|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
135-467 |
3.06e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.55 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 135 NEKAHLEQRIEELECTVHNLDDERMEQMANMTLMKETITTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDL 214
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 215 SDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGATLNDLAKEKECLQACLDKKSENIASLGESLAMK 294
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 295 EKTISGMKNIIAEMEQASRQSTEALIMCEQDISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKK 374
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 375 LNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQL-RKANEDAENWENKARQTEAENNTLKLELITAEAEGN 453
Cdd:TIGR02168 917 LEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALeNKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYE 996
|
330
....*....|....
gi 1039728166 454 RLKEKVDALNREVE 467
Cdd:TIGR02168 997 ELKERYDFLTAQKE 1010
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
117-680 |
2.20e-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: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 117 TERDSLRERLKIAQETAFNEKAHLEQRIEELECTVHNLDDErmeqmanmtlMKETITTVEKEMKSLARKAMDTESELGRQ 196
Cdd:pfam15921 292 SQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSE----------LREAKRMYEDKIEELEKQLVLANSELTEA 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 197 KAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEK-------IDNFTRQNIAQREEISILGATLNDLAKE 269
Cdd:pfam15921 362 RTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 270 ----KECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEM--EQASRQSTEALIM-CEQDISRMRRQLDETNDELGQ 342
Cdd:pfam15921 442 cqgqMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtaKKMTLESSERTVSdLTASLQEKERAIEATNAEITK 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 343 IARERDILAHENDNLQ---EQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRK 419
Cdd:pfam15921 522 LRSRVDLKLQELQHLKnegDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEIND 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 420 ANEDAENW-------ENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQHLNAERSYKSQIATLHKSLV---- 488
Cdd:pfam15921 602 RRLELQEFkilkdkkDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEvlkr 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 489 -------KMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMMENELDSARSEIELLRSQMTNer 561
Cdd:pfam15921 682 nfrnkseEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTN-- 759
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 562 ismqnleallvANRDKEYqsqiaLQEKESEIQLLKEHLCLAENKMA----IQSRDVAQFRNVVTQLEADLDITKRQLG-- 635
Cdd:pfam15921 760 -----------ANKEKHF-----LKEEKNKLSQELSTVATEKNKMAgeleVLRSQERRLKEKVANMEVALDKASLQFAec 823
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039728166 636 ---TERFERERA---------VQELRRQNYSSNAynlgPMKPN-TKCHSPERAHHRSP 680
Cdd:pfam15921 824 qdiIQRQEQESVrlklqhtldVKELQGPGYTSNS----SMKPRlLQPASFTRTHSNVP 877
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
255-568 |
2.55e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.47 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 255 EISILGATLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQDISRMRRQLd 334
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 335 etndelgQIARERDilahenDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIM 414
Cdd:TIGR02168 305 -------QILRERL------ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 415 EQLRKANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQHlnaersyksqiatlhkslvkmEEEL 494
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL---------------------LKKL 430
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039728166 495 QKVQFEKVSalADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMMENELDSARSEIELLRSQMTNERISMQNLE 568
Cdd:TIGR02168 431 EEAELKELQ--AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
74-402 |
1.32e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 74 EIARLRREMmksckspksTTAHAILRRVETERDVAFTDLRRMTTERDSLR---ERLKIAQETAFNEKAHLEQRIEELECT 150
Cdd:TIGR02168 678 EIEELEEKI---------EELEEKIAELEKALAELRKELEELEEELEQLRkelEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 151 VHNLDDERMEQMANMTLMKETITTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQL 230
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 231 TQEKIMCLDEKIDNFTRQNIAQREEISILGATLNDLAKEKECLQACLDKKSENIASLGESLAMKEKtisgmkniiaEMEQ 310
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS----------ELEE 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 311 ASRQSTEAlimcEQDISRMRRQLDETNDELGQIARERDILAHENDNLQEQFA-KVKQENQALSKKLNDTHNELSDIKQKV 389
Cdd:TIGR02168 899 LSEELREL----ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEEEARRRL 974
|
330
....*....|...
gi 1039728166 390 QDTNLEVNKLKNI 402
Cdd:TIGR02168 975 KRLENKIKELGPV 987
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
110-657 |
1.48e-11 |
|
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: 67.84 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 110 TDLRRMTTERDSL---RERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMANMTLMKETITTVEKEMKSLArka 186
Cdd:pfam15921 117 TKLQEMQMERDAMadiRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIL--- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 187 MDTESELGRQKAENNSLRLL-YENTEKDLSDTQRHLAKK---------KYELQL------TQEKIMCLDEKIDNFTRQNI 250
Cdd:pfam15921 194 VDFEEASGKKIYEHDSMSTMhFRSLGSAISKILRELDTEisylkgrifPVEDQLealkseSQNKIELLLQQHQDRIEQLI 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 251 AQRE-EISILGATLNDLAKEKECLQACLDKKSENIASLGeslAMKEKTISGMKNIIAEMEQASRqstEALIMCEQDISRM 329
Cdd:pfam15921 274 SEHEvEITGLTEKASSARSQANSIQSQLEIIQEQARNQN---SMYMRQLSDLESTVSQLRSELR---EAKRMYEDKIEEL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 330 RRQLDETNDELGQIARERDILAHENDNLQEQFAKV------KQENQALSKKLN------DTHNELS--DIKQKVQDTNLE 395
Cdd:pfam15921 348 EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLladlhkREKELSLEKEQNkrlwdrDTGNSITidHLRRELDDRNME 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 396 VNKLKNILKSEESENRQIMEQ----LRKANEDAENWENKARQTEAENNTLK--LELITAEAEGNRLKEK-VDALNREVEQ 468
Cdd:pfam15921 428 VQRLEALLKAMKSECQGQMERqmaaIQGKNESLEKVSSLTAQLESTKEMLRkvVEELTAKKMTLESSERtVSDLTASLQE 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 469 HLNAERSYKSQIATLHKSLVKMEEELQKVQFEK---VSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMMENELDS 545
Cdd:pfam15921 508 KERAIEATNAEITKLRSRVDLKLQELQHLKNEGdhlRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGA 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 546 ARSEIELLRSQMTNERISMQNLEALlvanRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQ---------- 615
Cdd:pfam15921 588 MQVEKAQLEKEINDRRLELQEFKIL----KDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQerdqllnevk 663
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1039728166 616 -FRNVVTQLEADLDITKRQLGTERFERERAVQELRRQNYSSNA 657
Cdd:pfam15921 664 tSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQS 706
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
323-597 |
2.65e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 323 EQDISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNI 402
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 403 LKSEESENRQIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQHLNAERSYKSQIAT 482
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 483 LHKSLVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMMENELDSARSEIELLRSQMTNERI 562
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270
....*....|....*....|....*....|....*
gi 1039728166 563 SMQNLEALLVANRDKEYQSQIALQEKESEIQLLKE 597
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
323-599 |
3.12e-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: 67.00 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 323 EQDISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQdtnlevnKLKNI 402
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-------QLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 403 LKSEESENRQIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQHLNAERSYKSQIAT 482
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 483 LHKSLVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMMENELDSARSEIELLRSQMTNERI 562
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270
....*....|....*....|....*....|....*..
