFEEQLVELSTEV 897
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1039728160 737 AIQSRDVAQFRNVVTQLEADL--DITKRQLGTERFERERAVQELRRQ 781
Cdd:TIGR00606 898 QSLIREIKDAKEQDSPLETFLekDQQEKEELISSKETSNKKAQDKVN 944
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
611-782 |
6.54e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 611 RQIMEQLRKAneDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQMENELDSARSEIELLRSQMTNE 690
Cdd:COG1196 216 RELKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 691 RISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFE 770
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170
....*....|..
gi 1039728160 771 RERAVQELRRQN 782
Cdd:COG1196 374 LAEAEEELEELA 385
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
59-637 |
1.13e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 59 RFISTLKLQIEDLKQTNHDLEEYVRKLLDSKEAVSTQVDDLANHNEHLCKELIKLDQLAEKLQKEKNfvvdtadkELEEA 138
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE--------EIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 139 KIELICQQNNITVLEDTIQRLKSIILETEKAQntspSRLDSFVKTLEADRDyYKTEAQNLRKMMRNRSKSPRRPSPTSRA 218
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEI----EELEEKVKELKELKE-KAEEYIKLSEFYEEYLDELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 219 ANCDVELLKSTARDREELKCMLEKYERHLAEIQGNVKVLtserDKTFLLYEQAQEEIARLRR-EMMKSCKSPKSttAHAI 297
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEL----EERHELYEEAKAKKEELERlKKRLTGLTPEK--LEKE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 298 LRRVETERDVAFTDLRRMTTERDSLRerlkiaqetafNEKAHLEQRIEELE--------CTVHNLDDERMEQMANMTLmk 369
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELK-----------KEIKELKKAIEELKkakgkcpvCGRELTEEHRKELLEEYTA-- 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 370 eTITTVEKEMKSLARKAMDTESELGR-QKAENNSLRLLyenTEKDLSDTQRHLAKKKYELQLtqEKIMCLDEKIDNFTRQ 448
Cdd:PRK03918 460 -ELKRIEKELKEIEEKERKLRKELRElEKVLKKESELI---KLKELAEQLKELEEKLKKYNL--EELEKKAEEYEKLKEK 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 449 NIAQREEISILGATL---NDLAKEKECLQACLDKKSENIASL-GESLAMKEKTISGMKNIIAEMEQASRQSTEA------ 518
Cdd:PRK03918 534 LIKLKGEIKSLKKELeklEELKKKLAELEKKLDELEEELAELlKELEELGFESVEELEERLKELEPFYNEYLELkdaeke 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 519 -------LIMCEQDISRMRRQLDETNDELGQIARERDILAHENDnlQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQD 591
Cdd:PRK03918 614 lereekeLKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREE 691
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1039728160 592 TNLEVNKLKNILKsEESENRQIMEQLRKANEDAENWENKARQTEAE 637
Cdd:PRK03918 692 IKKTLEKLKEELE-EREKAKKELEKLEKALERVEELREKVKKYKAL 736
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
463-785 |
1.47e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.27 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 463 LNDLAKEKECLQACLDKKSENIASLGESLamkEKTISGMKNIIAEMEQASRQSTEalimceqDISRMRRQLDETNDELGQ 542
Cdd:pfam07888 43 RAELLQAQEAANRQREKEKERYKRDREQW---ERQRRELESRVAELKEELRQSRE-------KHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 543 IARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQdtnlevnKLKNILKSEESENRQImeqlrkane 622
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAK-------KAGAQRKEEEAERKQL--------- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 623 daenwENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQMENELDSAR---SEIELLRSQMTNER----ISMQ 695
Cdd:pfam07888 177 -----QAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHrkeAENEALLEELRSLQerlnASER 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 696 NLEAL------LVANRDKEYQS--QIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNV------VTQLEADLDITK 761
Cdd:pfam07888 252 KVEGLgeelssMAAQRDRTQAElhQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAeadkdrIEKLSAELQRLE 331
|
330 340
....*....|....*....|....
