|
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 |
2.75e-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: 2.75e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 112 IRKGIPHHFRAIVWQLLCSATDMPVKN---QYSELLKMSSPCEKL----IRRDIARTYPEHEFFKGQDSLGQEVLFNVMK 184
Cdd:smart00164 1 VRKGVPPSLRGVVWKLLLNAQPMDTSAdkdLYSRLLKETAPDDKSivhqIEKDLRRTFPEHSFFQDKEGPGQESLRRVLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 185 AYSLVDREVGYCQGSAFIVGLLLMQMP-EEEAFCVFVRLMQEYRLReLFKPSMAELGLCIYQFEYMLQEQLPDLNTHFRS 263
Cdd:smart00164 81 AYALYNPEVGYCQGMNFLAAPLLLVMEdEEDAFWCLVKLMERYGPN-FYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 229577000 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 |
6.48e-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: 6.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 152 KLIRRDIARTYPEHEFFKGQDslGQEVLFNVMKAYSLVDREVGYCQGSAFIVGLLLMQ-MPEEEAFCVFVRLMQEYRLRE 230
Cdd:pfam00566 10 EQIEKDVPRTFPHSFFFDNGP--GQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLVyLDEEDAFWCFVSLLENYLLRD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 231 LFKPSMAELGLCIYQFEYMLQEQLPDLNTHFRSQSFHTSMYASSWFLTLFLTTFPLPVATRVFDIFMYEGLEIV-FRVGL 309
Cdd:pfam00566 88 FYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVlFRVAL 167
|
170
....*....|.
gi 229577000 310 ALLQVNQAELM 320
Cdd:pfam00566 168 AILKRFREELL 178
|
|
| COG5210 |
COG5210 |
GTPase-activating protein [General function prediction only]; |
108-330 |
1.71e-43 |
|
GTPase-activating protein [General function prediction only];
Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 164.98 E-value: 1.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 108 LKELIRKGIPHHFRAIVWQLLCSATDM--PVKNQYSELLKM-------SSPCEKLIRRDIARTYPEHEFFKGQDSLGQEV 178
Cdd:COG5210 205 LRELIRKGIPNELRGDVWEFLLGIGFDldKNPGLYERLLNLhreakipTQEIISQIEKDLSRTFPDNSLFQTEISIRAEN 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 179 LFNVMKAYSLVDREVGYCQGSAFIVGLLLMQMPEEE-AFCVFVRLMQEYRLRELFKPSMAELGLCIYQFEYMLQEQLPDL 257
Cdd:COG5210 285 LRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVLESEEqAFWCLVKLLKNYGLPGYFLKNLSGLHRDLKVLDDLVEELDPEL 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 229577000 258 NTHFRSQSFHTSMYASSWFLTLFLTTFPLPVATRVFDIFMYEGLEIVFRVGLALLQVNQAELMQLDMEGMSQY 330
Cdd:COG5210 365 YEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKLDSDELLDL 437
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
363-762 |
9.84e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.36 E-value: 9.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 363 LEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYVIKRELAVVRQQCSSAAE 442
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 443 DLQKAQSTIRQLQEQQENprltedfvshLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLpdENNVAQLQEELKAL 522
Cdd:COG1196 345 ELEEAEEELEEAEAELAE----------AEEALLEAEAELAEAEEELEELAEELLEALRAAAEL--AAQLEELEEAEEAL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 523 KVREGQAVASTRELKLQLQELSDTwqahlarggrwkesprklvVGELQDELMSVRLREAQALAEGRELRQRVVELETQDH 602
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEE-------------------EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 603 IHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVMAVRLREADSMAAVAEMRQRIAELEIQR 682
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVV 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 683 EegriqgqlNHSDSSQYIRELKDQIEELKAEVRLLKGPPPFEDPLAFDGLSLARHLDEDSLPSSDEELLGVGVGAALQDA 762
Cdd:COG1196 554 E--------DDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
376-719 |
8.15e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.40 E-value: 8.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 376 EEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQeaeenyvIKRELAVVRQQCSSAAEDLQKAQSTIRQLQ 455
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ-------LRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 456 EQQENprlTEDFVSHLETELEQSRLRETETLGALREMQDKVLDMEKRnsslpdennVAQLQEELKALKVREGQAVASTRE 535
Cdd:TIGR02168 747 ERIAQ---LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ---------IEQLKEELKALREALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 536 LKLQLQELSDTWQAHLARGGRWKESprklvVGELQDELMSVRLREAQALAEGRELRQRVVELETQDHIHRNLLNRVEAER 615
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERR-----LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 616 AALQEKLQYLAAQNKGLQTQLSESRRKqaeaeckskeevmavrLREADSMAAVAEMRQRIAELEIQREEGRI--QGQLNH 693
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRE----------------LEELREKLAQLELRLEGLEVRIDNLQERLseEYSLTL 953
|
330 340
....*....|....*....|....*.
gi 229577000 694 SDSSQYIRELKDQIEELKAEVRLLKG 719
Cdd:TIGR02168 954 EEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
373-763 |
9.59e-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: 9.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 373 KEMEEQIE-IKRLRTEnrlLKQRIETLEKEsaaladrliqgqvtrAQEAEENYVIKRELAVVRQQcsSAAEDLQKAQSTI 451
Cdd:COG1196 182 EATEENLErLEDILGE---LERQLEPLERQ---------------AEKAERYRELKEELKELEAE--LLLLKLRELEAEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 452 RQLQEQQEnprltedfvsHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDENN-----VAQLQEELKALKVRE 526
Cdd:COG1196 242 EELEAELE----------ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellaeLARLEQDIARLEERR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 527 GQAVASTRELKLQLQELSDTWQAHLARGGRWKESprklvVGELQDELMSVRLREAQALAEGRELRQRVVELETQDHIHRN 606
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEE-----LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 607 LLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAEcKSKEEVMAVRLREADSMAAVAEMRQRIAELEIQREEGR 686
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE-EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 229577000 687 IQGQLNHSDSSQYIRELKDQIEELKAEVRLLKgpPPFEDPLAFDGLSLARHLDEDSLPSSDEELLGVGVGAALQDAL 763
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLL--EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
361-713 |
2.31e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 361 KRLEKEYAAMKSKEMEEQI--------------------EIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEA 420
Cdd:COG1196 285 EAQAEEYELLAELARLEQDiarleerrreleerleeleeELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 421 EENYVIKRELAVVRQQCSSAAEDLQKAQSTIRQLQEQQENPRLTEDFVSHLETELEQSRLRETETLGALREMQDKVLDME 500
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 501 KRnsslpDENNVAQLQEELKALKVREGQAVASTRELKLQLQELSDTWQAHLARgGRWKESPRKLVVGELQDELMSVRLRE 580
Cdd:COG1196 445 EE-----AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR-LLLLLEAEADYEGFLEGVKAALLLAG 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 581 AQALA-EGRELRQRVVELETQDHIH--RNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEvmAV 657
Cdd:COG1196 519 LRGLAgAVAVLIGVEAAYEAALEAAlaAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALAR--GA 596
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 229577000 658 RLREADSMAAVAEMRQRIAELEIQREEGRIQGQLNHSDSSQYIRELKDQIEELKAE 713
Cdd:COG1196 597 IGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLE 652
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
351-711 |
2.99e-09 |
|
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: 60.52 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 351 YQVKYNPKKMKrlEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYVIKREL 430
Cdd:pfam17380 256 YTVRYNGQTMT--ENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 431 AVVRQQCSSAAEDlQKAQSTIRQLQEQQENPRLTEDfvshlETELEQSRLRETETLGALREMQD-------------KVL 497
Cdd:pfam17380 334 AIYAEQERMAMER-ERELERIRQEERKRELERIRQE-----EIAMEISRMRELERLQMERQQKNervrqeleaarkvKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 498 DMEKRNSSLPDENNVAQLQEELKALKVREGQAVASTRELKLQLQELSDTWQAHLARGGRWKESPRKLVVGELQDElmsvr 577
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE----- 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 578 lREAQALAEgrELRQRVVELETQdhihrnllnrvEAERAALQE--KLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVM 655
Cdd:pfam17380 483 -KRDRKRAE--EQRRKILEKELE-----------ERKQAMIEEerKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEM 548
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 229577000 656 AVRLREADSMAAVAEMRQRIAELEIQREEGRiqgQLNHSDSSQYIRELKDQIEELK 711
Cdd:pfam17380 549 EERRRIQEQMRKATEERSRLEAMEREREMMR---QIVESEKARAEYEATTPITTIK 601
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
359-714 |
5.12e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.08 E-value: 5.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 359 KMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYVIKRELAVVRQQCS 438
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 439 SAAEDLQKAQSTIRQLQEQQENP--RLTEDFVSHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDE-NNVAQL 515
Cdd:TIGR02169 762 ELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEiQELQEQ 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 516 QEELKALKVREGQAVAstrELKLQLQELsdtwQAHLARggrwkespRKLVVGELQDELMSVRLREAQALAEGRELRQRVV 595
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIE---NLNGKKEEL----EEELEE--------LEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 596 ELETQDHIHRNLLNRVEAERAALQEKL-QYLAAQNKGLQTQLSESRRKQAEAECKSKEEvmAVRLREADSMAAV---AEM 671
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKLEALEEELsEIEDPKGEDEEIPEEELSLEDVQAELQRVEE--EIRALEPVNMLAIqeyEEV 984
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 229577000 672 RQRIAELEIQREegriqgQLNHSDSSqyIRELKDQIEELKAEV 714
Cdd:TIGR02169 985 LKRLDELKEKRA------KLEEERKA--ILERIEEYEKKKREV 1019
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
392-641 |
9.69e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 9.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 392 KQRIETLEKESAALADRL--IQGQVTRAQEAEENYVIKRELAVVRQQCSSAAEDLQKAQSTIRQLQEQQENPRLTEDFVS 469
Cdd:COG4913 609 RAKLAALEAELAELEEELaeAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 470 HLETELEQSRLRETETLGALREMQDKVLDMEKRnsslpdennVAQLQEELKALKVREGQAVASTRElkLQLQELSDTWQA 549
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKE---------LEQAEEELDELQDRLEAAEDLARL--ELRALLEERFAA 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 550 HLARGgrwkesPRKLVVGELQDELMSVRLREAQALAEGRELRQRVVE---LETQDHI--------HRNLLNRVEAER-AA 617
Cdd:COG4913 758 ALGDA------VERELRENLEERIDALRARLNRAEEELERAMRAFNRewpAETADLDadleslpeYLALLDRLEEDGlPE 831
|
250 260
....*....|....*....|....*....