gi 1039728166 563 SMQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHL 599
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
361-652 |
3.55e-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: 66.62 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 361 FAKVKQENQALSKKlndthNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAEnwenkarQTEAENNT 440
Cdd:TIGR02168 663 GGSAKTNSSILERR-----REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-------ELSRQISA 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 441 LKLELITAEAEGNRLKEKVDALNREVEQHLNAERSYKSQIATLHKSLVKMEEELQKVQFEKVSALADLSSTRELCIKLDS 520
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 521 SKELLNRQLVAKDQEIEMMENELDSARSEIELLRSQMTNERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHLC 600
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1039728166 601 LAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERAVQELRRQN 652
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
339-599 |
4.31e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 4.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 339 ELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLR 418
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 419 KANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQHLNAERSYKSQIATLHKSLVKMEEELQKVQ 498
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 499 FEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMMENELDSARSEIELLRSQMTNERISMQNLEALLVANRDKE 578
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260
....*....|....*....|.
gi 1039728166 579 YQSQIALQEKESEIQLLKEHL 599
Cdd:COG1196 466 AELLEEAALLEAALAELLEEL 486
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
330-649 |
1.72e-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: 64.69 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 330 RRQLDETNDELgqiARERDILAHEN---DNLQEQfAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEvnKLKNILKSE 406
Cdd:TIGR02168 178 ERKLERTRENL---DRLEDILNELErqlKSLERQ-AEKAERYKELKAELRELELALLVLRLEELREELE--ELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 407 ESENRQIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQHLNAERSYKSQIATLHKS 486
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 487 LVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMMENELDSARSEIELLRSQMTNERISMQN 566
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 567 LEallvANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRdVAQFRNVVTQLEAdLDITKRQLGTERFERERAVQ 646
Cdd:TIGR02168 412 LE----DRRERLQQEIEELLKKLEEAELKELQAELEELEEELEEL-QEELERLEEALEE-LREELEEAEQALDAAERELA 485
|
...
gi 1039728166 647 ELR 649
Cdd:TIGR02168 486 QLQ 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
305-593 |
7.36e-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: 62.38 E-value: 7.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 305 IAEMEQASRQSTEALIMCEQDISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSD 384
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 385 IKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNR 464
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 465 EVEQHLNAER-------SYKSQIATLHKSLVKMEEELQKVQFEKVSALADLSSTRELCIKLDSS-KEL------LNRQLV 530
Cdd:TIGR02168 839 RLEDLEEQIEelsedieSLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEElRELeskrseLRRELE 918
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039728166 531 AKDQEIEMMENELDSARSEIELLRSQMTNE-RISMQNLEALLVANRDKEYQSQIALQEKESEIQ 593
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
323-652 |
1.89e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 323 EQDISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNI 402
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 403 LKSEESENRQIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQHLNAERSYKSQIAT 482
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 483 LHKSLVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMMENELDSARSEIELLRSQMTNERI 562
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 563 SMQnlEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQfrnVVTQLEADLDITKRQLGTERFERE 642
Cdd:COG1196 485 ELA--EAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAA---YEAALEAALAAALQNIVVEDDEVA 559
|
330
....*....|
gi 1039728166 643 RAVQELRRQN 652
Cdd:COG1196 560 AAAIEYLKAA 569
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
255-537 |
2.98e-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: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 255 EISILGATLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQAS-------RQSTEALIMCEQDIS 327
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELeeaqaeeYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 328 RMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDtnlEVNKLKNILKSEE 407
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE---AEAELAEAEEELE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 408 SENRQIMEQLRKANEDaenwENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQHLNAERSYKSQIATLHKSL 487
Cdd:COG1196 383 ELAEELLEALRAAAEL----AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1039728166 488 VKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIE 537
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
66-650 |
5.07e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 5.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 66 LLYEQAQEEIARLRREMMKSckspksTTAHAILRRVETERDVAFTDLRRMTTERDSLRERLKIAQETAFNEKAHLEQRIE 145
Cdd:TIGR02168 232 LRLEELREELEELQEELKEA------EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 146 ELectvhnldDERMEQmanmtlmketittVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKK 225
Cdd:TIGR02168 306 IL--------RERLAN-------------LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 226 YELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGATLNDLAKEKECLQACLDKKSENIASLGESLAMKEK-----TISG 300
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkelqaELEE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 301 MKNIIAEMEQASRQSTEALIMCEQDISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSkKLNDTHN 380
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS-GLSGILG 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 381 ELSDI------------------KQKVQDTNLE-VNKLKNILKSEESENRQIMEQLRKANEDAENWENKARQTEAENNTL 441
Cdd:TIGR02168 524 VLSELisvdegyeaaieaalggrLQAVVVENLNaAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGV 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 442 KLELITAE--------------------AEGNRLKEKVDALNREV-----------------EQHLNAERSYKSQIATLH 484
Cdd:TIGR02168 604 AKDLVKFDpklrkalsyllggvlvvddlDNALELAKKLRPGYRIVtldgdlvrpggvitggsAKTNSSILERRREIEELE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 485 KSLVKMEEELQkvqfEKVSALADLSSTRELcikLDSSKELLNRQLVAKDQEIEMMENELDSARSEIELLRSQMTNERISM 564
Cdd:TIGR02168 684 EKIEELEEKIA----ELEKALAELRKELEE---LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 565 QNLEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERA 644
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
....*.
