|
Name |
Accession |
Description |
Interval |
E-value |
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
8-636 |
9.77e-48 |
|
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: 180.76 E-value: 9.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 8 LESRVRELEDMLDLERDARVRAERHAADMSFQVDALSERLDEAGGNSSQTHELLKRREMEIGKLRKDLENANASLEMAET 87
Cdd:pfam01576 269 LEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 88 SMRRRHQTALNELAAEVENLQKQKGKAEKDKNSLIMEVGNVLGQLDGALKAKQSAESKLEGLDAQLNRLKGLTDDLQRQL 167
Cdd:pfam01576 349 EMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQR 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 168 NDLNAAKARLTSENFELLHANQEYEAQVLNLSKSRSSLESAVDDLKRSLDDEAKSRFNLQAQLTSLQMDYDNLQAKYEEE 247
Cdd:pfam01576 429 AELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEE 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 248 SEEASNLRNQVSKFNADLAAMKSKFERELMSkTEEYEELKRKLTLRITELEDTAERERARASNLEKIKAKLTIEIKDLQN 327
Cdd:pfam01576 509 EEAKRNVERQLSTLQAQLSDMKKKLEEDAGT-LEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLV 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 328 EVDSLSAENAELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQLEAENMRLKSQVNDLVDKNAALDRENRQLSDQVK 407
Cdd:pfam01576 588 DLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEME 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 408 DLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAEEALREVDQKYQNAQAALNHLKSEMEQRLREKDEELETLRKST 487
Cdd:pfam01576 668 DLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQL 747
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 488 TRTIEELTVTItEMEVKYKSELSRLKKRYESNIAELELQLDTANKANANLMKENKTLAQRVKDLEAFLEEERRLREAAES 567
Cdd:pfam01576 748 VKQVRELEAEL-EDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILA 826
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42559524 568 NLQASERKRIQLSSEVEELRGALEAADRARKHAENEMNEAQTRVSELTMQVNTLTNDKRRLEGDISVMQ 636
Cdd:pfam01576 827 QSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLE 895
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
8-637 |
4.12e-20 |
|
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: 95.24 E-value: 4.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 8 LESRVRELEDMLDLERDARVRAERHAADMSFQVDALSERLDEAGGNSSQTHELLKRREMEIGKLRKD---LENANASLEM 84
Cdd:pfam01576 73 LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDillLEDQNSKLSK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 85 AETSMRRRHQTALNELAAEVE---NLQKQKGKAEkdknsliMEVGNVLGQLDGALKAKQSAESKLEGLDAQLNRLKGLTD 161
Cdd:pfam01576 153 ERKLLEERISEFTSNLAEEEEkakSLSKLKNKHE-------AMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 162 DLQRQLNDLNAAKARLTSENFELLHANQEYEAQVLNLSKSRSSLESAVDDLKRSLDDEAKSRFNLQAQLTSLQMDYDNLQ 241
Cdd:pfam01576 226 ELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALK 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 242 AKYEEESEEASNLRNQVSKFNADLAAMKSKFERELMSKTEEYEELKRKLTLRITELEDTAERERARASNLEKIKAKLTIE 321
Cdd:pfam01576 306 TELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 322 IKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQLEAENMRLKSQVNDLVDKNAALDRENRQ 401
Cdd:pfam01576 386 NAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSS 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 402 LSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAEEALREVDQKYQNAQAALNHLKSEMEQRLrEKDEELE 481
Cdd:pfam01576 466 LESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALE 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 482 TLRKSTTRTIEELTVTITEMEVKYKsELSRLKKRYESNIAELELQLDTANKANANLMKENKTLAQRVKDLEAFLEEERRL 561
Cdd:pfam01576 545 EGKKRLQRELEALTQQLEEKAAAYD-KLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEE 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 562 REAAESNLQASERKRIQLSSEVEELRGALEAADRARKH----------------------------AENEMNEAQTRVSE 613
Cdd:pfam01576 624 RDRAEAEAREKETRALSLARALEEALEAKEELERTNKQlraemedlvsskddvgknvhelerskraLEQQVEEMKTQLEE 703
|
650 660
....*....|....*....|....
gi 42559524 614 LTMQVNTLTNDKRRLEGDISVMQA 637
Cdd:pfam01576 704 LEDELQATEDAKLRLEVNMQALKA 727
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
8-623 |
1.75e-19 |
|
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: 93.32 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 8 LESRVRELEDMLDLERDARVRAERHAADMSFQVDALSERLDEAGGNSSQTHELLKRREMEIGKLRKDLENANASLEMAET 87
Cdd:pfam01576 466 LESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEE 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 88 SmRRRHQTALNELAAEVENLQKQKGKAEKDKNSLIMEVGNVLGQLDGALKAKQSAESKLEGLDAQLNRLKGLTDDLQRQL 167
Cdd:pfam01576 546 G-KKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEER 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 168 NDLNAAKARLTSENFELLHANQEYEAQVLNLSKSRSSLESAVDDLKRSLDDEAKSRFNLQAQLTSLQMDYDNLQAKYEEE 247
Cdd:pfam01576 625 DRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEEL 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 248 SEEASNLRNQVSKFNADLAAMKSKFERELMSKTEEYEELKRKLTLRITELEDTAERERARASNLEKIKAKLTIEIKDLQN 327
Cdd:pfam01576 705 EDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEA 784
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 328 EVDSLSAENAELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQLEAENMRLKSQVNDLVDKNAALDRENRQLSDQVK 407
Cdd:pfam01576 785 QIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERD 864
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 408 DLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAEEALREVDQKYQNAQAALNHLKSEMEQRlREKDEELETLRKST 487
Cdd:pfam01576 865 ELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAE-RSTSQKSESARQQL 943
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 488 TRTIEELTVTITEMEVKYKSELSRLKKRYESNIAELELQLDTANKANANLMKENKTLAQRVKDLEAFLEEERRLREAAES 567
Cdd:pfam01576 944 ERQNKELKAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKD 1023
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 42559524 568 NLQASERKRIQLSSEVEELRGALEAADRARKHAENEMNEAQTRVSELTMQVNTLTN 623
Cdd:pfam01576 1024 QAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKS 1079
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
6-630 |
5.75e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.46 E-value: 5.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 6 TRLESRVRELEDMLD-LERDARVrAERHAAdmsfqvdaLSERLDEAGGNSSQTHelLKRREMEIGKLRKDLENANASLEM 84
Cdd:COG1196 189 ERLEDILGELERQLEpLERQAEK-AERYRE--------LKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 85 AETSMRRRhQTALNELAAEVENLQKQKGKAEKDKNSLIMEVGNVLGQLDGALKAKQSAESKLEGLDAQLNRLKGLTDDLQ 164
Cdd:COG1196 258 LEAELAEL-EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 165 RQLNDLNAAKARLTSENFELLHANQEYEAQVLNLSKSRSSLESAVDDLKRSLDDEAKSRFNLQAQLTSLQMDYDNLQAKY 244
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 245 EEESEEASNLRNQVSKFNADLAAMKSKFERELMSKTEEYEELKRKLTLRITELEDTAERERARASNLEKIKAKLTIEIKD 324
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 325 LQNEVDslsAENAELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQLEAENMRLKSQVNDLVDKNAALDRENRQLSD 404
Cdd:COG1196 497 LEAEAD---YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGR 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 405 QV-----KDLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAEEALREVDQKYQNAQAALNHLKSEMEQRLREKDE- 478
Cdd:COG1196 574 ATflpldKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEg 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 479 -----------ELETLRKSTTRTIEELTVTITEMEVKYKSELSRLKKRYESNIAELELQLDTANKANANLMKENKTLAQR 547
Cdd:COG1196 654 eggsaggsltgGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 548 VKDLEAFLEEERRLREAAESNLQASERKRIQLSSEVEELRGALEA------AdrarkhAENEMNEAQTRVSELTMQVNTL 621
Cdd:COG1196 734 REELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnlL------AIEEYEELEERYDFLSEQREDL 807
|
....*....
gi 42559524 622 TNDKRRLEG 630
Cdd:COG1196 808 EEARETLEE 816
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-634 |
6.22e-17 |
|
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: 85.11 E-value: 6.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 4 STTRLESRVRELEDMLDLERDARVRAERHAADMS----------FQVDALSERLDEAGGNSSQTHELLKRREMEIGKLRK 73
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQeleekleelrLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 74 DLENANASLEMAETSmRRRHQTALNELAAEVENLQKQKGKAEKDKNSLimevgnvLGQLDGALKAKQSAESKLEGLDAQL 153
Cdd:TIGR02168 310 RLANLERQLEELEAQ-LEELESKLDELAEELAELEEKLEELKEELESL-------EAELEELEAELEELESRLEELEEQL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 154 NRLKGLTDDLQRQLNDLNAAKARLTSENFELLHANQEYEAQVLNLSKSRSslESAVDDLKRSLDDEAKSRFNLQAQLTSL 233
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERL 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 234 QMDYDNLQAKYEEESEEASNLRNQVSKFNADLAAMKSKFER--------------------------ELMSKTEEYEE-- 285
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENlegfsegvkallknqsglsgilgvlsELISVDEGYEAai 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 286 -------------------------LKRKLTLRITELEDTAERERA-----------------RASNLEKIKAKLTIEIK 323
Cdd:TIGR02168 540 eaalggrlqavvvenlnaakkaiafLKQNELGRVTFLPLDSIKGTEiqgndreilkniegflgVAKDLVKFDPKLRKALS 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 324 DLQNE---VDSLsAENAELARRAKAAEN---LANDLQRR--------------VDELTIEINNLHSQNSQLEAENMRLKS 383
Cdd:TIGR02168 620 YLLGGvlvVDDL-DNALELAKKLRPGYRivtLDGDLVRPggvitggsaktnssILERRREIEELEEKIEELEEKIAELEK 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 384 QVNDLVDKNAALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAEEALREVDQKYQNAQAALN 463
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 464 HLKSEMEQrLREKDEELETLRKSTTRTIEELTVTITEMEVKYKSELSRLkKRYESNIAELELQLDTANKANANLMKENKT 543
Cdd:TIGR02168 779 EAEAEIEE-LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL-ESLERRIAATERRLEDLEEQIEELSEDIES 856
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 544 LAQRVKDLEAFLEEERRLREAAESNLQASERKRIQLSSEVEELRGALEAADRARKHAENEMNEAQTRVSELTMQVNTLTN 623
Cdd:TIGR02168 857 LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV 936
|
730
....*....|.
gi 42559524 624 DKRRLEGDISV 634
Cdd:TIGR02168 937 RIDNLQERLSE 947
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
8-621 |
3.43e-16 |
|
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: 82.80 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 8 LESRVRELEDMLDLERDARVRAERHAADMSFQVDALSERLDEAGGNSSQTHEllkrremEIGKLRKDLENANaslemaet 87
Cdd:TIGR02168 370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ-------EIEELLKKLEEAE-------- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 88 smRRRHQTALNELAAEVENLQKQKGKAEKDKNSLIMEVGNVLGQLDGALKAKQSAESKLEGLDAQLNRLKGLTDDLQRQL 167
Cdd:TIGR02168 435 --LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 168 N---DLNAAKARLTsenfELLHANQEYEAQVLN---------LSKSRSSLESAVDDLKRSldDEAKSRFNLQAQLTSLQM 235
Cdd:TIGR02168 513 KnqsGLSGILGVLS----ELISVDEGYEAAIEAalggrlqavVVENLNAAKKAIAFLKQN--ELGRVTFLPLDSIKGTEI 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 236 DYDNLQAKYEEESEE--ASNLRNQVSKFNADLAAMkskFERELMSKT-EEYEELKRKLT--LRITELED---------TA 301
Cdd:TIGR02168 587 QGNDREILKNIEGFLgvAKDLVKFDPKLRKALSYL---LGGVLVVDDlDNALELAKKLRpgYRIVTLDGdlvrpggviTG 663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 302 ERERARASNLEKIK--AKLTIEIKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQLEAENM 379
Cdd:TIGR02168 664 GSAKTNSSILERRReiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 380 RLKSQVNDLVDKNAALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAEEALREVDQKYQNAQ 459
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 460 AALNHLKSEMEqRLREKDEELETLRKSTTRTIEELTVTITEMEVKYKSELSRLKKRYESnIAELELQLDTANKANANLMK 539
Cdd:TIGR02168 824 ERLESLERRIA-ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE-RASLEEALALLRSELEELSE 901
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 540 ENKTLAQRVKDLEAFLEEERRLREAAESNLQASERKRIQLSSEV-EELRGALEAADRARKHAENEMNEAQTRVSELTMQV 618
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
...
gi 42559524 619 NTL 621
Cdd:TIGR02168 982 KEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
139-630 |
7.79e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.52 E-value: 7.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 139 KQSAESKLEGLDAQLNRLKGLTDDLQRQLNDL-----NAAKARLTSENFELLHAnqeyEAQVLNLSKSRSSLESAVDDLK 213
Cdd:COG1196 174 KEEAERKLEATEENLERLEDILGELERQLEPLerqaeKAERYRELKEELKELEA----ELLLLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 214 RslddeaksrfnLQAQLTSLQMDYDNLQAKYEEESEEASNLRNQVSKFNADLAAMKSKFERELMSKTEEyEELKRKLTLR 293
Cdd:COG1196 250 E-----------LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL-EERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 294 ITELEDTAERERARASNLEKIKAKLTIEIKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQ 373
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 374 LEAENMRLKSQVNDLVDKNAALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAEEALREVDQ 453
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 454 KYQNAQAALNHLKSEMEQRLREKDEELETLRKSTTRTIEELTVTITEmevkYKSELSRLKKRYESNIAELelqldtankA 533
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG----AVAVLIGVEAAYEAALEAA---------L 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 534 NANLMKENKTLAQRVKDLEAFLEEERRLREAAESNLQASERKRIQLSSEVEELRGALEAADRARKHAENEMNEAQTRVSE 613
Cdd:COG1196 545 AAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG 624
|
490
....*....|....*..
gi 42559524 614 LTMQVNTLTNDKRRLEG 630
Cdd:COG1196 625 RTLVAARLEAALRRAVT 641
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
62-632 |
5.87e-15 |
|
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: 78.52 E-value: 5.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 62 KRREMEIGKLRKDLENANASLEMAETSMRRRHQ--TALNELAAEVENLQKQKGKAEKDKNSLIMEVGNVLGQLDGALKAK 139
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEkiNNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKND 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 140 QSAESKLEgldAQLNRLKGLTDDLQRQLNDLNAAKARLTSENFELLHANQEYEAQVLNLSKSRSSLESAVDDLKRSLDDE 219
Cdd:TIGR04523 116 KEQKNKLE---VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 220 AKSRFNLQAQLTSLQM---DYDNLQAKYEEESEEASNLRNQVSKFNADLAAMKSKFER---ELMSKTEEYEELKRKLTLR 293
Cdd:TIGR04523 193 KNKLLKLELLLSNLKKkiqKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNtqtQLNQLKDEQNKIKKQLSEK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 294 ITELEDTaereRARASNLEKIKAKLTIEIKDLQN--EVDSLSAENAELARRAKAAENLANDL---QRRVDELTIEINNLH 368
Cdd:TIGR04523 273 QKELEQN----NKKIKELEKQLNQLKSEISDLNNqkEQDWNKELKSELKNQEKKLEEIQNQIsqnNKIISQLNEQISQLK 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 369 SQNSQLEAENMRLKSQVNDLVDKNAALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAErdnlasaLHDAEEAL 448
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQ-------IKKLQQEK 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 449 REVDQKYQNAQAALNHLKSEMEqRLREKDEELETLRKSTTRTIEELTVTITEMEVKYKSElsrlkkryESNIAELELQLD 528
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIK-DLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKI--------KQNLEQKQKELK 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 529 TANKANANLMKENKTLAQRVKDLEAFLEEERRLREAAESNLQASERKRIQLSSEVEELRGALEaadraRKHAENEMNEAQ 608
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK-----KENLEKEIDEKN 567
|
570 580
....*....|....*....|....