gi 1039728160 762 RQLGTERFERERAVQELRRQNYSS 785
Cdd:pfam07888 332 ERLQEERMEREKLEVELGREKDCN 355
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
557-748 |
1.57e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 557 LQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKARQTEA 636
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 637 ENNTLKLELITAEAEGNRLKEKVDALNREVEQMENELDSARSEIELLRSQMTNERISMQNLEALLVANRDKEYQSQIALQ 716
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190
....*....|....*....|....*....|..
gi 1039728160 717 EKESEIQLLKEHLCLAENKMAIQSRDVAQFRN 748
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEEL 220
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
526-742 |
2.63e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 526 ISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKS 605
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 606 EESENRQIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQMENEL--DSARSEIELL 683
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELqaLSEAEAEQAL 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039728160 684 RSQMTNERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRD 742
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
507-691 |
2.85e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 507 EMEQASRQsTEALimceQDISRMRRQLDETNDELGQIARERDILAHENDnlQEQFAKVKQENQALSKKLNDTHNELSDIK 586
Cdd:COG4913 243 ALEDAREQ-IELL----EPIRELAERYAAARERLAELEYLRAALRLWFA--QRRLELLEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 587 QKVQDTNLEVNKLKNILKSEESENR-QIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNRE 665
Cdd:COG4913 316 ARLDALREELDELEAQIRGNGGDRLeQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA 395
|
170 180
....*....|....*....|....*.
gi 1039728160 666 VEQMENELDSARSEIELLRSQMTNER 691
Cdd:COG4913 396 LEEELEALEEALAEAEAALRDLRREL 421
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
373-574 |
3.36e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 43.65 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 373 TTVEKEMKSLARKAMDTESELgrqKAENNSLRLLYENTEKDLSDTQRHlakkkyeLQLTQEKIMCLDEKIDNFTRQNIAQ 452
Cdd:pfam15905 148 DGTQKKMSSLSMELMKLRNKL---EAKMKEVMAKQEGMEGKLQVTQKN-------LEHSKGKVAQLEEKLVSTEKEKIEE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 453 REEISILGATLndlaKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEalimceqDISRMRRQ 532
Cdd:pfam15905 218 KSETEKLLEYI----TELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIK-------DLNEKCKL 286
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039728160 533 LDETNDELGQIARERDI-LAHENDNLQEQFAKVKQENQALSKK 574
Cdd:pfam15905 287 LESEKEELLREYEEKEQtLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
616-781 |
3.41e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 616 QLRKANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQMENELDSARSEIELLRSQMTNERISMQ 695
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 696 N-------LEALLVAN------RDKEYQSQIALQEKEsEIQLLKEhlclAENKMAIQSRDVAQFRNVVTQLEADLDITKR 762
Cdd:COG3883 97 RsggsvsyLDVLLGSEsfsdflDRLSALSKIADADAD-LLEELKA----DKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170
....*....|....*....
gi 1039728160 763 QLGTERFERERAVQELRRQ 781
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAE 190
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
494-727 |
3.95e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 43.86 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 494 KEKTISGMKNIIAEMEQASRQSTEAlimcEQDISRMRRQLDETNDELGQIARERDILA---HENDNLQEQFAKVKQENQA 570
Cdd:pfam05667 242 KRKRTKLLKRIAEQLRSAALAGTEA----TSGASRSAQDLAELLSSFSGSSTTDTGLTkgsRFTHTEKLQFTNEAPAATS 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 571 LSKKLNDTHN--------ELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRkaNEDAENWENKArQTEAENNTLK 642
Cdd:pfam05667 318 SPPTKVETEEelqqqreeELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELE--ELKEQNEELEK-QYKVKKKTLD 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 643 LeLITAEAEGNRLKEKVDALNREVEQMENELDSARS----EIELLRSQMTNERISMQNLEALLVANRDKEYQSQIALQEK 718
Cdd:pfam05667 395 L-LPDAEENIAKLQALVDASAQRLVELAGQWEKHRVplieEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQK 473
|
250
....*....|
gi 1039728160 719 ESEI-QLLKE 727
Cdd:pfam05667 474 EELYkQLVAE 483
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
312-667 |
4.56e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.19 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 312 LRRMTTERDSLRERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQmanmtlmketITTVEKEMKSLARKAMDTES 391
Cdd:pfam02463 175 LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEE----------YLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 392 ELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGATLNDLAKEKE 471
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 472 CLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQDISRMRRQLDETNDELGQIARERDILA 551
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 552 HENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKA 631
Cdd:pfam02463 405 KEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQE 484
|
330 340 350
....*....|....*....|....*....|....*.