gi 229577000 618 LQEKL-QYLAAQNK----GLQTQLSESRR 641
Cdd:COG4913 832 YEERFkELLNENSIefvaDLLSKLRRAIR 860
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
437-652 |
1.85e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 437 CSSAAEDLQKAQSTIRQLQEQQENprltedfvshLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLpdENNVAQLQ 516
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAE----------LEKELAALKKEEKALLKQLAALERRIAALARRIRAL--EQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 517 EELKALKVREGQAVASTRELKLQLQELSDTWQAhLARGGRWK-----ESPRKLV-VGELQDELMSVRLREAQALAEGR-E 589
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAELLRALYR-LGRQPPLAlllspEDFLDAVrRLQYLKYLAPARREQAEELRADLaE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 229577000 590 LRQRVVELETQDHIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKE 652
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
362-710 |
1.88e-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: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 362 RLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYVIKRELAVVRQQ---CS 438
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARlllLL 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 439 SAAEDLQKAQSTIRQLQEQQENPRLTEDFVSHLETELEQSRLRETETLGALremQDKVLDmekrnsslpDENNVAQLQEE 518
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL---QNIVVE---------DDEVAAAAIEY 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 519 LKALKVREGQAVASTRELKLQLQELSDTWQAH------LARGGRWKESPRKLVVGELQDELMSV-RLREAQALAEGRELR 591
Cdd:COG1196 566 LKAAKAGRATFLPLDKIRARAALAAALARGAIgaavdlVASDLREADARYYVLGDTLLGRTLVAaRLEAALRRAVTLAGR 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 592 QRVVELETQDHI------------HRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAE---CKSKEEVMA 656
Cdd:COG1196 646 LREVTLEGEGGSaggsltggsrreLLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEeerLEEELEEEA 725
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 229577000 657 VRLREADSMAAVAEMRQRIAELEIQREEGRIQGQLNHSDSSQYIRELKDQIEEL 710
Cdd:COG1196 726 LEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
358-717 |
2.02e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 358 KKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAAL--------ADRLIQGQVTRAQEAEENYvikRE 429
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLplyqeleaLEAELAELPERLEELEERL---EE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 430 LAVVRQQCSSAAEDLQKAQSTIRQLQEQQENPRLTEdfVSHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDE 509
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQLSLATEEE--LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 510 NNVAQLQEELKALKV--------------------------------------------REGQAVASTRELKLQLQELSD 545
Cdd:COG4717 236 LEAAALEERLKEARLllliaaallallglggsllsliltiagvlflvlgllallflllaREKASLGKEAEELQALPALEE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 546 ----TWQAHLARGGRwKESPRKLVVGELQDELMSVRLREAQALAEGRELRQRVVELETQDHIHRNLLNRVEAERAALQEK 621
Cdd:COG4717 316 leeeELEELLAALGL-PPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 622 LQYLAAQNKG--LQTQLSESRRKQAEAECKSKEEVMAVRLREADsmAAVAEMRQRIAELeiQREEGRIQGQLNHSDSSQY 699
Cdd:COG4717 395 EEYQELKEELeeLEEQLEELLGELEELLEALDEEELEEELEELE--EELEELEEELEEL--REELAELEAELEQLEEDGE 470
|
410
....*....|....*...
gi 229577000 700 IRELKDQIEELKAEVRLL 717
Cdd:COG4717 471 LAELLQELEELKAELREL 488
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
358-717 |
7.60e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 7.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 358 KKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYVIKRELAVVRQQC 437
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 438 SSAAEDLQKAQSTI---RQLQEQQENPRLTEDF--VSHLETeLEQSRLRETETLGALREMQDKVLDMEKRNSSLPD---- 508
Cdd:PRK02224 429 AELEATLRTARERVeeaEALLEAGKCPECGQPVegSPHVET-IEEDRERVEELEAELEDLEEEVEEVEERLERAEDlvea 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 509 ENNVAQLQEELKALKVREGQAVASTRELKLQLQELSDTWQAHLARGGRWKESPRklvvgELQDELMSVRLREA---QALA 585
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAA-----EAEEEAEEAREEVAelnSKLA 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 586 EGRELRQRVVELETQDhihrNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEE-VMAVRLREADS 664
Cdd:PRK02224 583 ELKERIESLERIRTLL----AAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEArIEEAREDKERA 658
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 229577000 665 MAAVAEMRQRIAELEIQREEgrIQGQLNHSDSS-QYIRELKDQIEELKAEVRLL 717
Cdd:PRK02224 659 EEYLEQVEEKLDELREERDD--LQAEIGAVENElEELEELRERREALENRVEAL 710
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
348-623 |
1.24e-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: 52.37 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 348 LKAYQVKYNPKK--MKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYV 425
Cdd:TIGR02168 262 LQELEEKLEELRleVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 426 IKRELAVVRQQCSSAAEDLQKAQSTIRQLQEQQENprltedfvshLETELEQSRLRETETLGALREMQDKVLDMEKRNSS 505
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEE----------LEEQLETLRSKVAQLELQIASLNNEIERLEARLER 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 506 LpdENNVAQLQEELKAL--KVREGQAVASTRELKLQLQELSDTwQAHLARGGRWKEsprklvvgELQDELMSVRLREAQA 583
Cdd:TIGR02168 412 L--EDRRERLQQEIEELlkKLEEAELKELQAELEELEEELEEL-QEELERLEEALE--------ELREELEEAEQALDAA 480
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 229577000 584 LAEGRELRQRVVELETQDhihRNLLNRVEAERAALQEKLQ 623
Cdd:TIGR02168 481 ERELAQLQARLDSLERLQ---ENLEGFSEGVKALLKNQSG 517
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
363-713 |
1.57e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 363 LEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLE-------KESAALADRLIQGQVTRAQEAEENYVIKRELAVVRQ 435
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEeraeelrEEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 436 QCSSAAEDLQKAQSTIRQLQEQQEnpRLTEDfVSHLETELE--QSRLRETETL---GALREMQDKVLDMEKRNSSLPDEN 510
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERD--ELRER-EAELEATLRtaRERVEEAEALleaGKCPECGQPVEGSPHVETIEEDRE 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 511 NVAQLQEELKALKVREgQAVASTRELKLQLQELSDTWQAHLARGGRWKE--SPRKLVVGELQDELMSVRLREAQALAEGR 588
Cdd:PRK02224 476 RVEELEAELEDLEEEV-EEVEERLERAEDLVEAEDRIERLEERREDLEEliAERRETIEEKRERAEELRERAAELEAEAE 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 589 ELRQRVVELETQDHIHRNLLNRVEAERAALQEKLQYLAAqnkgLQTQLSESRRKQAEAEcKSKEEVMAVRLREADSMAAV 668
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER----IRTLLAAIADAEDEIE-RLREKREALAELNDERRERL 629
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 229577000 669 AEMRQRIAELEIQREEGRIQG-QLNHSDSSQYIRELKDQIEELKAE 713
Cdd:PRK02224 630 AEKRERKRELEAEFDEARIEEaREDKERAEEYLEQVEEKLDELREE 675
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
361-714 |
1.94e-06 |
|
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: 51.51 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 361 KRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYVIKRELAVVRQQCSSA 440
Cdd:TIGR00618 392 TQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKER 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 441 AEDLQKAQSTIRQ-----------LQEQQENPRLTEDFVSHLETELEQSRLRETETlgalREMQDKVLDMEKRNSSLpdE 509
Cdd:TIGR00618 472 EQQLQTKEQIHLQetrkkavvlarLLELQEEPCPLCGSCIHPNPARQDIDNPGPLT----RRMQRGEQTYAQLETSE--E 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 510 NNVAQLQEELKALKvregqavastrELKLQLQELSDTWQAHLARGGRWKESPRKL--VVGELQDEL-MSVRLREAQALAE 586
Cdd:TIGR00618 546 DVYHQLTSERKQRA-----------SLKEQMQEIQQSFSILTQCDNRSKEDIPNLqnITVRLQDLTeKLSEAEDMLACEQ 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 587 GRELRQRVVELETQDhihrnllnrVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKS-KEEVMAVRLREADsm 665
Cdd:TIGR00618 615 HALLRKLQPEQDLQD---------VRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVlPKELLASRQLALQ-- 683
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 229577000 666 aavaEMRQRIAELEIQREEgriqgqLNHSDSSqyIRELKDQIEELKAEV 714
Cdd:TIGR00618 684 ----KMQSEKEQLTYWKEM------LAQCQTL--LRELETHIEEYDREF 720
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
435-684 |
1.08e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 435 QQCSSAAEDLQKAQSTIRQLQEQQENprlTEDFVSHLETELEQSRLRETETLGALREMQDKvldmekrnsslpdennVAQ 514
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA---LKKEEKALLKQLAALERRIAALARRIRALEQE----------------LAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 515 LQEELKALKVREGQAVASTRELKLQLQELSDTWQahlaRGGRwkESPRKLVVGELQDELMSVRLREAQALAEGRelRQRV 594
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALY----RLGR--QPPLALLLSPEDFLDAVRRLQYLKYLAPAR--REQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 595 VELETQdhihRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEVMAVRLREADSMAAVAEMRQR 674
