|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
335-667 |
1.67e-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: 74.32 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 335 NEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDL 414
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 415 SD-------TQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKKSENIASL 487
Cdd:TIGR02168 757 TEleaeieeLEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 488 GESLAMKEKTISGMKNIIAEMEQASRQCTEALivceqdvSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKAKQE 567
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELI-------EELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 568 NQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQL-RKANEDAENWENKARQSEADNNTLKLELI 646
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALeNKIEDDEEEARRRLKRLENKIKELGPVNL 989
|
330 340
....*....|....*....|.
gi 1034616912 647 TAEAEGNRLKEKVDSLNREVE 667
Cdd:TIGR02168 990 AAIEEYEELKERYDFLTAQKE 1010
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
302-602 |
1.17e-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: 68.54 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 302 ETERDVAFTDLRRMTTERDSLR---ERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKE 378
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRkelEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 379 MKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISI 458
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 459 LGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKtisgmkniiaEMEQASRQCTEAlivcEQDVSRMRRQLDETND 538
Cdd:TIGR02168 857 LAAEIEELEELIEELESELEALLNERASLEEALALLRS----------ELEELSEELREL----ESKRSELRRELEELRE 922
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034616912 539 ELAQIARERDILAHDNDNLQEQFA-KAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNI 602
Cdd:TIGR02168 923 KLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPV 987
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
455-738 |
6.25e-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: 66.23 E-value: 6.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 455 EISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLd 534
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 535 etndelaQIARERDilahdnDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMM 614
Cdd:TIGR02168 305 -------QILRERL------ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 615 EQLRKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLnaERSYKSQISTLHKSVVKMEEEL 694
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL--KKLEEAELKELQAELEELEEEL 449
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1034616912 695 QKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEM 738
Cdd:TIGR02168 450 EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
310-738 |
1.29e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 58.59 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 310 TDLRRMTTERDSL---RERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLArka 386
Cdd:pfam15921 117 TKLQEMQMERDAMadiRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIL--- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 387 MDTESELGRQKAENNSLRLL-YENTEKDLSDTQRHLAKK---------KYELQL------TQEKIMCLDEKIDNFTRQNI 450
Cdd:pfam15921 194 VDFEEASGKKIYEHDSMSTMhFRSLGSAISKILRELDTEisylkgrifPVEDQLealkseSQNKIELLLQQHQDRIEQLI 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 451 AQRE-EISILGGTLNDLAKEKECLQACLDKKSENIASLGeslAMKEKTISGMKNIIAEMEQASRqctEALIVCEQDVSRM 529
Cdd:pfam15921 274 SEHEvEITGLTEKASSARSQANSIQSQLEIIQEQARNQN---SMYMRQLSDLESTVSQLRSELR---EAKRMYEDKIEEL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 530 RRQLDETNDELAQIARERDILAHDNDNLQEQFAK------AKQENQALSKKLN------DTHNEL--NDIKQKVQDTNLE 595
Cdd:pfam15921 348 EKQLVLANSELTEARTERDQFSQESGNLDDQLQKlladlhKREKELSLEKEQNkrlwdrDTGNSItiDHLRRELDDRNME 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 596 VNKLKNILKSEESENRQMMEQ----LRKANEDAENWENKARQSEADNNTLK--LELITAEAEGNRLKEK-VDSLNREVEQ 668
Cdd:pfam15921 428 VQRLEALLKAMKSECQGQMERqmaaIQGKNESLEKVSSLTAQLESTKEMLRkvVEELTAKKMTLESSERtVSDLTASLQE 507
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 669 HLNAERSYKSQISTLHKSVVKMEEELQKVQFEKvsalADLSSTRELCikldsskELLNRQLVAKDQEIEM 738
Cdd:pfam15921 508 KERAIEATNAEITKLRSRVDLKLQELQHLKNEG----DHLRNVQTEC-------EALKLQMAEKDKVIEI 566
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
378-707 |
3.07e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 378 EMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEIS 457
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 458 ILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMkektiSGMKNIIAEMEQAsrqctealivcEQDVSRMRRQLDETN 537
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLSH-----SRIPEIQAELSKL-----------EEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 538 DELAQIARERDILAHDNDNLQEQfakakqenqalskkLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQL 617