gi 1039728160 632 RQTEAENNTLKLELITAEAEGNRLKEKVDALNREVE 667
Cdd:pfam02463 485 QLELLLSRQKLEERSQKESKARSGLKVLLALIKDGV 520
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
553-788 |
6.44e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 553 ENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKAR 632
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 633 QTEAENNTLKLeLITAEAEGNRLkEKVDALNREVEQMENELDSARSEIELLRSQMTNERISMQNLEALLVANRDKEYQSQ 712
Cdd:COG3883 97 RSGGSVSYLDV-LLGSESFSDFL-DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039728160 713 IALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERAVQELRRQNYSSNAY 788
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
312-642 |
6.81e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 312 LRRMTTERDSLRERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMANMTLMKETITTVEKEMKSLARKAMDTES 391
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 392 ELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGATLNDLAKEKE 471
Cdd:TIGR04523 441 EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 472 CLQacldkksENIASLGESLAMKEKTISGMKNIIAEMEQasrqstealimcEQDISRMRRQLDETNDELGQIARERDILA 551
Cdd:TIGR04523 521 SLK-------EKIEKLESEKKEKESKISDLEDELNKDDF------------ELKKENLEKEIDEKNKEIEELKQTQKSLK 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 552 HENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKA 631
Cdd:TIGR04523 582 KKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKW 661
|
330
....*....|.
gi 1039728160 632 RQTEAENNTLK 642
Cdd:TIGR04523 662 PEIIKKIKESK 672
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
230-700 |
7.25e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 230 ARDREELKCMLEKYERHLAEIQ---GNVKVLTSERDKTFLLYEQAQEEIARLRREMMKSCKSPKSTTAHAILRRVETERd 306
Cdd:PRK02224 233 RETRDEADEVLEEHEERREELEtleAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEA- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 307 vafTDLRR--MTTERDSLRERL--KIAQETAFNEKAH--------LEQRIEELECTVHNLDDERMEQMANMTLMKETITT 374
Cdd:PRK02224 312 ---VEARReeLEDRDEELRDRLeeCRVAAQAHNEEAEslredaddLEERAEELREEAAELESELEEAREAVEDRREEIEE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 375 VEKEMKSLARKAMDTESELGRQKAENNSLRLLYENT---EKDLSDTQRHLAKKKYELQLTQEKIMC-------------- 437
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELrerEAELEATLRTARERVEEAEALLEAGKCpecgqpvegsphve 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 438 ----LDEKIDNFTRQNIAQREEISILGATLN------DLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAE 507
Cdd:PRK02224 469 tieeDRERVEELEAELEDLEEEVEEVEERLEraedlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 508 MEQASRQSTEALIMCEQDISRMRRQLDETNDELGQIARERDILahenDNLQEQFAKVKQENQALSkKLNDTHNELSDIKQ 587
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL----ERIRTLLAAIADAEDEIE-RLREKREALAELND 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 588 KVQDTNLEVNKLKNILKSEESENR--QIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAE---GNRLKEKVDAL 662
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEFDEARieEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENEleeLEELRERREAL 703
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1039728160 663 NREVEQmeneLDSARSEIELLRSQMTNERISM--QNLEAL 700
Cdd:PRK02224 704 ENRVEA----LEALYDEAEELESMYGDLRAELrqRNVETL 739
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
335-685 |
7.29e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.09 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 335 NEKAHLEQRIEELECTVHNLDDERMEQMANMTLMKETI---TTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTE 411
Cdd:TIGR04523 173 NELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIqknKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 412 KDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQ------------NIAQREEISILGATLNDLAKEKECLQACLDK 479