Cdd:COG4942 153 EELRAD----LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
250
....*....|
gi 229577000 675 IAELEIQREE 684
Cdd:COG4942 229 IARLEAEAAA 238
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
359-623 |
1.19e-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: 49.28 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 359 KMKRLEKEyaamkSKEMEEQIEikRLRTENRLLKQRIETLEKESAALAdRLIQGQVTRAQEAEEnyvikrELAVVRQQCS 438
Cdd:TIGR02168 254 ELEELTAE-----LQELEEKLE--ELRLEVSELEEEIEELQKELYALA-NEISRLEQQKQILRE------RLANLERQLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 439 SAAEDLQKAQStirQLQEQQENPRLTEDFVSHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLpdENNVAQLQEE 518
Cdd:TIGR02168 320 ELEAQLEELES---KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL--RSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 519 LKALKVREGQAVASTRELKLQLQELSDTWQAHLARGGRWKESPRKLVVGELQDELMSVRLREAQALAEGRELRQRVVELE 598
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE 474
|
250 260
....*....|....*....|....*
gi 229577000 599 TQDHIHRNLLNRVEAERAALQEKLQ 623
Cdd:TIGR02168 475 QALDAAERELAQLQARLDSLERLQE 499
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
364-711 |
1.70e-05 |
|
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: 48.15 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 364 EKEYAAMKSKEMEEQI-----EIKRLRTENRLLKQRI---ETLEKESAALADRLIQGQVTRAQEAEENY----------- 424
Cdd:pfam05622 8 EKDELAQRCHELDQQVsllqeEKNSLQQENKKLQERLdqlESGDDSGTPGGKKYLLLQKQLEQLQEENFrletarddyri 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 425 ---VIKRELAVVRQQcssaAEDLQKAQSTIRQLQEQQENPRLTEDFVSHLETELEQSRlRETETLGALREmQDKVLdmEK 501
Cdd:pfam05622 88 kceELEKEVLELQHR----NEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYK-KKLEDLGDLRR-QVKLL--EE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 502 RNSSLPDENnvAQLQEELKalkvREGQAVASTRELKLQLQELSDTWQAHLARGGRWKESPRKL-----VVGELQDELMSV 576
Cdd:pfam05622 160 RNAEYMQRT--LQLEEELK----KANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLeekleALQKEKERLIIE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 577 R--LREAQ-----ALAEGRELRQRVVELETQDHIHRNLlnRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECK 649
Cdd:pfam05622 234 RdtLRETNeelrcAQLQQAELSQADALLSPSSDPGDNL--AAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQ 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 229577000 650 SKEEVMAVR--LREADSMAavaemRQRIAELEIQREE--GRIQGQLNHS-DSSQYIRELKDQIEELK 711
Cdd:pfam05622 312 LLEDANRRKneLETQNRLA-----NQRILELQQQVEElqKALQEQGSKAeDSSLLKQKLEEHLEKLH 373
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
452-683 |
1.77e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 452 RQLQEQQENPRLTEDFvshLETELEQSRLRetetlgaLREMQDKVLDMEKRNSSLPDENNVAQLQEELKALKVREGQAVA 531
Cdd:COG3206 164 QNLELRREEARKALEF---LEEQLPELRKE-------LEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 532 STRELKLQLQELSDTWQAHLARGGRWKESPrklVVGELQDELMSVRLREAQALAEG-------RELRQRVVELETQ-DHI 603
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQSP---VIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQlQQE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 604 HRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEaeckskeevMAVRLREADSMAAV-AEMRQRIAELEIQR 682
Cdd:COG3206 311 AQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE---------LRRLEREVEVARELyESLLQRLEEARLAE 381
|
.
gi 229577000 683 E 683
Cdd:COG3206 382 A 382
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
364-718 |
2.08e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 364 EKEYAAMK-SKEMEEQIEIKRLRTENRllKQRIETLEKESAAladrliQGQVTRAQEAEENYVIKRELAVVRQQCSSAAE 442
Cdd:PTZ00121 1078 DFDFDAKEdNRADEATEEAFGKAEEAK--KTETGKAEEARKA------EEAKKKAEDARKAEEARKAEDARKAEEARKAE 1149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 443 DlQKAQSTIRQLQEQQ--ENPRLTEDfVSHLEtelEQSRLRETETLGALREMQDKVLDMEKRNSSlpdenNVAQLQEELK 520
Cdd:PTZ00121 1150 D-AKRVEIARKAEDARkaEEARKAED-AKKAE---AARKAEEVRKAEELRKAEDARKAEAARKAE-----EERKAEEARK 1219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 521 ALKVREGQAVASTRELKLQLQELSDTWQAHLARGGRWKESPRKLVVGELQDELMSVRLREAQALAEGRELRqRVVELETQ 600
Cdd:PTZ00121 1220 AEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKK-KADEAKKA 1298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 601 DHIHRNLLNRVEAERAALQEKLQYLAAQNKglqtQLSESRRKQAEaECKSKEEVMAVRLREADSMAAVAEMRQRIAELEI 680
Cdd:PTZ00121 1299 EEKKKADEAKKKAEEAKKADEAKKKAEEAK----KKADAAKKKAE-EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK 1373
|
330 340 350
....*....|....*....|....*....|....*...
gi 229577000 681 QREEGRIQGQLNHSDSSQYIRELKDQIEELKAEVRLLK 718
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELK 1411
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
358-691 |
2.35e-05 |
|
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: 48.25 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 358 KKMKRLEKEYAAMKSKEMEEQIEIKRLRTENR---------LLKQRIETLEKESAALADRLIQGQVTRAQEAEENYVIKR 428
Cdd:pfam01576 208 KAKRKLEGESTDLQEQIAELQAQIAELRAQLAkkeeelqaaLARLEEETAQKNNALKKIRELEAQISELQEDLESERAAR 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 429 ELAvvRQQCSSAAEDLQ-------------KAQSTIRQLQEQQ--ENPRLTEDFVSHLETELEQSRLRETETLGALREMQ 493
Cdd:pfam01576 288 NKA--EKQRRDLGEELEalkteledtldttAAQQELRSKREQEvtELKKALEEETRSHEAQLQEMRQKHTQALEELTEQL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 494 DKV----LDMEKRNSSLPDENNvaQLQEELKALKVREGQAVASTRELKLQLQELsdtwQAHLARGGRWKESpRKLVVGEL 569
Cdd:pfam01576 366 EQAkrnkANLEKAKQALESENA--ELQAELRTLQQAKQDSEHKRKKLEGQLQEL----QARLSESERQRAE-LAEKLSKL 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 570 QDELMSVRLREAQALAEGRELRQRVVELETQDHIHRNLLN--------------RVEAERAALQEKL-------QYLAAQ 628
Cdd:pfam01576 439 QSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQeetrqklnlstrlrQLEDERNSLQEQLeeeeeakRNVERQ 518
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 229577000 629 NKGLQTQLSESRRKQAE--AECKSKEEVMAVRLREADsmAAVAEMRQRIAELE-IQREEGRIQGQL 691
Cdd:pfam01576 519 LSTLQAQLSDMKKKLEEdaGTLEALEEGKKRLQRELE--ALTQQLEEKAAAYDkLEKTKNRLQQEL 582
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
373-715 |
4.14e-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: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 373 KEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRL--IQGQVTRAQEAEENY-------------VIKRELAVVRQQC 437
Cdd:COG4913 275 EYLRAALRLWFAQRRLELLEAELEELRAELARLEAELerLEARLDALREELDELeaqirgnggdrleQLEREIERLEREL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 438 SSAAEDLQKAQSTIRQLQEQ--------QENPRLTEDFVSHLETELEQSRLRETETLGALREMQDK-------VLDMEKR 502
Cdd:COG4913 355 EERERRRARLEALLAALGLPlpasaeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRElreleaeIASLERR 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 503 NSSLPDEnnVAQLQEEL-KALKVREGQA--VAstrELkLQLQELSDTWQ------------------AHLARGGRWKES- 560
Cdd:COG4913 435 KSNIPAR--LLALRDALaEALGLDEAELpfVG---EL-IEVRPEEERWRgaiervlggfaltllvppEHYAAALRWVNRl 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 561 -PRKLVVGElqdelmsvRLREAQALAEGRELRQR--VVELETQDHIHRNLLNRVEAERAAL------------------- 618
Cdd:COG4913 509 hLRGRLVYE--------RVRTGLPDPERPRLDPDslAGKLDFKPHPFRAWLEAELGRRFDYvcvdspeelrrhpraitra 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 619 ----------------------------QEKLQYLAAQNKGLQTQLSESRRKQAEAEckSKEEVMAVRLREADSMAAVAE 670
Cdd:COG4913 581 gqvkgngtrhekddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALE--AELDALQERREALQRLAEYSW 658
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 229577000 671 MRQRIAELeiQREEGRIQGQLNH-SDSSQYIRELKDQIEELKAEVR 715
Cdd:COG4913 659 DEIDVASA--EREIAELEAELERlDASSDDLAALEEQLEELEAELE 702
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
381-718 |
6.24e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 381 IKRLR--TENRLLKQRIETLEKESAALADRL--IQGQVTRAQEAEENYVIKRElavvrqqcsSAAEDLQKAQSTIRQLQE 456
Cdd:PRK02224 178 VERVLsdQRGSLDQLKAQIEEKEEKDLHERLngLESELAELDEEIERYEEQRE---------QARETRDEADEVLEEHEE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 457 QQENprltedfVSHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDENNVAQLQEELKAlkvregqavASTREL 536
Cdd:PRK02224 249 RREE-------LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDD---------ADAEAV 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 537 KLQLQELSDtwqahlarggrwKESprklvvgELQDELMSVR------------LREAQALAEGR--ELRQRVVELETQDH 602
Cdd:PRK02224 313 EARREELED------------RDE-------ELRDRLEECRvaaqahneeaesLREDADDLEERaeELREEAAELESELE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 603 IHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAEckskEEVMAVRLREADSMAAVAEMRQRIAELEIQR 682
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR----EERDELREREAELEATLRTARERVEEAEALL 449
|
330 340 350
....*....|....*....|....*....|....*....
