|
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 ... |
2-1197 |
1.53e-125 |
|
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: 415.52 E-value: 1.53e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 2 YIKQVIIQGFRSYRdQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSD-EFSHLRPEQRLALLHEGTGPRVISAFVEI 80
Cdd:pfam02463 1 YLKRIEIEGFKSYA-KTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGErSAKSLRSERLSDLIHSKSGAFVNSAEVEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 81 IFDNSDNRLPIDKEEVSLRRVIGAKKD-QYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKLL 159
Cdd:pfam02463 80 TFDNEDHELPIDKEEVSIRRRVYRGGDsEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 160 REVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKL 239
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 240 DELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGN 319
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 320 SEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKEL 399
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 400 KSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWR-EENA 478
Cdd:pfam02463 400 KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLkETQL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 479 EQQALAAKREDLEKKQQLLRAATGKAILNGIDSINKVLEHFRRKGINQHVQNGYHGIVMNNFECEPAFYTCVEVTAGNRL 558
Cdd:pfam02463 480 VKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADE 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 559 FYHIVDSDEVSTKILMEFNKMNLPGEVTFLPLNKLDVrdtaypetndaipmisklryNPRFDKAFKHVFGKTLICRSMEV 638
Cdd:pfam02463 560 VEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV--------------------LEIDPILNLAQLDKATLEADEDD 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 639 STQLARAFTMDCITLEGDQVSHRGALTGGYYDTRKSRLELQKDVRKAEEELGELEAKLNENLRRNIERINNEIDQLMNQM 718
Cdd:pfam02463 620 KRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQL 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 719 QQIETQQRKFKASRDSILSEMKMlKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVD 798
Cdd:pfam02463 700 EIKKKEQREKEELKKLKLEAEEL-LADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAE 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 799 ALNDEIRQLQQEnrqllneriKLEGIITRVETYLNENLRKRLDQVEQELNELRETEGGTVLTATTSELEAINKRVKDTMA 878
Cdd:pfam02463 779 EREKTEKLKVEE---------EKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLE 849
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 879 RSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEAFEK-- 956
Cdd:pfam02463 850 KLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAei 929
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 957 ------YQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGYKSIMELMNVLELRKYEAIQ 1030
Cdd:pfam02463 930 llkyeeEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIR 1009
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1031 LTFKQVSKNFSEVFQKLVPggkatlvMKKGDVEGSQSQDEGEGSGEsergsgsqsSVPSVDQFTGVGIRVSFTGKQGEMR 1110
Cdd:pfam02463 1010 AIIEETCQRLKEFLELFVS-------INKGWNKVFFYLELGGSAEL---------RLEDPDDPFSGGIEISARPPGKGVK 1073
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1111 EMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYGVK 1190
Cdd:pfam02463 1074 NLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVT 1153
|
....*...
gi 36031035 1191 F-RNKVSH 1197
Cdd:pfam02463 1154 MvENGVST 1161
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-1192 |
3.28e-102 |
|
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: 350.91 E-value: 3.28e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 2 YIKQVIIQGFRSYRDQTIVdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSH-LRPEQRLALLHEG-TGPRVISAFVE 79
Cdd:TIGR02169 1 YIERIELENFKSFGKKKVI-PFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKaMRAERLSDLISNGkNGQSGNEAYVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 80 IIFDNSDNRLPiDKEEVSLRRVIG--AKKDQYFLDKKMVTKNDVMNLLESAGFSrSNPYYIVKQGKINQMATAPDSQRLK 157
Cdd:TIGR02169 80 VTFKNDDGKFP-DELEVVRRLKVTddGKYSYYYLNGQRVRLSEIHDFLAAAGIY-PEGYNVVLQGDVTDFISMSPVERRK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 158 LLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRA 237
Cdd:TIGR02169 158 IIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALER 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 238 KLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAM--------KEEKEQLSAERQEQIKQRTKLELKA 309
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERSIAEKEREL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 310 KDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQE----RTDLYAKQGRGSQF 385
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEfaetRDELKDYREKLEKL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 386 TSK-----EERDKWIkKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKN 460
Cdd:TIGR02169 398 KREinelkRELDRLQ-EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 461 KKDELQSERNYLWRE-ENAEQQALAAKREdlekkqQLLRAATGKAILNGIDsinkvlehfrrkginqhvqnGYHGIVMNN 539
Cdd:TIGR02169 477 EYDRVEKELSKLQRElAEAEAQARASEER------VRGGRAVEEVLKASIQ--------------------GVHGTVAQL 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 540 FECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLpGEVTFLPLNKLDV--RDTAYPETNDAIPM-ISKLRYN 616
Cdd:TIGR02169 531 GSVGERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKA-GRATFLPLNKMRDerRDLSILSEDGVIGFaVDLVEFD 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 617 PRFDKAFKHVFGKTLICRSMEVSTQLARAFTMdcITLEGDQVSHRGALTGGYYDTRKSRLELQKDVRKAEEELGELEAKL 696
Cdd:TIGR02169 610 PKYEPAFKYVFGDTLVVEDIEAARRLMGKYRM--VTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLK 687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 697 NE--NLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTR 774
Cdd:TIGR02169 688 RElsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARI 767
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 775 ESLKAELGTdllSQLSLEDQKRVDAlNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRL---DQVEQELNELR 851
Cdd:TIGR02169 768 EELEEDLHK---LEEALNDLEARLS-HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEyleKEIQELQEQRI 843
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 852 ETEGGTVltATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGM 931
Cdd:TIGR02169 844 DLKEQIK--SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 932 LLKKKEECMKKIRELGSLPQEAFE-KYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRG 1010
Cdd:TIGR02169 922 LKAKLEALEEELSEIEDPKGEDEEiPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1011 YKSIMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKLvPGGKATLVMKKGDvegsqsqdegegsgesergsgsqssvpsv 1090
Cdd:TIGR02169 1002 RKAILERIEEYEKKKREVFMEAFEAINENFNEIFAEL-SGGTGELILENPD----------------------------- 1051
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1091 DQFTGvGIRVSFTGKQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQF 1170
Cdd:TIGR02169 1052 DPFAG-GLELSAKPKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQF 1130
|
1210 1220
....*....|....*....|..
gi 36031035 1171 ITTTFRPELLESADKFYGVKFR 1192
Cdd:TIGR02169 1131 IVVSLRSPMIEYADRAIGVTMR 1152
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
3-158 |
6.19e-95 |
|
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: 303.80 E-value: 6.19e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 3 IKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPRVISAFVEIIF 82
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEPFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALLHEGSGPSVMSAYVEIIF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 36031035 83 DNSDNRLPIDKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKL 158
Cdd:cd03272 81 DNSDNRFPIDKEEVRLRRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMKQDEQQEM 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-1198 |
1.77e-93 |
|
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: 326.24 E-value: 1.77e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 2 YIKQVIIQGFRSYRDQTIVDpFSSKHNVIVGRNGSGKSNFFYAIQFVLSdefshlrpEQRLALLHEGTGPRVI------- 74
Cdd:TIGR02168 1 RLKKLELAGFKSFADPTTIN-FDKGITGIVGPNGCGKSNIVDAIRWVLG--------EQSAKALRGGKMEDVIfngsetr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 75 ----SAFVEIIFDNSDNRLP-IDKEEVSLRRVIGAKKD-QYFLDKKMVTKNDVMNLLESAGFSRSNpYYIVKQGKINQMA 148
Cdd:TIGR02168 72 kplsLAEVELVFDNSDGLLPgADYSEISITRRLYRDGEsEYFINGQPCRLKDIQDLFLDTGLGKRS-YSIIEQGKISEII 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 149 TAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIY 228
Cdd:TIGR02168 151 EAKPEERRAIFEEAAGISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 229 NQELNETRAKLDELSAKREtsgEKSRQLRDAQQDARDKMEDIErqvrELKTKISAMKEEKEQLSAERQEQIKQRTKLELK 308
Cdd:TIGR02168 231 VLRLEELREELEELQEELK---EAEEELEELTAELQELEEKLE----ELRLEVSELEEEIEELQKELYALANEISRLEQQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 309 AKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLyakqgrgsqftsk 388
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL------------- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 389 EERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKyyEVKNKKDELQSE 468
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK--ELQAELEELEEE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 469 RNYLWREENAEQQALAAKREDLEKKQQLLRAATGKA--ILNGIDSINKVLEHFRRKGI-------NQHVQNGYHGIVMNN 539
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELaqLQARLDSLERLQENLEGFSEgvkallkNQSGLSGILGVLSEL 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 540 FECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILmEFNKMNLPGEVTFLPLNKLDVRDTAYPETNDAIPMISKLR----- 614
Cdd:TIGR02168 529 ISVDEGYEAAIEAALGGRLQAVVVENLNAAKKAI-AFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGvakdl 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 615 --YNPRFDKAFKHVFGKTLICRSMEVSTQLARA--FTMDCITLEGDQVSHRGALTGGYYDTRKSRL-------ELQKDVR 683
Cdd:TIGR02168 608 vkFDPKLRKALSYLLGGVLVVDDLDNALELAKKlrPGYRIVTLDGDLVRPGGVITGGSAKTNSSILerrreieELEEKIE 687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 684 KAEEELGELEAKLNEnLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTF-------MPK 756
Cdd:TIGR02168 688 ELEEKIAELEKALAE-LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELteleaeiEEL 766
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 757 QRSLQSLEASLHAMESTRESLKAELgTDLLSQLSLEDqKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLnENL 836
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQI-EQLKEELKALR-EALDELRAELTLLNEEAANLRERLESLERRIAATERRL-EDL 843
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 837 RKRLDQVEQELNELRE--TEGGTVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKsmerwKNMEKEHmdA 914
Cdd:TIGR02168 844 EEQIEELSEDIESLAAeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES-----KRSELRR--E 916
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 915 INHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQE---AFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFV 991
Cdd:TIGR02168 917 LEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeaeALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYE 996
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 992 NFSEQKEKLIKRQEELDRGYKSIMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKLVPGGKATLVMKKGDvegsqsqDEG 1071
Cdd:TIGR02168 997 ELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRVFPKLFGGGEAELRLTDPE-------DLL 1069
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1072 EgsgesergsgsqssvpsvdqfTGVGIRVSFTGKQgeMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDA 1151
Cdd:TIGR02168 1070 E---------------------AGIEIFAQPPGKK--NQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDD 1126
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....*...
gi 36031035 1152 QHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYGVKFRNK-VSHI 1198
Cdd:TIGR02168 1127 ANVERFANLLKEFSKNTQFIVITHNKGTMEVADQLYGVTMQEKgVSKI 1174
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-1189 |
7.40e-73 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 262.95 E-value: 7.40e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1 MYIKQVIIQGFRSYRDQTIVdPFSSKHNVIVGRNGSGKSNFFYAIQFVL---SdeFSHLRPEQRLALLHEGTGPR--VIS 75
Cdd:COG1196 1 MRLKRLELAGFKSFADPTTI-PFEPGITAIVGPNGSGKSNIVDAIRWVLgeqS--AKSLRGGKMEDVIFAGSSSRkpLGR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 76 AFVEIIFDNSDNRLPIDKEEVSLRRVIGAKKD-QYFLDKKMVTKNDVMNLLESAGFSRsNPYYIVKQGKINQMATAPDSQ 154
Cdd:COG1196 78 AEVSLTFDNSDGTLPIDYDEVTITRRLYRSGEsEYYINGKPCRLKDIQDLFLDTGLGP-ESYSIIGQGMIDRIIEAKPEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 155 RLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNE 234
Cdd:COG1196 157 RRAIIEEAAGISKYKERKEEAERKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 235 TRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQD 314
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 315 ELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTdlyAKQGRGSQFTSKEERdkw 394
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA---EAEEELEELAEELLE--- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 395 IKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWR 474
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 475 EENAEQQALAAKREDLEKKQQLLRAATgkailngidSINKVLEHFRRKGINQHV---QNGYHGIVMNNFECEPAFYTCVE 551
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLL---------EAEADYEGFLEGVKAALLlagLRGLAGAVAVLIGVEAAYEAALE 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 552 VTAGNRLFYHIVDSDEVSTKILmEFNKMNLPGEVTFLPLNKLDVRDTAYPETNDA--IPMISKLRYNPRFDKAFKHVFGK 629
Cdd:COG1196 542 AALAAALQNIVVEDDEVAAAAI-EYLKAAKAGRATFLPLDKIRARAALAAALARGaiGAAVDLVASDLREADARYYVLGD 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 630 TLICRSMEVSTQLARAFTMDciTLEGDQVSHRGALTGGyydtrksrlelqkdvrkaeeelgeleaklnenlrrnierinn 709
Cdd:COG1196 621 TLLGRTLVAARLEAALRRAV--TLAGRLREVTLEGEGG------------------------------------------ 656
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 710 eidqlmNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKtfmpkqrsLQSLEASLHAMESTRESLKAELGTDLLSQL 789
Cdd:COG1196 657 ------SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE--------LELEEALLAEEEEERELAEAEEERLEEELE 722
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 790 SLEDQKRVDALNDEIRQLQQENRQLLNEriklEGIITRVETYLNENLRKRLDQVEQELNELretegGTV-LTAtTSELEA 868
Cdd:COG1196 723 EEALEEQLEAEREELLEELLEEEELLEE----EALEELPEPPDLEELERELERLEREIEAL-----GPVnLLA-IEEYEE 792
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 869 INKRVKDTMARSEDLDNSIDKTEAGIKElqksmerwknmekehmdaINHDTKELekmtnrqgmllkkkeecmkkirelgs 948
Cdd:COG1196 793 LEERYDFLSEQREDLEEARETLEEAIEE------------------IDRETRER-------------------------- 828
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 949 lpqeafekyqtlslkqlfrkleqcntelkkyshvnkkaldqfvnFSEqkeklikrqeeldrgyksimelmnvlelrkyea 1028
Cdd:COG1196 829 --------------------------------------------FLE--------------------------------- 831
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1029 iqlTFKQVSKNFSEVFQKLVPGGKATLVMKKGDvegsqsqdegegsgesergsgsqssvpsvDQF-TGVGIRVSFTGKqg 1107
Cdd:COG1196 832 ---TFDAVNENFQELFPRLFGGGEAELLLTDPD-----------------------------DPLeTGIEIMAQPPGK-- 877
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1108 EMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQ--HRkaVSDMIMELAVHAQFITTTFRPELLESADK 1185
Cdd:COG1196 878 KLQRLSLLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDAnvER--FAELLKEMSEDTQFIVITHNKRTMEAADR 955
|
....
gi 36031035 1186 FYGV 1189
Cdd:COG1196 956 LYGV 959
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1105-1199 |
3.64e-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: 3.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1105 KQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESAD 1184
Cdd:cd03272 149 KQDEQQEMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVAD 228
|
90
....*....|....*
gi 36031035 1185 KFYGVKFRNKVSHID 1199
Cdd:cd03272 229 KFYGVKFRNKVSTID 243
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1062-1197 |
7.48e-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: 7.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1062 VEGSQSQDEGEGSGESERGSGSQSSVPSVDqftgVGI----RVSFTgKQGEMREMqqLSGGQKSLVALALIFAIQKCDPA 1137
Cdd:cd03239 45 VLGGKAAKLRRGSLLFLAGGGVKAGINSAS----VEItfdkSYFLV-LQGKVEQI--LSGGEKSLSALALIFALQEIKPS 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 36031035 1138 PFYLFDEIDQALDAQHRKAVSDMIMELAVH-AQFITTTFRPELLESADKFYGVKFRNKVSH 1197
Cdd:cd03239 118 PFYVLDEIDAALDPTNRRRVSDMIKEMAKHtSQFIVITLKKEMFENADKLIGVLFVHGVST 178
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-85 |
1.02e-30 |
|
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: 119.34 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 3 IKQVIIQGFRSYRDQTIVdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPRVISAFVEIIF 82
Cdd:cd03239 1 IKQITLKNFKSYRDETVV-GGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAGGGVKAGINSASVEITF 79
|
...
gi 36031035 83 DNS 85
Cdd:cd03239 80 DKS 82
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
530-642 |
3.41e-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: 110.01 E-value: 3.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 530 NGYHGIVMNNFECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILmEFNKMNLPGEVTFLPLNKLD--------VRDTAYP 601
Cdd:smart00968 1 PGVLGRVADLISVDPKYETALEAALGGRLQAVVVDTEETAKKAI-EFLKKNRLGRATFLPLDKIKprspagskLREALLP 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 36031035 602 ETNDAIPMISKLRYNPRFDKAFKHVFGKTLICRSMEVSTQL 642
Cdd:smart00968 80 EPGFVGPAIDLVEYDPELRPALEYLLGNTLVVDDLETARRL 120
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1114-1193 |
2.71e-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: 2.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1114 QLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVH-AQFITTTFRPELLESADKFYGVKFR 1192
Cdd:cd03227 77 QLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKgAQVIVITHLPELAELADKLIHIKKV 156
|
.
