|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2-1173 |
4.35e-111 |
|
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: 375.46 E-value: 4.35e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 2 YIKQVIIQGFRSYRdQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSD-EFSHLRPEQRLALLH-------------- 66
Cdd:pfam02463 1 YLKRIEIEGFKSYA-KTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGErSAKSLRSERLSDLIHsksgafvnsaevei 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 67 ----------IDKEEVSLRRVIGAKKD-QYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKLL 135
Cdd:pfam02463 80 tfdnedhelpIDKEEVSIRRRVYRGGDsEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 136 REVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKL 215
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 216 DELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGN 295
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 296 SEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKEL 375
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 376 KSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWR-EENA 454
Cdd:pfam02463 400 KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLkETQL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 455 EQQALAAKREDLEKKQQLLRAATGKAILNGIDSINKVLDHFRRKGINQHVQNGYHGIVMNNFECEPAFYTCVEVTAGNRL 534
Cdd:pfam02463 480 VKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADE 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 535 FYHIVDSDEVSTKILMEFNKMNLPGEVTFLPLNKLDVrdtaypetndaipmisklryNPRFDKAFKHVFGKTLICRSMEV 614
Cdd:pfam02463 560 VEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV--------------------LEIDPILNLAQLDKATLEADEDD 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 615 STQLARAFTMDCITLEGDQVSHRGALTGGYYDTRKSRLELQKDVRKAEEELGELEAKLNENLRRNIERINNEIDQLMNQM 694
Cdd:pfam02463 620 KRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQL 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 695 QQIETQQRKFKASRDSILSEMKMlKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVD 774
Cdd:pfam02463 700 EIKKKEQREKEELKKLKLEAEEL-LADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAE 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 775 ALNDEIRQLQQEnrqllneriKLEGIITRVETYLNENLRKRLDQVEQELNELRETEGGTVLTATTSELEAINKRVKDTMA 854
Cdd:pfam02463 779 EREKTEKLKVEE---------EKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLE 849
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 855 RSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEAFEK-- 932
Cdd:pfam02463 850 KLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAei 929
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 933 ------YQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGYKSIMELMNVLELRKYEAIQ 1006
Cdd:pfam02463 930 llkyeeEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIR 1009
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1007 LTFKQVSKNFSEVFQKLVPggkatlvMKKGDVEGSQSQDEGEGSGEsergsgsqsSVPSVDQFTGVGIRVSFTGKQGEMR 1086
Cdd:pfam02463 1010 AIIEETCQRLKEFLELFVS-------INKGWNKVFFYLELGGSAEL---------RLEDPDDPFSGGIEISARPPGKGVK 1073
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1087 EMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYGVK 1166
Cdd:pfam02463 1074 NLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVT 1153
|
....*...
gi 1958644837 1167 F-RNKVSH 1173
Cdd:pfam02463 1154 MvENGVST 1161
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-1168 |
4.27e-95 |
|
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: 330.49 E-value: 4.27e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 2 YIKQVIIQGFRSYRDQTIVdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSH-LRPEQRLALLHIDKE---------- 70
Cdd:TIGR02169 1 YIERIELENFKSFGKKKVI-PFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKaMRAERLSDLISNGKNgqsgneayvt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 71 --------------EVSLRRVIG--AKKDQYFLDKKMVTKNDVMNLLESAGFSrSNPYYIVKQGKINQMATAPDSQRLKL 134
Cdd:TIGR02169 80 vtfknddgkfpdelEVVRRLKVTddGKYSYYYLNGQRVRLSEIHDFLAAAGIY-PEGYNVVLQGDVTDFISMSPVERRKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 135 LREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAK 214
Cdd:TIGR02169 159 IDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 215 LDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAM--------KEEKEQLSAERQEQIKQRTKLELKAK 286
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERSIAEKERELE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 287 DLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARL------AQATQERTDLY--AKQGRG 358
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELeevdkeFAETRDELKDYreKLEKLK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 359 SQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKK 438
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 439 DELQSERNYLWRE-ENAEQQALAAKREdlekkqQLLRAATGKAILNGIDsinkvldhfrrkginqhvqnGYHGIVMNNFE 517
Cdd:TIGR02169 479 DRVEKELSKLQRElAEAEAQARASEER------VRGGRAVEEVLKASIQ--------------------GVHGTVAQLGS 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 518 CEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLpGEVTFLPLNKLDV--RDTAYPETNDAIPM-ISKLRYNPR 594
Cdd:TIGR02169 533 VGERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKA-GRATFLPLNKMRDerRDLSILSEDGVIGFaVDLVEFDPK 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 595 FDKAFKHVFGKTLICRSMEVSTQLARAFTMdcITLEGDQVSHRGALTGGYYDTRKSRLELQKDVRKAEEELGELEAKLNE 674
Cdd:TIGR02169 612 YEPAFKYVFGDTLVVEDIEAARRLMGKYRM--VTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRE 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 675 --NLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRES 752
Cdd:TIGR02169 690 lsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE 769
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 753 LKAELGTdllSQLSLEDQKRVDAlNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRL---DQVEQELNELRET 829
Cdd:TIGR02169 770 LEEDLHK---LEEALNDLEARLS-HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEyleKEIQELQEQRIDL 845
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 830 EGGTVltATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLL 909
Cdd:TIGR02169 846 KEQIK--SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 910 KKKEECMKKIRELGSLPQEAFE-KYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGYK 988
Cdd:TIGR02169 924 AKLEALEEELSEIEDPKGEDEEiPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERK 1003
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 989 SIMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKLvPGGKATLVMKKGDvegsqsqdegegsgesergsgsqssvpsvDQ 1068
Cdd:TIGR02169 1004 AILERIEEYEKKKREVFMEAFEAINENFNEIFAEL-SGGTGELILENPD-----------------------------DP 1053
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1069 FTGvGIRVSFTGKQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFIT 1148
Cdd:TIGR02169 1054 FAG-GLELSAKPKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFIV 1132
|
1210 1220
....*....|....*....|
gi 1958644837 1149 TTFRPELLESADKFYGVKFR 1168
Cdd:TIGR02169 1133 VSLRSPMIEYADRAIGVTMR 1152
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-1174 |
4.22e-84 |
|
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: 298.89 E-value: 4.22e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 2 YIKQVIIQGFRSYRDQTIVDpFSSKHNVIVGRNGSGKSNFFYAIQFVLSDE-FSHLRPEQ-----------RLALLH--- 66
Cdd:TIGR02168 1 RLKKLELAGFKSFADPTTIN-FDKGITGIVGPNGCGKSNIVDAIRWVLGEQsAKALRGGKmedvifngsetRKPLSLaev 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 67 -------------IDKEEVSLRRVIGAKKD-QYFLDKKMVTKNDVMNLLESAGFSRSNpYYIVKQGKINQMATAPDSQRL 132
Cdd:TIGR02168 80 elvfdnsdgllpgADYSEISITRRLYRDGEsEYFINGQPCRLKDIQDLFLDTGLGKRS-YSIIEQGKISEIIEAKPEERR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 133 KLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETR 212
Cdd:TIGR02168 159 AIFEEAAGISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 213 AKLDELSAKREtsgEKSRQLRDAQQDARDKMEDIErqvrELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDEL 292
Cdd:TIGR02168 239 EELEELQEELK---EAEEELEELTAELQELEEKLE----ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 293 AGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLyakqgrgsqftskEERDKWIK 372
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL-------------ESRLEELE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 373 KELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKyyEVKNKKDELQSERNYLWREE 452
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEEL 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 453 NAEQQALAAKREDLEKKQQLLRAATGKA--ILNGIDSINKVLDHFRRKGI-------NQHVQNGYHGIVMNNFECEPAFY 523
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELaqLQARLDSLERLQENLEGFSEgvkallkNQSGLSGILGVLSELISVDEGYE 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 524 TCVEVTAGNRLFYHIVDSDEVSTKILmEFNKMNLPGEVTFLPLNKLDVRDTAYPETNDAIPMISKLR-------YNPRFD 596
Cdd:TIGR02168 537 AAIEAALGGRLQAVVVENLNAAKKAI-AFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGvakdlvkFDPKLR 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 597 KAFKHVFGKTLICRSMEVSTQLARA--FTMDCITLEGDQVSHRGALTGGYYDTRKSRL-------ELQKDVRKAEEELGE 667
Cdd:TIGR02168 616 KALSYLLGGVLVVDDLDNALELAKKlrPGYRIVTLDGDLVRPGGVITGGSAKTNSSILerrreieELEEKIEELEEKIAE 695
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 668 LEAKLNEnLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTF-------MPKQRSLQSLE 740
Cdd:TIGR02168 696 LEKALAE-LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELteleaeiEELEERLEEAE 774
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 741 ASLHAMESTRESLKAELgTDLLSQLSLEDqKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLnENLRKRLDQVE 820
Cdd:TIGR02168 775 EELAEAEAEIEELEAQI-EQLKEELKALR-EALDELRAELTLLNEEAANLRERLESLERRIAATERRL-EDLEEQIEELS 851
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 821 QELNELRE--TEGGTVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKsmerwKNMEKEHmdAINHDTKEL 898
Cdd:TIGR02168 852 EDIESLAAeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES-----KRSELRR--ELEELREKL 924
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 899 EKMTNRQGMLLKKKEECMKKIRELGSLPQE---AFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEK 975
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEYSLTLEeaeALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDF 1004
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 976 LIKRQEELDRGYKSIMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKLVPGGKATLVMKKGDvegsqsqDEGEgsgeser 1055
Cdd:TIGR02168 1005 LTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRVFPKLFGGGEAELRLTDPE-------DLLE------- 1070
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1056 gsgsqssvpsvdqfTGVGIRVSFTGKQgeMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSD 1135
Cdd:TIGR02168 1071 --------------AGIEIFAQPPGKK--NQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFAN 1134
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|
gi 1958644837 1136 MIMELAVHAQFITTTFRPELLESADKFYGVKFRNK-VSHI 1174
Cdd:TIGR02168 1135 LLKEFSKNTQFIVITHNKGTMEVADQLYGVTMQEKgVSKI 1174
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
3-134 |
1.51e-72 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 241.40 E-value: 1.51e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 3 IKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLH---------------- 66
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEPFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALLHegsgpsvmsayveiif 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644837 67 --------IDKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKL 134
Cdd:cd03272 81 dnsdnrfpIDKEEVRLRRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMKQDEQQEM 156
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-1165 |
3.08e-63 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 234.06 E-value: 3.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1 MYIKQVIIQGFRSYRDQTIVdPFSSKHNVIVGRNGSGKSNFFYAIQFVL---------SDEF-------SHLRPEQRLA- 63
Cdd:COG1196 1 MRLKRLELAGFKSFADPTTI-PFEPGITAIVGPNGSGKSNIVDAIRWVLgeqsakslrGGKMedvifagSSSRKPLGRAe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 64 ----------LLHIDKEEVSLRRVIGAKKD-QYFLDKKMVTKNDVMNLLESAGFSRsNPYYIVKQGKINQMATAPDSQRL 132
Cdd:COG1196 80 vsltfdnsdgTLPIDYDEVTITRRLYRSGEsEYYINGKPCRLKDIQDLFLDTGLGP-ESYSIIGQGMIDRIIEAKPEERR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 133 KLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETR 212
Cdd:COG1196 159 AIIEEAAGISKYKERKEEAERKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 213 AKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDEL 292
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 293 AGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTdlyAKQGRGSQFTSKEERdkwIK 372
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA---EAEEELEELAEELLE---AL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 373 KELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREE 452
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 453 NAEQQALAAKREDLEKKQQLLRAATgkailngidSINKVLDHFRRKGINQHV---QNGYHGIVMNNFECEPAFYTCVEVT 529
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLL---------EAEADYEGFLEGVKAALLlagLRGLAGAVAVLIGVEAAYEAALEAA 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 530 AGNRLFYHIVDSDEVSTKILmEFNKMNLPGEVTFLPLNKLDVRDTAYPETNDA--IPMISKLRYNPRFDKAFKHVFGKTL 607
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAI-EYLKAAKAGRATFLPLDKIRARAALAAALARGaiGAAVDLVASDLREADARYYVLGDTL 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 608 ICRSMEVSTQLARAFTMDciTLEGDQVSHRGALTGGyydtrksrlelqkdvrkaeeelgeleaklnenlrrnierinnei 687
Cdd:COG1196 623 LGRTLVAARLEAALRRAV--TLAGRLREVTLEGEGG-------------------------------------------- 656
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 688 dqlmNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKtfmpkqrsLQSLEASLHAMESTRESLKAELGTDLLSQLSL 767
Cdd:COG1196 657 ----SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE--------LELEEALLAEEEEERELAEAEEERLEEELEEE 724
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 768 EDQKRVDALNDEIRQLQQENRQLLNEriklEGIITRVETYLNENLRKRLDQVEQELNELretegGTV-LTAtTSELEAIN 846
Cdd:COG1196 725 ALEEQLEAEREELLEELLEEEELLEE----EALEELPEPPDLEELERELERLEREIEAL-----GPVnLLA-IEEYEELE 794
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 847 KRVKDTMARSEDLDNSIDKTEAGIKElqksmerwknmekehmdaINHDTKELekmtnrqgmllkkkeecmkkirelgslp 926
Cdd:COG1196 795 ERYDFLSEQREDLEEARETLEEAIEE------------------IDRETRER---------------------------- 828
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 927 qeafekyqtlslkqlfrkleqcntelkkyshvnkkaldqfvnFSEqkeklikrqeeldrgyksimelmnvlelrkyeaiq 1006
Cdd:COG1196 829 ------------------------------------------FLE----------------------------------- 831
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1007 lTFKQVSKNFSEVFQKLVPGGKATLVMKKGDvegsqsqdegegsgesergsgsqssvpsvDQF-TGVGIRVSFTGKqgEM 1085
Cdd:COG1196 832 -TFDAVNENFQELFPRLFGGGEAELLLTDPD-----------------------------DPLeTGIEIMAQPPGK--KL 879
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1086 REMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQ--HRkaVSDMIMELAVHAQFITTTFRPELLESADKFY 1163
Cdd:COG1196 880 QRLSLLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDAnvER--FAELLKEMSEDTQFIVITHNKRTMEAADRLY 957
|
..
gi 1958644837 1164 GV 1165
Cdd:COG1196 958 GV 959
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1081-1175 |
3.36e-57 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 197.87 E-value: 3.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1081 KQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESAD 1160
Cdd:cd03272 149 KQDEQQEMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVAD 228
|
90
....*....|....*
gi 1958644837 1161 KFYGVKFRNKVSHID 1175
Cdd:cd03272 229 KFYGVKFRNKVSTID 243
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1038-1173 |
6.91e-38 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 140.14 E-value: 6.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1038 VEGSQSQDEGEGSGESERGSGSQSSVPSVDqftgVGI----RVSFTgKQGEMREMqqLSGGQKSLVALALIFAIQKCDPA 1113
Cdd:cd03239 45 VLGGKAAKLRRGSLLFLAGGGVKAGINSAS----VEItfdkSYFLV-LQGKVEQI--LSGGEKSLSALALIFALQEIKPS 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958644837 1114 PFYLFDEIDQALDAQHRKAVSDMIMELAVH-AQFITTTFRPELLESADKFYGVKFRNKVSH 1173
Cdd:cd03239 118 PFYVLDEIDAALDPTNRRRVSDMIKEMAKHtSQFIVITLKKEMFENADKLIGVLFVHGVST 178
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
506-618 |
2.97e-28 |
|
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 214944 [Multi-domain] Cd Length: 120 Bit Score: 110.40 E-value: 2.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 506 NGYHGIVMNNFECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILmEFNKMNLPGEVTFLPLNKLD--------VRDTAYP 577
Cdd:smart00968 1 PGVLGRVADLISVDPKYETALEAALGGRLQAVVVDTEETAKKAI-EFLKKNRLGRATFLPLDKIKprspagskLREALLP 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1958644837 578 ETNDAIPMISKLRYNPRFDKAFKHVFGKTLICRSMEVSTQL 618
Cdd:smart00968 80 EPGFVGPAIDLVEYDPELRPALEYLLGNTLVVDDLETARRL 120
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1090-1169 |
2.65e-27 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 108.99 E-value: 2.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1090 QLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVH-AQFITTTFRPELLESADKFYGVKFR 1168
Cdd:cd03227 77 QLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKgAQVIVITHLPELAELADKLIHIKKV 156
|
.
gi 1958644837 1169 N 1169
Cdd:cd03227 157 I 157
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1080-1172 |
1.18e-23 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 99.85 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1080 GKQgeMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESA 1159
Cdd:cd03278 105 GKK--VQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAA 182
|
90
....*....|....
gi 1958644837 1160 DKFYGVKFRNK-VS 1172
Cdd:cd03278 183 DRLYGVTMQESgVS 196
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-123 |
1.22e-23 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 99.30 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 3 IKQVIIQGFRSYRDQTIVdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHidkEEVslrrvigakk 82
Cdd:cd03239 1 IKQITLKNFKSYRDETVV-GGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAG---GGV---------- 66
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1958644837 83 dqyfldKKMVTKNDVMNLLEsagfsrsNPYYIVKQGKINQM 123
Cdd:cd03239 67 ------KAGINSASVEITFD-------KSYFLVLQGKVEQI 94
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
506-619 |
1.77e-23 |
|
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 461926 [Multi-domain] Cd Length: 116 Bit Score: 96.56 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 506 NGYHGIVMNNFECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLpGEVTFLPLNKLDVRDTAYPET--NDAI 583
Cdd:pfam06470 2 KGVLGRLADLIEVDEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKL-GRATFLPLDRLKPRPRRPGADlkGGAG 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 1958644837 584 PMISKLRYNPRFDKAFKHVFGKTLICRSMEVSTQLA 619
Cdd:pfam06470 81 PLLDLVEYDDEYRKALRYLLGNTLVVDDLDEALELA 116
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1090-1175 |
2.97e-18 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 85.81 E-value: 2.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1090 QLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYGVKFRN 1169
Cdd:cd03273 166 ELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNANVLFRTRFVD 245
|
....*.
gi 1958644837 1170 KVSHID 1175
Cdd:cd03273 246 GTSTVT 251
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1086-1174 |
8.61e-17 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 81.46 E-value: 8.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1086 REMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAV-HAQFITTTFRPELLESADKFYG 1164
Cdd:cd03275 151 RDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGpNFQFIVISLKEEFFSKADALVG 230
|
90
....*....|...
gi 1958644837 1165 VkFRNK---VSHI 1174
Cdd:cd03275 231 V-YRDQecnSSKV 242
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-120 |
1.21e-16 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 81.19 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1 MYIKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLS-DEFSHLRPEQRLALLH------IDKEEVS 73
Cdd:cd03273 1 MHIKEIILDGFKSYATRTVISGFDPQFNAITGLNGSGKSNILDAICFVLGiTNLSTVRASNLQDLIYkrgqagITKASVT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 74 L-----------------------RRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKI 120
Cdd:cd03273 81 IvfdnsdksqspigfenypeitvtRQIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRI 150
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-479 |
1.79e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 85.12 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFVL-SDEFSHLRPEQRLALLHIDKEEVSLRRVIG 79
Cdd:PRK03918 1 MKIEELKIKNFRSHKSSVV--EFDDGINLIIGQNGSGKSSILEAILVGLyWGHGSKPKGLKKDDFTRIGGSGTEIELKFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 80 AKKDQYFLDKKMVTKNDVMNLLESAGFSRSN------------PYYI------VKQGKINQMATApDSQRLKLLREVAGT 141
Cdd:PRK03918 79 KNGRKYRIVRSFNRGESYLKYLDGSEVLEEGdssvrewverliPYHVflnaiyIRQGEIDAILES-DESREKVVRQILGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 142 RVYDERKEESISLMKETEGKREKINELLKY---IEERLHTLEEEKEELAqyqkwdkmrraleytiynQELNETRAKLDEL 218
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRtenIEELIKEKEKELEEVL------------------REINEISSELPEL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 219 SAKRETSGEKSRQLrdaqQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQdELAGNSEQ 298
Cdd:PRK03918 220 REELEKLEKEVKEL----EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 299 RKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGiarlaqatqertdlyakqgrgsqfTSKEERDKWIKKELKSL 378
Cdd:PRK03918 295 YIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL------------------------EEKEERLEELKKKLKEL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 379 DqainDKKRQIAAIHKDLEDTEAnKEKNLEQYNKLDQDLNevkarVEELDRKYYEVKNKKDELQSERNYLwreeNAEQQA 458
Cdd:PRK03918 351 E----KRLEELEERHELYEEAKA-KKEELERLKKRLTGLT-----PEKLEKELEELEKAKEEIEEEISKI----TARIGE 416
|
490 500
....*....|....*....|.