gi 229577000 683 EEGRIQ--GQ-LNHSDSSQYIRELKDQIEELKAEVRLLK 718
Cdd:PRK02224 450 EAGKCPecGQpVEGSPHVETIEEDRERVEELEAELEDLE 488
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
353-718 |
8.55e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 8.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 353 VKYNPKKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLiqGQVTRAQEAEENYV------- 425
Cdd:PRK03918 226 LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV--KELKELKEKAEEYIklsefye 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 426 --------IKRELAVVRQQCSSAAEDLQKAQSTIRQLQEQQENPRLTEDFVSHLETELEQ-----------SRLRETETL 486
Cdd:PRK03918 304 eyldelreIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyeeakakkeelERLKKRLTG 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 487 GALREMQDKVLDMEKRNSslpdennvaQLQEELKALKVREGQAVASTRELKLQLQELSDTWQAHLARGGRWKESPRKLVV 566
Cdd:PRK03918 384 LTPEKLEKELEELEKAKE---------EIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 567 GELQDELMSVRLREAQALAEGRELRQRVVELETQDHIHRNLL-------------------NRVEAERAA-----LQEKL 622
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIklkelaeqlkeleeklkkyNLEELEKKAeeyekLKEKL 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 623 QYLAAQNKGLQTQLS-----ESRRKQAEAECKSKEEVMAVRLREADSMA--AVAEMRQRIAELE---------------I 680
Cdd:PRK03918 535 IKLKGEIKSLKKELEkleelKKKLAELEKKLDELEEELAELLKELEELGfeSVEELEERLKELEpfyneylelkdaekeL 614
|
410 420 430
....*....|....*....|....*....|....*....
gi 229577000 681 QREEGRIQG-QLNHSDSSQYIRELKDQIEELKAEVRLLK 718
Cdd:PRK03918 615 EREEKELKKlEEELDKAFEELAETEKRLEELRKELEELE 653
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
480-719 |
1.20e-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: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 480 LRETETLGALREMQDKVLDMEKRNSSLPDEnnVAQLQEELKALKVREGQAVASTRELKLQLQELSdtwQAHLARGGRWKE 559
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSSLQSE--LRRIENRLDELSQELSDASRKIGEIEKEIEQLE---QEEEKLKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 560 SPRKLvvGELQDELMSVRlreaqalAEGRELRQRVVELETQDHIHRNLLNRVEAERAalQEKLQYLAAQNKGLQTQLSES 639
Cdd:TIGR02169 742 LEEDL--SSLEQEIENVK-------SELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 640 RRKQAEAECKSKEEvmavRLREADSMAAVAEMRQRIAELEIQREEGRIQGQLNHSDssqyIRELKDQIEELKAEVRLLKG 719
Cdd:TIGR02169 811 EARLREIEQKLNRL----TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK----KEELEEELEELEAALRDLES 882
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
363-718 |
1.23e-04 |
|
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: 45.50 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 363 LEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYVIKrELAVVRQQCSSAAE 442
Cdd:pfam05557 109 LKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIK-ELEFEIQSQEQDSE 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 443 DLQKAQSTIRQLQEQQENPRLTEDFVSHLETELEQSRLRETET------LGALREMQDKVLDMEKRNSSLPDE------- 509
Cdd:pfam05557 188 IVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVedlkrkLEREEKYREEAATLELEKEKLEQElqswvkl 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 510 ---------------NNVAQLQEELKALKVREGQAVASTRELKLQLQELSDTWQAHLA-----RGGRWKESP------RK 563
Cdd:pfam05557 268 aqdtglnlrspedlsRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKkiedlNKKLKRHKAlvrrlqRR 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 564 LVVGELQDELMSVRLR----EAQALAEGRELRQRVVELETQDHIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSES 639
Cdd:pfam05557 348 VLLLTKERDGYRAILEsydkELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQAL 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 640 RRKQAEAE-CKSKEEVMAVRLREADSMAAVAEMRQRIAELEIQREEGRIQGQLNHSDS----------SQYIRELKDQIE 708
Cdd:pfam05557 428 RQQESLADpSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTkvlhlsmnpaAEAYQQRKNQLE 507
|
410
....*....|
gi 229577000 709 ELKAEVRLLK 718
Cdd:pfam05557 508 KLQAEIERLK 517
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
358-718 |
1.28e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 358 KKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLK--------QRIETLEKESAALADRLiqgqvTRAQEAEENYviKRE 429
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEaqirgnggDRLEQLEREIERLEREL-----EERERRRARL--EAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 430 LAVVRQQCSSAAEDLQKAQSTIRQLQEQqenprlTEDFVSHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDE 509
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAALLEA------LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 510 nnVAQLQEEL-KALKVREGQA--VAstrELkLQLQELSDTWQ------------------AHLARGGRWKES---PRKLV 565
Cdd:COG4913 442 --LLALRDALaEALGLDEAELpfVG---EL-IEVRPEEERWRgaiervlggfaltllvppEHYAAALRWVNRlhlRGRLV 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 566 ---VGELQDELMSVRLrEAQALAE-----------------GR-----------ELRQ---------------RVVELET 599
Cdd:COG4913 516 yerVRTGLPDPERPRL-DPDSLAGkldfkphpfrawleaelGRrfdyvcvdspeELRRhpraitragqvkgngTRHEKDD 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 600 QDHIHRNL---------LNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRK------------------QAEAECKSKE 652
Cdd:COG4913 595 RRRIRSRYvlgfdnrakLAALEAELAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdeidvaSAEREIAELE 674
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 229577000 653 EVMAvRLREADSmaAVAEMRQRIAELEIQREEGRIQ-GQLNHSdssqyIRELKDQIEELKAEVRLLK 718
Cdd:COG4913 675 AELE-RLDASSD--DLAALEEQLEELEAELEELEEElDELKGE-----IGRLEKELEQAEEELDELQ 733
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
457-679 |
1.34e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 45.70 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 457 QQENPRLTE------DFVSHLETELEQSRlretetlgALREMQDKVLDMEKRNSslpdennvaqlqEELK-ALKV-REGQ 528
Cdd:PLN03188 1050 EQERLRWTEaeskwiSLAEELRTELDASR--------ALAEKQKHELDTEKRCA------------EELKeAMQMaMEGH 1109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 529 AvastRELKlQLQELSDTWQAHLARGGRwkesprklvvgeLQDELMSVRLREAQALAEGRELRqrvveletqdhihrnLL 608
Cdd:PLN03188 1110 A----RMLE-QYADLEEKHIQLLARHRR------------IQEGIDDVKKAAARAGVRGAESK---------------FI 1157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 229577000 609 NRVEAERAAL----QEKLQYLAAQNKGLQTQLsesrRKQAEAECKSKEevMAVRLREADSMAAVAEMRQRIAELE 679
Cdd:PLN03188 1158 NALAAEISALkverEKERRYLRDENKSLQAQL----RDTAEAVQAAGE--LLVRLKEAEEALTVAQKRAMDAEQE 1226
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
380-542 |
1.58e-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: 44.15 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 380 EIKRLRTENRLLKQRIETLEKESAALADRLIQgqvtraqeaeenyvIKRELAVVRQQCSSAAEDLQKAQSTIRQLQEQQE 459
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEA--------------AKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 460 NPRLTEDFvSHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLpdENNVAQLQEELKALKVREGQAVASTRELKLQ 539
Cdd:COG1579 84 NVRNNKEY-EALQKEIESLKRRISDLEDEILELMERIEELEEELAEL--EAELAELEAELEEKKAELDEELAELEAELEE 160
|
...