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQ--------------RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 618 RKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEqHLNAERSYKSQISTLHKSVVKMEEELQKV 697
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS-EIEDPKGEDEEIPEEELSLEDVQAELQRV 963
|
330
....*....|
gi 1034616912 698 QfEKVSALAD 707
Cdd:TIGR02169 964 E-EEIRALEP 972
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
40-701 |
4.87e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 56.67 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 40 EAENYQNTLQLEQEVRNQDRFIstLKLQIEDLKQTNHGLEEYVRKLLDSKEVVSSQVDDLTSHNEHLCKELIKIDQLAEQ 119
Cdd:pfam15921 86 QVKDLQRRLNESNELHEKQKFY--LRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKED 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 120 LEKEKNFVVDSANKELeeakidlicqqnniIVLEDTIKRLKSIILDTEKAQNKSPSRLDSFVKTleadkdHYKSEAQHLR 199
Cdd:pfam15921 164 MLEDSNTQIEQLRKMM--------------LSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTM------HFRSLGSAIS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 200 KMMRsrsksprrpsptargancdvellktttrdreELKCMLEKYERHLAEIQGNVKVLKSE-RDKIFLLYEQAQEEITRL 278
Cdd:pfam15921 224 KILR-------------------------------ELDTEISYLKGRIFPVEDQLEALKSEsQNKIELLLQQHQDRIEQL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 279 RREmmksckspksttaHAILRRVETERDVAftdlrrMTTERDSLRERLKIAQETAFNEKAHLEQRIEELECTVHNLDDEr 358
Cdd:pfam15921 273 ISE-------------HEVEITGLTEKASS------ARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSE- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 359 meqmsnmtlMKETISTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCL 438
Cdd:pfam15921 333 ---------LREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 439 DEK-------IDNFTRQNIAQREEISILGGTLNDLAKEKE---------------------CLQACLDKKSENIASLGES 490
Cdd:pfam15921 404 WDRdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQgqmerqmaaiqgkneslekvsSLTAQLESTKEMLRKVVEE 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 491 LAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDILAH---DNDNLQEQFAKAKQ- 566
Cdd:pfam15921 484 LTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNvqtECEALKLQMAEKDKv 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 567 ---------------------------ENQALSKKLNDTHNELNDIK--------------QKVQDTNLEVNKLKNI--- 602
Cdd:pfam15921 564 ieilrqqienmtqlvgqhgrtagamqvEKAQLEKEINDRRLELQEFKilkdkkdakireleARVSDLELEKVKLVNAgse 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 603 ----LKSEESENRQMMEQLRKA-------NEDAE----NWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNRE-- 665
Cdd:pfam15921 644 rlraVKDIKQERDQLLNEVKTSrnelnslSEDYEvlkrNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSdg 723
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1034616912 666 --------VEQHLNAERsykSQISTLHKSVVKMEEELQKVQFEK 701
Cdd:pfam15921 724 hamkvamgMQKQITAKR---GQIDALQSKIQFLEEAMTNANKEK 764
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
290-712 |
4.90e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 290 KSTTAHAILRRVETERDVAFTDLRRMTTERDSLRERLKIAQETaFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMK 369
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEV-LEEHEERREELETLEAEIEDLRETIAETEREREELA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 370 ETISTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNF---- 445
Cdd:PRK02224 279 EEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLeera 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 446 ----------------TRQNIAQR--------EEISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGM 501
Cdd:PRK02224 359 eelreeaaeleseleeAREAVEDRreeieeleEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTA 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 502 KNIIAEMEQ--ASRQCTEalivCEQDV--SRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKAKQenqalskkLND 577
Cdd:PRK02224 439 RERVEEAEAllEAGKCPE----CGQPVegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED--------LVE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 578 THNELNDIKQKVQDtnleVNKLKNILKSEESENRQMMEQLRkanEDAENWENKARQSEADNNtlkleliTAEAEGNRLKE 657
Cdd:PRK02224 507 AEDRIERLEERRED----LEELIAERRETIEEKRERAEELR---ERAAELEAEAEEKREAAA-------EAEEEAEEARE 572
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1034616912 658 KVDSLNREVEQhLNAERSYKSQISTLHKSVVKMEEELQKVQfEKVSALADLSSTR 712
Cdd:PRK02224 573 EVAELNSKLAE-LKERIESLERIRTLLAAIADAEDEIERLR-EKREALAELNDER 625
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
480-737 |
6.18e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 6.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 480 KSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDILAHDNDNLQE 559
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 560 QFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEADNN 639
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 640 TLKLELITAEAEGNRLKEKVDSLNREVEQhlnaersyksqistLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLD 719
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEE--------------LEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
250
....*....|....*...
