|
Name |
Accession |
Description |
Interval |
E-value |
| TBC |
smart00164 |
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ... |
112-320 |
2.43e-78 |
|
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.
Pssm-ID: 214540 [Multi-domain] Cd Length: 216 Bit Score: 251.46 E-value: 2.43e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 112 IRKGIPHHFRAIVWQLLCSATDMPVKN---QYSELLKMSSPCEKL----IRRDIARTYPEHEFFKGQDSLGQEVLFNVMK 184
Cdd:smart00164 1 VRKGVPPSLRGVVWKLLLNAQPMDTSAdkdLYSRLLKETAPDDKSivhqIEKDLRRTFPEHSFFQDKEGPGQESLRRVLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 185 AYSLVDREVGYCQGSAFIVGLLLMQMP-EEEAFCVFVRLMQEYRLReLFKPSMAELGLCIYQFEYMLQEQLPDLNTHFRS 263
Cdd:smart00164 81 AYALYNPEVGYCQGMNFLAAPLLLVMEdEEDAFWCLVKLMERYGPN-FYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21687020 264 QSFHTSMYASSWFLTLFLTTFPLPVATRVFDIFMYEGLEIVFRVGLALLQVNQAELM 320
Cdd:smart00164 160 LGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
|
|
| RabGAP-TBC |
pfam00566 |
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ... |
152-320 |
6.32e-57 |
|
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are GTPase activator proteins of yeast Ypt6 and Ypt7, implies that these domains are GTPase activator proteins of Rab-like small GTPases.
Pssm-ID: 459855 Cd Length: 178 Bit Score: 192.47 E-value: 6.32e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 152 KLIRRDIARTYPEHEFFKGQDslGQEVLFNVMKAYSLVDREVGYCQGSAFIVGLLLMQ-MPEEEAFCVFVRLMQEYRLRE 230
Cdd:pfam00566 10 EQIEKDVPRTFPHSFFFDNGP--GQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLVyLDEEDAFWCFVSLLENYLLRD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 231 LFKPSMAELGLCIYQFEYMLQEQLPDLNTHFRSQSFHTSMYASSWFLTLFLTTFPLPVATRVFDIFMYEGLEIV-FRVGL 309
Cdd:pfam00566 88 FYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVlFRVAL 167
|
170
....*....|.
gi 21687020 310 ALLQVNQAELM 320
Cdd:pfam00566 168 AILKRFREELL 178
|
|
| COG5210 |
COG5210 |
GTPase-activating protein [General function prediction only]; |
108-330 |
1.74e-43 |
|
GTPase-activating protein [General function prediction only];
Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 164.98 E-value: 1.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 108 LKELIRKGIPHHFRAIVWQLLCSATDM--PVKNQYSELLKM-------SSPCEKLIRRDIARTYPEHEFFKGQDSLGQEV 178
Cdd:COG5210 205 LRELIRKGIPNELRGDVWEFLLGIGFDldKNPGLYERLLNLhreakipTQEIISQIEKDLSRTFPDNSLFQTEISIRAEN 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 179 LFNVMKAYSLVDREVGYCQGSAFIVGLLLMQMPEEE-AFCVFVRLMQEYRLRELFKPSMAELGLCIYQFEYMLQEQLPDL 257
Cdd:COG5210 285 LRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVLESEEqAFWCLVKLLKNYGLPGYFLKNLSGLHRDLKVLDDLVEELDPEL 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21687020 258 NTHFRSQSFHTSMYASSWFLTLFLTTFPLPVATRVFDIFMYEGLEIVFRVGLALLQVNQAELMQLDMEGMSQY 330
Cdd:COG5210 365 YEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKLDSDELLDL 437
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
363-751 |
9.63e-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: 9.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 363 LEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKG---QVTRAQEAEENYV-IKRELAVVRQQCSSAAEDLQKAQS 438
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDiarLEERRRELEERLEeLEEELAELEEELEELEEELEELEE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 439 TIRQLQEQQENPRLTEDFVSHLETELEQSRLRETETLGALREMQdkvldMEKRNSSLPDENNVAQLQEELKALKVREGQA 518
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL-----LEALRAAAELAAQLEELEEAEEALLERLERL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 519 VASTRELKLQLQELSDTwqahlarggrwkesprklvVGELQDELMSVRLREAQALAEGRELRQRVVELETQDHIHRNLLN 598
Cdd:COG1196 420 EEELEELEEALAELEEE-------------------EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 599 RVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVMAVRLREADSMAAVAEMRQRIAELEIQREegriqg 678
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE------ 554
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21687020 679 qlNHSDSSQYIRELKDQIEELKAEVRLLKGPPPFEDPLAFDGLSLARHLDEDSLPSSDEELLGVGVGAALQDA 751
Cdd:COG1196 555 --DDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
373-707 |
4.81e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 4.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 373 KEMEEQIE-IKRLRTEnrlLKQRIETLEKgQVTRAQEAEEnyvIKRELAVVRQQcsSAAEDLQKAQSTIRQLQEQQEnpr 451
Cdd:COG1196 182 EATEENLErLEDILGE---LERQLEPLER-QAEKAERYRE---LKEELKELEAE--LLLLKLRELEAELEELEAELE--- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 452 ltedfvsHLETELEQSRLRETETLGALREMQDKVLDMEKRnsslpdennVAQLQEELKALKVREGQAVASTRELKLQLQE 531
Cdd:COG1196 250 -------ELEAELEELEAELAELEAELEELRLELEELELE---------LEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 532 LSDTWQahlarggrwkesprklvvgELQDELMSVRLREAQALAEGRELRQRVVELETQDHIHRNLLNRVEAERAALQEKL 611
Cdd:COG1196 314 LEERLE-------------------ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 612 QYLAAQNKGLQTQLSESRRKQAEAEcKSKEEVMAVRLREADSMAAVAEMRQRIAELEIQREEGRIQGQLNHSDSSQYIRE 691
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELA-AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
330
....*....|....*.
gi 21687020 692 LKDQIEELKAEVRLLK 707
Cdd:COG1196 454 LEEEEEALLELLAELL 469
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
358-704 |
7.41e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 7.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 358 KKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKG------------------QVTRAQEAEENYVIKREL 419
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEleelsrqisalrkdlarlEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 420 AVVRQQCSSAAEDLQKAQSTI----RQLQEQQENPRLTEDFVSHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSL 495
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELaeaeAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 496 PDENNvaQLQEELKALKVREGQAVASTRELKLQLQELSDTWQAHLARggrwkesprklvVGELQDELMSVRLREAQALAE 575
Cdd:TIGR02168 837 ERRLE--DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE------------RASLEEALALLRSELEELSEE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 576 GRELRQRVVELETQdhihrnlLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAeckSKEEVMAVRLREADSMA 655
Cdd:TIGR02168 903 LRELESKRSELRRE-------LEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE---AEALENKIEDDEEEARR 972
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 21687020 656 AVAEMRQRIAEL---------EIQREEGRIQGQLNHS-DSSQYIRELKDQIEELKAEVR 704
Cdd:TIGR02168 973 RLKRLENKIKELgpvnlaaieEYEELKERYDFLTAQKeDLTEAKETLEEAIEEIDREAR 1031
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
351-700 |
8.75e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 62.45 E-value: 8.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 351 YQVKYNPKKMKRLE------------KEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEK-GQVTRAQEAEenyvIKR 417
Cdd:pfam17380 256 YTVRYNGQTMTENEflnqllhivqhqKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKlEEAEKARQAE----MDR 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 418 ELAVVRQQCSSAAEDlQKAQSTIRQLQEQQENPRLTEDfvshlETELEQSRLRETETLGALREMQD-------------K 484
Cdd:pfam17380 332 QAAIYAEQERMAMER-ERELERIRQEERKRELERIRQE-----EIAMEISRMRELERLQMERQQKNervrqeleaarkvK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 485 VLDMEKRNSSLPDENNVAQLQEELKALKVREGQAVASTRELKLQLQELSDTWQAHLARGGRWKESPRKLVVGELQDElms 564
Cdd:pfam17380 406 ILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE--- 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 565 vrlREAQALAEgrELRQRVVELETQdhihrnllnrvEAERAALQE--KLQYLAAQNKGLQTQLSESRRKQAEAECKSKEE 642
Cdd:pfam17380 483 ---KRDRKRAE--EQRRKILEKELE-----------ERKQAMIEEerKRKLLEKEMEERQKAIYEEERRREAEEERRKQQ 546
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 21687020 643 VMAVRLREADSMAAVAEMRQRIAELEIQREEGRiqgQLNHSDSSQYIRELKDQIEELK 700
Cdd:pfam17380 547 EMEERRRIQEQMRKATEERSRLEAMEREREMMR---QIVESEKARAEYEATTPITTIK 601
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
416-708 |
2.26e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 416 KRELAVVRQQCSSAAEDLQKAQSTIRQLQEQQENprltedfvshLETELEQSRLRETETLGALREMQDKVLDMEKRNSSL 495
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEE----------LEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 496 PDEN-----NVAQLQEELKALKVREGQAVASTRELKLQLQELSDTWQAHLARGGRWKESPRKL--VVGELQDELMSVRLR 568
Cdd:TIGR02168 746 EERIaqlskELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELraELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 569 EAQALAEGRELRQRVVELETQDHIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAecKSKEEVMAVRL 648
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL--RSELEELSEEL 903
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21687020 649 READS------------MAAVAEMRQRIAELEIQREEgrIQGQLN--HSDSSQYIRELK----DQIEELKAEVRLLKG 708
Cdd:TIGR02168 904 RELESkrselrreleelREKLAQLELRLEGLEVRIDN--LQERLSeeYSLTLEEAEALEnkieDDEEEARRRLKRLEN 979
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
358-659 |
4.11e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 358 KKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKGQVTRAQEAEE----NYVIKRELAVVRQQCSSAAEDL 433
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkeLYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 434 QKAQSTIRQLQEQQENPRltedfvSHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPD-ENNVAQLQEELKALK 512
Cdd:TIGR02168 312 ANLERQLEELEAQLEELE------SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEElESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 513 VREGQAVASTRELKLQLQELSDTWQAHLARGGRWKESprklvVGELQDELMSVRLREAQALAEgrELRQRVVELETQDHI 592
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE-----IEELLKKLEEAELKELQAELE--ELEEELEELQEELER 458
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21687020 593 HRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLS--ESRRKQAEAECKSKEEVMAVRLREADSMAAVAE 659
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAERELAQLQARLDslERLQENLEGFSEGVKALLKNQSGLSGILGVLSE 527
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
426-641 |
1.41e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 426 CSSAAEDLQKAQSTIRQLQEQQENprltedfvshLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLpdENNVAQLQ 505
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAE----------LEKELAALKKEEKALLKQLAALERRIAALARRIRAL--EQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 506 EELKALKVREGQAVASTRELKLQLQELSDTWQAhLARGGRWK-----ESPRKLV-VGELQDELMSVRLREAQALAEGR-E 578
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAELLRALYR-LGRQPPLAlllspEDFLDAVrRLQYLKYLAPARREQAEELRADLaE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21687020 579 LRQRVVELETQDHIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKE 641
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
358-702 |
1.64e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 358 KKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKGQVTRAQEAEEnyvIKRELAVVRQQCSSAAEDLQKAQ 437
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE---AEAELAEAEEALLEAEAELAEAE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 438 STIRQLQEQQENPRLTEDFVSHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDENNVAQLQEELKALKVREGQ 517
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 518 A------VASTRELKLQLQELSDtwQAHLARGGRWKESPRKLVVGELQDELMSVRLREAQALA-----EGRELRQRVVEL 586
Cdd:COG1196 459 EallellAELLEEAALLEAALAE--LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLrglagAVAVLIGVEAAY 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 587 ETQDHIH--RNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEvmAVRLREADSMAAVAEMRQRI 664
Cdd:COG1196 537 EAALEAAlaAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALAR--GAIGAAVDLVASDLREADAR 614
|
330 340 350
....*....|....*....|....*....|....*...