gi 229577000 540 LQE 542
Cdd:COG1579 161 LEA 163
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
376-711 |
1.62e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 376 EEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYVIKRELAVVRQQCSSAA---EDLQKAQSTIR 452
Cdd:PRK02224 248 ERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEarrEELEDRDEELR 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 453 QLQEQQ---------ENPRLTEDFVSH-------------LETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPD-- 508
Cdd:PRK02224 328 DRLEECrvaaqahneEAESLREDADDLeeraeelreeaaeLESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVdl 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 509 ---ENNVAQLQEELKALKVREGQAVASTRELKLQLQELsdtwQAHLARGG------RWKESPRKLVVGELQDELMSVRLR 579
Cdd:PRK02224 408 gnaEDFLEELREERDELREREAELEATLRTARERVEEA----EALLEAGKcpecgqPVEGSPHVETIEEDRERVEELEAE 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 580 EAQALAEGRELRQRVVELETQDHIHRNlLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKEEvmavRL 659
Cdd:PRK02224 484 LEDLEEEVEEVEERLERAEDLVEAEDR-IERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEK----RE 558
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 229577000 660 READSMAAVAEMRQRIAELEIQREE--GRIQGQLNHSDSSQYIRELKDQIEELK 711
Cdd:PRK02224 559 AAAEAEEEAEEAREEVAELNSKLAElkERIESLERIRTLLAAIADAEDEIERLR 612
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
358-602 |
1.82e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 358 KKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALadrliqgqvtraqeaeenyviKRELAVVRQQC 437
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT---------------------ERRLEDLEEQI 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 438 SSAAEDLQKAQSTIRQLQEQQEnpRLTEDFVSHLEtELEQSRLRETETLGALREMQDKVLDMEKRNSSLpdENNVAQLQE 517
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIE--ELESELEALLN-ERASLEEALALLRSELEELSEELRELESKRSEL--RRELEELRE 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 518 ELKALKVREGQAVASTRELKLQLQEL-SDTWQAHLArggrwKESPRKLVVGELQDELMSVRLREAQ-------ALAEGRE 589
Cdd:TIGR02168 923 KLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEA-----LENKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEE 997
|
250
....*....|...
gi 229577000 590 LRQRVVELETQDH 602
Cdd:TIGR02168 998 LKERYDFLTAQKE 1010
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
389-714 |
1.86e-04 |
|
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: 45.11 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 389 RLLKQRIETLEKESAALADRLIQGQvTRAQEAEENyviKRELAVVRQQCSSAAEDLQ-KAQSTIRQLQEQQEnprLTEDF 467
Cdd:pfam15921 92 RRLNESNELHEKQKFYLRQSVIDLQ-TKLQEMQME---RDAMADIRRRESQSQEDLRnQLQNTVHELEAAKC---LKEDM 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 468 VSHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDEnnvaqlQEELKALKVRE-GQAVAST-RELKLQLQELSd 545
Cdd:pfam15921 165 LEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYE------HDSMSTMHFRSlGSAISKIlRELDTEISYLK- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 546 twqahlargGRwkesprklvVGELQDELMSVRLREaqalaegrelrQRVVELETQDHIHR--NLLNRVEAERAALQEKLQ 623
Cdd:pfam15921 238 ---------GR---------IFPVEDQLEALKSES-----------QNKIELLLQQHQDRieQLISEHEVEITGLTEKAS 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 624 YLAAQNKGLQTQL---SESRRKQAE------AECKSKEEVMAVRLREADSMaavaeMRQRIAELEIQREEGRIQGQLNHS 694
Cdd:pfam15921 289 SARSQANSIQSQLeiiQEQARNQNSmymrqlSDLESTVSQLRSELREAKRM-----YEDKIEELEKQLVLANSELTEART 363
|
330 340
....*....|....*....|...
gi 229577000 695 DSSQYIRE---LKDQIEELKAEV 714
Cdd:pfam15921 364 ERDQFSQEsgnLDDQLQKLLADL 386
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
363-684 |
1.90e-04 |
|
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: 45.33 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 363 LEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQ-VTRAQEAEENYvikrelavvRQQCSSAA 441
Cdd:COG3096 290 LRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQtALRQQEKIERY---------QEDLEELT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 442 EDLQKAQSTIRQLQEQ----QENPRLTEDFVSHLETELE--QSRLRETETLgALREMQD-KVLDMEKRNSSLPDEnNVAQ 514
Cdd:COG3096 361 ERLEEQEEVVEEAAEQlaeaEARLEAAEEEVDSLKSQLAdyQQALDVQQTR-AIQYQQAvQALEKARALCGLPDL-TPEN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 515 LQEELKALKVREGQAVASTRELKlqlQELSDTwQAHLARGGRWKESPRKlVVGELQDELMSVRLREaqALAEGRElrqrv 594
Cdd:COG3096 439 AEDYLAAFRAKEQQATEEVLELE---QKLSVA-DAARRQFEKAYELVCK-IAGEVERSQAWQTARE--LLRRYRS----- 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 595 veletqdhiHRNLLNRVEAERAALQEKLQYLAAQNKG--LQTQLSESRRKQAEAECKSKEEVMAVRLREADSMAAVAEMR 672
Cdd:COG3096 507 ---------QQALAQRLQQLRAQLAELEQRLRQQQNAerLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAV 577
|
330
....*....|..
gi 229577000 673 QRIAELEIQREE 684
Cdd:COG3096 578 EQRSELRQQLEQ 589
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
569-717 |
2.21e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 569 LQDELMSVRLREAQALAEGRELRQR--VVELETQDHIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRR----- 641
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDalpel 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 642 ---------KQAEAECKSKEEVMAVRLREADSmaAVAEMRQRIAELE--IQREEGRIQGQLNHSDSSQYIRE--LKDQIE 708
Cdd:COG3206 260 lqspviqqlRAQLAELEAELAELSARYTPNHP--DVIALRAQIAALRaqLQQEAQRILASLEAELEALQAREasLQAQLA 337
|
....*....
gi 229577000 709 ELKAEVRLL 717
Cdd:COG3206 338 QLEARLAEL 346
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
364-711 |
4.19e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.19 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 364 EKEYAAMKsKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQE------------AEENYVIKRELA 431
Cdd:pfam02463 169 RKKKEALK-KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEeyllyldylklnEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 432 VVRQQCSSAAEDLQKAQSTIRQLQEQQENP----RLTEDFVSHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLP 507
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEekekKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 508 DENN-----VAQLQEELKALKVREGQAVASTRELKLQLQELSDTWQAHLA-RGGRWKESPRKLVVGELQDELMSVRLREA 581
Cdd:pfam02463 328 KELKkekeeIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAkKKLESERLSSAAKLKEEELELKSEEEKEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 582 QALAEgrelrqrvvELETQDHIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEaecKSKEEVMAVRLRE 661
Cdd:pfam02463 408 QLLLE---------LARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK---DELELKKSEDLLK 475
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 229577000 662 ADSMaaVAEMRQRIAELEIQREEGRIQGQLNHSDSSQYIRELKDQIEELK 711
Cdd:pfam02463 476 ETQL--VKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGR 523
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
429-687 |
8.46e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 429 ELAVVRQQCSSAAEDLQKAQSTIRQLQEQQENPRLTedfVSHLETELEQSRLRETETLGA-LREMQDKVLDMEKRNSSLP 507
Cdd:PRK04863 838 ELRQLNRRRVELERALADHESQEQQQRSQLEQAKEG---LSALNRLLPRLNLLADETLADrVEEIREQLDEAEEAKRFVQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 508 D--------ENNVAQLQ---EELKALKVREGQAVASTRELKLQLQELSDTWQ--AHLArggrWKESPRKLVVGELQDELM 574
Cdd:PRK04863 915 QhgnalaqlEPIVSVLQsdpEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrrAHFS----YEDAAEMLAKNSDLNEKL 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 575 SVRLREA-QALAEGRE-LRQRVVELETQDHIHRNLLNRVEAERAALQEKLQYLAAqnkgLQTQLSESrrkqAEAECKSKE 652
Cdd:PRK04863 991 RQRLEQAeQERTRAREqLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQD----LGVPADSG----AEERARARR 1062
|
250 260 270
....*....|....*....|....*....|....*
gi 229577000 653 EVMAVRLREADSMAAVAEMRQRIAELEIQREEGRI 687
Cdd:PRK04863 1063 DELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKL 1097
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
442-630 |
9.26e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 9.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 442 EDLQKAQSTIRQLQEQQENPRLTEDFVSHLETELEQSRLRetetlgaLREMQDKVLDMEKRNSSLPDENNVAQLQEELKA 521
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE-------LEELREELEKLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 522 LKVRegqavasTRELKLQLQELSDtWQAHLARGGRWKESPRKLVVGELQDELMSVRLREAQALAEGRELRQRVVELETQD 601
Cdd:COG4717 144 LPER-------LEELEERLEELRE-LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
170 180
....*....|....*....|....*....