gi 36031035 1193 N 1193
Cdd:cd03227 157 I 157
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-144 |
5.45e-24 |
|
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: 102.38 E-value: 5.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1 MYIKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLS-DEFSHLRPEQRLALLHEGTGPRVISAFVE 79
Cdd:cd03273 1 MHIKEIILDGFKSYATRTVISGFDPQFNAITGLNGSGKSNILDAICFVLGiTNLSTVRASNLQDLIYKRGQAGITKASVT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 80 IIFDNSD-NRLPIDKE---EVSLRRVIG-AKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKI 144
Cdd:cd03273 81 IVFDNSDkSQSPIGFEnypEITVTRQIVlGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRI 150
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1104-1196 |
1.31e-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: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1104 GKQgeMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESA 1183
Cdd:cd03278 105 GKK--VQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAA 182
|
90
....*....|....
gi 36031035 1184 DKFYGVKFRNK-VS 1196
Cdd:cd03278 183 DRLYGVTMQESgVS 196
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
530-643 |
1.86e-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: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 530 NGYHGIVMNNFECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLpGEVTFLPLNKLDVRDTAYPET--NDAI 607
Cdd:pfam06470 2 KGVLGRLADLIEVDEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKL-GRATFLPLDRLKPRPRRPGADlkGGAG 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 36031035 608 PMISKLRYNPRFDKAFKHVFGKTLICRSMEVSTQLA 643
Cdd:pfam06470 81 PLLDLVEYDDEYRKALRYLLGNTLVVDDLDEALELA 116
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1114-1199 |
3.22e-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: 3.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1114 QLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYGVKFRN 1193
Cdd:cd03273 166 ELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNANVLFRTRFVD 245
|
....*.
gi 36031035 1194 KVSHID 1199
Cdd:cd03273 246 GTSTVT 251
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1110-1198 |
9.59e-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: 81.08 E-value: 9.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1110 REMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAV-HAQFITTTFRPELLESADKFYG 1188
Cdd:cd03275 151 RDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGpNFQFIVISLKEEFFSKADALVG 230
|
90
....*....|...
gi 36031035 1189 VkFRNK---VSHI 1198
Cdd:cd03275 231 V-YRDQecnSSKV 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-503 |
2.11e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 84.73 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFVL-SDEFSHLRPEQRLALLHEGTGPRVISAFVE 79
Cdd:PRK03918 1 MKIEELKIKNFRSHKSSVV--EFDDGINLIIGQNGSGKSSILEAILVGLyWGHGSKPKGLKKDDFTRIGGSGTEIELKFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 80 iiFDNSDNRL--PIDKEEVSLRRVIGAKKDqyfLDKKMVTKNDVMNLLESAGFsrSNPYYIvKQGKINQMATApDSQRLK 157
Cdd:PRK03918 79 --KNGRKYRIvrSFNRGESYLKYLDGSEVL---EEGDSSVREWVERLIPYHVF--LNAIYI-RQGEIDAILES-DESREK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 158 LLREVAGTRVYDERKEESISLMKETEGKREKINELLKY---IEERLHTLEEEKEELAqyqkwdkmrraleytiynQELNE 234
Cdd:PRK03918 150 VVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRtenIEELIKEKEKELEEVL------------------REINE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 235 TRAKLDELSAKRETSGEKSRQLrdaqQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQd 314
Cdd:PRK03918 212 ISSELPELREELEKLEKEVKEL----EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 315 ELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGiarlaqatqertdlyakqgrgsqfTSKEERDKW 394
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL------------------------EEKEERLEE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 395 IKKELKSLDqainDKKRQIAAIHKDLEDTEAnKEKNLEQYNKLDQDLNevkarVEELDRKYYEVKNKKDELQSERNYLwr 474
Cdd:PRK03918 343 LKKKLKELE----KRLEELEERHELYEEAKA-KKEELERLKKRLTGLT-----PEKLEKELEELEKAKEEIEEEISKI-- 410
|
490 500
....*....|....*....|....*....
gi 36031035 475 eeNAEQQALAAKREDLEKKQQLLRAATGK 503
Cdd:PRK03918 411 --TARIGELKKEIKELKKAIEELKKAKGK 437
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
3-129 |
7.66e-16 |
|
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: 78.38 E-value: 7.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 3 IKQVIIQGFRSYRDQTIVDPFSSkHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEG--TGPRVISAFVEI 80
Cdd:cd03275 1 LKRLELENFKSYKGRHVIGPFDR-FTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYRArvGKPDSNSAYVTA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 36031035 81 IFDNSDNrlpidkEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAG 129
Cdd:cd03275 80 VYEDDDG------EEKTFRRIITGGSSSYRINGKVVSLKEYNEELEKIN 122
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
5-82 |
1.01e-15 |
|
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: 75.86 E-value: 1.01e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 36031035 5 QVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPeqrlallHEGTGPRVISAFVEIIF 82
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRR-------RSGVKAGCIVAAVSAEL 71
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1110-1189 |
2.83e-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: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1110 REMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYGV 1189
Cdd:cd03274 123 KNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELADRLVGI 202
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
3-205 |
1.35e-14 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 73.89 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 3 IKQVIIQGFRSYRDQTIVDpFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHlRPEQRLALLHEGTGprviSAFVEIIF 82
Cdd:COG0419 2 LLRLRLENFRSYRDTETID-FDDGLNLIVGPNGAGKSTILEAIRYALYGKARS-RSKLRSDLINVGSE----EASVELEF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 83 DNSDNRlpidkeevslrrvigakkdqyfldkkmvtkndvmnllesagfsrsnpYYIVK-QGKINQMATAPDSQRLKLLRE 161
Cdd:COG0419 76 EHGGKR-----------------------------------------------YRIERrQGEFAEFLEAKPSERKEALKR 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 36031035 162 VAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEE 205
Cdd:COG0419 109 LLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQLSG 152
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1114-1190 |
4.26e-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: 4.26e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 36031035 1114 QLSGGQKSLVALALIFAIQkcdpAPFYLFDEIDQALDAQHRKAVSDMIMELAVH-AQFITTTFRPELLE-SADKFYGVK 1190
Cdd:cd00267 80 QLSGGQRQRVALARALLLN----PDLLLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAElAADRVIVLK 154
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
3-159 |
1.07e-12 |
|
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: 68.26 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 3 IKQVIIQGFRSYRDQTIVdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSH-LRPEQRLALLHEGTGPR--VISAFVE 79
Cdd:cd03278 1 LKKLELKGFKSFADKTTI-PFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKsLRGEKMSDVIFAGSETRkpANFAEVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 80 IIFDNSDNRlpidkeevslrrvigakkdqyfldkkmvtkndvmnllesagfsrsnpYYIVKQGKINQMATAPD--SQRLK 157
Cdd:cd03278 80 LTFDNSDGR-----------------------------------------------YSIISQGDVSEIIEAPGkkVQRLS 112
|
..
gi 36031035 158 LL 159
Cdd:cd03278 113 LL 114
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-89 |
1.37e-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: 70.80 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFS-HLRPEQrlalLHEGTGPRVISAFVE 79
Cdd:COG3593 1 MKLEKIKIKNFRSIKDLSI--ELSDDLTVLVGENNSGKSSILEALRLLLGPSSSrKFDEED----FYLGDDPDLPEIEIE 74
|
90
....*....|
gi 36031035 80 IIFDNSDNRL 89
Cdd:COG3593 75 LTFGSLLSRL 84
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
113-481 |
2.51e-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: 71.31 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 113 KKMVTKNDVMNLLESagFSRSNPYYIVKqgkINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINEL 192
Cdd:pfam17380 234 EKMERRKESFNLAED--VTTMTPEYTVR---YNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEK 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 193 LKYIEERLHTLEEEKEELAQYQKwdkmrralEYTIYnqelnetrAKLDELSAKRETSGEKSRQlrdaqQDARDKMEDIER 272
Cdd:pfam17380 309 AREVERRRKLEEAEKARQAEMDR--------QAAIY--------AEQERMAMERERELERIRQ-----EERKRELERIRQ 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 273 QvrELKTKISAMKEeKEQLSAERQEQiKQRTKLELKAKDLQDELagnSEQRKRLLKERQKLLEKIEEKQKELAETEpkFN 352
Cdd:pfam17380 368 E--EIAMEISRMRE-LERLQMERQQK-NERVRQELEAARKVKIL---EEERQRKIQQQKVEMEQIRAEQEEARQRE--VR 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 353 SVKEKEERGIARLAQATQERTD----------------LYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAI 416
Cdd:pfam17380 439 RLEEERAREMERVRLEEQERQQqverlrqqeeerkrkkLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLL 518
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 417 HKDLED-----TEANKEKNLEQYNKLDQDLNEVKaRVEELDRKYYEVKNKKDELQSERNYLWREENAEQQ 481
Cdd:pfam17380 519 EKEMEErqkaiYEEERRREAEEERRKQQEMEERR-RIQEQMRKATEERSRLEAMEREREMMRQIVESEKA 587
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
139-499 |
3.10e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.22 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 139 VKQGKINQMATAPDSQRLKL---LREVAGTRVYDERKEESislmketegkREKINELLKYIEERLHTLEEEKEELAQYQK 215
Cdd:PRK02224 135 VRQGEVNKLINATPSDRQDMiddLLQLGKLEEYRERASDA----------RLGVERVLSDQRGSLDQLKAQIEEKEEKDL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 216 WDKMRRaleytiYNQELNETRAKLDELSAKRETSGEKSRQLR---DAQQDARDKMEDIERQVRELKTKISAMKEEKEQLS 292
Cdd:PRK02224 205 HERLNG------LESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDLRETIAETEREREELA 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 293 AERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAEtepkfnsvkekeergiARLAQatqer 372
Cdd:PRK02224 279 EEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEE----------------CRVAA----- 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 373 tdlyakqgrgSQFTSKEERdkwIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELD 452
Cdd:PRK02224 338 ----------QAHNEEAES---LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAP 404
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 36031035 453 RKYYEVKNKKDELQSERNYLwREENAEQQA-LAAKREDLEKKQQLLRA 499
Cdd:PRK02224 405 VDLGNAEDFLEELREERDEL-REREAELEAtLRTARERVEEAEALLEA 451
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-495 |
1.45e-11 |
|
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: 69.23 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1 MYIKQVIIQGFRSYRDQTIVDPFSSKHN-VIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPRVISAFVE 79
Cdd:TIGR00618 1 MKPLRLTLKNFGSYKGTHTIDFTALGPIfLICGKTGAGKTTLLDAITYALYGKLPRRSEVIRSLNSLYAAPSEAAFAELE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 80 IIFDNSDNRLPI---------DKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATA 150
Cdd:TIGR00618 81 FSLGTKIYRVHRtlrctrshrKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 151 PDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINE----LLKYIEERLHTLEEEKEELAQYQKwdkmrralEYT 226
Cdd:TIGR00618 161 KSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLrsqlLTLCTPCMPDTYHERKQVLEKELK--------HLR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 227 IYNQELNETRAKLDELSAKRETSGEKSRQLRDAQqdardkmedieRQVRELKTKISAMKEEKEQLSAERQ-----EQIKQ 301
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLR-----------ARIEELRAQEAVLEETQERINRARKaaplaAHIKA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 302 RTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEK---IEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAK 378
Cdd:TIGR00618 302 VTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQqssIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 379 QGRGSQFTSKEERDKWIKKELKSLD----------QAINDKKRQIAAIHKDLedtEANKEKNLEQYNKLDQDLNEVKARV 448
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQSLCKELDILQreqatidtrtSAFRDLQGQLAHAKKQQ---ELQQRYAELCAAAITCTAQCEKLEK 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 36031035 449 EELDRKYYEVKNKKDELQSERNYLWREEnaEQQALAAKREDLEKKQQ 495
Cdd:TIGR00618 459 IHLQESAQSLKEREQQLQTKEQIHLQET--RKKAVVLARLLELQEEP 503
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
169-494 |
1.81e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.01 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 169 DERKEESISLMKETEGKReKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELN---ETRAKLDELSAK 245
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKK-KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKkkaEEAKKADEAKKK 1452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 246 RETSgEKSRQLRDAQQDARdKMEDIERQVRELKTKISAMKEEKEqlSAERQEQIKQRTKLELKAKDLQ--DELAGNSEQR 323
Cdd:PTZ00121 1453 AEEA-KKAEEAKKKAEEAK-KADEAKKKAEEAKKADEAKKKAEE--AKKKADEAKKAAEAKKKADEAKkaEEAKKADEAK 1528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 324 KRLLKERQKLLEKIEEKQKelAETEPKFNSVKEKEERGIARLAQATQERTDLY---------AKQGRGSQFTSKEERDKW 394
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKK--ADELKKAEELKKAEEKKKAEEAKKAEEDKNMAlrkaeeakkAEEARIEEVMKLYEEEKK 1606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 395 IKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQ---DLNEVKARVEELDRKYYEVKNKKDELQSErny 471
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkkAEEENKIKAAEEAKKAEEDKKKAEEAKKA--- 1683
|
330 340
....*....|....*....|...
gi 36031035 472 lwrEENAEQQALAAKREDLEKKQ 494
Cdd:PTZ00121 1684 ---EEDEKKAAEALKKEAEEAKK 1703
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
258-500 |
3.32e-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: 66.71 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 258 DAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKI 337
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 338 EEKQKELAetepkfnsvkekeERGIARLAQATQERTDLYAKQGRGSQFTskeerdkwikKELKSLDQAINDKKRQIAAIH 417
Cdd:COG4942 100 EAQKEELA-------------ELLRALYRLGRQPPLALLLSPEDFLDAV----------RRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 418 KDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKyyevKNKKDELQSErnyLWREENAEQQALAAKREDLEKKQQLL 497
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEAL----KAERQKLLAR---LEKELAELAAELAELQQEAEELEALI 229
|
...
gi 36031035 498 RAA 500
Cdd:COG4942 230 ARL 232
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
170-510 |
3.80e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.86 E-value: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 170 ERKEESISLMKETEGKReKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRETS 249
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEEAK-KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE 1532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 250 GEKSRQLRDAQQ----DARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQ--RTKLELKAKDLQDELAGNSEQR 323
Cdd:PTZ00121 1533 AKKADEAKKAEEkkkaDELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeEARIEEVMKLYEEEKKMKAEEA 1612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 324 KRLLKERQKLLE-KIEEKQKELAETEPKfnsvKEKEERGIARLAQATQERTDLyakqgRGSQFTSKEERDKWIKKELKSL 402
Cdd:PTZ00121 1613 KKAEEAKIKAEElKKAEEEKKKVEQLKK----KEAEEKKKAEELKKAEEENKI-----KAAEEAKKAEEDKKKAEEAKKA 1683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 403 DQainDKKRQIAAIHKDLEdtEANK--------EKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELqsernylwR 474
Cdd:PTZ00121 1684 EE---DEKKAAEALKKEAE--EAKKaeelkkkeAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA--------K 1750
|
330 340 350
....*....|....*....|....*....|....*.
gi 36031035 475 EENAEQQALAAKREDLEKKQQLLRAATGKAILNGID 510
Cdd:PTZ00121 1751 KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
168-503 |
4.76e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.40 E-value: 4.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 168 YDERKEESISLMKETEGKREKINELLKYIEErlhtLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRE 247
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERLEELKKKLKE----LEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 248 TSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEK-------EQLSAERQEQIKQRTKLELkaKDLQDELAgNS 320
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgRELTEEHRKELLEEYTAEL--KRIEKELK-EI 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 321 EQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEER----GIARLAQATQERTDLYAK----QGRGSQFTSKEERD 392
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKlkkyNLEELEKKAEEYEKLKEKliklKGEIKSLKKELEKL 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 393 KWIKKELKSLDQAINDKKRQIAAIHKDLEdteankEKNLEQYNKLDQDLNEvkarVEELDRKYYEVKNKKDELQSERNYL 472
Cdd:PRK03918 552 EELKKKLAELEKKLDELEEELAELLKELE------ELGFESVEELEERLKE----LEPFYNEYLELKDAEKELEREEKEL 621
|
330 340 350
....*....|....*....|....*....|.