gi 1039728166 645 VQELRR 650
Cdd:TIGR02168 837 ERRLED 842
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
26-642 |
3.60e-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: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 26 LKSTARDREELKCMLEKYERHLAEIQGNVKVLTSERDKTFLLYEQAQEEIA--RLRREMMKSCKSPKSTTAHAILRRVEt 103
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEeeRKRRDKLTEEYAELKEELEDLRAELE- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 104 ERDVAFTDLRRmttERDSLRERLkiaqETAFNEKAHLEQRIEELECTVHNLDDERMEQMANMTLMKETITTVEKEMKSLA 183
Cdd:TIGR02169 375 EVDKEFAETRD---ELKDYREKL----EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 184 RKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGATL 263
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTV 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 264 NDLAKEKECLQACLD----KKSENIASLGESLA------MKEKTISGMK----NIIAEMEQASRQSTEA--------LIM 321
Cdd:TIGR02169 528 AQLGSVGERYATAIEvaagNRLNNVVVEDDAVAkeaielLKRRKAGRATflplNKMRDERRDLSILSEDgvigfavdLVE 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 322 CE-----------------QDISRMRRQLD---------ETNDELGQI---ARERDILAHENDNLQEQFAKVKQENQALS 372
Cdd:TIGR02169 608 FDpkyepafkyvfgdtlvvEDIEAARRLMGkyrmvtlegELFEKSGAMtggSRAPRGGILFSRSEPAELQRLRERLEGLK 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 373 KKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAEG 452
Cdd:TIGR02169 688 RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARI 767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 453 NRLKEKVDALNREVEqhlNAERSY-KSQIATLHKSLVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVA 531
Cdd:TIGR02169 768 EELEEDLHKLEEALN---DLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID 844
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 532 KDQEIEMMENELDSARSEIELLRSQMTNERISMQNLEALL------VANRDKEY-QSQIALQEKESEIQLLKEHLCLAEN 604
Cdd:TIGR02169 845 LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLgdlkkeRDELEAQLrELERKIEELEAQIEKKRKRLSELKA 924
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1039728166 605 KMAIQSRDVAQFRNVVTQL----EADLDITKRQLGTERFERE 642
Cdd:TIGR02169 925 KLEALEEELSEIEDPKGEDeeipEEELSLEDVQAELQRVEEE 966
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
90-641 |
6.00e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.20 E-value: 6.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 90 KSTTAHAILRRVETERDVAFTDLRRMTTERDSLRERLKIAQETaFNEKAHLEQRIEELECTVHNLDDERMEQMANMTLMK 169
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEV-LEEHEERREELETLEAEIEDLRETIAETEREREELA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 170 ETITTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQN 249
Cdd:PRK02224 279 EEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 250 IAQREEISILGATLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQDISRM 329
Cdd:PRK02224 359 EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTA 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 330 RRQLDETN---------------------DELGQIARERDILAHENDNLQEQFAKVKQENQALsKKLNDTHNELSDIKQK 388
Cdd:PRK02224 439 RERVEEAEalleagkcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEER 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 389 VQDtnleVNKLKNILKSEESENRQIMEQLRkanEDAENWENKARQTEAENNtlkleliTAEAEGNRLKEKVDALNREVEQ 468
Cdd:PRK02224 518 RED----LEELIAERRETIEEKRERAEELR---ERAAELEAEAEEKREAAA-------EAEEEAEEAREEVAELNSKLAE 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 469 hLNAERSYKSQIATLHKSLVKMEEELQKVQfEKVSALADLSstrelciklDSSKEllnrQLVAKDQEIEMMENELDSARs 548
Cdd:PRK02224 584 -LKERIESLERIRTLLAAIADAEDEIERLR-EKREALAELN---------DERRE----RLAEKRERKRELEAEFDEAR- 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 549 eIELLRSQMTNERISMQNLEALLVANRDKEYQSQIALQEKESEIQ----LLKEHLCLAENKMAIQS--RDVAQFRNVVTQ 622
Cdd:PRK02224 648 -IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEeleeLRERREALENRVEALEAlyDEAEELESMYGD 726
|
570
....*....|....*....
gi 1039728166 623 LEADLditkRQLGTERFER 641
Cdd:PRK02224 727 LRAEL----RQRNVETLER 741
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
178-451 |
1.65e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 178 EMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEIS 257
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 258 ILGATLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQDISRMRRQLDETN 337
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 338 DELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKlkniLKSEESENRQIMEQL 417
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE----LEEEEEALLELLAEL 468
|
250 260 270
....*....|....*....|....*....|....