gi 1958644837 459 LAAKREDLEKKQQLLRAATGK 479
Cdd:PRK03918 417 LKKEIKELKKAIEELKKAKGK 437
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1086-1165 |
2.74e-15 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 76.18 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1086 REMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYGV 1165
Cdd:cd03274 123 KNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELADRLVGI 202
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
3-181 |
5.53e-15 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 75.05 E-value: 5.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 3 IKQVIIQGFRSYRDQTIVDpFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHlRPEQRLALLHIDKEEVSLRrvigakk 82
Cdd:COG0419 2 LLRLRLENFRSYRDTETID-FDDGLNLIVGPNGAGKSTILEAIRYALYGKARS-RSKLRSDLINVGSEEASVE------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 83 dqyfldkkmvtkndvmnlLEsagFSRSNPYYIVK--QGKINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEG 160
Cdd:COG0419 73 ------------------LE---FEHGGKRYRIErrQGEFAEFLEAKPSERKEALKRLLGLEIYEELKERLKELEEALES 131
|
170 180
....*....|....*....|.
gi 1958644837 161 KREKINELLKYIEERLHTLEE 181
Cdd:COG0419 132 ALEELAELQKLKQEILAQLSG 152
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
5-59 |
3.86e-13 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 68.54 E-value: 3.86e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1958644837 5 QVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPE 59
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRR 55
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1090-1166 |
4.17e-13 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 68.04 E-value: 4.17e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958644837 1090 QLSGGQKSLVALALIFAIQkcdpAPFYLFDEIDQALDAQHRKAVSDMIMELAVH-AQFITTTFRPELLE-SADKFYGVK 1166
Cdd:cd00267 80 QLSGGQRQRVALARALLLN----PDLLLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAElAADRVIVLK 154
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
3-105 |
2.39e-12 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 68.37 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 3 IKQVIIQGFRSYRDQTIVDPFSSkHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLH---------------- 66
Cdd:cd03275 1 LKRLELENFKSYKGRHVIGPFDR-FTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYrarvgkpdsnsayvta 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1958644837 67 ----IDKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAG 105
Cdd:cd03275 80 vyedDDGEEKTFRRIITGGSSSYRINGKVVSLKEYNEELEKIN 122
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
89-457 |
2.95e-12 |
|
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: 70.92 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 89 KKMVTKNDVMNLLESagFSRSNPYYIVKqgkINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINEL 168
Cdd:pfam17380 234 EKMERRKESFNLAED--VTTMTPEYTVR---YNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEK 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 169 LKYIEERLHTLEEEKEELAQYQKwdkmrralEYTIYnqelnetrAKLDELSAKRETSGEKSRQlrdaqQDARDKMEDIER 248
Cdd:pfam17380 309 AREVERRRKLEEAEKARQAEMDR--------QAAIY--------AEQERMAMERERELERIRQ-----EERKRELERIRQ 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 249 QvrELKTKISAMKEeKEQLSAERQEQiKQRTKLELKAKDLQDELagnSEQRKRLLKERQKLLEKIEEKQKELAETEpkFN 328
Cdd:pfam17380 368 E--EIAMEISRMRE-LERLQMERQQK-NERVRQELEAARKVKIL---EEERQRKIQQQKVEMEQIRAEQEEARQRE--VR 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 329 SVKEKEERGIARLAQATQERTD----------------LYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAI 392
Cdd:pfam17380 439 RLEEERAREMERVRLEEQERQQqverlrqqeeerkrkkLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLL 518
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 393 HKDLED-----TEANKEKNLEQYNKLDQDLNEVKaRVEELDRKYYEVKNKKDELQSERNYLWREENAEQQ 457
Cdd:pfam17380 519 EKEMEErqkaiYEEERRREAEEERRKQQEMEERR-RIQEQMRKATEERSRLEAMEREREMMRQIVESEKA 587
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
115-475 |
3.71e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.84 E-value: 3.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 115 VKQGKINQMATAPDSQRLKL---LREVAGTRVYDERKEESislmketegkREKINELLKYIEERLHTLEEEKEELAQYQK 191
Cdd:PRK02224 135 VRQGEVNKLINATPSDRQDMiddLLQLGKLEEYRERASDA----------RLGVERVLSDQRGSLDQLKAQIEEKEEKDL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 192 WDKMRRaleytiYNQELNETRAKLDELSAKRETSGEKSRQLR---DAQQDARDKMEDIERQVRELKTKISAMKEEKEQLS 268
Cdd:PRK02224 205 HERLNG------LESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDLRETIAETEREREELA 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 269 AERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAEtepkfnsvkekeergiARLAQatqer 348
Cdd:PRK02224 279 EEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEE----------------CRVAA----- 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 349 tdlyakqgrgSQFTSKEERdkwIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELD 428
Cdd:PRK02224 338 ----------QAHNEEAES---LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAP 404
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958644837 429 RKYYEVKNKKDELQSERNYLwREENAEQQA-LAAKREDLEKKQQLLRA 475
Cdd:PRK02224 405 VDLGNAEDFLEELREERDEL-REREAELEAtLRTARERVEEAEALLEA 451
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-52 |
5.32e-12 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 68.88 E-value: 5.32e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1958644837 1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDE 52
Cdd:COG3593 1 MKLEKIKIKNFRSIKDLSI--ELSDDLTVLVGENNSGKSSILEALRLLLGPS 50
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-476 |
6.44e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.80 E-value: 6.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEfshlrpeqrlallhIDKEEVSLRRVIGa 80
Cdd:COG4717 1 MKIKELEIYGFGKFRDRTI--EFSPGLNVIYGPNEAGKSTLLAFIRAMLLER--------------LEKEADELFKPQG- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 81 kkdqyfldkkmvtKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDS--QRLKLLREVAGTRVYDERKEESISLMKET 158
Cdd:COG4717 64 -------------RKPELNLKELKELEEELKEAEEKEEEYAELQEELEEleEELEELEAELEELREELEKLEKLLQLLPL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 159 EGKREKINELLKYIEERLHTLEEEKEELAQYQ-KWDKMRRALE------YTIYNQELNETRAKLDELSAKRETSGEKSRQ 231
Cdd:COG4717 131 YQELEALEAELAELPERLEELEERLEELRELEeELEELEAELAelqeelEELLEQLSLATEEELQDLAEELEELQQRLAE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 232 LRDAQQDARDKMEDIERQVRELKTKISAmKEEKEQLSAERQ--------------------------------------- 272
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENELEA-AALEERLKEARLllliaaallallglggsllsliltiagvlflvlgllall 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 273 --EQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKL-------LEKIEEKQKELAETEPKFNSVKEKEERgiARLAQ 343
Cdd:COG4717 290 flLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppdlsPEELLELLDRIEELQELLREAEELEEE--LQLEE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 344 ATQERTDLYAKQGrgsqFTSKEERDKWIK--KELKSLDQAINDKKRQIAAIHKDLED--TEANKEKNLEQYNKLDQDLNE 419
Cdd:COG4717 368 LEQEIAALLAEAG----VEDEEELRAALEqaEEYQELKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELEE 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644837 420 VKARVEELDRKYYEVKNKKDELQSERNYlwREENAEQQALAAKREDLEKKQQLLRAA 476
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGEL--AELLQELEELKAELRELAEEWAALKLA 498
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
145-470 |
3.00e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 68.24 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 145 DERKEESISLMKETEGKReKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELN---ETRAKLDELSAK 221
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKK-KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKkkaEEAKKADEAKKK 1452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 222 RETSgEKSRQLRDAQQDARdKMEDIERQVRELKTKISAMKEEKEqlSAERQEQIKQRTKLELKAKDLQ--DELAGNSEQR 299
Cdd:PTZ00121 1453 AEEA-KKAEEAKKKAEEAK-KADEAKKKAEEAKKADEAKKKAEE--AKKKADEAKKAAEAKKKADEAKkaEEAKKADEAK 1528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 300 KRLLKERQKLLEKIEEKQKelAETEPKFNSVKEKEERGIARLAQATQERTDLY---------AKQGRGSQFTSKEERDKW 370
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKK--ADELKKAEELKKAEEKKKAEEAKKAEEDKNMAlrkaeeakkAEEARIEEVMKLYEEEKK 1606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 371 IKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQ---DLNEVKARVEELDRKYYEVKNKKDELQSErny 447
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkkAEEENKIKAAEEAKKAEEDKKKAEEAKKA--- 1683
|
330 340
....*....|....*....|...
gi 1958644837 448 lwrEENAEQQALAAKREDLEKKQ 470
Cdd:PTZ00121 1684 ---EEDEKKAAEALKKEAEEAKK 1703
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
234-476 |
4.46e-11 |
|
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: 66.33 E-value: 4.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 234 DAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKI 313
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 314 EEKQKELAetepkfnsvkekeERGIARLAQATQERTDLYAKQGRGSQFTskeerdkwikKELKSLDQAINDKKRQIAAIH 393
Cdd:COG4942 100 EAQKEELA-------------ELLRALYRLGRQPPLALLLSPEDFLDAV----------RRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 394 KDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKyyevKNKKDELQSErnyLWREENAEQQALAAKREDLEKKQQLL 473
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEAL----KAERQKLLAR---LEKELAELAAELAELQQEAEELEALI 229
|
...
gi 1958644837 474 RAA 476
Cdd:COG4942 230 ARL 232
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
146-486 |
5.65e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.47 E-value: 5.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 146 ERKEESISLMKETEGKReKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRETS 225
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEEAK-KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE 1532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 226 GEKSRQLRDAQQ----DARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQ--RTKLELKAKDLQDELAGNSEQR 299
Cdd:PTZ00121 1533 AKKADEAKKAEEkkkaDELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeEARIEEVMKLYEEEKKMKAEEA 1612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 300 KRLLKERQKLLE-KIEEKQKELAETEPKfnsvKEKEERGIARLAQATQERTDLyakqgRGSQFTSKEERDKWIKKELKSL 378
Cdd:PTZ00121 1613 KKAEEAKIKAEElKKAEEEKKKVEQLKK----KEAEEKKKAEELKKAEEENKI-----KAAEEAKKAEEDKKKAEEAKKA 1683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 379 DQainDKKRQIAAIHKDLEdtEANK--------EKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELqsernylwR 450
Cdd:PTZ00121 1684 EE---DEKKAAEALKKEAE--EAKKaeelkkkeAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA--------K 1750
|
330 340 350
....*....|....*....|....*....|....*.
gi 1958644837 451 EENAEQQALAAKREDLEKKQQLLRAATGKAILNGID 486
Cdd:PTZ00121 1751 KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
144-479 |
7.16e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 7.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 144 YDERKEESISLMKETEGKREKINELLKYIEErlhtLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRE 223
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERLEELKKKLKE----LEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 224 TSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEK-------EQLSAERQEQIKQRTKLELkaKDLQDELAgNS 296
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgRELTEEHRKELLEEYTAEL--KRIEKELK-EI 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 297 EQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEER----GIARLAQATQERTDLYAK----QGRGSQFTSKEERD 368
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKlkkyNLEELEKKAEEYEKLKEKliklKGEIKSLKKELEKL 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 369 KWIKKELKSLDQAINDKKRQIAAIHKDLEdteankEKNLEQYNKLDQDLNEvkarVEELDRKYYEVKNKKDELQSERNYL 448
Cdd:PRK03918 552 EELKKKLAELEKKLDELEEELAELLKELE------ELGFESVEELEERLKE----LEPFYNEYLELKDAEKELEREEKEL 621
|
330 340 350
....*....|....*....|....*....|.
gi 1958644837 449 WREENaeqqALAAKREDLEKKQQLLRAATGK 479
Cdd:PRK03918 622 KKLEE----ELDKAFEELAETEKRLEELRKE 648
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
238-879 |
6.61e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.78 E-value: 6.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 238 DARDKMEDIERQVRELkTKISAMKEEKEQLSAERQEQIKQRTKLELKAkdlqdelagnSEQRKRLLKERqkllekIEEKQ 317
Cdd:COG4913 239 RAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWF----------AQRRLELLEAE------LEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 318 KELAETEpkfnsvkEKEERGIARLAQATQERTDLYAKQgRGSQFTSKEErdkwIKKELKSLDQAINDKKRQIAAIHKDLE 397
Cdd:COG4913 302 AELARLE-------AELERLEARLDALREELDELEAQI-RGNGGDRLEQ----LEREIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 398 D----TEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERnylwREENAEQQALAAKREDLEKKQQLL 473
Cdd:COG4913 370 AlglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL----RELEAEIASLERRKSNIPARLLAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 474 RAATGKAIlnGIDSIN--------KVLDHFRRkginqhvqngyhgivmnnfeCEPAfytcVEVTAGNRLFYHIVDS---D 542
Cdd:COG4913 446 RDALAEAL--GLDEAElpfvgeliEVRPEEER--------------------WRGA----IERVLGGFALTLLVPPehyA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 543 EVSTKIlmefNKMNLPGEVTFLPLNKLDVRDTAYPETNDAIPmiSKLRYNPrfdkafkHVFGktlicrsMEVSTQLARAF 622
Cdd:COG4913 500 AALRWV----NRLHLRGRLVYERVRTGLPDPERPRLDPDSLA--GKLDFKP-------HPFR-------AWLEAELGRRF 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 623 TMDC-------------ITLEGdQVSHRGALtgGYYDTRK---SRLELQKDVRKAEeelgeleaklnENLRRNIERINNE 686
Cdd:COG4913 560 DYVCvdspeelrrhpraITRAG-QVKGNGTR--HEKDDRRrirSRYVLGFDNRAKL-----------AALEAELAELEEE 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 687 IDQLMNQMQQIETQQRKFKASRDSIlsemkmlkekRQQSEKTFMpkQRSLQSLEASLHAMESTRESLKAelgtdllsqls 766
Cdd:COG4913 626 LAEAEERLEALEAELDALQERREAL----------QRLAEYSWD--EIDVASAEREIAELEAELERLDA----------- 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 767 leDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVEtylnenlrKRLDQVEQELNELRETEGGTVLTATTSELEAIN 846
Cdd:COG4913 683 --SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE--------KELEQAEEELDELQDRLEAAEDLARLELRALLE 752
|
650 660 670
....*....|....*....|....*....|....*....
gi 1958644837 847 KRVKDTMAR------SEDLDNSIDKTEAGIKELQKSMER 879
Cdd:COG4913 753 ERFAAALGDaverelRENLEERIDALRARLNRAEEELER 791
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
158-443 |
6.93e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.52 E-value: 6.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 158 TEGKREKINELlkyiEERLHTLEEEKEELAQyqkwdKMRRAleytiynQELNETRAKLDELSAKRETSGEKsrqlrdaqq 237
Cdd:PRK02224 470 IEEDRERVEEL----EAELEDLEEEVEEVEE-----RLERA-------EDLVEAEDRIERLEERREDLEEL--------- 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 238 dardkMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAgNSEQRKRLLKERQKLLEKIEEKQ 317
Cdd:PRK02224 525 -----IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVA-ELNSKLAELKERIESLERIRTLL 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 318 KELAETEPKFNSVKEKEErgiARLAQATQERTDLYAKQGRGSQFTSK--EERDKWIKKELKSLDQAI---NDKKRQIAAI 392
Cdd:PRK02224 599 AAIADAEDEIERLREKRE---ALAELNDERRERLAEKRERKRELEAEfdEARIEEAREDKERAEEYLeqvEEKLDELREE 675
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958644837 393 HKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVknkkDELQS 443
Cdd:PRK02224 676 RDDLQAEIGAVENELEELEELRERREALENRVEALEALYDEA----EELES 722
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1-127 |
1.22e-09 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 59.62 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1 MYIKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHIDKEEVSLRRVIGA 80
Cdd:cd03274 1 LIITKLVLENFKSYAGEQVIGPFHKSFSAIVGPNGSGKSNVIDSMLFVFGFRASKMRQKKLSDLIHNSAGHPNLDSCSVE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1958644837 81 KKDQYFLDKKmvtkndvmnLLESAGFSRSNPYYIVKQGKINQMATAP 127
Cdd:cd03274 81 VHFQEIIDKP---------LLKSKGIDLDHNRFLILQGEVEQIAQMP 118
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
126-470 |
1.34e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.85 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 126 APDSQRLKLLREVAGTRVYDE-RKEESISLMKETEGKRE---KINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEY 201
Cdd:PTZ00121 1274 AEEARKADELKKAEEKKKADEaKKAEEKKKADEAKKKAEeakKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE 1353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 202 TIYNQ-ELNETRAKLDELSA-----KRETSGEKSRQLRDAQQdARDKMEDIERQVRELKTKISAMKEEKEqlSAERQEQI 275
Cdd:PTZ00121 1354 AAADEaEAAEEKAEAAEKKKeeakkKADAAKKKAEEKKKADE-AKKKAEEDKKKADELKKAAAAKKKADE--AKKKAEEK 1430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 276 KQRTKLELKAKDLQ--DELAGNSEQRKRLLKERQKLLEKIE-EKQKELAETEPKFNSVKEKEERGIARLAQATQ-ERTDL 351
Cdd:PTZ00121 1431 KKADEAKKKAEEAKkaDEAKKKAEEAKKAEEAKKKAEEAKKaDEAKKKAEEAKKADEAKKKAEEAKKKADEAKKaAEAKK 1510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 352 YAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELD--- 428
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkae 1590
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1958644837 429 --RKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQ 470
Cdd:PTZ00121 1591 eaRIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK 1634
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
156-363 |
1.54e-09 |
|
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: 61.32 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 156 KETEGKREKINELLKYIEERLHTLEEEKEELA-QYQKWDKMRRALEYTI--YNQELNETRAKLDELSAKRETSGEK---- 228
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLkQLAALERRIAALARRIraLEQELAALEAELAELEKEIAELRAEleaq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 229 ----SRQLRDAQQDAR----------DKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAG 294
Cdd:COG4942 103 keelAELLRALYRLGRqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644837 295 NSEQRKRL---LKERQKLLEKIE----EKQKELAEtepkfnsvKEKEERGIARLAQATQERTDLYAKQGRGSQFTS 363
Cdd:COG4942 183 LEEERAALealKAERQKLLARLEkelaELAAELAE--------LQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
3-135 |
1.87e-09 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 58.63 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 3 IKQVIIQGFRSYRDQTIVdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSdefshlrpEQRLALLHIDKeevsLRRVI--GA 80
Cdd:cd03278 1 LKKLELKGFKSFADKTTI-PFPPGLTAIVGPNGSGKSNIIDAIRWVLG--------EQSAKSLRGEK----MSDVIfaGS 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644837 81 KKdqyfldKKMVTKNDVmnlleSAGFSRSNPYY-IVKQGKINQMATAPD--SQRLKLL 135
Cdd:cd03278 68 ET------RKPANFAEV-----TLTFDNSDGRYsIISQGDVSEIIEAPGkkVQRLSLL 114
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
3-51 |
2.12e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 60.71 E-value: 2.12e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1958644837 3 IKQVIIQGFRSYRDQTI-VDPFsskhNVIVGRNGSGKSNFFYAIQFvLSD 51
Cdd:COG4637 2 ITRIRIKNFKSLRDLELpLGPL----TVLIGANGSGKSNLLDALRF-LSD 46
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
205-430 |
3.10e-09 |
|
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: 60.55 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 205 NQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELK 284
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 285 AKDLQDELAG-------NSEQR---------------------KRLLKERQKLLEKIEEKQKELAETEpkfnsvkekeer 336
Cdd:COG4942 99 LEAQKEELAEllralyrLGRQPplalllspedfldavrrlqylKYLAPARREQAEELRADLAELAALR------------ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 337 giARLAQATQERTDLYAKQgrgsqftskeerdkwiKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQD 416
Cdd:COG4942 167 --AELEAERAELEALLAEL----------------EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
250
....*....|....