gi 36031035 473 WREENaeqqALAAKREDLEKKQQLLRAATGK 503
Cdd:PRK03918 622 KKLEE----ELDKAFEELAETEKRLEELRKE 648
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-500 |
5.21e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.10 E-value: 5.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFshlrpEQRLALLHEGTGPRVISAFVEI 80
Cdd:COG4717 1 MKIKELEIYGFGKFRDRTI--EFSPGLNVIYGPNEAGKSTLLAFIRAMLLERL-----EKEADELFKPQGRKPELNLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 81 ifdnsdnrlpidKEEVSLRRVIGAKKDQYfldkkmvtkndvmnllesagfsrsnpyyivkQGKINQMATApDSQRLKLLR 160
Cdd:COG4717 74 ------------KELEEELKEAEEKEEEY-------------------------------AELQEELEEL-EEELEELEA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 161 EVAGTRVYDERKEESISLmKETEGKREKINELLKYIEERLHTLEEEKEELAQYQ-KWDKMRRALE------YTIYNQELN 233
Cdd:COG4717 110 ELEELREELEKLEKLLQL-LPLYQELEALEAELAELPERLEELEERLEELRELEeELEELEAELAelqeelEELLEQLSL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 234 ETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAmKEEKEQLSAERQ----------------- 296
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA-AALEERLKEARLllliaaallallglggs 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 297 ------------------------EQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKL-------LEKIEEKQKELA 345
Cdd:COG4717 268 llsliltiagvlflvlgllallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppdlsPEELLELLDRIE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 346 ETEPKFNSVKEKEERgiARLAQATQERTDLYAKQGrgsqFTSKEERDKWIK--KELKSLDQAINDKKRQIAAIHKDLED- 422
Cdd:COG4717 348 ELQELLREAEELEEE--LQLEELEQEIAALLAEAG----VEDEEELRAALEqaEEYQELKEELEELEEQLEELLGELEEl 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 36031035 423 -TEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYlwREENAEQQALAAKREDLEKKQQLLRAA 500
Cdd:COG4717 422 lEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL--AELLQELEELKAELRELAEEWAALKLA 498
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
3-181 |
1.64e-10 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 64.18 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 3 IKQVIIQGFRSYRDQTI-VDPFsskhNVIVGRNGSGKSNFFYAIQF---------------------VLSDEFSHLRPEQ 60
Cdd:COG4637 2 ITRIRIKNFKSLRDLELpLGPL----TVLIGANGSGKSNLLDALRFlsdaargglqdalarrggleeLLWRGPRTITEPI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 61 RLALLHEGTGPRVISAFVEIIFDNSDNRLPIDKEEVSLRRviGAKKDQYFLDKKMVTknDVMNLLESAGFSRSnpyyivk 140
Cdd:COG4637 78 RLELEFAEEDERDLRYELELGLPEPGGRPEVKEERLWLKR--GSGGRPFLDFRPKGR--AVGGEPERLDSPES------- 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 36031035 141 qgKINQMATAPDSQRLKLLRE-VAGTRVYDERkeesISLMKE 181
Cdd:COG4637 147 --LLSQLGDPERFPELRALREaLRSWRFYDFH----PAPLRQ 182
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
262-903 |
2.33e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.32 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 262 DARDKMEDIERQVRELkTKISAMKEEKEQLSAERQEQIKQRTKLELKAkdlqdelagnSEQRKRLLKERqkllekIEEKQ 341
Cdd:COG4913 239 RAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWF----------AQRRLELLEAE------LEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 342 KELAETEpkfnsvkEKEERGIARLAQATQERTDLYAKQgRGSQFTSKEErdkwIKKELKSLDQAINDKKRQIAAIHKDLE 421
Cdd:COG4913 302 AELARLE-------AELERLEARLDALREELDELEAQI-RGNGGDRLEQ----LEREIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 422 D----TEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERnylwREENAEQQALAAKREDLEKKQQLL 497
Cdd:COG4913 370 AlglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL----RELEAEIASLERRKSNIPARLLAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 498 RAATGKAIlnGIDSIN--------KVLEHFRRkginqhvqngyhgivmnnfeCEPAfytcVEVTAGNRLFYHIVDS---D 566
Cdd:COG4913 446 RDALAEAL--GLDEAElpfvgeliEVRPEEER--------------------WRGA----IERVLGGFALTLLVPPehyA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 567 EVSTKIlmefNKMNLPGEVTFLPLNKLDVRDTAYPETNDAIPmiSKLRYNPrfdkafkHVFGktlicrsMEVSTQLARAF 646
Cdd:COG4913 500 AALRWV----NRLHLRGRLVYERVRTGLPDPERPRLDPDSLA--GKLDFKP-------HPFR-------AWLEAELGRRF 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 647 TMDC-------------ITLEGdQVSHRGALtgGYYDTRK---SRLELQKDVRKAEeelgeleaklnENLRRNIERINNE 710
Cdd:COG4913 560 DYVCvdspeelrrhpraITRAG-QVKGNGTR--HEKDDRRrirSRYVLGFDNRAKL-----------AALEAELAELEEE 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 711 IDQLMNQMQQIETQQRKFKASRDSIlsemkmlkekRQQSEKTFMpkQRSLQSLEASLHAMESTRESLKAelgtdllsqls 790
Cdd:COG4913 626 LAEAEERLEALEAELDALQERREAL----------QRLAEYSWD--EIDVASAEREIAELEAELERLDA----------- 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 791 leDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVEtylnenlrKRLDQVEQELNELRETEGGTVLTATTSELEAIN 870
Cdd:COG4913 683 --SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE--------KELEQAEEELDELQDRLEAAEDLARLELRALLE 752
|
650 660 670
....*....|....*....|....*....|....*....
gi 36031035 871 KRVKDTMAR------SEDLDNSIDKTEAGIKELQKSMER 903
Cdd:COG4913 753 ERFAAALGDaverelRENLEERIDALRARLNRAEEELER 791
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1-151 |
2.52e-10 |
|
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: 61.54 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1 MYIKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTG-PRVISAFVE 79
Cdd:cd03274 1 LIITKLVLENFKSYAGEQVIGPFHKSFSAIVGPNGSGKSNVIDSMLFVFGFRASKMRQKKLSDLIHNSAGhPNLDSCSVE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 36031035 80 IIFdnsdnrlpidkeevslrrvigakkdQYFLDKKmvtkndvmnLLESAGFSRSNPYYIVKQGKINQMATAP 151
Cdd:cd03274 81 VHF-------------------------QEIIDKP---------LLKSKGIDLDHNRFLILQGEVEQIAQMP 118
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
182-467 |
5.60e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.91 E-value: 5.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 182 TEGKREKINELlkyiEERLHTLEEEKEELAQyqkwdKMRRAleytiynQELNETRAKLDELSAKRETSGEKsrqlrdaqq 261
Cdd:PRK02224 470 IEEDRERVEEL----EAELEDLEEEVEEVEE-----RLERA-------EDLVEAEDRIERLEERREDLEEL--------- 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 262 dardkMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAgNSEQRKRLLKERQKLLEKIEEKQ 341
Cdd:PRK02224 525 -----IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVA-ELNSKLAELKERIESLERIRTLL 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 342 KELAETEPKFNSVKEKEErgiARLAQATQERTDLYAKQGRGSQFTSK--EERDKWIKKELKSLDQAI---NDKKRQIAAI 416
Cdd:PRK02224 599 AAIADAEDEIERLREKRE---ALAELNDERRERLAEKRERKRELEAEfdEARIEEAREDKERAEEYLeqvEEKLDELREE 675
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 36031035 417 HKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVknkkDELQS 467
Cdd:PRK02224 676 RDDLQAEIGAVENELEELEELRERREALENRVEALEALYDEA----EELES 722
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-191 |
6.81e-10 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 59.82 E-value: 6.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 6 VIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLH---EGTGPRVISAFVEIIF 82
Cdd:pfam13476 1 LTIENFRSFRDQTI--DFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKgdiRIGLEGKGKAYVEITF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 83 DNSDNR-LPIDKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYI-VKQGKINQMATAPDSQRLKLLR 160
Cdd:pfam13476 79 ENNDGRyTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVfLGQEREEEFERKEKKERLEELE 158
|
170 180 190
....*....|....*....|....*....|.
gi 36031035 161 EVAGTRVYDERKEESISLMKETEGKREKINE 191
Cdd:pfam13476 159 KALEEKEDEKKLLEKLLQLKEKKKELEELKE 189
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
150-494 |
9.08e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 9.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 150 APDSQRLKLLREVAGTRVYDE-RKEESISLMKETEGKRE---KINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEY 225
Cdd:PTZ00121 1274 AEEARKADELKKAEEKKKADEaKKAEEKKKADEAKKKAEeakKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE 1353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 226 TIYNQ-ELNETRAKLDELSA-----KRETSGEKSRQLRDAQQdARDKMEDIERQVRELKTKISAMKEEKEqlSAERQEQI 299
Cdd:PTZ00121 1354 AAADEaEAAEEKAEAAEKKKeeakkKADAAKKKAEEKKKADE-AKKKAEEDKKKADELKKAAAAKKKADE--AKKKAEEK 1430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 300 KQRTKLELKAKDLQ--DELAGNSEQRKRLLKERQKLLEKIE-EKQKELAETEPKFNSVKEKEERGIARLAQATQ-ERTDL 375
Cdd:PTZ00121 1431 KKADEAKKKAEEAKkaDEAKKKAEEAKKAEEAKKKAEEAKKaDEAKKKAEEAKKADEAKKKAEEAKKKADEAKKaAEAKK 1510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 376 YAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELD--- 452
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkae 1590
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 36031035 453 --RKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQ 494
Cdd:PTZ00121 1591 eaRIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK 1634
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
180-387 |
1.05e-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: 61.70 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 180 KETEGKREKINELLKYIEERLHTLEEEKEELA-QYQKWDKMRRALEYTI--YNQELNETRAKLDELSAKRETSGEK---- 252
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLkQLAALERRIAALARRIraLEQELAALEAELAELEKEIAELRAEleaq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 253 ----SRQLRDAQQDAR----------DKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAG 318
Cdd:COG4942 103 keelAELLRALYRLGRqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 36031035 319 NSEQRKRL---LKERQKLLEKIE----EKQKELAEtepkfnsvKEKEERGIARLAQATQERTDLYAKQGRGSQFTS 387
Cdd:COG4942 183 LEEERAALealKAERQKLLARLEkelaELAAELAE--------LQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
229-454 |
2.48e-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: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 229 NQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELK 308
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 309 AKDLQDELAG-------NSEQR---------------------KRLLKERQKLLEKIEEKQKELAETEpkfnsvkekeer 360
Cdd:COG4942 99 LEAQKEELAEllralyrLGRQPplalllspedfldavrrlqylKYLAPARREQAEELRADLAELAALR------------ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 361 giARLAQATQERTDLYAKQgrgsqftskeerdkwiKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQD 440
Cdd:COG4942 167 --AELEAERAELEALLAEL----------------EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
250
....*....|....
gi 36031035 441 LNEVKARVEELDRK 454
Cdd:COG4942 229 IARLEAEAAAAAER 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
170-517 |
2.54e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.59 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 170 ERKEESISLMKETEGKREKINELLKYIEERLHTLEE---EKEELAQyQKWDKMRRALEYtiyNQELNETRAK-------- 238
Cdd:PRK02224 234 ETRDEADEVLEEHEERREELETLEAEIEDLRETIAEterEREELAE-EVRDLRERLEEL---EEERDDLLAEaglddada 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 239 ------LDELSAKRETSGEKSRQLRDAQQDA-------RDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKL 305
Cdd:PRK02224 310 eavearREELEDRDEELRDRLEECRVAAQAHneeaeslREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 306 ELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQAT-----QERTDlyakQG 380
Cdd:PRK02224 390 EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgQPVEG----SP 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 381 RGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIhKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKN 460
Cdd:PRK02224 466 HVETIEEDRERVEELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE 544
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 36031035 461 KKDELQSErnylwrEENAEQQAlAAKREDLEKKQQLLRAATGK--AILNGIDSINKVLE 517
Cdd:PRK02224 545 RAAELEAE------AEEKREAA-AEAEEEAEEAREEVAELNSKlaELKERIESLERIRT 596
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
8-524 |
2.69e-09 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 61.29 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 8 IQGFRSYRDQTIVDPFSSKhNVIVGRNGSGK---SNFFYAIQfvLSDEFSHLRPEQRLALLHEGTGPRVI---SAFVEII 81
Cdd:COG4694 8 LKNVGAFKDFGWLAFFKKL-NLIYGENGSGKstlSRILRSLE--LGDTSSEVIAEFEIEAGGSAPNPSVRvfnRDFVEEN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 82 FDNSDNRLPI---DKEEVSLRRVIGAKKDQyfLDKKMVTKNDVMNLLESAgfsrsnpyyivkqgkinqmatapDSQRLKL 158
Cdd:COG4694 85 LRSGEEIKGIftlGEENIELEEEIEELEKE--IEDLKKELDKLEKELKEA-----------------------KKALEKL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 159 LREVAGTRVyderkeESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAK 238
Cdd:COG4694 140 LEDLAKSIK------DDLKKLFASSGRNYRKANLEKKLSALKSSSEDELKEKLKLLKEEEPEPIAPITPLPDLKALLSEA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 239 LDELSAKRETSGEKsrQLRDAQQDardkmEDIERQVRELKTKISAMKEEK----EQ-LSAERQEQIKQRtklelkakdLQ 313
Cdd:COG4694 214 ETLLEKSAVSSAIE--ELAALIQN-----PGNSDWVEQGLAYHKEEEDDTcpfcQQeLAAERIEALEAY---------FD 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 314 DELAGNSEQRKRLLKERQKLLEKIEEkqKELAETEPKFNSVKEKEERGIARLAQATQE-RTDLYAKQGRGSQFTSKEERD 392
Cdd:COG4694 278 DEYEKLLAALKDLLEELESAINALSA--LLLEILRTLLPSAKEDLKAALEALNALLETlLAALEEKIANPSTSIDLDDQE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 393 KW--IKKELKSLDQAINDKKRQIAaihkDLEDTEANKEKNLEQY--NKLDQDLNEVKARVEELDRKYYEVKNKKDELQSe 468
Cdd:COG4694 356 LLdeLNDLIAALNALIEEHNAKIA----NLKAEKEEARKKLEAHelAELKEDLSRYKAEVEELIEELKTIKALKKALED- 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 36031035 469 rnylwreenaeqqaLAAKREDLEKKQqllraatgKAILNGIDSINKVLEHFRRKGI 524
Cdd:COG4694 431 --------------LKTEISELEAEL--------SSVDEAADEINEELKALGFDEF 464
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-472 |
4.48e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 61.07 E-value: 4.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1 MYIKQVIIQGFRSYRDQTIVdpFSSKHNVIVGRNGSGKSNFFYAIQFVLsdeFSHLRPEQRLALLHEGTGPRVISAFVEI 80
Cdd:PRK01156 1 MIIKRIRLKNFLSHDDSEIE--FDTGINIITGKNGAGKSSIVDAIRFAL---FTDKRTEKIEDMIKKGKNNLEVELEFRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 81 IFDNSDNRLPIDKEEVSLRRVIGAKKDQYFLDKKMvtkNDVMNLLESAGFSRSNPYYI----VKQGKINQMATAPDSQRL 156
Cdd:PRK01156 76 GGHVYQIRRSIERRGKGSRREAYIKKDGSIIAEGF---DDTTKYIEKNILGISKDVFLnsifVGQGEMDSLISGDPAQRK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 157 KLLREVAG----TRVYDERKEESISLMKETEGKREKINELLKYIEErlhtLEEEKEELAQYQKW------DKMRRALEYT 226
Cdd:PRK01156 153 KILDEILEinslERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLE----LENIKKQIADDEKShsitlkEIERLSIEYN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 227 IYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDardkMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLE 306
Cdd:PRK01156 229 NAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESD----LSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 307 lkakdlqdelaGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEErgiaRLAQATQERTDLYAKQGR-GSQF 385
Cdd:PRK01156 305 -----------NDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKS----RYDDLNNQILELEGYEMDyNSYL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 386 TSKEERDKWIKKELKsldqainDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDEL 465
Cdd:PRK01156 370 KSIESLKKKIEEYSK-------NIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDEL 442
|
....*..
gi 36031035 466 QSERNYL 472
Cdd:PRK01156 443 SRNMEML 449
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1101-1171 |
6.28e-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: 6.28e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 36031035 1101 SF-TGKQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELA---VHAQFI 1171
Cdd:cd03276 95 SFlTSNKAAVRDVKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAkkqPGRQFI 169
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
261-520 |
6.97e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 6.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 261 QDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKL---------ELKAKDLQDELAGNSEQRKRLLK--- 328
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdEIDVASAEREIAELEAELERLDAssd 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 329 ERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEER---DKWIKKELksLDQA 405
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRallEERFAAAL--GDAV 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 406 INDKKRQIAAIHKDLEDTEANKEKNLEqyNKLDQDLNEVKARVEELDrkyyevknkkDELQSERNYLWREENAEQQALAA 485
Cdd:COG4913 764 ERELRENLEERIDALRARLNRAEEELE--RAMRAFNREWPAETADLD----------ADLESLPEYLALLDRLEEDGLPE 831
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 36031035 486 KREDLekKQQLLRAATG-------------KAILNGIDSINKVLEHFR 520
Cdd:COG4913 832 YEERF--KELLNENSIEfvadllsklrraiREIKERIDPLNDSLKRIP 877
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
166-469 |
9.18e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 9.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 166 RVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKE----------ELAQYQKWDKMRRaleytiYNQELNET 235
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrELTEEHRKELLEE------YTAELKRI 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 236 RAKLDELSAKRETSGEKSRQLRDAQQDARD--KMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRT-KLELKAKDL 312
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiKLKGEIKSL 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 313 QDELagnsEQRKRLLKERQKLLEKIEEKQKELAETEPK-----FNSVKEKEERgIARLAQATQERTDLyakQGRGSQFTS 387
Cdd:PRK03918 545 KKEL----EKLEELKKKLAELEKKLDELEEELAELLKEleelgFESVEELEER-LKELEPFYNEYLEL---KDAEKELER 616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 388 KEERDKWIKKELKSLDQAINDKKRQIAAIHKDLED-----TEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKK 462
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELAETEKRLEELRKELEElekkySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTL 696
|
....*..