gi 229577000 602 HIHRNLLNRVEAERAALQEKLQYLAAQNK 630
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEER 244
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
404-628 |
1.13e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 404 ALADRLIQGQVTRAQEAEENYV--IKRELAVVRQQCSSAAEDLQ--KAQSTIRQLQEQQEnprLTEDFVSHLETELEQSR 479
Cdd:COG3206 156 ALAEAYLEQNLELRREEARKALefLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAK---LLLQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 480 LRETETLGALREMQDKVLDMEKRNSSLPDENNVAQLQEELKALKVREGQAVA-------STRELKLQLQELSDTWQAHLA 552
Cdd:COG3206 233 AELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQ 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 229577000 553 RGGRWKESPRKLV---VGELQDELMSVRLREAQALAEGRELRQRVVELETQDHIHRNLLNRVEAerAALQEKLQYLAAQ 628
Cdd:COG3206 313 RILASLEAELEALqarEASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE--ARLAEALTVGNVR 389
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
358-543 |
1.18e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 358 KKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQ-----GQVTRAQEAEENYVIKR---- 428
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekeiAELRAELEAQKEELAELlral 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 429 ---------ELAVVRQQCSSAAEDLQKAQSTIRQLQEQQENPRLTEDFVSHLETELEQSRLRETETLGALREMQDKVLDM 499
Cdd:COG4942 114 yrlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 229577000 500 EKRNSSLpdennVAQLQEELKALKVREGQAVASTRELKLQLQEL 543
Cdd:COG4942 194 KAERQKL-----LARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
580-684 |
1.21e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.31 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 580 EAQALAEGRELRQRVvELETQdhihrNLLNRVEAEraalQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSkeevmavRL 659
Cdd:PTZ00491 667 AARHQAELLEQEARG-RLERQ-----KMHDKAKAE----EQRTKLLELQAESAAVESSGQSRAEALAEAEA-------RL 729
|
90 100 110
....*....|....*....|....*....|.
gi 229577000 660 READSMAAVAEMR---QRI---AELEIQREE 684
Cdd:PTZ00491 730 IEAEAEVEQAELRakaLRIeaeAELEKLRKR 760
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
441-685 |
1.25e-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: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 441 AEDLQKAQSTIRQLQEQQENPRLTEDFVSHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDEnnvaqLQEELK 520
Cdd:pfam07888 44 AELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE-----LSEEKD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 521 ALKVREGQAVASTRELKLQLQELSDTWQAHLARGGRWKESPRKLVV--GELQDELMSVRLREAQALAEGRELRQRVVELe 598
Cdd:pfam07888 119 ALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAqrKEEEAERKQLQAKLQQTEEELRSLSKEFQEL- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 599 tqdhihRNLLNRVEAERAALQEKLQylaaqnkGLQTQLSESRRKQAEAEcKSKEEVMAVRLREADSMAAVAEMRQRIAEL 678
Cdd:pfam07888 198 ------RNSLAQRDTQVLQLQDTIT-------TLTQKLTTAHRKEAENE-ALLEELRSLQERLNASERKVEGLGEELSSM 263
|
....*..
gi 229577000 679 EIQREEG 685
Cdd:pfam07888 264 AAQRDRT 270
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
357-681 |
1.26e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 357 PKKMKRLEKEYAAMKSKEMEeqieIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYV-IKRELAVVRQ 435
Cdd:COG4717 145 PERLEELEERLEELRELEEE----LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAeLEEELEEAQE 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 436 QCSSAAEDLQKAQSTIRQLQEQQENPRLTEDFVSH---------------------------------------LETELE 476
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLLIAaallallglggsllsliltiagvlflvlgllallflllaREKASL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 477 QSRLRETETLGALREMQDKVLDMEKRNSSLPDENNVAQLQEELKAL-KVREGQAVASTRELKLQLQELSDTWQAHLARGG 555
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIeELQELLREAEELEEELQLEELEQEIAALLAEAG 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 556 ---------RWKESPRKLvvgELQDELMSVRLREAQALAEGRELRQRVVELETQDHIH--RNLLNRVEAERAALQEKLQY 624
Cdd:COG4717 381 vedeeelraALEQAEEYQ---ELKEELEELEEQLEELLGELEELLEALDEEELEEELEelEEELEELEEELEELREELAE 457
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 229577000 625 LAAQNKGLQTQLSESRRKQAEAECKSKEEVMAVRLREADSMAAVAEMRQRIAELEIQ 681
Cdd:COG4717 458 LEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
359-545 |
1.68e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 359 KMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYVIKRELavvrqqcS 438
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL-------D 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 439 SAAEDLQKAQSTIRQLQEQQENprlTEDFVSHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPD-----ENNVA 513
Cdd:TIGR02169 410 RLQEELQRLSEELADLNAAIAG---IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEeydrvEKELS 486
|
170 180 190
....*....|....*....|....*....|..
gi 229577000 514 QLQEELKALKVREGQAVASTRELKLQLQELSD 545
Cdd:TIGR02169 487 KLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
396-719 |
1.69e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 396 ETLEKESAALadrliqgqvTRAQEAEENYVIKRELAVVRQQCSSAAEDLQKAQSTI-RQLQEQQENPRLTEDFVSHLETE 474
Cdd:pfam01576 630 EAREKETRAL---------SLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVgKNVHELERSKRALEQQVEEMKTQ 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 475 LEQ----------SRLRETETLGAL-----REMQDKVLDMEKRNSSLPDEnnVAQLQEELKALKVREGQAVASTRELKLQ 539
Cdd:pfam01576 701 LEEledelqatedAKLRLEVNMQALkaqfeRDLQARDEQGEEKRRQLVKQ--VRELEAELEDERKQRAQAVAAKKKLELD 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 540 LQELsdtwQAHLARGGRWKESP----RKL--VVGELQDELMSVRLREAQALAEGRELRQRVVELE------TQDHIHRNL 607
Cdd:pfam01576 779 LKEL----EAQIDAANKGREEAvkqlKKLqaQMKDLQRELEEARASRDEILAQSKESEKKLKNLEaellqlQEDLAASER 854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 608 LNR-VEAERAALQEKlqyLAAQNKGLQTQLSESRRkqAEAECKSKEEvmavRLREADSMAAVAEMRQRIAELEIQREEGR 686
Cdd:pfam01576 855 ARRqAQQERDELADE---IASGASGKSALQDEKRR--LEARIAQLEE----ELEEEQSNTELLNDRLRKSTLQVEQLTTE 925
|
330 340 350
....*....|....*....|....*....|....
gi 229577000 687 IQGQLNHSDSSQYIRE-LKDQIEELKAEVRLLKG 719
Cdd:pfam01576 926 LAAERSTSQKSESARQqLERQNKELKAKLQEMEG 959
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
348-718 |
1.98e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 348 LKAYQVKYNPKKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYviK 427
Cdd:PRK03918 374 LERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHR--K 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 428 RELAVVRQQCSSAAEDLQKAQSTIRQLQEQqenprltedfvshlETELEQSRLRETEtLGALREMQDKVLDMEKRNSSLP 507
Cdd:PRK03918 452 ELLEEYTAELKRIEKELKEIEEKERKLRKE--------------LRELEKVLKKESE-LIKLKELAEQLKELEEKLKKYN 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 508 DEnNVAQLQEELKALKVREGQAVASTRELKLQLQELSD--TWQAHLARGGRWKESPRKLVVGELQDELMSVRLREAQALA 585
Cdd:PRK03918 517 LE-ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLK 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 586 EGRELRQRVVELETQDHIHRNLLNRVEAERAALQEKLQYLAAQNKGLQ---TQLSESRRKQAEAECKSKEEVMaVRLREa 662
Cdd:PRK03918 596 ELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEelrKELEELEKKYSEEEYEELREEY-LELSR- 673
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 229577000 663 dsmaAVAEMRQRIAELEIQREEGRiqgqlnhsDSSQYIRELKDQIEELKAEVRLLK 718
Cdd:PRK03918 674 ----ELAGLRAELEELEKRREEIK--------KTLEKLKEELEEREKAKKELEKLE 717
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
489-723 |
2.00e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 489 LREMQDKVLDMEKRNSSLPDennVAQLQEELKALKVREGQAVASTRELKL-QLQELSDTWQAHLARGGRWKEsprklvvg 567
Cdd:COG4913 237 LERAHEALEDAREQIELLEP---IRELAERYAAARERLAELEYLRAALRLwFAQRRLELLEAELEELRAELA-------- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 568 ELQDELMSVRLREAQALAEGRELR--------QRVVELETQDHIHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSES 639
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 640 RRKQAEAECKSKEEVMAVRLREADSMAAVAEMRQRIAEL--EIQREEGRiqgqlnHSDSSQYIRELKDQIEElkaEVRLL 717
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELeaEIASLERR------KSNIPARLLALRDALAE---ALGLD 456
|
....*.