gi 1958644837 417 LNEVKARVEELDRK 430
Cdd:COG4942 229 IARLEAEAAAAAER 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
146-493 |
3.28e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.21 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 146 ERKEESISLMKETEGKREKINELLKYIEERLHTLEE---EKEELAQyQKWDKMRRALEYtiyNQELNETRAK-------- 214
Cdd:PRK02224 234 ETRDEADEVLEEHEERREELETLEAEIEDLRETIAEterEREELAE-EVRDLRERLEEL---EEERDDLLAEaglddada 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 215 ------LDELSAKRETSGEKSRQLRDAQQDA-------RDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKL 281
Cdd:PRK02224 310 eavearREELEDRDEELRDRLEECRVAAQAHneeaeslREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 282 ELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQAT-----QERTDlyakQG 356
Cdd:PRK02224 390 EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgQPVEG----SP 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 357 RGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIhKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKN 436
Cdd:PRK02224 466 HVETIEEDRERVEELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE 544
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958644837 437 KKDELQSErnylwrEENAEQQAlAAKREDLEKKQQLLRAATGK--AILNGIDSINKVLD 493
Cdd:PRK02224 545 RAAELEAE------AEEKREAA-AEAEEEAEEAREEVAELNSKlaELKERIESLERIRT 596
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1077-1147 |
6.09e-09 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 57.22 E-value: 6.09e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958644837 1077 SF-TGKQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELA---VHAQFI 1147
Cdd:cd03276 95 SFlTSNKAAVRDVKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAkkqPGRQFI 169
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-471 |
7.69e-09 |
|
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: 60.37 E-value: 7.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1 MYIKQVIIQGFRSYRDQTIVDPFSSKHN-VIVGRNGSGKSNFFYAI---------------------------------Q 46
Cdd:TIGR00618 1 MKPLRLTLKNFGSYKGTHTIDFTALGPIfLICGKTGAGKTTLLDAItyalygklprrsevirslnslyaapseaafaelE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 47 FVLSDEFSHLRPEQRLALLHIDKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATA 126
Cdd:TIGR00618 81 FSLGTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 127 PDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKInellkyiEERLHTLEEEKEELAQyqkwdkmrralEYTIYNQ 206
Cdd:TIGR00618 161 KSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELL-------TLRSQLLTLCTPCMPD-----------TYHERKQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 207 ELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVR---ELKTKISAMKEEKEQLSAERQ-----EQIKQR 278
Cdd:TIGR00618 223 VLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRArieELRAQEAVLEETQERINRARKaaplaAHIKAV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 279 TKLELKAKDLQDELAGNSEQRKRLLKERQKLLEK---IEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQ 355
Cdd:TIGR00618 303 TQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQqssIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIH 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 356 GRGSQFTSKEERDKWIKKELKSLD----------QAINDKKRQIAAIHKDLedtEANKEKNLEQYNKLDQDLNEVKARVE 425
Cdd:TIGR00618 383 TLQQQKTTLTQKLQSLCKELDILQreqatidtrtSAFRDLQGQLAHAKKQQ---ELQQRYAELCAAAITCTAQCEKLEKI 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1958644837 426 ELDRKYYEVKNKKDELQSERNYLWREEnaEQQALAAKREDLEKKQQ 471
Cdd:TIGR00618 460 HLQESAQSLKEREQQLQTKEQIHLQET--RKKAVVLARLLELQEEP 503
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-312 |
8.52e-09 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 59.15 E-value: 8.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLH----IDKEEVSLRR 76
Cdd:pfam13175 1 MKIKSIIIKNFRCLKDTEI--DLDEDLTVLIGKNNSGKSSILEALDIFLNNKEKFFEDDFLVLYLKdvikIDKEDLNIFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 77 VIGAKKD-----QYFLDKKMVTKNDVMNLLESAGFSRsnPYYIVKQGKINQMatAPDSQRLKLLREVAGTRVYDERKEES 151
Cdd:pfam13175 79 NISFSIDieidvEFLLILFGYLEIKKKYLCLASKGKA--KEYEKTLHPKGAN--KADLLLELKISDLKKYLKQFKIYIYN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 152 ISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQE--LNETRAKLDELSAKRETSGEKS 229
Cdd:pfam13175 155 NYYLDEKKNVFDKKSKYELPSLKEEFLNSEKEEIKVDKEDLKKLINELEKSINYHEnvLENLQIKKLLISADRNASDEDS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 230 RQLRDA-----QQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKlelkaKDLQDELAGNSEQRKRLLK 304
Cdd:pfam13175 235 EKINSLlgalkQRIFEEALQEELELTEKLKETQNKLKEIDKTLAEELKNILFKKID-----KLKDFGYPPFLNPEIEIKK 309
|
....*...
gi 1958644837 305 ERQKLLEK 312
Cdd:pfam13175 310 DDEDLPLN 317
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
142-445 |
1.25e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 142 RVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKE----------ELAQYQKWDKMRRaleytiYNQELNET 211
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrELTEEHRKELLEE------YTAELKRI 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 212 RAKLDELSAKRETSGEKSRQLRDAQQDARD--KMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRT-KLELKAKDL 288
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiKLKGEIKSL 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 289 QDELagnsEQRKRLLKERQKLLEKIEEKQKELAETEPK-----FNSVKEKEERgIARLAQATQERTDLyakQGRGSQFTS 363
Cdd:PRK03918 545 KKEL----EKLEELKKKLAELEKKLDELEEELAELLKEleelgFESVEELEER-LKELEPFYNEYLEL---KDAEKELER 616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 364 KEERDKWIKKELKSLDQAINDKKRQIAAIHKDLED-----TEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKK 438
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELAETEKRLEELRKELEElekkySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTL 696
|
....*..
gi 1958644837 439 DELQSER 445
Cdd:PRK03918 697 EKLKEEL 703
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
203-473 |
2.31e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 58.59 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 203 IYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLE 282
Cdd:pfam15921 304 IQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 283 LKAKDLQDELAGNSEQRKRLLKER-------QKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAK- 354
Cdd:pfam15921 384 ADLHKREKELSLEKEQNKRLWDRDtgnsitiDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKv 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 355 QGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAaihkDLEDTEANKEKNLEQYNkldQDLNEVKARVEELDRKYYEV 434
Cdd:pfam15921 464 SSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVS----DLTASLQEKERAIEATN---AEITKLRSRVDLKLQELQHL 536
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958644837 435 KNKKDEL---QSERNYLWREENAEQQALAAKREDLEKKQQLL 473
Cdd:pfam15921 537 KNEGDHLrnvQTECEALKLQMAEKDKVIEILRQQIENMTQLV 578
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-78 |
2.47e-08 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 56.54 E-value: 2.47e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644837 1 MYIKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHIDKEEVSLRRVI 78
Cdd:COG3950 1 MRIKSLTIENFRGFEDLEIDFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNGEFGDSAKLI 78
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
237-496 |
3.02e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 237 QDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKL---------ELKAKDLQDELAGNSEQRKRLLK--- 304
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdEIDVASAEREIAELEAELERLDAssd 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 305 ERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEER---DKWIKKELksLDQA 381
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRallEERFAAAL--GDAV 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 382 INDKKRQIAAIHKDLEDTEANKEKNLEqyNKLDQDLNEVKARVEELDrkyyevknkkDELQSERNYLWREENAEQQALAA 461
Cdd:COG4913 764 ERELRENLEERIDALRARLNRAEEELE--RAMRAFNREWPAETADLD----------ADLESLPEYLALLDRLEEDGLPE 831
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1958644837 462 KREDLekKQQLLRAATG-------------KAILNGIDSINKVLDHFR 496
Cdd:COG4913 832 YEERF--KELLNENSIEfvadllsklrraiREIKERIDPLNDSLKRIP 877
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
156-363 |
3.38e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.15 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 156 KETEGKREKINELLKYIEERLHTLEEEKEELAQyqKWDKMRRALEYTiyNQELNETRAKLDELSAKRETSGEK-SRQLRD 234
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNE--EYNELQAELEAL--QAEIDKLQAEIAEAEAEIEERREElGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 235 AQQ------------------DARDKMEDIER-------QVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQ 289
Cdd:COG3883 95 LYRsggsvsyldvllgsesfsDFLDRLSALSKiadadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958644837 290 DELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTS 363
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
162-432 |
4.41e-08 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 57.63 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 162 REKINELLKYIEER--LHtLEEEKEELAQyqkwDKMRRALEYTIynqELNETRAKLDELSAKRETSGE-----KSRQLRD 234
Cdd:PRK05771 15 KSYKDEVLEALHELgvVH-IEDLKEELSN----ERLRKLRSLLT---KLSEALDKLRSYLPKLNPLREekkkvSVKSLEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 235 AQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERqEQIKQRTKLELKAKDLQDElaGNSEQRKRLLKERQKLLEKIE 314
Cdd:PRK05771 87 LIKDVEEELEKIEKEIKELEEEISELENEIKELEQEI-ERLEPWGNFDLDLSLLLGF--KYVSVFVGTVPEDKLEELKLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 315 EKQKELAETEPKFNSV-------KEKEERGIARLAQATQERTDLYAKQgrgsqfTSKEERDKwIKKELKSLDQAINDKKR 387
Cdd:PRK05771 164 SDVENVEYISTDKGYVyvvvvvlKELSDEVEEELKKLGFERLELEEEG------TPSELIRE-IKEELEEIEKERESLLE 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1958644837 388 QIAAIHKDLEDTEankeknLEQYNKLDQDLNEVKARVEELDRKYY 432
Cdd:PRK05771 237 ELKELAKKYLEEL------LALYEYLEIELERAEALSKFLKTDKT 275
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-57 |
5.36e-08 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 56.32 E-value: 5.36e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644837 1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFvlsdeFSHLR 57
Cdd:PRK00064 1 MYLTRLSLTDFRNYEELDL--ELSPGVNVLVGENGQGKTNLLEAIYL-----LAPGR 50
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
126-426 |
6.27e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 6.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 126 APDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEytiyn 205
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE----- 1657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 206 qelnETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQ------VRELKTKISAMKEEKEQLSAERQE---QIK 276
Cdd:PTZ00121 1658 ----ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEaeeakkAEELKKKEAEEKKKAEELKKAEEEnkiKAE 1733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 277 QRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKfnSVKEKEERGIARLAQATQERTDLYA--- 353
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE--ELDEEDEKRRMEVDKKIKDIFDNFAnii 1811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 354 ---KQGRGSQFTSKEERDKWIKKELKSLDQAIND----KKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEE 426
Cdd:PTZ00121 1812 eggKEGNLVINDSKEMEDSAIKEVADSKNMQLEEadafEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIE 1891
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
206-347 |
7.54e-08 |
|
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: 54.55 E-value: 7.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 206 QELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKIsamkEEKEQLSAERQEQIKQ-RTKLELK 284
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI----EEVEARIKKYEEQLGNvRNNKEYE 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958644837 285 AkdLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQE 347
Cdd:COG1579 93 A--LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-448 |
9.14e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.45 E-value: 9.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1 MYIKQVIIQGFRSYRDQTIVdpFSSKHNVIVGRNGSGKSNFFYAIQFVLsdeFSHLRPEQRLALLHIDKE--EVSLRRVI 78
Cdd:PRK01156 1 MIIKRIRLKNFLSHDDSEIE--FDTGINIITGKNGAGKSSIVDAIRFAL---FTDKRTEKIEDMIKKGKNnlEVELEFRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 79 GAKKDQYFLDKKMVTKN-------DVMNLLESAGFSRSNPY----------------YIVKQGKINQMATAPDSQRLKLL 135
Cdd:PRK01156 76 GGHVYQIRRSIERRGKGsrreayiKKDGSIIAEGFDDTTKYieknilgiskdvflnsIFVGQGEMDSLISGDPAQRKKIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 136 REVAG----TRVYDERKEESISLMKETEGKREKINELLKYIEErlhtLEEEKEELAQYQKW------DKMRRALEYTIYN 205
Cdd:PRK01156 156 DEILEinslERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLE----LENIKKQIADDEKShsitlkEIERLSIEYNNAM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 206 QELNETRAKLDELSAKRETSGEKSRQLRDAQQDardkMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLElka 285
Cdd:PRK01156 232 DDYNNLKSALNELSSLEDMKNRYESEIKTAESD----LSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYK--- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 286 kdlqdelaGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEErgiaRLAQATQERTDLYAKQGR-GSQFTSK 364
Cdd:PRK01156 305 --------NDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKS----RYDDLNNQILELEGYEMDyNSYLKSI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 365 EERDKWIKKELKsldqainDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSE 444
Cdd:PRK01156 373 ESLKKKIEEYSK-------NIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRN 445
|
....
gi 1958644837 445 RNYL 448
Cdd:PRK01156 446 MEML 449
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-191 |
1.01e-07 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 53.27 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 6 VIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHIDKEEVSlrrvIGAKKDQY 85
Cdd:pfam13476 1 LTIENFRSFRDQTI--DFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDIRIGL----EGKGKAYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 86 FLDKKMVTKNDVMNLLESAGFSRSNP-YYIVKQGKINQMATAPD--SQRLKLLREVAGTRVYDERKEESISLMKETEGKR 162
Cdd:pfam13476 75 EITFENNDGRYTYAIERSRELSKKKGkTKKKEILEILEIDELQQfiSELLKSDKIILPLLVFLGQEREEEFERKEKKERL 154
|
170 180
....*....|....*....|....*....
gi 1958644837 163 EKINELLKYIEERLHTLEEEKEELAQYQK 191
Cdd:pfam13476 155 EELEKALEEKEDEKKLLEKLLQLKEKKKE 183
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
162-350 |
1.20e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 162 REKInELLKYIEERLHTLEEEKEELAQyqkWDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARD 241
Cdd:COG4913 248 REQI-ELLEPIRELAERYAAARERLAE---LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALRE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 242 KMEDIERQVR--------ELKTKISAMKEEKEQLSAERQEQIKQRTKLELKA------------------KDLQDELAGN 295
Cdd:COG4913 324 ELDELEAQIRgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLpasaeefaalraeaaallEALEEELEAL 403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958644837 296 SEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTD 350
Cdd:COG4913 404 EEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEA 458
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
162-435 |
1.52e-07 |
|
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: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 162 REKINEL---LKYIEERLHTLEEEKEEL-AQYQKWDKMRRAL----EYTIYNQELNETRAKLDELSAKR---ETSGEKSR 230
Cdd:COG4913 609 RAKLAALeaeLAELEEELAEAEERLEALeAELDALQERREALqrlaEYSWDEIDVASAEREIAELEAELerlDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 231 QLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQE---------QIKQRTKLELKAKDLQDELAGNSEQ--R 299
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDElqdrleaaeDLARLELRALLEERFAAALGDAVERelR 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 300 KRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERG-----------IARLAQatQERTDLYAKQGR-GSQFTSKEER 367
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAMRAFNREWPAETADldadleslpeyLALLDR--LEEDGLPEYEERfKELLNENSIE 846
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644837 368 DkwiKKELKS-LDQAINDKKRQIAAIHKDLEDTEANKEKNL---------EQYNKLDQDLNEVKARVEELDRKYYEVK 435
Cdd:COG4913 847 F---VADLLSkLRRAIREIKERIDPLNDSLKRIPFGPGRYLrlearprpdPEVREFRQELRAVTSGASLFDEELSEAR 921
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
146-437 |
2.06e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 54.15 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 146 ERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQyqkwdkMRRALeytiyNQELNETRAKLDELSAKRETS 225
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAE------KRDEL-----NAQVKELREEAQELREKRDEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 226 GEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDE--LAGNSEQRKRLL 303
Cdd:COG1340 70 NEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEkeLVEKIKELEKEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 304 KERQKLLEKIEEKQKELAETEPKFNSVKEKEERgIARLAQATQERTDLYAKQgrgsqftsKEERDKwIKKELKSLDQAIN 383
Cdd:COG1340 150 EKAKKALEKNEKLKELRAELKELRKEAEEIHKK-IKELAEEAQELHEEMIEL--------YKEADE-LRKEADELHKEIV 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644837 384 DKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVK--ARVEELDRKYYEVKNK 437
Cdd:COG1340 220 EAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKreKEKEELEEKAEEIFEK 275
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
3-190 |
2.68e-07 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 53.89 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 3 IKQVIIQGFRSYRDQTIVDPFSSKH-----NVIVGRNGSGKSNFFYAIQF----VLSDEFSHLRPEQRLALLHIDKEEVS 73
Cdd:COG1106 2 LISFSIENFRSFKDELTLSMVASGLrllrvNLIYGANASGKSNLLEALYFlrnlVLNSSQPGDKLVEPFLLDSESKNEPS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 74 LRRVIgakkdqyFLDKKMVTkndvmnlleSAGFSRSNP-------YYIVKQGKINQMATAPDSQRLKllREVagtrVYDE 146
Cdd:COG1106 82 EFEIL-------FLLDGVRY---------EYGFELDKEriisewlYFLSTAAQLNVPLLSPLYDWFD--NNI----SLDT 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958644837 147 RKEESISLMKETEGKREKINELLKYIE---ERLHTLEEEKEELAQYQ 190
Cdd:COG1106 140 SSDGLTLLLKEDESLKEELLELLKIADpgiEDIEVEEEEIEDLVERK 186
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
159-351 |
3.76e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 159 EGKREKINELLKYIEERLHTLEEEKEE----LAQY-QKWDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLR 233
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEaeaaLEEFrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 234 DAQQDARDKMEDIERQVRelktkISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAgnsEQRKRLLKERQKLLEKI 313
Cdd:COG3206 247 AQLGSGPDALPELLQSPV-----IQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIA---ALRAQLQQEAQRILASL 318
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958644837 314 EEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDL 351
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRL 356
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
263-480 |
3.86e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 263 EKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEpkfNSVKEKEERgIARLA 342
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREE-LGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 343 QATQER----------------TDLYAKQGRGSQFTskeERDKWIKKELKSLDQAINDKKRQIAaihKDLEDTEANKEKN 406
Cdd:COG3883 93 RALYRSggsvsyldvllgsesfSDFLDRLSALSKIA---DADADLLEELKADKAELEAKKAELE---AKLAELEALKAEL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958644837 407 LEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQLLRAATGKA 480
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
8-500 |
4.70e-07 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 53.97 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 8 IQGFRSYRDQTIVDPFSSKhNVIVGRNGSGK---SNFFYAIQ-------FVLSDEFSHLRPEQRLALLHIDKEEVS-LRR 76
Cdd:COG4694 8 LKNVGAFKDFGWLAFFKKL-NLIYGENGSGKstlSRILRSLElgdtsseVIAEFEIEAGGSAPNPSVRVFNRDFVEeNLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 77 VIGAKKDQYFLDKKMVtknDVMNLLESAGFSRSNpyYIVKQGKINQMATAPDSQRLKLLREVAGTRVyderkeESISLMK 156
Cdd:COG4694 87 SGEEIKGIFTLGEENI---ELEEEIEELEKEIED--LKKELDKLEKELKEAKKALEKLLEDLAKSIK------DDLKKLF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 157 ETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKsrQLRDAQ 236
Cdd:COG4694 156 ASSGRNYRKANLEKKLSALKSSSEDELKEKLKLLKEEEPEPIAPITPLPDLKALLSEAETLLEKSAVSSAIE--ELAALI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 237 QDardkmEDIERQVRELKTKISAMKEEK----EQ-LSAERQEQIKQRtklelkakdLQDELAGNSEQRKRLLKERQKLLE 311
Cdd:COG4694 234 QN-----PGNSDWVEQGLAYHKEEEDDTcpfcQQeLAAERIEALEAY---------FDDEYEKLLAALKDLLEELESAIN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 312 KIEEkqKELAETEPKFNSVKEKEERGIARLAQATQE-RTDLYAKQGRGSQFTSKEERDKW--IKKELKSLDQAINDKKRQ 388
Cdd:COG4694 300 ALSA--LLLEILRTLLPSAKEDLKAALEALNALLETlLAALEEKIANPSTSIDLDDQELLdeLNDLIAALNALIEEHNAK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 389 IAaihkDLEDTEANKEKNLEQY--NKLDQDLNEVKARVEELDRKYYEVKNKKDELQSernylwreenaeqqaLAAKREDL 466
Cdd:COG4694 378 IA----NLKAEKEEARKKLEAHelAELKEDLSRYKAEVEELIEELKTIKALKKALED---------------LKTEISEL 438
|
490 500 510
....*....|....*....|....*....|....