gi 21687020 665 AELEIQREEGRIQGQLNHSDSSQYIRELKDQIEELKAE 702
Cdd:COG1196 615 YYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLE 652
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
359-703 |
2.93e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 359 KMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKGQVTRAQEAEENYVIKRELAVVRQQCSSAAEDLQKAQS 438
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 439 TIR-QLQEQQENPRLTEDFVSHLETELEQSRLRETEtlGALREMQDKVLDMEKRNSSLPDENNVAQLQEELKALKVREgq 517
Cdd:TIGR02169 762 ELEaRIEELEEDLHKLEEALNDLEARLSHSRIPEIQ--AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE-- 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 518 AVASTRELKLQLQELSDTWQAHLARGGRWKESPRKL--VVGELQDELMSVRLREAQALAEGRELRQRVVELETQDHIHRN 595
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELeaALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 596 LLNRVEAERAALQEKL-QYLAAQNKGLQTQLSESRRKQAEAECKSKEEvmAVRLREADSMAAV---AEMRQRIAELEIQR 671
Cdd:TIGR02169 918 RLSELKAKLEALEEELsEIEDPKGEDEEIPEEELSLEDVQAELQRVEE--EIRALEPVNMLAIqeyEEVLKRLDELKEKR 995
|
330 340 350
....*....|....*....|....*....|..
gi 21687020 672 EegriqgQLNHSDSSqyIRELKDQIEELKAEV 703
Cdd:TIGR02169 996 A------KLEEERKA--ILERIEEYEKKKREV 1019
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
358-707 |
5.06e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 5.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 358 KKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKgqvtrAQEAEENYVIKRELAVVRQQCSSAAEDLQKAQ 437
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK-----LLQLLPLYQELEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 438 STIRQLQEQQENprlTEDFVSHLETELEQSRLRET-ETLGALREMQDKVLDMEKRNSSLpdENNVAQLQEELKALKVREG 516
Cdd:COG4717 156 EELRELEEELEE---LEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAEL--EEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 517 QAVASTRELKLQlQELSDTWQAHLARGGRwkesprkLVVGELQDELMSVRLREAQALAEGRELRqrvveletqdHIHRNL 596
Cdd:COG4717 231 QLENELEAAALE-ERLKEARLLLLIAAAL-------LALLGLGGSLLSLILTIAGVLFLVLGLL----------ALLFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 597 LNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVMAVRLREADSMAAVAEMRQRIAELEIQREEGRI 676
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI 372
|
330 340 350
....*....|....*....|....*....|....*.
gi 21687020 677 QGQLNHSDSS-----QYIRELKDQIEELKAEVRLLK 707
Cdd:COG4717 373 AALLAEAGVEdeeelRAALEQAEEYQELKEELEELE 408
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
363-702 |
6.62e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 363 LEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEkgqvTRAQEA-EENYVIKRELAVVRQQCSSAAEDLQKAQSTIR 441
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLE----ERAEELrEEAAELESELEEAREAVEDRREEIEELEEEIE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 442 QLQEQQENPRLT----EDFVSHLETELEQSRLRETETLGALREMQDKVldmeKRNSSLPDENNVAQLQEELK------AL 511
Cdd:PRK02224 395 ELRERFGDAPVDlgnaEDFLEELREERDELREREAELEATLRTARERV----EEAEALLEAGKCPECGQPVEgsphveTI 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 512 KVREGQaVASTRELKLQLQELSDTWQAHLARGGRWKESPRKLVVGELQDELMSVRLREAQALAEGR-----ELRQRVVEL 586
Cdd:PRK02224 471 EEDRER-VEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKreraeELRERAAEL 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 587 ETQDHIHRnllNRVEAERAALQEKLQYLAAQNKGLQT------QLSESRRKQAEAECKSKEevmAVRLREADSMAA---- 656
Cdd:PRK02224 550 EAEAEEKR---EAAAEAEEEAEEAREEVAELNSKLAElkerieSLERIRTLLAAIADAEDE---IERLREKREALAelnd 623
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 21687020 657 -----VAEMRQRIAELEIQREEGRIQG-QLNHSDSSQYIRELKDQIEELKAE 702
Cdd:PRK02224 624 errerLAEKRERKRELEAEFDEARIEEaREDKERAEEYLEQVEEKLDELREE 675
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
361-699 |
9.81e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 9.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 361 KRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKGQVTRAQEAEENYVIKRELAVVRQQCSSAAEDLQKAQSTI 440
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 441 RQLQEQQENPRLTEDFVSHLETELEQSRLRETETLGALremQDKVLDmekrnsslpDENNVAQLQEELKALKVREGQAVA 520
Cdd:COG1196 511 KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL---QNIVVE---------DDEVAAAAIEYLKAAKAGRATFLP 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 521 STRELKLQLQELSDTWQAH------LARGGRWKESPRKLVVGELQDELMSV-RLREAQALAEGRELRQRVVELETQDHI- 592
Cdd:COG1196 579 LDKIRARAALAAALARGAIgaavdlVASDLREADARYYVLGDTLLGRTLVAaRLEAALRRAVTLAGRLREVTLEGEGGSa 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 593 -----------HRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAE---CKSKEEVMAVRLREADSMAAVA 658
Cdd:COG1196 659 ggsltggsrreLLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEeerLEEELEEEALEEQLEAEREELL 738
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 21687020 659 EMRQRIAELEIQREEGRIQGQLNHSDSSQYIRELKDQIEEL 699
Cdd:COG1196 739 EELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
381-630 |
1.63e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 381 IKRLRTENRLLKQRIETLEKgQVTRAQEAEENYVIKRELAVVRQQCSSAAEDLQKAQSTIRQLQEQQENPRLTEDFVSHL 460
Cdd:COG4913 612 LAALEAELAELEEELAEAEE-RLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 461 ETELEQSRLRETETLGALREMQDKVLDMEKRnsslpdennVAQLQEELKALKVREGQAVASTRElkLQLQELSDTWQAHL 540
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKE---------LEQAEEELDELQDRLEAAEDLARL--ELRALLEERFAAAL 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 541 ARGgrwkesPRKLVVGELQDELMSVRLREAQALAEGRELRQRVVE---LETQDHI--------HRNLLNRVEAER-AALQ 608
Cdd:COG4913 760 GDA------VERELRENLEERIDALRARLNRAEEELERAMRAFNRewpAETADLDadleslpeYLALLDRLEEDGlPEYE 833
|
250 260
....*....|....*....|....*..