gi 1034616912 720 SSKELLNRQLVAKDQEIE 737
Cdd:TIGR02168 901 EELRELESKRSELRRELE 918
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
453-737 |
7.41e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 453 REEISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISgmkniiaEMEQASRQCTEALIVCEQDVSRMRRQ 532
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE-------EAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 533 LDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDtnlEVNKLKNILKSEESENRQ 612
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE---AEAELAEAEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 613 MMEQLRKANEDaenwENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEE 692
Cdd:COG1196 388 LLEALRAAAEL----AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1034616912 693 ELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIE 737
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
231-550 |
4.53e-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: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 231 RDREELKCMLEKYERHLAEIQGNVKVLKSERDKIfLLYEQAQEEitrlRREMMKSCKSPKSTTAHAILRRVETERDVAFT 310
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKA-ERYQALLKE----KREYEGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 311 DLRRMTTERDSLRERLkiaqetafnekAHLEQRIEELECTVHNLDDERMEQM--------SNMTLMKETISTVEKEMKSL 382
Cdd:TIGR02169 252 ELEKLTEEISELEKRL-----------EEIEQLLEELNKKIKDLGEEEQLRVkekigeleAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 383 ARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGT 462
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 463 LNDLAKEKECLQACLDKKSENIASLGESLAMKE----KTISGMKNIIAEMEQASR---QCTEALIVCEQDVSRMRRQLDE 535
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEakinELEEEKEDKALEIKKQEWkleQLAADLSKYEQELYDLKEEYDR 480
|
330
....*....|....*
gi 1034616912 536 TNDELAQIARERDIL 550
Cdd:TIGR02169 481 VEKELSKLQRELAEA 495
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
378-651 |
7.48e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 7.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 378 EMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEIS 457
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 458 ILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETN 537
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 538 DELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKlkniLKSEESENRQMMEQL 617
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE----LEEEEEALLELLAEL 468
|
250 260 270
....*....|....*....|....*....|....
gi 1034616912 618 RKANEDAENWENKARQSEADNNTLKLELITAEAE 651
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
377-677 |
9.76e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 9.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 377 KEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEI 456
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 457 SILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQctealivceqdvsrMRRQLDET 536
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE--------------LESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 537 NDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVnklkniLKSEESENRQMMEQ 616
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE------LQAELEELEEELEE 451
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034616912 617 LRKANEDAENWENKARQSEAdnnTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYK 677
Cdd:TIGR02168 452 LQEELERLEEALEELREELE---EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
408-637 |
1.96e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 408 ENTEKDLSDTQRHLAKKKYELQLTQEKIMC-------LDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKK 480
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKAllkqlaaLERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 481 SENIASLgeslamkektisgmkniIAEMEQASRQCTEALIVCEQDVSRMRRQLdetnDELAQIARERDILAHDNDNLQEQ 560
Cdd:COG4942 103 KEELAEL-----------------LRALYRLGRQPPLALLLSPEDFLDAVRRL----QYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034616912 561 FAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEAD 637
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
247-587 |
3.21e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 247 LAEIQGNVKVLKSERDKiFLLYEQAQEEITRLRREMMKSckspksttahailrrvetERDVAFTDLRRMTTERDSLRERL 326
Cdd:COG1196 195 LGELERQLEPLERQAEK-AERYRELKEELKELEAELLLL------------------KLRELEAELEELEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 327 KIAQEtafnEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLARKAMDTESELGRQKAENNSLRLL 406
Cdd:COG1196 256 EELEA----ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 407 YENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISilggtlNDLAKEKECLQACLDKKSENIAs 486
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE------ELAEELLEALRAAAELAAQLEE- 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 487 lgeslamKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKAKQ 566
Cdd:COG1196 405 -------LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
330 340
....*....|....*....|.
gi 1034616912 567 ENQALSKKLNDTHNELNDIKQ 587
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
269-619 |
6.39e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 269 EQAQEEITRLRREMmkSCKSPKSTTAHAILRRVETERDVAFTDLRRMTTERDSLRERLKIAQETAFN---EKAHLEQRIE 345
Cdd:TIGR02169 691 SSLQSELRRIENRL--DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvksELKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 346 ELECTVHNLDD-----ERMEQMSNMTLMKETISTVEKEMKSLARKAMDTESELGRqkaennslrllyentekdlsdtqrh 420
Cdd:TIGR02169 769 ELEEDLHKLEEalndlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR------------------------- 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 421 lakKKYELQLtqekimcLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISG 500
Cdd:TIGR02169 824 ---LTLEKEY-------LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 501 MKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARE--RDILAHDNDNLQEQFAKAKQENQALSKKLNDT 578
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPkgEDEEIPEEELSLEDVQAELQRVEEEIRALEPV 973
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1034616912 579 HNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRK 619
Cdd:TIGR02169 974 NMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
523-693 |
1.39e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 523 EQDVSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNI 602
Cdd:COG3883 29 QAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 603 LKSEE---------------SENRQMMEQLRKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEK----VDSLN 663
Cdd:COG3883 109 LGSESfsdfldrlsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEqealLAQLS 188
|
170 180 190
....*....|....*....|....*....|
gi 1034616912 664 REVEQHLNAERSYKSQISTLHKSVVKMEEE 693
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
235-566 |
2.31e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 235 ELKCMLEKYERHLAEIQgnVKVLKSERDKIFLLYEQAQEEITRLRREMmksckspksttahailrrveTERDVAFTDLRR 314
Cdd:TIGR02168 217 ELKAELRELELALLVLR--LEELREELEELQEELKEAEEELEELTAEL--------------------QELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 315 MTTERDSLRERLKIAQETAFNEKAHLEQRIEELectvhnldDERMEQmsnmtlmketistVEKEMKSLARKAMDTESELG 394
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQIL--------RERLAN-------------LERQLEELEAQLEELESKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 395 RQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQ 474
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 475 ACLDKKSENIASLGESLAMKEK-----TISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDI 549
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEEAELkelqaELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
330
....*....|....*..