gi 1039728166 418 RKANEDAENWENKARQTEAENNTLKLELITAEAE 451
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
208-437 |
1.67e-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: 54.00 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 208 ENTEKDLSDTQRHLAKKKYELQLTQEKIMC-------LDEKIDNFTRQNIAQREEISILGATLNDLAKEKECLQACLDKK 280
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKAllkqlaaLERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 281 SENIASLgeslamkektisgmkniIAEMEQASRQSTEALIMCEQDISRMRRQLdetnDELGQIARERDILAHENDNLQEQ 360
Cdd:COG4942 103 KEELAEL-----------------LRALYRLGRQPPLALLLSPEDFLDAVRRL----QYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039728166 361 FAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKARQTEAE 437
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
266-556 |
2.33e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 266 LAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALI-MCEQDISRMRRQLDETNdelGQIA 344
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdLGEEEQLRVKEKIGELE---AEIA 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 345 RERDILAHENDNLQEQFAKVKQENQALSKKLNdthnELSDIKQKVQDTNLEVNKLKNILKSEESEnrqiMEQLRkaneda 424
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLAKLEAEIDKLLA----EIEELEREIEEERKRRDKLTEEYAELKEE----LEDLR------ 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 425 enweNKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQHLNAERSYKSQIATLHKSLVKMEEELQKVQFEKVSA 504
Cdd:TIGR02169 371 ----AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK 446
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1039728166 505 LADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMMENELDSARSEIELLRSQ 556
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
136-507 |
4.68e-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: 4.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 136 EKAHLEQRIEELECTVHNLDDERMEQmanmtlmketittvEKEMKSLARKAMDTESELGRQKAENNSLrllyentEKDLS 215
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRI--------------ENRLDELSQELSDASRKIGEIEKEIEQL-------EQEEE 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 216 DTQRHLAKKKYELQLTQEKIMCLDEKIDnftrqniaqreeisilgatlnDLAKEKECLQACLDKKSENIASLGESLAMke 295
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELK---------------------ELEARIEELEEDLHKLEEALNDLEARLSH-- 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 296 ktiSGMKNIIAEMEQAsrqstealimcEQDISRMRRQLDETNDELGQIARERDILAHENDNLQEQfakvkqenqalskkL 375
Cdd:TIGR02169 791 ---SRIPEIQAELSKL-----------EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ--------------R 842
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 376 NDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAEGNRL 455
Cdd:TIGR02169 843 IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1039728166 456 KEKVDALNREVEQHLNAERSYKSQIATLhKSLVKMEEELQKVQfEKVSALAD 507
Cdd:TIGR02169 923 KAKLEALEEELSEIEDPKGEDEEIPEEE-LSLEDVQAELQRVE-EEIRALEP 972
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
69-419 |
8.22e-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: 52.76 E-value: 8.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 69 EQAQEEIARLRREMmkSCKSPKSTTAHAILRRVETERDVAFTDLRRMTTERDSLRERLKIAQETAFN---EKAHLEQRIE 145
Cdd:TIGR02169 691 SSLQSELRRIENRL--DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvksELKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 146 ELECTVHNLddermeqmanmtlmketittvEKEMKSLarKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKK 225
Cdd:TIGR02169 769 ELEEDLHKL---------------------EEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 226 YELQLtqekimcLDEKIDNFTRQNIAQREEISILGATLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNII 305
Cdd:TIGR02169 826 LEKEY-------LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 306 AEMEQASRQSTEALIMCEQDISRMRRQLDETNDELGQIARE--RDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELS 383
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPkgEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAI 978
|
330 340 350
....*....|....*....|....*....|....*.
gi 1039728166 384 DIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRK 419
Cdd:TIGR02169 979 QEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
31-350 |
9.50e-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: 52.38 E-value: 9.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 31 RDREELKCMLEKYERHLAEIQGNVKVLTSERDKTfLLYEQAQEEiarlRREMMKSCKSPKSTTAHAILRRVETERDVAFT 110
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKA-ERYQALLKE----KREYEGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 111 DLRRMTTERDSLRERLkiaqetafnekAHLEQRIEELECTVHNLDDERMEQM--------ANMTLMKETITTVEKEMKSL 182
Cdd:TIGR02169 252 ELEKLTEEISELEKRL-----------EEIEQLLEELNKKIKDLGEEEQLRVkekigeleAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 183 ARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGAT 262
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 263 LNDLAKEKECLQACLDKKSENIASLGESLAMKE----KTISGMKNIIAEMEQASR---QSTEALIMCEQDISRMRRQLDE 335
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEakinELEEEKEDKALEIKKQEWkleQLAADLSKYEQELYDLKEEYDR 480
|
330
....*....|....*
gi 1039728166 336 TNDELGQIARERDIL 350
Cdd:TIGR02169 481 VEKELSKLQRELAEA 495
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
142-599 |
1.47e-06 |
|
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: 51.56 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 142 QRIEELECTVHNLDDERMEQMANMTLMKETITTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHL 221
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 222 AKKKYELQLTQEKIM---CLDEKIDNFTRQNI--------------AQREEISILGATLNDLAKEKECLQACLDKKSENI 284
Cdd:TIGR04523 197 LKLELLLSNLKKKIQknkSLESQISELKKQNNqlkdniekkqqeinEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 285 ASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALImcEQDISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKV 364
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKEL--KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNS 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 365 KQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKARQTEAENNTLKLE 444
Cdd:TIGR04523 355 ESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 445 LITAEAEGNRLKEKVDALNREVEQHLNAERSYKSQIATLHKSLVKMEEELQKVQFE---KVSALADL------------- 508
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKElksKEKELKKLneekkeleekvkd 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 509 -----SSTRELCIKLDSSKELLNRQLVAKDQEIEMMENELDSARSEIELLRSQMTNERISmQNLEALLVANRDKeyqsQI 583
Cdd:TIGR04523 515 ltkkiSSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELK-QTQKSLKKKQEEK----QE 589
|
490
....*....|....*.