gi 42559524 609 TRVSELTMQVNTLTNDKRRLEGDI 632
Cdd:TIGR04523 568 KEIEELKQTQKSLKKKQEEKQELI 591
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
94-550 |
4.21e-13 |
|
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: 72.36 E-value: 4.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 94 QTALNELAAEVENLQKQKGKAEKDKNSLIMEVGNVLGQLDGALKAKQSAESKLEGLDAQLNRLKGLTDDLQRQLNDLNAA 173
Cdd:TIGR04523 217 ESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 174 KARLTSENFELLHAN------------QEYEAQVLNLSKSRSSLESAVDDLKRSLDDEAKSRFNLQAQLTSLQMDYDNLQ 241
Cdd:TIGR04523 297 ISDLNNQKEQDWNKElkselknqekklEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 242 AKYEEESEEASNLRNQVSKFNADLAAMKsKFERELMSKTEEYEELKRKLTLRITELEDTAERERARASNLEKIKAKLTIE 321
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQNQE-KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 322 IKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQLEAENMRLKSQVNDLVDKNAALDRENRQ 401
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 402 LSDQVKDLKSTLRDANRRLTdlealRSQLEAERDNLASALhdaeealrevdQKYQNAQAALNHLKSEMEQRLREKDEELE 481
Cdd:TIGR04523 536 KESKISDLEDELNKDDFELK-----KENLEKEIDEKNKEI-----------EELKQTQKSLKKKQEEKQELIDQKEKEKK 599
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42559524 482 TLRK---STTRTIEELTVTITEMEVKYK---SELSRLKKRYESNIAELEL---QLDTANKANANLMKENKTLAQRVKD 550
Cdd:TIGR04523 600 DLIKeieEKEKKISSLEKELEKAKKENEklsSIIKNIKSKKNKLKQEVKQikeTIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
303-630 |
3.85e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 303 RERARASNLEKIKAKLTIEIKDLQNEVDSLSAENA-----ELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQLEAE 377
Cdd:TIGR02168 196 NELERQLKSLERQAEKAERYKELKAELRELELALLvlrleELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 378 NMRLKSQVNDLVDKNAALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAEEALREVDQKYQN 457
Cdd:TIGR02168 276 VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 458 AQAALNHLKS---EMEQRLREKDEELETLRK---STTRTIEELTVTITEMEvkykSELSRLKKRYESNIAELELQLDTAN 531
Cdd:TIGR02168 356 LEAELEELEAeleELESRLEELEEQLETLRSkvaQLELQIASLNNEIERLE----ARLERLEDRRERLQQEIEELLKKLE 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 532 KAnanlmkenktlaqRVKDLEAFLEEERRLREaaesnlqaserkriQLSSEVEELRGALEAADRARKHAENEMNEAQTRV 611
Cdd:TIGR02168 432 EA-------------ELKELQAELEELEEELE--------------ELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
330
....*....|....*....
gi 42559524 612 SELTMQVNTLTNDKRRLEG 630
Cdd:TIGR02168 485 AQLQARLDSLERLQENLEG 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-564 |
6.45e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 6.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 7 RLESRVRELEDMLDLERDARVRAERHAADMSFQVDALSERLDEAGGNSSQTHELLKRREMEIGKLRKDLENANASLEMAE 86
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 87 tsmrrrhqTALNELAAEVENLQKQKGKAEKDKNSLIMEVGNVLGQLDGALKAKQSAESKLEGLDAQLNRLKGLTDDLQRQ 166
Cdd:COG1196 351 --------EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 167 LNDLNAAKARLTSENFELLHANQEYEAQVLNLSKSRSSLESAVDDLKRSLDDEAKSRFNLQAQLTSLQMDYDNLQAKYEE 246
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 247 ESEEASNLRNQVSKFNADLAAMKSKFERELMSKTEEYEELKRKLTLRITELEDTAERERARASNLEKIKAKLTIEIKDLQ 326
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKI 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 327 nEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEINNLHSQNS---QLEAENMRLKSQVNDLVDKNAALDRENRQLS 403
Cdd:COG1196 583 -RARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLvaaRLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 404 DQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAEEALREVDQKYQNAQAALNHLKSEMEQRLREKDEELETL 483
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 484 RKSTTRTIEELTVTITEMEV--KYKSELSRLKKRYES----NIAELElQLDTANKANANLMKENKTLAQRVKDLEAFLEE 557
Cdd:COG1196 742 LEEEELLEEEALEELPEPPDleELERELERLEREIEAlgpvNLLAIE-EYEELEERYDFLSEQREDLEEARETLEEAIEE 820
|
570
....*....|..
gi 42559524 558 -----ERRLREA 564
Cdd:COG1196 821 idretRERFLET 832
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
143-500 |
8.39e-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: 68.54 E-value: 8.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 143 ESKLEGLDAQLNRLKGLTDDLQRQLNDLNAAKARLTSENFELLHANQEYEAQVLNLSKSRSSLESAVDDLKRSLDDEAKS 222
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 223 RFNLQAQLTSLQMDYDNLQAKYEEESEEASNLRNQVSKFNADLAAmkskFERELMSKTEEYEELKR---KLTLRITELED 299
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA----LREALDELRAELTLLNEeaaNLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 300 TAERERARASNLEKIKAKLTIEIKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQLEAENM 379
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 380 RLKSQVNDLVDKNAALDRENRQLSDQVKDLKSTLR-DANRRLTDLEALRSQLEAERDNLASALHDAEEALREVDQKYQNA 458
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAA 991
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 42559524 459 QAALNHLKSEMEQrLREKDEELETLRKSTTRTIEELTVTITE 500
Cdd:TIGR02168 992 IEEYEELKERYDF-LTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
50-452 |
9.06e-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: 68.54 E-value: 9.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 50 AGGNSSQTHELLKRREmEIGKLRKDLENANASLEMAETsmrrrhqtALNELAAEVENLQKQKGKAEKDKNSLIMEVGNVL 129
Cdd:TIGR02168 662 TGGSAKTNSSILERRR-EIEELEEKIEELEEKIAELEK--------ALAELRKELEELEEELEQLRKELEELSRQISALR 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 130 GQLDGALKAKQSAESKLEGLDAQLNRLKGLTDDLQRQLNDLNAAKARLTSENFELLHANQEYEAQVLNLSKSRSSLESAV 209
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 210 DDLKRSLDDEAKSRFNLQAQLTSLQMDYDNLQAKYEEESEEASNLRNQVSKFNADLAamksKFERELMSKTEEYEELKRK 289
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE----ELESELEALLNERASLEEA 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 290 LTLRITELEDtaererarasnlekikakltieikdLQNEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEINNLHS 369
Cdd:TIGR02168 889 LALLRSELEE-------------------------LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 370 Q-NSQLEAENMRLKSQVNDLVDKNAALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAEEAL 448
Cdd:TIGR02168 944 RlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAI 1023
|
....
gi 42559524 449 REVD 452
Cdd:TIGR02168 1024 EEID 1027
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
250-591 |
1.06e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 250 EASNLRNQVSKFNADLAAMKSKFErELMSKTEEYEELKRKLTLRITELED-------TAERERARASNLEKIKAKLTIEI 322
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALA-ELRKELEELEEELEQLRKELEELSRqisalrkDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 323 KDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQLEAENMRLK-------SQVNDLVDKNAAL 395
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeaanlrERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 396 DRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAEEALREVDQKYQNAQAALNhlksEMEQRLRE 475
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR----ELESKRSE 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 476 KDEELETLRKSttrtIEELTVTITEMEVKYKSELSRLKKRYEsniAELELQLDTANKANANLMKenktLAQRVKDLEAFL 555
Cdd:TIGR02168 913 LRRELEELREK----LAQLELRLEGLEVRIDNLQERLSEEYS---LTLEEAEALENKIEDDEEE----ARRRLKRLENKI 981
|
330 340 350
....*....|....*....|....*....|....*.
gi 42559524 556 EEERRLREAAESNLQASERKRIQLSSEVEELRGALE 591
Cdd:TIGR02168 982 KELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKE 1017
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
273-633 |
1.22e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 273 ERELMSKTEEYEELKRKltlrITELEDTAERERARASNLEKIKAKLTIEIKDLQNEVDSLSAENAELARRAKAAENLAND 352
Cdd:TIGR02168 676 RREIEELEEKIEELEEK----IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 353 LQRRVDELTIEINNLHSQNSQLEAENMRLKSQVndlvdknAALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEA 432
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEI-------EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 433 ERDNLASALHDAEEALREVDQKYQNAQ---AALNHLKSEMEQRLREKDEELETLRKSTTRTIEELTVTITEMEvkyksEL 509
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSediESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE-----EL 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 510 SRLKKRYESNIAELELQLDTANKANANL-MKENKTLAQRVKDLEAFLEEERRLREAAESNLQASERKRIQLSSEVEELRG 588
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQLeLRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 42559524 589 ALEAADRARKHAENEMNEAQTRVSELTMQVNTLTNDKRRLEGDIS 633
Cdd:TIGR02168 980 KIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIE 1024
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
96-637 |
2.54e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.00 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 96 ALNELAAEVENLQKQKGKAEKDKnslimEVGNVLGQLDGALKAKQsaeskLEGLDAQLNRLKGLTDDLQRQLNDLNAAKA 175
Cdd:TIGR02168 194 ILNELERQLKSLERQAEKAERYK-----ELKAELRELELALLVLR-----LEELREELEELQEELKEAEEELEELTAELQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 176 RLTSENFELLHANQEYEAQVLNLSKSRSSLESAVDDLKRSLDDEAKSRFNLQAQLTSLQMDYDNLQAKYEEESEEASNLR 255
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 256 NQVSKFNADLAAMKSKFERelmsKTEEYEELKRKLTLRITELEDTAERERARASNLEKIKAKLT---IEIKDLQNEVDSL 332
Cdd:TIGR02168 344 EKLEELKEELESLEAELEE----LEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIErleARLERLEDRRERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 333 SAENAELARRAKAAEnlANDLQRRVDELTIEINNLHSQNSQLEAENMRLKSQVNDLVDKNAALDRENRQLS---DQVKDL 409
Cdd:TIGR02168 420 QQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarlDSLERL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 410 KSTLRDANRRLTDLEALRSQLEAERDNLASALHDAEE-------ALRE-----VDQKYQNAQAALNHLKSEMEQR----- 472
Cdd:TIGR02168 498 QENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyeaaieaALGGrlqavVVENLNAAKKAIAFLKQNELGRvtflp 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 473 LREKDEELETLRKSTTRTIEELTVTITEMEVKYKSELS--------------------RLKKRYESNIAELELQLDTANK 532
Cdd:TIGR02168 578 LDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvddldnalELAKKLRPGYRIVTLDGDLVRP 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 533 ANANLMKENKTLAQRVKdLEAFLEEERRLREAAESNLQASERKRIQLSSEVEELRGALEAADRARKHAENEMNEAQTRVS 612
Cdd:TIGR02168 658 GGVITGGSAKTNSSILE-RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
570 580
....*....|....*....|....*
gi 42559524 613 ELTMQVNTLTNDKRRLEGDISVMQA 637
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEA 761
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
130-487 |
2.80e-11 |
|
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: 67.02 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 130 GQLDGALKAKQSAESKLEGLDAQLNRLKGLTDDLQRQLNDLNAAKARLTSENFELLHANQEYEAQVLNLSKSRSSLESAV 209
Cdd:TIGR02169 653 GAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEE 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 210 DDLKRSLDDEAKSRFNLQAQLTSLQMDYDNLQAKYEEESEEASNLRNQVSKFNADLAAMKSKFERELMSKTEEY----EE 285
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEvsriEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 286 LKRKLTLRITELEDTAERERARASNLEKIKAKLTIEIKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEIN 365
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 366 NLHSQNS-------QLEAENMRLKSQVNDLVDKNAALDRENRQLSDQVKDLKSTlRDANRRLTDLEALRSQLEAERDNLA 438
Cdd:TIGR02169 893 ELEAQLRelerkieELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI-PEEELSLEDVQAELQRVEEEIRALE 971
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 42559524 439 SALHDAEEALREVDQKYQNAQAALNHLKSEMEQrLREKDEELETLRKST 487
Cdd:TIGR02169 972 PVNMLAIQEYEEVLKRLDELKEKRAKLEEERKA-ILERIEEYEKKKREV 1019
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
128-460 |
3.08e-11 |
|
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: 66.63 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 128 VLGQLDGALKAKQSAESKLEGLDAQLNRLKGLTDDLQRQLnDLNAAKARLtsENFELLHANQEYEAQVLNLSKSRSSLES 207
Cdd:TIGR02169 175 ALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQ-ALLKEKREY--EGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 208 AVDDLKRSLDDEAKsrfnlqaQLTSLQMDYDNLQAKYEEESEEASN-LRNQVSKFNADLAAMKSKfERELMSKTEEYEEL 286
Cdd:TIGR02169 252 ELEKLTEEISELEK-------RLEEIEQLLEELNKKIKDLGEEEQLrVKEKIGELEAEIASLERS-IAEKERELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 287 KRKLTLRITELEDTAERERARASNLEKIKAKLTIEIKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEINN 366
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 367 LHSQNSQLEAENMRLKSQVNDLVDKNAALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAEE 446
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483
|
330
....*....|....
