|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
383-753 |
1.47e-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: 71.63 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 383 STTGSSPNNASELS----LASLTEKIQKMEENhhstAEELQATLQELSDQQQmvqELTAENEKLVDEKTILETSFHQHRE 458
Cdd:TIGR02168 661 ITGGSAKTNSSILErrreIEELEEKIEELEEK----IAELEKALAELRKELE---ELEEELEQLRKELEELSRQISALRK 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 459 RAEQLSHENEKLINLLQErvkkeepgtQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTcslrKAEEENQGAAEMIQR 538
Cdd:TIGR02168 734 DLARLEAEVEQLEERIAQ---------LSKELTELEAEIEELEERLEEAEEELAEAEAEIE----ELEAQIEQLKEELKA 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 539 LKEENEKLNGLLELERQNSGVMAQTLEECTVTLEGLKIENGSLKAYLE-NEKQKAIVTSSMGQTAEGC-EIQEMLKVARA 616
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEeLSEDIESLAAEIEELEELIeELESELEALLN 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 617 EKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELE 696
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALE 960
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 987976904 697 DQVE-----QHRAVKLHNNQL----------ITELESSVMK---LEGQKADLERQLKTLTKQIKEETEEWR-RFQA 753
Cdd:TIGR02168 961 NKIEddeeeARRRLKRLENKIkelgpvnlaaIEEYEELKERydfLTAQKEDLTEAKETLEEAIEEIDREAReRFKD 1036
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
487-794 |
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: 62.77 E-value: 7.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 487 EGKVLELEQKCTEILEQGRCEREKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEKLNGLLELERQNSGVMAQTLEE 566
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 567 CTVTLEGLKIENGSLKAYLENEKQkaivtssmgqtaegceIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLL 646
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEE----------------LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 647 AKVEKDYSYLKEicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEGQ 726
Cdd:TIGR02168 827 ESLERRIAATER----RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 987976904 727 KADLERQLKTLTKQIKEETEEWRRFQADLQtavvvandikcEAQQELRTVKRRLLEEEEKNARLQKEL 794
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLE-----------GLEVRIDNLQERLSEEYSLTLEEAEAL 959
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
403-792 |
3.14e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 403 KIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETsFHQHRERAEQLSHENEKlinlLQERVKKEE 482
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-RHELYEEAKAKKEELER----LKKRLTGLT 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 483 PGTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTcSLRKAEEENQGA---AEMIQRLKEENEKLNGLLELERQNSGV 559
Cdd:PRK03918 386 PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIK-ELKKAIEELKKAkgkCPVCGRELTEEHRKELLEEYTAELKRI 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 560 mAQTLEECTVTLEGLKIENGSLKAYLENEKQkaivTSSMGQTAEGC-EIQEMLKVARAEKdqLELSCTE---LKQELLKA 635
Cdd:PRK03918 465 -EKELKEIEEKERKLRKELRELEKVLKKESE----LIKLKELAEQLkELEEKLKKYNLEE--LEKKAEEyekLKEKLIKL 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 636 HGEIKHVSSLLAKV---EKDYSYLKEICDHQAEQLSRTSLKLQEKASESdaeIKDMKETIFELE----------DQVEQH 702
Cdd:PRK03918 538 KGEIKSLKKELEKLeelKKKLAELEKKLDELEEELAELLKELEELGFES---VEELEERLKELEpfyneylelkDAEKEL 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 703 RAVKLHNNQLITELESSVMKLEGQKADLERQLKTLT-----------KQIKEETEEWRRFQADLQTAVVVANDIKCEAQQ 771
Cdd:PRK03918 615 EREEKELKKLEEELDKAFEELAETEKRLEELRKELEelekkyseeeyEELREEYLELSRELAGLRAELEELEKRREEIKK 694
|
410 420
....*....|....*....|.
gi 987976904 772 ELRTVKRRLLEEEEKNARLQK 792
Cdd:PRK03918 695 TLEKLKEELEEREKAKKELEK 715
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
606-804 |
1.17e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 606 EIQEMLKVARAEKDQLELSCtELKQELLKAHGEIKHVSSLLAKV-----EKDYSYLKEICDHQAEQLSRtslkLQEKASE 680
Cdd:COG4913 239 RAHEALEDAREQIELLEPIR-ELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELAR----LEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 681 SDAEIKDMKETIFELEDQVEQHRAVKLHN-NQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAV 759
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALL 393
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 987976904 760 VVANDIKCEAQQELRTVKRRLLEEEEKNARLQKELGDMQGHGSDL 804
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNI 438
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
416-795 |
3.90e-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: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 416 EELQATLQELsdqqQMVQELTAENEKLVDEKtiletsfhqhRERAEQLSHENEKLINLLQERVKKEEpgtQEGKVLELEQ 495
Cdd:TIGR02169 170 RKKEKALEEL----EEVEENIERLDLIIDEK----------RQQLERLRREREKAERYQALLKEKRE---YEGYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 496 KCTEI-LEQGRCEREkllSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEKLNGLLElERQNSgvMAQTLEECTVTLEGL 574
Cdd:TIGR02169 233 EALERqKEAIERQLA---SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE-EEQLR--VKEKIGELEAEIASL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 575 KienGSLKAYLENEKQkaivtssmgqtaegceIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYS 654
Cdd:TIGR02169 307 E---RSIAEKERELED----------------AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 655 YLKEicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEGQKADLERQL 734
Cdd:TIGR02169 368 DLRA----ELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 987976904 735 KTLTKQIKEETEEWRRFQADLQTAVVVANDIKceaqQELRTVKRRLLEEEEKNARLQKELG 795
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLK----EEYDRVEKELSKLQRELAEAEAQAR 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
391-654 |
4.26e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 391 NASELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKL 470
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 471 INLLQERVKKEEpgTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLtcsLRKAEEENQGAAEMIQRLKEENEKLNGLL 550
Cdd:COG1196 329 EEELEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---AEAEEELEELAEELLEALRAAAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 551 ELERQNSGvMAQTLEECTVTLEGLKIENGSLKAYLENEKQKAivTSSMGQTAEGCEIQEMLKVARAEKDQLELSCTELKQ 630
Cdd:COG1196 404 ELEEAEEA-LLERLERLEEELEELEEALAELEEEEEEEEEAL--EEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
250 260
....*....|....*....|....