gi 36031035 463 DELQSER 469
Cdd:PRK03918 697 EKLKEEL 703
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-336 |
1.26e-08 |
|
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: 58.76 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPrvisafVEI 80
Cdd:pfam13175 1 MKIKSIIIKNFRCLKDTEI--DLDEDLTVLIGKNNSGKSSILEALDIFLNNKEKFFEDDFLVLYLKDVIKI------DKE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 81 IFDNSDNRLPIDKEEVSLrrvigakkdqYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKInqmATAPDSQRLKLLR 160
Cdd:pfam13175 73 DLNIFENISFSIDIEIDV----------EFLLILFGYLEIKKKYLCLASKGKAKEYEKTLHPKG---ANKADLLLELKIS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 161 EVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQE--LNETRAK 238
Cdd:pfam13175 140 DLKKYLKQFKIYIYNNYYLDEKKNVFDKKSKYELPSLKEEFLNSEKEEIKVDKEDLKKLINELEKSINYHEnvLENLQIK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 239 LDELSAKRETSGEKSRQLRDA-----QQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKlelkaKDLQ 313
Cdd:pfam13175 220 KLLISADRNASDEDSEKINSLlgalkQRIFEEALQEELELTEKLKETQNKLKEIDKTLAEELKNILFKKID-----KLKD 294
|
330 340
....*....|....*....|...
gi 36031035 314 DELAGNSEQRKRLLKERQKLLEK 336
Cdd:pfam13175 295 FGYPPFLNPEIEIKKDDEDLPLN 317
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
186-497 |
1.58e-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: 59.36 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 186 REKINELLKYIEERLHTLEEeKEELAQYQKwDKMRRALEyTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARD 265
Cdd:pfam15921 266 QDRIEQLISEHEVEITGLTE-KASSARSQA-NSIQSQLE-IIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYED 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 266 KMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKER-------QKLLEKIE 338
Cdd:pfam15921 343 KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDtgnsitiDHLRRELD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 339 EKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAK-QGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAaih 417
Cdd:pfam15921 423 DRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKvSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVS--- 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 418 kDLEDTEANKEKNLEQYNkldQDLNEVKARVEELDRKYYEVKNKKDEL---QSERNYLWREENAEQQALAAKREDLEKKQ 494
Cdd:pfam15921 500 -DLTASLQEKERAIEATN---AEITKLRSRVDLKLQELQHLKNEGDHLrnvQTECEALKLQMAEKDKVIEILRQQIENMT 575
|
...
gi 36031035 495 QLL 497
Cdd:pfam15921 576 QLV 578
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
180-387 |
2.41e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.53 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 180 KETEGKREKINELLKYIEERLHTLEEEKEELAQyqKWDKMRRALEYTiyNQELNETRAKLDELSAKRETSGEK-SRQLRD 258
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNE--EYNELQAELEAL--QAEIDKLQAEIAEAEAEIEERREElGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 259 AQQ------------------DARDKMEDIER-------QVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQ 313
Cdd:COG3883 95 LYRsggsvsyldvllgsesfsDFLDRLSALSKiadadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 36031035 314 DELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTS 387
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-65 |
2.82e-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: 2.82e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 36031035 1 MYIKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALL 65
Cdd:COG3950 1 MRIKSLTIENFRGFEDLEIDFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLL 65
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
186-456 |
4.92e-08 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 57.24 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 186 REKINELLKYIEER--LHtLEEEKEELAQyqkwDKMRRALEYTIynqELNETRAKLDELSAKRETSGE-----KSRQLRD 258
Cdd:PRK05771 15 KSYKDEVLEALHELgvVH-IEDLKEELSN----ERLRKLRSLLT---KLSEALDKLRSYLPKLNPLREekkkvSVKSLEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 259 AQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERqEQIKQRTKLELKAKDLQDElaGNSEQRKRLLKERQKLLEKIE 338
Cdd:PRK05771 87 LIKDVEEELEKIEKEIKELEEEISELENEIKELEQEI-ERLEPWGNFDLDLSLLLGF--KYVSVFVGTVPEDKLEELKLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 339 EKQKELAETEPKFNSV-------KEKEERGIARLAQATQERTDLYAKQgrgsqfTSKEERDKwIKKELKSLDQAINDKKR 411
Cdd:PRK05771 164 SDVENVEYISTDKGYVyvvvvvlKELSDEVEEELKKLGFERLELEEEG------TPSELIRE-IKEELEEIEKERESLLE 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 36031035 412 QIAAIHKDLEDTEankeknLEQYNKLDQDLNEVKARVEELDRKYY 456
Cdd:PRK05771 237 ELKELAKKYLEEL------LALYEYLEIELERAEALSKFLKTDKT 275
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
150-450 |
4.99e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 150 APDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEytiyn 229
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE----- 1657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 230 qelnETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQ------VRELKTKISAMKEEKEQLSAERQE---QIK 300
Cdd:PTZ00121 1658 ----ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEaeeakkAEELKKKEAEEKKKAEELKKAEEEnkiKAE 1733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 301 QRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKfnSVKEKEERGIARLAQATQERTDLYA--- 377
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE--ELDEEDEKRRMEVDKKIKDIFDNFAnii 1811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 378 ---KQGRGSQFTSKEERDKWIKKELKSLDQAIND----KKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEE 450
Cdd:PTZ00121 1812 eggKEGNLVINDSKEMEDSAIKEVADSKNMQLEEadafEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIE 1891
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
230-371 |
5.43e-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: 54.93 E-value: 5.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 230 QELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKIsamkEEKEQLSAERQEQIKQ-RTKLELK 308
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI----EEVEARIKKYEEQLGNvRNNKEYE 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 36031035 309 AkdLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQE 371
Cdd:COG1579 93 A--LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-57 |
5.49e-08 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 56.32 E-value: 5.49e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 36031035 1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFvlsdeFSHLR 57
Cdd:PRK00064 1 MYLTRLSLTDFRNYEELDL--ELSPGVNVLVGENGQGKTNLLEAIYL-----LAPGR 50
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
170-461 |
1.08e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 54.92 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 170 ERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQyqkwdkMRRALeytiyNQELNETRAKLDELSAKRETS 249
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAE------KRDEL-----NAQVKELREEAQELREKRDEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 250 GEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDE--LAGNSEQRKRLL 327
Cdd:COG1340 70 NEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEkeLVEKIKELEKEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 328 KERQKLLEKIEEKQKELAETEPKFNSVKEKEERgIARLAQATQERTDLYAKQgrgsqftsKEERDKwIKKELKSLDQAIN 407
Cdd:COG1340 150 EKAKKALEKNEKLKELRAELKELRKEAEEIHKK-IKELAEEAQELHEEMIEL--------YKEADE-LRKEADELHKEIV 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 36031035 408 DKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVK--ARVEELDRKYYEVKNK 461
Cdd:COG1340 220 EAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKreKEKEELEEKAEEIFEK 275
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
186-374 |
1.11e-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: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 186 REKInELLKYIEERLHTLEEEKEELAQyqkWDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARD 265
Cdd:COG4913 248 REQI-ELLEPIRELAERYAAARERLAE---LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALRE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 266 KMEDIERQVR--------ELKTKISAMKEEKEQLSAERQEQIKQRTKLELKA------------------KDLQDELAGN 319
Cdd:COG4913 324 ELDELEAQIRgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLpasaeefaalraeaaallEALEEELEAL 403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 36031035 320 SEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTD 374
Cdd:COG4913 404 EEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEA 458
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
186-459 |
1.23e-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: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 186 REKINEL---LKYIEERLHTLEEEKEEL-AQYQKWDKMRRAL----EYTIYNQELNETRAKLDELSAKR---ETSGEKSR 254
Cdd:COG4913 609 RAKLAALeaeLAELEEELAEAEERLEALeAELDALQERREALqrlaEYSWDEIDVASAEREIAELEAELerlDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 255 QLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQE---------QIKQRTKLELKAKDLQDELAGNSEQ--R 323
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDElqdrleaaeDLARLELRALLEERFAAALGDAVERelR 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 324 KRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERG-----------IARLAQatQERTDLYAKQGR-GSQFTSKEER 391
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAMRAFNREWPAETADldadleslpeyLALLDR--LEEDGLPEYEERfKELLNENSIE 846
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 36031035 392 DkwiKKELKS-LDQAINDKKRQIAAIHKDLEDTEANKEKNL---------EQYNKLDQDLNEVKARVEELDRKYYEVK 459
Cdd:COG4913 847 F---VADLLSkLRRAIREIKERIDPLNDSLKRIPFGPGRYLrlearprpdPEVREFRQELRAVTSGASLFDEELSEAR 921
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
3-214 |
2.12e-07 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 54.28 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 3 IKQVIIQGFRSYRDQTIVDPFSSKH-----NVIVGRNGSGKSNFFYAIQFVLS-DEFSHLRPEQRLALLHEGTGPRVISA 76
Cdd:COG1106 2 LISFSIENFRSFKDELTLSMVASGLrllrvNLIYGANASGKSNLLEALYFLRNlVLNSSQPGDKLVEPFLLDSESKNEPS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 77 FVEIIFDNSDNRLPIdKEEVSLRRVIgaKKDQYFLdkkmvtkndvmnlleSAGFSRSNPYYIvkqgkinqmatapdsqrl 156
Cdd:COG1106 82 EFEILFLLDGVRYEY-GFELDKERII--SEWLYFL---------------STAAQLNVPLLS------------------ 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 36031035 157 KLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIE---ERLHTLEEEKEELAQYQ 214
Cdd:COG1106 126 PLYDWFDNNISLDTSSDGLTLLLKEDESLKEELLELLKIADpgiEDIEVEEEEIEDLVERK 186
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
287-504 |
2.91e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 287 EKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEpkfNSVKEKEERgIARLA 366
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREE-LGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 367 QATQER----------------TDLYAKQGRGSQFTskeERDKWIKKELKSLDQAINDKKRQIAaihKDLEDTEANKEKN 430
Cdd:COG3883 93 RALYRSggsvsyldvllgsesfSDFLDRLSALSKIA---DADADLLEELKADKAELEAKKAELE---AKLAELEALKAEL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 36031035 431 LEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQLLRAATGKA 504
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
183-375 |
3.17e-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: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 183 EGKREKINELLKYIEERLHTLEEEKEE----LAQY-QKWDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLR 257
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEaeaaLEEFrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 258 DAQQDARDKMEDIERQVRelktkISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAgnsEQRKRLLKERQKLLEKI 337
Cdd:COG3206 247 AQLGSGPDALPELLQSPV-----IQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIA---ALRAQLQQEAQRILASL 318
|
170 180 190
....*....|....*....|....*....|....*...
gi 36031035 338 EEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDL 375
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRL 356
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
172-498 |
3.51e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.80 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 172 KEESISLMKEtegKREKINELLKYIEERLHTLEEEKEELAQ--------YQKWDKMRRALEYTiyNQELNETrakLDELS 243
Cdd:pfam01576 10 KEEELQKVKE---RQQKAESELKELEKKHQQLCEEKNALQEqlqaetelCAEAEEMRARLAAR--KQELEEI---LHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 244 AKRETSGEKSRQLRDAQQDARDKMEDIERQVRElktkisamkEEkeqlsAERQEQIKQRTKLELKAKDLQDELAGNSEQR 323
Cdd:pfam01576 82 SRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE---------EE-----AARQKLQLEKVTTEAKIKKLEEDILLLEDQN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 324 KRLLKERQKLLEKIEEKQKELAETEPK---FNSVKEKEERGIA----RLAQATQERTDLyAKQGRGSQFTSKEERDkwik 396
Cdd:pfam01576 148 SKLSKERKLLEERISEFTSNLAEEEEKaksLSKLKNKHEAMISdleeRLKKEEKGRQEL-EKAKRKLEGESTDLQE---- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 397 kELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELdrkyyevknkKDELQSERNYlwrEE 476
Cdd:pfam01576 223 -QIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISEL----------QEDLESERAA---RN 288
|
330 340
....*....|....*....|..
gi 36031035 477 NAEQQalaakREDLEKKQQLLR 498
Cdd:pfam01576 289 KAEKQ-----RRDLGEELEALK 305
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
143-505 |
3.94e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 143 KINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRA 222
Cdd:PTZ00121 1213 KAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 223 LEYtiynqELNETRAKLDELSAKRETSgEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQR 302
Cdd:PTZ00121 1293 DEA-----KKAEEKKKADEAKKKAEEA-KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 303 TKLELK---AKDLQDELAGNSEQRKR---LLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLY 376
Cdd:PTZ00121 1367 EAAEKKkeeAKKKADAAKKKAEEKKKadeAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA 1446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 377 AKQGRGSQFTSKEERDKWIKKELKSLDQ-----------------AINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQ 439
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEakkkaeeakkadeakkkAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 36031035 440 DLNEVKARVEELDRKYYEVKnKKDELQSERNYLWREEnaEQQALAAKREDLEKKQQLLRAATGKAI 505
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKK-KADELKKAEELKKAEE--KKKAEEAKKAEEDKNMALRKAEEAKKA 1589
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
169-464 |
4.34e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 169 DERKEESISLMKETEGKREKINELLKYiEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELsakrET 248
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKKESELIKL-KELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSL----KK 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 249 SGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLK 328
Cdd:PRK03918 547 ELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEE 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 329 ERQKLLEKIEEKQKELAETEPKFNSVKEKeergiarlaqatqertdlYAKQgrgsQFTSKEERDKWIKKELKSLDQAIND 408
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKK------------------YSEE----EYEELREEYLELSRELAGLRAELEE 684
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 36031035 409 KKRQIAAIHKDLEDTEANKEKnLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDE 464
Cdd:PRK03918 685 LEKRREEIKKTLEKLKEELEE-REKAKKELEKLEKALERVEELREKVKKYKALLKE 739
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
170-453 |
4.80e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 170 ERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAqyqkwdkmrraleytiynqelnETRAKLDELSAKRETS 249
Cdd:PRK02224 499 ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAE----------------------ELRERAAELEAEAEEK 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 250 GEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLsAERQEQIKQRTKLELKAKDLQDElagNSEQRKRL--L 327
Cdd:PRK02224 557 REAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLL-AAIADAEDEIERLREKREALAEL---NDERRERLaeK 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 328 KERQKLLE------KIEEKQKELAETEPKFNSVKEKeergiarLAQATQERTDLYAKQGRgsqftskeerdkwIKKELKS 401
Cdd:PRK02224 633 RERKRELEaefdeaRIEEAREDKERAEEYLEQVEEK-------LDELREERDDLQAEIGA-------------VENELEE 692
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 36031035 402 LDqAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNevKARVEELDR 453
Cdd:PRK02224 693 LE-ELRERREALENRVEALEALYDEAEELESMYGDLRAELR--QRNVETLER 741
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
166-457 |
5.44e-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: 54.07 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 166 RVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETR-AKLDELSA 244
Cdd:pfam12128 657 RLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALdAQLALLKA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 245 KREtsgeKSRQLRDAQQDA---------------RDKMEDIERQVRELKTKISAMKEEK-----------EQLSAERQEQ 298
Cdd:pfam12128 737 AIA----ARRSGAKAELKAletwykrdlaslgvdPDVIAKLKREIRTLERKIERIAVRRqevlryfdwyqETWLQRRPRL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 299 IKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSvkekEERGIARL---AQATQERTDL 375
Cdd:pfam12128 813 ATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRC----EMSKLATLkedANSEQAQGSI 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 376 YAKQGRGSQFTSKEERDKW-IKKELKSLDQAINDKKRQIAAIH----KDLEDTEANKEKNLEQYNKLDQDLNEV-KARVE 449
Cdd:pfam12128 889 GERLAQLEDLKLKRDYLSEsVKKYVEHFKNVIADHSGSGLAETweslREEDHYQNDKGIRLLDYRKLVPYLEQWfDVRVP 968
|
....*...