gi 1039728166 584 ALQEKESEIQLLKEHL 599
Cdd:TIGR04523 590 LIDQKEKEKKDLIKEI 605
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
207-643 |
7.08e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 7.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 207 YENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGATLNDLAKEKECLQAC---LDKKSEN 283
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEvkeLEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 284 IASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQDISR-------------MRRQLDETNDELGQIARERDIL 350
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkelkekaeeyikLSEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 351 AHENDNLQEQFAKV---KQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNIlksEESENRQIMEQLRKANEDAENW 427
Cdd:PRK03918 320 EEEINGIEERIKELeekEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL---ERLKKRLTGLTPEKLEKELEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 428 ENKARQTEAENNTLKLELITAEAEGNRLKEKVDAL----------NREVEQHLNAE--RSYKSQIATLHKSLVKMEEELQ 495
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELkkakgkcpvcGRELTEEHRKEllEEYTAELKRIEKELKEIEEKER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 496 KVQFEKVSALADLSSTRELCIKLDSSKELLN----------RQLVAKDQEIEMMENELDSARSEIELLRSQMTNERISMQ 565
Cdd:PRK03918 477 KLRKELRELEKVLKKESELIKLKELAEQLKEleeklkkynlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 566 NLEALLVANRDKE-------------------------------YQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVA 614
Cdd:PRK03918 557 KLAELEKKLDELEeelaellkeleelgfesveeleerlkelepfYNEYLELKDAEKELEREEKELKKLEEELDKAFEELA 636
|
490 500
....*....|....*....|....*....
gi 1039728166 615 QFRNVVTQLEADLDITKRQLGTERFERER 643
Cdd:PRK03918 637 ETEKRLEELRKELEELEKKYSEEEYEELR 665
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
31-597 |
7.18e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 7.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 31 RDREELKCMLEKYERHLAEIQGNVKVLTSERDKTFLLYEQAQEEIARLRREmmksckspksttahaiLRRVETERDVAFT 110
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE----------------LEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 111 DLRRMTTERDSLRERLKIAQEtafnEKAHLEQRIEELECTVHNLDDERMEQMANMTLMKETITTVEKEMKSLARKAMDTE 190
Cdd:COG1196 289 EEYELLAELARLEQDIARLEE----RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 191 SELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGATLNDLAKEK 270
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 271 ECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMcEQDISRMRRQLDETNDELGQIARERDIL 350
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL-LLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 351 AHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQD----------TNLEVNKLKNILKSEESENRQIMEQLRKA 420
Cdd:COG1196 524 GAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEylkaakagraTFLPLDKIRARAALAAALARGAIGAAVDL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 421 NEDAENWENKARQTEAenNTLKLELITAEAEGNRLKEKVDALNREVEQHLNAERSYKSQIATLHKSLVKMEEELQKVQFE 500
Cdd:COG1196 604 VASDLREADARYYVLG--DTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 501 KVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMMENELDSARSEIELLRSQMTNERISMQNLEALLVANRDKEYQ 580
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
570
....*....|....*..
gi 1039728166 581 sqiaLQEKESEIQLLKE 597
Cdd:COG1196 762 ----LEELERELERLER 774
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
323-512 |
1.06e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 323 EQDISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNI 402
Cdd:COG3883 29 QAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 403 LKSEE---------------SENRQIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVE 467
Cdd:COG3883 109 LGSESfsdfldrlsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLS 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039728166 468 QhlnAERSYKSQIATLHKSLVKMEEELQKVQFEKVSALADLSSTR 512
Cdd:COG3883 189 A---EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
211-440 |
1.19e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 211 EKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGATLNDLAKEKECLQACLDKKSENIASLGES 290
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 291 LAMKEKTISGMKNIIaemeqaSRQSTEALImceQDISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQA 370
Cdd:COG3883 95 LYRSGGSVSYLDVLL------GSESFSDFL---DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 371 LSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKARQTEAENNT 440
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
281-498 |
2.28e-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: 47.07 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 281 SENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQDISRMRRQLDETNDELGQIARERDILAHENDNLQEQ 360
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 361 FAKVKQENQALSKKL--NDTHNELSDIKQkvQDTNLEVNKLKNILKSEESENRQIMEQLRkanEDAENWENKARQTEAEN 438
Cdd:COG4942 99 LEAQKEELAELLRALyrLGRQPPLALLLS--PEDFLDAVRRLQYLKYLAPARREQAEELR---ADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 439 NTLKLELITAEAEGNRLKEKVDALNREVEQHLNAERSYKSQIATLHKSLVKMEEELQKVQ 498
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
251-451 |
2.70e-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: 47.07 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 251 AQREEISILGATLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQDISRMR 330
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 331 RQLDETNDELG-------------------------QIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDI 385
Cdd:COG4942 97 AELEAQKEELAellralyrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039728166 386 KQKVQdtnlEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAE 451
Cdd:COG4942 177 EALLA----ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
380-599 |
3.41e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 380 NELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKV 459
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 460 DALNREVEQHLNAerSYKSQIATLHKSLVKMEEELQkvqfeKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMM 539
Cdd:COG4942 100 EAQKEELAELLRA--LYRLGRQPPLALLLSPEDFLD-----AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 540 ENELDSARSEIELLRSQMTNERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHL 599
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
369-559 |
7.45e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 369 QALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQimEQLRKANEDAEnwENKARQTEAENNTLKLELITA 448
Cdd:COG4913 258 RELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELR--AELARLEAELE--RLEARLDALREELDELEAQIR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 449 EAEGNR---LKEKVDALNREVEQHLNAERSYKSQIATLHKSLVKMEEELQKVQFEKVSALADLSSTRelcikldsskELL 525
Cdd:COG4913 334 GNGGDRleqLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL----------EAL 403
|
170 180 190
....*....|....*....|....*....|....