gi 987976904 631 ELLKAHGEIKHVSSLLAKVEKDYS 654
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
391-665 |
6.86e-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: 56.60 E-value: 6.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 391 NASELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETS---FHQHRERAEQLSHEN 467
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQleeLESKLDELAEELAEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 468 EKLINLLQERVK--KEEPGTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQ---LTCSLRKAEEENQGAAEMIQRLKEE 542
Cdd:TIGR02168 343 EEKLEELKEELEslEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiasLNNEIERLEARLERLEDRRERLQQE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 543 NEKLNGLLELERqnsgvmaqtLEECTVTLEGLKIENGSLKAYLEnekqkaivtssmgqtaegcEIQEMLKVARAEKDQLE 622
Cdd:TIGR02168 423 IEELLKKLEEAE---------LKELQAELEELEEELEELQEELE-------------------RLEEALEELREELEEAE 474
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 987976904 623 LSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAE 665
Cdd:TIGR02168 475 QALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
391-798 |
1.34e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 391 NASELSLASLTEKIQKMEENHH---STAEELQATLQELSDQQQMVQELTAENEKLVD-------EKTILETSFHQHRERA 460
Cdd:PRK02224 209 NGLESELAELDEEIERYEEQREqarETRDEADEVLEEHEERREELETLEAEIEDLREtiaeterEREELAEEVRDLRERL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 461 EQLSHENEKL-------------INLLQERVKKEEPGTQEgKVLELEQKCTEILEQGRCEREKLLSIQQQ---------- 517
Cdd:PRK02224 289 EELEEERDDLlaeaglddadaeaVEARREELEDRDEELRD-RLEECRVAAQAHNEEAESLREDADDLEERaeelreeaae 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 518 LTCSLRKAEEENQGAAEMIQRLKEENEKLNGLLELERQNSGVMAQTLEECTVTLEGLKIENGSLKAYLENEK-------- 589
Cdd:PRK02224 368 LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARerveeaea 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 590 -QKAIVTSSMGQTAEGCEIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSlLAKVEKDYSYLKE-------ICD 661
Cdd:PRK02224 448 lLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEErredleeLIA 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 662 HQAEQLSRTSLKLQEK---ASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEgqkaDLERQLKTLT 738
Cdd:PRK02224 527 ERRETIEEKRERAEELrerAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE----RIRTLLAAIA 602
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 739 kQIKEETEEWRRFQADLQTavvvANDIKCEAQQELRTvKRRLLEEEEKNARLQKELGDMQ 798
Cdd:PRK02224 603 -DAEDEIERLREKREALAE----LNDERRERLAEKRE-RKRELEAEFDEARIEEAREDKE 656
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
606-794 |
1.49e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 606 EIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRtslkLQEKASESDAEI 685
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE----LEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 686 KDMKETIFELEDQVEQHRAVKLhnnQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDI 765
Cdd:COG1196 326 AELEEELEELEEELEELEEELE---EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
170 180
....*....|....*....|....*....
gi 987976904 766 KcEAQQELRTVKRRLLEEEEKNARLQKEL 794
Cdd:COG1196 403 E-ELEEAEEALLERLERLEEELEELEEAL 430
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
397-651 |
1.84e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 397 LASLTEKIQKMEENHHSTAEELQATLQELSD-------QQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEK 469
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEElrlevseLEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 470 LINLLQERVKK-----EEPGTQEGKVLELEQKCTEILEQGrcerEKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENE 544
Cdd:TIGR02168 321 LEAQLEELESKldelaEELAELEEKLEELKEELESLEAEL----EELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 545 KLNGllELERqnsgvMAQTLEECTVTLEGLKIENGSLKAYLENEKQKAIVTSSMGQTAEGCEIQEMLKVARAEKDQLELS 624
Cdd:TIGR02168 397 SLNN--EIER-----LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
250 260
....*....|....*....|....*..