gi 21687020 609 EKL-QYLAAQNK----GLQTQLSESRR 630
Cdd:COG4913 834 ERFkELLNENSIefvaDLLSKLRRAIR 860
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
358-706 |
2.17e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 358 KKMKRLEKEYAAMKSK--EMEEQIEIKRLRTENRLLKQRIETLEkgqvTRAQEAEENYvikRELAVVRQQCSSAAEDLQK 435
Cdd:COG4717 102 EELEELEAELEELREEleKLEKLLQLLPLYQELEALEAELAELP----ERLEELEERL---EELRELEEELEELEAELAE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 436 AQSTIRQLQEQQENPRLTEdfVSHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDENNVAQLQEELKALKV-- 513
Cdd:COG4717 175 LQEELEELLEQLSLATEEE--LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLll 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 514 ------------------------------------------REGQAVASTRELKLQLQELSD----TWQAHLARGGRwK 547
Cdd:COG4717 253 liaaallallglggsllsliltiagvlflvlgllallflllaREKASLGKEAEELQALPALEEleeeELEELLAALGL-P 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 548 ESPRKLVVGELQDELMSVRLREAQALAEGRELRQRVVELETQDHIHRNLLNRVEAERAALQEKLQYLAAQNKG--LQTQL 625
Cdd:COG4717 332 PDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELeeLEEQL 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 626 SESRRKQAEAECKSKEEVMAVRLREADsmAAVAEMRQRIAELeiQREEGRIQGQLNHSDSSQYIRELKDQIEELKAEVRL 705
Cdd:COG4717 412 EELLGELEELLEALDEEELEEELEELE--EELEELEEELEEL--REELAELEAELEQLEEDGELAELLQELEELKAELRE 487
|
.
gi 21687020 706 L 706
Cdd:COG4717 488 L 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
489-704 |
2.59e-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: 51.21 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 489 EKRNSSLPDENNVAQLQEELKAL--KVREG-QAVASTRELKLQLQELSDTWQAHLARGGRwKESPRKLVVGELQDELMSV 565
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELeeKIAELeKALAELRKELEELEEELEQLRKELEELSR-QISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 566 RLREAQALAEGRELRQRVVELETQDHIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEaeckSKEEVMA 645
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL----LNEEAAN 821
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21687020 646 VRLREADSMAAVAEMRQRIAELE---IQREEGRIQGQLNHSDSSQYIRELKDQIEELKAEVR 704
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEeqiEELSEDIESLAAEIEELEELIEELESELEALLNERA 883
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
356-707 |
3.36e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 356 NPKKMKRLEKEYAAMKSKEME---EQIEIKRLRTENRLLKQRIETLEKgQVTRAQEAEENYVIKRELAVVRQQCSSAAED 432
Cdd:COG4717 69 NLKELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELRE-ELEKLEKLLQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 433 LQKAQSTIRQLQEQQENPRLTEDFVSHLETELEQSRLRET-ETLGALREMQDKVLDMEKRNSSLpdENNVAQLQEELKAL 511
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAEL--EEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 512 KVREGQAVASTRELKL--QLQELSDTW-----------QAHLARGGRWKESPRKLVVGELQDELMSVRLREAQALAEGRE 578
Cdd:COG4717 226 EEELEQLENELEAAALeeRLKEARLLLliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 579 LRQRVVELET-QDHIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVMAVRLREA-----D 652
Cdd:COG4717 306 ELQALPALEElEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAgvedeE 385
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 653 SMAAVAEMRQRIAELEIQREE-----GRIQGQLNHSDSSQYIRELKDQIEELKAEVRLLK 707
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEEleeqlEELLGELEELLEALDEEELEEELEELEEELEELE 445
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
424-673 |
7.86e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 7.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 424 QQCSSAAEDLQKAQSTIRQLQEQQENprlTEDFVSHLETELEQSRLRETETLGALREMQDKvldmekrnsslpdennVAQ 503
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA---LKKEEKALLKQLAALERRIAALARRIRALEQE----------------LAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 504 LQEELKALKVREGQAVASTRELKLQLQELSDTWQahlaRGGRwkESPRKLVVGELQDELMSVRLREAQALAEGRelRQRV 583
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALY----RLGR--QPPLALLLSPEDFLDAVRRLQYLKYLAPAR--REQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 584 VELETQdhihRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVMAVRLREADSMAAVAEMRQR 663
Cdd:COG4942 153 EELRAD----LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
250
....*....|
gi 21687020 664 IAELEIQREE 673
Cdd:COG4942 229 IARLEAEAAA 238
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
441-672 |
1.12e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 441 RQLQEQQENPRLTEDFvshLETELEQSRLRetetlgaLREMQDKVLDMEKRNSSLPDENNVAQLQEELKALKVREGQAVA 520
Cdd:COG3206 164 QNLELRREEARKALEF---LEEQLPELRKE-------LEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 521 STRELKLQLQELSDTWQAHLARGGRWKESPrklVVGELQDELMSVRLREAQALAEG-------RELRQRVVELETQ-DHI 592
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQSP---VIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQlQQE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 593 HRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEaeckskeevMAVRLREADSMAAV-AEMRQRIAELEIQR 671
Cdd:COG3206 311 AQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE---------LRRLEREVEVARELyESLLQRLEEARLAE 381
|
.
gi 21687020 672 E 672
Cdd:COG3206 382 A 382
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
386-706 |
2.84e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 386 TENRLLKQRIETLEKGqvtRAQEAEENYVI----KRELAVVRQQCSSAAEDLQKAQSTIRQLQEQQEnpRLTEdfVSHLE 461
Cdd:COG4913 578 TRAGQVKGNGTRHEKD---DRRRIRSRYVLgfdnRAKLAALEAELAELEEELAEAEERLEALEAELD--ALQE--RREAL 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 462 TELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDennVAQLQEELKALKVREGQAVASTRELKLQLQELSDTWQAHLA 541
Cdd:COG4913 651 QRLAEYSWDEIDVASAEREIAELEAELERLDASSDD---LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE 727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 542 RggrwkesprklvVGELQDELMSVRLREAQALAEGRELRqrvVELETQDHIHRNLLNRVEAERAALQEKLQYLAAQnkgL 621
Cdd:COG4913 728 E------------LDELQDRLEAAEDLARLELRALLEER---FAAALGDAVERELRENLEERIDALRARLNRAEEE---L 789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 622 QTQLSESRRKQAEAecksKEEVMAvrlrEADSMAAVAEMRQRIAELEIQREEGRIQGQLN---HSDSSQYIRELKDQIEE 698
Cdd:COG4913 790 ERAMRAFNREWPAE----TADLDA----DLESLPEYLALLDRLEEDGLPEYEERFKELLNensIEFVADLLSKLRRAIRE 861
|
....*...
gi 21687020 699 LKAEVRLL 706
Cdd:COG4913 862 IKERIDPL 869
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
359-706 |
2.87e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 359 KMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEkgqVTRAQEAEENYVIKRELAVVRQQCSSAAEDLQKAQS 438
Cdd:PRK02224 364 EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAP---VDLGNAEDFLEELREERDELREREAELEATLRTARE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 439 TI---RQLQEQQENPRLTEDF--VSHLETeLEQSRLRETETLGALREMQDKVLDMEKRNSSLPD----ENNVAQLQEELK 509
Cdd:PRK02224 441 RVeeaEALLEAGKCPECGQPVegSPHVET-IEEDRERVEELEAELEDLEEEVEEVEERLERAEDlveaEDRIERLEERRE 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 510 ALKVREGQAVASTRELKLQLQELSDTWQAHLARGGRWKESPRklvvgELQDELMSVRLREA---QALAEGRELRQRVVEL 586
Cdd:PRK02224 520 DLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAA-----EAEEEAEEAREEVAelnSKLAELKERIESLERI 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 587 ETQDhihrNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEE-VMAVRLREADSMAAVAEMRQRIA 665
Cdd:PRK02224 595 RTLL----AAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEEKLD 670
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 21687020 666 ELEIQREEgrIQGQLNHSDSS-QYIRELKDQIEELKAEVRLL 706
Cdd:PRK02224 671 ELREERDD--LQAEIGAVENElEELEELRERREALENRVEAL 710
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
358-704 |
4.07e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 358 KKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLK--------QRIETLEKgQVTRAQEAEENyvIKRELAVVRQQCSSA 429
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEaqirgnggDRLEQLER-EIERLERELEE--RERRRARLEALLAAL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 430 -------AEDLQKAQSTIRQLQEQqenprlTEDFVSHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDEnnVA 502
Cdd:COG4913 372 glplpasAEEFAALRAEAAALLEA------LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR--LL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 503 QLQEEL-KALKVREGQA--VAstrELkLQLQELSDTWQ------------------AHLARGGRWKES--PRKLVVGElq 559
Cdd:COG4913 444 ALRDALaEALGLDEAELpfVG---EL-IEVRPEEERWRgaiervlggfaltllvppEHYAAALRWVNRlhLRGRLVYE-- 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 560 delmsvRLREAQALAEGRELRQR--VVELETQDHIHRNLLNRVEAERAAL------------------------------ 607
Cdd:COG4913 518 ------RVRTGLPDPERPRLDPDslAGKLDFKPHPFRAWLEAELGRRFDYvcvdspeelrrhpraitragqvkgngtrhe 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 608 -----------------QEKLQYLAAQNKGLQTQLSESRRKQAEAEckSKEEVMAVRLREADSMAAVAEMRQRIAELeiQ 670
Cdd:COG4913 592 kddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALE--AELDALQERREALQRLAEYSWDEIDVASA--E 667
|
410 420 430
....*....|....*....|....*....|....*
gi 21687020 671 REEGRIQGQLNH-SDSSQYIRELKDQIEELKAEVR 704
Cdd:COG4913 668 REIAELEAELERlDASSDDLAALEEQLEELEAELE 702
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
363-668 |
4.21e-05 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 47.24 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 363 LEKEYAAMKS-----KEMEE--------QIEIKRLRTENRLLK------QRIETLEKGQVTRAQEaeeNYVIKRELAVVR 423
Cdd:PLN03188 938 LEEELASLMHehkllKEKYEnhpevlrtKIELKRVQDELEHYRnfydmgEREVLLEEIQDLRSQL---QYYIDSSLPSAR 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 424 QQCS------SAAEDLQKAQSTIRQLQE-------QQENPRLTE------DFVSHLETELEQSRlretetlgALREMQDK 484
Cdd:PLN03188 1015 KRNSllkltySCEPSQAPPLNTIPESTDespekklEQERLRWTEaeskwiSLAEELRTELDASR--------ALAEKQKH 1086
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 485 VLDMEKRNSslpdennvaqlqEELK-ALKV-REGQAvastRELKlQLQELSDTWQAHLARGGRwkesprklvvgeLQDEL 562
Cdd:PLN03188 1087 ELDTEKRCA------------EELKeAMQMaMEGHA----RMLE-QYADLEEKHIQLLARHRR------------IQEGI 1137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 563 MSVRLREAQALAEGRELRqrvveletqdhihrnLLNRVEAERAAL----QEKLQYLAAQNKGLQTQLsesrRKQAEAECK 638
Cdd:PLN03188 1138 DDVKKAAARAGVRGAESK---------------FINALAAEISALkverEKERRYLRDENKSLQAQL----RDTAEAVQA 1198
|
330 340 350
....*....|....*....|....*....|
gi 21687020 639 SKEevMAVRLREADSMAAVAEMRQRIAELE 668
Cdd:PLN03188 1199 AGE--LLVRLKEAEEALTVAQKRAMDAEQE 1226
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
382-703 |
7.34e-05 |
|
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: 46.65 E-value: 7.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 382 KRLRTENRLLKQRIETLEKGQVTRAQEAEENYVIKRELAVVRQQCSSAAEDLQ-KAQSTIRQLQEQQEnprLTEDFVSHL 460
Cdd:pfam15921 92 RRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRnQLQNTVHELEAAKC---LKEDMLEDS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 461 ETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDEnnvaqlQEELKALKVRE-GQAVAST-RELKLQLQELSdtwqa 538
Cdd:pfam15921 169 NTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYE------HDSMSTMHFRSlGSAISKIlRELDTEISYLK----- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 539 hlargGRwkesprklvVGELQDELMSVRLREaqalaegrelrQRVVELETQDHIHR--NLLNRVEAERAALQEKLQYLAA 616
Cdd:pfam15921 238 -----GR---------IFPVEDQLEALKSES-----------QNKIELLLQQHQDRieQLISEHEVEITGLTEKASSARS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 617 QNKGLQTQL---SESRRKQAE------AECKSKEEVMAVRLREADSMaavaeMRQRIAELEIQREEGRIQGQLNHSDSSQ 687
Cdd:pfam15921 293 QANSIQSQLeiiQEQARNQNSmymrqlSDLESTVSQLRSELREAKRM-----YEDKIEELEKQLVLANSELTEARTERDQ 367
|
330
....*....|....*....