gi 42559524 447 ALREVDQKYQNAQA 460
Cdd:TIGR02169 484 ELSKLQRELAEAEA 497
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
98-621 |
3.94e-11 |
|
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: 66.20 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 98 NELAAEVENLQKQKGKAEKDKNSLIMEVGNVLGQLDGALKAKQSAESKLEGLDAQLNRLKGLTDDLQRQLNDLNAAKARL 177
Cdd:TIGR04523 120 NKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 178 TSENFELLHANQEY---EAQVLNLSKSRSSLESAVDDLKRSLDDEAKSRFNLQAQLTSLQMDYDNLQAKYEEESEEASNL 254
Cdd:TIGR04523 200 ELLLSNLKKKIQKNkslESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 255 RNQVSKFNADLAAMKSKFERelmSKTEEYEELKRKLTLRITELEDTAERERARASNLEKIKAKLTIEIKDLQNEVDSLSA 334
Cdd:TIGR04523 280 NKKIKELEKQLNQLKSEISD---LNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 335 ENAELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQLEAENMRLKSQVNDLVDKNAALDRENRQLSDQVKDLKSTLR 414
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 415 DANRRLTDLEALRSQLEAERDNLASALHDAEEALREVDQKYQNAQAALNHLKSEMEQR-------------LREKDEELE 481
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKekelkklneekkeLEEKVKDLT 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 482 TLRKSTTRTIEELTVTITEMEVKYKSELSRLKK---------------RYESNIAELELQLDTANKANANLMKENKTLAQ 546
Cdd:TIGR04523 517 KKISSLKEKIEKLESEKKEKESKISDLEDELNKddfelkkenlekeidEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK 596
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42559524 547 RVKDLEAFLEEERRLREAAESNLQASERKRIQLSSEVEELRGALEAADRARKHAENEMNEAQTRVSELTMQVNTL 621
Cdd:TIGR04523 597 EKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKES 671
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-375 |
1.20e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 7 RLESRVRELEDMLDLERDARVRAERHAADMSFQVDALSERLDEAGGNSSQTHELLKRREMEIGKLrkdlenanaslemae 86
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL--------------- 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 87 TSMRRRHQTALNELAAEVENLQKQKGKAEKDKNSLIMEVGNVLGQLDGALKAKQSAESKLEGLDAQLNRLKGLTDDLQRQ 166
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 167 LNDLNAAKARLTSENFELLHANQEYEAQVLNLSKSRSSLESAVDDLKRSLDDEAKSRFNLQAQLTSLQMDYDNLQAKYEE 246
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 247 ESEEASNLRNQVskfnadlaamkskfeRELMSKTEEYEELKRKLTLRITELEDT-AERERARASNLEKIKAKLTIEIKDL 325
Cdd:TIGR02168 906 LESKRSELRREL---------------EELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEA 970
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 42559524 326 QNEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQLE 375
Cdd:TIGR02168 971 RRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
204-552 |
3.69e-10 |
|
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: 63.16 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 204 SLESAVDDLKRSLDDEAKSRFNLQAQLTSLQMDYDNLQAKYEEESEEASNLRNQVSKFNADLAamksKFERELMSKTEEY 283
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE----KLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 284 EELKRKLTLRITELEDTAERERARASNLEKIKAKL-TIEIKDLQNEVDSLSAENAELarrakaaENLANDLQRRVDELTI 362
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALnDLEARLSHSRIPEIQAELSKL-------EEEVSRIEARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 363 EINNLHSQNSQLEAENMRLKSQVNDLVDKNAALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALH 442
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 443 DAEEALREVDQKYQNAQAALNHLK---SEMEQRLREKDEELETLRKSTTRT--IEELTVTITEMEVKYKSeLSRLKKRYE 517
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKaklEALEEELSEIEDPKGEDEEIPEEElsLEDVQAELQRVEEEIRA-LEPVNMLAI 978
|
330 340 350
....*....|....*....|....*....|....*
gi 42559524 518 SNIAELELQLDTANKANANLMKENKTLAQRVKDLE 552
Cdd:TIGR02169 979 QEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
4-629 |
4.43e-10 |
|
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: 62.83 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 4 STTRLESRVRELEDMLDLERDARVRAERHAADMSFQVDALSERLDEAggnSSQTHELLKRREMEIGKLRK---------- 73
Cdd:pfam15921 111 SVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAA---KCLKEDMLEDSNTQIEQLRKmmlshegvlq 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 74 -------DLENANASLEMAETSMRRRH--------QTALNELAAEVENLQKQKGKAEKDKNSLIMEVGNVLGQLdgalka 138
Cdd:pfam15921 188 eirsilvDFEEASGKKIYEHDSMSTMHfrslgsaiSKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELL------ 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 139 KQSAESKLEGLDAQLN-RLKGLTDDLQRQLNDLNAAKARLTSENFELLHANQEYEAQVLNLSKSRSSLESAVDDLKRSLD 217
Cdd:pfam15921 262 LQQHQDRIEQLISEHEvEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYE 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 218 DEAKSrfnLQAQLTSLQMDYDNLQAKYEEESEEASNLRNQVSKFNADLaamkSKFERELMSKTEEYEELkrkltlritel 297
Cdd:pfam15921 342 DKIEE---LEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADL----HKREKELSLEKEQNKRL----------- 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 298 edtAERERARASNLEKIKAKL---TIEIKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDELTieinnlhsqnSQL 374
Cdd:pfam15921 404 ---WDRDTGNSITIDHLRRELddrNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLT----------AQL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 375 EAENMRLKSQVNDLVDKNAALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLasalhdaeEALREVDQK 454
Cdd:pfam15921 471 ESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQEL--------QHLKNEGDH 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 455 YQNAQAALNHLKSEMEQR------LREKDEELETLRKSTTRTIEELTVTITEMEVKYK------SELSRLKKRYESNIAE 522
Cdd:pfam15921 543 LRNVQTECEALKLQMAEKdkvieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINdrrlelQEFKILKDKKDAKIRE 622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 523 LE-----LQLDTANKANA---------NLMKENKTLAQRVK----DLEAFLEE----ERRLREAAESNLQASERKRIQL- 579
Cdd:pfam15921 623 LEarvsdLELEKVKLVNAgserlravkDIKQERDQLLNEVKtsrnELNSLSEDyevlKRNFRNKSEEMETTTNKLKMQLk 702
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 42559524 580 --SSEVEELRGALEAADRARKHAENEMNEAQTRVSELTMQVNTLTNDKRRLE 629
Cdd:pfam15921 703 saQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLE 754
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
75-445 |
6.22e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.39 E-value: 6.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 75 LENANASLEMAETSMRRrHQTALNELAAEVENLQKQKGKAEKDKnSLIMEVGNVLGQLdgALKAKQSAESKLEGLDAQLN 154
Cdd:TIGR02169 172 KEKALEELEEVEENIER-LDLIIDEKRQQLERLRREREKAERYQ-ALLKEKREYEGYE--LLKEKEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 155 RLKGLTDDLQRQLNDLnaakarltsenfellhaNQEYEAqvlnlsksrssLESAVDDLKRSLDDEAKSRFN-LQAQLTSL 233
Cdd:TIGR02169 248 SLEEELEKLTEEISEL-----------------EKRLEE-----------IEQLLEELNKKIKDLGEEEQLrVKEKIGEL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 234 QMDYDNLQAKYEEESEEASNLRNQVSKFNADLAAMKSKFErELMSKTEEYEELKRKLTLRITELEDTAERERARASNLEK 313
Cdd:TIGR02169 300 EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE-ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 314 IKAKLTIEIKDLQNEVDSLSAEnaelarrakaaenlANDLQRRVDELTIEINNLHSQNSQLEAENMRLKSQVNDLVDKNA 393
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKRE--------------INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE 444
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 42559524 394 ALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAE 445
Cdd:TIGR02169 445 DKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
28-636 |
1.37e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 28 RAERHAADMSFQVDALSERLDEAGGNSSQTHELLKRR--------EMEIGKLRKDLENANASLEMAETSM------RRRH 93
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERSIAEKERELedaeerLAKL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 94 QTALNELAAEVENLQKQKGKAEKDKNSLIMEVGNVLGQLDGALKAKQSAESKLEGLDAQLNRLKGLTDDLQRQLNDLNAA 173
Cdd:TIGR02169 328 EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRE 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 174 KARLTSENFELLHANQEYEAQVLNLSKSRSSLESAVDDLKRSLDDEAKSRFNLQAQLTSLQMDYDNLQAKYEEESEEASN 253
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 254 LRNQVSKFNADLAAMKSKFE--------------------RELMSKTEEY---------------------------EEL 286
Cdd:TIGR02169 488 LQRELAEAEAQARASEERVRggraveevlkasiqgvhgtvAQLGSVGERYataievaagnrlnnvvveddavakeaiELL 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 287 KRKLTLRITELEDTAERERARASNLEKIKAKLTIEI------KDLQNEV-----DSLSAENAELARRAKAAE---NLAND 352
Cdd:TIGR02169 568 KRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVdlvefdPKYEPAFkyvfgDTLVVEDIEAARRLMGKYrmvTLEGE 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 353 LQRRVDELTIEINNLHSQNS---QLEAENMRLKSQVNDLVDKNAALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQ 429
Cdd:TIGR02169 648 LFEKSGAMTGGSRAPRGGILfsrSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 430 LEAERDNLASALHDAEEALREVDQKYQNAQAALNHLKSEMEQRLREKDEELETLRKSTTRTIEELTVTITEMEVKYKSEL 509
Cdd:TIGR02169 728 LEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEV 807
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 510 SRLKKRyesnIAELELQLDTANKANANLMKENKTLAQRVKDLEAFLEEERRLREAAESNLQASERKRIQLSSEVEELRGA 589
Cdd:TIGR02169 808 SRIEAR----LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 42559524 590 LEAADRARKHAENEMNEAQTRVSELTMQVNTLTNDKRRLEGDISVMQ 636
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
9-614 |
1.81e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 9 ESRVRELEDMLDLERDARvrAERHAADMSFQVDALSERLDEAGGNSSQTHELLKRREMEIGKLRKDLENANASLE--MAE 86
Cdd:PRK03918 145 ESREKVVRQILGLDDYEN--AYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPelREE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 87 TSMRRRHQTALNELAAEVENLQKQKGKAEKDKNSLIMEVGNVLGQLDGALKAKQSAESK------LEGLDAQLNRLKGLT 160
Cdd:PRK03918 223 LEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkelkeLKEKAEEYIKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 161 DDLQRQLNDLNAAKARLTSENFEL---LHANQEYEAQVLNLSKSRSSLESAVDDLKRSLD--DEAKSRFNLQAQLTSLQM 235
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIeerIKELEEKEERLEELKKKLKELEKRLEELEERHElyEEAKAKKEELERLKKRLT 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 236 DY--DNLQAKYEEESEEASNLRNQVSKFNADLAAMKSKfERELMSKTEEYEELKRKLTLRITELEDTAERErarasnlek 313
Cdd:PRK03918 383 GLtpEKLEKELEELEKAKEEIEEEISKITARIGELKKE-IKELKKAIEELKKAKGKCPVCGRELTEEHRKE--------- 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 314 IKAKLTIEIKDLQNEVDSLSAENAELARRAKAAENLANDLQR--RVDELTIEINNLHSQNSQLEAENMRLKS-QVNDLVD 390
Cdd:PRK03918 453 LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEELEKKAeEYEKLKE 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 391 KNAALDRENRQLSDQVK---DLKSTLRDANRRLTDLEALRSQLEAERDNLA-SALHDAEEALREVDQKYQNAQAALNhlk 466
Cdd:PRK03918 533 KLIKLKGEIKSLKKELEkleELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKD--- 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 467 seMEQRLREKDEELETLRKSTTRTIEELTVTITEMEvKYKSELSRLKKRYesniaelelqldtANKANANLMKENKTLAQ 546
Cdd:PRK03918 610 --AEKELEREEKELKKLEEELDKAFEELAETEKRLE-ELRKELEELEKKY-------------SEEEYEELREEYLELSR 673
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42559524 547 RVKDLEAFLEEERRLREAAESNLqaserkriqlssevEELRGALEAADRARKHAENeMNEAQTRVSEL 614
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTL--------------EKLKEELEEREKAKKELEK-LEKALERVEEL 726
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
264-530 |
1.88e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 264 DLAAMKSKFERELMSKTEEYEELKRKLTLRITELEdtaERERARASNLEKIKAKLTIEIKDLQNEVDSLSAENAELARRA 343
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLE---EIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 344 KAAENLANDLQRRVDELTIEINNLHSQNSQLEAENMRLKSQVNDLVDKNAALDRENRQLSDQVKDLKSTLRDANRRLTDL 423
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 424 EALRSQLEAERDNLASALHDAEEALREVDQKYQNAQAALNHLksemEQRLREKDEELETLRKStTRTIEELTVTITEMEV 503
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI----EAKINELEEEKEDKALE-IKKQEWKLEQLAADLS 465
|
250 260 270
....*....|....*....|....*....|
gi 42559524 504 KYKSELSRLK---KRYESNIAELELQLDTA 530
Cdd:TIGR02169 466 KYEQELYDLKeeyDRVEKELSKLQRELAEA 495
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
189-618 |
8.06e-09 |
|
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: 58.98 E-value: 8.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 189 QEYEAQVLNLSKSRSSLESAVDDLKRSLddeAKSRFNLQAQLTSLQMDYDNLQAKYEEESEEASNLRNQVSKFNADLAAM 268
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNELHEKQKFYL---RQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 269 KSKFERELMSKTEEYEELkRKLTLR-----------ITELEDTAERE------------RARASNLEKIKAKLTIEIKDL 325
Cdd:pfam15921 158 KCLKEDMLEDSNTQIEQL-RKMMLShegvlqeirsiLVDFEEASGKKiyehdsmstmhfRSLGSAISKILRELDTEISYL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 326 QNEV----DSLSAENAELARRAKAAENLAND-LQRRVDELTIEINNLHSQNSQLEAENMRLKSQVNDLVD----KNAALD 396
Cdd:pfam15921 237 KGRIfpveDQLEALKSESQNKIELLLQQHQDrIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEqarnQNSMYM 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 397 RENRQLSDQVKDLKSTLRDANRRLTD-LEALRSQLEAERDNLASALHDAEEALRE---VDQKYQNAQAALNH------LK 466
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMYEDkIEELEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKLLADLHKrekelsLE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 467 SEMEQRLREKDEELETLRKSTTRTIEELTVTITEMEVKYKSELSRLKKRYESNIAELELQ---LDTANKANANLMKENKT 543
Cdd:pfam15921 397 KEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKnesLEKVSSLTAQLESTKEM 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 544 LAQRVKDLEA---FLEEERRLREAAESNLQASERKRIQLSSEVEELRGALEAADRARKHAENE---MNEAQTRVSELTMQ 617
Cdd:pfam15921 477 LRKVVEELTAkkmTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQ 556
|
.
gi 42559524 618 V 618
Cdd:pfam15921 557 M 557
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
7-509 |
1.19e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 7 RLESRVRELEDMLDLERDARVRAERhaadmsfQVDALSERLDEaggnSSQTHELLKRREMEIGKLRKDLENANASLEMAE 86
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARE-------TRDEADEVLEE----HEERREELETLEAEIEDLRETIAETEREREELA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 87 TSMRRRHQTALnELAAEVENLQKQKGKAEKDKNSlimevgnVLGQLDGALKAKQSAESKLEGLDAQLNRLKGLTDDLQRQ 166
Cdd:PRK02224 279 EEVRDLRERLE-ELEEERDDLLAEAGLDDADAEA-------VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 167 LNDLNAAKARLTSENFELLHANQEYEAQVLNLSKSRSSLESAVDDLKRSLDDEAKSRFNLQAQLTSLQMDYDNLQAKYEE 246
Cdd:PRK02224 351 ADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 247 ESEEASNLRNQVSKFNADLAAMK------------------------SKFERELMSKTEEYEELKRKLTL--RITELEDT 300
Cdd:PRK02224 431 LEATLRTARERVEEAEALLEAGKcpecgqpvegsphvetieedrervEELEAELEDLEEEVEEVEERLERaeDLVEAEDR 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 301 AERERARASNLEKIKAKLTIEIKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQLEAENMR 380
Cdd:PRK02224 511 IERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 381 LKsQVNDLVDKNAALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAE------------RDNLASALHDAEEAL 448
Cdd:PRK02224 591 LE-RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEfdearieearedKERAEEYLEQVEEKL 669
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42559524 449 REVDQKYQNAQAALNHLKSEMEQ--RLREKDEELETlRKSTTRTIEELTVTITEMEVKYKSEL 509
Cdd:PRK02224 670 DELREERDDLQAEIGAVENELEEleELRERREALEN-RVEALEALYDEAEELESMYGDLRAEL 731
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
339-565 |
1.22e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 339 LARRAKAAENLANDLQRRVDELTIEINnlhsqnsQLEAENMRLKSQVNDLVDKNAALDRENRQLSDQVKDLKSTLRDANR 418
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIA-------ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 419 RLTDLE----ALRSQLEAERDNLASALHDAE--------------EALREVDQKYQNAQAALNHLKSEMEQrLREKDEEL 480
Cdd:COG4942 84 ELAELEkeiaELRAELEAQKEELAELLRALYrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEE-LRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 481 ETLRKSTTRTIEELTVTITEMEVKyKSELSRLKKRYESNIAELELQLDTANKANANLMKENKTLAQRVKDLEAFLEEERR 560
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEE-RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
....*
gi 42559524 561 LREAA 565
Cdd:COG4942 242 RTPAA 246
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
74-571 |
1.65e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.99 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 74 DLENANASLEMAETSMRrrhqtalnELAAEVENLQKQKGKAEKDKNSLIMEVGNVLGQLDGALKAKQ---SAESKLEGLD 150
Cdd:PRK01156 198 ELENIKKQIADDEKSHS--------ITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESeikTAESDLSMEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 151 AQLNRLKGLTDDLQRQLNDLNAAKARLTSENFELLHANQEYEAQVLNLSKSRSSLESAV---DDLKRSLDD--EAKSRF- 224
Cdd:PRK01156 270 EKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIkklSVLQKDYNDyiKKKSRYd 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 225 ---NLQAQLTSLQMDYDNLQAKYEEESEEASNLRNQVSKFNADLAAMKSKFERELMSKTEEYEELKRKLTLRITELEDTA 301
Cdd:PRK01156 350 dlnNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLN 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 302 ERERARASNLEKIKAKLTIE---------------------IKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDEL 360
Cdd:PRK01156 430 QRIRALRENLDELSRNMEMLngqsvcpvcgttlgeeksnhiINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYL 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 361 -TIEINNLHSQNSQLEAENMRLKSQVNDLV------DKNAALDRENRQLSDQVKDLKSTL---RDANRRLTDLEALRSQl 430
Cdd:PRK01156 510 eSEEINKSINEYNKIESARADLEDIKIKINelkdkhDKYEEIKNRYKSLKLEDLDSKRTSwlnALAVISLIDIETNRSR- 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 431 eaeRDNLASALHDAEEALREVDQKYQNAQAALNHLKSEMEQRLREKD------EELETLRKSTTRTIEELTVTITEME-- 502
Cdd:PRK01156 589 ---SNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNnkyneiQENKILIEKLRGKIDNYKKQIAEIDsi 665
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42559524 503 VKYKSELSRLKKRYESNIAELELQLDTANKANANLMKENKTLAQRVKDLEAFLEEERRLREAAESNLQA 571
Cdd:PRK01156 666 IPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKA 734
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
92-602 |
2.55e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 92 RHQTALNELAAEVENLQKQKGKAEKDKNslimEVGNVLGQLDGALKAKQSAESKLEGLDAQLNRLKGLTDDLQRQLNDLN 171
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRD----EADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 172 AAKARLTSENFELLHANQEYEAQVLNLSKSRSSLESAVDDLKRSLDDEAKSRFNLQAQLTSLQMDYDNLQAKYEEESEEA 251
Cdd:PRK02224 286 ERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 252 SNLRNQVSKFNADLAamksKFERELMSKTEEYEELKRKLTLRITELEDTAERERARASNLEKIKAKLTIEIKDLQNEVDS 331
Cdd:PRK02224 366 AELESELEEAREAVE----DRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARER 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 332 LsAENAELARRAKAAEnLANDLQRRVDELTIEinNLHSQNSQLEAENMRLKSQVNDLVDKNAALDrENRQLSDQVKDLKS 411
Cdd:PRK02224 442 V-EEAEALLEAGKCPE-CGQPVEGSPHVETIE--EDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEE 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 412 TLRDANRRLTD----LEALRSQLEAERDNLASALHDAEEALREVDQKYQNAQAALNHLKsEMEQRLREKDEELETLRKst 487
Cdd:PRK02224 517 RREDLEELIAErretIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVA-ELNSKLAELKERIESLER-- 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 488 trtIEELTVTITEmevkYKSELSRLKKRYEsNIAELELQldtankananlMKEN-KTLAQRVKDLEAFLEEER-----RL 561
Cdd:PRK02224 594 ---IRTLLAAIAD----AEDEIERLREKRE-ALAELNDE-----------RRERlAEKRERKRELEAEFDEARieearED 654
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 42559524 562 REAAESNLQASERKRIQLSSEVEELRGALEAADRARKHAEN 602
Cdd:PRK02224 655 KERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
299-535 |
3.75e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 299 DTAERERARASNLEKIKAKLTIEIKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQLEAEn 378
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 379 mrLKSQVNDLVDKNAALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALhdaeEALREVDQKYQNA 458
Cdd:COG4942 99 --LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL----AELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42559524 459 QAALNHLKSEMEQRLRekdeELETLRKSTTRTIEELTVTITEMEVKYKsELSRLKKRYESNIAELELQLDTANKANA 535
Cdd:COG4942 173 RAELEALLAELEEERA----ALEALKAERQKLLARLEKELAELAAELA-ELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
92-614 |
3.96e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 92 RHQTALNELAAEVENLQKQKGKAEKDKNSLIMEVGNVLGQLDGALKAKQSAE-SKLEGLDAQLNRLKGLTDDLQRQLNDL 170
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 171 NAAKARLTsenfellhanqeyeaqvLNLSKSRSSLESAVDDLKRSLDDEAKSRFNLQAQLTSLQMDYDNLQAKYEEESEE 250
Cdd:COG4913 365 EALLAALG-----------------LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 251 ASNLRNQVSKFNADLAAMKSKFERELMSKTEEyeelkrkltLRIT-ELEDTAERERARASNLEKI--KAKLTIeIKDLQN 327
Cdd:COG4913 428 IASLERRKSNIPARLLALRDALAEALGLDEAE---------LPFVgELIEVRPEEERWRGAIERVlgGFALTL-LVPPEH 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 328 EVDSLSAENAELARRA----KAAENLANDLQRRVDELTIeINNLHSQNSQLEAENMRLKSQVNDL--VDKNAALDRENRQ 401
Cdd:COG4913 498 YAAALRWVNRLHLRGRlvyeRVRTGLPDPERPRLDPDSL-AGKLDFKPHPFRAWLEAELGRRFDYvcVDSPEELRRHPRA 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 402 LSD--QVKDLKSTLR-DANRRLT-------DLEALRSQLEAERDNLASALHDAEEALREVDQKYQNAQAALNHLksemeQ 471
Cdd:COG4913 577 ITRagQVKGNGTRHEkDDRRRIRsryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL-----Q 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 472 RLREKDEELETLRkSTTRTIEELTVTITEMEvKYKSELSRLKKRyesnIAELELQLDTANKANANLMKENKTLAQRVKDL 551
Cdd:COG4913 652 RLAEYSWDEIDVA-SAEREIAELEAELERLD-ASSDDLAALEEQ----LEELEAELEELEEELDELKGEIGRLEKELEQA 725
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42559524 552 EAFLEEERRLREAAEsnlqasERKRIQLSSEVEELRGAL---EAADRARKHAENEMNEAQTRVSEL 614
Cdd:COG4913 726 EEELDELQDRLEAAE------DLARLELRALLEERFAAAlgdAVERELRENLEERIDALRARLNRA 785
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
55-585 |
4.58e-08 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 56.29 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 55 SQTHELLKRREMEIGKLRKDLENANASLEMAETSMRRRHQtalnELAAEVENLQKQKGKAEKDKNSLIMEVGNVLGQLDG 134
Cdd:pfam05557 12 SQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQ----ELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 135 ALKAKQSAESKLEGLDAQLNRLKGLTDDLQRQLNDLNAAKARLTSENFELLHANQEYEAQVLNLSKSRSSLESAVDDLKR 214
Cdd:pfam05557 88 LNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 215 SLDDEAKSRFNLQAQLTSLQM------------DYDNLQAKYEEESEEASNLRNQVSKFNADLAAMKSKFERELMSKTE- 281
Cdd:pfam05557 168 AEQRIKELEFEIQSQEQDSEIvknskselaripELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEa 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 282 -----EYEELKRKL--------------------TLRITELEDTAERERARASNLEKIKAKLTIEIKDLQNEVDSLSAEN 336
Cdd:pfam05557 248 atlelEKEKLEQELqswvklaqdtglnlrspedlSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 337 AELARRAKAAENLANDLQRRVDELTIEINNLHSQnsqleaenmrLKSQVNDLVDKNAAldrenRQLSDQVKDLKSTLRDA 416
Cdd:pfam05557 328 EDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAI----------LESYDKELTMSNYS-----PQLLERIEEAEDMTQKM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 417 NRRLTDLEALRSQLEAErdnLASALHDAEEALREVDQKYQNAQAALNHLKSEMEQRLREKDEELETLRKSTTRTIEELTV 496
Cdd:pfam05557 393 QAHNEEMEAQLSVAEEE---LGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEM 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 497 TITEMEVKYKSELSRLKKRYESNIAELELQLDTANKANAnLMKENKTLAQRVKDLEAFLEEERRLreaAESNLQASERKR 576
Cdd:pfam05557 470 ELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEK-LQAEIERLKRLLKKLEDDLEQVLRL---PETTSTMNFKEV 545
|
....*....