gi 987976904 625 CTELKQELLKAHGEIKHVSSLLAKVEK 651
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLER 496
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
393-809 |
2.39e-07 |
|
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: 54.80 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 393 SELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKL-- 470
Cdd:pfam01576 24 AESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMqq 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 471 -INLLQERVKKEEPGTQ---------EGKVLELEQKCTEILEQ-GRCEREKLLSIQQQLTCSLRKAEEENQgaAEMIQRL 539
Cdd:pfam01576 104 hIQDLEEQLDEEEAARQklqlekvttEAKIKKLEEDILLLEDQnSKLSKERKLLEERISEFTSNLAEEEEK--AKSLSKL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 540 KEENEKLNGLLELERQNSGVMAQTLEECTVTLEG-----------LKIENGSLKAYL---ENEKQKAIVTSSMGQTAEG- 604
Cdd:pfam01576 182 KNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGestdlqeqiaeLQAQIAELRAQLakkEEELQAALARLEEETAQKNn 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 605 ------------CEIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKdysyLKEICDHQAEQLSRTsl 672
Cdd:pfam01576 262 alkkireleaqiSELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE----LRSKREQEVTELKKA-- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 673 kLQEKASESDAEIKDMKE----TIFELEDQVEQHRAVKlhnnqliTELESSVMKLEGQKADLERQLKTLTkQIKEETEEW 748
Cdd:pfam01576 336 -LEEETRSHEAQLQEMRQkhtqALEELTEQLEQAKRNK-------ANLEKAKQALESENAELQAELRTLQ-QAKQDSEHK 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 987976904 749 RRFQ----ADLQTAVVVANDIKCEA-------QQELRTVKRRLLEEEEKNARLQKELGDMQGHGSDLQTYLQ 809
Cdd:pfam01576 407 RKKLegqlQELQARLSESERQRAELaeklsklQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ 478
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
397-794 |
6.28e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.43 E-value: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 397 LASLTEKIQKmeeNHHSTAEELQATLQELSD-QQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENE------K 469
Cdd:TIGR00618 181 LALMEFAKKK---SLHGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREaqeeqlK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 470 LINLLQERVKKEEPGTQEGKVLELEQKCTEIleqgRCEREKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEKLNGL 549
Cdd:TIGR00618 258 KQQLLKQLRARIEELRAQEAVLEETQERINR----ARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAH 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 550 L--ELERQNSGVMAQTLEECTVTLEGLKIENGSLKAYLENE--------KQKAIVTSSMGQTAEGCEIQEMLKVARAEKD 619
Cdd:TIGR00618 334 VkqQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQhtltqhihTLQQQKTTLTQKLQSLCKELDILQREQATID 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 620 QLELSCTELKQELLKAHGEI----KHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQ-----EKASESDAEIKDMKE 690
Cdd:TIGR00618 414 TRTSAFRDLQGQLAHAKKQQelqqRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQqlqtkEQIHLQETRKKAVVL 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 691 TIfeLEDQVEQHRAVK---LHNNQ-------------LITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQAD 754
Cdd:TIGR00618 494 AR--LLELQEEPCPLCgscIHPNParqdidnpgpltrRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS 571
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 987976904 755 LQTAVVVANDIKCEAQQeLRTVKRRLLEEEEKNARLQKEL 794
Cdd:TIGR00618 572 FSILTQCDNRSKEDIPN-LQNITVRLQDLTEKLSEAEDML 610
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
397-791 |
6.41e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 6.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 397 LASLTEKIQKMEENHHSTAEELQATLQELS--DQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKLINLL 474
Cdd:COG4717 90 YAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 475 QERVKKEEPGTQEGKVLELEQKctEILEQGRCEREKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEKLNGLLELER 554
Cdd:COG4717 170 AELAELQEELEELLEQLSLATE--EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 555 QNSGVMAQTLeecTVTLEGLKIENGSLK----------------AYLENEKQKAIVTSSMGQTAEGCEIQEMLKVARAE- 617
Cdd:COG4717 248 ARLLLLIAAA---LLALLGLGGSLLSLIltiagvlflvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELEEl 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 618 KDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYS--YLKEICDHQAEQLSR---TSLKLQEKASESDAEIKDMKETI 692
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEelQLEELEQEIAALLAEagvEDEEELRAALEQAEEYQELKEEL 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 693 FELEDQVEQHRAVKLHNNQLITELEssvmkLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVvvANDIKCEAQQE 772
Cdd:COG4717 405 EELEEQLEELLGELEELLEALDEEE-----LEEELEELEEELEELEEELEELREELAELEAELEQLE--EDGELAELLQE 477
|
410
....*....|....*....
gi 987976904 773 LRTVKRRLLEEEEKNARLQ 791
Cdd:COG4717 478 LEELKAELRELAEEWAALK 496
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
523-786 |
6.92e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 523 RKAEEENQGAAEMIQRLKEENEKLNGLLELERQNSGVMAQTLEECTVTLEGLKIENGSLKAYLE--NEKQKAIVTSSMGQ 600
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEklKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 601 TAEGCEIQEMLKVARAEKDQLELSCTELKQELLK-----AHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRtslKLQ 675
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR---LTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 676 EKASESDaEIKDMKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADL 755
Cdd:TIGR02169 827 EKEYLEK-EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
250 260 270
....*....|....*....|....*....|.