gi 21687020 688 YIRE---LKDQIEELKAEV 703
Cdd:pfam15921 368 FSQEsgnLDDQLQKLLADL 386
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
523-707 |
8.04e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 523 RELKLQLQELsdtwQAHLArGGRWKESPRKL-----VVGELQDELMSVRLREAQALAEGRELRQRVVELETQDHI----- 592
Cdd:TIGR02168 216 KELKAELREL----ELALL-VLRLEELREELeelqeELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkel 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 593 --HRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAecksKEEVMAVRLREADSMAAVAEMRQRIAELEIQ 670
Cdd:TIGR02168 291 yaLANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL----AEELAELEEKLEELKEELESLEAELEELEAE 366
|
170 180 190
....*....|....*....|....*....|....*..
gi 21687020 671 REEgriqgqlnhsdSSQYIRELKDQIEELKAEVRLLK 707
Cdd:TIGR02168 367 LEE-----------LESRLEELEEQLETLRSKVAQLE 392
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
363-707 |
9.21e-05 |
|
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: 45.89 E-value: 9.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 363 LEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKgqvtRAQEAEENYvikrelAVVRQQCSSAAEDLQKAQSTIRQ 442
Cdd:pfam05557 109 LKNELSELRRQIQRAELELQSTNSELEELQERLDLLKA----KASEAEQLR------QNLEKQQSSLAEAEQRIKELEFE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 443 LQEQQENPRLTEDF------VSHLETELEQ-----SRLRET-ETLGALRE--------------MQDKVLDMEKRNSSLP 496
Cdd:pfam05557 179 IQSQEQDSEIVKNSkselarIPELEKELERlrehnKHLNENiENKLLLKEevedlkrklereekYREEAATLELEKEKLE 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 497 DE----------------------NNVAQLQEELKALKVREGQAVASTRELKLQLQELSDTWQAHLA-----RGGRWKES 549
Cdd:pfam05557 259 QElqswvklaqdtglnlrspedlsRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKkiedlNKKLKRHK 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 550 P------RKLVVGELQDELMSVRLR----EAQALAEGRELRQRVVELETQDHIHRNLLNRVEAERAALQEKLQYLAAQNK 619
Cdd:pfam05557 339 AlvrrlqRRVLLLTKERDGYRAILEsydkELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQ 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 620 GLQTQLSESRRKQAEAE-CKSKEEVMAVRLREADSMAAVAEMRQRIAELEIQREEGRIQGQLNHSDS----------SQY 688
Cdd:pfam05557 419 TLERELQALRQQESLADpSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTkvlhlsmnpaAEA 498
|
410
....*....|....*....
gi 21687020 689 IRELKDQIEELKAEVRLLK 707
Cdd:pfam05557 499 YQQRKNQLEKLQAEIERLK 517
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
469-708 |
1.04e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 469 LRETETLGALREMQDKVLDMEKRNSSLPDEnnVAQLQEELKALKVREGQAVASTRELKLQLQELSdtwQAHLARGGRWKE 548
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSSLQSE--LRRIENRLDELSQELSDASRKIGEIEKEIEQLE---QEEEKLKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 549 SPRKLvvGELQDELMSVRlreaqalAEGRELRQRVVELETQDHIHRNLLNRVEAERAalQEKLQYLAAQNKGLQTQLSES 628
Cdd:TIGR02169 742 LEEDL--SSLEQEIENVK-------SELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 629 RRKQAEAECKSKEEvmavRLREADSMAAVAEMRQRIAELEIQREEGRIQGQLNHSDssqyIRELKDQIEELKAEVRLLKG 708
Cdd:TIGR02169 811 EARLREIEQKLNRL----TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK----KEELEEELEELEAALRDLES 882
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
354-700 |
1.04e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 354 KYNPKKMKRLEKEYAAMKSKEMEEQIEIKRLRTENR--------------LLKQRIETLEKGQVTR-AQEAEENYVIKRE 418
Cdd:PTZ00121 1105 KTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARkaeearkaedakrvEIARKAEDARKAEEARkAEDAKKAEAARKA 1184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 419 LAVVRQQCSSAAEDLQKAQSTIRQLQEQQ-ENPRLTEDFVSHLET-ELEQSRLRETETLGA--LREMQDKVLDMEKRNSS 494
Cdd:PTZ00121 1185 EEVRKAEELRKAEDARKAEAARKAEEERKaEEARKAEDAKKAEAVkKAEEAKKDAEEAKKAeeERNNEEIRKFEEARMAH 1264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 495 LPDENNVAQLQEELKALKVREGQAVASTREL-KLQLQELSDTWQAHLARGGRWKESPRKLVVGELQDELMSVRLREAQAL 573
Cdd:PTZ00121 1265 FARRQAAIKAEEARKADELKKAEEKKKADEAkKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 574 AEGRELRQRvvelETQDHIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEV--MAVRLREA 651
Cdd:PTZ00121 1345 AEAAKAEAE----AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELkkAAAAKKKA 1420
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 21687020 652 DSMAAVAEMRQRIAELEIQREEGRIQGQL-NHSDSSQYIRELKDQIEELK 700
Cdd:PTZ00121 1421 DEAKKKAEEKKKADEAKKKAEEAKKADEAkKKAEEAKKAEEAKKKAEEAK 1470
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
558-706 |
1.54e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 558 LQDELMSVRLREAQALAEGRELRQR--VVELETQDHIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRR----- 630
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDalpel 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 631 ---------KQAEAECKSKEEVMAVRLREADSmaAVAEMRQRIAELE--IQREEGRIQGQLNHSDSSQYIRE--LKDQIE 697
Cdd:COG3206 260 lqspviqqlRAQLAELEAELAELSARYTPNHP--DVIALRAQIAALRaqLQQEAQRILASLEAELEALQAREasLQAQLA 337
|
....*....