gi 42559524 577 IQLSSEVEE 585
Cdd:pfam05557 546 LDLRKELES 554
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
263-485 |
5.52e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 5.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 263 ADLAAMKSKFErELMSKTEEYEELKRKLTL--RITELEDTAERERARASNLEKIKAKLTI-----EIKDLQNEVDSLSAE 335
Cdd:COG4913 225 EAADALVEHFD-DLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 336 NAELARRAKAAENLANDLQRRVDELTIEINNlhSQNSQLEaenmRLKSQVNDLVDKNAALDRENRQLSDQVKDLKSTLRD 415
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRG--NGGDRLE----QLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 416 AnrrLTDLEALRSQLEAERDNLASALHDAEEALREVDQKYQNAQaalnhlksemeQRLREKDEELETLRK 485
Cdd:COG4913 378 S---AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR-----------RELRELEAEIASLER 433
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
204-627 |
2.13e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 204 SLESAVDDLKRSLDDEAKSRFNLQAQLTSLqmdyDNLQAKYEEESEEASNLRNQVSKFNADLAAMKSK---FERELMSKT 280
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEA----DEVLEEHEERREELETLEAEIEDLRETIAETEREreeLAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 281 EEYEELKRkltlRITELEDTAERERARASNLEKikakltiEIKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDEL 360
Cdd:PRK02224 286 ERLEELEE----ERDDLLAEAGLDDADAEAVEA-------RREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 361 TIEINNLHSQNSQLEAENMRLKSQVNDLVDKNAALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASA 440
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 441 LHDAEEALREvdqkyqnAQAALNHLK-SEMEQRL------------REKDEELETLRKSTTRTIEELTVTITEME--VKY 505
Cdd:PRK02224 435 LRTARERVEE-------AEALLEAGKcPECGQPVegsphvetieedRERVEELEAELEDLEEEVEEVEERLERAEdlVEA 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 506 KSELSRLKKRYESNIAELELQLDTANKANANLmkenKTLAQRVKDLEAFLEEERRLREAAESNLQASERKRIQLSSEVEE 585
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERA----EELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE 583
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 42559524 586 LRGALEAADRARKHAEnEMNEAQTRVSELTMQVNTLT--NDKRR 627
Cdd:PRK02224 584 LKERIESLERIRTLLA-AIADAEDEIERLREKREALAelNDERR 626
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
398-638 |
4.06e-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: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 398 ENRQLSDQVKDLKSTLRDANRRLTDLEALRSQL-EAERDNLASALHDAEEALREVDQKYQNAQAALNHLK---SEMEQRL 473
Cdd:TIGR02169 188 RLDLIIDEKRQQLERLRREREKAERYQALLKEKrEYEGYELLKEKEALERQKEAIERQLASLEEELEKLTeeiSELEKRL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 474 REKDEELETLRKSTTRTIEELTVTITEMEVKYKSELSRLkkryESNIAELELQLDTANKANANLMKENKTLAQRVKDLEA 553
Cdd:TIGR02169 268 EEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASL----ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELER 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 554 FLEEERRLREAAESNLQASERKRIQLSSEVEELRGALEAADRARKHAENEMNEAQTRVSELTMQVNTLTNDKRRLEGDIS 633
Cdd:TIGR02169 344 EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELA 423
|
....*
gi 42559524 634 VMQAD 638
Cdd:TIGR02169 424 DLNAA 428
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
60-623 |
5.89e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.81 E-value: 5.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 60 LLKRREMEIGKLRKDLENANASLEMAETSMRRR---HQTALNELAAEVENLQKQKGKAEKDKNSLIMEVGNVLGQLDGAl 136
Cdd:pfam15921 79 VLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSvidLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAA- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 137 kaKQSAESKLEGLDAQLNRLKGLTDDLQRQLNDLnaakaRLTSENFELLHANQEYEAQVLNLSKSRSsLESAVDDLKRSL 216
Cdd:pfam15921 158 --KCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEI-----RSILVDFEEASGKKIYEHDSMSTMHFRS-LGSAISKILREL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 217 DDEA---KSR-FNLQAQLTSLQMDYDN---------------LQAKYEEE----SEEASNLRNQVSKFNADLAAMKSKFE 273
Cdd:pfam15921 230 DTEIsylKGRiFPVEDQLEALKSESQNkielllqqhqdrieqLISEHEVEitglTEKASSARSQANSIQSQLEIIQEQAR 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 274 RELMSKTEEYEELKRKLTLRITELEDTAERERARASNLEKIKAKLTIEIKDLQNEVDSLSAENAELARRAkaaENLANDL 353
Cdd:pfam15921 310 NQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL---QKLLADL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 354 QRRVDELTIEinnlHSQNSQLEAENMrlksqvndlvDKNAALDRENRQLSDQVKDLKstlrdanRRLTDLEALRSQLEAE 433
Cdd:pfam15921 387 HKREKELSLE----KEQNKRLWDRDT----------GNSITIDHLRRELDDRNMEVQ-------RLEALLKAMKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 434 RDNLASALHDAEEALREVDQKYQNAQAALNHLKSEMEQrLREKDEELEtlrkSTTRTIEELTVTITEMEVKYK---SELS 510
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEE-LTAKKMTLE----SSERTVSDLTASLQEKERAIEatnAEIT 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 511 RLKKRYESNIAELElQLDTANKANANLMKENKTLAQRVKDLEAFLEeerRLREAAESNLQ----------ASERKRIQLS 580
Cdd:pfam15921 521 KLRSRVDLKLQELQ-HLKNEGDHLRNVQTECEALKLQMAEKDKVIE---ILRQQIENMTQlvgqhgrtagAMQVEKAQLE 596
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 42559524 581 SEVEELRGALEAADRARKHAENEMNEAQTRVSELTMQVNTLTN 623
Cdd:pfam15921 597 KEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVN 639
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
380-612 |
7.96e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 7.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 380 RLKSQVNDLVDKNAALDRENRQLS--DQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALhdAEEALREVDQKYQN 457
Cdd:COG4913 229 ALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 458 AQAALNHLKSEMEQRLREKDEELETLRKSTTRTIEELtvtitemevkykselsrlkkryESNIAELELQLDTANKANANL 537
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGNGGDRLEQL----------------------EREIERLERELEERERRRARL 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42559524 538 MKENKTLAQRVKDLEAFLEEerrLREAAESNLQASERKRIQLSSEVEELRGALEAADRARKHAENEMNEAQTRVS 612
Cdd:COG4913 365 EALLAALGLPLPASAEEFAA---LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
134-359 |
1.49e-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: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 134 GALKAKQSAESKLEGLDAQLNRLKGLTDDLQRQLNDLNAAKARLTSENFELLHANQEYEAQVLNLSKSRSSLESAVDDLK 213
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 214 RSLDDEaksRFNLQAQLTSLQMDYDNLQAKYEEESEEASNLRNQVSKFNADLAAMKSKFErELMSKTEEYEELKRKLTLR 293
Cdd:COG4942 97 AELEAQ---KEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAE-ELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42559524 294 ITELEDTAERERARASNLEKIKAKLTIEIKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDE 359
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
396-632 |
2.71e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 396 DRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAEEALREVD------QKYQNAQAALNHLKSEM 469
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELEtleaeiEDLRETIAETEREREEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 470 EQRLREKDEELETLRKSTTRTIEELTVTITEMEV--KYKSELSRLKKRYESNIAELELQLDTANKANANLMKENKTLAQR 547
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAveARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 548 VKDLEAFLEEERRLREAAESNLQASERKRIQLSSEVEELRGALEAADRARKHAENEMNEAQTRVSELTMQVNTLTNDKRR 627
Cdd:PRK02224 358 AEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRT 437
|
....*
gi 42559524 628 LEGDI 632
Cdd:PRK02224 438 ARERV 442
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
84-318 |
3.19e-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: 49.76 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 84 MAETSMRRRHQTALNELAAEVENLQKQKGKAEKDKNSLIMEVGNVLGQLDGALKAKQSAESKLEGLDAQLNRLKGLTDDL 163
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 164 QRQLNDLNAAKA-------RLTSENFELLHANQEYEAQVLNLSKSRSSLESAVDDLKRSLDDEAKSRFNLQAQLTSLQMD 236
Cdd:COG4942 96 RAELEAQKEELAellralyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 237 YDNLQAKYEEESEEASNLRNQVSKFNADLAAMKSKFERELMSKTEEYEELKRKLTLRITELEdtAERERARASNLEKIKA 316
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA--AAAERTPAAGFAALKG 253
|
..
gi 42559524 317 KL 318
Cdd:COG4942 254 KL 255
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
9-457 |
3.36e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 9 ESRVRELEDMLDLERDARVRAERHAADMSFQVDALSERLDEAGGNSSQTHELLKRRE------MEIGKLRKDLENANASL 82
Cdd:PRK03918 292 AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKelekrlEELEERHELYEEAKAKK 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 83 EMAETSMRRRHQTALNELAAEVENLQKQKGKAEKDKNSLIMEVGNV---LGQLDGALKAKQSAESKLEGLDAQLNR--LK 157
Cdd:PRK03918 372 EELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELkkeIKELKKAIEELKKAKGKCPVCGRELTEehRK 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 158 GLTDDLQRQLNDLNAAKARLTSENFELLHANQEYEAQVLNLSKSRSSLESAvdDLKRSLDDEAKSrFNLQaQLTSLQMDY 237
Cdd:PRK03918 452 ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA--EQLKELEEKLKK-YNLE-ELEKKAEEY 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 238 DNLQAKYEEESEEASNLRNQVSKFNaDLAAMKSKFERELMSKTEEYEELKRKLTLRITELEDTAEReraRASNLEKIKAK 317
Cdd:PRK03918 528 EKLKEKLIKLKGEIKSLKKELEKLE-ELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEE---RLKELEPFYNE 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 318 LtIEIKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQLEAENMRLKSQvnDLVDKNAALDR 397
Cdd:PRK03918 604 Y-LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYL--ELSRELAGLRA 680
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 398 ENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEaerdNLASALHDAEEaLREVDQKYQN 457
Cdd:PRK03918 681 ELEELEKRREEIKKTLEKLKEELEEREKAKKELE----KLEKALERVEE-LREKVKKYKA 735
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
403-607 |
3.87e-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: 49.38 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 403 SDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAEEALREVDQKYQNAQAALNhlksEMEQRLREKDEELET 482
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA----ALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 483 LRKSTTRTIEEL---------------------------TVTITEMEVKYKSELSRLKKRYESNIAELELQLDTANKANA 535
Cdd:COG4942 95 LRAELEAQKEELaellralyrlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42559524 536 NLMKENKTLAQRVKDLEAFLEEERRLREAAESNLQASERKRIQLSSEVEELRGALEAADRARKHAENEMNEA 607
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
309-596 |
4.43e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 309 SNLEKIKAkLTIEIKDLQNEVDSLSAENAELARRAKAAENLANDLQR--RVDELTIEINNLHSQNSQLEAENMRLKSQVN 386
Cdd:COG4913 607 DNRAKLAA-LEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 387 DLvdknAALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAEEALR-----EVDQKYQNA--Q 459
Cdd:COG4913 686 DL----AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelraLLEERFAAAlgD 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 460 AALNHLKSEMEQRLREKDEELETLRKSTTRTIE-----------ELTVTITEMEvKYKSELSRLKK----RYESNIAELE 524
Cdd:COG4913 762 AVERELRENLEERIDALRARLNRAEEELERAMRafnrewpaetaDLDADLESLP-EYLALLDRLEEdglpEYEERFKELL 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 525 LQLDTANKAN-ANLMKE------------NKTLAQ----------------RVKDLEAFLEEERRLREAA-ESNLQASER 574
Cdd:COG4913 841 NENSIEFVADlLSKLRRaireikeridplNDSLKRipfgpgrylrlearprPDPEVREFRQELRAVTSGAsLFDEELSEA 920
|
330 340
....*....|....*....|..
gi 42559524 575 KRIQLSSEVEELRGALEAADRA 596
Cdd:COG4913 921 RFAALKRLIERLRSEEEESDRR 942
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
493-618 |
4.81e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 48.76 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 493 ELTVTITEMEVKYKSELSRLKKRYESNIAELELQLDTANKANANLMKENKTLAQRVKDLEAFLEEERRLREAAESNLQAS 572
Cdd:pfam00038 29 LLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGL 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 42559524 573 ER-------KRIQLSSEVEELRGALEAadrARKHAENEMNEAQTRVSELTMQV 618
Cdd:pfam00038 109 RKdldeatlARVDLEAKIESLKEELAF---LKKNHEEEVRELQAQVSDTQVNV 158
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6-323 |
5.14e-06 |
|
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: 49.67 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 6 TRLESRVRELEDMLDLERDARVRAERHAADMSFQVDALSERLDEAGGNSSQTHELLKRREMEIGKLRKDLENANASLEMA 85
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 86 ETSMRRRHQTaLNELAAEVENLQKQKGKAEKDKNSLIMEVGNVLGQLDGALKAKQSAESKLEGLDAQLNRLKGLTDDLQR 165
Cdd:TIGR02168 781 EAEIEELEAQ-IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 166 QLNDLNAAKARLTSENFELLHANQEYEAQVL-------NLSKSRSSLESAVDDLKRSLDDEAKSRFNLQAQLTSLQMDYD 238
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALAllrseleELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 239 NLQAK----YEEESEEASNLRNQVSKFNADLAAMKSKFEREL-------MSKTEEYEELKRKLTLRITELEDTaerERAR 307
Cdd:TIGR02168 940 NLQERlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIkelgpvnLAAIEEYEELKERYDFLTAQKEDL---TEAK 1016
|
330
....*....|....*.