gi 36031035 450 ELDRKYYE 457
Cdd:pfam12128 969 QSIMVLRE 976
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
143-494 |
7.12e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 7.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 143 KINQMATAPDSQRLKLLREVAGTRVYDE-RKEESISLMKETEGKRE--------KINELLKYIEERLHTLEEEKEELAQY 213
Cdd:PTZ00121 1141 KAEEARKAEDAKRVEIARKAEDARKAEEaRKAEDAKKAEAARKAEEvrkaeelrKAEDARKAEAARKAEEERKAEEARKA 1220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 214 Q---KWDKMRRALEytiynqelnetrAKLDELSAKRetsGEKSRQLRDAQQDARDKMEDIERqvRELKTKISAMKEEKEQ 290
Cdd:PTZ00121 1221 EdakKAEAVKKAEE------------AKKDAEEAKK---AEEERNNEEIRKFEEARMAHFAR--RQAAIKAEEARKADEL 1283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 291 LSAERQEQIKQRTKLELKAKdlQDELAGNSEQRKRL--LKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQA 368
Cdd:PTZ00121 1284 KKAEEKKKADEAKKAEEKKK--ADEAKKKAEEAKKAdeAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 369 TQERTDlyAKQGRGSQFTSKEERDKWIKKELKSLDQAiNDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQdlnevKARV 448
Cdd:PTZ00121 1362 AEEKAE--AAEKKKEEAKKKADAAKKKAEEKKKADEA-KKKAEEDKKKADELKKAAAAKKKADEAKKKAEE-----KKKA 1433
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 36031035 449 EELDRKYYEvKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQ 494
Cdd:PTZ00121 1434 DEAKKKAEE-AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK 1478
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
179-357 |
1.05e-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: 52.46 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 179 MKETEGKREKINELLKYIEERLHTLEEEKEEL-AQYQKWDKMRRALEYTIY-------------NQELNETRAKLDELSA 244
Cdd:COG4942 64 IAALARRIRALEQELAALEAELAELEKEIAELrAELEAQKEELAELLRALYrlgrqpplalllsPEDFLDAVRRLQYLKY 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 245 KRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRK 324
Cdd:COG4942 144 LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
170 180 190
....*....|....*....|....*....|...
gi 36031035 325 RLlkerQKLLEKIEEKQKELAETEPKFNSVKEK 357
Cdd:COG4942 224 EL----EALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
289-510 |
1.09e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 289 EQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERgIARLAQA 368
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK-LEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 369 TQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANK-EKNLEQYNKLDQDLNEVKAR 447
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 36031035 448 VEELDRKYYEVKNKKDELQSErnylwREENAEQQALAAKREDLEKKQQLLRAATGKAILNGID 510
Cdd:COG4717 208 LAELEEELEEAQEELEELEEE-----LEQLENELEAAALEERLKEARLLLLIAAALLALLGLG 265
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
181-343 |
1.14e-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: 52.65 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 181 ETEGKREKINELLKYIEERLHTLEEEKEELAQYQKwdkmRRALEYTIYNQELNETRAKLDELSAKRetsgekSRQLRDAQ 260
Cdd:pfam15709 349 EVERKRREQEEQRRLQQEQLERAEKMREELELEQQ----RRFEEIRLRKQRLEEERQRQEEEERKQ------RLQLQAAQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 261 QDARDKMEDIERQVRELKTKisamkeeKEQLSAERQEQIKQRTK-LELKAKDLQDELAGNSE------QRKRLLKERQKL 333
Cdd:pfam15709 419 ERARQQQEEFRRKLQELQRK-------KQQEEAERAEAEKQRQKeLEMQLAEEQKRLMEMAEeerleyQRQKQEAEEKAR 491
|
170
....*....|
gi 36031035 334 LEKIEEKQKE 343
Cdd:pfam15709 492 LEAEERRQKE 501
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
146-412 |
1.24e-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: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 146 QMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKRE--KINELlkyieerlhtleeEKEELAQYQKWDKMRRAL 223
Cdd:pfam17380 332 QAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEisRMREL-------------ERLQMERQQKNERVRQEL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 224 EYTIYNQELNETRAKldelsaKRETSGEKSRQLRDAQQDARdkmediERQVRELKTKISAMKEEKEQLSAERQEQIKQRT 303
Cdd:pfam17380 399 EAARKVKILEEERQR------KIQQQKVEMEQIRAEQEEAR------QREVRRLEEERAREMERVRLEEQERQQQVERLR 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 304 KLELKAKDLQDELAGNSEQRKRLLKERQKLLEK---------IEEKQKEL---AETEPKFNSVKEKEERGIA----RLAQ 367
Cdd:pfam17380 467 QQEEERKRKKLELEKEKRDRKRAEEQRRKILEKeleerkqamIEEERKRKlleKEMEERQKAIYEEERRREAeeerRKQQ 546
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 36031035 368 ATQERTDLyakQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQ 412
Cdd:pfam17380 547 EMEERRRI---QEQMRKATEERSRLEAMEREREMMRQIVESEKAR 588
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
2-47 |
1.49e-06 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 51.69 E-value: 1.49e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 36031035 2 YIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQF 47
Cdd:COG1195 1 RLKRLSLTNFRNYESLEL--EFSPGINVLVGPNGQGKTNLLEAIYL 44
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
267-359 |
1.65e-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: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 267 MEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRtklELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAE 346
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASFERLAELRDE---LAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPE 489
|
90
....*....|...
gi 36031035 347 TEPKFNSVKEKEE 359
Cdd:COG0542 490 LEKELAELEEELA 502
|
|
| recN |
TIGR00634 |
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ... |
795-1213 |
2.77e-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: 51.66 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 795 KRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNEnlrkrLDQVEQELNELRETEGGTVLTattSELEAINKRVK 874
Cdd:TIGR00634 161 KAYRELYQAWLKARQQLKDRQQKEQELAQRLDFLQFQLEE-----LEEADLQPGEDEALEAEQQRL---SNLEKLRELSQ 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 875 DTMAR-SEDLDNSIDKTEAGIKELQKSMErwknmekehmdaiNHDTKELEKMTNRQGMLLKKKEECMKKIRELGS----L 949
Cdd:TIGR00634 233 NALAAlRGDVDVQEGSLLEGLGEAQLALA-------------SVIDGSLRELAEQVGNALTEVEEATRELQNYLDelefD 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 950 PQEAFEKYQTLS-LKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGYksIMELMNVLELRKYEA 1028
Cdd:TIGR00634 300 PERLNEIEERLAqIKRLKRKYGASVEEVLEYAEKIKEELDQLDDSDESLEALEEEVDKLEEEL--DKAAVALSLIRRKAA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1029 iqltfKQVSKNFSEVFQKLvpggkaTLVMKKGDVEGSQSQDEGEGSGESERGsgsqssvpsVDQftgvgIRVSFTGKQGE 1108
Cdd:TIGR00634 378 -----ERLAKRVEQELKAL------AMEKAEFTVEIKTSLPSGAKARAGAYG---------ADQ-----VEFLFSANTGE 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1109 mrEMQQL----SGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESAD 1184
Cdd:TIGR00634 433 --PVKPLakvaSGGELSRVMLALKVVLSSSAAVTTLIFDEVDVGVSGETAQAIAKKLAQLSERHQVLCVTHLPQVAAHAD 510
|
410 420
....*....|....*....|....*....
gi 36031035 1185 KFYGVKfrnKVShIDVITAEMAKDFVEDD 1213
Cdd:TIGR00634 511 AHFKVE---KEG-LDGRTATRVRPLSGEE 535
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
168-489 |
2.85e-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: 51.88 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 168 YDERKEESISLMKETEGKREKINELLKYIEERLHTLEEE----KEELAQYQKWDKM--RRALEYTIYNQELNETRA--KL 239
Cdd:COG3096 352 YQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEvdslKSQLADYQQALDVqqTRAIQYQQAVQALEKARAlcGL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 240 DELSAKretsgeksrQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSA------------ERQEQIKQRTKLEL 307
Cdd:COG3096 432 PDLTPE---------NAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKayelvckiagevERSQAWQTARELLR 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 308 KAKDLQdELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGrgsqfTS 387
Cdd:COG3096 503 RYRSQQ-ALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAA-----EA 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 388 KEERdkwikKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQS 467
Cdd:COG3096 577 VEQR-----SELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAA 651
|
330 340
....*....|....*....|..
gi 36031035 468 ERNYLwrEENAEQQALAAKRED 489
Cdd:COG3096 652 RKQAL--ESQIERLSQPGGAED 671
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-58 |
3.13e-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: 49.14 E-value: 3.13e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 36031035 3 IKQVIIQGFRSYRDQTIVDpFSSKHNVIVGRNGSGKSNFFYAIQFVLsdeFSHLRP 58
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIE-FFSPLTLIVGQNGAGKTTIIEALKYAL---TGELPP 52
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
245-494 |
3.42e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.29 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 245 KRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRK 324
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 325 RLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERgIARLAQATQ-------ERTDLYAKQGRGSQFTSKEERDKWIKK 397
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGGSIDKLRKE-IERLEWRQQtevlspeEEKELVEKIKELEKELEKAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 398 ELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREEN 477
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
250
....*....|....*..
gi 36031035 478 AEQQALAAKREDLEKKQ 494
Cdd:COG1340 241 ELRKELKKLRKKQRALK 257
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
231-447 |
3.86e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 231 ELNETRAKLDELSAKRETSGEksrQLRDAQQDARDKMEDIER---QVRELKTKISAMKEE---KEQLSAERQEQIKQR-- 302
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQA---ELDALQAELEELNEEYNElqaELEALQAEIDKLQAEiaeAEAEIEERREELGERar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 303 ---------TKLE--LKAKDLQDeLAGNSEQRKRLLKERQKLLEKIEEKQKELAETEpkfNSVKEKEERGIARLAQATQE 371
Cdd:COG3883 94 alyrsggsvSYLDvlLGSESFSD-FLDRLSALSKIADADADLLEELKADKAELEAKK---AELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 36031035 372 RTDLYAKQgrgsqfTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKAR 447
Cdd:COG3883 170 KAELEAQQ------AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
699-1029 |
4.15e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 699 NLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEktfmpkqRSLQSLEASLHAMESTRE--- 775
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELR-------EELEKLEKEVKELEELKEeie 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 776 SLKAELGTDLLSQLSLEDQKRvdALNDEIRQLQQENRQLLNERIKLEGIITRVETYlnENLRKRLDQVEQELNELRETEG 855
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIR--ELEERIEELKKEIEELEEKVKELKELKEKAEEY--IKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 856 G-----TVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRqg 930
Cdd:PRK03918 318 RleeeiNGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEE-- 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 931 mLLKKKEECMKKIREL----GSLPQEAFEKYQTLS-LKQLFRKLEQCNTEL---------KKYSHVNKKALDQFVNFSEQ 996
Cdd:PRK03918 396 -LEKAKEEIEEEISKItariGELKKEIKELKKAIEeLKKAKGKCPVCGRELteehrkellEEYTAELKRIEKELKEIEEK 474
|
330 340 350
....*....|....*....|....*....|...
gi 36031035 997 KEKLIKRQEELDrgyksiMELMNVLELRKYEAI 1029
Cdd:PRK03918 475 ERKLRKELRELE------KVLKKESELIKLKEL 501
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
152-504 |
4.68e-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: 51.27 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 152 DSQRLKLLREVagtrvydERKEESISLMKETE--------GKREKINELLKYIEERlhTLEEEK-EELAQYQKWDKMRRA 222
Cdd:pfam15921 376 DDQLQKLLADL-------HKREKELSLEKEQNkrlwdrdtGNSITIDHLRRELDDR--NMEVQRlEALLKAMKSECQGQM 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 223 LEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTkisAMKEEKEQLSAERQEQIKQR 302
Cdd:pfam15921 447 ERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTA---SLQEKERAIEATNAEITKLR 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 303 TKLELKAKDLQdELAGNSEQRKRLLKERQKLLEKIEEKQKElaetepkfnsvkekeergIARLAQATQERTDLYAKQGR- 381
Cdd:pfam15921 524 SRVDLKLQELQ-HLKNEGDHLRNVQTECEALKLQMAEKDKV------------------IEILRQQIENMTQLVGQHGRt 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 382 -GSQFTSKEERDKWIK------KELKSLDQAINDKKRQIAAIHKDLE------------------DTEANKEKNLEQYNK 436
Cdd:pfam15921 585 aGAMQVEKAQLEKEINdrrlelQEFKILKDKKDAKIRELEARVSDLElekvklvnagserlravkDIKQERDQLLNEVKT 664
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 437 LDQDLNEVKARVEELDRKY---------------YEVKNKKDELQSERNYLWREENAE----------QQALAAKR---E 488
Cdd:pfam15921 665 SRNELNSLSEDYEVLKRNFrnkseemetttnklkMQLKSAQSELEQTRNTLKSMEGSDghamkvamgmQKQITAKRgqiD 744
|
410
....*....|....*.
gi 36031035 489 DLEKKQQLLRAATGKA 504
Cdd:pfam15921 745 ALQSKIQFLEEAMTNA 760
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
178-492 |
5.09e-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: 50.79 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 178 LMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKwDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLR 257
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK-ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 258 DAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKI 337
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 338 EEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQgrgSQFTSKEERdkwIKKELKSLDQAINDKKRQIAAIH 417
Cdd:TIGR04523 471 KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV---KDLTKKISS---LKEKIEKLESEKKEKESKISDLE 544
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 36031035 418 KDLE--DTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEK 492
Cdd:TIGR04523 545 DELNkdDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
143-470 |
5.48e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 5.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 143 KINQMATAPDSQRLKLLREVAGTRVYDE-RKEESISLMKETEGKREKINEllkyiEERLHTLEEEKEELAQYQKwdkmRR 221
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADElKKAEELKKAEEKKKAEEAKKA-----EEDKNMALRKAEEAKKAEE----AR 1593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 222 ALEYTIYNQELNETRAkldELSAKRETSGEKSRQLRDAQQDaRDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQ 301
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKA---EEAKKAEEAKIKAEELKKAEEE-KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 302 RTKLELKAKDLQDELAGNSEQRKRLLKERQKLlEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQErtdlyakqgr 381
Cdd:PTZ00121 1670 AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE---------- 1738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 382 gsqftskEERDKWIKKELKSLDQaindKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVeELDRKYYEVKNK 461
Cdd:PTZ00121 1739 -------AEEDKKKAEEAKKDEE----EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRM-EVDKKIKDIFDN 1806
|
....*....
gi 36031035 462 KDELQSERN 470
Cdd:PTZ00121 1807 FANIIEGGK 1815
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
669-987 |
5.77e-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: 50.82 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 669 YDTRKSRLELQKDVRKAEEELGELEAKLNENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQ 748
Cdd:TIGR00606 205 HQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKD 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 749 SEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLsqlslEDQKRVDALNDEIRQLQQENRQLLNERIKL------- 821
Cdd:TIGR00606 285 NSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELV-----DCQRELEKLNKERRLLNQEKTELLVEQGRLqlqadrh 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 822 -EGIITRVETYLNENLRKRLDQVEQELNELRETEGGTVLTATTSELEA--INKRVKDTMARSEDLDNSIDKTEAGIKELQ 898
Cdd:TIGR00606 360 qEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAktAAQLCADLQSKERLKQEQADEIRDEKKGLG 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 899 KSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEA----------FEKYQTLSLKQLFRK 968
Cdd:TIGR00606 440 RTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSltetlkkevkSLQNEKADLDRKLRK 519
|
330
....*....|....*....
gi 36031035 969 LEQCNTELKKYSHVNKKAL 987
Cdd:TIGR00606 520 LDQEMEQLNHHTTTRTQME 538
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
181-350 |
6.70e-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: 48.77 E-value: 6.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 181 ETEGKREKINELLKYIEERLHTLEEEKEELAQyqkwdkmrralEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQ 260
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEA-----------RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 261 QDARD--KMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIE 338
Cdd:COG1579 83 GNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|..
gi 36031035 339 EKQKELAETEPK 350
Cdd:COG1579 163 AEREELAAKIPP 174
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1104-1185 |
1.25e-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: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1104 GKQGEMremqqLSGGQKSLVALALIFaiqkCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESA 1183
Cdd:TIGR02857 453 GEGGAG-----LSGGQAQRLALARAF----LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALA 523
|
..