gi 229577000 718 KGPPPF 723
Cdd:COG4913 457 EAELPF 462
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
380-506 |
2.07e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 39.16 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 380 EIKRLRTENRLLKQRIETLEKESAALADRLiQGQVTRAQEAEENYviKREL---AVVRQQCSSAAEDLQKAQSTIRQLQE 456
Cdd:pfam07926 2 ELSSLQSEIKRLKEEAADAEAQLQKLQEDL-EKQAEIAREAQQNY--ERELvlhAEDIKALQALREELNELKAEIAELKA 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 229577000 457 QqenprlTEDFVSHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSL 506
Cdd:pfam07926 79 E------AESAKAELEESEESWEEQKKELEKELSELEKRIEDLNEQNKLL 122
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
429-719 |
2.40e-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: 41.48 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 429 ELAVVRQQCSSAAEDLQKAQSTIRQLQEQQEN--PRLTE-----DFVSHLETELEQSRLRE-TETLGALREMQDKVLDME 500
Cdd:COG3096 837 ELAALRQRRSELERELAQHRAQEQQLRQQLDQlkEQLQLlnkllPQANLLADETLADRLEElREELDAAQEAQAFIQQHG 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 501 KRNSSLpdENNVAQLQ---EELKALKVREGQAVASTRELKLQLQELSDTWQ--AHLArggrWKESPRklvvgelqdelms 575
Cdd:COG3096 917 KALAQL--EPLVAVLQsdpEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQrrPHFS----YEDAVG------------- 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 576 vRLREAQALAEgrELRQRVVELETQdhihrnllnRVEAERAALQEKLQYlaAQNKGLQTQLSESRRKQAEAECKSKEEVM 655
Cdd:COG3096 978 -LLGENSDLNE--KLRARLEQAEEA---------RREAREQLRQAQAQY--SQYNQVLASLKSSRDAKQQTLQELEQELE 1043
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 229577000 656 AVRLREADSMAAVAEMRQRiaeleiqreegRIQGQLNHSDSSqyIRELKDQIEELKAEVRLLKG 719
Cdd:COG3096 1044 ELGVQADAEAEERARIRRD-----------ELHEELSQNRSR--RSQLEKQLTRCEAEMDSLQK 1094
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
579-719 |
2.42e-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: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 579 REAQALAEGRELRQRVVELETQDHIHRNLLNRVEAERA------ALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKE 652
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREkaeryqALLKEKREYEGYELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 229577000 653 EVMAVRLREADsmaavaEMRQRIAELEIQREEgrIQGQLNHSDSSQYIReLKDQIEELKAEVRLLKG 719
Cdd:TIGR02169 251 EELEKLTEEIS------ELEKRLEEIEQLLEE--LNKKIKDLGEEEQLR-VKEKIGELEAEIASLER 308
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
363-726 |
2.52e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 363 LEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQ-VTRAQEAEENYVIkrELAVVRQQCSSAA 441
Cdd:PRK04863 291 LRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQtALRQQEKIERYQA--DLEELEERLEEQN 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 442 EDLQKAQStirQLQEQQENPRLTEDFVSHLETELE--QSRLRETETLgALREMQDK-VLDMEKRNSSLPD--ENNVAQLQ 516
Cdd:PRK04863 369 EVVEEADE---QQEENEARAEAAEEEVDELKSQLAdyQQALDVQQTR-AIQYQQAVqALERAKQLCGLPDltADNAEDWL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 517 EELKAlkvregQAVASTRELkLQL-QELSDTwQAHLARGGRWKESPRKLVVG----ELQDELMSV--RLREAQALAEGRE 589
Cdd:PRK04863 445 EEFQA------KEQEATEEL-LSLeQKLSVA-QAAHSQFEQAYQLVRKIAGEvsrsEAWDVARELlrRLREQRHLAEQLQ 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 590 -LRQRVVELETQDHIHRNL----------LNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAECKSKE------ 652
Cdd:PRK04863 517 qLRMRLSELEQRLRQQQRAerllaefckrLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQlqariq 596
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 229577000 653 --EVMAVRLREADsmAAVAEMRQRIAE--LEIQREEGRIQGQLNHSDSSQYIR-ELKDQIEELKAEVRLLKGPPPFEDP 726
Cdd:PRK04863 597 rlAARAPAWLAAQ--DALARLREQSGEefEDSQDVTEYMQQLLERERELTVERdELAARKQALDEEIERLSQPGGSEDP 673
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
358-545 |
2.65e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 358 KKMKRLEKEyaamksKEMEEQiEIKRLRTENRLLKQRIETLEKESAALA------DRLIQGQVTRAQEAEENY-VIKREL 430
Cdd:TIGR04523 412 EQIKKLQQE------KELLEK-EIERLKETIIKNNSEIKDLTNQDSVKEliiknlDNTRESLETQLKVLSRSInKIKQNL 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 431 AVVRQQCSSAAEDLQKAQSTIRQLQEQQENprLTEDfVSHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSLPDEN 510
Cdd:TIGR04523 485 EQKQKELKSKEKELKKLNEEKKELEEKVKD--LTKK-ISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEK 561
|
170 180 190
....*....|....*....|....*....|....*
gi 229577000 511 NVAQLQEELKALKVREGQAVASTRELKLQLQELSD 545
Cdd:TIGR04523 562 EIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK 596
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
513-718 |
3.32e-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: 40.52 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 513 AQLQEELKALKVREGQAVASTRELKLQLQELSDTWQAHLARggrwkesprklvVGELQDELMSVRLREAQALAEGRELRQ 592
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR------------IAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 593 RVVELETQDHIHRNLLNRV--EAERAALQEKLQYLAAQNKGLQT--------QLSESRRKQAEAECKSKEEVMAVRlrea 662
Cdd:COG4942 91 EIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEDFLDAvrrlqylkYLAPARREQAEELRADLAELAALR---- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 229577000 663 dsmAAVAEMRQRIAELEIQREEGRIQGQLNHSDSSQYIRELKDQIEELKAEVRLLK 718
Cdd:COG4942 167 ---AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
384-718 |
3.33e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.26 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 384 LRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEENYVIKRELAVVRQQCSSAAEDLQKAQSTIRQLQEQQENPRL 463
Cdd:pfam15921 333 LREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 464 TEDfvsHLETELEqSRLRETETLGALRemqdKVLDMEKRnsslpdennvAQLQEELKALKVREgQAVASTRELKLQLQEL 543
Cdd:pfam15921 413 TID---HLRRELD-DRNMEVQRLEALL----KAMKSECQ----------GQMERQMAAIQGKN-ESLEKVSSLTAQLEST 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 544 sdtwqahlarggrwKESPRKlVVGELQDELMSVRLREAQALAEGRELRQRVVELETQDHIHRNLLNRVEAEraaLQEkLQ 623
Cdd:pfam15921 474 --------------KEMLRK-VVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLK---LQE-LQ 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 624 YLAAQNKGLQtqlsesrrkQAEAECKskeevmAVRLREADSMAAVAEMRQRIAEL-EIQREEGRIQGQLnHSDSSQYIRE 702
Cdd:pfam15921 535 HLKNEGDHLR---------NVQTECE------ALKLQMAEKDKVIEILRQQIENMtQLVGQHGRTAGAM-QVEKAQLEKE 598
|
330
....*....|....*.
gi 229577000 703 LKDQIEELKaEVRLLK 718
Cdd:pfam15921 599 INDRRLELQ-EFKILK 613
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
357-647 |
3.69e-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: 40.52 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 357 PKKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLiqgqvtRAQEAEenyvikrelavvrqq 436
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI------RALEQE--------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 437 cssaaedLQKAQSTIRQLQEQQEnprltedfvsHLETELEQSRLRETETLGALREMQDKVLDMEKRNSSlpdenNVAQLQ 516
Cdd:COG4942 78 -------LAALEAELAELEKEIA----------ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPE-----DFLDAV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 517 EELKALKVREGQAVASTRELKLQLQELSdtwqahlarggrwkesprklvvgELQDELMSVRLREAQALAEGRELRQRVVE 596
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELA-----------------------ALRAELEAERAELEALLAELEEERAALEA 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 229577000 597 LETQdhiHRNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAE 647
Cdd:COG4942 193 LKAE---RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
519-680 |
4.43e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 40.03 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 519 LKALKVREGQAVA--------STRELKLQLQELS---DTWQAHLARGGRWKESPRKLVVGELQDELMSVRLREAQalaeg 587
Cdd:COG1566 56 VTEVLVKEGDRVKkgqvlarlDPTDLQAALAQAEaqlAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQ----- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 588 RELrQRVVELETQDHIHRNLLNRVEAERAALQEKLQylAAQnkglqtqlseSRRKQAEAECKSKEEVMAVRLREADSMAA 667
Cdd:COG1566 131 REL-ERYQALYKKGAVSQQELDEARAALDAAQAQLE--AAQ----------AQLAQAQAGLREEEELAAAQAQVAQAEAA 197
|
170
....*....|...