Cdd:TIGR04523 253 TQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQlnqlkseisdlnNQKEQDWNKELKSELKNQEKKLEEIQNQISQ 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 480 KSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCE-------QDISRMRRQLDETNDELGQIARERDILAH 552
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKkenqsykQEIKNLESQINDLESKIQNQEKLNQQKDE 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 553 ENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKAR 632
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELK 492
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1039728160 633 QTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQMENELDSARSEIELLRS 685
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED 545
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
555-781 |
8.32e-04 |
|
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: 8.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 555 DNLQEQFakvkqenqalsKKLNDTHNELSDIKQKVqdtnlevnklknilkseesenrqimEQLRKANEDAENWEnKARQT 634
Cdd:COG4913 228 DALVEHF-----------DDLERAHEALEDAREQI-------------------------ELLEPIRELAERYA-AARER 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 635 EAENNTLK--LELITAEAEGNRLKEKVDALNREVEQMENELDSARSEIELLRsqmtnerismqnlEALLVANRDKEYQSQ 712
Cdd:COG4913 271 LAELEYLRaaLRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALR-------------EELDELEAQIRGNGG 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 713 IALQEKESEIQLLKEHLCLAENKMAIQSRDVAQF--------------RNVVTQLEADLDITKRQLGTERFERERAVQEL 778
Cdd:COG4913 338 DRLEQLEREIERLERELEERERRRARLEALLAALglplpasaeefaalRAEAAALLEALEEELEALEEALAEAEAALRDL 417
|
...
gi 1039728160 779 RRQ 781
Cdd:COG4913 418 RRE 420
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
450-698 |
8.82e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 450 IAQREEISiLGATLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTIS---GMKNIIAEMEQASRQSTEALIMCEQDI 526
Cdd:PRK02224 196 IEEKEEKD-LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEeheERREELETLEAEIEDLRETIAETERER 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 527 SRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSE 606
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 607 ESENRQIMEQLRKANEDAENWENKARQTEAEnntlkLELITAEAEGNRlkEKVDALNREVEQMENELDSARSEIELLRSQ 686
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREE-----IEELEEEIEELR--ERFGDAPVDLGNAEDFLEELREERDELRER 427
|
250
....*....|..
gi 1039728160 687 MTNERISMQNLE 698
Cdd:PRK02224 428 EAELEATLRTAR 439
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
442-682 |
9.44e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 442 IDNFTRQNIAQREEISilGATLNDLAKEKECLQACLD---------KKSENIASLGESLAMKEKTISGMKNIIAEMeQAS 512
Cdd:COG3206 158 AEAYLEQNLELRREEA--RKALEFLEEQLPELRKELEeaeaaleefRQKNGLVDLSEEAKLLLQQLSELESQLAEA-RAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 513 RQSTEALImceqdiSRMRRQLDETNDELGQIARERDIlahenDNLQEQFAKVKQENQALSKKLNDTHnelsdikQKVQDT 592
Cdd:COG3206 235 LAEAEARL------AALRAQLGSGPDALPELLQSPVI-----QQLRAQLAELEAELAELSARYTPNH-------PDVIAL 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 593 NLEVNKLKNILKSEEsenRQIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQMENE 672
Cdd:COG3206 297 RAQIAALRAQLQQEA---QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQR 373
|
250
....*....|
gi 1039728160 673 LDSARSEIEL 682
Cdd:COG3206 374 LEEARLAEAL 383
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
335-546 |
1.01e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 335 NEKAHLEQRIEELECTVHNLDDERMEQMANMTLMKETITTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDL 414