gi 36031035 1184 DK 1185
Cdd:TIGR02857 524 DR 525
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
171-499 |
1.67e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 171 RKEESISLMKETEGKREKINELLKYIEERLHTLEEEK---EELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRE 247
Cdd:PRK01156 347 RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSkniERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVS 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 248 TSGEKSRQLRDAQQDARDKM------------------EDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKA 309
Cdd:PRK01156 427 SLNQRIRALRENLDELSRNMemlngqsvcpvcgttlgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRK 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 310 KDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEK---------EERGIARL-AQATQERTDLYAKQ 379
Cdd:PRK01156 507 EYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRykslkledlDSKRTSWLnALAVISLIDIETNR 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 380 GRGSQFTSK----EER---------------DKWIKK---ELKSLDQAIN---DKKRQIAAIHKDLEDTE---ANKEKNL 431
Cdd:PRK01156 587 SRSNEIKKQlndlESRlqeieigfpddksyiDKSIREienEANNLNNKYNeiqENKILIEKLRGKIDNYKkqiAEIDSII 666
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 36031035 432 EQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQLLRA 499
Cdd:PRK01156 667 PDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKA 734
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
1100-1165 |
1.68e-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: 1.68e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 36031035 1100 VSFtgKQGEmrEMQQL-----SGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELA 1165
Cdd:cd03277 111 VKF--REGE--QLQELdphhqSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVETA 177
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
168-468 |
2.18e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.86 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 168 YDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRAleytiynqELNETRAKLDELSAKRE 247
Cdd:TIGR04523 382 YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII--------KNNSEIKDLTNQDSVKE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 248 TSGEKSRQLRDAQQDardKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLL 327
Cdd:TIGR04523 454 LIIKNLDNTRESLET---QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 328 KERQKLLEKIEEKQKELAE--TEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTS-KEERDKWIKKELKSLDQ 404
Cdd:TIGR04523 531 SEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDqKEKEKKDLIKEIEEKEK 610
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 36031035 405 AINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQdlnEVKARVEELDrkyyEVKNKKDELQSE 468
Cdd:TIGR04523 611 KISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQ---EVKQIKETIK----EIRNKWPEIIKK 667
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
183-482 |
2.28e-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: 49.02 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 183 EGKREKINELLKYIEERLHTLEEEKEELAQYQKwdkMRRALEYtiynqELNETRAKLDELSAKREtsgEKSRQLRDAQ-- 260
Cdd:pfam01576 738 EQGEEKRRQLVKQVRELEAELEDERKQRAQAVA---AKKKLEL-----DLKELEAQIDAANKGRE---EAVKQLKKLQaq 806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 261 --------QDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQK 332
Cdd:pfam01576 807 mkdlqrelEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRR 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 333 LLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQE-RTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDK-K 410
Cdd:pfam01576 887 LEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTElAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKfK 966
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 411 RQIAAIHKDLEDTEANKE---KNLEQYNKL----DQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWRE-ENAEQQA 482
Cdd:pfam01576 967 SSIAALEAKIAQLEEQLEqesRERQAANKLvrrtEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQlEEAEEEA 1046
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1105-1190 |
2.31e-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: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1105 KQGE-----MREMQQLSGGQKSLVALALIFAIQK--CDPAPFYLFDEIDQALDAQHRKAVSDMIMELA---VHAQFITTT 1174
Cdd:cd03240 101 HQGEsnwplLDMRGRCSGGEKVLASLIIRLALAEtfGSNCGILALDEPTTNLDEENIEESLAEIIEERksqKNFQLIVIT 180
|
90
....*....|....*.
gi 36031035 1175 FRPELLESADKFYGVK 1190
Cdd:cd03240 181 HDEELVDAADHIYRVE 196
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
242-447 |
2.92e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 242 LSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTK----------------ISAMKEEKEQLSAERQEQIKQRTKL 305
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKnglvdlseeaklllqqLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 306 ELKAKDLQDELA--GNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQErtdlyAKQGRGS 383
Cdd:COG3206 246 RAQLGSGPDALPelLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQR-----ILASLEA 320
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 36031035 384 QFTSKEERDKWIKKELKSLDQAIndkkRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKAR 447
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARL----AELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
226-468 |
3.31e-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: 47.97 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 226 TIYNQELNETRAKLDELSAKRETSgekSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEkeqLSAERQEQikqrTKL 305
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAA---NRQREKEKERYKRDREQWERQRRELESRVAELKEE---LRQSREKH----EEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 306 ELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELA-------ETEPKFNSVKEKEERGIARLAQATQERTDLYAK 378
Cdd:pfam07888 100 EEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKtltqrvlERETELERMKERAKKAGAQRKEEEAERKQLQAK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 379 qgrgsqFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDT----------EANKEKNLEQYNKLDQDLNEVKARV 448
Cdd:pfam07888 180 ------LQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLtqklttahrkEAENEALLEELRSLQERLNASERKV 253
|
250 260
....*....|....*....|
gi 36031035 449 EELDRKYYEVKNKKDELQSE 468
Cdd:pfam07888 254 EGLGEELSSMAAQRDRTQAE 273
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
200-495 |
3.37e-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: 48.50 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 200 LHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKretsGEKSRQLRDAQQDARDKMEDIERQVRELKT 279
Cdd:TIGR00606 799 MELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSK----IELNRKLIQDQQEQIQHLKSKTNELKSEKL 874
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 280 KISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKelaETEPKFNSVKEKEE 359
Cdd:TIGR00606 875 QIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNK---KAQDKVNDIKEKVK 951
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 360 RGIAR---LAQATQERTDLYAKQ------GRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKE-K 429
Cdd:TIGR00606 952 NIHGYmkdIENKIQDGKDDYLKQketelnTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENElK 1031
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 36031035 430 NLEQYNK-LDQDLNEVkaRVEELDRKYYEVKNKKDELQSERNYLW-REENAEQQALAAKREDLEKKQQ 495
Cdd:TIGR00606 1032 EVEEELKqHLKEMGQM--QVLQMKQEHQKLEENIDLIKRNHVLALgRQKGYEKEIKHFKKELREPQFR 1097
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
316-504 |
3.69e-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: 47.45 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 316 LAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLyakqgrgsqftskeerdkwi 395
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL-------------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 396 KKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNL---------------------------------------EQYNK 436
Cdd:COG4942 75 EQELAALEAELAELEKEIAELRAELEAQKEELAELLralyrlgrqpplalllspedfldavrrlqylkylaparrEQAEE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 36031035 437 LDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQLLRAATGKA 504
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
180-370 |
3.96e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 180 KETEGKREKInelLKYIEERLHTLEEEKEeLAQYQKWDKMRRALEytiynQELNETRAKLDE-----------LSAKRET 248
Cdd:PRK12704 34 KEAEEEAKRI---LEEAKKEAEAIKKEAL-LEAKEEIHKLRNEFE-----KELRERRNELQKlekrllqkeenLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 249 SGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQR--TKLELKAKdlqdelagnseqrkrl 326
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEIllEKVEEEAR---------------- 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 36031035 327 lKERQKLLEKIEEKQKELAetepkfnsvkEKEERGIarLAQATQ 370
Cdd:PRK12704 169 -HEAAVLIKEIEEEAKEEA----------DKKAKEI--LAQAIQ 199
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
148-415 |
4.91e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.74 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 148 ATAPDSQRLKL-LREVAGTRVYDERK-----EESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQyqKWDKMRR 221
Cdd:PRK10929 20 ATAPDEKQITQeLEQAKAAKTPAQAEivealQSALNWLEERKGSLERAKQYQQVIDNFPKLSAELRQQLNN--ERDEPRS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 222 A---LEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDA-------QQDARDKMEDIERQVRELKTKISAmkEEKEQL 291
Cdd:PRK10929 98 VppnMSTDALEQEILQVSSQLLEKSRQAQQEQDRAREISDSlsqlpqqQTEARRQLNEIERRLQTLGTPNTP--LAQAQL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 292 SAERQEQIKQRTKLElkakdlQDELAGNS-EQRKRLLKERQKLLEK-IEEKQKELAETEPKFNSVKEKEergiarlAQAT 369
Cdd:PRK10929 176 TALQAESAALKALVD------ELELAQLSaNNRQELARLRSELAKKrSQQLDAYLQALRNQLNSQRQRE-------AERA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 36031035 370 QERTDLYAKQGRG------SQFTSKEERDKWIKKELKSLDQaINDKKRQIAA 415
Cdd:PRK10929 243 LESTELLAEQSGDlpksivAQFKINRELSQALNQQAQRMDL-IASQQRQAAS 293
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
698-1046 |
5.43e-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: 47.74 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 698 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEmkmlkeKRQQSEKTFmpKQRSLQSLEASLHAMESTRESL 777
Cdd:TIGR01612 934 EKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLID------KINELDKAF--KDASLNDYEAKNNELIKYFNDL 1005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 778 KAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERI-----------KLEGIITRVETYLNENLRKRLDQVEQE 846
Cdd:TIGR01612 1006 KANLGKNKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIaihtsiyniidEIEKEIGKNIELLNKEILEEAEINITN 1085
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 847 LNELRETEGGTVLTATTSE-----LEAINKrVKDTMarsEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAI------ 915
Cdd:TIGR01612 1086 FNEIKEKLKHYNFDDFGKEenikyADEINK-IKDDI---KNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLedvadk 1161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 916 ---NHDTKELE-KMTNRQGMLLKKK---EECMKKIRELGSLP--QEAFEKYQTL------SLKQLFrkLEQCNTELKKYS 980
Cdd:TIGR01612 1162 aisNDDPEEIEkKIENIVTKIDKKKniyDEIKKLLNEIAEIEkdKTSLEEVKGInlsygkNLGKLF--LEKIDEEKKKSE 1239
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 36031035 981 HVNKKALDQFVNFSEQKEK--LIKRQEELDRGYKSIMELMNVLElRKYEAIQLTFKQVSKNFSEVFQK 1046
Cdd:TIGR01612 1240 HMIKAMEAYIEDLDEIKEKspEIENEMGIEMDIKAEMETFNISH-DDDKDHHIISKKHDENISDIREK 1306
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
251-428 |
6.13e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 251 EKSRQlRDAQQDARDKMEDI----ERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRL 326
Cdd:PRK09510 78 EEQRK-KKEQQQAEELQQKQaaeqERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 327 LKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAI 406
Cdd:PRK09510 157 AAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKA 236
|
170 180
....*....|....*....|..
gi 36031035 407 NDKKrqiAAIHKDLEDTEANKE 428
Cdd:PRK09510 237 AAEK---AAAAKAAEKAAAAKA 255
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
182-496 |
6.32e-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: 47.53 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 182 TEGKREKINELLKYIEERLHTLEEEKEELAQYQ-KWDKMRRALEYTIynQELNETRAKLDELS-AKRETSGEKSRQLRDA 259
Cdd:pfam12128 599 EEELRERLDKAEEALQSAREKQAAAEEQLVQANgELEKASREETFAR--TALKNARLDLRRLFdEKQSEKDKKNKALAER 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 260 QQDARDKMEDIERQVRELKTKISAMKEE-KEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEkiE 338
Cdd:pfam12128 677 KDSANERLNSLEAQLKQLDKKHQAWLEEqKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALE--T 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 339 EKQKELAETEPKFNSVKeKEERGI----ARLAQATQERTDLyAKQGRGSQFTSKEERDKwIKKELKSLDQAINDKKRQIA 414
Cdd:pfam12128 755 WYKRDLASLGVDPDVIA-KLKREIrtleRKIERIAVRRQEV-LRYFDWYQETWLQRRPR-LATQLSNIERAISELQQQLA 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 415 AIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQ 494
Cdd:pfam12128 832 RLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKK 911
|
..
gi 36031035 495 QL 496
Cdd:pfam12128 912 YV 913
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
238-359 |
7.52e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 238 KLDELSAKREtsgEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKlELKA------KD 311
Cdd:PRK00409 517 KLNELIASLE---ELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIK-EAKKeadeiiKE 592
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 36031035 312 L-QDELAGNSEQRKRLLKERQKLL-EKIEEKQKELAETEPKFNSVKEKEE 359
Cdd:PRK00409 593 LrQLQKGGYASVKAHELIEARKRLnKANEKKEKKKKKQKEKQEELKVGDE 642
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
254-470 |
9.72e-05 |
|
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: 9.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 254 RQLRDAQQDARDKMEDIERQVRELKTKISAmkeekeqlsAERQ-EQIKQRTK---LELKAKDLQDELAGNSEQRKRLLKE 329
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEE---------AEAAlEEFRQKNGlvdLSEEAKLLLQQLSELESQLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 330 RQKLLEKIEEKQKELAETEPKFNSVKEKEE--RGIARLAQATQERTDLyakqgrGSQFTSKEERDKWIKKELKSLDQAIN 407
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDALPELLQSPViqQLRAQLAELEAELAEL------SARYTPNHPDVIALRAQIAALRAQLQ 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 36031035 408 DKKRQI-AAIHKDLEDTEANK---EKNLEQYNKLDQDLNEVKARVEELDRKY------YE-VKNKKDELQSERN 470
Cdd:COG3206 309 QEAQRIlASLEAELEALQAREaslQAQLAQLEARLAELPELEAELRRLEREVevarelYEsLLQRLEEARLAEA 382
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1115-1187 |
1.48e-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: 1.48e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 36031035 1115 LSGGQKSLVALALIFaIQKcdpAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFY 1187
Cdd:cd03228 97 LSGGQRQRIAIARAL-LRD---PPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRII 165
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
1-100 |
1.75e-04 |
|
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: 45.42 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIqFVLSDEFSHlRPEQRLALLHEGTgPRvisAFVEI 80
Cdd:TIGR00611 1 MYLSRLELTDFRNYDAVDL--ELSPGVNVIVGPNGQGKTNLLEAI-YYLALGRSH-RTSRDKPLIRFGA-EA---FVIEG 72
|
90 100
....*....|....*....|
gi 36031035 81 IFDNSDNRLPIDKEEVSLRR 100
Cdd:TIGR00611 73 RVSKGDREVTIPLEGLLKKK 92
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
173-522 |
1.79e-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: 45.45 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 173 EESISLMKETEGKREKINEL-----------LKYIEERlHTLEEEKEELAQYQKW-DKMR--------RALEYTIYNQEL 232
Cdd:pfam05622 28 EEKNSLQQENKKLQERLDQLesgddsgtpggKKYLLLQ-KQLEQLQEENFRLETArDDYRikceelekEVLELQHRNEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 233 ----NETRAKLDELSAKRETSgEKSRQLRDAQQDARDKME---DIERQVREL------------------------KTKI 281
Cdd:pfam05622 107 tslaEEAQALKDEMDILRESS-DKVKKLEATVETYKKKLEdlgDLRRQVKLLeernaeymqrtlqleeelkkanalRGQL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 282 SAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKqkelaetepKFNSVKEKEERG 361
Cdd:pfam05622 186 ETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRETNEEL---------RCAQLQQAELSQ 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 362 IARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKsLDQAINDKKRqIAAIHKDLEDTEANKEKNLEQYNKLDQDL 441
Cdd:pfam05622 257 ADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLR-LGQEGSYRER-LTELQQLLEDANRRKNELETQNRLANQRI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 442 NEVKARVEELDRKYYEVKNKKDELQSernyLWREENAEQQALAAKREDLEKKQQLLRAATGKAILNGIDSINKVLEHFRR 521
Cdd:pfam05622 335 LELQQQVEELQKALQEQGSKAEDSSL----LKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQEALRK 410
|
.
gi 36031035 522 K 522
Cdd:pfam05622 411 K 411
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
670-899 |
1.81e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 670 DTRKSRLELQKDVRKAEEELGELEAKLNEnLRRNIERINNEIDQLMnqmQQIETQQRKFKASRDSILSEMKMLKEKRQQS 749
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRIRA-LEQELAALEAELAELE---KEIAELRAELEAQKEELAELLRALYRLGRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 750 EKTFMPKQRSLQSLEASLHamestreslkaelgtdLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVE 829
Cdd:COG4942 121 PLALLLSPEDFLDAVRRLQ----------------YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 830 TylnenLRKRLDQVEQELNELreteggtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQK 899
Cdd:COG4942 185 E-----ERAALEALKAERQKL--------LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
180-482 |
1.88e-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: 45.72 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 180 KETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETraKLDELSAKRETSGEKSRQLRDA 259
Cdd:COG5185 156 VETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESE--TGNLGSESTLLEKAKEIINIEE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 260 QQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTK-LELKAKDLQDELAgNSEQRKRLLKERQKLLEKIE 338
Cdd:COG5185 234 ALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKrLNENANNLIKQFE-NTKEKIAEYTKSIDIKKATE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 339 EKQKELAETEP--KFNSVKEKEERGIARL-AQATQERTDLYAKQ-----GRGSQFTSKEERDKwiKKELKSLDQAINDKK 410
Cdd:COG5185 313 SLEEQLAAAEAeqELEESKRETETGIQNLtAEIEQGQESLTENLeaikeEIENIVGEVELSKS--SEELDSFKDTIESTK 390
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 36031035 411 RQIAAIHKDLEDTEANKEKNLEQYNKL-DQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQA 482
Cdd:COG5185 391 ESLDEIPQNQRGYAQEILATLEDTLKAaDRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQS 463
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
157-348 |
2.16e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 157 KLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETR 236
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELK 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 237 AKLDELSAKRetsgEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMK-----EEKEQLSAE----RQEQIKQRTKLEl 307
Cdd:PRK03918 609 DAEKELEREE----KELKKLEEELDKAFEELAETEKRLEELRKELEELEkkyseEEYEELREEylelSRELAGLRAELE- 683
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 36031035 308 KAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETE 348
Cdd:PRK03918 684 ELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
173-505 |
2.22e-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: 45.55 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 173 EESISLMKETEGKREKINELLkyiEERLH----TLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRET 248
Cdd:pfam01576 137 EEDILLLEDQNSKLSKERKLL---EERISeftsNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 249 SGEKSrqlrdaqqDARDKMEDIERQVRELKTKISAMKEE-------KEQLSAERQEQIKQRTKLELKAKDLQDELAGNSE 321
Cdd:pfam01576 214 EGEST--------DLQEQIAELQAQIAELRAQLAKKEEElqaalarLEEETAQKNNALKKIRELEAQISELQEDLESERA 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 322 QRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKE---KEERGIARLAQATQERTDLYA------KQGRGSQFTSKEERD 392
Cdd:pfam01576 286 ARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQElrsKREQEVTELKKALEEETRSHEaqlqemRQKHTQALEELTEQL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 393 KWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSErnyl 472
Cdd:pfam01576 366 EQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSE---- 441
|
330 340 350
....*....|....*....|....*....|...