gi 1034616912 550 LAHDNDNLQEQFAKAKQ 566
Cdd:TIGR02168 494 LERLQENLEGFSEGVKA 510
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
112-697 |
2.43e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.71 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 112 KIDQLAEQLEKEKNfvvDSANKELEEAKID--LICQQNNIIVLEDTIKRLKSII------LDTEKAQ----NKSPSRLDS 179
Cdd:TIGR04523 34 EEKQLEKKLKTIKN---ELKNKEKELKNLDknLNKDEEKINNSNNKIKILEQQIkdlndkLKKNKDKinklNSDLSKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 180 FVKTLEADKDHYKSEAQHLRKMMRSRSKSPRRPSPTARGANCDVELL----KTTTRDREELKCMLEKYERHLAEIQGNVK 255
Cdd:TIGR04523 111 EIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLnnkyNDLKKQKEELENELNLLEKEKLNIQKNID 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 256 VLKSERDKIFLLY---EQAQEEITRLRREMMKSCKSPKSTTAHAILRRVE-----TERDVAFTDLRRMTTERDSLRERLK 327
Cdd:TIGR04523 191 KIKNKLLKLELLLsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEinektTEISNTQTQLNQLKDEQNKIKKQLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 328 IAQ---ETAFNEKAHLEQRIEELECTVHNLDDERMEQMSN------------MTLMKETISTVEKEMKSLARKAMDTESE 392
Cdd:TIGR04523 271 EKQkelEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKelkselknqekkLEEIQNQISQNNKIISQLNEQISQLKKE 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 393 LGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKEC 472
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 473 LQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDILAH 552
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEE 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 553 DNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQdtNLEVNKLKNILKSEESENRQMMEQLRKANEDAEN----WE 628
Cdd:TIGR04523 511 KVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN--KDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKkqeeKQ 588
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034616912 629 NKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQKV 697
Cdd:TIGR04523 589 ELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEI 657
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
226-737 |
2.57e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 226 LKTTTRDREELKCMLEKYERHLAEIQGNVKVLKSERDKIFLLYEQAQEEITRLRREmmksckspksttahaiLRRVETER 305
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE----------------LARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 306 DVAFTDLRRMTTERDSLRERLKIAQEtafnEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLARK 385
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEE----ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 386 AMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLND 465
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 466 LAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEA-LIVCEQDVSRMRRQLDETNDELAQIA 544
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAlLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 545 RERDILAHDNDNLQEQFAKAKQENQALSKKLNdthnelndikqkvQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDA 624
Cdd:COG1196 541 EAALAAALQNIVVEDDEVAAAAIEYLKAAKAG-------------RATFLPLDKIRARAALAAALARGAIGAAVDLVASD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 625 ENWENKARQSEADnnTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQKVQFEKVSA 704
Cdd:COG1196 608 LREADARYYVLGD--TLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685
|
490 500 510
....*....|....*....|....*....|...
gi 1034616912 705 LADLSSTRELCIKLDSSKELLNRQLVAKDQEIE 737
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEERELAEAEEERLE 718
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
451-651 |
5.28e-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: 46.30 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 451 AQREEISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMR 530
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 531 RQLDETNDELA-------------------------QIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDI 585
Cdd:COG4942 97 AELEAQKEELAellralyrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034616912 586 KQKVQdtnlEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEADNNTLKLELITAEAE 651
Cdd:COG4942 177 EALLA----ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
45-448 |
5.56e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 45 QNTLQLEQEVRNQDRFISTLKLQIEDLKQTNHGLEEYVRKLLDSKEVVSSQVDDLTSHNEHLCKELIKIDQLAEQLEKEk 124
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER- 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 125 nfvVDSANKELEEAKIDLICQQNNIIVLEDTIKRLKSIILDTEKAQNKSPSRLDSFVKTLEADKDHYKSEAQHLRKMMRS 204
Cdd:TIGR02168 749 ---IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 205 RSKSPRRPSPTARGANCDVELLKTTTRDREELKCMLEKYERHLAEIQGNVKVLKSERDKIFLLYEQAQEEITRLRREmmk 284
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE--- 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 285 sckspksttahaiLRRVETERdvaftdlRRMTTERDSLRERLkiaqetafnekAHLEQRIEELECTVHNLDDERMEQMSn 364
Cdd:TIGR02168 903 -------------LRELESKR-------SELRRELEELREKL-----------AQLELRLEGLEVRIDNLQERLSEEYS- 950
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 365 mtLMKETISTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDN 444
Cdd:TIGR02168 951 --LTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
....