gi 1039728166 526 NRQLVAKDQEIEMMENELDSARSEIELLRSQMTN 559
Cdd:COG4913 404 EEALAEAEAALRDLRRELRELEAEIASLERRKSN 437
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
26-513 |
3.63e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 26 LKSTARDREELKCMLEKYERHLAEIQGNVKVLTSERDKTFLLYEQAQEEIARLRREMmksckSPKSTTAHAILRRVETER 105
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL-----AEAEEELEELAEELLEAL 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 106 DVAF------TDLRRMTTERDSLRERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMANMTLMKETITTVEKEM 179
Cdd:COG1196 393 RAAAelaaqlEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 180 KSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDnftRQNIAQREEISIL 259
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY---EAALEAALAAALQ 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 260 GATLNDLAKEKECLQAcLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQDISRMRRQLDETNDE 339
Cdd:COG1196 550 NIVVEDDEVAAAAIEY-LKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLV 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 340 LGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRK 419
Cdd:COG1196 629 AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE 708
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 420 ANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQHLNAERSYKSQIATLHKSLVKM-------EE 492
Cdd:COG1196 709 LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnllaIE 788
|
490 500
....*....|....*....|....
gi 1039728166 493 ELQKVQFEK---VSALADLSSTRE 513
Cdd:COG1196 789 EYEELEERYdflSEQREDLEEARE 812
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
326-659 |
3.69e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 326 ISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKS 405
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 406 EESENRQIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQHLNAERSYKSQIATLHK 485
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 486 SLVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMMENELDSARSEIELlrsqmtNERISMQ 565
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL------EEVILKE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 566 NLEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERAV 645
Cdd:COG4372 260 IEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAEL 339
|
330
....*....|....
gi 1039728166 646 QELRRQNYSSNAYN 659
Cdd:COG4372 340 ADLLQLLLVGLLDN 353
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
173-374 |
7.34e-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: 42.49 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 173 TTVEKEMKSLARKAMDTESELgrqKAENNSLRLLYENTEKDLSDTQRHlakkkyeLQLTQEKIMCLDEKIDNFTRQNIAQ 252
Cdd:pfam15905 148 DGTQKKMSSLSMELMKLRNKL---EAKMKEVMAKQEGMEGKLQVTQKN-------LEHSKGKVAQLEEKLVSTEKEKIEE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 253 REEISILGATLndlaKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEalimceqDISRMRRQ 332
Cdd:pfam15905 218 KSETEKLLEYI----TELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIK-------DLNEKCKL 286
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039728166 333 LDETNDELGQIARERDI-LAHENDNLQEQFAKVKQENQALSKK 374
Cdd:pfam15905 287 LESEKEELLREYEEKEQtLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
17-649 |
8.60e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.79 E-value: 8.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 17 RAANCDVELLKSTARDREELKCMLEKYERHLAEIQGNVKVLTSE--------RDKTFLLYEQAQ-----EEIARLRREMM 83
Cdd:pfam05483 205 QAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQitekenkmKDLTFLLEESRDkanqlEEKTKLQDENL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 84 KSCKSPKsttaHAILRRVEterDVAFTDLRRMTTERdSLRERLKIAQETAFnekahleQRIEELECTVHNLDDERMEQMA 163
Cdd:pfam05483 285 KELIEKK----DHLTKELE---DIKMSLQRSMSTQK-ALEEDLQIATKTIC-------QLTEEKEAQMEELNKAKAAHSF 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 164 NMTLMKETITTVEKEMKSLARKamdteselgrqkaennslrllYENTEKDLSDTQRHLAKKKYELqltqekimcldEKID 243
Cdd:pfam05483 350 VVTEFEATTCSLEELLRTEQQR---------------------LEKNEDQLKIITMELQKKSSEL-----------EEMT 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 244 NFTRQNIAQREEISILGATLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMkniiaEMEQASRQSTEALIMce 323
Cdd:pfam05483 398 KFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDL-----EIQLTAIKTSEEHYL-- 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 324 QDISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNIL 403
Cdd:pfam05483 471 KEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDEL 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 404 KSEESENRQIMEQLR-KANEDAENwenkARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQHLNAERSYKSQIAT 482
Cdd:pfam05483 551 ESVREEFIQKGDEVKcKLDKSEEN----ARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSA 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 483 LHKSLVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMMENELDSARSEIELLRSQMTNERI 562
Cdd:pfam05483 627 ENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMV 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 563 SMQnleallvanRDKEYQSQIALQEKESEIQLLKehlclaeNKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERE 642
Cdd:pfam05483 707 ALM---------EKHKHQYDKIIEERDSELGLYK-------NKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKE 770
|
....*..
gi 1039728166 643 RAVQELR 649
Cdd:pfam05483 771 KLKMEAK 777
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
112-467 |
8.90e-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: 42.65 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 112 LRRMTTERDSLRERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQmanmtlmketITTVEKEMKSLARKAMDTES 191
Cdd:pfam02463 175 LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEE----------YLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 192 ELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGATLNDLAKEKE 271
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 272 CLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQDISRMRRQLDETNDELGQIARERDILA 351
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 352 HENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKA 431
Cdd:pfam02463 405 KEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQE 484
|
330 340 350
....*....|....*....|....*....|....*.