gi 987976904 756 QTAVVVANdiKCEAQQELRTVKRRLLEEEEK 786
Cdd:TIGR02169 906 EELEAQIE--KKRKRLSELKAKLEALEEELS 934
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
396-793 |
7.40e-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: 53.15 E-value: 7.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 396 SLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLShenEKLINLLQ 475
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE---EDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 476 ERV-KKEEPGTQEGKVLELEQKCTEI-LEQGRCEREKLLSIQQQLTCSLRKAEEENQgaaEMIQRLKEENEKLNGLLEle 553
Cdd:TIGR02169 752 EIEnVKSELKELEARIEELEEDLHKLeEALNDLEARLSHSRIPEIQAELSKLEEEVS---RIEARLREIEQKLNRLTL-- 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 554 rqnsgvmaqtleectvtleglkiengsLKAYLENEKQKAIvtssmgqtAEGCEIQEMLKVARAEKDQLELSCTELKQELL 633
Cdd:TIGR02169 827 ---------------------------EKEYLEKEIQELQ--------EQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 634 KAHGEIKHVSSLLAKVEKDYSylkeicdhqaeqlsrtslKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLI 713
Cdd:TIGR02169 872 ELEAALRDLESRLGDLKKERD------------------ELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 714 TELESSVMKLEGQKADlERQLKTLTKQIKEETEEWRRFQadlqtavvvanDIKCEAQQELRTVKRRLLEEEEKNARLQKE 793
Cdd:TIGR02169 934 SEIEDPKGEDEEIPEE-ELSLEDVQAELQRVEEEIRALE-----------PVNMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
661-794 |
2.31e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 661 DHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEGQKADLERQLKTLTKQ 740
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 987976904 741 IKEETEEWRRFQADLQTA---VVVANDIKCEAQQELRTVKRRLLEEEEKNARLQKEL 794
Cdd:COG1196 325 LAELEEELEELEEELEELeeeLEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
397-730 |
4.19e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 397 LASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTaENEKLVDEKTILEtsFHQHRERAEQLSHENEKLINLLQE 476
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG-EEEQLRVKEKIGE--LEAEIASLERSIAEKERELEDAEE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 477 RVKK--EEPGTQEGKVLELEQKcteiLEQGRCEREKLLSI----QQQLTCSLRKAEEENQGAAEMIQRLKEENEKLngll 550
Cdd:TIGR02169 323 RLAKleAEIDKLLAEIEELERE----IEEERKRRDKLTEEyaelKEELEDLRAELEEVDKEFAETRDELKDYREKL---- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 551 elerqnsgvmaqtleectvtlEGLKIENGSLKA---YLENEKQKAivtssmgqTAEGCEIQEMLKVARAEKDQLELSCTE 627
Cdd:TIGR02169 395 ---------------------EKLKREINELKReldRLQEELQRL--------SEELADLNAAIAGIEAKINELEEEKED 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 628 LKQELLKAHGEIKHVSSLLAKVEKDYSylkeicdhqaeqlsrtslKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKL 707
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELY------------------DLKEEYDRVEKELSKLQRELAEAEAQARASEERVR 507
|
330 340
....*....|....*....|...
gi 987976904 708 HNNQLITELESSVMKLEGQKADL 730
Cdd:TIGR02169 508 GGRAVEEVLKASIQGVHGTVAQL 530
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
453-808 |
5.33e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 453 FHQHRERAEQLSHEneklINLLQERVKKEEPGTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTCSLRKAEEENQGA 532
Cdd:COG1196 215 YRELKEELKELEAE----LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 533 AEMIQRLKEENEKLNGLLELERQNSgvmaqtleectVTLEGLKIENGSLKAYLENEKQKAIvtssmgqtaegcEIQEMLK 612
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELE-----------ERLEELEEELAELEEELEELEEELE------------ELEEELE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 613 VARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEicdhQAEQLSRTSLKLQEKASESDAEIKDMKETI 692
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR----AAAELAAQLEELEEAEEALLERLERLEEEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 693 FELEDQVEQHRAVKLHNNQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIK-CEAQQ 771
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLeAEADY 503
|
330 340 350
....*....|....*....|....*....|....*..
gi 987976904 772 ELRTVKRRLLEEEEKNARLQKELGDMQGHGSDLQTYL 808
Cdd:COG1196 504 EGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
391-783 |
5.91e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.12 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 391 NASELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAEneklvdektiletsfHQHRERA-EQLSHENEK 469
Cdd:pfam15921 457 NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTAS---------------LQEKERAiEATNAEITK 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 470 LINLLQERVKKEEPGTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEKLNGL 549
Cdd:pfam15921 522 LRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEIND 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 550 LELERQNSGVMAQTLEECTVTLEGlKIENgslkayLENEKQKAIVTSSmgqtaegceiqEMLKVARaekdqlelsctELK 629
Cdd:pfam15921 602 RRLELQEFKILKDKKDAKIRELEA-RVSD------LELEKVKLVNAGS-----------ERLRAVK-----------DIK 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 630 QELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHN 709
Cdd:pfam15921 653 QERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGM 732
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 987976904 710 NQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQeLRTVKRRLLEE 783
Cdd:pfam15921 733 QKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEV-LRSQERRLKEK 805
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
394-795 |
7.01e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 7.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 394 ELSLASLTEKIQKMEENHHSTAEEL---QATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLshenEKL 470
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELeklEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL----KKE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 471 INLLQERVKKEEpgtqegkvlELEQKCTEILEQGRcEREKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEKLNGLL 550
Cdd:PRK03918 275 IEELEEKVKELK---------ELKEKAEEYIKLSE-FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 551 ELERQNSGVMAQtLEECTVTLEGLKiengSLKAYLENEKQKAivtssMGQTAEgcEIQEMLKVARAEKDQLELSCTELKQ 630
Cdd:PRK03918 345 KKLKELEKRLEE-LEERHELYEEAK----AKKEELERLKKRL-----TGLTPE--KLEKELEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 631 ELLKAHGEIKHVSSLLAKVEKdysyLKEIC---------DHQAEQLSRTSLKL---QEKASESDAEIKDMKETIFELEDQ 698
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKK----AKGKCpvcgrelteEHRKELLEEYTAELkriEKELKEIEEKERKLRKELRELEKV 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 699 VEQHRAVkLHNNQLITELESSVMKLEgqKADLErQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKcEAQQELRTVKR 778
Cdd:PRK03918 489 LKKESEL-IKLKELAEQLKELEEKLK--KYNLE-ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE-ELKKKLAELEK 563
|
410
....*....|....*..