gi 21687020 698 ELKAEVRLL 706
Cdd:COG3206 338 QLEARLAEL 346
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
364-700 |
2.04e-04 |
|
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: 44.68 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 364 EKEYAAMKSKEMEEQI-----EIKRLRTENRLLKQRIETLEKG----------------QVTRAQE-------AEENYVI 415
Cdd:pfam05622 8 EKDELAQRCHELDQQVsllqeEKNSLQQENKKLQERLDQLESGddsgtpggkkylllqkQLEQLQEenfrletARDDYRI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 416 K-----RELAVVRQQcssaAEDLQKAQSTIRQLQEQQENPRLTEDFVSHLETELEQSRlRETETLGALREmQDKVLdmEK 490
Cdd:pfam05622 88 KceeleKEVLELQHR----NEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYK-KKLEDLGDLRR-QVKLL--EE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 491 RNSSLPDENnvAQLQEELKalkvREGQAVASTRELKLQLQELSDTWQAHLARGGRWKESPRKL-----VVGELQDELMSV 565
Cdd:pfam05622 160 RNAEYMQRT--LQLEEELK----KANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLeekleALQKEKERLIIE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 566 R--LREAQ-----ALAEGRELRQRVVELETQDHIHRNLlnRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECK 638
Cdd:pfam05622 234 RdtLRETNeelrcAQLQQAELSQADALLSPSSDPGDNL--AAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQ 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21687020 639 SKEEVMAVR--LREADSMAavaemRQRIAELEIQREE--GRIQGQLNHS-DSSQYIRELKDQIEELK 700
Cdd:pfam05622 312 LLEDANRRKneLETQNRLA-----NQRILELQQQVEElqKALQEQGSKAeDSSLLKQKLEEHLEKLH 373
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
359-703 |
2.90e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 359 KMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLekgQVTRAQEAEENYVIKRELAVVRQQCSSAAEDLQKAQS 438
Cdd:TIGR00618 404 ILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELC---AAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQ 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 439 TIRQ-----------LQEQQENPRLTEDFVSHLETELEQSRLRETETlgalREMQDKVLDMEKRNSSLpdENNVAQLQEE 507
Cdd:TIGR00618 481 IHLQetrkkavvlarLLELQEEPCPLCGSCIHPNPARQDIDNPGPLT----RRMQRGEQTYAQLETSE--EDVYHQLTSE 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 508 LKALKvregqavastrELKLQLQELSDTWQAHLARGGRWKESPRKL--VVGELQDEL-MSVRLREAQALAEGRELRQRVV 584
Cdd:TIGR00618 555 RKQRA-----------SLKEQMQEIQQSFSILTQCDNRSKEDIPNLqnITVRLQDLTeKLSEAEDMLACEQHALLRKLQP 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 585 ELETQDhihrnllnrVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKS-KEEVMAVRLREADsmaavaEMRQR 663
Cdd:TIGR00618 624 EQDLQD---------VRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVlPKELLASRQLALQ------KMQSE 688
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 21687020 664 IAELEIQREEgriqgqLNHSDSSqyIRELKDQIEELKAEV 703
Cdd:TIGR00618 689 KEQLTYWKEM------LAQCQTL--LRELETHIEEYDREF 720
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
358-702 |
3.09e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 358 KKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKgqvtRAQEAEEnyvIKRELAVVRQQCSSAAEDLQKAQ 437
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEE---LEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 438 STIRQLQEQQENprlTEDFVSHLEtELEQSRLRETETLGALREMQDKVLDMEKRNSSLpdENNVAQLQEELKALKVREGQ 517
Cdd:PRK03918 266 ERIEELKKEIEE---LEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL--EEEINGIEERIKELEEKEER 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 518 AvastRELKLQLQELSDtwqahlaRGGRWKESPRKLvvgelqDELMSVrlreaqaLAEGRELRQRVVELETQDHIhrNLL 597
Cdd:PRK03918 340 L----EELKKKLKELEK-------RLEELEERHELY------EEAKAK-------KEELERLKKRLTGLTPEKLE--KEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 598 NRVEAERAALQEKLQYLAAQNKGLQTQLSESRR-----KQAEAEC---------KSKEEVMAVRLREadsMAAVAEMRQR 663
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKaieelKKAKGKCpvcgrelteEHRKELLEEYTAE---LKRIEKELKE 470
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 21687020 664 IAELE--IQREEGRIQGQLNHSDSSQYIRELKDQIEELKAE 702
Cdd:PRK03918 471 IEEKErkLRKELRELEKVLKKESELIKLKELAEQLKELEEK 511
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
374-707 |
3.34e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 374 EMEEQIEIKrlrtENRLLKQRIETLEKgQVTRAQEAEENYVIKRElavvrqqcsSAAEDLQKAQSTIRQLQEQQENprlt 453
Cdd:PRK02224 191 QLKAQIEEK----EEKDLHERLNGLES-ELAELDEEIERYEEQRE---------QARETRDEADEVLEEHEERREE---- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 454 edfVSHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDENNVAQLQEELKAlkvregqavASTRELKLQLQELS 533
Cdd:PRK02224 253 ---LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDD---------ADAEAVEARREELE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 534 DtwqahlarggrwKESprklvvgELQDELMSVR------------LREAQALAEGR--ELRQRVVELETQDHIHRNLLNR 599
Cdd:PRK02224 321 D------------RDE-------ELRDRLEECRvaaqahneeaesLREDADDLEERaeELREEAAELESELEEAREAVED 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 600 VEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAEckskEEVMAVRLREADSMAAVAEMRQRIAELEIQREEGRIQ-- 677
Cdd:PRK02224 382 RREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR----EERDELREREAELEATLRTARERVEEAEALLEAGKCPec 457
|
330 340 350
....*....|....*....|....*....|.
gi 21687020 678 GQ-LNHSDSSQYIRELKDQIEELKAEVRLLK 707
Cdd:PRK02224 458 GQpVEGSPHVETIEEDRERVEELEAELEDLE 488
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
380-531 |
4.19e-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: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 380 EIKRLRTENRLLKQRIETLEKgQVTRAQEAEENyvIKRELAVVRQQCSSAAEDLQKAQSTIRQLQEQQENPRLTEDFvSH 459
Cdd:COG1579 18 ELDRLEHRLKELPAELAELED-ELAALEARLEA--AKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEY-EA 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21687020 460 LETELEQSRLRETETLGALREMQDKVLDMEKRNSSLpdENNVAQLQEELKALKVREGQAVASTRELKLQLQE 531
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAEL--EAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
349-700 |
4.57e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 349 KAYQVKYNPKKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKGQVT--RAQEAEENYVIKRELAVVRQQC 426
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAkkKADEAKKKAEEKKKADEAKKKA 1440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 427 SSA--AEDLQKAQSTIRQ---LQEQQENPRLTEDfvshLETELEQSRLREtETLGALREMQDKVLDMEKRNSSLPDENNV 501
Cdd:PTZ00121 1441 EEAkkADEAKKKAEEAKKaeeAKKKAEEAKKADE----AKKKAEEAKKAD-EAKKKAEEAKKKADEAKKAAEAKKKADEA 1515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 502 AQLQEELKALKVREGQAVASTRELKlQLQELSDTWQAHLARGGRWKESPRKLVVGELQDELMSVRLREAQALAEGRELRQ 581
Cdd:PTZ00121 1516 KKAEEAKKADEAKKAEEAKKADEAK-KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 582 RVVE--LETQDHIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVMAVRlreADSMAAVAE 659
Cdd:PTZ00121 1595 EEVMklYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK---AAEEAKKAE 1671
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 21687020 660 MRQRIAElEIQREEgriQGQLNHSDSSQYIRELKDQIEELK 700
Cdd:PTZ00121 1672 EDKKKAE-EAKKAE---EDEKKAAEALKKEAEEAKKAEELK 1708
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
362-680 |
4.89e-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: 43.63 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 362 RLEKEYAAMKSKEMEEQIE----IKRLRTENRLLKQRIETLEKGQVTRAQEAEENYVIKRELAVVRQQCSSAAeDLQKAQ 437
Cdd:pfam01576 240 KKEEELQAALARLEEETAQknnaLKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTL-DTTAAQ 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 438 STIRQLQEQQ--ENPRLTEDFVSHLETELEQSRLRETETLGALREMQDKV----LDMEKRNSSLPDENNvaQLQEELKAL 511
Cdd:pfam01576 319 QELRSKREQEvtELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAkrnkANLEKAKQALESENA--ELQAELRTL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 512 KVREGQAVASTRELKLQLQELsdtwQAHLARGGRWKESpRKLVVGELQDELMSVRLREAQALAEGRELRQRVVELETQDH 591
Cdd:pfam01576 397 QQAKQDSEHKRKKLEGQLQEL----QARLSESERQRAE-LAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQ 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 592 IHRNLLN--------------RVEAERAALQEKL-------QYLAAQNKGLQTQLSESRRKQAE--AECKSKEEVMAVRL 648
Cdd:pfam01576 472 DTQELLQeetrqklnlstrlrQLEDERNSLQEQLeeeeeakRNVERQLSTLQAQLSDMKKKLEEdaGTLEALEEGKKRLQ 551
|
330 340 350
....*....|....*....|....*....|...