gi 1958644837 467 EKKQqllraatgKAILNGIDSINKVLDHFRRKGI 500
Cdd:COG4694 439 EAEL--------SSVDEAADEINEELKALGFDEF 464
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
145-440 |
5.33e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 145 DERKEESISLMKETEGKREKINELLKYiEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELsakrET 224
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKKESELIKL-KELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSL----KK 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 225 SGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLK 304
Cdd:PRK03918 547 ELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEE 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 305 ERQKLLEKIEEKQKELAETEPKFNSVKEKeergiarlaqATQERtdlyakqgrgsqFTSKEERDKWIKKELKSLDQAIND 384
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKK----------YSEEE------------YEELREEYLELSRELAGLRAELEE 684
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644837 385 KKRQIAAIHKDLEDTEANKEKnLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDE 440
Cdd:PRK03918 685 LEKRREEIKKTLEKLKEELEE-REKAKKELEKLEKALERVEELREKVKKYKALLKE 739
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
146-429 |
5.37e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 146 ERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAqyqkwdkmrraleytiynqelnETRAKLDELSAKRETS 225
Cdd:PRK02224 499 ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAE----------------------ELRERAAELEAEAEEK 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 226 GEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLsAERQEQIKQRTKLELKAKDLQDElagNSEQRKRL--L 303
Cdd:PRK02224 557 REAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLL-AAIADAEDEIERLREKREALAEL---NDERRERLaeK 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 304 KERQKLLE------KIEEKQKELAETEPKFNSVKEKeergiarLAQATQERTDLYAKQGRgsqftskeerdkwIKKELKS 377
Cdd:PRK02224 633 RERKRELEaefdeaRIEEAREDKERAEEYLEQVEEK-------LDELREERDDLQAEIGA-------------VENELEE 692
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1958644837 378 LDqAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNevKARVEELDR 429
Cdd:PRK02224 693 LE-ELRERREALENRVEALEALYDEAEELESMYGDLRAELR--QRNVETLER 741
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
119-481 |
5.87e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 5.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 119 KINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRA 198
Cdd:PTZ00121 1213 KAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 199 LEYtiynqELNETRAKLDELSAKRETSgEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQR 278
Cdd:PTZ00121 1293 DEA-----KKAEEKKKADEAKKKAEEA-KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 279 TKLELK---AKDLQDELAGNSEQRKR---LLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLY 352
Cdd:PTZ00121 1367 EAAEKKkeeAKKKADAAKKKAEEKKKadeAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA 1446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 353 AKQGRGSQFTSKEERDKWIKKELKSLDQ-----------------AINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQ 415
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEakkkaeeakkadeakkkAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644837 416 DLNEVKARVEELDRKYYEVKnKKDELQSERNYLWREEnaEQQALAAKREDLEKKQQLLRAATGKAI 481
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKK-KADELKKAEELKKAEE--KKKAEEAKKAEEDKNMALRKAEEAKKA 1589
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
142-433 |
7.32e-07 |
|
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: 53.69 E-value: 7.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 142 RVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETR-AKLDELSA 220
Cdd:pfam12128 657 RLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALdAQLALLKA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 221 KREtsgeKSRQLRDAQQDA---------------RDKMEDIERQVRELKTKISAMKEEK-----------EQLSAERQEQ 274
Cdd:pfam12128 737 AIA----ARRSGAKAELKAletwykrdlaslgvdPDVIAKLKREIRTLERKIERIAVRRqevlryfdwyqETWLQRRPRL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 275 IKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSvkekEERGIARL---AQATQERTDL 351
Cdd:pfam12128 813 ATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRC----EMSKLATLkedANSEQAQGSI 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 352 YAKQGRGSQFTSKEERDKW-IKKELKSLDQAINDKKRQIAAIH----KDLEDTEANKEKNLEQYNKLDQDLNEV-KARVE 425
Cdd:pfam12128 889 GERLAQLEDLKLKRDYLSEsVKKYVEHFKNVIADHSGSGLAETweslREEDHYQNDKGIRLLDYRKLVPYLEQWfDVRVP 968
|
....*...
gi 1958644837 426 ELDRKYYE 433
Cdd:pfam12128 969 QSIMVLRE 976
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
148-474 |
7.79e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 53.64 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 148 KEESISLMKEtegKREKINELLKYIEERLHTLEEEKEELAQ--------YQKWDKMRRALEYTiyNQELNETrakLDELS 219
Cdd:pfam01576 10 KEEELQKVKE---RQQKAESELKELEKKHQQLCEEKNALQEqlqaetelCAEAEEMRARLAAR--KQELEEI---LHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 220 AKRETSGEKSRQLRDAQQDARDKMEDIERQVRElktkisamkEEkeqlsAERQEQIKQRTKLELKAKDLQDELAGNSEQR 299
Cdd:pfam01576 82 SRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE---------EE-----AARQKLQLEKVTTEAKIKKLEEDILLLEDQN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 300 KRLLKERQKLLEKIEEKQKELAETEPK---FNSVKEKEERGIA----RLAQATQERTDLyAKQGRGSQFTSKEERDkwik 372
Cdd:pfam01576 148 SKLSKERKLLEERISEFTSNLAEEEEKaksLSKLKNKHEAMISdleeRLKKEEKGRQEL-EKAKRKLEGESTDLQE---- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 373 kELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELdrkyyevknkKDELQSERNYlwrEE 452
Cdd:pfam01576 223 -QIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISEL----------QEDLESERAA---RN 288
|
330 340
....*....|....*....|..
gi 1958644837 453 NAEQQalaakREDLEKKQQLLR 474
Cdd:pfam01576 289 KAEKQ-----RRDLGEELEALK 305
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
119-470 |
1.18e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 119 KINQMATAPDSQRLKLLREVAGTRVYDE-RKEESISLMKETEGKRE--------KINELLKYIEERLHTLEEEKEELAQY 189
Cdd:PTZ00121 1141 KAEEARKAEDAKRVEIARKAEDARKAEEaRKAEDAKKAEAARKAEEvrkaeelrKAEDARKAEAARKAEEERKAEEARKA 1220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 190 Q---KWDKMRRALEytiynqelnetrAKLDELSAKRetsGEKSRQLRDAQQDARDKMEDIERqvRELKTKISAMKEEKEQ 266
Cdd:PTZ00121 1221 EdakKAEAVKKAEE------------AKKDAEEAKK---AEEERNNEEIRKFEEARMAHFAR--RQAAIKAEEARKADEL 1283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 267 LSAERQEQIKQRTKLELKAKdlQDELAGNSEQRKRL--LKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQA 344
Cdd:PTZ00121 1284 KKAEEKKKADEAKKAEEKKK--ADEAKKKAEEAKKAdeAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 345 TQERTDlyAKQGRGSQFTSKEERDKWIKKELKSLDQAiNDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQdlnevKARV 424
Cdd:PTZ00121 1362 AEEKAE--AAEKKKEEAKKKADAAKKKAEEKKKADEA-KKKAEEDKKKADELKKAAAAKKKADEAKKKAEE-----KKKA 1433
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958644837 425 EELDRKYYEvKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQ 470
Cdd:PTZ00121 1434 DEAKKKAEE-AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK 1478
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
122-388 |
1.33e-06 |
|
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: 52.82 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 122 QMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKRE--KINELlkyieerlhtleeEKEELAQYQKWDKMRRAL 199
Cdd:pfam17380 332 QAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEisRMREL-------------ERLQMERQQKNERVRQEL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 200 EYTIYNQELNETRAKldelsaKRETSGEKSRQLRDAQQDARdkmediERQVRELKTKISAMKEEKEQLSAERQEQIKQRT 279
Cdd:pfam17380 399 EAARKVKILEEERQR------KIQQQKVEMEQIRAEQEEAR------QREVRRLEEERAREMERVRLEEQERQQQVERLR 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 280 KLELKAKDLQDELAGNSEQRKRLLKERQKLLEK---------IEEKQKEL---AETEPKFNSVKEKEERGIA----RLAQ 343
Cdd:pfam17380 467 QQEEERKRKKLELEKEKRDRKRAEEQRRKILEKeleerkqamIEEERKRKlleKEMEERQKAIYEEERRREAeeerRKQQ 546
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1958644837 344 ATQERTDLyakQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQ 388
Cdd:pfam17380 547 EMEERRRI---QEQMRKATEERSRLEAMEREREMMRQIVESEKAR 588
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
155-333 |
1.37e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 155 MKETEGKREKINELLKYIEERLHTLEEEKEEL-AQYQKWDKMRRALEYTIY-------------NQELNETRAKLDELSA 220
Cdd:COG4942 64 IAALARRIRALEQELAALEAELAELEKEIAELrAELEAQKEELAELLRALYrlgrqpplalllsPEDFLDAVRRLQYLKY 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 221 KRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRK 300
Cdd:COG4942 144 LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
170 180 190
....*....|....*....|....*....|...
gi 1958644837 301 RLlkerQKLLEKIEEKQKELAETEPKFNSVKEK 333
Cdd:COG4942 224 EL----EALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
265-486 |
1.40e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 265 EQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERgIARLAQA 344
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK-LEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 345 TQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANK-EKNLEQYNKLDQDLNEVKAR 423
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958644837 424 VEELDRKYYEVKNKKDELQSErnylwREENAEQQALAAKREDLEKKQQLLRAATGKAILNGID 486
Cdd:COG4717 208 LAELEEELEEAQEELEELEEE-----LEQLENELEAAALEERLKEARLLLLIAAALLALLGLG 265
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
2-47 |
1.52e-06 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 51.69 E-value: 1.52e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1958644837 2 YIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQF 47
Cdd:COG1195 1 RLKRLSLTNFRNYESLEL--EFSPGINVLVGPNGQGKTNLLEAIYL 44
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
157-319 |
1.62e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 52.26 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 157 ETEGKREKINELLKYIEERLHTLEEEKEELAQYQKwdkmRRALEYTIYNQELNETRAKLDELSAKRetsgekSRQLRDAQ 236
Cdd:pfam15709 349 EVERKRREQEEQRRLQQEQLERAEKMREELELEQQ----RRFEEIRLRKQRLEEERQRQEEEERKQ------RLQLQAAQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 237 QDARDKMEDIERQVRELKTKisamkeeKEQLSAERQEQIKQRTK-LELKAKDLQDELAGNSE------QRKRLLKERQKL 309
Cdd:pfam15709 419 ERARQQQEEFRRKLQELQRK-------KQQEEAERAEAEKQRQKeLEMQLAEEQKRLMEMAEeerleyQRQKQEAEEKAR 491
|
170
....*....|
gi 1958644837 310 LEKIEEKQKE 319
Cdd:pfam15709 492 LEAEERRQKE 501
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
243-335 |
1.63e-06 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 52.39 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 243 MEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRtklELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAE 322
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASFERLAELRDE---LAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPE 489
|
90
....*....|...
gi 1958644837 323 TEPKFNSVKEKEE 335
Cdd:COG0542 490 LEKELAELEEELA 502
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-58 |
2.84e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.53 E-value: 2.84e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644837 3 IKQVIIQGFRSYRDQTIVDpFSSKHNVIVGRNGSGKSNFFYAIQFVLsdeFSHLRP 58
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIE-FFSPLTLIVGQNGAGKTTIIEALKYAL---TGELPP 52
|
|
| recN |
TIGR00634 |
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ... |
771-1189 |
3.36e-06 |
|
DNA repair protein RecN; All proteins in this family for which functions are known are ATP binding proteins involved in the initiation of recombination and recombinational repair. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273187 [Multi-domain] Cd Length: 563 Bit Score: 51.27 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 771 KRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNEnlrkrLDQVEQELNELRETEGGTVLTattSELEAINKRVK 850
Cdd:TIGR00634 161 KAYRELYQAWLKARQQLKDRQQKEQELAQRLDFLQFQLEE-----LEEADLQPGEDEALEAEQQRL---SNLEKLRELSQ 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 851 DTMAR-SEDLDNSIDKTEAGIKELQKSMErwknmekehmdaiNHDTKELEKMTNRQGMLLKKKEECMKKIRELGS----L 925
Cdd:TIGR00634 233 NALAAlRGDVDVQEGSLLEGLGEAQLALA-------------SVIDGSLRELAEQVGNALTEVEEATRELQNYLDelefD 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 926 PQEAFEKYQTLS-LKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGYksIMELMNVLELRKYEA 1004
Cdd:TIGR00634 300 PERLNEIEERLAqIKRLKRKYGASVEEVLEYAEKIKEELDQLDDSDESLEALEEEVDKLEEEL--DKAAVALSLIRRKAA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1005 iqltfKQVSKNFSEVFQKLvpggkaTLVMKKGDVEGSQSQDEGEGSGESERGsgsqssvpsVDQftgvgIRVSFTGKQGE 1084
Cdd:TIGR00634 378 -----ERLAKRVEQELKAL------AMEKAEFTVEIKTSLPSGAKARAGAYG---------ADQ-----VEFLFSANTGE 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1085 mrEMQQL----SGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESAD 1160
Cdd:TIGR00634 433 --PVKPLakvaSGGELSRVMLALKVVLSSSAAVTTLIFDEVDVGVSGETAQAIAKKLAQLSERHQVLCVTHLPQVAAHAD 510
|
410 420
....*....|....*....|....*....
gi 1958644837 1161 KFYGVKfrnKVShIDVITAEMAKDFVEDD 1189
Cdd:TIGR00634 511 AHFKVE---KEG-LDGRTATRVRPLSGEE 535
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
144-465 |
3.44e-06 |
|
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: 51.49 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 144 YDERKEESISLMKETEGKREKINELLKYIEERLHTLEEE----KEELAQYQKWDKM--RRALEYTIYNQELNETRA--KL 215
Cdd:COG3096 352 YQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEvdslKSQLADYQQALDVqqTRAIQYQQAVQALEKARAlcGL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 216 DELSAKretsgeksrQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSA------------ERQEQIKQRTKLEL 283
Cdd:COG3096 432 PDLTPE---------NAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKayelvckiagevERSQAWQTARELLR 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 284 KAKDLQdELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGrgsqfTS 363
Cdd:COG3096 503 RYRSQQ-ALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAA-----EA 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 364 KEERdkwikKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQS 443
Cdd:COG3096 577 VEQR-----SELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAA 651
|
330 340
....*....|....*....|..
gi 1958644837 444 ERNYLwrEENAEQQALAAKRED 465
Cdd:COG3096 652 RKQAL--ESQIERLSQPGGAED 671
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
221-470 |
5.32e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.52 E-value: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 221 KRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRK 300
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 301 RLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERgIARLAQATQ-------ERTDLYAKQGRGSQFTSKEERDKWIKK 373
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGGSIDKLRKE-IERLEWRQQtevlspeEEKELVEKIKELEKELEKAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 374 ELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREEN 453
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
250
....*....|....*..
gi 1958644837 454 AEQQALAAKREDLEKKQ 470
Cdd:COG1340 241 ELRKELKKLRKKQRALK 257
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
207-423 |
5.39e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 207 ELNETRAKLDELSAKRETSGEksrQLRDAQQDARDKMEDIER---QVRELKTKISAMKEE---KEQLSAERQEQIKQR-- 278
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQA---ELDALQAELEELNEEYNElqaELEALQAEIDKLQAEiaeAEAEIEERREELGERar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 279 ---------TKLE--LKAKDLQDeLAGNSEQRKRLLKERQKLLEKIEEKQKELAETEpkfNSVKEKEERGIARLAQATQE 347
Cdd:COG3883 94 alyrsggsvSYLDvlLGSESFSD-FLDRLSALSKIADADADLLEELKADKAELEAKK---AELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644837 348 RTDLYAKQgrgsqfTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKAR 423
Cdd:COG3883 170 KAELEAQQ------AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
675-1005 |
5.74e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 675 NLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEktfmpkqRSLQSLEASLHAMESTRE--- 751
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELR-------EELEKLEKEVKELEELKEeie 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 752 SLKAELGTDLLSQLSLEDQKRvdALNDEIRQLQQENRQLLNERIKLEGIITRVETYlnENLRKRLDQVEQELNELRETEG 831
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIR--ELEERIEELKKEIEELEEKVKELKELKEKAEEY--IKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 832 G-----TVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRqg 906
Cdd:PRK03918 318 RleeeiNGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEE-- 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 907 mLLKKKEECMKKIREL----GSLPQEAFEKYQTLS-LKQLFRKLEQCNTEL---------KKYSHVNKKALDQFVNFSEQ 972
Cdd:PRK03918 396 -LEKAKEEIEEEISKItariGELKKEIKELKKAIEeLKKAKGKCPVCGRELteehrkellEEYTAELKRIEKELKEIEEK 474
|
330 340 350
....*....|....*....|....*....|...
gi 1958644837 973 KEKLIKRQEELDrgyksiMELMNVLELRKYEAI 1005
Cdd:PRK03918 475 ERKLRKELRELE------KVLKKESELIKLKEL 501
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
645-963 |
7.01e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.43 E-value: 7.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 645 YDTRKSRLELQKDVRKAEEELGELEAKLNENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQ 724
Cdd:TIGR00606 205 HQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKD 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 725 SEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLsqlslEDQKRVDALNDEIRQLQQENRQLLNERIKL------- 797
Cdd:TIGR00606 285 NSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELV-----DCQRELEKLNKERRLLNQEKTELLVEQGRLqlqadrh 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 798 -EGIITRVETYLNENLRKRLDQVEQELNELRETEGGTVLTATTSELEA--INKRVKDTMARSEDLDNSIDKTEAGIKELQ 874
Cdd:TIGR00606 360 qEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAktAAQLCADLQSKERLKQEQADEIRDEKKGLG 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 875 KSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEA----------FEKYQTLSLKQLFRK 944
Cdd:TIGR00606 440 RTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSltetlkkevkSLQNEKADLDRKLRK 519
|
330
....*....|....*....
gi 1958644837 945 LEQCNTELKKYSHVNKKAL 963
Cdd:TIGR00606 520 LDQEMEQLNHHTTTRTQME 538
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
119-446 |
8.02e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 8.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 119 KINQMATAPDSQRLKLLREVAGTRVYDE-RKEESISLMKETEGKREKINEllkyiEERLHTLEEEKEELAQYQKwdkmRR 197
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADElKKAEELKKAEEKKKAEEAKKA-----EEDKNMALRKAEEAKKAEE----AR 1593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 198 ALEYTIYNQELNETRAkldELSAKRETSGEKSRQLRDAQQDaRDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQ 277
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKA---EEAKKAEEAKIKAEELKKAEEE-KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 278 RTKLELKAKDLQDELAGNSEQRKRLLKERQKLlEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQErtdlyakqgr 357
Cdd:PTZ00121 1670 AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE---------- 1738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 358 gsqftskEERDKWIKKELKSLDQaindKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVeELDRKYYEVKNK 437
Cdd:PTZ00121 1739 -------AEEDKKKAEEAKKDEE----EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRM-EVDKKIKDIFDN 1806
|
....*....
gi 1958644837 438 KDELQSERN 446
Cdd:PTZ00121 1807 FANIIEGGK 1815
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
154-468 |
8.35e-06 |
|
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: 50.02 E-value: 8.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 154 LMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKwDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLR 233
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK-ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 234 DAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKI 313
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 314 EEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLyakqgrGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIH 393
Cdd:TIGR04523 471 KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEL------EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE 544
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644837 394 KDLE--DTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEK 468
Cdd:TIGR04523 545 DELNkdDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
206-480 |
9.07e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.12 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 206 QELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTkisAMKEEKEQLSAERQEQIKQRTKLELKA 285
Cdd:pfam15921 454 QGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTA---SLQEKERAIEATNAEITKLRSRVDLKL 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 286 KDLQdELAGNSEQRKRLLKERQKLLEKIEEKQKElaetepkfnsvkekeergIARLAQATQERTDLYAKQGR--GSQFTS 363
Cdd:pfam15921 531 QELQ-HLKNEGDHLRNVQTECEALKLQMAEKDKV------------------IEILRQQIENMTQLVGQHGRtaGAMQVE 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 364 KEERDKWIK------KELKSLDQAINDKKRQIAAIHKDLE------------------DTEANKEKNLEQYNKLDQDLNE 419
Cdd:pfam15921 592 KAQLEKEINdrrlelQEFKILKDKKDAKIRELEARVSDLElekvklvnagserlravkDIKQERDQLLNEVKTSRNELNS 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 420 VKARVEELDRKY---------------YEVKNKKDELQSERNYLWREENAE----------QQALAAKR---EDLEKKQQ 471
Cdd:pfam15921 672 LSEDYEVLKRNFrnkseemetttnklkMQLKSAQSELEQTRNTLKSMEGSDghamkvamgmQKQITAKRgqiDALQSKIQ 751
|
....*....