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 415 SDTQRHLAKKKYELQ-----------LTQEKIMCLDEKIDNFTRQNIAQREEISILGATLNDLAKEKECLQACLDKKSEN 483
Cdd:COG4942 100 EAQKEELAELLRALYrlgrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039728160 484 IASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQDISRMRRQLDETNDELGQIARE 546
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
234-780 |
1.31e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 234 EELKCMLEKYERHLAEIQGNVKVLTSERDKTFLLYEQAQEEIARLRREMMKSCKSPKSTTAhaiLRRVETERDVAF-TDL 312
Cdd:pfam01576 415 QELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQE---LLQEETRQKLNLsTRL 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 313 RRMTTERDSLRERLKIAQETafneKAHLEQRIEELECTVHNLDDERMEQMANMTLMKETITTVEKEMKSLARKAMDTESE 392
Cdd:pfam01576 492 RQLEDERNSLQEQLEEEEEA----KRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAA 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 393 LGRQKAENNSLRLLYENTEKDLsDTQRHLA------KKKYELQLTQEKIMCL----------------DEKIDNFTRQNI 450
Cdd:pfam01576 568 YDKLEKTKNRLQQELDDLLVDL-DHQRQLVsnlekkQKKFDQMLAEEKAISAryaeerdraeaearekETRALSLARALE 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 451 AQREEISILGATLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQDISRMR 530
Cdd:pfam01576 647 EALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALK 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 531 RQLD---ETNDELGQiARERDILAHENDNLQEQFAKVKQENQALS---------------------------KKLNDTHN 580
Cdd:pfam01576 727 AQFErdlQARDEQGE-EKRRQLVKQVRELEAELEDERKQRAQAVAakkkleldlkeleaqidaankgreeavKQLKKLQA 805
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 581 ELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVD 660
Cdd:pfam01576 806 QMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKR 885
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 661 ALNREVEQMENELDSARSEIELLRSQMTNERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKehLCLAENKMAIQS 740
Cdd:pfam01576 886 RLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELK--AKLQEMEGTVKS 963
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1039728160 741 RdvaqFRNVVTQLEADLDITKRQLGTERFERERAVQELRR 780
Cdd:pfam01576 964 K----FKSSIAALEAKIAQLEEQLEQESRERQAANKLVRR 999
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
45-709 |
2.06e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.96 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 45 QNTFQLEQEVRTQDRFISTLKLQIEDLKQTNHDLEEYVRKLLDSKEAVSTQ---VDDLANHNEHLCKELIK-LDQLAEKL 120
Cdd:TIGR01612 582 KDLFDKYLEIDDEIIYINKLKLELKEKIKNISDKNEYIKKAIDLKKIIENNnayIDELAKISPYQVPEHLKnKDKIYSTI 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 121 QKEKNFVV-DTADKELEEakIELICQQNNITVLED--TIQRLKSII-LETEKAQNTSPSRLDSFVKTLEADRDYYKTEAQ 196
Cdd:TIGR01612 662 KSELSKIYeDDIDALYNE--LSSIVKENAIDNTEDkaKLDDLKSKIdKEYDKIQNMETATVELHLSNIENKKNELLDIIV 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 197 NLRKMMRnrsksprrpSPTSRAANCDVELLKSTAR-------DREELKCMLEKYERHLAEI------QGNVKVLTSERDK 263
Cdd:TIGR01612 740 EIKKHIH---------GEINKDLNKILEDFKNKEKelsnkinDYAKEKDELNKYKSKISEIknhyndQINIDNIKDEDAK 810
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 264 TFllYEQAQEEIARLrremmksckSPKSTTAHAILRRVETERDVAFTDLRRMTTERDSLRERLKiAQETAFNE---KAHL 340
Cdd:TIGR01612 811 QN--YDKSKEYIKTI---------SIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEKID-SEHEQFAEltnKIKA 878
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 341 EQRIEELECTVHNLDDERmeqmanmTLMKETITTVEKEMKSL-ARKAMDTESELGRQKAEN-----NSLRLLYENTEKDL 414
Cdd:TIGR01612 879 EISDDKLNDYEKKFNDSK-------SLINEINKSIEEEYQNInTLKKVDEYIKICENTKESiekfhNKQNILKEILNKNI 951
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 415 SDTQR-HLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREE-----ISILGATLNDLAKEKE-CLQACLDKKSENIASL 487