gi 21687020 649 READsmAAVAEMRQRIAELE-IQREEGRIQGQL 680
Cdd:pfam01576 552 RELE--ALTQQLEEKAAAYDkLEKTKNRLQQEL 582
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
358-700 |
6.12e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 358 KKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKgQVTRAQEAEENYV-IKRELAVVrqqcssaaEDLQKA 436
Cdd:PRK03918 293 EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE-KEERLEELKKKLKeLEKRLEEL--------EERHEL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 437 QSTIRQLQEQQEN--PRLTEDFVSHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPD----------------- 497
Cdd:PRK03918 364 YEEAKAKKEELERlkKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKaieelkkakgkcpvcgr 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 498 -------ENNVAQLQEELKALKVREGQAVASTRELKLQLQELsDTWQAHLARGGRWKESPRKLVvgELQDELMSVRLREA 570
Cdd:PRK03918 444 elteehrKELLEEYTAELKRIEKELKEIEEKERKLRKELREL-EKVLKKESELIKLKELAEQLK--ELEEKLKKYNLEEL 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 571 QALA-EGRELRQRVVELETQDHIHRNLLNRVEA---ERAALQEKLQYLAAQNKGLQTQLSE---SRRKQAEAECKSKEEV 643
Cdd:PRK03918 521 EKKAeEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEElgfESVEELEERLKELEPF 600
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 21687020 644 MA--VRLREADSMAAVAEMRQRIAELEIQREEGRIQGQLNHsdssqyIRELKDQIEELK 700
Cdd:PRK03918 601 YNeyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKR------LEELRKELEELE 653
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
418-676 |
6.61e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 418 ELAVVRQQCSSAAEDLQKAQSTIRQLQEQQENPRLTedfVSHLETELEQSRLRETETLGA-LREMQDKVLDMEKRNSSLP 496
Cdd:PRK04863 838 ELRQLNRRRVELERALADHESQEQQQRSQLEQAKEG---LSALNRLLPRLNLLADETLADrVEEIREQLDEAEEAKRFVQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 497 D--------ENNVAQLQ---EELKALKVREGQAVASTRELKLQLQELSDTWQ--AHLArggrWKESPRKLVVGELQDELM 563
Cdd:PRK04863 915 QhgnalaqlEPIVSVLQsdpEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrrAHFS----YEDAAEMLAKNSDLNEKL 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 564 SVRLREA-QALAEGRE-LRQRVVELETQDHIHRNLLNRVEAERAALQEKLQYLAAqnkgLQTQLSESrrkqAEAECKSKE 641
Cdd:PRK04863 991 RQRLEQAeQERTRAREqLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQD----LGVPADSG----AEERARARR 1062
|
250 260 270
....*....|....*....|....*....|....*
gi 21687020 642 EVMAVRLREADSMAAVAEMRQRIAELEIQREEGRI 676
Cdd:PRK04863 1063 DELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKL 1097
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
375-617 |
7.31e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 375 MEEQIEIKRLRTENRL--LKQRIETLEKgQVTRAQEAEENYvikrelavvrqqcssaaedlqKAQSTIRQLQEQQEnprL 452
Cdd:COG3206 162 LEQNLELRREEARKALefLEEQLPELRK-ELEEAEAALEEF---------------------RQKNGLVDLSEEAK---L 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 453 TEDFVSHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDENNVAQLQEELKALKVREGQAVA-------STREL 525
Cdd:COG3206 217 LLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSArytpnhpDVIAL 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 526 KLQLQELSDTWQAHLARGGRWKESPRKLV---VGELQDELMSVRLREAQALAEGRELRQRVVELETQDHIHRNLLNRVEA 602
Cdd:COG3206 297 RAQIAALRAQLQQEAQRILASLEAELEALqarEASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE 376
|
250
....*....|....*
gi 21687020 603 erAALQEKLQYLAAQ 617
Cdd:COG3206 377 --ARLAEALTVGNVR 389
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
347-526 |
8.63e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 347 VLKAYQVKYNPKKMKRLEKEYAAMKSKEMEEQIEIKRlrTENRLLKQRIETLEKGQVTRAQEaEENYVIKRELAVVRQQC 426
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK--KVEQLKKKEAEEKKKAEELKKAE-EENKIKAAEEAKKAEED 1673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 427 SSAAEDLQKAQSTIR----QLQEQQENPRLTEDFVSHLETEL---EQSRLRETETLGALREMQDKVLDMEKRNSSLPDE- 498
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKkaaeALKKEAEEAKKAEELKKKEAEEKkkaEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDe 1753
|
170 180 190
....*....|....*....|....*....|...
gi 21687020 499 ---NNVAQL--QEELKALKVREGQAVASTRELK 526
Cdd:PTZ00121 1754 eekKKIAHLkkEEEKKAEEIRKEKEAVIEEELD 1786
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
357-636 |
9.02e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 9.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 357 PKKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEkgqvtraqeaeenyvikRELAVVRQQCSSAAEDLQKA 436
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE-----------------RRIAALARRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 437 QSTIRQLQEQQEnprltedfvsHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSlpdenNVAQLQEELKALKVREG 516
Cdd:COG4942 82 EAELAELEKEIA----------ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPE-----DFLDAVRRLQYLKYLAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 517 QAVASTRELKLQLQELSdtwqahlarggrwkesprklvvgELQDELMSVRLREAQALAEGRELRQRVVELETQdhiHRNL 596
Cdd:COG4942 147 ARREQAEELRADLAELA-----------------------ALRAELEAERAELEALLAELEEERAALEALKAE---RQKL 200
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 21687020 597 LNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAE 636
Cdd:COG4942 201 LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
430-674 |
1.10e-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: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 430 AEDLQKAQSTIRQLQEQQENPRLTEDFVSHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDEnnvaqLQEELK 509
Cdd:pfam07888 44 AELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE-----LSEEKD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 510 ALKVREGQAVASTRELKLQLQELSDTWQAHLARGGRWKESPRKLVV--GELQDELMSVRLREAQALAEGRELRQRVVELe 587
Cdd:pfam07888 119 ALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAqrKEEEAERKQLQAKLQQTEEELRSLSKEFQEL- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 588 tqdhihRNLLNRVEAERAALQEKLQYlaaqnkgLQTQLSESRRKQAEAEcKSKEEVMAVRLREADSMAAVAEMRQRIAEL 667
Cdd:pfam07888 198 ------RNSLAQRDTQVLQLQDTITT-------LTQKLTTAHRKEAENE-ALLEELRSLQERLNASERKVEGLGEELSSM 263
|
....*..
gi 21687020 668 EIQREEG 674
Cdd:pfam07888 264 AAQRDRT 270
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
569-673 |
1.17e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.31 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 569 EAQALAEGRELRQRVvELETQdhihrNLLNRVEAEraalQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSkeevmavRL 648
Cdd:PTZ00491 667 AARHQAELLEQEARG-RLERQ-----KMHDKAKAE----EQRTKLLELQAESAAVESSGQSRAEALAEAEA-------RL 729
|
90 100 110
....*....|....*....|....*....|.
gi 21687020 649 READSMAAVAEMR---QRI---AELEIQREE 673
Cdd:PTZ00491 730 IEAEAEVEQAELRakaLRIeaeAELEKLRKR 760
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
380-671 |
1.46e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.09 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 380 EIKRLRTENRLLKQRIETLekgqvTRAQEaeenyvIKRELAVVRQQCSSAAEDLQKAQSTIRQLQEQQ--ENPRLTEDFV 457
Cdd:PRK10246 231 EEKQLLTAQQQQQQSLNWL-----TRLDE------LQQEASRRQQALQQALAAEEKAQPQLAALSLAQpaRQLRPHWERI 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 458 SHLETELEQSRLRETETLGALREMQdkVLDMEKRNSSLpdeNNVAQLQEELKALkvreGQAVASTRELKLQLQELSDtWQ 537
Cdd:PRK10246 300 QEQSAALAHTRQQIEEVNTRLQSTM--ALRARIRHHAA---KQSAELQAQQQSL----NTWLAEHDRFRQWNNELAG-WR 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 538 AHLARGGRWKESPRKLvvgelQDELMSVRLRE---------------AQALA---EGRELRQRVVELETQdhiHRNLLNR 599
Cdd:PRK10246 370 AQFSQQTSDREQLRQW-----QQQLTHAEQKLnalpaitltltadevAAALAqhaEQRPLRQRLVALHGQ---IVPQQKR 441
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21687020 600 veaeRAALQEKLQYLAAQNKGLQTQLSESRRKQAEaeckSKEEVMAVRlreadsmaAVAEMRQRIAELEIQR 671
Cdd:PRK10246 442 ----LAQLQVAIQNVTQEQTQRNAALNEMRQRYKE----KTQQLADVK--------TICEQEARIKDLEAQR 497
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
431-712 |
1.56e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 431 EDLQKAQSTIRQLQEQQEnpRLT---EDFVSHLETELEQSRLRETETLGALREMQDKVLDMEKRnsslpdennVAQLQEE 507
Cdd:COG4913 235 DDLERAHEALEDAREQIE--LLEpirELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE---------LEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 508 LKALKVREGQAVASTRELKLQLQELSdtwQAHLARGGRwkesprklvvgelqdelmsvRLREAQalaegRELRQRVVELE 587
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELE---AQIRGNGGD--------------------RLEQLE-----REIERLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 588 tqdhihrnllnRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVMAVRLREADSMAAVAEMRQRIAEL 667
Cdd:COG4913 356 -----------ERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL 424
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 21687020 668 --EIQREEGRiqgqlnHSDSSQYIRELKDQIEElkaEVRLLKGPPPF 712
Cdd:COG4913 425 eaEIASLERR------KSNIPARLLALRDALAE---ALGLDEAELPF 462
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
354-700 |