gi 1958644837 472 LLRAATGKA 480
Cdd:pfam15921 752 FLEEAMTNA 760
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
157-326 |
9.27e-06 |
|
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: 48.38 E-value: 9.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 157 ETEGKREKINELLKYIEERLHTLEEEKEELAQyqkwdkmrralEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQ 236
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEA-----------RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 237 QDARD--KMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIE 314
Cdd:COG1579 83 GNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|..
gi 1958644837 315 EKQKELAETEPK 326
Cdd:COG1579 163 AEREELAAKIPP 174
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1080-1161 |
1.23e-05 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 49.21 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1080 GKQGEMremqqLSGGQKSLVALALIFaiqkCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESA 1159
Cdd:TIGR02857 453 GEGGAG-----LSGGQAQRLALARAF----LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALA 523
|
..
gi 1958644837 1160 DK 1161
Cdd:TIGR02857 524 DR 525
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
1076-1141 |
1.57e-05 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 47.21 E-value: 1.57e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958644837 1076 VSFtgKQGEmrEMQQL-----SGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELA 1141
Cdd:cd03277 111 VKF--REGE--QLQELdphhqSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVETA 177
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
147-475 |
2.04e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 147 RKEESISLMKETEGKREKINELLKYIEERLHTLEEEK---EELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRE 223
Cdd:PRK01156 347 RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSkniERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVS 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 224 TSGEKSRQLRDAQQDARDKM------------------EDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKA 285
Cdd:PRK01156 427 SLNQRIRALRENLDELSRNMemlngqsvcpvcgttlgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRK 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 286 KDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEK---------EERGIARL-AQATQERTDLYAKQ 355
Cdd:PRK01156 507 EYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRykslkledlDSKRTSWLnALAVISLIDIETNR 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 356 GRGSQFTSK----EER---------------DKWIKK---ELKSLDQAIN---DKKRQIAAIHKDLEDTE---ANKEKNL 407
Cdd:PRK01156 587 SRSNEIKKQlndlESRlqeieigfpddksyiDKSIREienEANNLNNKYNeiqENKILIEKLRGKIDNYKkqiAEIDSII 666
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644837 408 EQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQLLRA 475
Cdd:PRK01156 667 PDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKA 734
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1081-1166 |
2.22e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.83 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1081 KQGE-----MREMQQLSGGQKSLVALALIFAIQK--CDPAPFYLFDEIDQALDAQHRKAVSDMIMELA---VHAQFITTT 1150
Cdd:cd03240 101 HQGEsnwplLDMRGRCSGGEKVLASLIIRLALAEtfGSNCGILALDEPTTNLDEENIEESLAEIIEERksqKNFQLIVIT 180
|
90
....*....|....*.
gi 1958644837 1151 FRPELLESADKFYGVK 1166
Cdd:cd03240 181 HDEELVDAADHIYRVE 196
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
1-95 |
2.58e-05 |
|
recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. 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: 273173 [Multi-domain] Cd Length: 365 Bit Score: 48.12 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIqFVLSDEFSHlRPEQRLALLHIDKEEVSLRRVIGA 80
Cdd:TIGR00611 1 MYLSRLELTDFRNYDAVDL--ELSPGVNVIVGPNGQGKTNLLEAI-YYLALGRSH-RTSRDKPLIRFGAEAFVIEGRVSK 76
|
90
....*....|....*
gi 1958644837 81 KKDQYFLDKKMVTKN 95
Cdd:TIGR00611 77 GDREVTIPLEGLLKK 91
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
144-444 |
3.26e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 144 YDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRAleytiynqELNETRAKLDELSAKRE 223
Cdd:TIGR04523 382 YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII--------KNNSEIKDLTNQDSVKE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 224 TSGEKSRQLRDAQQDardKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLL 303
Cdd:TIGR04523 454 LIIKNLDNTRESLET---QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 304 KERQKLLEKIEEKQKELAE--TEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTS-KEERDKWIKKELKSLDQ 380
Cdd:TIGR04523 531 SEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDqKEKEKKDLIKEIEEKEK 610
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958644837 381 aindkkrQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSE 444
Cdd:TIGR04523 611 -------KISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKK 667
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
218-423 |
3.33e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 218 LSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTK----------------ISAMKEEKEQLSAERQEQIKQRTKL 281
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKnglvdlseeaklllqqLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 282 ELKAKDLQDELA--GNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQErtdlyAKQGRGS 359
Cdd:COG3206 246 RAQLGSGPDALPelLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQR-----ILASLEA 320
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958644837 360 QFTSKEERDKWIKKELKSLDQAIndkkRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKAR 423
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARL----AELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
159-458 |
3.52e-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: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 159 EGKREKINELLKYIEERLHTLEEEKEELAQYQKwdkMRRALEYtiynqELNETRAKLDELSAKREtsgEKSRQLRDAQ-- 236
Cdd:pfam01576 738 EQGEEKRRQLVKQVRELEAELEDERKQRAQAVA---AKKKLEL-----DLKELEAQIDAANKGRE---EAVKQLKKLQaq 806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 237 --------QDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQK 308
Cdd:pfam01576 807 mkdlqrelEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRR 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 309 LLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQE-RTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDK-K 386
Cdd:pfam01576 887 LEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTElAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKfK 966
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 387 RQIAAIHKDLEDTEANKE---KNLEQYNKL----DQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWRE-ENAEQQA 458
Cdd:pfam01576 967 SSIAALEAKIAQLEEQLEqesRERQAANKLvrrtEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQlEEAEEEA 1046
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
156-346 |
4.33e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 156 KETEGKREKInelLKYIEERLHTLEEEKEeLAQYQKWDKMRRALEytiynQELNETRAKLDE-----------LSAKRET 224
Cdd:PRK12704 34 KEAEEEAKRI---LEEAKKEAEAIKKEAL-LEAKEEIHKLRNEFE-----KELRERRNELQKlekrllqkeenLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 225 SGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQR--TKLELKAKdlqdelagnseqrkrl 302
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEIllEKVEEEAR---------------- 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958644837 303 lKERQKLLEKIEEKQKELAetepkfnsvkEKEERGIarLAQATQ 346
Cdd:PRK12704 169 -HEAAVLIKEIEEEAKEEA----------DKKAKEI--LAQAIQ 199
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
176-471 |
4.58e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.73 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 176 LHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKretsGEKSRQLRDAQQDARDKMEDIERQVRELKT 255
Cdd:TIGR00606 799 MELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSK----IELNRKLIQDQQEQIQHLKSKTNELKSEKL 874
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 256 KISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKelaETEPKFNSVKEKEE 335
Cdd:TIGR00606 875 QIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNK---KAQDKVNDIKEKVK 951
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 336 RGIAR---LAQATQERTDLYAKQ------GRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKE-K 405
Cdd:TIGR00606 952 NIHGYmkdIENKIQDGKDDYLKQketelnTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENElK 1031
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644837 406 NLEQYNK-LDQDLNEVkaRVEELDRKYYEVKNKKDELQSERNYLW-REENAEQQALAAKREDLEKKQQ 471
Cdd:TIGR00606 1032 EVEEELKqHLKEMGQM--QVLQMKQEHQKLEENIDLIKRNHVLALgRQKGYEKEIKHFKKELREPQFR 1097
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
292-480 |
4.73e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 292 LAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLyakqgrgsqftskeerdkwi 371
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL-------------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 372 KKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNL---------------------------------------EQYNK 412
Cdd:COG4942 75 EQELAALEAELAELEKEIAELRAELEAQKEELAELLralyrlgrqpplalllspedfldavrrlqylkylaparrEQAEE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644837 413 LDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQLLRAATGKA 480
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
202-444 |
4.93e-05 |
|
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: 47.20 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 202 TIYNQELNETRAKLDELSAKRETSgekSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEkeqLSAERQEQikqrTKL 281
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAA---NRQREKEKERYKRDREQWERQRRELESRVAELKEE---LRQSREKH----EEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 282 ELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELA-------ETEPKFNSVKEKEERGIARLAQATQERTDLYAK 354
Cdd:pfam07888 100 EEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKtltqrvlERETELERMKERAKKAGAQRKEEEAERKQLQAK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 355 qgrgsqFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDT----------EANKEKNLEQYNKLDQDLNEVKARV 424
Cdd:pfam07888 180 ------LQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLtqklttahrkEAENEALLEELRSLQERLNASERKV 253
|
250 260
....*....|....*....|
gi 1958644837 425 EELDRKYYEVKNKKDELQSE 444
Cdd:pfam07888 254 EGLGEELSSMAAQRDRTQAE 273
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
124-391 |
5.00e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.74 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 124 ATAPDSQRLKL-LREVAGTRVYDERK-----EESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQyqKWDKMRR 197
Cdd:PRK10929 20 ATAPDEKQITQeLEQAKAAKTPAQAEivealQSALNWLEERKGSLERAKQYQQVIDNFPKLSAELRQQLNN--ERDEPRS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 198 A---LEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDA-------QQDARDKMEDIERQVRELKTKISAmkEEKEQL 267
Cdd:PRK10929 98 VppnMSTDALEQEILQVSSQLLEKSRQAQQEQDRAREISDSlsqlpqqQTEARRQLNEIERRLQTLGTPNTP--LAQAQL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 268 SAERQEQIKQRTKLElkakdlQDELAGNS-EQRKRLLKERQKLLEK-IEEKQKELAETEPKFNSVKEKEergiarlAQAT 345
Cdd:PRK10929 176 TALQAESAALKALVD------ELELAQLSaNNRQELARLRSELAKKrSQQLDAYLQALRNQLNSQRQRE-------AERA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1958644837 346 QERTDLYAKQGRG------SQFTSKEERDKWIKKELKSLDQaINDKKRQIAA 391
Cdd:PRK10929 243 LESTELLAEQSGDlpksivAQFKINRELSQALNQQAQRMDL-IASQQRQAAS 293
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
158-472 |
7.37e-05 |
|
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: 47.14 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 158 TEGKREKINELLKYIEERLHTLEEEKEELAQYQ-KWDKMRRALEYTIynQELNETRAKLDELS-AKRETSGEKSRQLRDA 235
Cdd:pfam12128 599 EEELRERLDKAEEALQSAREKQAAAEEQLVQANgELEKASREETFAR--TALKNARLDLRRLFdEKQSEKDKKNKALAER 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 236 QQDARDKMEDIERQVRELKTKISAMKEE-KEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEkiE 314
Cdd:pfam12128 677 KDSANERLNSLEAQLKQLDKKHQAWLEEqKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALE--T 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 315 EKQKELAETEPKFNSVKeKEERGI----ARLAQATQERTDLyAKQGRGSQFTSKEERDKwIKKELKSLDQAINDKKRQIA 390
Cdd:pfam12128 755 WYKRDLASLGVDPDVIA-KLKREIrtleRKIERIAVRRQEV-LRYFDWYQETWLQRRPR-LATQLSNIERAISELQQQLA 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 391 AIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQ 470
Cdd:pfam12128 832 RLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKK 911
|
..
gi 1958644837 471 QL 472
Cdd:pfam12128 912 YV 913
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
227-404 |
7.45e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 227 EKSRQlRDAQQDARDKMEDI----ERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRL 302
Cdd:PRK09510 78 EEQRK-KKEQQQAEELQQKQaaeqERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 303 LKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAI 382
Cdd:PRK09510 157 AAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKA 236
|
170 180
....*....|....*....|..
gi 1958644837 383 NDKKrqiAAIHKDLEDTEANKE 404
Cdd:PRK09510 237 AAEK---AAAAKAAEKAAAAKA 255
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
214-335 |
7.86e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 7.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 214 KLDELSAKREtsgEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKlELKA------KD 287
Cdd:PRK00409 517 KLNELIASLE---ELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIK-EAKKeadeiiKE 592
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1958644837 288 L-QDELAGNSEQRKRLLKERQKLL-EKIEEKQKELAETEPKFNSVKEKEE 335
Cdd:PRK00409 593 LrQLQKGGYASVKAHELIEARKRLnKANEKKEKKKKKQKEKQEELKVGDE 642
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
674-1022 |
8.44e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 47.35 E-value: 8.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 674 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEmkmlkeKRQQSEKTFmpKQRSLQSLEASLHAMESTRESL 753
Cdd:TIGR01612 934 EKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLID------KINELDKAF--KDASLNDYEAKNNELIKYFNDL 1005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 754 KAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERI-----------KLEGIITRVETYLNENLRKRLDQVEQE 822
Cdd:TIGR01612 1006 KANLGKNKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIaihtsiyniidEIEKEIGKNIELLNKEILEEAEINITN 1085
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 823 LNELRETEGGTVLTATTSE-----LEAINKrVKDTMarsEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAI------ 891
Cdd:TIGR01612 1086 FNEIKEKLKHYNFDDFGKEenikyADEINK-IKDDI---KNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLedvadk 1161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 892 ---NHDTKELE-KMTNRQGMLLKKK---EECMKKIRELGSLP--QEAFEKYQTL------SLKQLFrkLEQCNTELKKYS 956
Cdd:TIGR01612 1162 aisNDDPEEIEkKIENIVTKIDKKKniyDEIKKLLNEIAEIEkdKTSLEEVKGInlsygkNLGKLF--LEKIDEEKKKSE 1239
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644837 957 HVNKKALDQFVNFSEQKEK--LIKRQEELDRGYKSIMELMNVLElRKYEAIQLTFKQVSKNFSEVFQK 1022
Cdd:TIGR01612 1240 HMIKAMEAYIEDLDEIKEKspEIENEMGIEMDIKAEMETFNISH-DDDKDHHIISKKHDENISDIREK 1306
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
163-982 |
9.71e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.65 E-value: 9.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 163 EKINELLKYIEERLHtleeEKEELAQYQKWdkmrraleytIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDK 242
Cdd:pfam15921 81 EEYSHQVKDLQRRLN----ESNELHEKQKF----------YLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 243 MEDierQVRELKtkisAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDE----LAGNSEQRKRLLKER------------ 306
Cdd:pfam15921 147 LQN---TVHELE----AAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEirsiLVDFEEASGKKIYEHdsmstmhfrslg 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 307 ---QKLLEKIEEK----QKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQ------GRGSQFTSKEERDKWIKK 373
Cdd:pfam15921 220 saiSKILRELDTEisylKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEheveitGLTEKASSARSQANSIQS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 374 ELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDlnevkaRVEELDRKYYEVKNKKDELQSERNYLWRE-- 451
Cdd:pfam15921 300 QLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYED------KIEELEKQLVLANSELTEARTERDQFSQEsg 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 452 --ENAEQQALA--AKRE---DLEKKQ--QLLRAATGKAIlngidsinkVLDHFRRK--GINQHVQNGYHGIVMNNFECEP 520
Cdd:pfam15921 374 nlDDQLQKLLAdlHKREkelSLEKEQnkRLWDRDTGNSI---------TIDHLRREldDRNMEVQRLEALLKAMKSECQG 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 521 AFYTCVEVTAG--------NRLFYHIVDSDEVSTKILMEFN--KMNLP-GEVTFLPLN-KLDVRDTAYPETNDAipmISK 588
Cdd:pfam15921 445 QMERQMAAIQGkneslekvSSLTAQLESTKEMLRKVVEELTakKMTLEsSERTVSDLTaSLQEKERAIEATNAE---ITK 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 589 LRynPRFDKAFKHvfgktlicrsmevstqlaraftMDCITLEGDQVSHrgaltggyYDTRKSRLELQkdvrkaeeelGEL 668
Cdd:pfam15921 522 LR--SRVDLKLQE----------------------LQHLKNEGDHLRN--------VQTECEALKLQ----------MAE 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 669 EAKLNENLRRNIERINNEIDQ---LMNQMQQIETQQRKFKASRDSILSEMKMLKEKrqqsektfmpKQRSLQSLEASlha 745
Cdd:pfam15921 560 KDKVIEILRQQIENMTQLVGQhgrTAGAMQVEKAQLEKEINDRRLELQEFKILKDK----------KDAKIRELEAR--- 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 746 mestreslkaelgtdlLSQLSLEDQKRVDALNDEIR---QLQQENRQLLNE----RIKLEGIITRVETyLNENLRKRLDQ 818
Cdd:pfam15921 627 ----------------VSDLELEKVKLVNAGSERLRavkDIKQERDQLLNEvktsRNELNSLSEDYEV-LKRNFRNKSEE 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 819 VEQELNELRETeggtvLTATTSELEainkRVKDTMARSEDLDNSIDKTEAGikelqksMERWKNMEKEHMDAINHDTKEL 898
Cdd:pfam15921 690 METTTNKLKMQ-----LKSAQSELE----QTRNTLKSMEGSDGHAMKVAMG-------MQKQITAKRGQIDALQSKIQFL 753
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 899 EK-MTNRQGMLLKKKEECMKKIRELGSLpqeAFEKYQTLSLKQLFRKLEQcntELKKYSHVNKKALDQF-VNFSEQKEkL 976
Cdd:pfam15921 754 EEaMTNANKEKHFLKEEKNKLSQELSTV---ATEKNKMAGELEVLRSQER---RLKEKVANMEVALDKAsLQFAECQD-I 826
|
....*.
gi 1958644837 977 IKRQEE 982
Cdd:pfam15921 827 IQRQEQ 832
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
230-446 |
1.14e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 230 RQLRDAQQDARDKMEDIERQVRELKTKISAmkeekeqlsAERQ-EQIKQRTK---LELKAKDLQDELAGNSEQRKRLLKE 305
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEE---------AEAAlEEFRQKNGlvdLSEEAKLLLQQLSELESQLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 306 RQKLLEKIEEKQKELAETEPKFNSVKEKEE--RGIARLAQATQERTDLyakqgrGSQFTSKEERDKWIKKELKSLDQAIN 383
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDALPELLQSPViqQLRAQLAELEAELAEL------SARYTPNHPDVIALRAQIAALRAQLQ 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958644837 384 DKKRQI-AAIHKDLEDTEANK---EKNLEQYNKLDQDLNEVKARVEELDRKY------YE-VKNKKDELQSERN 446
Cdd:COG3206 309 QEAQRIlASLEAELEALQAREaslQAQLAQLEARLAELPELEAELRRLEREVevarelYEsLLQRLEEARLAEA 382
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1091-1163 |
1.36e-04 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 43.91 E-value: 1.36e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958644837 1091 LSGGQKSLVALALIFaIQKcdpAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFY 1163
Cdd:cd03228 97 LSGGQRQRIAIARAL-LRD---PPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRII 165
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
646-875 |
2.28e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 646 DTRKSRLELQKDVRKAEEELGELEAKLNEnLRRNIERINNEIDQLMnqmQQIETQQRKFKASRDSILSEMKMLKEKRQQS 725
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRIRA-LEQELAALEAELAELE---KEIAELRAELEAQKEELAELLRALYRLGRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 726 EKTFMPKQRSLQSLEASLHamestreslkaelgtdLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVE 805
Cdd:COG4942 121 PLALLLSPEDFLDAVRRLQ----------------YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 806 TylnenLRKRLDQVEQELNELreteggtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQK 875
Cdd:COG4942 185 E-----ERAALEALKAERQKL--------LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
149-446 |
2.51e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.29 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 149 EESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYN-----QELNETrakLDELSAKRE 223
Cdd:PRK11281 66 EQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLSlrqleSRLAQT---LDQLQNAQN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 224 TSGEKSRQLRDAQ-QDARDKMEDIERQVR--ELKTKISAMKEEKEQLSAERQEQIK-QRTKLELKAKDLQDELAGNSEQR 299
Cdd:PRK11281 143 DLAEYNSQLVSLQtQPERAQAALYANSQRlqQIRNLLKGGKVGGKALRPSQRVLLQaEQALLNAQNDLQRKSLEGNTQLQ 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 300 KRLLKERQKLLEKIEEKQKELAETEpkfNSVKEKeergiaRLAQATQErtdlyAKQGRGSQFTSKEERDKWIKKELksld 379
Cdd:PRK11281 223 DLLQKQRDYLTARIQRLEHQLQLLQ---EAINSK------RLTLSEKT-----VQEAQSQDEAARIQANPLVAQEL---- 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644837 380 qaindkkrqiaaihkdledtEANKeknleqynKLDQDLNEVKARVEELDRKYYEVKNKKDEL-QSERN 446
Cdd:PRK11281 285 --------------------EINL--------QLSQRLLKATEKLNTLTQQNLRVKNWLDRLtQSERN 324
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
133-324 |
2.77e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 133 KLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETR 212
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELK 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 213 AKLDELSAKRetsgEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMK-----EEKEQLSAE----RQEQIKQRTKLEl 283
Cdd:PRK03918 609 DAEKELEREE----KELKKLEEELDKAFEELAETEKRLEELRKELEELEkkyseEEYEELREEylelSRELAGLRAELE- 683
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958644837 284 KAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETE 324
Cdd:PRK03918 684 ELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
156-458 |
2.79e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.95 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 156 KETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETraKLDELSAKRETSGEKSRQLRDA 235
Cdd:COG5185 156 VETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESE--TGNLGSESTLLEKAKEIINIEE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 236 QQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTK-LELKAKDLQDELAgNSEQRKRLLKERQKLLEKIE 314
Cdd:COG5185 234 ALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKrLNENANNLIKQFE-NTKEKIAEYTKSIDIKKATE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 315 EKQKELAETEP--KFNSVKEKEERGIARL-AQATQERTDLYAKQ-----GRGSQFTSKEERDKwiKKELKSLDQAINDKK 386
Cdd:COG5185 313 SLEEQLAAAEAeqELEESKRETETGIQNLtAEIEQGQESLTENLeaikeEIENIVGEVELSKS--SEELDSFKDTIESTK 390
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958644837 387 RQIAAIHKDLEDTEANKEKNLEQYNKL-DQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQA 458
Cdd:COG5185 391 ESLDEIPQNQRGYAQEILATLEDTLKAaDRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQS 463
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
674-995 |
2.82e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.45 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 674 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEM--KMLKEKRQQSEKtfmPKQRSLQSLEASLHAMESTRE 751
Cdd:COG5022 810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFgrSLKAKKRFSLLK---KETIYLQSAQRVELAERQLQE 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 752 sLKAELGT-DLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERI-KLEGIITRVETylnENLRKRLDQVEQELNELRET 829
Cdd:COG5022 887 -LKIDVKSiSSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIaRLKKLLNNIDL---EEGPSIEYVKLPELNKLHEV 962
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 830 EGGtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEH-------------MDAINHDTK 896
Cdd:COG5022 963 ESK--LKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLkelpvevaelqsaSKIISSEST 1040
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 897 ELEKMTNRQ---GMLLKKKEECMKKIRELG----SLPQEAFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNF 969
Cdd:COG5022 1041 ELSILKPLQklkGLLLLENNQLQARYKALKlrreNSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVA 1120
|
330 340
....*....|....*....|....*.