gi 36031035 473 wreenaeqqalaakredLEKKQQLLRAATGKAI 505
Cdd:pfam01576 442 -----------------LESVSSLLNEAEGKNI 457
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
173-470 |
2.25e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 173 EESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYN-----QELNETrakLDELSAKRE 247
Cdd:PRK11281 66 EQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLSlrqleSRLAQT---LDQLQNAQN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 248 TSGEKSRQLRDAQ-QDARDKMEDIERQVR--ELKTKISAMKEEKEQLSAERQEQIK-QRTKLELKAKDLQDELAGNSEQR 323
Cdd:PRK11281 143 DLAEYNSQLVSLQtQPERAQAALYANSQRlqQIRNLLKGGKVGGKALRPSQRVLLQaEQALLNAQNDLQRKSLEGNTQLQ 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 324 KRLLKERQKLLEKIEEKQKELAETEpkfNSVKEKeergiaRLAQATQErtdlyAKQGRGSQFTSKEERDKWIKKELksld 403
Cdd:PRK11281 223 DLLQKQRDYLTARIQRLEHQLQLLQ---EAINSK------RLTLSEKT-----VQEAQSQDEAARIQANPLVAQEL---- 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 36031035 404 qaindkkrqiaaihkdledtEANKeknleqynKLDQDLNEVKARVEELDRKYYEVKNKKDEL-QSERN 470
Cdd:PRK11281 285 --------------------EINL--------QLSQRLLKATEKLNTLTQQNLRVKNWLDRLtQSERN 324
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
11-79 |
2.34e-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: 44.60 E-value: 2.34e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 36031035 11 FRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFvLSDEFSHLRPEQRlALLHEGTGPRVISAFVE 79
Cdd:cd03242 9 FRNYAELEL--EFEPGVTVLVGENAQGKTNLLEAISL-LATGKSHRTSRDK-ELIRWGAEEAKISAVLE 73
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
698-1019 |
2.42e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.45 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 698 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEM--KMLKEKRQQSEKtfmPKQRSLQSLEASLHAMESTRE 775
Cdd:COG5022 810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFgrSLKAKKRFSLLK---KETIYLQSAQRVELAERQLQE 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 776 sLKAELGT-DLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERI-KLEGIITRVETylnENLRKRLDQVEQELNELRET 853
Cdd:COG5022 887 -LKIDVKSiSSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIaRLKKLLNNIDL---EEGPSIEYVKLPELNKLHEV 962
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 854 EGGtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEH-------------MDAINHDTK 920
Cdd:COG5022 963 ESK--LKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLkelpvevaelqsaSKIISSEST 1040
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 921 ELEKMTNRQ---GMLLKKKEECMKKIRELG----SLPQEAFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNF 993
Cdd:COG5022 1041 ELSILKPLQklkGLLLLENNQLQARYKALKlrreNSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVA 1120
|
330 340
....*....|....*....|....*.
gi 36031035 994 SEQKEKLIKRQEELDRGYKSIMELMN 1019
Cdd:COG5022 1121 QMIKLNLLQEISKFLSQLVNTLEPVF 1146
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
229-513 |
2.78e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 229 NQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELK 308
Cdd:COG4372 51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 309 AKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSK 388
Cdd:COG4372 131 RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 389 EERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSE 468
Cdd:COG4372 211 SLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 36031035 469 RNYLWREENAEQQALAAKREDLEKKQQLLRAATGKAILNGIDSIN 513
Cdd:COG4372 291 AALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1110-1172 |
2.91e-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: 2.91e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 36031035 1110 REMQQLSGGQKSLVALALIFAIQkcdpAPFYLFDEIDQALDAQHRKAVSDMIMELavHAQFIT 1172
Cdd:cd03225 130 RSPFTLSGGQKQRVAIAGVLAMD----PDILLLDEPTAGLDPAGRRELLELLKKL--KAEGKT 186
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
275-489 |
3.32e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.94 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 275 RELKTKISAMKEEKEQlsAERQeqiKQRTklelkakdlqdelagnsEQRK-RLlkERQKLlEKiEEKQKELAE--TEPKF 351
Cdd:PRK05035 432 RQAKAEIRAIEQEKKK--AEEA---KARF-----------------EARQaRL--EREKA-AR-EARHKKAAEarAAKDK 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 352 NSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKS---LDQAINDKKRQIAAihkDLEDTEANKE 428
Cdd:PRK05035 486 DAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAekqAAAAADPKKAAVAA---AIARAKAKKA 562
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 36031035 429 KNLEQYNKLDQDLNEVKARVEELDRKyyeVKNKKDELQSErnylwREENAEQQALAAKRED 489
Cdd:PRK05035 563 AQQAANAEAEEEVDPKKAAVAAAIAR---AKAKKAAQQAA-----SAEPEEQVAEVDPKKA 615
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
151-500 |
3.44e-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: 44.96 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 151 PDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQ 230
Cdd:TIGR00618 274 AQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 231 ELNETRAKLDELSAKRETSGEKS--RQLRDAQQD----------ARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQ 298
Cdd:TIGR00618 354 EIHIRDAHEVATSIREISCQQHTltQHIHTLQQQkttltqklqsLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQ 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 299 IKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIE---------EKQKELAETEPKFNSVKEKEERGI-ARLAQA 368
Cdd:TIGR00618 434 ELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQqlqtkeqihLQETRKKAVVLARLLELQEEPCPLcGSCIHP 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 369 TQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARV 448
Cdd:TIGR00618 514 NPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNIT 593
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 36031035 449 EELDRKYYEVKNKKDELQSERNYLWREENAEQ--QALAAKREDLEKKQQLLRAA 500
Cdd:TIGR00618 594 VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQdlQDVRLHLQQCSQELALKLTA 647
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
253-428 |
3.71e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 253 SRQLRDAQQDARDKMEDIERQVrelktkiSAMKEEKEqLSAeRQEQIKQRTKLELKAKDLQDELAGNSE---QRKRLLKE 329
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEA-------EAIKKEAL-LEA-KEEIHKLRNEFEKELRERRNELQKLEKrllQKEENLDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 330 RQKLLEKIEEK-QKELAETEPKFNSVKEKEERgIARLAQATQERTDlyakqgRGSQFTSKEerdkwIKKELksLDQAIND 408
Cdd:PRK12704 101 KLELLEKREEElEKKEKELEQKQQELEKKEEE-LEELIEEQLQELE------RISGLTAEE-----AKEIL--LEKVEEE 166
|
170 180
....*....|....*....|...
gi 36031035 409 KKRQIAAIHKDLED---TEANKE 428
Cdd:PRK12704 167 ARHEAAVLIKEIEEeakEEADKK 189
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
742-903 |
3.93e-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: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 742 LKEKRQQSEKT--FMPKQrsLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERI 819
Cdd:COG3206 166 LELRREEARKAleFLEEQ--LPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 820 KLEGIITRVETYLNE--------NLRKRLDQVEQELNELRE--TEGGTVLTATTSELEAINKRVKDTMARS-EDLDNSID 888
Cdd:COG3206 244 ALRAQLGSGPDALPEllqspviqQLRAQLAELEAELAELSAryTPNHPDVIALRAQIAALRAQLQQEAQRIlASLEAELE 323
|
170
....*....|....*
gi 36031035 889 KTEAGIKELQKSMER 903
Cdd:COG3206 324 ALQAREASLQAQLAQ 338
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
28-115 |
4.14e-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: 43.92 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 28 NVIVGRNGSGKSNFFYAIQFvLSDEFSHLRPEQRLALLHEGTG----------PRVISAFVEIIFDNSDNR----LPIDK 93
Cdd:pfam13304 2 NVLIGPNGSGKSNLLEALRF-LADFDALVIGLTDERSRNGGIGgipsllngidPKEPIEFEISEFLEDGVRyrygLDLER 80
|
90 100
....*....|....*....|....
gi 36031035 94 EEVS--LRRVIGAKKDQYFLDKKM 115
Cdd:pfam13304 81 EDVEekLSSKPTLLEKRLLLREDS 104
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
169-491 |
4.41e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 169 DERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQyqkwdkmrralEYTIYNQELNETRAKLDELSAKRET 248
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARS-----------ELEQLEEELEELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 249 SGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLK 328
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 329 E--RQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAI 406
Cdd:COG4372 179 AeaEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 407 NDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAK 486
Cdd:COG4372 259 EIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAE 338
|
....*
gi 36031035 487 REDLE 491
Cdd:COG4372 339 LADLL 343
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1110-1171 |
4.77e-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: 4.77e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 36031035 1110 REMQQLSGGQKSLVALAlIFAIQKCDpapFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFI 1171
Cdd:cd03236 135 RNIDQLSGGELQRVAIA-AALARDAD---FYFFDEPSSYLDIKQRLNAARLIRELAEDDNYV 192
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
165-495 |
5.63e-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: 44.27 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 165 TRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAqyqkwDKMRRAleytiyNQELNETRAKLDELSA 244
Cdd:TIGR00606 704 LRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELR-----NKLQKV------NRDIQRLKNDIEEQET 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 245 KRETSGEKSRQLRDAQQDArDKMEDIERQVRELKTKIsamkeekEQLSAERQEqikqrTKLELKAKDLQDELAGNSEQRK 324
Cdd:TIGR00606 773 LLGTIMPEEESAKVCLTDV-TIMERFQMELKDVERKI-------AQQAAKLQG-----SDLDRTVQQVNQEKQEKQHELD 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 325 RLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEergiARLAQATQERTDLyakqgrgsqftskEERDKWIKKELKSLDQ 404
Cdd:TIGR00606 840 TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEK----LQIGTNLQRRQQF-------------EEQLVELSTEVQSLIR 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 405 AINDKKRQIAAIHKDLEDTEANKEKNL---EQYNKLDQDlnEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQ 481
Cdd:TIGR00606 903 EIKDAKEQDSPLETFLEKDQQEKEELIsskETSNKKAQD--KVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELN 980
|
330
....*....|....
gi 36031035 482 ALAAKREDLEKKQQ 495
Cdd:TIGR00606 981 TVNAQLEECEKHQE 994
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
207-485 |
5.68e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 207 KEELAQYQKWDKMRRALEYTiyNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKM---EDIERQVRELKtKISA 283
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAE--QYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALrqqEKIERYQADLE-ELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 284 MKEEKEQLSAERQEQIKQR----TKLELKAKDLQDELA----GNSEQRKRLLKERQ--KLLEKIEEkQKELAETEPKfnS 353
Cdd:PRK04863 363 RLEEQNEVVEEADEQQEENearaEAAEEEVDELKSQLAdyqqALDVQQTRAIQYQQavQALERAKQ-LCGLPDLTAD--N 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 354 VKEKEERGIARLAQATQERTDLYAK----QGRGSQFT-------------SKEERDKWIKKELKSL--DQAINDKKRQIA 414
Cdd:PRK04863 440 AEDWLEEFQAKEQEATEELLSLEQKlsvaQAAHSQFEqayqlvrkiagevSRSEAWDVARELLRRLreQRHLAEQLQQLR 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 415 AIHKDLE---DTEANKEKNLEQYNK------------------LDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLW 473
Cdd:PRK04863 520 MRLSELEqrlRQQQRAERLLAEFCKrlgknlddedeleqlqeeLEARLESLSESVSEARERRMALRQQLEQLQARIQRLA 599
|
330
....*....|..
gi 36031035 474 REENAEQQALAA 485
Cdd:PRK04863 600 ARAPAWLAAQDA 611
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
234-379 |
5.80e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 234 ETRAKLDELSAKRETSgeksRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKakdlQ 313
Cdd:PRK12704 52 EAIKKEALLEAKEEIH----KLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK----Q 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 36031035 314 DELAGNSEQRKRLLKERQKLLEKI-----EEKQKELAEtepkfnSVKEKEERGIARLAQATQERTDLYAKQ 379
Cdd:PRK12704 124 QELEKKEEELEELIEEQLQELERIsgltaEEAKEILLE------KVEEEARHEAAVLIKEIEEEAKEEADK 188
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
111-464 |
6.06e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 44.27 E-value: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 111 LDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKIN 190
Cdd:PTZ00108 1026 LVITNAKKKDLVKELKKLGYVRFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSYDYLLSMPIWSLTKEKVE 1105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 191 ELLKYIEERLhtleeekeelaqyQKWDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDI 270
Cdd:PTZ00108 1106 KLNAELEKKE-------------KELEKLKNTTPKDMWLEDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKP 1172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 271 ERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKD-------LQDELAGNSEQRKRLLKERQKLLEKIEEKQKE 343
Cdd:PTZ00108 1173 KLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPdnkksnsSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSK 1252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 344 LAETEPKFNSVKEKEERGIARL---AQATQERTDLYAKQGRGSQFTSKEERDkwikkELKSLDQAINDKKRQIAAIHKDL 420
Cdd:PTZ00108 1253 SSEDNDEFSSDDLSKEGKPKNApkrVSAVQYSPPPPSKRPDGESNGGSKPSS-----PTKKKVKKRLEGSLAALKKKKKS 1327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 36031035 421 EDTEANKEKNLEQYNK-LDQDLNEVKAR---------VEELDRKYYEVKNKKDE 464
Cdd:PTZ00108 1328 EKKTARKKKSKTRVKQaSASQSSRLLRRprkkksdssSEDDDDSEVDDSEDEDD 1381
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1114-1185 |
7.26e-04 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 43.15 E-value: 7.26e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 36031035 1114 QLSGGQKSLVALALIFAIQkcdpAPFYLFDEIDQALDAQHRKAVSDMIMELavHAQF-ITTTF----RPELLESADK 1185
Cdd:PRK10851 136 QLSGGQKQRVALARALAVE----PQILLLDEPFGALDAQVRKELRRWLRQL--HEELkFTSVFvthdQEEAMEVADR 206
|
|
| F-BAR_CIP4-like |
cd07653 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 ... |
388-482 |
8.18e-04 |
|
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: 42.63 E-value: 8.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 388 KEERDKWIKkELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELdRKYYEVKNKKDElQS 467
Cdd:cd07653 104 RQERKKHLS-EGSKLQQKLESSIKQLEKSKKAYEKAFKEAEKAKQKYEKADADMNLTKADVEKA-KANANLKTQAAE-EA 180
|
90
....*....|....*..
gi 36031035 468 ERNY--LWREENAEQQA 482
Cdd:cd07653 181 KNEYaaQLQKFNKEQRQ 197
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
281-504 |
8.19e-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: 8.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 281 ISAMKEEKEQLSAERqEQIKQRtklELKAKDLQDElAGNSEQRKRLLKERQKLLEKIEEKQKELAETEP-KFNSVKEKEE 359
Cdd:NF012221 1534 VVATSESSQQADAVS-KHAKQD---DAAQNALADK-ERAEADRQRLEQEKQQQLAAISGSQSQLESTDQnALETNGQAQR 1608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 360 RGIARLAQA-TQERTDLyaKQG----RGSQFTSKEERDKW--------IKKELKSLDQA-------INDKKRQIAAIHKD 419
Cdd:NF012221 1609 DAILEESRAvTKELTTL--AQGldalDSQATYAGESGDQWrnpfagglLDRVQEQLDDAkkisgkqLADAKQRHVDNQQK 1686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 420 LEDTEANKEKNLEQ--YNKLDQDLNEVKARVeeldrkyyEVKNKKDELQSERNylwREENAEQQALAAKREDLEKKQQLL 497
Cdd:NF012221 1687 VKDAVAKSEAGVAQgeQNQANAEQDIDDAKA--------DAEKRKDDALAKQN---EAQQAESDANAAANDAQSRGEQDA 1755
|
....*..