gi 229577000 668 VAEMRQRIAELEI 680
Cdd:COG1566 198 LAQAELNLARTTI 210
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
348-507 |
4.86e-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: 40.49 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 348 LKAYQVKYNPKKMKRLEKEYAA----MKSKEMEEQIEIKRLRTENRLLKQRIETLEKESAALADRLIQGQVTRAQEAEEN 423
Cdd:pfam17380 425 IRAEQEEARQREVRRLEEERARemerVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEER 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 424 Y-----------VIKRELAvVRQQCSSAAEDLQKAQSTIRQLQEQQENPRLTEDFVSHLEtelEQSRLretETLGALREM 492
Cdd:pfam17380 505 KqamieeerkrkLLEKEME-ERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE---ERSRL---EAMEREREM 577
|
170
....*....|....*
gi 229577000 493 QDKVLDMEKRNSSLP 507
Cdd:pfam17380 578 MRQIVESEKARAEYE 592
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
562-717 |
5.30e-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: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 562 RKLVVGELQDELMSVRLREAQALAEGRELRQRVVELETQdhihrnlLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRR 641
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQ-------VERLEAEVEELEAELEEKDERIERLERELSEARS 455
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 229577000 642 KQAEAECKSKEevmavrlreadsmaaVAEMRQRIAELEIQREEGRiqgqlnhsdssQYIRELKDQIEELKAEVRLL 717
Cdd:COG2433 456 EERREIRKDRE---------------ISRLDREIERLERELEEER-----------ERIEELKRKLERLKELWKLE 505
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
391-711 |
5.61e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.28 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 391 LKQRIETLEK------ESAALADRLIQGQVTRAQEAEenyvIKRELAVVRQQCSSAAEDLQKAQSTIRQLQEQqENPRLT 464
Cdd:PRK11281 41 VQAQLDALNKqklleaEDKLVQQDLEQTLALLDKIDR----QKEETEQLKQQLAQAPAKLRQAQAELEALKDD-NDEETR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 465 EDFVSHLETELEQsrlRETETLGALREMQdkvldmekrnsslpdeNNVAQLQEELKALKVREGQAVASTRELKLQLQELS 544
Cdd:PRK11281 116 ETLSTLSLRQLES---RLAQTLDQLQNAQ----------------NDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 545 dtwqAHLARGGRWKESPRKLVVGELQDELMSVrlrEAQAlaegrELRQRVVELETQdhihrnLLNRVEAERAALQEKLQY 624
Cdd:PRK11281 177 ----NLLKGGKVGGKALRPSQRVLLQAEQALL---NAQN-----DLQRKSLEGNTQ------LQDLLQKQRDYLTARIQR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 625 LAAQNKGLQTQLSESRRKQAE---AECKSKEEvmAVRLRE----ADSMAAVAEMRQRIAEL-----EIQREEGRIQGQLN 692
Cdd:PRK11281 239 LEHQLQLLQEAINSKRLTLSEktvQEAQSQDE--AARIQAnplvAQELEINLQLSQRLLKAteklnTLTQQNLRVKNWLD 316
|
330
....*....|....*....
gi 229577000 693 HSDSSQyiRELKDQIEELK 711
Cdd:PRK11281 317 RLTQSE--RNIKEQISVLK 333
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
534-718 |
5.72e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.43 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 534 RELKLQLQELsdtwQAHLArGGRWKEsprklvvgeLQDELMSVRLREAQALAEGRELRQRVVELETQDHIHRNLLNRVEA 613
Cdd:TIGR02168 216 KELKAELREL----ELALL-VLRLEE---------LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 614 ERAALQEKLQYLAAQNKGLQTQLSESRRKQAEAEckSKEEVMAVRLREADSM-----AAVAEMRQRIAELEIQREEGRIQ 688
Cdd:TIGR02168 282 EIEELQKELYALANEISRLEQQKQILRERLANLE--RQLEELEAQLEELESKldelaEELAELEEKLEELKEELESLEAE 359
|
170 180 190
....*....|....*....|....*....|...
gi 229577000 689 GQLNHS---DSSQYIRELKDQIEELKAEVRLLK 718
Cdd:TIGR02168 360 LEELEAeleELESRLEELEEQLETLRSKVAQLE 392
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
426-682 |
6.08e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.17 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 426 IKRELAVVRQQCSSAAEDLQKAQSTIRQLQEQQ--ENPRLTEDFVSHLETELEQSRLRETETLGALREMQdkVLDMEKRN 503
Cdd:PRK10246 255 LQQEASRRQQALQQALAAEEKAQPQLAALSLAQpaRQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTM--ALRARIRH 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 504 SSLpdeNNVAQLQEELKALkvreGQAVASTRELKLQLQELSDtWQAHLARGGRWKESPRKLvvgelQDELMSVRLRE--- 580
Cdd:PRK10246 333 HAA---KQSAELQAQQQSL----NTWLAEHDRFRQWNNELAG-WRAQFSQQTSDREQLRQW-----QQQLTHAEQKLnal 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 581 ------------AQALA---EGRELRQRVVELETQdhiHRNLLNRveaeRAALQEKLQYLAAQNKGLQTQLSESRRKQAE 645
Cdd:PRK10246 400 paitltltadevAAALAqhaEQRPLRQRLVALHGQ---IVPQQKR----LAQLQVAIQNVTQEQTQRNAALNEMRQRYKE 472
|
250 260 270
....*....|....*....|....*....|....*..
gi 229577000 646 aeckSKEEVMAVRlreadsmaAVAEMRQRIAELEIQR 682
Cdd:PRK10246 473 ----KTQQLADVK--------TICEQEARIKDLEAQR 497
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
357-543 |
6.08e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 357 PKKMKRLEKEYAamKSKEMEEQIEIKRLRTENRLLKQRI----ETLEKESAA------LADRLIQgQVTRAQeaEENYVI 426
Cdd:PRK04778 255 EKEIQDLKEQID--ENLALLEELDLDEAEEKNEEIQERIdqlyDILEREVKArkyvekNSDTLPD-FLEHAK--EQNKEL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 427 KRELAVVRQQCSSAAEDLQKAQSTIRQLQEQQENprltedfVSHLETELEQSRLRETETLGALREMQDKVLDMEKrnssl 506
Cdd:PRK04778 330 KEEIDRVKQSYTLNESELESVRQLEKQLESLEKQ-------YDEITERIAEQEIAYSELQEELEEILKQLEEIEK----- 397
|
170 180 190
....*....|....*....|....*....|....*..
gi 229577000 507 pdenNVAQLQEELKALKVREGQAVASTRELKLQLQEL 543
Cdd:PRK04778 398 ----EQEKLSEMLQGLRKDELEAREKLERYRNKLHEI 430
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
358-713 |
6.36e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 358 KKMKRLEKEYAAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKesaaladrliqgqvtRAQEAEEnyvIKRELAVVRQQC 437
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE---------------LKEEIEE---LEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 438 SSAAEDLQKAQSTIRQLQEQQENprlTEDFVSHLEtELEQSRLRETETLGALREMQDKVLDMEKRNSSLpdENNVAQLQE 517
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEE---LEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL--EEEINGIEE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 518 ELKALKVREGQAvastRELKLQLQELSDtwqahlaRGGRWKESPRKLvvgelqDELMSVrlreaqaLAEGRELRQRVVEL 597
Cdd:PRK03918 329 RIKELEEKEERL----EELKKKLKELEK-------RLEELEERHELY------EEAKAK-------KEELERLKKRLTGL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 598 ETQDHIhrNLLNRVEAERAALQEKLQYLAAQNKGLQTQLSESRR-----KQAEAEC---------KSKEEVMAVRLREad 663
Cdd:PRK03918 385 TPEKLE--KELEELEKAKEEIEEEISKITARIGELKKEIKELKKaieelKKAKGKCpvcgrelteEHRKELLEEYTAE-- 460
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 229577000 664 sMAAVAEMRQRIAELE--IQREEGRIQGQLNHSDSSQYIRELKDQIEELKAE 713
Cdd:PRK03918 461 -LKRIEKELKEIEEKErkLRKELRELEKVLKKESELIKLKELAEQLKELEEK 511
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
426-716 |
9.08e-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: 39.82 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 426 IKRELAVVRQQCSSAAEDLQKAQSTIRQLQEQQENPRLTEDFVShleTELEQSRLRETETLGALREMQDKVLDMEKRNSS 505
Cdd:pfam12128 602 LRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFAR---TALKNARLDLRRLFDEKQSEKDKKNKALAERKD 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 506 LPDENnVAQLQEELKALKVREGQAVASTRElklQLQELSDTWQAHlarggrwkespRKLVVGELQDELMSVR----LREA 581
Cdd:pfam12128 679 SANER-LNSLEAQLKQLDKKHQAWLEEQKE---QKREARTEKQAY-----------WQVVEGALDAQLALLKaaiaARRS 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 582 QALAE--------GRELR------QRVVELETQdhiHRNLLNRVEAERAALQEKLQY-------LAAQNKGLQTQLSESR 640
Cdd:pfam12128 744 GAKAElkaletwyKRDLAslgvdpDVIAKLKRE---IRTLERKIERIAVRRQEVLRYfdwyqetWLQRRPRLATQLSNIE 820
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 229577000 641 RKQAEAeckskeevmavrlrEADSMAAVAEMRQRIAELEIQREEGRIQGQLnhsdSSQYIRELKDQIEELkAEVRL 716
Cdd:pfam12128 821 RAISEL--------------QQQLARLIADTKLRRAKLEMERKASEKQQVR----LSENLRGLRCEMSKL-ATLKE 877
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
347-537 |
9.32e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 9.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 347 VLKAYQVKYNPKKMKRLEKEY---AAMKSKEMEEQIEIKRLRTENRLLKQRIETLEKEsaalADRLIQGQVTRAQEaEEN 423
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKkmkAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE----AEEKKKAEELKKAE-EEN 1659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577000 424 YVIKRELAVVRQQCSSAAEDLQKAQSTIR----QLQEQQENPRLTEDFVSHLETEL---EQSRLRETETLGALREMQDKV 496
Cdd:PTZ00121 1660 KIKAAEEAKKAEEDKKKAEEAKKAEEDEKkaaeALKKEAEEAKKAEELKKKEAEEKkkaEELKKAEEENKIKAEEAKKEA 1739
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 229577000 497 LDMEKRNSSLPDE----NNVAQL--QEELKALKVREGQAVASTRELK 537
Cdd:PTZ00121 1740 EEDKKKAEEAKKDeeekKKIAHLkkEEEKKAEEIRKEKEAVIEEELD 1786
|
|
| |