gi 1034616912 445 FTRQ 448
Cdd:TIGR02168 1029 EARE 1032
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
434-640 |
5.95e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 5.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 434 KIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISG----MKNIIAEME 509
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreeLGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 510 QASRQCTEALIVCEQD--------VSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNE 581
Cdd:COG3883 97 RSGGSVSYLDVLLGSEsfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034616912 582 LNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEADNNT 640
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
455-737 |
6.47e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 455 EISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVceqdvsRMRRQLD 534
Cdd:TIGR02169 224 EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL------RVKEKIG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 535 ETNDELAQIARERDILAHDNDNLQEQFAKAKQEnqalskkLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMM 614
Cdd:TIGR02169 298 ELEAEIASLERSIAEKERELEDAEERLAKLEAE-------IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 615 EQLRKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEEL 694
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1034616912 695 QKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIE 737
Cdd:TIGR02169 451 KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
532-735 |
8.01e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 532 QLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKS------ 605
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 606 EESENRQMMEQLRKANEDAE---NWENKARQSEADNNTLKlELITAEAEGNRLKEKVDSLNREVEQHL----NAERSYKS 678
Cdd:COG3883 97 RSGGSVSYLDVLLGSESFSDfldRLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKaeleAAKAELEA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034616912 679 QISTLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQE 735
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
77-433 |
1.07e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 77 GLEEYVRKLLDSKEvvssqvdDLTSHNEHLCKELIKIDQLAEQL-----EKEKNFVVDSANKELEEAKIDLICQQNNIiv 151
Cdd:TIGR02169 164 GVAEFDRKKEKALE-------ELEEVEENIERLDLIIDEKRQQLerlrrEREKAERYQALLKEKREYEGYELLKEKEA-- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 152 LEDTIKRLKSIILDTEKAQNKSPSRLDSFVKTLEADKDHYKSEAQHLRKMMRSRSKSPRRPsptargancdvelLKTTTR 231
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEK-------------IGELEA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 232 DREELKCMLEKYERHLAEIQGNVKVLKSERDKIFLLYEQAQEEIT--RLRREMMKSCKSPKSTTAHAILRRVEtERDVAF 309
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEeeRKRRDKLTEEYAELKEELEDLRAELE-EVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 310 TDLRRMTTER-------DSLRERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSL 382
Cdd:TIGR02169 381 AETRDELKDYrekleklKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1034616912 383 ARKAMDTESELGRQKAEnnslrllYENTEKDLSDTQRHLAKKKYELQLTQE 433
Cdd:TIGR02169 461 AADLSKYEQELYDLKEE-------YDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
298-632 |
1.78e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 298 LRRVETERDVAFTDLRRMTTERDSLRERLKIAQEtafnEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEK 377
Cdd:TIGR04523 372 IEKLKKENQSYKQEIKNLESQINDLESKIQNQEK----LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 378 EMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEIS 457
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 458 ILGGTLNDLAKEKECLQACLDKKSENI--ASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLdE 535
Cdd:TIGR04523 528 KLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI-E 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 536 TNDELAqiarerdilahdnDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMME 615
Cdd:TIGR04523 607 EKEKKI-------------SSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKT 673
|
330
....*....|....*..
gi 1034616912 616 QLRKANEDAENWENKAR 632
Cdd:TIGR04523 674 KIDDIIELMKDWLKELS 690
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
112-333 |
4.32e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 112 KIDQLAEQLEKEKNfVVDSANKELEEAKIDLICQQNNIIVLEDTIKRLKSIILDTEKAQNKSPSRLDSFVKTLEADKDHY 191