gi 42559524 308 ASnLEKIKAKLTIEIK 323
Cdd:TIGR02168 1017 ET-LEEAIEEIDREAR 1031
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
214-626 |
5.88e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 214 RSLDDEAKSRFNLQAQLTSLQMDYDNLQAKYEEESEEASNLRNQVSkfNADLAAMKSKFERELMSKTEEYEELKRkltlR 293
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ--LLPLYQELEALEAELAELPERLEELEE----R 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 294 ITELEDTAERERARASNLEKIKAKLtieikdlqnevdslsaeNAELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQ 373
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEEL-----------------EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 374 LEAENMRLKSQVNDLVDKNAALDRENRqlsdqVKDLKSTLRDANRRLTdLEALRSQLEAERDNLASALHDAEEALREVDQ 453
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEER-----LKEARLLLLIAAALLA-LLGLGGSLLSLILTIAGVLFLVLGLLALLFL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 454 KYQNAQAALNHLKSEMEQRLREKDEELETLRKSTTRTIEELTVTITEMEVKYKSELSRLKKRYESNIAELELQLDTANKA 533
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 534 NANLMKENK-----TLAQRVKDLEAFLEEERRLREAAES-NLQASERKRIQLSSEVEELRGALEAADRARKHAENEMNEA 607
Cdd:COG4717 372 IAALLAEAGvedeeELRAALEQAEEYQELKEELEELEEQlEELLGELEELLEALDEEELEEELEELEEELEELEEELEEL 451
|
410
....*....|....*....
gi 42559524 608 QTRVSELTMQVNTLTNDKR 626
Cdd:COG4717 452 REELAELEAELEQLEEDGE 470
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
227-625 |
7.29e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.74 E-value: 7.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 227 QAQLTSLQMDYDNLQAKYEEESEEASNLRNQVSKFNADLAAMKSKFERELMSKTEEYEELKRKLTlritELEDTAERERA 306
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYK----ELSASSEELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 307 RASNLEKIKAKLTIEIKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQLEAENMRLKSQVN 386
Cdd:pfam07888 116 EKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 387 DLVDKNAALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAEEalrevdqkyqnaqaalnhLK 466
Cdd:pfam07888 196 ELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEG------------------LG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 467 SEMEQRLREKDEELETLRKSTTRTiEELTVTITEMEVKYKSELSRLKKRYESNIAELELQLDTANKANANLMKenktlaq 546
Cdd:pfam07888 258 EELSSMAAQRDRTQAELHQARLQA-AQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQR------- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 547 rvkdLEAFLEEERRLREAAESNL-QASERKRIQLSS---EVEELRGALEAADRARKHAENEMNEAQTRVSELTMQVNTLT 622
Cdd:pfam07888 330 ----LEERLQEERMEREKLEVELgREKDCNRVQLSEsrrELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVA 405
|
...
gi 42559524 623 NDK 625
Cdd:pfam07888 406 DAK 408
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
166-415 |
8.39e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.86 E-value: 8.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 166 QLNDLNAAKARLTSENFELL-----HANQEYEAQVLNLSKSRSSLESAVDDLKRSLDDEAKSRFNLQAQLTSLQMDYDNL 240
Cdd:PHA02562 167 EMDKLNKDKIRELNQQIQTLdmkidHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 241 QAKYEEESeeasnlrNQVSKFNADLAAMKSKFERelMSKTEEYEELKRKLTLRITELEDTAERerarasnLEKIKAKlti 320
Cdd:PHA02562 247 VMDIEDPS-------AALNKLNTAAAKIKSKIEQ--FQKVIKMYEKGGVCPTCTQQISEGPDR-------ITKIKDK--- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 321 eIKDLQNEVDSLSAENAELARRakaaENLANDLQRRVDELTIEINNLHSQNSQLEAENMRLKSQVNDLVDKNAALDRENR 400
Cdd:PHA02562 308 -LKELQHSLEKLDTAIDELEEI----MDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELA 382
|
250
....*....|....*
gi 42559524 401 QLSDQVKDLKSTLRD 415
Cdd:PHA02562 383 KLQDELDKIVKTKSE 397
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
103-629 |
1.02e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 103 EVENLQKQKGKAEKDKNSLIMEVgnvlgqlDGALKAKQSAESKLEGLDAQLNRLKGLTDDLQRQLNDLNAAKARLTSEnf 182
Cdd:PRK01156 198 ELENIKKQIADDEKSHSITLKEI-------ERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSME-- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 183 ellhanqeyEAQVLNLSKSRSSLESAVDDLKRSLDDEAKSRFNLQAQLTSLQMDYDNLQA---KYEEESEEASNLRnqvs 259
Cdd:PRK01156 269 ---------LEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAeinKYHAIIKKLSVLQ---- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 260 KFNADLAAMKSKFErELMSKTEEYEELKRKLTLRITELEDTAERERARASNLEKIKAKLTIEIKDLQNEVDSLSAENAEL 339
Cdd:PRK01156 336 KDYNDYIKKKSRYD-DLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 340 ARRAKAAENLANDLQRRVDELTIEINNLHSQNSQLEAENM-----------RLKSQVNDLVDKNAALDRENRQLSDQVKD 408
Cdd:PRK01156 415 NVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgttlgeeKSNHIINHYNEKKSRLEEKIREIEIEVKD 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 409 LKSTLRDANRRLTDLEALR-SQLEAERDNLASALHDAEE---ALREVDQKYQNAQAALNHLKSEMEQRLREKDEE----- 479
Cdd:PRK01156 495 IDEKIVDLKKRKEYLESEEiNKSINEYNKIESARADLEDikiKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSwlnal 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 480 -------LETLRKSTTRTIEELTVTITEMEvKYKSELSRLKKRYESNIAELELQLDTANKaNANLMKENKTLAQRVKDLE 552
Cdd:PRK01156 575 avislidIETNRSRSNEIKKQLNDLESRLQ-EIEIGFPDDKSYIDKSIREIENEANNLNN-KYNEIQENKILIEKLRGKI 652
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42559524 553 AFLEEERRLREAAESNLQASERKRIQLSSEVEELRGALEA--ADRARKHAENEMNeaQTRVSELTMQVNTLTNDKRRLE 629
Cdd:PRK01156 653 DNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDakANRARLESTIEIL--RTRINELSDRINDINETLESMK 729
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
298-487 |
1.16e-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: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 298 EDTAERERARASNLEKIKAKLTIEIKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQLEAE 377
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 378 NMRLKSQVN------------DLVDKNAALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAE 445
Cdd:COG3883 95 LYRSGGSVSyldvllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 42559524 446 EALREVDQKYQNAQAALNHLKSEMEQRLREKDEELETLRKST 487
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
189-394 |
1.49e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 189 QEYEAQVLNLSKSRSSLESAVDDLKRSLDDEAKSRFNLQAQLTSLQMDYDNLQAKYEEESEEASNLRNQVSKFNADLAAM 268
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 269 KSKFERELMSKTEEYEELKRKLTL--RITE-LEDTAERERARASNLEKIKAKLTIEIKDLQNEVDSLSAENAELARRAKA 345
Cdd:COG4942 117 GRQPPLALLLSPEDFLDAVRRLQYlkYLAPaRREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 42559524 346 AENLANDLQRRVDELTIEINNLHSQNSQLEAENMRLKSQVNDLVDKNAA 394
Cdd:COG4942 197 RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
347-633 |
1.52e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 347 ENLANDLQRRVDELTIEINNLHSQNSQLEAENMRLKSQVNDLvdknAALDRENRQLSDQVKDLKSTLRDANRRLTDLEAL 426
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKEL----EEVLREINEISSELPELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 427 RSQLEAERDNLASAlhdaEEALREVDQKYQNAQAALNHLKSEMEQrLREKDEELETLRKSttrtiEELTVTITEMEVKYK 506
Cdd:PRK03918 237 KEEIEELEKELESL----EGSKRKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKEK-----AEEYIKLSEFYEEYL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 507 SELSRLKK---RYESNIAELELQLDTANKANAnlmkenktlaqRVKDLEAFLEEERRLREAAESNLQASERKRiQLSSEV 583
Cdd:PRK03918 307 DELREIEKrlsRLEEEINGIEERIKELEEKEE-----------RLEELKKKLKELEKRLEELEERHELYEEAK-AKKEEL 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 42559524 584 EELRGALeaADRARKHAENEMNEAQTRVSELTMQVNTLTNDKRRLEGDIS 633
Cdd:PRK03918 375 ERLKKRL--TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIK 422
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
321-593 |
4.26e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 321 EIKDLQNEVDSLSA--ENAELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQLEAENMRLKSQVndLVDKNAALDRE 398
Cdd:COG4913 226 AADALVEHFDDLERahEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 399 NRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAER-DNLASALHDAEEALREVDQKYQNAQAALNHLksemEQRLREKD 477
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAAL----GLPLPASA 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 478 EELETLRKSTTRTIEELtvtitemevkykselSRLKKRYESNIAELELQLDTANKANANLMKENKTLAQRVKDLEAFLEe 557
Cdd:COG4913 380 EEFAALRAEAAALLEAL---------------EEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL- 443
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 42559524 558 erRLREAAESNLQASERK------RIQLSSEVEELRGALEAA 593
Cdd:COG4913 444 --ALRDALAEALGLDEAElpfvgeLIEVRPEEERWRGAIERV 483
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
226-483 |
4.48e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 4.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 226 LQAQLTSLQMDYDNLQAKYEEESEEASNLRNQ------VSKFNADLAAMKSKfERELMSKTEEYEELkRKLTLRITELED 299
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERrealqrLAEYSWDEIDVASA-EREIAELEAELERL-DASSDDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 300 TAERERARASNLEKIKAKLTIEIKDLQNEVDSLSAENAELARRAKAAENLAN-----DLQRRVDELTIEiNNLHSQNSQL 374
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelraLLEERFAAALGD-AVERELRENL 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 375 EAENMRLKSQVNDLVDK-NAALDRENRQLSDQVKDLKSTLRDANrrltDLEALRSQLEAERdnlasaLHDAEEALREvdQ 453
Cdd:COG4913 772 EERIDALRARLNRAEEElERAMRAFNREWPAETADLDADLESLP----EYLALLDRLEEDG------LPEYEERFKE--L 839
|
250 260 270
....*....|....*....|....*....|
gi 42559524 454 KYQNAQAALNHLKSEMEQRLREKDEELETL 483
Cdd:COG4913 840 LNENSIEFVADLLSKLRRAIREIKERIDPL 869
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
318-475 |
5.87e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.73 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 318 LTIEIKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDeltieinNLHSQNSQLEAENMRLKSQVNDLVDKNAALDR 397
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVA-------NLRASLSAAEAERSRLQALLAELAGAGAAAEG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 398 ENRQLSDQVKDLKSTLRDANRRLTDL----EALRSQLEAerdnLASALHDAEEALREVDQKYQN---------AQAA--L 462
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLnqqiAALRRQLAA----LEAALDASEKRDRESQAKIADlgrrlnvalAQRVqeL 192
|
170
....*....|...
gi 42559524 463 NHLKSEMEQRLRE 475
Cdd:PRK09039 193 NRYRSEFFGRLRE 205
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
293-495 |
6.47e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 293 RITELEDTAERERARASNLEkikakltiEIKDLQNEVDSLSAENAELARRAKAAENLANdlQRRVDELTIEINNLHSQNS 372
Cdd:COG4913 236 DLERAHEALEDAREQIELLE--------PIRELAERYAAARERLAELEYLRAALRLWFA--QRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 373 QLEAENMRLKSQVNDLVDKNAALDRENRQLS-DQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAEEALREV 451
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL 385
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 42559524 452 DQKYQNAQAALNHLKSEMEQRLREKDEELETLRKSTTRTIEELT 495
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
161-405 |
7.68e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.30 E-value: 7.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 161 DDLQRQLNDLNAAKARLTSENFELLHANQEYEAQVLNLSKSRSSLESAVDDLKRSLDDEAKSRFNLQAQLTSLQMDYDNL 240
Cdd:pfam00038 57 EDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 241 QAKYEEESEEasnLRNQVSKFNAdLAAMKSKFERELmskTEEYEELKRkltlritELEDTAERERARASNLEKIKaklti 320
Cdd:pfam00038 137 KKNHEEEVRE---LQAQVSDTQV-NVEMDAARKLDL---TSALAEIRA-------QYEEIAAKNREEAEEWYQSK----- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 321 eIKDLQNEVDSLSAEnaelarrAKAAENLANDLQRRVDELTIEINNLHSQNSQLEAE----NMRLKSQVNDLVDKNAALD 396
Cdd:pfam00038 198 -LEELQQAAARNGDA-------LRSAKEEITELRRTIQSLEIELQSLKKQKASLERQlaetEERYELQLADYQELISELE 269
|
....*....
gi 42559524 397 RENRQLSDQ 405
Cdd:pfam00038 270 AELQETRQE 278
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
275-441 |
8.37e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 275 ELMSKTEEYEELKRKLTLRITELEDTAERERARASNLEKIKAKLTIEIKDLQNEVDSLSAENAELARRAKAAENlandlQ 354
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN-----N 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 355 RRVDELTIEINNLHSQNSQLEAENMRLKSQVNdlvDKNAALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAER 434
Cdd:COG1579 89 KEYEALQKEIESLKRRISDLEDEILELMERIE---ELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
....*..
gi 42559524 435 DNLASAL 441
Cdd:COG1579 166 EELAAKI 172
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
353-617 |
1.15e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.27 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 353 LQRRVDELTIEINNLHSQnsqLEAENMRLKSQVNDLVDKNAALDRENRQLSDQVKDLKSTLRDANRRLTDLE-------A 425
Cdd:pfam07888 32 LQNRLEECLQERAELLQA---QEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEekykelsA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 426 LRSQLEAERDNLASALHDAEEALREVDQKYQNAQAALNHLKSEMEqRLREKDEELETLRKSTTRTIEELTVTITEMEVKY 505
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELE-RMKERAKKAGAQRKEEEAERKQLQAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 506 KSeLSRLKKRYESNIAELELQLDTANKANANLMKENKTLAQRVKDLEAFLEEERRLREaaesNLQASERKriqlsseVEE 585
Cdd:pfam07888 188 RS-LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQE----RLNASERK-------VEG 255
|
250 260 270
....*....|....*....|....*....|..