gi 1958644837 970 SEQKEKLIKRQEELDRGYKSIMELMN 995
Cdd:COG5022 1121 QMIKLNLLQEISKFLSQLVNTLEPVF 1146
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1086-1148 |
2.90e-04 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 43.61 E-value: 2.90e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958644837 1086 REMQQLSGGQKSLVALALIFAIQkcdpAPFYLFDEIDQALDAQHRKAVSDMIMELavHAQFIT 1148
Cdd:cd03225 130 RSPFTLSGGQKQRVAIAGVLAMD----PDILLLDEPTAGLDPAGRRELLELLKKL--KAEGKT 186
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
251-465 |
3.39e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.94 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 251 RELKTKISAMKEEKEQlsaerQEQIKQRTklelkakdlqdelagnsEQRK-RLlkERQKLlEKiEEKQKELAE--TEPKF 327
Cdd:PRK05035 432 RQAKAEIRAIEQEKKK-----AEEAKARF-----------------EARQaRL--EREKA-AR-EARHKKAAEarAAKDK 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 328 NSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKS---LDQAINDKKRQIAAihkDLEDTEANKE 404
Cdd:PRK05035 486 DAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAekqAAAAADPKKAAVAA---AIARAKAKKA 562
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958644837 405 KNLEQYNKLDQDLNEVKARVEELDRKyyeVKNKKDELQSErnylwREENAEQQALAAKRED 465
Cdd:PRK05035 563 AQQAANAEAEEEVDPKKAAVAAAIAR---AKAKKAAQQAA-----SAEPEEQVAEVDPKKA 615
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
149-481 |
3.40e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 149 EESISLMKETEGKREKINELLkyiEERLH----TLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRET 224
Cdd:pfam01576 137 EEDILLLEDQNSKLSKERKLL---EERISeftsNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 225 SGEKSrqlrdaqqDARDKMEDIERQVRELKTKISAMKEE-------KEQLSAERQEQIKQRTKLELKAKDLQDELAGNSE 297
Cdd:pfam01576 214 EGEST--------DLQEQIAELQAQIAELRAQLAKKEEElqaalarLEEETAQKNNALKKIRELEAQISELQEDLESERA 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 298 QRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKE---KEERGIARLAQATQERTDLYA------KQGRGSQFTSKEERD 368
Cdd:pfam01576 286 ARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQElrsKREQEVTELKKALEEETRSHEaqlqemRQKHTQALEELTEQL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 369 KWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSErnyl 448
Cdd:pfam01576 366 EQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSE---- 441
|
330 340 350
....*....|....*....|....*....|...
gi 1958644837 449 wreenaeqqalaakredLEKKQQLLRAATGKAI 481
Cdd:pfam01576 442 -----------------LESVSSLLNEAEGKNI 457
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
229-404 |
4.09e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 229 SRQLRDAQQDARDKMEDIERQVrelktkiSAMKEEKEqLSAeRQEQIKQRTKLELKAKDLQDELAGNSE---QRKRLLKE 305
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEA-------EAIKKEAL-LEA-KEEIHKLRNEFEKELRERRNELQKLEKrllQKEENLDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 306 RQKLLEKIEEK-QKELAETEPKFNSVKEKEERgIARLAQATQERTDlyakqgRGSQFTSKEerdkwIKKELksLDQAIND 384
Cdd:PRK12704 101 KLELLEKREEElEKKEKELEQKQQELEKKEEE-LEELIEEQLQELE------RISGLTAEE-----AKEIL--LEKVEEE 166
|
170 180
....*....|....*....|...
gi 1958644837 385 KKRQIAAIHKDLED---TEANKE 404
Cdd:PRK12704 167 ARHEAAVLIKEIEEeakEEADKK 189
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
718-879 |
4.32e-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: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 718 LKEKRQQSEKT--FMPKQrsLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERI 795
Cdd:COG3206 166 LELRREEARKAleFLEEQ--LPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 796 KLEGIITRVETYLNE--------NLRKRLDQVEQELNELRE--TEGGTVLTATTSELEAINKRVKDTMARS-EDLDNSID 864
Cdd:COG3206 244 ALRAQLGSGPDALPEllqspviqQLRAQLAELEAELAELSAryTPNHPDVIALRAQIAALRAQLQQEAQRIlASLEAELE 323
|
170
....*....|....*
gi 1958644837 865 KTEAGIKELQKSMER 879
Cdd:COG3206 324 ALQAREASLQAQLAQ 338
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
205-493 |
4.50e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 205 NQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELK 284
Cdd:COG4372 51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 285 AKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSK 364
Cdd:COG4372 131 RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 365 EERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSE 444
Cdd:COG4372 211 SLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1958644837 445 RNYLWREENAEQQALAAKREDLEKKQQLLRAATGKAILNGIDSINKVLD 493
Cdd:COG4372 291 AALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAEL 339
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1086-1147 |
4.67e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 43.51 E-value: 4.67e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958644837 1086 REMQQLSGGQKSLVALAlIFAIQKCDpapFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFI 1147
Cdd:cd03236 135 RNIDQLSGGELQRVAIA-AALARDAD---FYFFDEPSSYLDIKQRLNAARLIRELAEDDNYV 192
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
127-476 |
5.27e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 127 PDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQ 206
Cdd:TIGR00618 274 AQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 207 ELNETRAKLDELSAKRETSGEKS--RQLRDAQQD----------ARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQ 274
Cdd:TIGR00618 354 EIHIRDAHEVATSIREISCQQHTltQHIHTLQQQkttltqklqsLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQ 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 275 IKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIE---------EKQKELAETEPKFNSVKEKEERGI-ARLAQA 344
Cdd:TIGR00618 434 ELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQqlqtkeqihLQETRKKAVVLARLLELQEEPCPLcGSCIHP 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 345 TQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARV 424
Cdd:TIGR00618 514 NPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNIT 593
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1958644837 425 EELDRKYYEVKNKKDELQSERNYLWREENAEQ--QALAAKREDLEKKQQLLRAA 476
Cdd:TIGR00618 594 VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQdlQDVRLHLQQCSQELALKLTA 647
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
210-355 |
6.01e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 6.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 210 ETRAKLDELSAKRETSgeksRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKakdlQ 289
Cdd:PRK12704 52 EAIKKEALLEAKEEIH----KLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK----Q 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958644837 290 DELAGNSEQRKRLLKERQKLLEKI-----EEKQKELAEtepkfnSVKEKEERGIARLAQATQERTDLYAKQ 355
Cdd:PRK12704 124 QELEKKEEELEELIEEQLQELERIsgltaEEAKEILLE------KVEEEARHEAAVLIKEIEEEAKEEADK 188
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
149-471 |
6.16e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.91 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 149 EESISLMKETEGKREKINEL-----------LKYIEERlHTLEEEKEELAQYQKW-DKMR--------RALEYTIYNQEL 208
Cdd:pfam05622 28 EEKNSLQQENKKLQERLDQLesgddsgtpggKKYLLLQ-KQLEQLQEENFRLETArDDYRikceelekEVLELQHRNEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 209 ----NETRAKLDELSAKRETSgEKSRQLRDAQQDARDKME---DIERQVREL------------------------KTKI 257
Cdd:pfam05622 107 tslaEEAQALKDEMDILRESS-DKVKKLEATVETYKKKLEdlgDLRRQVKLLeernaeymqrtlqleeelkkanalRGQL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 258 SAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKqkelaetepKFNSVKEKEERG 337
Cdd:pfam05622 186 ETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRETNEEL---------RCAQLQQAELSQ 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 338 IARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKsLDQAINDKKRqIAAIHKDLEDTEANKEKNLEQYNKLDQDL 417
Cdd:pfam05622 257 ADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLR-LGQEGSYRER-LTELQQLLEDANRRKNELETQNRLANQRI 334
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 418 NEVKARVEELDRKYYEVKNKKDELQSERNYL------WREENAEQQALAAKREDLEKKQQ 471
Cdd:pfam05622 335 LELQQQVEELQKALQEQGSKAEDSSLLKQKLeehlekLHEAQSELQKKKEQIEELEPKQD 394
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
87-440 |
6.17e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 44.27 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 87 LDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKIN 166
Cdd:PTZ00108 1026 LVITNAKKKDLVKELKKLGYVRFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSYDYLLSMPIWSLTKEKVE 1105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 167 ELLKYIEERLhtleeekeelaqyQKWDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDI 246
Cdd:PTZ00108 1106 KLNAELEKKE-------------KELEKLKNTTPKDMWLEDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKP 1172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 247 ERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKD-------LQDELAGNSEQRKRLLKERQKLLEKIEEKQKE 319
Cdd:PTZ00108 1173 KLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPdnkksnsSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSK 1252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 320 LAETEPKFNSVKEKEERGIARL---AQATQERTDLYAKQGRGSQFTSKEERDkwikkELKSLDQAINDKKRQIAAIHKDL 396
Cdd:PTZ00108 1253 SSEDNDEFSSDDLSKEGKPKNApkrVSAVQYSPPPPSKRPDGESNGGSKPSS-----PTKKKVKKRLEGSLAALKKKKKS 1327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1958644837 397 EDTEANKEKNLEQYNK-LDQDLNEVKAR---------VEELDRKYYEVKNKKDE 440
Cdd:PTZ00108 1328 EKKTARKKKSKTRVKQaSASQSSRLLRRprkkksdssSEDDDDSEVDDSEDEDD 1381
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1090-1161 |
7.10e-04 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 43.15 E-value: 7.10e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644837 1090 QLSGGQKSLVALALIFAIQkcdpAPFYLFDEIDQALDAQHRKAVSDMIMELavHAQF-ITTTF----RPELLESADK 1161
Cdd:PRK10851 136 QLSGGQKQRVALARALAVE----PQILLLDEPFGALDAQVRKELRRWLRQL--HEELkFTSVFvthdQEEAMEVADR 206
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
141-471 |
7.59e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.88 E-value: 7.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 141 TRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAqyqkwDKMRRAleytiyNQELNETRAKLDELSA 220
Cdd:TIGR00606 704 LRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELR-----NKLQKV------NRDIQRLKNDIEEQET 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 221 KRETSGEKSRQLRDAQQDArDKMEDIERQVRELKTKIsamkeekEQLSAERQEqikqrTKLELKAKDLQDELAGNSEQRK 300
Cdd:TIGR00606 773 LLGTIMPEEESAKVCLTDV-TIMERFQMELKDVERKI-------AQQAAKLQG-----SDLDRTVQQVNQEKQEKQHELD 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 301 RLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEergiARLAQATQERTDLyakqgrgsqftskEERDKWIKKELKSLDQ 380
Cdd:TIGR00606 840 TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEK----LQIGTNLQRRQQF-------------EEQLVELSTEVQSLIR 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 381 AINDKKRQIAAIHKDLEDTEANKEKNL---EQYNKLDQDlnEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQ 457
Cdd:TIGR00606 903 EIKDAKEQDSPLETFLEKDQQEKEELIsskETSNKKAQD--KVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELN 980
|
330
....*....|....
gi 1958644837 458 ALAAKREDLEKKQQ 471
Cdd:TIGR00606 981 TVNAQLEECEKHQE 994
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
28-50 |
7.78e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 43.15 E-value: 7.78e-04
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
183-461 |
7.78e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 183 KEELAQYQKWDKMRRALEYTiyNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKM---EDIERQVRELKtKISA 259
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAE--QYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALrqqEKIERYQADLE-ELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 260 MKEEKEQLSAERQEQIKQR----TKLELKAKDLQDELA----GNSEQRKRLLKERQ--KLLEKIEEkQKELAETEPKfnS 329
Cdd:PRK04863 363 RLEEQNEVVEEADEQQEENearaEAAEEEVDELKSQLAdyqqALDVQQTRAIQYQQavQALERAKQ-LCGLPDLTAD--N 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 330 VKEKEERGIARLAQATQERTDLYAK----QGRGSQFT-------------SKEERDKWIKKELKSL--DQAINDKKRQIA 390
Cdd:PRK04863 440 AEDWLEEFQAKEQEATEELLSLEQKlsvaQAAHSQFEqayqlvrkiagevSRSEAWDVARELLRRLreQRHLAEQLQQLR 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 391 AIHKDLE---DTEANKEKNLEQYNK------------------LDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLW 449
Cdd:PRK04863 520 MRLSELEqrlRQQQRAERLLAEFCKrlgknlddedeleqlqeeLEARLESLSESVSEARERRMALRQQLEQLQARIQRLA 599
|
330
....*....|..
gi 1958644837 450 REENAEQQALAA 461
Cdd:PRK04863 600 ARAPAWLAAQDA 611
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
257-480 |
8.00e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 44.05 E-value: 8.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 257 ISAMKEEKEQLSAERqEQIKQRtklELKAKDLQDElAGNSEQRKRLLKERQKLLEKIEEKQKELAETEP-KFNSVKEKEE 335
Cdd:NF012221 1534 VVATSESSQQADAVS-KHAKQD---DAAQNALADK-ERAEADRQRLEQEKQQQLAAISGSQSQLESTDQnALETNGQAQR 1608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 336 RGIARLAQA-TQERTDLyaKQG----RGSQFTSKEERDKW--------IKKELKSLDQA-------INDKKRQIAAIHKD 395
Cdd:NF012221 1609 DAILEESRAvTKELTTL--AQGldalDSQATYAGESGDQWrnpfagglLDRVQEQLDDAkkisgkqLADAKQRHVDNQQK 1686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 396 LEDTEANKEKNLEQ--YNKLDQDLNEVKARVeeldrkyyEVKNKKDELQSERNylwREENAEQQALAAKREDLEKKQQLL 473
Cdd:NF012221 1687 VKDAVAKSEAGVAQgeQNQANAEQDIDDAKA--------DAEKRKDDALAKQN---EAQQAESDANAAANDAQSRGEQDA 1755
|
....*..
gi 1958644837 474 RAATGKA 480
Cdd:NF012221 1756 SAAENKA 1762
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
148-467 |
8.13e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 148 KEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKwdkmrralEYTIYNQELNETRAKLDELSAKRETSGE 227
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARS--------ELEQLEEELEELNEQLQAAQAELAQAQE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 228 KSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKE-- 305
Cdd:COG4372 102 ELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAea 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 306 RQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDK 385
Cdd:COG4372 182 EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 386 KRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKRED 465
Cdd:COG4372 262 ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELAD 341
|
..
gi 1958644837 466 LE 467
Cdd:COG4372 342 LL 343
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
11-47 |
8.35e-04 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 42.67 E-value: 8.35e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1958644837 11 FRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQF 47
Cdd:cd03242 9 FRNYAELEL--EFEPGVTVLVGENAQGKTNLLEAISL 43
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
163-433 |
9.94e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 9.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 163 EKINELLKYIEERLHTLEEEkeELAQYQKWDKMRRALeytiynQELNETRAKLDELsaKRETSGEKSRQLRDAQQDARDK 242
Cdd:PRK04863 840 RQLNRRRVELERALADHESQ--EQQQRSQLEQAKEGL------SALNRLLPRLNLL--ADETLADRVEEIREQLDEAEEA 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 243 MEDIERQ---VRELKTKISAMKEEKEQLSAERQ--EQIKQRTKLELKAKDLQDELAGNS-----EQRKRLLKERQKLLEK 312
Cdd:PRK04863 910 KRFVQQHgnaLAQLEPIVSVLQSDPEQFEQLKQdyQQAQQTQRDAKQQAFALTEVVQRRahfsyEDAAEMLAKNSDLNEK 989
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 313 IEEKQKElAETEPkfNSVKEKEERGIARLAQATQERTDLyakqgrGSQFTSKEERDKWIKKELKSL---------DQAIN 383
Cdd:PRK04863 990 LRQRLEQ-AEQER--TRAREQLRQAQAQLAQYNQVLASL------KSSYDAKRQMLQELKQELQDLgvpadsgaeERARA 1060
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1958644837 384 DKKRqiaaIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYE 433
Cdd:PRK04863 1061 RRDE----LHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHE 1106
|
|
| F-BAR_CIP4-like |
cd07653 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 ... |
364-458 |
1.01e-03 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Cdc42-Interacting Protein 4 (CIP4), Formin Binding Protein 17 (FBP17), FormiN Binding Protein 1-Like (FNBP1L), and similar proteins. CIP4 and FNBP1L are Cdc42 effectors that bind Wiskott-Aldrich syndrome protein (WASP) and function in endocytosis. CIP4 and FBP17 bind to the Fas ligand and may be implicated in the inflammatory response. CIP4 may also play a role in phagocytosis. Members of this subfamily typically contain an N-terminal F-BAR domain and a C-terminal SH3 domain. In addition, some members such as FNBP1L contain a central Cdc42-binding HR1 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153337 [Multi-domain] Cd Length: 251 Bit Score: 42.24 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 364 KEERDKWIKkELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELdRKYYEVKNKKDElQS 443
Cdd:cd07653 104 RQERKKHLS-EGSKLQQKLESSIKQLEKSKKAYEKAFKEAEKAKQKYEKADADMNLTKADVEKA-KANANLKTQAAE-EA 180
|
90
....*....|....*..