Cdd:TIGR01612 952 DTIKEsNLIEKSYKDKFDNTLIDKINELDKAFKDASLNDYEAknnelIKYFNDLKANLGKNKEnMLYHQFDEKEKATNDI 1031
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 488 GESLAMKEKTISGMK--------NIIAEMEQASRQSTEAL---IMCEQDISRMrrQLDETNDELgQIARERDILAHENDN 556
Cdd:TIGR01612 1032 EQKIEDANKNIPNIEiaihtsiyNIIDEIEKEIGKNIELLnkeILEEAEINIT--NFNEIKEKL-KHYNFDDFGKEENIK 1108
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 557 LQEQFAKVKQENQALSKKLNDTHNELSDIKQK----VQDTNLEVNKLKNILKS-------EESENRQ------------I 613
Cdd:TIGR01612 1109 YADEINKIKDDIKNLDQKIDHHIKALEEIKKKsenyIDEIKAQINDLEDVADKaisnddpEEIEKKIenivtkidkkknI 1188
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 614 MEQLRK-ANEDAENWENKARQTEAEN---------NTLKLELITAEaegnrlKEKVDALNREVEQMENELDSARSEIELL 683
Cdd:TIGR01612 1189 YDEIKKlLNEIAEIEKDKTSLEEVKGinlsygknlGKLFLEKIDEE------KKKSEHMIKAMEAYIEDLDEIKEKSPEI 1262
|
730 740
....*....|....*....|....*..
gi 1039728160 684 RSQMTNERISMQNLEALLVAN-RDKEY 709
Cdd:TIGR01612 1263 ENEMGIEMDIKAEMETFNISHdDDKDH 1289
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
392-675 |
2.63e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.36 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 392 ELGRQKAENNSLRLLYENTEKDL---SDTQRHLAKK-----KYELQLTQEKIMCLDEKIDNFTRQNIAQREEISilGATL 463
Cdd:pfam12128 633 ELEKASREETFARTALKNARLDLrrlFDEKQSEKDKknkalAERKDSANERLNSLEAQLKQLDKKHQAWLEEQK--EQKR 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 464 NDLAKEKECLQACLDKKSENIASLGESLAMKEktiSGMKNIIAEMEQASRQSTEALIMCEQDISRMRRQLDETNDELGQI 543
Cdd:pfam12128 711 EARTEKQAYWQVVEGALDAQLALLKAAIAARR---SGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERI 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 544 ARERDILAHENDNLQEQFAkvkQENQALSKKLNDTHNELSDIKQ----KVQDTNLEVNKLKNILKSEESENRQIMEQLRK 619
Cdd:pfam12128 788 AVRRQEVLRYFDWYQETWL---QRRPRLATQLSNIERAISELQQqlarLIADTKLRRAKLEMERKASEKQQVRLSENLRG 864
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039728160 620 AneDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQMENELDS 675
Cdd:pfam12128 865 L--RCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKN 918
|
|
| PRK10361 |
PRK10361 |
DNA recombination protein RmuC; Provisional |
507-575 |
3.26e-03 |
|
DNA recombination protein RmuC; Provisional
Pssm-ID: 182409 [Multi-domain] Cd Length: 475 Bit Score: 40.74 E-value: 3.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039728160 507 EMEQASRQSTEALImceqdiSRMRRQLD----ETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKL 575
Cdd:PRK10361 129 RVDEQNRQSLNSLL------SPLREQLDgfrrQVQDSFGKEAQERHTLAHEIRNLQQLNAQMAQEAINLTRAL 195
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
554-764 |
3.90e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 554 NDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTnlevnKLKNILKSEESENRQIMEQLRKANEDAENWENKARQ 633
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEF-----RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 634 TEAENNTLKLEL---------ITAEAEGNRLKEKVDALNREVEQMENELDSARSEIELLRSQMTNERISMQNLEALLVAN 704
Cdd:COG3206 238 AEARLAALRAQLgsgpdalpeLLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 705 RDKEYQsqiALQEKESEIQLLKEHLclaENKMAIQSRDVAQFRnvvtQLEADLDITKRQL 764
Cdd:COG3206 318 LEAELE---ALQAREASLQAQLAQL---EARLAELPELEAELR----RLEREVEVARELY 367
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
539-707 |
5.18e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 539 ELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKseesENRQIMEQLR 618
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK----KYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 619 KANEdaenwenkARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQMENELDSARSEIELLRSQMTNERISMQNLE 698
Cdd:COG1579 87 NNKE--------YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
....*....