gi 42559524 586 LRGALEAADRARKHAENEMNEAQTRVSELTMQ 617
Cdd:pfam07888 256 LGEELSSMAAQRDRTQAELHQARLQAAQLTLQ 287
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
139-365 |
1.43e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 139 KQSAESKLEGLDAQLNRLKGLTDDLQRQLNDLNAAKARLTSENfellhanqeyeaQVLNLSKSRSSLESAVDDLKRSLDD 218
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKN------------GLVDLSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 219 EAKSRFNLQAQLTSL--QMDYDNLQAKYEEESEEASNLRNQVSKFNADLAAMKSKFERE---LMSKTEEYEELKRKLTLR 293
Cdd:COG3206 231 ARAELAEAEARLAALraQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQE 310
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42559524 294 ITELEDTAERERARASNLEKIKAKLTIEIKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEIN 365
Cdd:COG3206 311 AQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
89-475 |
2.11e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.51 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 89 MRRRHQTALNELAAEVENLQKQKGKAEKDKNSLIMEVGNVLGQLDGALKAKQSAESKLEGLD-AQLNRLKGLTD-DLQRQ 166
Cdd:PLN02939 37 ARRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDDHNrASMQRDEAIAAiDNEQQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 167 LNdlNAAKARLTSENFE-LLHANQEYEAQVLNLSKSRSSlesAVDDLKRSLDDEAKsrfnLQAQLTSLQMDYDNLQAKYE 245
Cdd:PLN02939 117 TN--SKDGEQLSDFQLEdLVGMIQNAEKNILLLNQARLQ---ALEDLEKILTEKEA----LQGKINILEMRLSETDARIK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 246 EESEEasnlrnqvsKFNAD-LAAMKSKFERELMSKTEEYEELKRKLTLritELEDTAERERARASNLEKIKAKLtIEIKD 324
Cdd:PLN02939 188 LAAQE---------KIHVEiLEEQLEKLRNELLIRGATEGLCVHSLSK---ELDVLKEENMLLKDDIQFLKAEL-IEVAE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 325 LQNEVDSLSAENAELARRAKAAENLANDLQRRVDEL-TIEINNLHSQNSQLEAENMRLKSQVndlvDKNAALDRENRQLS 403
Cdd:PLN02939 255 TEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLsPLQYDCWWEKVENLQDLLDRATNQV----EKAALVLDQNQDLR 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42559524 404 DQVKDLKSTLRDAN---RRLTDLEALRSQLEAERDNLASALHDAEEALREVDQKYQNAQAALNHLKSEMEQRLRE 475
Cdd:PLN02939 331 DKVDKLEASLKEANvskFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEESKKRSLE 405
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
354-638 |
2.30e-04 |
|
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: 44.40 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 354 QRRVDELTIEINNLHSQNSQLEAENMRLKSQVNDLVDKNAALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAE 433
Cdd:pfam01576 18 KERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 434 RDNLASALHDAEEALREVD---QKYQNAQAALNHLKSEMEQR---LREKDEELETLRKSTTRTIEELTVTITEMEVKYKS 507
Cdd:pfam01576 98 KKKMQQHIQDLEEQLDEEEaarQKLQLEKVTTEAKIKKLEEDillLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 508 eLSRLKKRYESNIAELELQLDTANKANANLMKENKTLAqrvkdleafleeerrlREAAESNLQASErkriqLSSEVEELR 587
Cdd:pfam01576 178 -LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLE----------------GESTDLQEQIAE-----LQAQIAELR 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 42559524 588 GALeaadrARKhaENEMNEAQTRVSELTMQVNTLTNDKRRLEGDISVMQAD 638
Cdd:pfam01576 236 AQL-----AKK--EEELQAALARLEEETAQKNNALKKIRELEAQISELQED 279
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
373-633 |
2.92e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.37 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 373 QLEAENMRLKSQVNDLVDKNAALDRENRQLSDQvkdlksTLRDANRRLTDLEALRSQLEAERDNLAsalhdaeEALREVD 452
Cdd:pfam00038 22 FLEQQNKLLETKISELRQKKGAEPSRLYSLYEK------EIEDLRRQLDTLTVERARLQLELDNLR-------LAAEDFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 453 QKYqnaqaalnhlksEMEQRLREKDE-ELETLRKsttrTIEELTVTITEMEVKYKS---ELSRLKKRYESNIAELELQLd 528
Cdd:pfam00038 89 QKY------------EDELNLRTSAEnDLVGLRK----DLDEATLARVDLEAKIESlkeELAFLKKNHEEEVRELQAQV- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 529 taNKANANLMKENktlaQRVKDLEAFLEEERRLREA-AESNLQASERkriQLSSEVEELRGALEAADRARKHAENEMNEA 607
Cdd:pfam00038 152 --SDTQVNVEMDA----ARKLDLTSALAEIRAQYEEiAAKNREEAEE---WYQSKLEELQQAAARNGDALRSAKEEITEL 222
|
250 260
....*....|....*....|....*.
gi 42559524 608 QTRVSELTMQVNTLTNDKRRLEGDIS 633
Cdd:pfam00038 223 RRTIQSLEIELQSLKKQKASLERQLA 248
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
187-417 |
3.29e-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: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 187 ANQEYEAQVLNLSKSRSSLESAVDDLKRSLDDEAKSRFNLQAQLTSLQMDYDNLQAKYEEESEEASNLRNQVSKFNADLA 266
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 267 AMKSKFEREL--MSKTEEYEELKrkLTLRITELEDTAererARASNLEKIKAKLTIEIKDLQNEVDSLSAENAELARRAK 344
Cdd:COG4942 101 AQKEELAELLraLYRLGRQPPLA--LLLSPEDFLDAV----RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42559524 345 AAENLANDLQRRVDELTIEINNLHSQNSQLEAENMRLKSQVNDLVDKNAALDRENRQLSDQVKDLKSTLRDAN 417
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
320-485 |
3.31e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 320 IEIKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQLEaenmrlksqvNDLVDKNAALDREN 399
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLE----------LEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 400 RQLsDQVKDLKStLRDANRRLTDLEALRSQLEAERDNLASALHDAEEALREVDQKYQNAQAALNHLKSEMEQRLREKDEE 479
Cdd:COG1579 80 EQL-GNVRNNKE-YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
....*.
gi 42559524 480 LETLRK 485
Cdd:COG1579 158 LEELEA 163
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
413-633 |
3.92e-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: 43.89 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 413 LRDANRRLTDLEALRSQLEAERDNLasalhdaeEALREVDQKYQNAQAALNHLKSEME-QRLREKDEELETLRKSTTRTI 491
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSL--------ERQAEKAERYKELKAELRELELALLvLRLEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 492 EELTvtitemevkyksELSRLKKRYESNIAELELQLDTANKANANLMKENKTLAQRVKDLEAFLEEERRLREAAESNLQA 571
Cdd:TIGR02168 253 EELE------------ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 572 SERKRIQ----------------------------LSSEVEELRGALEAADRARKHAENEMNEAQTRVSELTMQVNTLTN 623
Cdd:TIGR02168 321 LEAQLEEleskldelaeelaeleekleelkeelesLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
250
....*....|
gi 42559524 624 DKRRLEGDIS 633
Cdd:TIGR02168 401 EIERLEARLE 410
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
327-614 |
4.29e-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: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 327 NEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEIN----NLHSQNSQLEAE-NMRLKSQVNDLVDKNAALDR-ENR 400
Cdd:pfam12128 251 NTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNqllrTLDDQWKEKRDElNGELSAADAAVAKDRSELEAlEDQ 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 401 QLSDQVKDLKSTLRDANRrltdLEALRSQLEAERDNLASALHDAEEALREVDQKYQNAQAALNHLKSEMEQRLREKDEEL 480
Cdd:pfam12128 331 HGAFLDADIETAAADQEQ----LPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 481 ETLRKSTTRTIEELTVTITEMEVKYKSELSRLKKRYESNIAELELQLDTANKANANLMkenktlaqrvkDLEAFLEEERR 560
Cdd:pfam12128 407 DRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLL-----------QLENFDERIER 475
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 42559524 561 LREAAEsnlqaserkriQLSSEVEELRGALEAADRARKHAENEMNEAQTRVSEL 614
Cdd:pfam12128 476 AREEQE-----------AANAEVERLQSELRQARKRRDQASEALRQASRRLEER 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
5-502 |
4.56e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 5 TTRLESRVRELEDMLDLERDARVRAERHAADMSFQVDALSERLDEAggnssqthELLKRREMEIGKLRKDLENANASLEM 84
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL--------EELAEELLEALRAAAELAAQLEELEE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 85 AETSMRRRhqtaLNELAAEVENLQKQKGKAEKDKNSLIMEVGNVLGQLDGALKAKQSAESKLEGLDAQLNRLKGLTDDLQ 164
Cdd:COG1196 408 AEEALLER----LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 165 RQLNDLNAAKARLTSENFELLHANQEYEAQVLNLSKSRSSLESAVDdlkrsLDDEAKSRFNLQAQLTSLQMDYDNLQAKY 244
Cdd:COG1196 484 EELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL-----IGVEAAYEAALEAALAAALQNIVVEDDEV 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 245 EEESEEASNLRNQVSKFNADLAAMKSKFERELmskteeyEELKRKLTLRITELEDTAERERARASNLEKIKAKLTIEIKD 324
Cdd:COG1196 559 AAAAIEYLKAAKAGRATFLPLDKIRARAALAA-------ALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 325 LQNEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQLEAENMRLKSQVNDLVDKNAALDRENRQLSD 404
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 405 QVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAEEALREVDQKYQNAQAALNHLKSEME-------------Q 471
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEalgpvnllaieeyE 791
|
490 500 510
....*....|....*....|....*....|.
gi 42559524 472 RLREKDEELETLRKSTTRTIEELTVTITEME 502
Cdd:COG1196 792 ELEERYDFLSEQREDLEEARETLEEAIEEID 822
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
98-404 |
4.59e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 98 NELAAEVENLQKQKGKAEKDKNsLIMEVGNVLGQLDgalkAKQSAESKLEGLDAQLNRLKGLTDDLQRQLNDLNAAKARL 177
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAEDKL-VQQDLEQTLALLD----KIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 178 TSENFEllhanqeyeaqvlnlsksrsslesavddlKRSLDDeaksrfnLQAQLTSLQmdyDNLQakyeeeseeasNLRNQ 257
Cdd:PRK11281 114 TRETLS-----------------------------TLSLRQ-------LESRLAQTL---DQLQ-----------NAQND 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 258 VSKFNADLAAMKSKFERelmSKTEEYEELKRKLTLRITELEDTAERERARASNLEKikakltieikdLQNEVDSLSAENA 337
Cdd:PRK11281 144 LAEYNSQLVSLQTQPER---AQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVL-----------LQAEQALLNAQND 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 338 ELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQL-----------------EAENMRL--KSQVNDLVDKNAALdre 398
Cdd:PRK11281 210 LQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLqeainskrltlsektvqEAQSQDEaaRIQANPLVAQELEI--- 286
|
....*.
gi 42559524 399 NRQLSD 404
Cdd:PRK11281 287 NLQLSQ 292
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
140-435 |
5.89e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 140 QSAESKLEGLDAQLNRLKGLTDDLQRQLNDLNAAKARLTS--ENFELLHANQEYEAQVLNLSKSRSSLESAVDDLKRSLD 217
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQErrEALQRLAEYSWDEIDVASAEREIAELEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 218 DEAKsrfnLQAQLTSLQMDYDNLQAKYEEESEEASNLRNQVSKFNADLAAMKSKFERELMSKTEEYEElkrkltlritEL 297
Cdd:COG4913 686 DLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA----------LL 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 298 EDTAERERARASnLEKIKAKLTIEIKDLQNEVDSLSAENAELARRAKAA-ENLANDLQRRVDEL--------TIEINNLH 368
Cdd:COG4913 752 EERFAAALGDAV-ERELRENLEERIDALRARLNRAEEELERAMRAFNREwPAETADLDADLESLpeylalldRLEEDGLP 830
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42559524 369 SQNSQLeaENMRLKSQVNDLVDKNAALDRENRQLSDQVKDLKSTLRD----ANRRLTdLEALRSQLEAERD 435
Cdd:COG4913 831 EYEERF--KELLNENSIEFVADLLSKLRRAIREIKERIDPLNDSLKRipfgPGRYLR-LEARPRPDPEVRE 898
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
7-631 |
6.34e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 7 RLESRVRELEDMLDLERDARVRAERHAADMsfQVDALSERLDEAGGNSSQTHELLKRREMEIGK---LRKDLENANASLE 83
Cdd:PTZ00121 1134 RKAEDARKAEEARKAEDAKRVEIARKAEDA--RKAEEARKAEDAKKAEAARKAEEVRKAEELRKaedARKAEAARKAEEE 1211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 84 MAETSMRRRHQTALNELAAEVENLQKQKGKAEKDKNSLIMEVGNVLGQLDGALKAKQSAESKLEGldaqlnrlKGLTDDL 163
Cdd:PTZ00121 1212 RKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE--------ARKADEL 1283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 164 QRQLNDLNAAKARLTSE--NFELLHANQEYEAQVLNLSKSRSSLESAVDDLKRSLDDEAKSrfnlqAQLTSLQMDYDNLQ 241
Cdd:PTZ00121 1284 KKAEEKKKADEAKKAEEkkKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA-----AEAAKAEAEAAADE 1358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 242 AKYEEESEEASNLRNQVSKFNADLAAMKSKFERELMSKTEEYEELKRKLTLRITELEDTAERERARASNLEKIKAKLTIE 321
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK 1438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 322 IKDLQNEVDSLSaENAELARRAKAAENLANDlQRRVDELTIEINNLH-SQNSQLEAENMRLKSQVNDLVDKNAALDRENR 400
Cdd:PTZ00121 1439 KAEEAKKADEAK-KKAEEAKKAEEAKKKAEE-AKKADEAKKKAEEAKkADEAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 401 QLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAEEaLREVDQKYQNAQAALNHLKSEMEQRLREKDEEL 480
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEE-KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE 1595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 481 ETLRKSTTRTIEELTVTITEMEVKYKSELSRLKKRYESNIAELELQLDTANKANANLMKENKTLAQRVKDLEAFLEEERR 560
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK 1675
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42559524 561 LREAAESNLQASERKRIQLSSEVEELRgaleAADRARKHAENEMNEAQTRVSELTMQVNTLTNDKRRLEGD 631
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAEALKKEAEEAK----KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED 1742
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
145-631 |
6.55e-04 |
|
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: 43.11 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 145 KLEGLDAQLNRLKGLTDDLQRQLNDLNAAKARLTSENFELlhanQEYEAQVLNLSKSRSSLESAVDDLkrSLDDEAKSRF 224
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKEL----QQLEGSSDRILELDQELRKAEREL--SKAEKNSLTE 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 225 NLQAQLTSLQMDYDNLQAKYEEESEEASNLRNQVSKFNADLAAMKSK---FERELMSKTEEYEELKRKLTL--RITELED 299
Cdd:TIGR00606 498 TLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKmdkDEQIRKIKSRHSDELTSLLGYfpNKKQLED 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 300 TAERERARASNLEKIKAKLTIEIKDLQNEVDSLSAENAEL-ARRAKAAENL-----ANDLQRRVDELTIEINNLHSQNSQ 373
Cdd:TIGR00606 578 WLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKeEQLSSYEDKLfdvcgSQDEESDLERLKEEIEKSSKQRAM 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 374 LEAENMRLKSQVNDLVDKNAA-------LDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNL-------AS 439
Cdd:TIGR00606 658 LAGATAVYSQFITQLTDENQSccpvcqrVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglapgrQS 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 440 ALHDAEEALREVDQKYQNAQAALNHLKSEMEqrlrEKDEELETLrKSTTRTIEELTVTITEMEvKYKSELSRLKKRYESN 519
Cdd:TIGR00606 738 IIDLKEKEIPELRNKLQKVNRDIQRLKNDIE----EQETLLGTI-MPEEESAKVCLTDVTIME-RFQMELKDVERKIAQQ 811
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 520 IAelELQLDTANKANANLMKENKTLAQRVKDLEAFLEEERRLREAAESNLQASERKRIQLSSEVEELRGALEAADRARKH 599
Cdd:TIGR00606 812 AA--KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQ 889
|
490 500 510
....*....|....*....|....*....|..
gi 42559524 600 AENEMNEAQTRVSELTMQVNTLTNDKRRLEGD 631
Cdd:TIGR00606 890 LVELSTEVQSLIREIKDAKEQDSPLETFLEKD 921
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
5-542 |
8.18e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.40 E-value: 8.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 5 TTRLESRVRELEDMLDLERDARVRAERHAADMSFQVDALSERLDEAGGNSSQTHELLKRREMEIGKLRKDLENANASL-- 82
Cdd:pfam05483 249 ITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTIcq 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 83 --EMAETSM------RRRHQTALNELAAEV----ENLQKQKGKAEKDKNSL---IMEVGNVLGQLDGALKAKQSAESKLE 147
Cdd:pfam05483 329 ltEEKEAQMeelnkaKAAHSFVVTEFEATTcsleELLRTEQQRLEKNEDQLkiiTMELQKKSSELEEMTKFKNNKEVELE 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 148 GLDAQLNRLKGLTDDlQRQLNDLNAAKARLTSENFELLHANQ----EYEAQVLNLSKSRSSLESAVDDLKRSLDDEaksr 223
Cdd:pfam05483 409 ELKKILAEDEKLLDE-KKQFEKIAEELKGKEQELIFLLQAREkeihDLEIQLTAIKTSEEHYLKEVEDLKTELEKE---- 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 224 fnlQAQLTSLQMDYDNLQAKYEEESEEASNLRNQVSKFNADLAAMKSKFERELmsktEEYEELKRKLTLRITELEDTAER 303
Cdd:pfam05483 484 ---KLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERML----KQIENLEEKEMNLRDELESVREE 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 304 ERARAsnlEKIKAKLtieiKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQLEAENMRLKS 383
Cdd:pfam05483 557 FIQKG---DEVKCKL----DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENK 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 384 QVNDLVDKNAALDREnrqLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAEEALREVDQKYQNAQAALN 463
Cdd:pfam05483 630 QLNAYEIKVNKLELE---LASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMV 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 464 HL----KSEMEQRLREKDEELeTLRKSTTRTIEELTVTITEMEVKYKSELSRLKKRYESNIAELElQLDTANKANANLMK 539
Cdd:pfam05483 707 ALmekhKHQYDKIIEERDSEL-GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKE-KLKMEAKENTAILK 784
|
...
gi 42559524 540 ENK 542
Cdd:pfam05483 785 DKK 787
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
23-332 |
1.02e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 23 RDARvraERHAADMSFQVDALSERLDEAGGNSSQTHELLKRREMEIGKLRKDLENANASLEMAETsmRRRHQTALNELAA 102
Cdd:PRK04863 781 RAAR---EKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAFEADPEAELRQL--NRRRVELERALAD 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 103 EVENLQKQKGKAEKDKNSLIMeVGNVLGQLDgaLKAKQSAESKLEGLDAQLNRLKGLTDDLQRQLNDLN-----AAKARL 177
Cdd:PRK04863 856 HESQEQQQRSQLEQAKEGLSA-LNRLLPRLN--LLADETLADRVEEIREQLDEAEEAKRFVQQHGNALAqlepiVSVLQS 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 178 TSENFELLHANQEYEAQVLNLSKSRSSLESAVDDLKRSLD-DEAKSRFNLQAQLT-SLQMDYDNLQAKYEEESEEASNLR 255
Cdd:PRK04863 933 DPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSyEDAAEMLAKNSDLNeKLRQRLEQAEQERTRAREQLRQAQ 1012
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 256 NQVSKFNADLAAMKSKFERelmsKTEEYEELKR---------------KLTLRITELEDTAERERARASNLEKIKAKLTI 320
Cdd:PRK04863 1013 AQLAQYNQVLASLKSSYDA----KRQMLQELKQelqdlgvpadsgaeeRARARRDELHARLSANRSRRNQLEKQLTFCEA 1088
|
330
....*....|..