1.62e-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: 42.27 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 354 KYNPKKMKRLEKEyAAMKSKEMEEQIEIKRL-RTENRLLKQRIETLEKGQVTRAQEAEENYVI---------------KR 417
Cdd:pfam02463 166 RLKRKKKEALKKL-IEETENLAELIIDLEELkLQELKLKEQAKKALEYYQLKEKLELEEEYLLyldylklneeridllQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 418 ELAVVRQQCSSAAEDLQKAQSTIRQLQEQQENP----RLTEDFVSHLETELEQSRLRETETLGALREMQDKVLDMEKRNS 493
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEekekKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 494 SLPDENN-----VAQLQEELKALKVREGQAVASTRELKLQLQELSDTWQAHLA-RGGRWKESPRKLVVGELQDELMSVRL 567
Cdd:pfam02463 325 KAEKELKkekeeIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAkKKLESERLSSAAKLKEEELELKSEEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 568 REAQALAEgrelrqrvvELETQDHIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEaecKSKEEVMAVR 647
Cdd:pfam02463 405 KEAQLLLE---------LARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK---DELELKKSED 472
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 21687020 648 LREADSMaaVAEMRQRIAELEIQREEGRIQGQLNHSDSSQYIRELKDQIEELK 700
Cdd:pfam02463 473 LLKETQL--VKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGR 523
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
418-708 |
1.82e-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: 41.86 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 418 ELAVVRQQCSSAAEDLQKAQSTIRQLQEQQEN--PRLTE-----DFVSHLETELEQSRLRE-TETLGALREMQDKVLDME 489
Cdd:COG3096 837 ELAALRQRRSELERELAQHRAQEQQLRQQLDQlkEQLQLlnkllPQANLLADETLADRLEElREELDAAQEAQAFIQQHG 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 490 KRNSSLpdENNVAQLQ---EELKALKVREGQAVASTRELKLQLQELSDTWQ--AHLArggrWKESPRklvvgelqdelms 564
Cdd:COG3096 917 KALAQL--EPLVAVLQsdpEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQrrPHFS----YEDAVG------------- 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 565 vRLREAQALAEgrELRQRVVELETQdhihrnllnRVEAERAALQEKLQYlaAQNKGLQTQLSESRRKQAEAECKSKEEVM 644
Cdd:COG3096 978 -LLGENSDLNE--KLRARLEQAEEA---------RREAREQLRQAQAQY--SQYNQVLASLKSSRDAKQQTLQELEQELE 1043
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21687020 645 AVRLREADSMAAVAEMRQRiaeleiqreegRIQGQLNHSDSSqyIRELKDQIEELKAEVRLLKG 708
Cdd:COG3096 1044 ELGVQADAEAEERARIRRD-----------ELHEELSQNRSR--RSQLEKQLTRCEAEMDSLQK 1094
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
568-708 |
2.13e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 568 REAQALAEGRELRQRVVELETQDHIHRNLLNRVEAERA------ALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKE 641
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREkaeryqALLKEKREYEGYELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21687020 642 EVMAVRLREADsmaavaEMRQRIAELEIQREEgrIQGQLNHSDSSQYIReLKDQIEELKAEVRLLKG 708
Cdd:TIGR02169 251 EELEKLTEEIS------ELEKRLEEIEQLLEE--LNKKIKDLGEEEQLR-VKEKIGELEAEIASLER 308
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
502-707 |
2.41e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 502 AQLQEELKALKVREGQAVASTRELKLQLQELSDTWQAHLARggrwkesprklvVGELQDELMSVRLREAQALAEGRELRQ 581
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR------------IAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 582 RVVELETQDHIHRNLLNRV--EAERAALQEKLQYLAAQNKGLQT--------QLSESRRKQAEAECKSKEEVMAVRlrea 651
Cdd:COG4942 91 EIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEDFLDAvrrlqylkYLAPARREQAEELRADLAELAALR---- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21687020 652 dsmAAVAEMRQRIAELEIQREEGRIQGQLNHSDSSQYIRELKDQIEELKAEVRLLK 707
Cdd:COG4942 167 ---AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
508-669 |
3.36e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 40.42 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 508 LKALKVREGQAVA--------STRELKLQLQELS---DTWQAHLARGGRWKESPRKLVVGELQDELMSVRLREAQalaeg 576
Cdd:COG1566 56 VTEVLVKEGDRVKkgqvlarlDPTDLQAALAQAEaqlAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQ----- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 577 RELrQRVVELETQDHIHRNLLNRVEAERAALQEKLQylAAQnkglqtqlseSRRKQAEAECKSKEEVMAVRLREADSMAA 656
Cdd:COG1566 131 REL-ERYQALYKKGAVSQQELDEARAALDAAQAQLE--AAQ----------AQLAQAQAGLREEEELAAAQAQVAQAEAA 197
|
170
....*....|...
gi 21687020 657 VAEMRQRIAELEI 669
Cdd:COG1566 198 LAQAELNLARTTI 210
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
406-708 |
3.40e-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: 40.93 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 406 AQEAEENYVIKRELAVVRQQCSSAAEDLQKAQSTI-RQLQEQQENPRLTEDFVSHLETELEQ----------SRLRETET 474
Cdd:pfam01576 642 ARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVgKNVHELERSKRALEQQVEEMKTQLEEledelqatedAKLRLEVN 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 475 LGAL-----REMQDKVLDMEKRNSSLPDEnnVAQLQEELKALKVREGQAVASTRELKLQLQELsdtwQAHLARGGRWKES 549
Cdd:pfam01576 722 MQALkaqfeRDLQARDEQGEEKRRQLVKQ--VRELEAELEDERKQRAQAVAAKKKLELDLKEL----EAQIDAANKGREE 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 550 P----RKL--VVGELQDELMSVRLREAQALAEGRELRQRVVELE------TQDHIHRNLLNR-VEAERAALQEKlqyLAA 616
Cdd:pfam01576 796 AvkqlKKLqaQMKDLQRELEEARASRDEILAQSKESEKKLKNLEaellqlQEDLAASERARRqAQQERDELADE---IAS 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 617 QNKGLQTQLSESRRkqAEAECKSKEEvmavRLREADSMAAVAEMRQRIAELEIQREEGRIQGQLNHSDSSQYIRE-LKDQ 695
Cdd:pfam01576 873 GASGKSALQDEKRR--LEARIAQLEE----ELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQqLERQ 946
|
330
....*....|...
gi 21687020 696 IEELKAEVRLLKG 708
Cdd:pfam01576 947 NKELKAKLQEMEG 959
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
348-707 |
3.56e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 348 LKAYQVKYNPKKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKGqVTRAQEAE-ENYVIKREL------- 419
Cdd:PRK03918 374 LERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKA-IEELKKAKgKCPVCGRELteehrke 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 420 --AVVRQQCSSAAEDLQKAQSTIRQLQEQqenprltedfvshlETELEQSRLRETEtLGALREMQDKVLDMEKRNSSLPD 497
Cdd:PRK03918 453 llEEYTAELKRIEKELKEIEEKERKLRKE--------------LRELEKVLKKESE-LIKLKELAEQLKELEEKLKKYNL 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 498 EnNVAQLQEELKALKVREGQAVASTRELKLQLQELSD--TWQAHLARGGRWKESPRKLVVGELQDELMSVRLREAQALAE 575
Cdd:PRK03918 518 E-ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKE 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 576 GRELRQRVVELETQDHIHRNLLNRVEAERAALQEKLQYLAAQNKGLQ---TQLSESRRKQAEAECKSKEEVMaVRLREad 652
Cdd:PRK03918 597 LEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEelrKELEELEKKYSEEEYEELREEY-LELSR-- 673
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 21687020 653 smaAVAEMRQRIAELEIQREEGRiqgqlnhsDSSQYIRELKDQIEELKAEVRLLK 707
Cdd:PRK03918 674 ---ELAGLRAELEELEKRREEIK--------KTLEKLKEELEEREKAKKELEKLE 717
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
387-701 |
3.82e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 387 ENRLlkqrieTLEKGQVTRAQEAEENYVIKRELAVV----------RQQCSSAAEDLQKAQSTIRQLQEQQENpRLTE-- 454
Cdd:PRK04863 241 ENRM------TLEAIRVTQSDRDLFKHLITESTNYVaadymrhaneRRVHLEEALELRRELYTSRRQLAAEQY-RLVEma 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 455 -------DFVSHLETELEQSRLRETETLGALREmQDK----VLDMEKRNSSLPDENNVAQL-QEELKALKVREGQAVAST 522
Cdd:PRK04863 314 relaelnEAESDLEQDYQAASDHLNLVQTALRQ-QEKieryQADLEELEERLEEQNEVVEEaDEQQEENEARAEAAEEEV 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 523 RELKLQLqelSDTWQAHLA---RGGRWKESPRKLVVGELQDELMSVRLREAQAL-----AEGRELRQRVVELETQDHIHR 594
Cdd:PRK04863 393 DELKSQL---ADYQQALDVqqtRAIQYQQAVQALERAKQLCGLPDLTADNAEDWleefqAKEQEATEELLSLEQKLSVAQ 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 595 NLLNR--------------VEAERAALQ--------EKLQYLAAQNKGLQTQLSESRR---KQAEAECKSKEEVMAVRLR 649
Cdd:PRK04863 470 AAHSQfeqayqlvrkiageVSRSEAWDVarellrrlREQRHLAEQLQQLRMRLSELEQrlrQQQRAERLLAEFCKRLGKN 549
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 21687020 650 EADSMAAVAEMRQRIAELEIQREEGRIQGQlNHSDSSQYIRELKDQIEELKA 701
Cdd:PRK04863 550 LDDEDELEQLQEELEARLESLSESVSEARE-RRMALRQQLEQLQARIQRLAA 600
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
358-670 |
4.43e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 358 KKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKgQVTRAQEAEENYVIKRELAVVRQQCSSAAEDLQKAQ 437
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 438 STIRQLQEQQENPRLTEDFVSHL--ETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDENNVAQLQEELKAL-KVR 514
Cdd:COG4717 271 LILTIAGVLFLVLGLLALLFLLLarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIeELQ 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 515 EGQAVASTRELKLQLQELSDTWQAHLARGG---------RWKESPRKLvvgELQDELMSVRLREAQALAEGRELRQRVVE 585
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAALLAEAGvedeeelraALEQAEEYQ---ELKEELEELEEQLEELLGELEELLEALDE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 586 LETQDHIH--RNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVMAVRLREADSMAAVAEMRQR 663
Cdd:COG4717 428 EELEEELEelEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEARE 507
|
....*..