gi 987976904 779 RLLEEEEKNARLQKELG 795
Cdd:PRK03918 564 KLDELEEELAELLKELE 580
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
391-747 |
1.30e-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: 48.86 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 391 NASELSLASLTEKIQKMEEnhhstaeeLQATLQELSDQQQMVQE-LTAENEKLVDEKTILETSfhqhRERAEQLSHENEK 469
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKS--------LESQISELKKQNNQLKDnIEKKQQEINEKTTEISNT----QTQLNQLKDEQNK 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 470 LINLLQERVKKEEpgTQEGKVLELEQKCTEIleqgrceREKLLSIQQQltcslrKAEEENQGAAEMIQRLKEENEKLNGL 549
Cdd:TIGR04523 265 IKKQLSEKQKELE--QNNKKIKELEKQLNQL-------KSEISDLNNQ------KEQDWNKELKSELKNQEKKLEEIQNQ 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 550 LELERQNSGVMAQTLEECTVTLEGLKIENGSLKAYLEnEKQKAIVTssmgqtaEGCEIQEMLKvaraEKDQLELSCTELK 629
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE-EKQNEIEK-------LKKENQSYKQ----EIKNLESQINDLE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 630 QELLKAHGEIKHVSSLLAKVEKDYsylkeicdhqaEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHN 709
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEK-----------ELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL 466
|
330 340 350
....*....|....*....|....*....|....*...
gi 987976904 710 NQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEE 747
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
508-805 |
1.89e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 508 REKLLSIQQQLTCSLR----KAEEENQGAAEMIQRLKEENEKLNGLLELERQNSGVMAQT---LEECTVTLEGLKIENGS 580
Cdd:TIGR02168 199 ERQLKSLERQAEKAERykelKAELRELELALLVLRLEELREELEELQEELKEAEEELEELtaeLQELEEKLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 581 LKAYLEnekqkaivtssmgqtaegcEIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEIC 660
Cdd:TIGR02168 279 LEEEIE-------------------ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 661 DHQAEQLSRtslkLQEKASESDAEIKDMKETIFELEDQVEQHRA---------------VKLHNNQL------ITELESS 719
Cdd:TIGR02168 340 AELEEKLEE----LKEELESLEAELEELEAELEELESRLEELEEqletlrskvaqlelqIASLNNEIerlearLERLEDR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 720 VMKLEGQKADLERQLKTLTKQ-IKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKNARLQKE---LG 795
Cdd:TIGR02168 416 RERLQQEIEELLKKLEEAELKeLQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARldsLE 495
|
330
....*....|
gi 987976904 796 DMQGHGSDLQ 805
Cdd:TIGR02168 496 RLQENLEGFS 505
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
416-742 |
2.45e-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: 48.09 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 416 EELQATLQELSDQQQMVQELTAENEKLVDEKTILETsfhQHRERAEQLSHENEKLINLLQER-VKKEEPGTQEGKVLELE 494
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES---ENSEKQRELEEKQNEIEKLKKENqSYKQEIKNLESQINDLE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 495 QKCTEILEQgrcerekllsiQQQLTCSLRKAEEENQGAAEMIQRLKEENEKLNGLL-ELERQNSGV------MAQTLEEC 567
Cdd:TIGR04523 398 SKIQNQEKL-----------NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIkDLTNQDSVKeliiknLDNTRESL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 568 TVTLEGLKIENGSLKAYLENEKQ--KAIVTSSMGQTAEGCEIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSL 645
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKelKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 646 LAKV--EKDYSYLKEICDHQA---EQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLITELESSV 720
Cdd:TIGR04523 547 LNKDdfELKKENLEKEIDEKNkeiEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKEN 626
|
330 340
....*....|....*....|..
gi 987976904 721 MKLEGQKADLERQLKTLTKQIK 742
Cdd:TIGR04523 627 EKLSSIIKNIKSKKNKLKQEVK 648
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
386-803 |
3.64e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.66 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 386 GSSPNNASELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSH 465
Cdd:pfam02463 129 GISPEAYNFLVQGGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKK 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 466 ENEKLINLLQERVKKEEPgTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEK 545
Cdd:pfam02463 209 ALEYYQLKEKLELEEEYL-LYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 546 LNGLLELERQNSGVMAQTLEECTVTLEGLKIENGSL-KAYLENEKQKAIVTSSMGQTAEGCEIQEMLKVARAEKDQLELS 624
Cdd:pfam02463 288 LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKkKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 625 CTELKQELLKAHG-EIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHR 703
Cdd:pfam02463 368 LEQLEEELLAKKKlESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLT 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 704 AVKLH-NNQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQElRTVKRRLLE 782
Cdd:pfam02463 448 EEKEElEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIK-DGVGGRIIS 526
|
410 420
....*....|....*....|.
gi 987976904 783 EEEKNARLQKELGDMQGHGSD 803
Cdd:pfam02463 527 AHGRLGDLGVAVENYKVAIST 547
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
606-809 |
4.87e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 606 EIQEMLKVARAEKDQLELSCTELKQELLKAhgEIKHVSSLLAKVEKDysylKEICDHQAEQLSRTSLKLQEKASESDAEI 685
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEA--ELEELEAELEELEAE----LAELEAELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 686 KDMKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDI 765
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 987976904 766 KCEAQQELRTVKRRLLEEEEKNARLQKELGDMQGHGSDLQTYLQ 809
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
606-798 |
1.16e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 606 EIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEI 685
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 686 KDMKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEwrrfQADLQTAVVVANDI 765
Cdd:COG4942 125 LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE----RAALEALKAERQKL 200
|
170 180 190
....*....|....*....|....*....|...