gi 1039728166 432 RQTEAENNTLKLELITAEAEGNRLKEKVDALNREVE 467
Cdd:pfam02463 485 QLELLLSRQKLEERSQKESKARSGLKVLLALIKDGV 520
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
456-584 |
9.25e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 456 KEKV-DALNREVEQ---HLNAERSYKSQiatlhkslvkMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVA 531
Cdd:PRK09039 51 KDSAlDRLNSQIAEladLLSLERQGNQD----------LQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGE 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1039728166 532 KDQEIEMMENELDSARSEIELLRSQMTNERISMQNLEALLVA--NRDKEYQSQIA 584
Cdd:PRK09039 121 LAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDAseKRDRESQAKIA 175
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
112-442 |
1.02e-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: 42.31 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 112 LRRMTTERDSLRERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMANMTLMKETITTVEKEMKSLARKAMDTES 191
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 192 ELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGATLNDLAKEKE 271
Cdd:TIGR04523 441 EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 272 CLQacldkksENIASLGESLAMKEKTISGMKNIIAEMEQasrqstealimcEQDISRMRRQLDETNDELGQIARERDILA 351
Cdd:TIGR04523 521 SLK-------EKIEKLESEKKEKESKISDLEDELNKDDF------------ELKKENLEKEIDEKNKEIEELKQTQKSLK 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 352 HENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKA 431
Cdd:TIGR04523 582 KKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKW 661
|
330
....*....|.
gi 1039728166 432 RQTEAENNTLK 442
Cdd:TIGR04523 662 PEIIKKIKESK 672
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
135-346 |
1.11e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 135 NEKAHLEQRIEELECTVHNLDDERMEQMANMTLMKETITTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDL 214
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 215 SDTQRHLAKKKYELQ-----------LTQEKIMCLDEKIDNFTRQNIAQREEISILGATLNDLAKEKECLQACLDKKSEN 283
Cdd:COG4942 100 EAQKEELAELLRALYrlgrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039728166 284 IASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQDISRMRRQLDETNDELGQIARE 346
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
15-271 |
1.49e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 15 TSRAANCDVELLKSTARdREELKCMLEKYERHLAEIQGNVKVLTSERDKTFLLYEQAQEEIARLRREMmkscKSPKSTTA 94
Cdd:TIGR02168 746 EERIAQLSKELTELEAE-IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL----TLLNEEAA 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 95 HAILRRVETERDVAftDLRRMTTERDSLRERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMANMTLMKETITT 174
Cdd:TIGR02168 821 NLRERLESLERRIA--ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 175 VEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQ---------------RHLAKKKYELQLTQEKIMCLD 239
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQerlseeysltleeaeALENKIEDDEEEARRRLKRLE 978
|
250 260 270
....*....|....*....|....*....|..
gi 1039728166 240 EKIDNFTRQNIAQREEISILGATLNDLAKEKE 271
Cdd:TIGR02168 979 NKIKELGPVNLAAIEEYEELKERYDFLTAQKE 1010
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
477-651 |
1.54e-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: 41.29 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 477 KSQIATLHKSLVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMMENELDSARSEIELLRSQ 556
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 557 M-----TNERISMQNLEALLV-------ANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRdvaqfRNVVTQLE 624
Cdd:COG4942 106 LaellrALYRLGRQPPLALLLspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE-----RAELEALL 180
|
170 180
....*....|....*....|....*..
gi 1039728166 625 ADLDITKRQLGTERFERERAVQELRRQ 651
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKE 207
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
395-599 |
1.57e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 395 EVNKLKNILKSEESENRQIMEQLRKANEDAENW-ENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQhlnae 473
Cdd:TIGR02169 181 EVEENIERLDLIIDEKRQQLERLRREREKAERYqALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEK----- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 474 rsYKSQIATLHKSLVKMEEELQKVQfEKVSALADLSSTR--ELCIKLDSSKELLNRQLVAKDQEIEMMEN-------ELD 544
Cdd:TIGR02169 256 --LTEEISELEKRLEEIEQLLEELN-KKIKDLGEEEQLRvkEKIGELEAEIASLERSIAEKERELEDAEErlakleaEID 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039728166 545 SARSEIELLRSQMTNERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHL 599
Cdd:TIGR02169 333 KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
395-573 |
2.77e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 395 EVNKLKNILKSEESENRQIMEQLRKANEDAENWENKARQTEAENNTLK--LELITAEAEGNRLKEKVDALNREVEQHLNA 472
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 473 ERsyksQIATLHKSLVKMEEELQKVQFEKVSALADLS-STRELCIKLDSSKELLNRQLVAKDQEIEMMENELDSARSEIE 551
Cdd:COG4717 155 LE----ELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180
....*....|....*....|..