Cdd:COG4942 21 AAAEAEAELEQLQQ-EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 192 KSEAQHLRKMMRSRSKSPRRPSPT-------ARGANCDVELLKTTTRDREELkcmLEKYERHLAEIQGNVKVLKSERDKI 264
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLAlllspedFLDAVRRLQYLKYLAPARREQ---AEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034616912 265 FLLYEQAQEEITRLRREMmksckspksTTAHAILRRVETERDVAFTDLRRMTTERDSLRERLKIAQETA 333
Cdd:COG4942 177 EALLAELEEERAALEALK---------AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
368-670 |
4.57e-04 |
|
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: 43.67 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 368 MKETISTVEKEMKSLARKAMDTESELG-------RQKAENNSLRLLYENTEKD---LSDTQRHLAKK-----KYELQLTQ 432
Cdd:pfam12128 602 LRERLDKAEEALQSAREKQAAAEEQLVqangeleKASREETFARTALKNARLDlrrLFDEKQSEKDKknkalAERKDSAN 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 433 EKIMCLDEKIDNFTRQNIAQREEISilgGTLNDLAKEK-ECLQACLDKKSENIASLGESLAMKEktiSGMKNIIAEMEQA 511
Cdd:pfam12128 682 ERLNSLEAQLKQLDKKHQAWLEEQK---EQKREARTEKqAYWQVVEGALDAQLALLKAAIAARR---SGAKAELKALETW 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 512 SRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAkakQENQALSKKLNDTHNELNDIKQ---- 587
Cdd:pfam12128 756 YKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWL---QRRPRLATQLSNIERAISELQQqlar 832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 588 KVQDTNLEVNKLKNILKSEESENRQMMEQLRKAnedaenwenKARQS-------EADNNTLKLELITAEAEGNRLKEKVD 660
Cdd:pfam12128 833 LIADTKLRRAKLEMERKASEKQQVRLSENLRGL---------RCEMSklatlkeDANSEQAQGSIGERLAQLEDLKLKRD 903
|
330
....*....|
gi 1034616912 661 SLNREVEQHL 670
Cdd:pfam12128 904 YLSESVKKYV 913
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
531-737 |
5.62e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 531 RQLDETNDELAQIARERDILAHDNDnLQEQFAKAKQEnqalskklndtHNELNDIKQKVQdtnLEVNKLKNILKSEESEN 610
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRE-LAERYAAARER-----------LAELEYLRAALR---LWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 611 RQmmEQLRKANEDAEnwENKARQSEADNNTLKLELITAEAEGNR---LKEKVDSLNREVEQHLNAERSYKSQISTLHKSV 687
Cdd:COG4913 300 LR--AELARLEAELE--RLEARLDALREELDELEAQIRGNGGDRleqLEREIERLERELEERERRRARLEALLAALGLPL 375
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1034616912 688 VKMEEELQKVQFEKVSALADLSSTRELC----IKLDSSKELLNRQLVAKDQEIE 737
Cdd:COG4913 376 PASAEEFAALRAEAAALLEALEEELEALeealAEAEAALRDLRRELRELEAEIA 429
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-713 |
8.45e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 110 LIKIDQLAEQLEkEKNFVVDSANKELEEAkidlicqQNNIIVLEDTIKRLKSIILDTEKAQNKSPSRLDSF---VKTLEA 186
Cdd:TIGR02168 231 VLRLEELREELE-ELQEELKEAEEELEEL-------TAELQELEEKLEELRLEVSELEEEIEELQKELYALaneISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 187 DKDHYKSEAQHLRKMmrsrsksprrpsptargancdvelLKTTTRDREELKCMLEKYERHLAEIQGNVKVLKSErdkifl 266
Cdd:TIGR02168 303 QKQILRERLANLERQ------------------------LEELEAQLEELESKLDELAEELAELEEKLEELKEE------ 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 267 lYEQAQEEITRLRREMmksckspksttahAILRRVETERDVAFTDLRRmttERDSLRERLKIAQetafNEKAHLEQRIEE 346
Cdd:TIGR02168 353 -LESLEAELEELEAEL-------------EELESRLEELEEQLETLRS---KVAQLELQIASLN----NEIERLEARLER 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 347 LECTVHNLDDERMEQMSNMtlmketistVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKY 426
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKL---------EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 427 ELQLTQEKIMCL---DEKIDNFTR---QNIAQREEISILGGTLNDLAKEKECLQACLDK-----------KSENIA---- 485
Cdd:TIGR02168 483 ELAQLQARLDSLerlQENLEGFSEgvkALLKNQSGLSGILGVLSELISVDEGYEAAIEAalggrlqavvvENLNAAkkai 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 486 ------SLGESLAMKEKTISGMKNIIAEMEQASRQ--CTEALIVCEQDVSRMRR-------------QLDETNDELAQIA 544
Cdd:TIGR02168 563 aflkqnELGRVTFLPLDSIKGTEIQGNDREILKNIegFLGVAKDLVKFDPKLRKalsyllggvlvvdDLDNALELAKKLR 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 545 RERDILAHDNDNLQEQFAKAKQENQALSKKLNdTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDA 624
Cdd:TIGR02168 643 PGYRIVTLDGDLVRPGGVITGGSAKTNSSILE-RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 625 EnwenkarQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQKVQFEKVSA 704
Cdd:TIGR02168 722 E-------ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794
|
....*....