gi 42559524 321 EIKDLQNEVDSL 332
Cdd:PRK04863 1089 EMDNLTKKLRKL 1100
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
424-613 |
1.04e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.19 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 424 EALRSQLEA---ERDNLASALHDAEEALREVDQKYQNAQAALNHLKSEMEQRLREKDEELETLRKSTTRTIEELT--VTI 498
Cdd:pfam07888 30 ELLQNRLEEclqERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKelSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 499 TEMEVKYKSELSRLKKRYESNIAELELQLDTANKANANLMKENKTLAQRVKDLEAFLEEERRLREAAESNLQASERKRIQ 578
Cdd:pfam07888 110 SEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRS 189
|
170 180 190
....*....|....*....|....*....|....*
gi 42559524 579 LSSEVEELRGALEAADRARKHAENEMNEAQTRVSE 613
Cdd:pfam07888 190 LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTT 224
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
55-390 |
1.15e-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: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 55 SQTHELLKRREMEIGKLRKDLENANaslemaetSMRRRHQTALNELAAEVENLQKQKGKAEKDKNSLIMEVGNVLGQLDG 134
Cdd:TIGR04523 331 SQNNKIISQLNEQISQLKKELTNSE--------SENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 135 ALKAKQSAESKLEGLDAQLNRLKGLTDDLQRQLNDLNAAKARLTSENFELlhanqeyEAQVLNLSKSRSSLESAVDDLKR 214
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK-------ELIIKNLDNTRESLETQLKVLSR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 215 SLDDEAKSRFNLQAQLTSLQMDYDNLQAKYEEESEEASNLRNQVSKFNA---DLAAMKSKFERELMSKTEEYEELKRKLT 291
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEkieKLESEKKEKESKISDLEDELNKDDFELK 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 292 L------------RITELEDTAERERARASNLEKIKAKLTIEIKD--------------LQNEVDSLSAENAELARRAKA 345
Cdd:TIGR04523 556 KenlekeideknkEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDlikeieekekkissLEKELEKAKKENEKLSSIIKN 635
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 42559524 346 AENLANDLQRRVDELTIEINNLHSQNSQLEAENMRLKSQVNDLVD 390
Cdd:TIGR04523 636 IKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIE 680
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
41-302 |
1.17e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.13 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 41 DALSERLDEAGGNSSQTHELLKRREMEIGKLRKDLENANASLEMAETSM---RRRHQTALNELAAEVENLQKQKGKAEKD 117
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALknaRLDLRRLFDEKQSEKDKKNKALAERKDS 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 118 KNSLIMEVGNVLGQLDGALKA--KQSAESKLEGLDAQLNRLKGLTDDLQRQLNDLNAAKARLTSENFELLHANQEYEAQV 195
Cdd:pfam12128 680 ANERLNSLEAQLKQLDKKHQAwlEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRD 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 196 LNL----SKSRSSLESAVDDLKRSLDDEAKSRFNLQAQLTSLQMDY----DNLQAKYEEESEEASNLRNQVSKFNADLAA 267
Cdd:pfam12128 760 LASlgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWlqrrPRLATQLSNIERAISELQQQLARLIADTKL 839
|
250 260 270
....*....|....*....|....*....|....*...
gi 42559524 268 MKSKFERELMSKTE---EYEELKRKLTLRITELEDTAE 302
Cdd:pfam12128 840 RRAKLEMERKASEKqqvRLSENLRGLRCEMSKLATLKE 877
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
295-597 |
1.46e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 41.55 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 295 TELEDTAERERARASNLEKIKAkltiEIKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEINNLH-----S 369
Cdd:pfam05701 124 AQLEVAKARHAAAVAELKSVKE----ELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELIATKeslesA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 370 QNSQLEAENMRLKSQVNDLVDKNaALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASAlhdAEEALR 449
Cdd:pfam05701 200 HAAHLEAEEHRIGAALAREQDKL-NWEKELKQAEEELQRLNQQLLSAKDLKSKLETASALLLDLKAELAAY---MESKLK 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 450 EVDQKYQNAQAALNHLKSEMEQrlreKDEELETLRKSTTRTIEE---LTVTITEMEV---KYKSELSRLKKRYE---SNI 520
Cdd:pfam05701 276 EEADGEGNEKKTSTSIQAALAS----AKKELEEVKANIEKAKDEvncLRVAAASLRSeleKEKAELASLRQREGmasIAV 351
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42559524 521 AELELQLDTANKANANLMKENKTLAQRVKDLEAFLEEERRLREAAESNLQASErkriqlssevEELRGALEAADRAR 597
Cdd:pfam05701 352 SSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAR----------EELRKAKEEAEQAK 418
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
241-453 |
1.51e-03 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 41.67 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 241 QAKYEEESEEASNLRNQVSKFNADLAAMKSKFERElmsKTEEYEELKRKLTLRITELEDTAE---RERARASNLEKIKAK 317
Cdd:COG1193 527 RRELEEEREEAERLREELEKLREELEEKLEELEEE---KEEILEKAREEAEEILREARKEAEeliRELREAQAEEEELKE 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 318 LTIEIKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDELT-----IEINNlhSQNSQLEAENMRLKSQVNDL--VD 390
Cdd:COG1193 604 ARKKLEELKQELEEKLEKPKKKAKPAKPPEELKVGDRVRVLSLGqkgevLEIPK--GGEAEVQVGILKMTVKLSDLekVE 681
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42559524 391 KNAALDRENRQLSDQVKDLKStlRDANRRLtDLEALRsqleaerdnlasalhdAEEALREVDQ 453
Cdd:COG1193 682 KKKPKKPKKRPAGVSVSVSKA--STVSPEL-DLRGMR----------------VEEALPELDK 725
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
439-637 |
1.62e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 439 SALHDAEEALREVDQKYQNAQAALNHLKSEMEQrLREKDEELETLRKSTTRTIEELTVTITEMEVKYKSELSRLKKRyes 518
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEE-LNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 519 nIAELELQLDTANKANANLMKEN-KTLAQRVKDLEAFLEEERRLREAAESNLQASERKRIQLSSEVEELRGALEAADRAR 597
Cdd:COG3883 92 -ARALYRSGGSVSYLDVLLGSESfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 42559524 598 KHAENEMNEAQTRVSELTMQVNTLTNDKRRLEGDISVMQA 637
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
143-638 |
1.77e-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: 41.70 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 143 ESKLEGLDAQLNRLKGLTDDLQRQLNDLNAAKARLTSENFEL---LHANQEYEAQV----LNLSKSRSSLESAVDDLKRS 215
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALqeqLQAETELCAEAeemrARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 216 LDDEAKSRFNLQAQLTSLQMDYDNLQAKYEEEseEASNLRNQVSKFNADlaAMKSKFERELMSKTEEYEEL---KRKLTL 292
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEE--EAARQKLQLEKVTTE--AKIKKLEEDILLLEDQNSKLskeRKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 293 RITELEDTAERERARASNLEKIKAKLTIEIKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEINNLHSQNS 372
Cdd:pfam01576 160 RISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 373 QLEAENMRLKSQVNDLVDKNAALDRENRQLSDQVKDLKStlrdanrrltDLEALRSQleaerdnlasalhdaeealrevd 452
Cdd:pfam01576 240 KKEEELQAALARLEEETAQKNNALKKIRELEAQISELQE----------DLESERAA----------------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 453 qkyqnaqaalnhlKSEMEQRLREKDEELETLRKSTTRTIEElTVTITEMEVKYKSELSRLKKRYESNIAELELQLDTANK 532
Cdd:pfam01576 287 -------------RNKAEKQRRDLGEELEALKTELEDTLDT-TAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQ 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 533 ANAnlmkenktlaQRVKDLEAFLEEERRLREAAESNLQAserkriqLSSEVEELRGALEAADRARKHAENEMNEAQTRVS 612
Cdd:pfam01576 353 KHT----------QALEELTEQLEQAKRNKANLEKAKQA-------LESENAELQAELRTLQQAKQDSEHKRKKLEGQLQ 415
|
490 500
....*....|....*....|....*.
gi 42559524 613 ELTMQVNTLTNDKRRLEGDISVMQAD 638
Cdd:pfam01576 416 ELQARLSESERQRAELAEKLSKLQSE 441
|
|
| PRK06975 |
PRK06975 |
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed |
325-494 |
1.94e-03 |
|
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
Pssm-ID: 235899 [Multi-domain] Cd Length: 656 Bit Score: 41.24 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 325 LQNEVDSLSAEnaeLARRAKAAENLANDLQRRVDELTIEINNLHSQNSQLEAenmrlksQVNDLVDKNAALDRENRQLSd 404
Cdd:PRK06975 344 LNRKVDRLDQE---LVQRQQANDAQTAELRVKTEQAQASVHQLDSQFAQLDG-------KLADAQSAQQALEQQYQDLS- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 405 qvkdlkstlrdanrrltdlealrsqleaeRDNLASALHDAEEALREVDQKYQ---NAQAALNHLKSeMEQRLREKDE-EL 480
Cdd:PRK06975 413 -----------------------------RNRDDWMIAEVEQMLSSASQQLQltgNVQLALIALQN-ADARLATSDSpQA 462
|
170
....*....|....
gi 42559524 481 ETLRKSTTRTIEEL 494
Cdd:PRK06975 463 VAVRKAIAQDIERL 476
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
338-533 |
2.40e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.83 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 338 ELARRAKAAENLANDLQRRVDELTIEINNLHSQN------SQLEAENMRLkSQVNDLVDK-NAALDrenrQLSDQVKDLK 410
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEELEAAAlqpgeeEELEEERRRL-SNAEKLREAlQEALE----ALSGGEGGAL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 411 STLRDANRRLTDLEALRSQLEAERDNLASALHDAEEALREVDQKYQNAQAALNHLkSEMEQRLrekdEELETLRKSTTRT 490
Cdd:COG0497 244 DLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERL-EEVEERL----ALLRRLARKYGVT 318
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 42559524 491 IEELTVTITEMEvkykSELSRLkKRYESNIAELELQLDTANKA 533
Cdd:COG0497 319 VEELLAYAEELR----AELAEL-ENSDERLEELEAELAEAEAE 356
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
375-596 |
2.50e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 375 EAENMRLKSQVNDLVDKNAALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAEEALREVDQK 454
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 455 YQNAQAALNH----LKSEMEQRLREKDEELETLRKSTTRTIEELTVTITEMEVKyKSELSRLKKRYESNIAELELQLDTA 530
Cdd:COG3883 95 LYRSGGSVSYldvlLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAK-KAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42559524 531 NKANANLMKENKTLAQRVKDLEAFLEEERRLREAAESNLQASERKRIQLSSEVEELRGALEAADRA 596
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
338-540 |
2.58e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 338 ELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQleaENMRLKSQVNDLVDKNAALDRENRQLSDQVKDLKSTLRDAN 417
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGE---NIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 418 RRLTDLEALRSQLEAERDNLA----------------SALHDAEEALREVDQKYQNAQAALNHLK---SEMEQRLREKDE 478
Cdd:PHA02562 255 AALNKLNTAAAKIKSKIEQFQkvikmyekggvcptctQQISEGPDRITKIKDKLKELQHSLEKLDtaiDELEEIMDEFNE 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42559524 479 ELETLR--KSTTRTIEELTVTITEMEVKYKSELSRLKKR---YESNIAELELQLDTANKANANLMKE 540
Cdd:PHA02562 335 QSKKLLelKNKISTNKQSLITLVDKAKKVKAAIEELQAEfvdNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
321-614 |
2.91e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.96 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 321 EIKDLQNEVDSLSAENAE-------LARRAKAAENLANDLQRRVDELTIE-------INNLHSQNSQLEAENMRLKSQVN 386
Cdd:pfam10174 304 ELLALQTKLETLTNQNSDckqhievLKESLTAKEQRAAILQTEVDALRLRleekesfLNKKTKQLQDLTEEKSTLAGEIR 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 387 DLVDKNAALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAEEALREVDQKYQNaqaalnhLK 466
Cdd:pfam10174 384 DLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIER-------LK 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 467 SEMEQRLREKDEELETLRKSTTRTIEELTVTITEMEVKYKSEL-----------SRLKK--RYESNIAELELQLDTANKA 533
Cdd:pfam10174 457 EQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIdlkehasslasSGLKKdsKLKSLEIAVEQKKEECSKL 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 534 NANLMK-ENKTLAQRVKdlEAFLEEERRLReaAESNLQASERKRIQlsSEVEELRGALeaadrarKHAENEMNEAQTRVS 612
Cdd:pfam10174 537 ENQLKKaHNAEEAVRTN--PEINDRIRLLE--QEVARYKEESGKAQ--AEVERLLGIL-------REVENEKNDKDKKIA 603
|
..
gi 42559524 613 EL 614
Cdd:pfam10174 604 EL 605
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
467-566 |
3.10e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 467 SEMEQRLREKDEELETLRKSTTRTIEELTVTITEMEVKYKSELSRLKKRYESNIAELELQLDTANKANANLMKENKTlAQ 546
Cdd:PRK00409 526 EELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYA-SV 604
|
90 100
....*....|....*....|
gi 42559524 547 RVKDLEaflEEERRLREAAE 566
Cdd:PRK00409 605 KAHELI---EARKRLNKANE 621
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
246-604 |
3.21e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.66 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 246 EESEEASNLRNQVSkFNADLAAMKSKFERELMSKTEEyEELKRKLTLRITELEDTAER----ERARASNLEKIKAKLTiE 321
Cdd:PLN02939 88 QKSTSSDDDHNRAS-MQRDEAIAAIDNEQQTNSKDGE-QLSDFQLEDLVGMIQNAEKNilllNQARLQALEDLEKILT-E 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 322 IKDLQNEVDSLSAENAELARRAKaaenLANDLQRRVDELTIEINNLHSQNSQLEAENmrlKSQVNDLVDKNAALDRENRQ 401
Cdd:PLN02939 165 KEALQGKINILEMRLSETDARIK----LAAQEKIHVEILEEQLEKLRNELLIRGATE---GLCVHSLSKELDVLKEENML 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 402 LSDQVKDLKSTL---RDANRRLTDLEALRSQLEAerdnlasalhdaeeALREVDQKYQNAQAALNHLKSEMEQRLREKDE 478
Cdd:PLN02939 238 LKDDIQFLKAELievAETEERVFKLEKERSLLDA--------------SLRELESKFIVAQEDVSKLSPLQYDCWWEKVE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 479 ELETLRKSTTRTIEELTVTITEmevkykselsrlKKRYESNIAELELQLDTANKANANLMKENkTLAQRVKDLeafleEE 558
Cdd:PLN02939 304 NLQDLLDRATNQVEKAALVLDQ------------NQDLRDKVDKLEASLKEANVSKFSSYKVE-LLQQKLKLL-----EE 365
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 42559524 559 RRLREAAESNLQaserkrIQLSSE-VEELRGAL-----EAADRARKHAENEM 604
Cdd:PLN02939 366 RLQASDHEIHSY------IQLYQEsIKEFQDTLsklkeESKKRSLEHPADDM 411
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
302-585 |
3.26e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 302 ERERARASNLEKIKAKLTIEIKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQLEAENMRL 381
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 382 KSQVNDLVDKNAALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAEEALREVDQKYQNAQAA 461
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 462 LNHLKSEMEQRLREKDEELETLRKSTTRTIEELTVTITEMEVKYKSELSRLKKRYESNIAELELQLDTANKANANLMKEN 541
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 42559524 542 KTLAQRVKDLEAFLEEERRLREAAESNLQASERKRIQLSSEVEE 585
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
282-596 |
3.43e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 282 EYEELKRKLTLRITELEDTAERERARASNLEKIKAKLTIEIKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDELT 361
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 362 IEINNLHSQNSQLEAENMRLKSQVNDLVDKNAALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNL---- 437
Cdd:COG4372 94 AELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALeqel 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 438 -----ASALHDAEEALREVDQKYQNAQAALNHLKSEMEQRLREKDEELETLRKSTTRTIEELTVTITEMEVKYKSELSRL 512
Cdd:COG4372 174 qalseAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 513 KKRYESNIAELELQLDTANKANANLMKENKTLAQRVKDLEAFLEEERRLREAAESNLQASERKRIQLSSEVEELRGALEA 592
Cdd:COG4372 254 EVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
|
....