gi 1039728166 552 LLRSQMTNERISMQNLEALLVA 573
Cdd:COG4717 231 QLENELEAAALEERLKEARLLL 252
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
192-486 |
3.06e-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: 40.98 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 192 ELGRQKAENNSLRLLYENTEKD---LSDTQRHLAKK-----KYELQLTQEKIMCLDEKIDNFTRQNIAQREEISilGATL 263
Cdd:pfam12128 633 ELEKASREETFARTALKNARLDlrrLFDEKQSEKDKknkalAERKDSANERLNSLEAQLKQLDKKHQAWLEEQK--EQKR 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 264 NDLAKEKECLQACLDKKSENIASLGESLAMKEktiSGMKNIIAEMEQASRQSTEALIMCEQDISRMRRQLDETNDELGQI 343
Cdd:pfam12128 711 EARTEKQAYWQVVEGALDAQLALLKAAIAARR---SGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERI 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 344 ARERDILAHENDNLQEQFAkvkQENQALSKKLNDTHNELSDIKQ----KVQDTNLEVNKLKNILKSEESENRQIMEQLRK 419
Cdd:pfam12128 788 AVRRQEVLRYFDWYQETWL---QRRPRLATQLSNIERAISELQQqlarLIADTKLRRAKLEMERKASEKQQVRLSENLRG 864
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039728166 420 AneDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQHLnaeRSYKSQIATLHKS 486
Cdd:pfam12128 865 L--RCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYV---EHFKNVIADHSGS 926
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
420-593 |
3.27e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 420 ANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQHLNAERSYKSQIATLHKSLVKMEEELQKV-- 497
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 498 -------QFEKVSALADLSSTRELCIKL-------DSSKELLNRQ------LVAKDQEIEMMENELDSARSEIELLRSQM 557
Cdd:COG3883 94 alyrsggSVSYLDVLLGSESFSDFLDRLsalskiaDADADLLEELkadkaeLEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 1039728166 558 TNERISMQNLEALLVANRDKEYQSQIALQEKESEIQ 593
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| PRK10361 |
PRK10361 |
DNA recombination protein RmuC; Provisional |
307-375 |
3.58e-03 |
|
DNA recombination protein RmuC; Provisional
Pssm-ID: 182409 [Multi-domain] Cd Length: 475 Bit Score: 40.35 E-value: 3.58e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039728166 307 EMEQASRQSTEALImceqdiSRMRRQLD----ETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKL 375
Cdd:PRK10361 129 RVDEQNRQSLNSLL------SPLREQLDgfrrQVQDSFGKEAQERHTLAHEIRNLQQLNAQMAQEAINLTRAL 195
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
23-504 |
3.85e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 23 VELLKSTARDREELKCMLEKYERHLAEIQGNVKVLTSERDKTFLLYEQAQEEIARLRREMMKSCKSPKSTTAHAILRRVE 102
Cdd:PRK03918 223 LEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 103 TERDVAFTD----LRRMTTERDSLRERLKIAQETA------FNEKAHLEQRIEELEcTVHNLDDERMEQMANMTLMK--- 169
Cdd:PRK03918 303 EEYLDELREiekrLSRLEEEINGIEERIKELEEKEerleelKKKLKELEKRLEELE-ERHELYEEAKAKKEELERLKkrl 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 170 --ETITTVEKEMKSLARKAMDTESELGRQKAENNSLrllyENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEK--IDNF 245
Cdd:PRK03918 382 tgLTPEKLEKELEELEKAKEEIEEEISKITARIGEL----KKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKelLEEY 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 246 TRQNIAQREEISILGATLNDLAKEKECLQACLDKKSENIA--SLGESLAMKEKTISGMKniIAEMEQASRQ---STEALI 320
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKlkELAEQLKELEEKLKKYN--LEELEKKAEEyekLKEKLI 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 321 MCEQDISRMRRQLDETND----------ELGQIARERDILAHENDNLQ-EQFAKVKQENQALsKKLNDTHNELSDIKQKV 389
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEElkkklaelekKLDELEEELAELLKELEELGfESVEELEERLKEL-EPFYNEYLELKDAEKEL 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 390 QDTNLEVNKLKNILKSEE---SENRQIMEQLRKANEDAENWENKARQTEAENNTLKL--ELITAEAEGNRLKEKVDALNR 464
Cdd:PRK03918 615 EREEKELKKLEEELDKAFeelAETEKRLEELRKELEELEKKYSEEEYEELREEYLELsrELAGLRAELEELEKRREEIKK 694
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1039728166 465 ---EVEQHLNAERSYKSQIATLHKSLVKMEEELQKVQFEKVSA 504
Cdd:PRK03918 695 tleKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALL 737
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
284-465 |
6.76e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 284 IASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQDISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAK 363
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 364 VKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKARQTEAENNTLKL 443
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
|
170 180
....*....|....*....|..
gi 1039728166 444 ELITAEAEGNRLKEKVDALNRE 465
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEK 207
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
333-615 |
7.37e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.94 E-value: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 333 LDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHN-ELSDIKQKVQDTNLEVNKLKnilkseesENR 411
Cdd:COG3096 838 LAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLlADETLADRLEELREELDAAQ--------EAQ 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 412 QIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVE--QHLNAERSYKSQIAT------L 483
Cdd:COG3096 910 AFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQrrPHFSYEDAVGLLGENsdlnekL 989
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 484 HKSLVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMMENELDSARSEiellrsqmtNERIS 563
Cdd:COG3096 990 RARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEE---------RARIR 1060
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1039728166 564 MQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQ 615
Cdd:COG3096 1061 RDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
26-199 |
8.78e-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: 38.98 E-value: 8.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 26 LKSTARDREELKCMLEKYERHLAEIQGNVKVLTSERDKTFLLYEQAQEEIARLRREMMKSCKSPK------STTAHAILR 99
Cdd:COG4942 57 LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPlalllsPEDFLDAVR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 100 RVETERDVAFTDLRRMTTERDSLrERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMANMTLMKETITTVEKEM 179
Cdd:COG4942 137 RLQYLKYLAPARREQAEELRADL-AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
170 180
....*....|....*....|
gi 1039728166 180 KSLARKAMDTESELGRQKAE 199
Cdd:COG4942 216 AELQQEAEELEALIARLEAE 235
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
172-373 |
9.61e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 9.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 172 ITTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIA 251
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728166 252 QREEISILGATLNdlakekeclqacldkkSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQDISRMRR 331
Cdd:COG3883 98 SGGSVSYLDVLLG----------------SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1039728166 332 QLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSK 373
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
|
| |