gi 1034616912 705 LADLSSTRE 713
Cdd:TIGR02168 795 KEELKALRE 803
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
335-546 |
8.59e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 8.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 335 NEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDL 414
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 415 SDTQRHLAKKKYELQ-----------LTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKKSEN 483
Cdd:COG4942 100 EAQKEELAELLRALYrlgrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034616912 484 IASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARE 546
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
224-737 |
9.44e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 224 ELLKTTTRDREELKCMLEKYERHLAEIQGNVKVLKSERDKIFLLYEQAQEEITRLRREMMKSCKSPKS-----TTAHAIL 298
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANlerqlEELEAQL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 299 RRVETERDVAFTDLRRMTTERDSLR---ERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTV 375
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKeelESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 376 EKEMKSLAR-------------------KAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIM 436
Cdd:TIGR02168 406 EARLERLEDrrerlqqeieellkkleeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 437 CLDEKID-------------NFTRQNIAQREEISILGGTLNDL---------AKEK---ECLQACLDKKSENIASLGESL 491
Cdd:TIGR02168 486 QLQARLDslerlqenlegfsEGVKALLKNQSGLSGILGVLSELisvdegyeaAIEAalgGRLQAVVVENLNAAKKAIAFL 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 492 AMKE-------------------------KTISGMKNIIAEMEQASRQCTEAL-------IVCE--QDVSRMRRQLD--- 534
Cdd:TIGR02168 566 KQNElgrvtflpldsikgteiqgndreilKNIEGFLGVAKDLVKFDPKLRKALsyllggvLVVDdlDNALELAKKLRpgy 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 535 ---------------------ETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTN 593
Cdd:TIGR02168 646 rivtldgdlvrpggvitggsaKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 594 LEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQhlnae 673
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA----- 800
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034616912 674 rsYKSQISTLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIE 737
Cdd:TIGR02168 801 --LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
39-600 |
1.37e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 39 SEAENYQNTLQLEQE-VRNQDrfiSTLKLQIEDLKQTNHGLEEYVRkllDSKEVVSSQVDDLTSHNEHLCKELIKIDQLA 117
Cdd:pfam15921 292 SQANSIQSQLEIIQEqARNQN---SMYMRQLSDLESTVSQLRSELR---EAKRMYEDKIEELEKQLVLANSELTEARTER 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 118 EQLEKEKNFVVDSANKEL-----EEAKIDLICQQNNIIVLEDTIKRLKSIILDTE-KAQNKSPSRLDSFVKTLEADkdhy 191
Cdd:pfam15921 366 DQFSQESGNLDDQLQKLLadlhkREKELSLEKEQNKRLWDRDTGNSITIDHLRRElDDRNMEVQRLEALLKAMKSE---- 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 192 kSEAQHLRKM--MRSRSKSPRRPSPTARGANCDVELLKTTTRDREELKCMLEKYERHLAEIQGNVKvlksERDKIFllyE 269
Cdd:pfam15921 442 -CQGQMERQMaaIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ----EKERAI---E 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 270 QAQEEITRLRREM---MKSCKSPKSTTAHaiLRRVETERDVaftdLRRMTTERDSLRERLKIAQETAFN----------- 335
Cdd:pfam15921 514 ATNAEITKLRSRVdlkLQELQHLKNEGDH--LRNVQTECEA----LKLQMAEKDKVIEILRQQIENMTQlvgqhgrtaga 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 336 ---EKAHLEQRIeelectvhnlDDERMEqMSNMTLMKEtistvEKEMKSLARKAMDTESELGRQKAENNSLRLLyenteK 412
Cdd:pfam15921 588 mqvEKAQLEKEI----------NDRRLE-LQEFKILKD-----KKDAKIRELEARVSDLELEKVKLVNAGSERL-----R 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 413 DLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISIlggTLNDLAKEKECLQACLDKKSENIASL--GES 490
Cdd:pfam15921 647 AVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMET---TTNKLKMQLKSAQSELEQTRNTLKSMegSDG 723
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 491 LAMK-----EKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKAK 565
Cdd:pfam15921 724 HAMKvamgmQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLK 803
|
570 580 590
....*....|....*....|....*....|....*
gi 1034616912 566 QENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLK 600
Cdd:pfam15921 804 EKVANMEVALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
342-728 |
1.76e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 342 QRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHL 421
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 422 AKKKYELQLTQEKIM---CLDEKIDNFTRQNI--------------AQREEISILGGTLNDLAKEKECLQACLDKKSENI 484
Cdd:TIGR04523 197 LKLELLLSNLKKKIQknkSLESQISELKKQNNqlkdniekkqqeinEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 485 ASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIvcEQDVSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKA 564
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKEL--KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNS 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 565 KQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEADNNTLKLE 644
Cdd:TIGR04523 355 ESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 645 LITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKEL 724
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKD 514
|
....
gi 1034616912 725 LNRQ 728
Cdd:TIGR04523 515 LTKK 518
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
312-574 |
1.97e-03 |
|
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: 40.95 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 312 LRRMTTERDSLRERLKIAQETAFNEKAHLEQRIEE---LECTVHNLDDERMEQMSNMTLMKETIS--TVEKEMKSLARKA 386
Cdd:pfam15905 82 IRALVQERGEQDKRLQALEEELEKVEAKLNAAVREktsLSASVASLEKQLLELTRVNELLKAKFSedGTQKKMSSLSMEL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 387 MDTESELgrqKAENNSLRLLYENTEKDLSDTQRHlakkkyeLQLTQEKIMCLDEKIDNFTRQNIAQREEIsilgGTLNDL 466
Cdd:pfam15905 162 MKLRNKL---EAKMKEVMAKQEGMEGKLQVTQKN-------LEHSKGKVAQLEEKLVSTEKEKIEEKSET----EKLLEY 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 467 AKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEalivceqDVSRMRRQLDETNDELAQIARE 546
Cdd:pfam15905 228 ITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIK-------DLNEKCKLLESEKEELLREYEE 300
|
250 260
....*....|....*....|....*....