gi 1958644837 444 ERNY--LWREENAEQQA 458
Cdd:cd07653 181 KNEYaaQLQKFNKEQRQ 197
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
3-464 |
1.01e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.50 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 3 IKQVIIQGFRSY----RDQTIVDpFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFshlrPEQRLALLHIDKEEVSLRRVI 78
Cdd:TIGR00606 3 FLKMSILGVRSFgiedKDKQIID-FFSPLTILVGPNGAGKTTIIECLKYICTGDF----PPGTKGNTFVHDPKVAQETDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 79 GAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYI------VKQGKINQMATAPDSQRLKLLREVAGTRV--------Y 144
Cdd:TIGR00606 78 RAQIRLQFRDVNGEECAVVRSMVCTQKTKKTEFKTLegvitrYKHGEKVSLSSKCAEIDREMISHLGVSKAvlnnvifcH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 145 DERKEESISLMKETEGKREKINELLKYIEErLHTLEEEKEELAQYQKWDKMRRALeYTIYNQELNETRAKLdelsAKRET 224
Cdd:TIGR00606 158 QEDSNWPLSEGKALKQKFDEIFSATRYIKA-LETLRQVRQTQGQKVQEHQMELKY-LKQYKEKACEIRDQI----TSKEA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 225 SGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDL----QDELAGNSEQRK 300
Cdd:TIGR00606 232 QLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVfqgtDEQLNDLYHNHQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 301 RLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARL---AQATQERTDLYAKQGRGSQFTSKE---ERDKWIKKE 374
Cdd:TIGR00606 312 RTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLqlqADRHQEHIRARDSLIQSLATRLELdgfERGPFSERQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 375 LKS----LDQAINDKKRQIAAIHKDLEDTEANKEKNLEQY-NKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLW 449
Cdd:TIGR00606 392 IKNfhtlVIERQEDEAKTAAQLCADLQSKERLKQEQADEIrDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD 471
|
490
....*....|....*
gi 1958644837 450 REENAEQQALAAKRE 464
Cdd:TIGR00606 472 RILELDQELRKAERE 486
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
147-318 |
1.07e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 147 RKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKM-RRALEYTIYNQELNETRAKLDELSAK---- 221
Cdd:COG3206 203 QKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSgPDALPELLQSPVIQQLRAQLAELEAElael 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 222 RETSGEKS---RQLRDAQQDARDKMED-IERQVRELKTKISAMKEEKEQLSAERQE---QIKQRTKLELKAKDLQDELAG 294
Cdd:COG3206 283 SARYTPNHpdvIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQleaRLAELPELEAELRRLEREVEV 362
|
170 180
....*....|....*....|....
gi 1958644837 295 NSEQRKRLLKERQKLleKIEEKQK 318
Cdd:COG3206 363 ARELYESLLQRLEEA--RLAEALT 384
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
371-479 |
1.15e-03 |
|
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: 41.83 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 371 IKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKD--ELQSERNYL 448
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyeALQKEIESL 101
|
90 100 110
....*....|....*....|....*....|.
gi 1958644837 449 WREENAEQQALAAKREDLEKKQQLLRAATGK 479
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAE 132
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
338-475 |
1.32e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 338 IARLAQATqerTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHK--DLEDTEANKEKNLEQYNKLDQ 415
Cdd:COG3206 150 AAAVANAL---AEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQknGLVDLSEEAKLLLQQLSELES 226
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 416 DLNEVKARVEELDRKYYEVKNKKDELQSERNYLwrEENAEQQALAAKREDLEKKQQLLRA 475
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGSGPDALPEL--LQSPVIQQLRAQLAELEAELAELSA 284
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
134-323 |
1.32e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.92 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 134 LLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKW-DKMRRALE------------ 200
Cdd:pfam06160 279 LEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYTLNENELERVRGLEKQlEELEKRYDeiverleekeva 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 201 YTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKIsamkeEKEQLSAERQEQIKQRTK 280
Cdd:pfam06160 359 YSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLV-----EKSNLPGLPESYLDYFFD 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958644837 281 LELKAKDLQDELAG---NSEQRKRLLKERQKLLEKIEEKQKELAET 323
Cdd:pfam06160 434 VSDEIEDLADELNEvplNMDEVNRLLDEAQDDVDTLYEKTEELIDN 479
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
693-865 |
1.37e-03 |
|
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: 41.83 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 693 QMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKR 772
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 773 VDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLnENLRKRLDQVEQELNELREteggtvltATTSELEAINKRVKDT 852
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEEL-AELEAELAELEAELEEKKA--------ELDEELAELEAELEEL 161
|
170
....*....|...
gi 1958644837 853 MARSEDLDNSIDK 865
Cdd:COG1579 162 EAEREELAAKIPP 174
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
205-333 |
1.50e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 41.63 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 205 NQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSA---ERQEQIKQRTKL 281
Cdd:pfam06008 53 AQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSsdlSRMLAEAQRMLG 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1958644837 282 ELKAKDLQDELAGNSEQrkrlLKERQKLLEKIEEKQKEL-AETEPKFNSVKEK 333
Cdd:pfam06008 133 EIRSRDFGTQLQNAEAE----LKAAQDLLSRIQTWFQSPqEENKALANALRDS 181
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
335-485 |
1.57e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.03 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 335 ERGIARLAQATQERTDLYAKQGR-----GSQFTSKEERDKwIKKELKSLDQAINDKKRQIAAIHKDLEDTEA-------N 402
Cdd:pfam00529 61 DSAEAQLAKAQAQVARLQAELDRlqaleSELAISRQDYDG-ATAQLRAAQAAVKAAQAQLAQAQIDLARRRVlapiggiS 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 403 KEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNylwREENAEQQALAAKREDLEKKQQLLRAATGKAIL 482
Cdd:pfam00529 140 RESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVR---SELSGAQLQIAEAEAELKLAKLDLERTEIRAPV 216
|
...
gi 1958644837 483 NGI 485
Cdd:pfam00529 217 DGT 219
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
208-445 |
1.73e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.79 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 208 LNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKE-------QLSAERQEQIKQRTK 280
Cdd:pfam05483 263 LEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatkticQLTEEKEAQMEELNK 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 281 LELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSvkEKEERgiarlaqatqertdlyakqgrgSQ 360
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSS--ELEEM----------------------TK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 361 FTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLnEVKARVEELDRKYY--EVKNKK 438
Cdd:pfam05483 399 FKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDL-EIQLTAIKTSEEHYlkEVEDLK 477
|
....*..
gi 1958644837 439 DELQSER 445
Cdd:pfam05483 478 TELEKEK 484
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
301-482 |
1.76e-03 |
|
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: 41.45 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 301 RLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLyakqgrgsqftsKEERDKwIKKELKSLDQ 380
Cdd:COG1579 7 RALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL------------EKEIKR-LELEIEEVEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 381 AINDKKRQIAAI--HKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQA 458
Cdd:COG1579 74 RIKKYEEQLGNVrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170 180
....*....|....*....|....
gi 1958644837 459 LAAKREDLEKKQQLLRAATGKAIL 482
Cdd:COG1579 154 LEAELEELEAEREELAAKIPPELL 177
|
|
| MAT1 |
pfam06391 |
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ... |
203-328 |
1.81e-03 |
|
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.
Pssm-ID: 461894 [Multi-domain] Cd Length: 202 Bit Score: 41.07 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 203 IYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQ--IKQRTK 280
Cdd:pfam06391 58 TNGIDVEETEKKIEQYEKENKDLILKNKMKLSQEEEELEELLELEKREKEERRKEEKQEEEEEKEKKEKAKQelIDELMT 137
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1958644837 281 LELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFN 328
Cdd:pfam06391 138 SNKDAEEIIAQHKKTAKKRKSERRRKLEELNRVLEQKPTQFSTGIKFG 185
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
149-475 |
1.88e-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: 42.31 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 149 EESISLMKETEGKREKINELlkyiEERLHTLEEEKEELAQYQKWDKMrralEYTIYNQELNETRAKLDELSAKRETSGEK 228
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNKL----EVELNKLEKQKKENKKNIDKFLT----EIKKKEKELEKLNNKYNDLKKQKEELENE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 229 SRQLRDAQQDARDKMEDIERQV-----------------RELKTKISAMKEEKEQLSaerqeqiKQRTKLELKAKDLQDE 291
Cdd:TIGR04523 175 LNLLEKEKLNIQKNIDKIKNKLlklelllsnlkkkiqknKSLESQISELKKQNNQLK-------DNIEKKQQEINEKTTE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 292 LAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRgSQFTSKEERDKWI 371
Cdd:TIGR04523 248 ISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELK-SELKNQEKKLEEI 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 372 KKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSE-RNYLWR 450
Cdd:TIGR04523 327 QNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKiQNQEKL 406
|
330 340
....*....|....*....|....*..
gi 1958644837 451 EENAEQQ--ALAAKREDLEKKQQLLRA 475
Cdd:TIGR04523 407 NQQKDEQikKLQQEKELLEKEIERLKE 433
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
260-441 |
2.03e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 42.16 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 260 MKEEKEQ-----LSAErQEQIKQRTKLELKAkdlqdELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKE 334
Cdd:PRK00106 26 MKSAKEAaeltlLNAE-QEAVNLRGKAERDA-----EHIKKTAKRESKALKKELLLEAKEEARKYREEIEQEFKSERQEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 335 ERGIARLAQ--ATQERTDlyakqgrgSQFTSKEerdkwikKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNK 412
Cdd:PRK00106 100 KQIESRLTEraTSLDRKD--------ENLSSKE-------KTLESKEQSLTDKSKHIDEREEQVEKLEEQKKAELERVAA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958644837 413 LDQD--------------LNEVKARVEELDRkyyEVKNKKDEL 441
Cdd:PRK00106 165 LSQAeareiilaetenklTHEIATRIREAER---EVKDRSDKM 204
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
349-480 |
2.10e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 349 TDLYAKQGRGSQFTSKEERdkwIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELD 428
Cdd:COG3883 16 PQIQAKQKELSELQAELEA---AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958644837 429 RKYYEVKNKKDEL------QSERNYLWR----------------EENAEQQALAAKREDLEKKQQLLRAATGKA 480
Cdd:COG3883 93 RALYRSGGSVSYLdvllgsESFSDFLDRlsalskiadadadlleELKADKAELEAKKAELEAKLAELEALKAEL 166
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
676-1008 |
2.55e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 676 LRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMpkqRSLQSLEASLHAMESTRESLKa 755
Cdd:pfam15921 262 LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYM---RQLSDLESTVSQLRSELREAK- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 756 ELGTDLLSQLsledQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNEnlRKRLDQVEQELNEL---RETEGG 832
Cdd:pfam15921 338 RMYEDKIEEL----EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHK--REKELSLEKEQNKRlwdRDTGNS 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 833 TVLTATTSELEAINKRVKdtmaRSEDLDNSIDkteagiKELQKSMERwknmekeHMDAINHDTKELEKMTNRQGMLLKKK 912
Cdd:pfam15921 412 ITIDHLRRELDDRNMEVQ----RLEALLKAMK------SECQGQMER-------QMAAIQGKNESLEKVSSLTAQLESTK 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 913 EECMKKIRELGS--LPQEAFEKY---QTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGY 987
Cdd:pfam15921 475 EMLRKVVEELTAkkMTLESSERTvsdLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALK 554
|
330 340
....*....|....*....|.
gi 1958644837 988 KSIMELMNVLELRKYEAIQLT 1008
Cdd:pfam15921 555 LQMAEKDKVIEILRQQIENMT 575
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
679-924 |
2.67e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 679 NIERINNEIDQLMNQMQQIETQQRKFKAsrdsiLSEMKMLKEKRQQsektfmpkqrsLQSLEASLHAMESTRESLKAELG 758
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDAREQIEL-----LEPIRELAERYAA-----------ARERLAELEYLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 759 TDLLsqlsledQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRLDQVEQELNELREteggtvltat 838
Cdd:COG4913 290 LELL-------EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLER---------- 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 839 tsELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINhdtKELEKMTNRQGMLLKKKEECMKK 918
Cdd:COG4913 353 --ELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE---EALAEAEAALRDLRRELRELEAE 427
|
....*.
gi 1958644837 919 IRELGS 924
Cdd:COG4913 428 IASLER 433
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
162-467 |
2.83e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.59 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 162 REKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRAlEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARD 241
Cdd:pfam19220 26 KADFSQLIEPIEAILRELPQAKSRLLELEALLAQERA-AYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 242 KMEDIERQVRELKTKISA----MKEEKEQLSAERQEQIKQRTKLELKAKDLQD---ELAGNSEQRKRLLKERQKLLEKIE 314
Cdd:pfam19220 105 AKEELRIELRDKTAQAEAlerqLAAETEQNRALEEENKALREEAQAAEKALQRaegELATARERLALLEQENRRLQALSE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 315 EKQKELAETEPKfnsVKEKEERGIARLAQATQERTDLYAKQ-GRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIH 393
Cdd:pfam19220 185 EQAAELAELTRR---LAELETQLDATRARLRALEGQLAAEQaERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 394 KDLEDTEANKEKNLEQYNKLDQDLNE-------VKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDL 466
Cdd:pfam19220 262 QLLAEARNQLRDRDEAIRAAERRLKEasierdtLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAAL 341
|
.
gi 1958644837 467 E 467
Cdd:pfam19220 342 E 342
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1090-1161 |
2.86e-03 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 40.79 E-value: 2.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644837 1090 QLSGGQKSLVALALIFAIqkcDPApFYLFDEIDQALDAQHRKAVSDMIMELavHAQF-ITTTF----RPELLESADK 1161
Cdd:cd03296 136 QLSGGQRQRVALARALAV---EPK-VLLLDEPFGALDAKVRKELRRWLRRL--HDELhVTTVFvthdQEEALEVADR 206
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
198-471 |
2.93e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 198 ALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARD--KMEDIERQVRELKTKISAMKEEKEQLSAERQEQI 275
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDarKAEEARKAEDARKAEEARKAEDAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 276 KQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLE--KIEEKQKelAETEPKFNSVKEKEErgiARLAQATQErtdlyA 353
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDarKAEAARK--AEEERKAEEARKAED---AKKAEAVKK-----A 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 354 KQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQ-DLNEVKARVEELDRKYY 432
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEaKKAEEKKKADEAKKKAE 1312
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958644837 433 EvKNKKDELQSernylwREENAEQQALAAKREDLEKKQQ 471
Cdd:PTZ00121 1313 E-AKKADEAKK------KAEEAKKKADAAKKKAEEAKKA 1344
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1086-1162 |
3.21e-03 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 40.15 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1086 REMQQLSGGQKSLVALALIFAIqkcdPAPFYLFDEIDQALDAQHRKAVSDMIMElavHAQ----FITTTFRPELLESADK 1161
Cdd:COG4133 127 LPVRQLSAGQKRRVALARLLLS----PAPLWLLDEPFTALDAAGVALLAELIAA---HLArggaVLLTTHQPLELAAARV 199
|
.
gi 1958644837 1162 F 1162
Cdd:COG4133 200 L 200
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1089-1161 |
3.23e-03 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 41.74 E-value: 3.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958644837 1089 QQLSGGQKSLVALA--LIfaiqkCDPaPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADK 1161
Cdd:COG2274 610 SNLSGGQRQRLAIAraLL-----RNP-RILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADR 678
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
149-405 |
3.30e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.63 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 149 EESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQyqkwdkMRRALEYTI--YNQELNETRAKLDELSAKRETSG 226
Cdd:pfam05483 506 QEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN------LRDELESVReeFIQKGDEVKCKLDKSEENARSIE 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 227 EKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKER 306
Cdd:pfam05483 580 YEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNY 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 307 QK-----------LLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAK--QGRGSQFTSKEERDKWIKK 373
Cdd:pfam05483 660 QKeiedkkiseekLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKiiEERDSELGLYKNKEQEQSS 739
|
250 260 270
....*....|....*....|....*....|..
gi 1958644837 374 ELKSLDQAINDKKRQIAAIHKDLEDTEANKEK 405
Cdd:pfam05483 740 AKAALEIELSNIKAELLSLKKQLEIEKEEKEK 771
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
129-469 |
3.60e-03 |
|
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: 41.49 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 129 SQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINEL-----LKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTI 203
Cdd:TIGR00618 436 QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLqtkeqIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNP 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 204 YNQELNETRAKLDELSAKRETSgeksRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLEL 283
Cdd:TIGR00618 516 ARQDIDNPGPLTRRMQRGEQTY----AQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQN 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 284 KAKDLQDELAGNSEQRKRLLKERQKLLEKIEEK-----------------QKELAETEPKFNSVKEKEERGIARLAQATQ 346
Cdd:TIGR00618 592 ITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEqdlqdvrlhlqqcsqelALKLTALHALQLTLTQERVREHALSIRVLP 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 347 ERT------DLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNE- 419
Cdd:TIGR00618 672 KELlasrqlALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHq 751
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 420 ----VKARVEELDRKYYEV------KNKKDELQSERNYLWREENAEQQALAAKREDLEKK 469
Cdd:TIGR00618 752 artvLKARTEAHFNNNEEVtaalqtGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQE 811
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1086-1140 |
3.60e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 40.74 E-value: 3.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1958644837 1086 REMQQLSGGQKSLVALALIFAIqkcDPApFYLFDEIDQALDAQHRKAVSDMIMEL 1140
Cdd:PRK13632 138 KEPQNLSGGQKQRVAIASVLAL---NPE-IIIFDESTSMLDPKGKREIKKIMVDL 188
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
254-458 |
3.69e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 254 KTKISAMKEEKEQLSAERQEQIKQRTKLELkakdlqdelagnSEQRKRLLKERQKLLEKIEEKQKELAETEpkfNSVKEK 333
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEAL------------LEAKEEIHKLRNEFEKELRERRNELQKLE---KRLLQK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 334 EErgiarlaqatqertdlyakqgrgsQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKL 413
Cdd:PRK12704 95 EE------------------------NLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958644837 414 DQDlnEVKARVeeldrkyyeVKNKKDELQSERNYLWR--EENAEQQA 458
Cdd:PRK12704 151 TAE--EAKEIL---------LEKVEEEARHEAAVLIKeiEEEAKEEA 186
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
161-480 |
3.75e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 161 KREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDAR 240
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 241 DKMEDIERQVRELKtKISAmkeekeqlsAERQEQIKQRTKLElKAKDlqdelAGNSEQRKRLLKERqklleKIEEKQKel 320
Cdd:PTZ00121 1163 ARKAEEARKAEDAK-KAEA---------ARKAEEVRKAEELR-KAED-----ARKAEAARKAEEER-----KAEEARK-- 1219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 321 AETEPKFNSVKEKEE--RGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKElksldqaindKKRQIAAIHKDLED 398
Cdd:PTZ00121 1220 AEDAKKAEAVKKAEEakKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE----------EARKADELKKAEEK 1289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 399 TEANKEKNLEQYNKLDQ--DLNEVKARVEELDRKYYEVKNKKDELQSernylwREENAEQQALAAKREDlEKKQQLLRAA 476
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEakKKAEEAKKADEAKKKAEEAKKKADAAKK------KAEEAKKAAEAAKAEA-EAAADEAEAA 1362
|
....