gi 987976904 766 KCEAQQELRTVKRRLLEEEEKNARLQKELGDMQ 798
Cdd:COG4942 201 LARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
415-800 |
1.47e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 415 AEELQATLQELSDQQQMVQELTAENEKLVDEKTIL--ETSFHQHRERAEQLSHENE-----KLINLLQERVKKEEPGTQE 487
Cdd:TIGR00618 448 TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHlqETRKKAVVLARLLELQEEPcplcgSCIHPNPARQDIDNPGPLT 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 488 GKVLELEQKCTEILEQGRCEREKLLSIQQQLTCSLRKAEEENQ---GAAEMIQRLKEENEKLNGLLELER----QNSGVM 560
Cdd:TIGR00618 528 RRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQsfsILTQCDNRSKEDIPNLQNITVRLQdlteKLSEAE 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 561 AQTLEECTVTLEGLKIE--NGSLKAYLEN-EKQKAIVTSSMGQTAEGCEIQEMLKVARAEKDQLELSCTELKQELLKAHG 637
Cdd:TIGR00618 608 DMLACEQHALLRKLQPEqdLQDVRLHLQQcSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQS 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 638 EIKHVSSLLAKVEKDYSYLKEICDH------QAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNq 711
Cdd:TIGR00618 688 EKEQLTYWKEMLAQCQTLLRELETHieeydrEFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNN- 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 712 liTELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKNARLQ 791
Cdd:TIGR00618 767 --NEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATL 844
|
....*....
gi 987976904 792 KELGDMQGH 800
Cdd:TIGR00618 845 GEITHQLLK 853
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
606-766 |
3.36e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 606 EIQEMLKVARAEKDQLELSCTELKQEL------LKAHGEIKHVSSLL-----AKVEKDYSYLKEICDH---QAEQLSRTS 671
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEELaellraLYRLGRQPPLALLLspedfLDAVRRLQYLKYLAPArreQAEELRADL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 672 LKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRF 751
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
170
....*....|....*
gi 987976904 752 QADLQTAVVVANDIK 766
Cdd:COG4942 240 AERTPAAGFAALKGK 254
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
615-808 |
3.75e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 615 RAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKdysylkeicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFE 694
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASR-----------KIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 695 LEDQVEQHRAVKLHNNQLITELESSVMKLEGQKADLER-----QLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCE- 768
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArlshsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEk 828
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 987976904 769 --AQQELRTVKRRLLEEEEKNARLQKELGDMQGHGSDLQTYL 808
Cdd:TIGR02169 829 eyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL 870
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
402-793 |
4.15e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 402 EKIQKMEENHHSTAEELQATLQELSDQQQMVQEltAENEKLVDE--KTILETSFHQHRERAEQLSHENEKLINLLQERVK 479
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKK--AEEKKKADEakKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 480 KEE---PGTQEGKVLELEQKCTEilEQGRCEREKLLSIQQQLTCSLRKAEEENQgAAEMiqRLKEENEKLNGLLELERQN 556
Cdd:PTZ00121 1472 ADEakkKAEEAKKADEAKKKAEE--AKKKADEAKKAAEAKKKADEAKKAEEAKK-ADEA--KKAEEAKKADEAKKAEEKK 1546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 557 SGVMAQTLEECTVTLEGLKIENgslKAYLENEKQKAIVTSSMGQTAEGCEIQEMLKVARAEKdqlelsctELKQELLKAH 636
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKAEE---AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK--------KMKAEEAKKA 1615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 637 GEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSlklQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHnnqlitEL 716
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE---ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE------ED 1686
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 987976904 717 ESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKN--ARLQKE 793
Cdd:PTZ00121 1687 EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKkiAHLKKE 1765
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
400-804 |
6.84e-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: 43.29 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 400 LTEKIQKMEENHHSTaEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKLINLLQERVK 479
Cdd:pfam12128 463 LLQLENFDERIERAR-EEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLR 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 480 KEEPGTQE--GKVLELEQKC-TEI-------------------LEQGRCEREKLLSIQQQLTCSLRKAEEENQGAAEMIQ 537
Cdd:pfam12128 542 KEAPDWEQsiGKVISPELLHrTDLdpevwdgsvggelnlygvkLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 538 RLKEENEKLNGLLELERQNSGVMAQTLEECTVTLEGLKIENGSLKAYLE-------NEKQKAIVTSSMGQTAEGCEIQEM 610
Cdd:pfam12128 622 AAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNkalaerkDSANERLNSLEAQLKQLDKKHQAW 701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 611 LKvarAEKDQLELSCTELKQELLKAHGEIK-HVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKL---QEKASESDAEIK 686
Cdd:pfam12128 702 LE---EQKEQKREARTEKQAYWQVVEGALDaQLALLKAAIAARRSGAKAELKALETWYKRDLASLgvdPDVIAKLKREIR 778
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 687 DMKETIfeleDQVEQHRAVKLHNNQLITELESSVM-KLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDI 765
Cdd:pfam12128 779 TLERKI----ERIAVRRQEVLRYFDWYQETWLQRRpRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQ 854
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 987976904 766 KCEAQQELRTVKRRL-----LEEEEKNARLQKELGDMQGHGSDL 804
Cdd:pfam12128 855 QVRLSENLRGLRCEMsklatLKEDANSEQAQGSIGERLAQLEDL 898
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
416-806 |
7.38e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 416 EELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKLINLLQERVKKEEPGTQEGKVLELEQ 495
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 496 KCTEILEQGRcEREKLLSIQQQLTCSLRKAEEENQGAAEM-IQRLKEENEKLNGLLELERQNSGVMAQTLEECTVTLEGL 574
Cdd:COG4717 154 RLEELRELEE-ELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 575 KIENGSLKAYLENEKQK-----------------AIVTSSMGQTAEGCEIQEMLKVARAEKDQLELSCTELKQELLKAHG 637
Cdd:COG4717 233 ENELEAAALEERLKEARlllliaaallallglggSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 638 EIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKetifelEDQVEQHRAVKLHNNQL--ITE 715
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ------LEELEQEIAALLAEAGVedEEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 716 LESSVMKLEgQKADLERQLKTLTKQIKEETEEWRRFQADLQTAvvvandikcEAQQELRTVKRRLLEEEEKNARLQKELG 795
Cdd:COG4717 387 LRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEALDEE---------ELEEELEELEEELEELEEELEELREELA 456
|
410
....*....|.