gi 1034616912 547 RDI-LAHDNDNLQEQFAKAKQENQALSKK 574
Cdd:pfam15905 301 KEQtLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
312-667 |
2.56e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 312 LRRMTTERDSLRERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQmsnmtlmketISTVEKEMKSLARKAMDTES 391
Cdd:pfam02463 175 LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEE----------YLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 392 ELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKE 471
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 472 CLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDILA 551
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 552 HDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKA 631
Cdd:pfam02463 405 KEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQE 484
|
330 340 350
....*....|....*....|....*....|....*.
gi 1034616912 632 RQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVE 667
Cdd:pfam02463 485 QLELLLSRQKLEERSQKESKARSGLKVLLALIKDGV 520
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
526-679 |
4.56e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 526 VSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKS 605
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034616912 606 EESENRQMMEQLRKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQ 679
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
224-452 |
5.13e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 224 ELLKTTTRDREELKCMLEKYERHlAEIQGNVKVLKSERDKI-----FLLYEQAQEEITRLRREmmksckspksttahaiL 298
Cdd:COG4913 242 EALEDAREQIELLEPIRELAERY-AAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAE----------------L 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 299 RRVETERDVAFTDLRRMTTERDSLRERLkiaQETAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKE 378
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQI---RGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034616912 379 MKSLARKAMDTESELGRQKAEnnsLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFtRQNIAQ 452
Cdd:COG4913 382 FAALRAEAAALLEALEEELEA---LEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL-RDALAE 451
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
438-588 |
5.31e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 438 LDEKIDNFTRQNIAQREEISILGGTLNDL-AKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCT 516
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALrEELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALG 372
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034616912 517 EALIVCEQDVSRMRRQLDETNDELAQIARErdilahdndnLQEQFAKAKQENQALSKKLNDTHNELNDIKQK 588
Cdd:COG4913 373 LPLPASAEEFAALRAEAAALLEALEEELEA----------LEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
553-626 |
5.41e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 39.71 E-value: 5.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034616912 553 DNDNLQEQFAKAKQENQALSKKLNDTHNELNDIK-QKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAEN 626
Cdd:TIGR04320 276 ALNTAQAALTSAQTAYAAAQAALATAQKELANAQaQALQTAQNNLATAQAALANAEARLAKAKEALANLNADLAK 350
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
616-737 |
5.60e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 616 QLRKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQ 695
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1034616912 696 KVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIE 737
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
311-730 |
8.25e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.64 E-value: 8.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 311 DLRRMTTERDSLRERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLARKAMD-T 389
Cdd:TIGR00606 713 STESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDvT 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 390 ESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKE 469
Cdd:TIGR00606 793 IMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 470 KECLqacldkkSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDI 549
Cdd:TIGR00606 873 KLQI-------GTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVND 945
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 550 LAHDNDNLQ------EQFAKAKQENQALSKK--LNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKAN 621
Cdd:TIGR00606 946 IKEKVKNIHgymkdiENKIQDGKDDYLKQKEteLNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRK 1025
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 622 EDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVvkMEEELQKVQFEK 701
Cdd:TIGR00606 1026 RENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL--REPQFRDAEEKY 1103
|
410 420
....*....|....*....|....*....
gi 1034616912 702 VSALADLSSTRELCIKLDSSKELLNRQLV 730
Cdd:TIGR00606 1104 REMMIVMRTTELVNKDLDIYYKTLDQAIM 1132
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
340-698 |
9.04e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.39 E-value: 9.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 340 LEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVE-------KEMKSLARKAMDTESELGRQKAENNSLRLLYENTEK 412
Cdd:pfam01576 108 LEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEdqnsklsKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 413 DLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLndlAKEKECLQACLDKKSENIASLGESLa 492
Cdd:pfam01576 188 MISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQL---AKKEEELQAALARLEEETAQKNNAL- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 493 mkeKTISGMKNIIAEME-----------QASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDILAHDNDNLQEQF 561
Cdd:pfam01576 264 ---KKIRELEAQISELQedleseraarnKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEET 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616912 562 AKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILkseESENRQMMEQLRKANEDAENWENKARQSEADNNTL 641
Cdd:pfam01576 341 RSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQAL---ESENAELQAELRTLQQAKQDSEHKRKKLEGQLQEL 417
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034616912 642 KLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQKVQ 698
Cdd:pfam01576 418 QARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ 474
|
|
| |