gi 1958644837 477 TGKA 480
Cdd:PTZ00121 1363 EEKA 1366
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
246-390 |
3.79e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 246 IERQVRELKTKISAMKEEKEQLSAERQEQikQRTKLELKAKDLQDELagnseqrKRLLKERQKLLEKIEEKQKELAETEP 325
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEER--ELTEEEEEIRRLEEQV-------ERLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958644837 326 KFNSVKEKEERGIARlaqatqERtdlyakqgrgsQFTSKEERDKWIKKELKSLDQAINDKKRQIA 390
Cdd:COG2433 449 ELSEARSEERREIRK------DR-----------EISRLDREIERLERELEEERERIEELKRKLE 496
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1091-1163 |
3.95e-03 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 40.15 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1091 LSGGQKSLVALALifAI-QKCDpapFYLFDEIDQALDAQhrkaVSDMIME------LAVHAQFITTTFRPELLESADKFY 1163
Cdd:cd03250 128 LSGGQKQRISLAR--AVySDAD---IYLLDDPLSAVDAH----VGRHIFEncilglLLNNKTRILVTHQLQLLPHADQIV 198
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
147-336 |
4.10e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 147 RKEESISLMKETEGKREKINELLKYIEERlhtlEEEKEELAQYQKWDKMrraleytiynQELNETRAKLDELSAKRETSG 226
Cdd:COG5022 912 KKSLSSDLIENLEFKTELIARLKKLLNNI----DLEEGPSIEYVKLPEL----------NKLHEVESKLKETSEEYEDLL 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 227 EKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQE---------QIKQRTKLELKAKDLQdELAGNSE 297
Cdd:COG5022 978 KKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEvaelqsaskIISSESTELSILKPLQ-KLKGLLL 1056
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958644837 298 QRKRLLKER------QKLLEKIEEKQKELAE-TEPKFNSVKEKEER 336
Cdd:COG5022 1057 LENNQLQARykalklRRENSLLDDKQLYQLEsTENLLKTINVKDLE 1102
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
145-475 |
4.15e-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: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 145 DERKEESISLMKETEGKREKINE---LLKYIEERLHTLEEEKEELAQ-YQKW-DKMRRALEYTIYNQELNETRAKLDELS 219
Cdd:COG3096 281 RELSERALELRRELFGARRQLAEeqyRLVEMARELEELSARESDLEQdYQAAsDHLNLVQTALRQQEKIERYQEDLEELT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 220 AKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTkisamkeekeQLsAERQEqikqrtklelkAKDLQDELAGNSEQR 299
Cdd:COG3096 361 ERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKS----------QL-ADYQQ-----------ALDVQQTRAIQYQQA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 300 KRLLKERQKLLekieekqkELAETEPKfnSVKEKEERGIARLAQATQERTDLYAK----QGRGSQF-------------T 362
Cdd:COG3096 419 VQALEKARALC--------GLPDLTPE--NAEDYLAAFRAKEQQATEEVLELEQKlsvaDAARRQFekayelvckiageV 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 363 SKEERDKWIKKELKSL--DQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDE 440
Cdd:COG3096 489 ERSQAWQTARELLRRYrsQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEE 568
|
330 340 350
....*....|....*....|....*....|....*
gi 1958644837 441 LQSERnylwREENAEQQALAAKREDLEKKQQLLRA 475
Cdd:COG3096 569 LEEQA----AEAVEQRSELRQQLEQLRARIKELAA 599
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
673-925 |
4.33e-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: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 673 NENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRES 752
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 753 LKAELGTDLLS----QLSLED-QKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLnENLRKRLDQVEQELNELR 827
Cdd:TIGR04523 466 LETQLKVLSRSinkiKQNLEQkQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKI-EKLESEKKEKESKISDLE 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 828 eteggtvltattSELEAINKRVKDTMARSE--DLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQ 905
Cdd:TIGR04523 545 ------------DELNKDDFELKKENLEKEidEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI 612
|
250 260
....*....|....*....|
gi 1958644837 906 GMLLKKKEECMKKIRELGSL 925
Cdd:TIGR04523 613 SSLEKELEKAKKENEKLSSI 632
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
711-945 |
4.49e-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: 41.26 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 711 ILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELG----TDLLSQLSLEDQKRVDALNDEIRQLQQE 786
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKArqaeMDRQAAIYAEQERMAMERERELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 787 NRQLLNERIKLEGIITRVETY-----LNENLRKRLDQVEQELNELR-----ETEGGTVLTATTSELEAInkRVKDTMARS 856
Cdd:pfam17380 357 ERKRELERIRQEEIAMEISRMrelerLQMERQQKNERVRQELEAARkvkilEEERQRKIQQQKVEMEQI--RAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 857 EDLDNSIDKTEAGIKEL-QKSMERWKNMEKEHMDAINHDTKELEKmtNRQGMLLKKKEECMKKIRElgslpQEAFEKYQT 935
Cdd:pfam17380 435 REVRRLEEERAREMERVrLEEQERQQQVERLRQQEEERKRKKLEL--EKEKRDRKRAEEQRRKILE-----KELEERKQA 507
|
250
....*....|
gi 1958644837 936 LSLKQLFRKL 945
Cdd:pfam17380 508 MIEEERKRKL 517
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
155-507 |
4.51e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 155 MKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEytiynQELNETRAKLDELSAKRETSGEKSRQLRD 234
Cdd:TIGR00606 600 LASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLK-----EEIEKSSKQRAMLAGATAVYSQFITQLTD 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 235 --------AQQDARDKMEdIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKER 306
Cdd:TIGR00606 675 enqsccpvCQRVFQTEAE-LQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKL 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 307 QKLLEKIEEKQKELAETEPKFNSVKEKEERG---------IARLAQATQERTDLYAKQGRGSQFTSkeerdkwIKKELKS 377
Cdd:TIGR00606 754 QKVNRDIQRLKNDIEEQETLLGTIMPEEESAkvcltdvtiMERFQMELKDVERKIAQQAAKLQGSD-------LDRTVQQ 826
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 378 LDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVK--------------ARVEELDRKYYEVKNKKDELQS 443
Cdd:TIGR00606 827 VNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKseklqigtnlqrrqQFEEQLVELSTEVQSLIREIKD 906
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644837 444 ERNYLWREENAEQQALAAKREDLEKKQQLLRAATGKailngIDSINKVLD--HFRRKGINQHVQNG 507
Cdd:TIGR00606 907 AKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDK-----VNDIKEKVKniHGYMKDIENKIQDG 967
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
131-349 |
5.30e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 131 RLKLLREVAGTRVYDE---RKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELaqyqkwDKMRRALEYtiynqe 207
Cdd:PRK05771 61 KLRSYLPKLNPLREEKkkvSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKEL------EQEIERLEP------ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 208 LNETRAKLDELSAKRETSGEKSRqlRDAQQDARDKMEDIERQVRELKTK-------ISAMKEEKEQLSAERQEQIKQRTK 280
Cdd:PRK05771 129 WGNFDLDLSLLLGFKYVSVFVGT--VPEDKLEELKLESDVENVEYISTDkgyvyvvVVVLKELSDEVEEELKKLGFERLE 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958644837 281 LELKaKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAE----TEPKFNSVKEKEErgiARLAQATQERT 349
Cdd:PRK05771 207 LEEE-GTPSELIREIKEELEEIEKERESLLEELKELAKKYLEellaLYEYLEIELERAE---ALSKFLKTDKT 275
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
159-479 |
5.38e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 159 EGKREKINELLKyiEERLHTLE-EEKEELAQYQKWDKMRRALEYTiynQELNETRAKLDELSAKRETSGEKSRQLRDAQQ 237
Cdd:pfam01576 600 EKKQKKFDQMLA--EEKAISARyAEERDRAEAEAREKETRALSLA---RALEEALEAKEELERTNKQLRAEMEDLVSSKD 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 238 DARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLE-----LKA---KDLQDELAGNSEQRKRLLKERQKL 309
Cdd:pfam01576 675 DVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEvnmqaLKAqfeRDLQARDEQGEEKRRQLVKQVREL 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 310 LEKIEEKQK--------------ELAETEPKFNSVKEKEERGIARLAQATQERTDLY-----AKQGRGSQFTSKEERDKW 370
Cdd:pfam01576 755 EAELEDERKqraqavaakkklelDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQreleeARASRDEILAQSKESEKK 834
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 371 IKKELKSLDQAIND------KKRQIAAIHKDLEDTEAN--KEKNLEQYNK---------LDQDLNEVKARVEELDRKY-- 431
Cdd:pfam01576 835 LKNLEAELLQLQEDlaaserARRQAQQERDELADEIASgaSGKSALQDEKrrleariaqLEEELEEEQSNTELLNDRLrk 914
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958644837 432 --YEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQLLRAATGK 479
Cdd:pfam01576 915 stLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSK 964
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
251-492 |
5.39e-03 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 40.91 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 251 RELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELA-----GNSEQRKRLLKERQKLLEKIEEKQKELaetEP 325
Cdd:pfam18971 559 RNLENKLTAKGLSLQEANKLIKDFLSSNKELAGKALNFNKAVAeakstGNYDEVKKAQKDLEKSLRKREHLEKEV---EK 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 326 KFNSVKEKEERGIARlAQATQERTDLYAKQGRGSqftSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDT--EANK 403
Cdd:pfam18971 636 KLESKSGNKNKMEAK-AQANSQKDEIFALINKEA---NRDARAIAYTQNLKGIKRELSDKLEKISKDLKDFSKSfdEFKN 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 404 EKNlEQYNKLDQDLNEVKARVEELDRKyYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQllRAATGKAILN 483
Cdd:pfam18971 712 GKN-KDFSKAEETLKALKGSVKDLGIN-PEWISKVENLNAALNEFKNGKNKDFSKVTQAKSDLENSVK--DVIINQKVTD 787
|
....*....
gi 1958644837 484 GIDSINKVL 492
Cdd:pfam18971 788 KVDNLNQAV 796
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
244-409 |
5.60e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 40.76 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 244 EDIERQVrELKTKISAMKEEKEQLSAERQEQIKQrtklELKAKdlQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAET 323
Cdd:pfam05262 188 EDNEKGV-NFRRDMTDLKERESQEDAKRAQQLKE----ELDKK--QIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 324 EPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKrqiAAIHKDLEDTEANK 403
Cdd:pfam05262 261 PKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKE---LEAQKKREPVAEDL 337
|
....*.
gi 1958644837 404 EKNLEQ 409
Cdd:pfam05262 338 QKTKPQ 343
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
143-340 |
5.79e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 143 VYDERKEESISLMKETEGKREKINELLKYIEERLHTLEE-------EKEELAQYQKWDKM-RRALEYTIYNQELNETRAK 214
Cdd:PHA02562 221 KYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKlntaaakIKSKIEQFQKVIKMyEKGGVCPTCTQQISEGPDR 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 215 LDELSAKRETSGEKSRQLrdaqQDARDKMEDIERQVRELKTKISAMkeeKEQLSAERQeqikQRTKLELKAKDLQDELag 294
Cdd:PHA02562 301 ITKIKDKLKELQHSLEKL----DTAIDELEEIMDEFNEQSKKLLEL---KNKISTNKQ----SLITLVDKAKKVKAAI-- 367
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958644837 295 nseqrKRLLKERQKLLEKIEEKQKELAET-EPKFNSVKEKEERGIAR 340
Cdd:PHA02562 368 -----EELQAEFVDNAEELAKLQDELDKIvKTKSELVKEKYHRGIVT 409
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1089-1140 |
5.93e-03 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 40.66 E-value: 5.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1958644837 1089 QQLSGGQKSLVALALIFAiqkCDPApFYLFDEIDQALDAQHRKAVSDMIMEL 1140
Cdd:COG1123 141 HQLSGGQRQRVAIAMALA---LDPD-LLIADEPTTALDVTTQAEILDLLREL 188
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1089-1141 |
6.13e-03 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 39.55 E-value: 6.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1958644837 1089 QQLSGGQKSLVALALIFAIQKcdpaPFYLFDEIDQALDAQHRKAVSDMIMELA 1141
Cdd:cd03226 125 LSLSGGQKQRLAIAAALLSGK----DLLIFDEPTSGLDYKNMERVGELIRELA 173
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
230-311 |
6.23e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 40.74 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 230 RQLRDAQQDARDKMED------IERQVRELKtkiSAMKEEKEQLsAERQEQIKQRTK-------LELKAKDLQD------ 290
Cdd:pfam13779 489 RRLRAAQERLSEALERgasdeeIAKLMQELR---EALDDYMQAL-AEQAQQNPQDLQqpddpnaQEMTQQDLQRmldrie 564
|
90 100
....*....|....*....|...
gi 1958644837 291 ELA--GNSEQRKRLLKERQKLLE 311
Cdd:pfam13779 565 ELArsGRRAEAQQMLSQLQQMLE 587
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
167-275 |
6.55e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 167 ELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEytiYNQELNETRAKLDELSAKretsGEKSRQLRDAQQDARDKMEDI 246
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEASFERLAE---LRDELAELEEELEALKAR----WEAEKELIEEIQELKEELEQR 483
|
90 100
....*....|....*....|....*....
gi 1958644837 247 ERQVRELKTKISAMKEEKEQLSAERQEQI 275
Cdd:COG0542 484 YGKIPELEKELAELEEELAELAPLLREEV 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
768-985 |
6.64e-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: 40.13 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 768 EDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNEnLRKRLDQVEQELNELRETeggtvLTATTSELEAINK 847
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-LARRIRALEQELAALEAE-----LAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 848 RVKDTMARSEDLDNSIDKT-EAGIKELQKSMERWKNMEK--EHMDAIN-HDTKELEKMTNRQGMLLKKKEECMKKIRELG 923
Cdd:COG4942 98 ELEAQKEELAELLRALYRLgRQPPLALLLSPEDFLDAVRrlQYLKYLApARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958644837 924 SLPQEAFEKYQTLSLKQLFRK--LEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDR 985
Cdd:COG4942 178 ALLAELEEERAALEALKAERQklLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
191-382 |
6.72e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 40.62 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 191 KWDKMRRALEYTIYNQELN--------ETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVR----ELKTKIS 258
Cdd:PRK00106 25 KMKSAKEAAELTLLNAEQEavnlrgkaERDAEHIKKTAKRESKALKKELLLEAKEEARKYREEIEQEFKserqELKQIES 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 259 AMKEEKEQLSAERQEQIKQRTKLELKAKDLQDelagnseqRKRLLKERQKLLEKIEEKQKELAEtepKFNSVKEKEERGI 338
Cdd:PRK00106 105 RLTERATSLDRKDENLSSKEKTLESKEQSLTD--------KSKHIDEREEQVEKLEEQKKAELE---RVAALSQAEAREI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958644837 339 ArLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAI 382
Cdd:PRK00106 174 I-LAETENKLTHEIATRIREAEREVKDRSDKMAKDLLAQAMQRL 216
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1086-1141 |
6.74e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.56 E-value: 6.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644837 1086 REMQQLSGG--QKSLVALALIfaiqkcDPAPFYLFDEIDQALDAQHRKAVSDMIMELA 1141
Cdd:PRK13409 208 RDISELSGGelQRVAIAAALL------RDADFYFFDEPTSYLDIRQRLNVARLIRELA 259
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1088-1137 |
6.76e-03 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 38.20 E-value: 6.76e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1958644837 1088 MQQLSGGQKSLVALALIFaIQKCDpapFYLFDEIDQALDAQHRKAVSDMI 1137
Cdd:cd03221 68 FEQLSGGEKMRLALAKLL-LENPN---LLLLDEPTNHLDLESIEALEEAL 113
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
168-346 |
6.92e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.46 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 168 LLKYIEERLHTLEEEKEELAQYQK-WDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQL--RDAQQDAR-DKM 243
Cdd:PRK12705 21 LVVLLKKRQRLAKEAERILQEAQKeAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLvqKEEQLDARaEKL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 244 EDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLElkakdlqdelagNSEQRKRLLKERQKLLEkiEEKQKELAET 323
Cdd:PRK12705 101 DNLENQLEEREKALSARELELEELEKQLDNELYRVAGLT------------PEQARKLLLKLLDAELE--EEKAQRVKKI 166
|
170 180
....*....|....*....|...
gi 1958644837 324 EPKFNSVKEKEERGIarLAQATQ 346
Cdd:PRK12705 167 EEEADLEAERKAQNI--LAQAMQ 187
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
149-480 |
7.18e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 149 EESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALeytiyNQELNETRAKLdelsakretsgek 228
Cdd:TIGR00606 234 ESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKD-----NSELELKMEKV------------- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 229 srqLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQK 308
Cdd:TIGR00606 296 ---FQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQS 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 309 LLEKIEEKQKE---LAETEPKfNSVKEKEERGIARLAQATQERTDLYAKQG-RGSQFTSKEERDKWIKKELKSLDQAIND 384
Cdd:TIGR00606 373 LATRLELDGFErgpFSERQIK-NFHTLVIERQEDEAKTAAQLCADLQSKERlKQEQADEIRDEKKGLGRTIELKKEILEK 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 385 KKRQIAAIHKDLEDTEANKEKNLEqynkLDQDLNEVKARVEELDRKYYEVKNKKDE--LQSERNYLWREENAEQQALAAK 462
Cdd:TIGR00606 452 KQEELKFVIKELQQLEGSSDRILE----LDQELRKAERELSKAEKNSLTETLKKEVksLQNEKADLDRKLRKLDQEMEQL 527
|
330
....*....|....*...
gi 1958644837 463 REDLEKKQQLLRAATGKA 480
Cdd:TIGR00606 528 NHHTTTRTQMEMLTKDKM 545
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
674-1023 |
7.85e-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: 40.39 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 674 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKasrdSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTresl 753
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK----SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQ---- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 754 kaelgtdlLSQLSLEDQKRVDALNDEIRQLQQENRQLlneriklegiitrvetylnENLRKRLDQVEQELNELRETEGGT 833
Cdd:TIGR04523 255 --------LNQLKDEQNKIKKQLSEKQKELEQNNKKI-------------------KELEKQLNQLKSEISDLNNQKEQD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 834 VLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKKKE 913
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 914 ECMKKIRELGSLPQEAFEKYQTL-----SLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKrqeELDRGYK 988
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKdeqikKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK---NLDNTRE 464
|
330 340 350
....*....|....*....|....*....|....*
gi 1958644837 989 SIMELMNVLElRKYEAIQLTFKQVSKNFSEVFQKL 1023
Cdd:TIGR04523 465 SLETQLKVLS-RSINKIKQNLEQKQKELKSKEKEL 498
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
646-860 |
8.35e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 646 DTRKSRLELQKDVRKAEEELGELEAKLNENLRRN-IERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQ 724
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEFRQKNgLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 725 SEKT--FMPKQRSLQSLEASLHAMESTRESLKAELGtdllsqlslEDQKRVDALNDEI----RQLQQENRQLLNE-RIKL 797
Cdd:COG3206 252 GPDAlpELLQSPVIQQLRAQLAELEAELAELSARYT---------PNHPDVIALRAQIaalrAQLQQEAQRILASlEAEL 322
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958644837 798 EGIITRVETylnenLRKRLDQVEQELNELRETEggTVLTATTSELEAINKRVKDTMARSEDLD 860
Cdd:COG3206 323 EALQAREAS-----LQAQLAQLEARLAELPELE--AELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
169-273 |
8.37e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 40.05 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 169 LKYIEERLHTLEE------EKEELAQYQKWDKMRRALEytiynqelnetrAKLDELSAKRETSGEKSRQLRDAQQDARDK 242
Cdd:PRK05431 4 IKLIRENPEAVKEalakrgFPLDVDELLELDEERRELQ------------TELEELQAERNALSKEIGQAKRKGEDAEAL 71
|
90 100 110
....*....|....*....|....*....|.
gi 1958644837 243 MEdierQVRELKTKISAMKEEKEQLSAERQE 273
Cdd:PRK05431 72 IA----EVKELKEEIKALEAELDELEAELEE 98
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1086-1148 |
8.49e-03 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 39.24 E-value: 8.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958644837 1086 REMQQLSGGQKSLVALALIFAIQkcdpaPFYL-FDEIDQALDAQHRKAVSDMIMELavHAQFIT 1148
Cdd:COG1122 130 RPPHELSGGQKQRVAIAGVLAME-----PEVLvLDEPTAGLDPRGRRELLELLKRL--NKEGKT 186
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
3-88 |
9.11e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 39.57 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 3 IKQVIIQGFRSYRDQTIvdPFSsKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEqRLALLHIDKEEVSLRRVIGaKK 82
Cdd:COG4938 1 IKSISIKNFGPFKEAEL--ELK-PLTLLIGPNGSGKSTLIQALLLLLQSNFIYLPAE-RSGPARLYPSLVRELSDLG-SR 75
|
....*.
gi 1958644837 83 DQYFLD 88
Cdd:COG4938 76 GEYTAD 81
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
115-439 |
9.24e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 115 VKQGKINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINEllKYIEERLHTLEEEKEELAQYQKWDK 194
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE--KKAAEALKKEAEEAKKAEELKKKEA 1712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 195 mrraleytiynqelnETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRElKTKISAMKEEKEQLSAERQEQ 274
Cdd:PTZ00121 1713 ---------------EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKIAHLKKEEEKKAEEIRKE 1776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 275 IKQRTKLELKAKDLQDELagnseQRKRLLKERQKLLEKIEEKQKelaETEPKFNSVKEKEERGIARLAQATQ---ERTDL 351
Cdd:PTZ00121 1777 KEAVIEEELDEEDEKRRM-----EVDKKIKDIFDNFANIIEGGK---EGNLVINDSKEMEDSAIKEVADSKNmqlEEADA 1848
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 352 YAKQGRGSQFTSKE----ERDKWIKKELKSLDQAINDKKRQIAAIHK-DLEDTEAN---KEKNLEQ-YNKLDQDlnEVKA 422
Cdd:PTZ00121 1849 FEKHKFNKNNENGEdgnkEADFNKEKDLKEDDEEEIEEADEIEKIDKdDIEREIPNnnmAGKNNDIiDDKLDKD--EYIK 1926
|
330
....*....|....*..
gi 1958644837 423 RVEELDRKYYEVKNKKD 439
Cdd:PTZ00121 1927 RDAEETREEIIKISKKD 1943
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
223-321 |
9.58e-03 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 38.65 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 223 ETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKD-------LQDELAGN 295
Cdd:pfam06785 79 ELDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEEqlaekqlLINEYQQT 158
|
90 100
....*....|....*....|....*.
gi 1958644837 296 SEQRKRLLKERQKLLEKIEEKQKELA 321
Cdd:pfam06785 159 IEEQRSVLEKRQDQIENLESKVRDLN 184
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
709-796 |
9.93e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 37.95 E-value: 9.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644837 709 DSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENR 788
Cdd:smart00935 7 QKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQ 86
|
....*...
gi 1958644837 789 QLLNERIK 796
Cdd:smart00935 87 KRQQEELQ 94
|
|
| |