gi 21687020 664 IAELEIQ 670
Cdd:COG4717 508 EYREERL 514
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
551-706 |
4.87e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 551 RKLVVGELQDELMSVRLREAQALAEGRELRQRVVELETQdhihrnlLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRR 630
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQ-------VERLEAEVEELEAELEEKDERIERLERELSEARS 455
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21687020 631 KQAEAECKSKEevmavrlreadsmaaVAEMRQRIAELEIQREEGRiqgqlnhsdssQYIRELKDQIEELKAEVRLL 706
Cdd:COG2433 456 EERREIRKDRE---------------ISRLDREIERLERELEEER-----------ERIEELKRKLERLKELWKLE 505
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
380-700 |
5.38e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.28 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 380 EIKRLRTENRLLKQRIE-TLEKGQVTRAQeaeenyviKRELAVVRQQCSSAAEDLQKAQSTIRQLQEQqENPRLTEDFVS 458
Cdd:PRK11281 50 KQKLLEAEDKLVQQDLEqTLALLDKIDRQ--------KEETEQLKQQLAQAPAKLRQAQAELEALKDD-NDEETRETLST 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 459 HLETELEQsrlRETETLGALREMQdkvldmekrnsslpdeNNVAQLQEELKALKVREGQAVASTRELKLQLQELSdtwqA 538
Cdd:PRK11281 121 LSLRQLES---RLAQTLDQLQNAQ----------------NDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIR----N 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 539 HLARGGRWKESPRKLVVGELQDELMSVrlrEAQAlaegrELRQRVVELETQdhihrnLLNRVEAERAALQEKLQYLAAQN 618
Cdd:PRK11281 178 LLKGGKVGGKALRPSQRVLLQAEQALL---NAQN-----DLQRKSLEGNTQ------LQDLLQKQRDYLTARIQRLEHQL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 619 KGLQTQLSESRRKQAE---AECKSKEEvmAVRLRE----ADSMAAVAEMRQRIAEL-----EIQREEGRIQGQLNHSDSS 686
Cdd:PRK11281 244 QLLQEAINSKRLTLSEktvQEAQSQDE--AARIQAnplvAQELEINLQLSQRLLKAteklnTLTQQNLRVKNWLDRLTQS 321
|
330
....*....|....
gi 21687020 687 QyiRELKDQIEELK 700
Cdd:PRK11281 322 E--RNIKEQISVLK 333
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
361-702 |
6.48e-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: 40.16 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 361 KRLEKEYAAMKSKEMEEQIEIKRL-RTENRL-------------LKQRIETLEKGQVTRAQEAEENYVIKRELAVVRQQC 426
Cdd:pfam01576 548 KRLQRELEALTQQLEEKAAAYDKLeKTKNRLqqelddllvdldhQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRA 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 427 SSAA-EDLQKAQSTIRQLQEQQENPRLTEDFVSHLETELEqsrlretETLGALREMQDKVLDMEKRNSSLpdENNVAQLQ 505
Cdd:pfam01576 628 EAEArEKETRALSLARALEEALEAKEELERTNKQLRAEME-------DLVSSKDDVGKNVHELERSKRAL--EQQVEEMK 698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 506 EELKALKVREGQAVASTRELKLQLQELSDTWQAHL-ARGGRWKESPRKLV--VGELQDELMSVRLREAQALAEGRELRQR 582
Cdd:pfam01576 699 TQLEELEDELQATEDAKLRLEVNMQALKAQFERDLqARDEQGEEKRRQLVkqVRELEAELEDERKQRAQAVAAKKKLELD 778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 583 VVELEtqDHIHRNLLNRVEAERaalqeKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVMAVRLREADSMA-----AV 657
Cdd:pfam01576 779 LKELE--AQIDAANKGREEAVK-----QLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQlqedlAA 851
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 21687020 658 AEMRQRIAELEiqREEgrIQGQLNHSDSSQYI-----RELKDQIEELKAE 702
Cdd:pfam01576 852 SERARRQAQQE--RDE--LADEIASGASGKSAlqdekRRLEARIAQLEEE 897
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
348-496 |
6.50e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.11 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 348 LKAYQVKYNPKKMKRLEKEYAA----MKSKEMEEQIEIKRLRTENRLLKQRIETLEKGQVTRAQEAEEN-YVIKREL--- 419
Cdd:pfam17380 425 IRAEQEEARQREVRRLEEERARemerVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRrKILEKELeer 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 420 --AVV---------------RQQCSSAAEDLQKAQSTIRQLQEQQENPRLTEDFVSHLEtelEQSRLretETLGALREMQ 482
Cdd:pfam17380 505 kqAMIeeerkrkllekemeeRQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE---ERSRL---EAMEREREMM 578
|
170
....*....|....
gi 21687020 483 DKVLDMEKRNSSLP 496
Cdd:pfam17380 579 RQIVESEKARAEYE 592
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
415-705 |
7.16e-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: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 415 IKRELAVVRQQCSSAAEDLQKAQSTIRQLQEQQENPRLTEDFVShleTELEQSRLRETETLGALREMQDKVLDMEKRNSS 494
Cdd:pfam12128 602 LRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFAR---TALKNARLDLRRLFDEKQSEKDKKNKALAERKD 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 495 LPDENnVAQLQEELKALKVREGQAVASTRElklQLQELSDTWQAHlarggrwkespRKLVVGELQDELMSVR----LREA 570
Cdd:pfam12128 679 SANER-LNSLEAQLKQLDKKHQAWLEEQKE---QKREARTEKQAY-----------WQVVEGALDAQLALLKaaiaARRS 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 571 QALAE--------GRELR------QRVVELETQdhiHRNLLNRVEAERAALQEKLQY-------LAAQNKGLQTQLSESR 629
Cdd:pfam12128 744 GAKAElkaletwyKRDLAslgvdpDVIAKLKRE---IRTLERKIERIAVRRQEVLRYfdwyqetWLQRRPRLATQLSNIE 820
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21687020 630 RKQAEAeckskeevmavrlrEADSMAAVAEMRQRIAELEIQREEGRIQGQLnhsdSSQYIRELKDQIEELkAEVRL 705
Cdd:pfam12128 821 RAISEL--------------QQQLARLIADTKLRRAKLEMERKASEKQQVR----LSENLRGLRCEMSKL-ATLKE 877
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
443-675 |
8.75e-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: 39.49 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 443 LQEQQENPRLTEDFVSHLETELEQSRLRETETLGALREMQDKVLDMEKrnsslpdenNVAQLQEELKALKVREGQAVAST 522
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKE---------ELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 523 RELKLQLQELSDTWQAHLARggrwkesprklvVGELQDELMSVRLREAQALAEGRELRQRVVELETQdhihrnlLNRVEA 602
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEAR------------IRELEEDIKTLTQRVLERETELERMKERAKKAGAQ-------RKEEEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21687020 603 ERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAEckskEEVMAVRLREADSMAAVAEMRQRIAELEIQREEGR 675
Cdd:pfam07888 172 ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRD----TQVLQLQDTITTLTQKLTTAHRKEAENEALLEELR 240
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
353-737 |
8.80e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 39.45 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 353 VKYNPKKmKRLEKEYAAMKSKEMEEQIEIKRLRTE------------NRLLKQRIETLEKGQVTRAQEAEENYVIKRELA 420
Cdd:PLN03229 411 VPVDPER-KVNMKKREAVKTPVRELEGEVEKLKEQilkakessskpsELALNEMIEKLKKEIDLEYTEAVIAMGLQERLE 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 421 VVRQQCSsaaedlqKAQStirqlQEQQENPRLTEDfVSHLETELEQsRLRETETLGALREMQDKvLDMEKRNSSLPDENN 500
Cdd:PLN03229 490 NLREEFS-------KANS-----QDQLMHPVLMEK-IEKLKDEFNK-RLSRAPNYLSLKYKLDM-LNEFSRAKALSEKKS 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 501 VAqlqEELKALKVREGQAVASTRELKLQLQELSDTWQ-AHLARGGRWKESPRKLVV---GELQDELMSVrLREAQALAEG 576
Cdd:PLN03229 555 KA---EKLKAEINKKFKEVMDRPEIKEKMEALKAEVAsSGASSGDELDDDLKEKVEkmkKEIELELAGV-LKSMGLEVIG 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 577 RELRQRVVELETQDhihrnllnrveaerAALQEKLQYLAAQ-NKGLQTQLSESrrkqaeaECKSKEEVMAVRLREADSMA 655
Cdd:PLN03229 631 VTKKNKDTAEQTPP--------------PNLQEKIESLNEEiNKKIERVIRSS-------DLKSKIELLKLEVAKASKTP 689
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 656 AVAEmRQRIAELEIQREEgRIQGQLNHSdssqyirELKDQIEELKAEVRLLKgpppfEDPLAFDGlSLARHLDEDSLPSS 735
Cdd:PLN03229 690 DVTE-KEKIEALEQQIKQ-KIAEALNSS-------ELKEKFEELEAELAAAR-----ETAAESNG-SLKNDDDKEEDSKE 754
|
..
gi 21687020 736 DE 737
Cdd:PLN03229 755 DG 756
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
416-588 |
9.23e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 39.63 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 416 KRELAVVRQQCSSAAEDLQKAQSTIRQLqeqqenprltEDFVSHLETELEQSRLrETETLGALREMQDKVLDMekrnssL 495
Cdd:pfam05667 334 EEELEELQEQLEDLESSIQELEKEIKKL----------ESSIKQVEEELEELKE-QNEELEKQYKVKKKTLDL------L 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687020 496 PD-ENNVAQLQEELKALKVRegqavastrelklqLQELSDTWQAH----------LARGGRWKESPRKLVVGELQDelMS 564
Cdd:pfam05667 397 PDaEENIAKLQALVDASAQR--------------LVELAGQWEKHrvplieeyraLKEAKSNKEDESQRKLEEIKE--LR 460
|
170 180
....*....|....*....|....*.
gi 21687020 565 VRLREAQALAEGRE--LRQRVVELET 588
Cdd:pfam05667 461 EKIKEVAEEAKQKEelYKQLVAEYER 486
|
|
| |