gi 42559524 593 ADRA 596
Cdd:COG4372 334 ILLA 337
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
284-596 |
4.47e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 284 EELKRKLTLRITELEDTAERERAR----ASNLEKIKAKLTI------------------EIKDLQNEVDSLSAENAELAR 341
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQeqqlRQQLDQLKEQLQLlnkllpqanlladetladRLEELREELDAAQEAQAFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 342 RAKAAENLANDLQR-RVDELTIEinNLHSQNSQLEAENMRLKSQV---NDLVDKNAALDREnrqlsdqvkdlkstlrDAN 417
Cdd:COG3096 915 HGKALAQLEPLVAVlQSDPEQFE--QLQADYLQAKEQQRRLKQQIfalSEVVQRRPHFSYE----------------DAV 976
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 418 RRLTDLEALRSQLEAERDNLASALHDAEEALREVDQKYQNAQAALNHLKSemeqRLREKDEELETLRksttRTIEELTVT 497
Cdd:COG3096 977 GLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKS----SRDAKQQTLQELE----QELEELGVQ 1048
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 498 I-TEMEVKYKSELSRLKKRYESN---IAELELQLDTANKANANLMKENKTLAQRVKDLEAFLEE-----ERRLREAAESN 568
Cdd:COG3096 1049 AdAEAEERARIRRDELHEELSQNrsrRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQakagwCAVLRLARDND 1128
|
330 340
....*....|....*....|....*...
gi 42559524 569 LQASERKRIQLSSEVEELRGALEAADRA 596
Cdd:COG3096 1129 VERRLHRRELAYLSADELRSMSDKALGA 1156
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
129-604 |
4.70e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.21 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 129 LGQLDGALKAKQSAES-KLEGLDAQLNRLKGLTDDLQRQLNDLNAAkarltsenfellhANQEYEAQVLNLSKSRSSLES 207
Cdd:pfam12128 260 LSHLHFGYKSDETLIAsRQEERQETSAELNQLLRTLDDQWKEKRDE-------------LNGELSAADAAVAKDRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 208 AVDDLKRSLDDEAKSRFNLQAQLTSLQMDYDNL--------------QAKYEE-ESEEASNLRNQVSKFNADLAAMKSKF 272
Cdd:pfam12128 327 LEDQHGAFLDADIETAAADQEQLPSWQSELENLeerlkaltgkhqdvTAKYNRrRSKIKEQNNRDIAGIKDKLAKIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 273 ERELMSKTEEYE----ELKRKLTLRITELEDTAERERARASNLEKIKAKLTI---EIKDLQNEVDSLSAENAELARRAKA 345
Cdd:pfam12128 407 DRQLAVAEDDLQalesELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAtpeLLLQLENFDERIERAREEQEAANAE 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 346 AENLAndlqrrvDELTIEINNLHSQNSQLEAENMRLKSQVNDLVDKNAALDRENRQLSDQVKDLKSTLRDANRRLTDLEA 425
Cdd:pfam12128 487 VERLQ-------SELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPEL 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 426 L-RSQLEAERDNLASA-------------------LHDAEEALRE----VDQKYQNAQAALNHLKSEMEQrLREKDEELE 481
Cdd:pfam12128 560 LhRTDLDPEVWDGSVGgelnlygvkldlkridvpeWAASEEELRErldkAEEALQSAREKQAAAEEQLVQ-ANGELEKAS 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 482 TLRKSTTRTIEELTVTITEMEVKYKSELSRLKKRYESNIAELELQLDTankananLMKENKTLAQRVKD-LEAFLEEERR 560
Cdd:pfam12128 639 REETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNS-------LEAQLKQLDKKHQAwLEEQKEQKRE 711
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 42559524 561 LREAAESNLQASERKR-IQLSSEVEELRGALEAADRARKHAENEM 604
Cdd:pfam12128 712 ARTEKQAYWQVVEGALdAQLALLKAAIAARRSGAKAELKALETWY 756
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
141-347 |
5.32e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 141 SAESKLEGLDAQLNRLKGLTDDLQRQLNDLNAAKARLTSENFELLHANQEYEAQVLNLSKSRSSLESAVDDLKRSLDDEA 220
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 221 KSRFNLQAQLTSLQMdydnlqakyEEESEEASNLRNQVSKFNADLAAMKSKFErELMSKTEEYEELKRKLTLRITELEDT 300
Cdd:COG3883 93 RALYRSGGSVSYLDV---------LLGSESFSDFLDRLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 42559524 301 AERERARASNLEKIKAKLTIEIKDLQNEVDSLSAENAELARRAKAAE 347
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
382-507 |
5.55e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.81 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 382 KSQVNDLVDKNAALDRENRQlsdQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALHD------------AEEALR 449
Cdd:PRK00409 515 KEKLNELIASLEELERELEQ---KAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKeaqqaikeakkeADEIIK 591
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 42559524 450 EVDQKYQNAQAALN-HLKSEMEQRLREKDEELETLRKSTTRTIEELTVTiteMEVKYKS 507
Cdd:PRK00409 592 ELRQLQKGGYASVKaHELIEARKRLNKANEKKEKKKKKQKEKQEELKVG---DEVKYLS 647
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
390-623 |
5.58e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 390 DKNAALDRENRQLSDQVKDLKSTLRDANRRLTDL--EALRSQLEAERDNLASALHDAEEALREVDQKYQNAQAALNHLKS 467
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 468 EMEQRLREKDEELETlrksttRTIEELTVTITEMEVKYKSELSRLKKRYESNIAelelqldtankananlmkenktLAQR 547
Cdd:COG3206 248 QLGSGPDALPELLQS------PVIQQLRAQLAELEAELAELSARYTPNHPDVIA----------------------LRAQ 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42559524 548 VKDLEAFLEEE-RRLREAAESNLQASERKRIQLSSEVEELRGALeaadrarkhaeNEMNEAQTRVSELTMQVNTLTN 623
Cdd:COG3206 300 IAALRAQLQQEaQRILASLEAELEALQAREASLQAQLAQLEARL-----------AELPELEAELRRLEREVEVARE 365
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
241-461 |
5.66e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 241 QAKYEEESEEASNLRNQVSKFNADLAAMkskfERELMSKTEEYEELKRKLTLRITELEDTAERERARASNLEKIKAKLTI 320
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDAL----QAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 321 EIKDLQNEVDSLSAENAELArrakaAENLANDLQRRVDeltieINNLHSQNSQLEAEnmrLKSQVNDLVDKNAALDRENR 400
Cdd:COG3883 91 RARALYRSGGSVSYLDVLLG-----SESFSDFLDRLSA-----LSKIADADADLLEE---LKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42559524 401 QLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAEEALREVDQKYQNAQAA 461
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
228-565 |
5.91e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 228 AQLTSLQMDYDNLQAKYEEESEEASNLRNQVSKFNADLAAMKS-KFERElmsKTEEYEELKRKLTLRITELEDTAERERA 306
Cdd:PRK04863 786 KRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAvAFEAD---PEAELRQLNRRRVELERALADHESQEQQ 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 307 RASNLEKIKAKLTI--EIKDLQN--EVDSLSAENAELARRAKAAENLANDLQR---RVDELTIEINNLHSQNSQLEAenm 379
Cdd:PRK04863 863 QRSQLEQAKEGLSAlnRLLPRLNllADETLADRVEEIREQLDEAEEAKRFVQQhgnALAQLEPIVSVLQSDPEQFEQ--- 939
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 380 rLKSQVNDLVDKNAALDRENRQLSDQVKDLKS-TLRDANRRLTDLEALRSQLEAERDNLASALHDAEEALREVDQKYQNA 458
Cdd:PRK04863 940 -LKQDYQQAQQTQRDAKQQAFALTEVVQRRAHfSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQY 1018
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 459 QAALNHLKSEMeQRLREKDEELEtlrksttRTIEELTVTITE-MEVKYKSELSRLKKRYESN---IAELELQLdtankan 534
Cdd:PRK04863 1019 NQVLASLKSSY-DAKRQMLQELK-------QELQDLGVPADSgAEERARARRDELHARLSANrsrRNQLEKQL------- 1083
|
330 340 350
....*....|....*....|....*....|.
gi 42559524 535 ANLMKENKTLAQRVKDLEAFLEEERRLREAA 565
Cdd:PRK04863 1084 TFCEAEMDNLTKKLRKLERDYHEMREQVVNA 1114
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
94-480 |
5.97e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 39.67 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 94 QTALNELAAEVENLQKQKGKAEKDKNSLIMEVGNV---LGQLDGALKAKQSAESKLEGLDAQLNRLKGLTDDLQRQLNDL 170
Cdd:pfam05622 6 QEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLqerLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 171 NAAKARLTSENFELLHANQEY-----EAQVL--------NLSKSRSSLESAVDDLKRSLDDEAksrfNLQAQLTSLQ--- 234
Cdd:pfam05622 86 RIKCEELEKEVLELQHRNEELtslaeEAQALkdemdilrESSDKVKKLEATVETYKKKLEDLG----DLRRQVKLLEern 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 235 MDYDNLQAKYEEESEEASNLRNQVSKFNADLAAMKSKFERElMSKTE----EYEELKRKLtlriteleDTAERERARASN 310
Cdd:pfam05622 162 AEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEE-SKKADklefEYKKLEEKL--------EALQKEKERLII 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 311 LEKIKAKLTIEIKDLQNEVDSLSAENAELARRAKAAENLA-----NDLQRRVDELTIEINNLH-SQNSQLEAENMRLKSQ 384
Cdd:pfam05622 233 ERDTLRETNEELRCAQLQQAELSQADALLSPSSDPGDNLAaeimpAEIREKLIRLQHENKMLRlGQEGSYRERLTELQQL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 385 VNDLVDKNAALDRENR-------QLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASALHDAEEALREVDQKYQN 457
Cdd:pfam05622 313 LEDANRRKNELETQNRlanqrilELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPK 392
|
410 420
....*....|....*....|...
gi 42559524 458 AQAALNHLKSEMEQRLREKDEEL 480
Cdd:pfam05622 393 QDSNLAQKIDELQEALRKKDEDM 415
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
314-441 |
6.77e-03 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 39.45 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 314 IKAKLTIEIKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQLEAENMRLKSQVNDLVDKNA 393
Cdd:COG5283 1 LQVILGAVDKPFKSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALDQAGIDTR 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 42559524 394 ALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRSQLEAERDNLASAL 441
Cdd:COG5283 81 QLSAAQRRLRSSLEQTNRQLERQQQRLARLGARQDRLKAARARLQRLA 128
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
11-381 |
7.19e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.56 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 11 RVRELEDMLDLERD-ARVRAERHAAD-----MSFQVDALSERLDEAGGNSSQTHELLK------RREMEIGKLRKDLENA 78
Cdd:PRK04863 281 RRVHLEEALELRRElYTSRRQLAAEQyrlveMARELAELNEAESDLEQDYQAASDHLNlvqtalRQQEKIERYQADLEEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 79 NASLEmaetsmrrrHQTALNELAAE-VENLQKQKGKAEKDKNSLIMEVGNVLGQLDGALK---AKQSAESKLEGLDaQLN 154
Cdd:PRK04863 361 EERLE---------EQNEVVEEADEqQEENEARAEAAEEEVDELKSQLADYQQALDVQQTraiQYQQAVQALERAK-QLC 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 155 RLKGLT-DDLQRQLNDLNAAKARLTSENFELLHANQEYEAQVLNLSKSRSSLESAVDDLKRSlddEAKSRF-NLQAQLTS 232
Cdd:PRK04863 431 GLPDLTaDNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRS---EAWDVArELLRRLRE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 233 LQMDYDNLQAKYEEESEEASNLRNQVSKFNAdLAAMKSKFERELmSKTEEYEELKRKLTLRITELEDTAERERARASNLE 312
Cdd:PRK04863 508 QRHLAEQLQQLRMRLSELEQRLRQQQRAERL-LAEFCKRLGKNL-DDEDELEQLQEELEARLESLSESVSEARERRMALR 585
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42559524 313 KIKAKLTIEIKDL----------QNEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEINNLHSQNSQLEAENMRL 381
Cdd:PRK04863 586 QQLEQLQARIQRLaarapawlaaQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERL 664
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
365-539 |
7.43e-03 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 38.12 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 365 NNLHSQNSQLEAENMRLKSQVNDLVDKNAALDRENRQLSDQVKDLKST----LRDANRRLTDLEALRSQLEAERDNLASA 440
Cdd:pfam05010 4 KDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTiaqmIEEKQKQKELEHAEIQKVLEEKDQALAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 441 LHDAEEALREVDQKYQNAQAALNHLKSEMEQRLREKDEELETLRKSTTR----------TIEELTVTITEMEVKYKSELS 510
Cdd:pfam05010 84 LNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRyqalkahaeeKLDQANEEIAQVRSKAKAETA 163
|
170 180 190
....*....|....*....|....*....|..
gi 42559524 511 RLK---KRYESNIAELELQLDTANKANANLMK 539
Cdd:pfam05010 164 ALQaslRKEQMKVQSLERQLEQKTKENEELTK 195
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
275-393 |
7.56e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 39.29 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 275 ELMSKTEEYEELKRKLTLRITELEDtAERERARASnlEKIKAKLTIEIKDLQNEVDSLSAENAElarrAKAAENLANDLQ 354
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEA-LKKEQDEAS--FERLAELRDELAELEEELEALKARWEA----EKELIEEIQELK 477
|
90 100 110
....*....|....*....|....*....|....*....
gi 42559524 355 RRVDELTIEINNLHSQNSQLEAENMRLKSQVNDLVDKNA 393
Cdd:COG0542 478 EELEQRYGKIPELEKELAELEEELAELAPLLREEVTEED 516
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
295-414 |
8.34e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.07 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 295 TELEDTAERERARASNLEKIKAKLTIEIKDLQNEVDSLSAENAELARRAKAAENLANDLQRRVDELTIEINNLHSQN--- 371
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDrei 467
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 42559524 372 SQLEAENMRLKSQVNDlvdknaaLDRENRQLSDQVKDLKSTLR 414
Cdd:COG2433 468 SRLDREIERLERELEE-------ERERIEELKRKLERLKELWK 503
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
161-329 |
9.06e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 39.27 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 161 DDLQRQLNDLNAAKARLTSENFELL-------HANQEYEAQVLNLSKSRSSLESAVDDLKRSLDDEAKSRFnlqaqlTSL 233
Cdd:pfam13166 282 TEFQNRLQKLIEKVESAISSLLAQLpavsdlaSLLSAFELDVEDIESEAEVLNSQLDGLRRALEAKRKDPF------KSI 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 234 QMDydNLQAKYEEESEEASNLRNQVSKFN---ADLAAMKSKFEREL-MSKTEEYEELKRKLTLRITELEDTAERERARAS 309
Cdd:pfam13166 356 ELD--SVDAKIESINDLVASINELIAKHNeitDNFEEEKNKAKKKLrLHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIK 433
|
170 180
....*....|....*....|
gi 42559524 310 NLEKIKAKLTIEIKDLQNEV 329
Cdd:pfam13166 434 NLEAEIKKLREEIKELEAQL 453
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
269-606 |
9.68e-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: 39.18 E-value: 9.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 269 KSKFERELMSKTEEYEELKRKLTLRITELEDTAERERARASNLEKIKAKLTIEIKDLQNEvdslsaENAELARRAKAAEN 348
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD------YLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 349 LANDLQRRVDELTIEINNLHSQNSQLEAENMRLKSQVNDLVDKNAALDRENRQLSDQVKDLKSTLRDANRRLTDLEALRS 428
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 429 QLEAERDNLASALHDAEEALREVDQKYQNAQAALNHLKSEMEQRLREKDEELETLRKSTTRTIEELTVTITEMEVKYKSE 508
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 509 LSRLKKRYESNIAELELQLDTANKANANLMKENKTLAQRVKDLEAFLEEERRLREAAESNLQASERKRIQLSSEVEELRG 588
Cdd:pfam02463 405 KEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQE 484
|
330
....*....|....*...
gi 42559524 589 ALEAADRARKHAENEMNE 606
Cdd:pfam02463 485 QLELLLSRQKLEERSQKE 502
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
71-341 |
1.00e-02 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 1.00e-02
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 71 LRKDLENANASLEMAETSMRRRhQTALNELAAEVENLQKQKGKAEKDKNslIMEVGNVLGQLDGALKAKQSAESKLEGLD 150
Cdd:COG4913 615 LEAELAELEEELAEAEERLEAL-EAELDALQERREALQRLAEYSWDEID--VASAEREIAELEAELERLDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 151 AQLNRLKGLTDDLQRQLNDLNAAKARLTSENFELLHANQEYEAQVLNLSKSRSSLESAVDDLKRSLDDEAKSRFNLQAQL 230
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENL 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559524 231 TSLQMDYDNLQAKYEEEseeasnLRNQVSKFNADLAAMKSKFERELMSkTEEYEELKRKL-TLRITELEDTAERERARAS 309
Cdd:COG4913 772 EERIDALRARLNRAEEE------LERAMRAFNREWPAETADLDADLES-LPEYLALLDRLeEDGLPEYEERFKELLNENS 844
|
250 260 270
....*....|....*....|....*....|....
gi 42559524 310 N--LEKIKAKLTIEIKDLQNEVDSLsaeNAELAR 341
Cdd:COG4913 845 IefVADLLSKLRRAIREIKERIDPL---NDSLKR 875
|
|
| |