gi 987976904 796 DMQGHGSDLQT 806
Cdd:COG4717 457 ELEAELEQLEE 467
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
417-783 |
1.46e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 417 ELQATLQELSDQ-QQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKLINLLQERVKKEEPGTQEGKVLELEQ 495
Cdd:pfam01576 226 ELQAQIAELRAQlAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALK 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 496 KCTEILEQGRCEREKLLSIQQQLTCSLRKAEEE-----NQGAAEMIQRLKEENEKLNGLLELERQNSgvmaQTLEECTVT 570
Cdd:pfam01576 306 TELEDTLDTTAAQQELRSKREQEVTELKKALEEetrshEAQLQEMRQKHTQALEELTEQLEQAKRNK----ANLEKAKQA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 571 LEGlkiENGSLKAYLENEKQKAIVTSSMGQTAEGcEIQEMlkvaRAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVE 650
Cdd:pfam01576 382 LES---ENAELQAELRTLQQAKQDSEHKRKKLEG-QLQEL----QARLSESERQRAELAEKLSKLQSELESVSSLLNEAE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 651 KDYSYLKEICDHQAEQLSRTSLKLQEKASES---DAEIKDMKETIFELEDQVEQHRAVKlhnnqliTELESSVMKLEGQK 727
Cdd:pfam01576 454 GKNIKLSKDVSSLESQLQDTQELLQEETRQKlnlSTRLRQLEDERNSLQEQLEEEEEAK-------RNVERQLSTLQAQL 526
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 987976904 728 ADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDiKCEAQQELRTVKRRLLEE 783
Cdd:pfam01576 527 SDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEE-KAAAYDKLEKTKNRLQQE 581
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
627-806 |
1.55e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 627 ELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEIcdhqaeqlsRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAvk 706
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQER---------REALQRLAEYSWDEIDVASAEREIAELEAELERLDA-- 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 707 lhNNQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRRLLEEEEK 786
Cdd:COG4913 683 --SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180
....*....|....*....|
gi 987976904 787 NARLQKELGDMQGHGSDLQT 806
Cdd:COG4913 761 DAVERELRENLEERIDALRA 780
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
606-795 |
1.61e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 606 EIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEK-ASESDAE 684
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSgGSVSYLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 685 IKDMKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEwrrfQADLQTAVVVAND 764
Cdd:COG3883 107 VLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA----KAELEAQQAEQEA 182
|
170 180 190
....*....|....*....|....*....|.
gi 987976904 765 IKCEAQQELRTVKRRLLEEEEKNARLQKELG 795
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
397-781 |
1.70e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.75 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 397 LASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLvdEKTILETSfHQHRERAEQLshenEKLINLLQE 476
Cdd:PRK04778 107 INEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYREL--RKSLLANR-FSFGPALDEL----EKQLENLEE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 477 RVKKEEPGTQEGKVLEleqkcteileqgrcerekllsiqqqltcslrkaeeenqgAAEMIQRLKEENEKLNGLLElerqn 556
Cdd:PRK04778 180 EFSQFVELTESGDYVE---------------------------------------AREILDQLEEELAALEQIME----- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 557 sgVMAQTLEECTVTLEGL--KIENGslkaYLENEKQKAIVTSsmgQTAEGcEIQEML-KVARAEKDQLELSCTELKQELL 633
Cdd:PRK04778 216 --EIPELLKELQTELPDQlqELKAG----YRELVEEGYHLDH---LDIEK-EIQDLKeQIDENLALLEELDLDEAEEKNE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 634 KAHGEIKHVSSLLakvEKDYSYLKEIcDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLI 713
Cdd:PRK04778 286 EIQERIDQLYDIL---EREVKARKYV-EKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQLEKQLESLE 361
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 987976904 714 TELESSVMKLEGQKA-------DLERQLKTLTkQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRRLL 781
Cdd:PRK04778 362 KQYDEITERIAEQEIayselqeELEEILKQLE-EIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLE 435
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
394-799 |
2.48e-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: 41.58 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 394 ELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDE-------KTILETSFHQHRERAEQLSHE 466
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKvaqlelqIASLNNEIERLEARLERLEDR 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 467 NEKLINLLQERVKKEEPG---TQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLtcslRKAEEENQGAAEMIQRLKEEN 543
Cdd:TIGR02168 416 RERLQQEIEELLKKLEEAelkELQAELEELEEELEELQEELERLEEALEELREEL----EEAEQALDAAERELAQLQARL 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 544 EKLNGLLELERQNS-GVMAQTLEECT------VTLEGLKIENG---SLKAYLENEKQKAIVTSSmgQTAEgcEIQEMLKV 613
Cdd:TIGR02168 492 DSLERLQENLEGFSeGVKALLKNQSGlsgilgVLSELISVDEGyeaAIEAALGGRLQAVVVENL--NAAK--KAIAFLKQ 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 614 ARAEK-----------DQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYL---------KEICDHQAEQL------ 667
Cdd:TIGR02168 568 NELGRvtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvddLDNALELAKKLrpgyri 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 668 ------------------SRTSLKLQEKASESD---AEIKDMKETIFELEDQVEQHRavklhnnQLITELESSVMKLEGQ 726
Cdd:TIGR02168 648 vtldgdlvrpggvitggsAKTNSSILERRREIEeleEKIEELEEKIAELEKALAELR-------KELEELEEELEQLRKE 720
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 987976904 727 KADLERQLKTLTKQIKEETEE---WRRFQADLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKNARLQKELGDMQG 799
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEveqLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
365-695 |
3.17e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 40.99 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 365 TPSRPLSSTSNPFKS--SKCSTTGSSPnnaSELSLASLTEKIQKMEENHHSTA-------EELQATLQEL----SDQQQM 431
Cdd:PLN03229 429 TPVRELEGEVEKLKEqiLKAKESSSKP---SELALNEMIEKLKKEIDLEYTEAviamglqERLENLREEFskanSQDQLM 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 432 VQELTAENEKLVDEktiletsFHQHRERA---EQLSHENEKLINLLQERVKKEEPGTQEGKVLELEQKCTEILEQGRCeR 508
Cdd:PLN03229 506 HPVLMEKIEKLKDE-------FNKRLSRApnyLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMDRPEI-K 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 509 EKLLSIQQQLtcslrkAEEENQGAAEMIQRLKEENEKLNGLLELErqnsgvMAQTLEECTVTLEGLKIENGSLKAYLENE 588
Cdd:PLN03229 578 EKMEALKAEV------ASSGASSGDELDDDLKEKVEKMKKEIELE------LAGVLKSMGLEVIGVTKKNKDTAEQTPPP 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 589 KQKAIVTSSMGQTAEgcEIQEMLKVAraekdQLELSCTELKQELLKAHGeikhvSSLLAKVEKDYSYLKEICDHQAEQLS 668
Cdd:PLN03229 646 NLQEKIESLNEEINK--KIERVIRSS-----DLKSKIELLKLEVAKASK-----TPDVTEKEKIEALEQQIKQKIAEALN 713
|
330 340
....*....|....*....|....*..