gi 1039728160 699 ALLVANRDK 707
Cdd:COG1579 159 EELEAEREE 167
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
484-723 |
5.52e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 484 IASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQDISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAK 563
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 564 VKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKARQTEAENNTLKL 643
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 644 ELITAEAEGNRLKEKVDALNREVEQMENELDSARSEIELLRSQMTNERISMQNLEALLVANRDKEYQSQIALQEKESEIQ 723
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
63-681 |
5.70e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 63 TLKLQIEDLKQTNHDLEEYVRKLLDSKEAVSTQVDDLANhnehlckeliKLDQLAEKLQKEKNfvvdtadkELEEAKIEL 142
Cdd:TIGR04523 215 SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQT----------QLNQLKDEQNKIKK--------QLSEKQKEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 143 ICQQNNITVLEDTIQRLKSIILETEKAQNtspsrldsfvktleadrdyykteaQNLRKMMRnrsksprrpsptsraancd 222
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNNQKE------------------------QDWNKELK------------------- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 223 vELLKSTARDREELKCMLEKYERHLAEIQGNVKVLTSERDKTFLLYEQAQEEIARLRREmmksckspksttahaiLRRVE 302
Cdd:TIGR04523 314 -SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNE----------------IEKLK 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 303 TERDVAFTDLRRMTTERDSLRERLKIAQEtafnEKAHLEQRIEELECTVHNLDDERMEQMANMTLMKETITTVEKEMKSL 382
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQNQEK----LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 383 ARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGAT 462
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 463 LNDLAKEKECLQACLDKKSENI--ASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQDISRMRRQLDETNDEL 540
Cdd:TIGR04523 533 KKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 541 gqiarerdilahenDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKA 620
Cdd:TIGR04523 613 --------------SSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDI 678
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039728160 621 NEDAENWENKARQTEAENNTLKLElITAEAEGNRLKEKVDALNREVEQMENELDSARSEIE 681
Cdd:TIGR04523 679 IELMKDWLKELSLHYKKYITRMIR-IKDLPKLEEKYKEIEKELKKLDEFSKELENIIKNFN 738
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
311-511 |
7.82e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.36 E-value: 7.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 311 DLRRMTTERDSLRERLKIAQETAFNEKAHLEQRIEELECTVHNLDDErmeqmanmtlmketITTVEKEMKSLARKAMDTE 390
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE--------------LAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 391 SELGRQKAE-NNSLRLLYENTE----------KDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISIL 459
Cdd:COG4942 97 AELEAQKEElAELLRALYRLGRqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039728160 460 GATLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQA 511
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
226-399 |
8.24e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.36 E-value: 8.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 226 LKSTARDREELKCMLEKYERHLAEIQGNVKVLTSERDKTFLLYEQAQEEIARLRREMMKSCKSPK------STTAHAILR 299
Cdd:COG4942 57 LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPlalllsPEDFLDAVR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728160 300 RVETERDVAFTDLRRMTTERDSLrERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMANMTLMKETITTVEKEM 379
Cdd:COG4942 137 RLQYLKYLAPARREQAEELRADL-AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
170 180
....*....|....*....|
gi 1039728160 380 KSLARKAMDTESELGRQKAE 399
Cdd:COG4942 216 AELQQEAEELEALIARLEAE 235
|
|
| |