gi 987976904 669 RTSLKlqEKASESDAEIKDMKETIFEL 695
Cdd:PLN03229 714 SSELK--EKFEELEAELAAARETAAES 738
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
372-763 |
4.71e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 40.33 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 372 STSNPFKSSKCSTTGSSPNNASE--LSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELtaenEKLVDEKTIL 449
Cdd:COG5185 190 KGISELKKAEPSGTVNSIKESETgnLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKL----EKLVEQNTDL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 450 ETS-FHQHRERAEQLSHENEKLINLLQERVKKEEPGTQEGKVLELEQKCTEILEQGRCERE---KLLSIQQQLTCSLRKA 525
Cdd:COG5185 266 RLEkLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQEleeSKRETETGIQNLTAEI 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 526 EEENQGAAEMIQRLKEENEKLNGLLELERQnsgvmAQTLEECTVTLEGLKIENGSLKAYLENEKQKAIVTssmgqtaegc 605
Cdd:COG5185 346 EQGQESLTENLEAIKEEIENIVGEVELSKS-----SEELDSFKDTIESTKESLDEIPQNQRGYAQEILAT---------- 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 606 eIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYsylkeicdhQAEQLSRTSLKLQEKASESDAEI 685
Cdd:COG5185 411 -LEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREA---------DEESQSRLEEAYDEINRSVRSKK 480
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 987976904 686 KDMKETIFELEDQVEQHRAvklhnnqlitelessvmKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVAN 763
Cdd:COG5185 481 EDLNEELTQIESRVSTLKA-----------------TLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
390-698 |
6.10e-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: 40.34 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 390 NNASELSLASLTEKIQKMEE--NHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHEN 467
Cdd:pfam02463 732 DKINEELKLLKQKIDEEEEEeeKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 468 EKLINLLQERVKKEepgtQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEKLN 547
Cdd:pfam02463 812 EEAELLEEEQLLIE----QEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDE 887
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 548 GLLELERQNsgvmAQTLEECTVTLEGLKIENGSLKAYLENEKQKAIvtssmgQTAEGCEIQEMLKVARAEKDQLELSCTE 627
Cdd:pfam02463 888 LESKEEKEK----EEKKELEEESQKLNLLEEKENEIEERIKEEAEI------LLKYEEEPEELLLEEADEKEKEENNKEE 957
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 987976904 628 LKQELLKAHGEIKHVSSLLAKVEKDYSYLKEicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQ 698
Cdd:pfam02463 958 EEERNKRLLLAKEELGKVNLMAIEEFEEKEE----RYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLE 1024
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
378-793 |
8.27e-03 |
|
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: 39.70 E-value: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 378 KSSKCSTTGSSPNNASELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTA----------ENEKLVDEKT 447
Cdd:pfam05483 339 ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKfknnkeveleELKKILAEDE 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 448 ILETSFHQHRERAEQLSHENEKLINLLQERVKK-EEPGTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTCSLRKAE 526
Cdd:pfam05483 419 KLLDEKKQFEKIAEELKGKEQELIFLLQAREKEiHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLL 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 527 EEN----QGAAEMIQRLKEENEKLNGLLELERQnsgvMAQTLEECTVTLEGLKIENGSLKAYLENEKQKAIVTSSMGQTA 602
Cdd:pfam05483 499 LENkeltQEASDMTLELKKHQEDIINCKKQEER----MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEEN 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 603 EGCEIQEMLKVARAEKdQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSY------LKEICDHQAE-QLSRTSLKLQ 675
Cdd:pfam05483 575 ARSIEYEVLKKEKQMK-ILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAenkqlnAYEIKVNKLElELASAKQKFE 653
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976904 676 EKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLITELESSVM-KLEGQKADLERQLKTLTKQIKEETEEWRRFQAD 754
Cdd:pfam05483 654 EIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQhKIAEMVALMEKHKHQYDKIIEERDSELGLYKNK 733
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 987976904 755 LQTAVVVANDIKCE---AQQELRTVKRRLLEEEEKNARLQKE 793
Cdd:pfam05483 734 EQEQSSAKAALEIElsnIKAELLSLKKQLEIEKEEKEKLKME 775
|
|
| |