gi 36031035 498 RAATGKA 504
Cdd:NF012221 1756 SAAENKA 1762
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
187-457 |
8.96e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 8.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 187 EKINELLKYIEERLHTLEEEkeELAQYQKWDKMRRALeytiynQELNETRAKLDELsaKRETSGEKSRQLRDAQQDARDK 266
Cdd:PRK04863 840 RQLNRRRVELERALADHESQ--EQQQRSQLEQAKEGL------SALNRLLPRLNLL--ADETLADRVEEIREQLDEAEEA 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 267 MEDIERQ---VRELKTKISAMKEEKEQLSAERQ--EQIKQRTKLELKAKDLQDELAGNS-----EQRKRLLKERQKLLEK 336
Cdd:PRK04863 910 KRFVQQHgnaLAQLEPIVSVLQSDPEQFEQLKQdyQQAQQTQRDAKQQAFALTEVVQRRahfsyEDAAEMLAKNSDLNEK 989
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 337 IEEKQKElAETEPkfNSVKEKEERGIARLAQATQERTDLyakqgrGSQFTSKEERDKWIKKELKSL---------DQAIN 407
Cdd:PRK04863 990 LRQRLEQ-AEQER--TRAREQLRQAQAQLAQYNQVLASL------KSSYDAKRQMLQELKQELQDLgvpadsgaeERARA 1060
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 36031035 408 DKKRqiaaIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYE 457
Cdd:PRK04863 1061 RRDE----LHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHE 1106
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
395-503 |
9.39e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 9.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 395 IKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKD--ELQSERNYL 472
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyeALQKEIESL 101
|
90 100 110
....*....|....*....|....*....|.
gi 36031035 473 WREENAEQQALAAKREDLEKKQQLLRAATGK 503
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAE 132
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
171-342 |
9.51e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 9.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 171 RKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKM-RRALEYTIYNQELNETRAKLDELSAK---- 245
Cdd:COG3206 203 QKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSgPDALPELLQSPVIQQLRAQLAELEAElael 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 246 RETSGEKS---RQLRDAQQDARDKMED-IERQVRELKTKISAMKEEKEQLSAERQE---QIKQRTKLELKAKDLQDELAG 318
Cdd:COG3206 283 SARYTPNHpdvIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQleaRLAELPELEAELRRLEREVEV 362
|
170 180
....*....|....*....|....
gi 36031035 319 NSEQRKRLLKERQKLleKIEEKQK 342
Cdd:COG3206 363 ARELYESLLQRLEEA--RLAEALT 384
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
232-469 |
1.06e-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: 43.17 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 232 LNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKE-------QLSAERQEQIKQRTK 304
Cdd:pfam05483 263 LEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatkticQLTEEKEAQMEELNK 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 305 LELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSvkEKEERgiarlaqatqertdlyakqgrgSQ 384
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSS--ELEEM----------------------TK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 385 FTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLnEVKARVEELDRKYY--EVKNKK 462
Cdd:pfam05483 399 FKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDL-EIQLTAIKTSEEHYlkEVEDLK 477
|
....*..
gi 36031035 463 DELQSER 469
Cdd:pfam05483 478 TELEKEK 484
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
717-889 |
1.08e-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: 42.22 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 717 QMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKR 796
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 797 VDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLnENLRKRLDQVEQELNELREteggtvltATTSELEAINKRVKDT 876
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEEL-AELEAELAELEAELEEKKA--------ELDEELAELEAELEEL 161
|
170
....*....|...
gi 36031035 877 MARSEDLDNSIDK 889
Cdd:COG1579 162 EAEREELAAKIPP 174
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
158-347 |
1.09e-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: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 158 LLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKW-DKMRRALE------------ 224
Cdd:pfam06160 279 LEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYTLNENELERVRGLEKQlEELEKRYDeiverleekeva 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 225 YTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKIsamkeEKEQLSAERQEQIKQRTK 304
Cdd:pfam06160 359 YSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLV-----EKSNLPGLPESYLDYFFD 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 36031035 305 LELKAKDLQDELAG---NSEQRKRLLKERQKLLEKIEEKQKELAET 347
Cdd:pfam06160 434 VSDEIEDLADELNEvplNMDEVNRLLDEAQDDVDTLYEKTEELIDN 479
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
173-499 |
1.10e-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: 43.09 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 173 EESISLMKETEGKREKINELlkyiEERLHTLEEEKEELAQYQKWDKMrralEYTIYNQELNETRAKLDELSAKRETSGEK 252
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNKL----EVELNKLEKQKKENKKNIDKFLT----EIKKKEKELEKLNNKYNDLKKQKEELENE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 253 SRQLRDAQQDARDKMEDIERQV-----------------RELKTKISAMKEEKEQLSaerqeqiKQRTKLELKAKDLQDE 315
Cdd:TIGR04523 175 LNLLEKEKLNIQKNIDKIKNKLlklelllsnlkkkiqknKSLESQISELKKQNNQLK-------DNIEKKQQEINEKTTE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 316 LAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRgSQFTSKEERDKWI 395
Cdd:TIGR04523 248 ISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELK-SELKNQEKKLEEI 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 396 KKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSE-RNYLWR 474
Cdd:TIGR04523 327 QNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKiQNQEKL 406
|
330 340
....*....|....*....|....*..
gi 36031035 475 EENAEQQ--ALAAKREDLEKKQQLLRA 499
Cdd:TIGR04523 407 NQQKDEQikKLQQEKELLEKEIERLKE 433
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
229-357 |
1.10e-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: 42.40 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 229 NQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSA---ERQEQIKQRTKL 305
Cdd:pfam06008 53 AQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSsdlSRMLAEAQRMLG 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 36031035 306 ELKAKDLQDELAGNSEQrkrlLKERQKLLEKIEEKQKEL-AETEPKFNSVKEK 357
Cdd:pfam06008 133 EIRSRDFGTQLQNAEAE----LKAAQDLLSRIQTWFQSPqEENKALANALRDS 181
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
362-499 |
1.16e-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: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 362 IARLAQATqerTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHK--DLEDTEANKEKNLEQYNKLDQ 439
Cdd:COG3206 150 AAAVANAL---AEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQknGLVDLSEEAKLLLQQLSELES 226
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 440 DLNEVKARVEELDRKYYEVKNKKDELQSERNYLwrEENAEQQALAAKREDLEKKQQLLRA 499
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGSGPDALPEL--LQSPVIQQLRAQLAELEAELAELSA 284
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
180-488 |
1.21e-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: 43.11 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 180 KETEGKREKINELLKYIEErLHTLEEEKEELAQYQKWDKMRRALeYTIYNQELNETRAKLdelsAKRETSGEKSRQLRDA 259
Cdd:TIGR00606 169 KALKQKFDEIFSATRYIKA-LETLRQVRQTQGQKVQEHQMELKY-LKQYKEKACEIRDQI----TSKEAQLESSREIVKS 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 260 QQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDL----QDELAGNSEQRKRLLKERQKLLE 335
Cdd:TIGR00606 243 YENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVfqgtDEQLNDLYHNHQRTVREKERELV 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 336 KIEEKQKELAETEPKFNSVKEKEERGIARL---AQATQERTDLYAKQGRGSQFTSKE---ERDKWIKKELKS----LDQA 405
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLqlqADRHQEHIRARDSLIQSLATRLELdgfERGPFSERQIKNfhtlVIER 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 406 INDKKRQIAAIHKDLEDTEANKEKNLEQY-NKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALA 484
Cdd:TIGR00606 403 QEDEAKTAAQLCADLQSKERLKQEQADEIrDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRK 482
|
....
gi 36031035 485 AKRE 488
Cdd:TIGR00606 483 AERE 486
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
325-506 |
1.35e-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: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 325 RLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLyakqgrgsqftsKEERDKwIKKELKSLDQ 404
Cdd:COG1579 7 RALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL------------EKEIKR-LELEIEEVEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 405 AINDKKRQIAAI--HKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQA 482
Cdd:COG1579 74 RIKKYEEQLGNVrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170 180
....*....|....*....|....
gi 36031035 483 LAAKREDLEKKQQLLRAATGKAIL 506
Cdd:COG1579 154 LEAELEELEAEREELAAKIPPELL 177
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
359-509 |
1.44e-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: 42.41 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 359 ERGIARLAQATQERTDLYAKQGR-----GSQFTSKEERDKwIKKELKSLDQAINDKKRQIAAIHKDLEDTEA-------N 426
Cdd:pfam00529 61 DSAEAQLAKAQAQVARLQAELDRlqaleSELAISRQDYDG-ATAQLRAAQAAVKAAQAQLAQAQIDLARRRVlapiggiS 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 427 KEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNylwREENAEQQALAAKREDLEKKQQLLRAATGKAIL 506
Cdd:pfam00529 140 RESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVR---SELSGAQLQIAEAEAELKLAKLDLERTEIRAPV 216
|
...
gi 36031035 507 NGI 509
Cdd:pfam00529 217 DGT 219
|
|
| MAT1 |
pfam06391 |
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ... |
227-352 |
1.57e-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: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 227 IYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQ--IKQRTK 304
Cdd:pfam06391 58 TNGIDVEETEKKIEQYEKENKDLILKNKMKLSQEEEELEELLELEKREKEERRKEEKQEEEEEKEKKEKAKQelIDELMT 137
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 36031035 305 LELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFN 352
Cdd:pfam06391 138 SNKDAEEIIAQHKKTAKKRKSERRRKLEELNRVLEQKPTQFSTGIKFG 185
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
700-1032 |
1.62e-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: 42.80 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 700 LRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMpkqRSLQSLEASLHAMESTRESLKa 779
Cdd:pfam15921 262 LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYM---RQLSDLESTVSQLRSELREAK- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 780 ELGTDLLSQLsledQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNEnlRKRLDQVEQELNEL---RETEGG 856
Cdd:pfam15921 338 RMYEDKIEEL----EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHK--REKELSLEKEQNKRlwdRDTGNS 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 857 TVLTATTSELEAINKRVKdtmaRSEDLDNSIDkteagiKELQKSMERwknmekeHMDAINHDTKELEKMTNRQGMLLKKK 936
Cdd:pfam15921 412 ITIDHLRRELDDRNMEVQ----RLEALLKAMK------SECQGQMER-------QMAAIQGKNESLEKVSSLTAQLESTK 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 937 EECMKKIRELGS--LPQEAFEKY---QTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGY 1011
Cdd:pfam15921 475 EMLRKVVEELTAkkMTLESSERTvsdLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALK 554
|
330 340
....*....|....*....|.
gi 36031035 1012 KSIMELMNVLELRKYEAIQLT 1032
Cdd:pfam15921 555 LQMAEKDKVIEILRQQIENMT 575
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
373-504 |
1.76e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 373 TDLYAKQGRGSQFTSKEERdkwIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELD 452
Cdd:COG3883 16 PQIQAKQKELSELQAELEA---AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 36031035 453 RKYYEVKNKKDEL------QSERNYLWR----------------EENAEQQALAAKREDLEKKQQLLRAATGKA 504
Cdd:COG3883 93 RALYRSGGSVSYLdvllgsESFSDFLDRlsalskiadadadlleELKADKAELEAKKAELEAKLAELEALKAEL 166
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
284-465 |
1.86e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 42.55 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 284 MKEEKEQ-----LSAErQEQIKQRTKLELKAkdlqdELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKE 358
Cdd:PRK00106 26 MKSAKEAaeltlLNAE-QEAVNLRGKAERDA-----EHIKKTAKRESKALKKELLLEAKEEARKYREEIEQEFKSERQEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 359 ERGIARLAQ--ATQERTDlyakqgrgSQFTSKEerdkwikKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNK 436
Cdd:PRK00106 100 KQIESRLTEraTSLDRKD--------ENLSSKE-------KTLESKEQSLTDKSKHIDEREEQVEKLEEQKKAELERVAA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 36031035 437 LDQD--------------LNEVKARVEELDRkyyEVKNKKDEL 465
Cdd:PRK00106 165 LSQAeareiilaetenklTHEIATRIREAER---EVKDRSDKM 204
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
173-429 |
2.08e-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: 42.40 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 173 EESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQyqkwdkMRRALEYTI--YNQELNETRAKLDELSAKRETSG 250
Cdd:pfam05483 506 QEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN------LRDELESVReeFIQKGDEVKCKLDKSEENARSIE 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 251 EKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKER 330
Cdd:pfam05483 580 YEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNY 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 331 QK-----------LLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAK--QGRGSQFTSKEERDKWIKK 397
Cdd:pfam05483 660 QKeiedkkiseekLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKiiEERDSELGLYKNKEQEQSS 739
|
250 260 270
....*....|....*....|....*....|..
gi 36031035 398 ELKSLDQAINDKKRQIAAIHKDLEDTEANKEK 429
Cdd:pfam05483 740 AKAALEIELSNIKAELLSLKKQLEIEKEEKEK 771
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
703-948 |
2.14e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 703 NIERINNEIDQLMNQMQQIETQQRKFKAsrdsiLSEMKMLKEKRQQsektfmpkqrsLQSLEASLHAMESTRESLKAELG 782
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDAREQIEL-----LEPIRELAERYAA-----------ARERLAELEYLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 783 TDLLsqlsledQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRLDQVEQELNELREteggtvltat 862
Cdd:COG4913 290 LELL-------EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLER---------- 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 863 tsELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINhdtKELEKMTNRQGMLLKKKEECMKK 942
Cdd:COG4913 353 --ELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE---EALAEAEAALRDLRRELRELEAE 427
|
....*.
gi 36031035 943 IRELGS 948
Cdd:COG4913 428 IASLER 433
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
186-491 |
2.17e-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: 41.98 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 186 REKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRAlEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARD 265
Cdd:pfam19220 26 KADFSQLIEPIEAILRELPQAKSRLLELEALLAQERA-AYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 266 KMEDIERQVRELKTKISA----MKEEKEQLSAERQEQIKQRTKLELKAKDLQD---ELAGNSEQRKRLLKERQKLLEKIE 338
Cdd:pfam19220 105 AKEELRIELRDKTAQAEAlerqLAAETEQNRALEEENKALREEAQAAEKALQRaegELATARERLALLEQENRRLQALSE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 339 EKQKELAETEPKfnsVKEKEERGIARLAQATQERTDLYAKQ-GRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIH 417
Cdd:pfam19220 185 EQAAELAELTRR---LAELETQLDATRARLRALEGQLAAEQaERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 418 KDLEDTEANKEKNLEQYNKLDQDLNE-------VKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDL 490
Cdd:pfam19220 262 QLLAEARNQLRDRDEAIRAAERRLKEasierdtLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAAL 341
|
.
gi 36031035 491 E 491
Cdd:pfam19220 342 E 342
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
153-493 |
2.31e-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: 42.26 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 153 SQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINEL-----LKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTI 227
Cdd:TIGR00618 436 QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLqtkeqIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNP 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 228 YNQELNETRAkldeLSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLEL 307
Cdd:TIGR00618 516 ARQDIDNPGP----LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQN 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 308 KAKDLQDELAGNSEQRKRLLKERQKLLEKIEEK-----------------QKELAETEPKFNSVKEKEERGIARLAQATQ 370
Cdd:TIGR00618 592 ITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEqdlqdvrlhlqqcsqelALKLTALHALQLTLTQERVREHALSIRVLP 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 371 ERT------DLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNE- 443
Cdd:TIGR00618 672 KELlasrqlALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHq 751
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 444 ----VKARVEELDRKYYEV------KNKKDELQSERNYLWREENAEQQALAAKREDLEKK 493
Cdd:TIGR00618 752 artvLKARTEAHFNNNEEVtaalqtGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQE 811
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
222-495 |
2.37e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 222 ALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARD--KMEDIERQVRELKTKISAMKEEKEQLSAERQEQI 299
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDarKAEEARKAEDARKAEEARKAEDAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 300 KQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLE--KIEEKQKelAETEPKFNSVKEKEErgiARLAQATQErtdlyA 377
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDarKAEAARK--AEEERKAEEARKAED---AKKAEAVKK-----A 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 378 KQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQ-DLNEVKARVEELDRKYY 456
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEaKKAEEKKKADEAKKKAE 1312
|
250 260 270
....*....|....*....|....*....|....*....
gi 36031035 457 EvKNKKDELQSernylwREENAEQQALAAKREDLEKKQQ 495
Cdd:PTZ00121 1313 E-AKKADEAKK------KAEEAKKKADAAKKKAEEAKKA 1344
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
697-945 |
2.61e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 697 NENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRES 776
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 777 LKAELGTDLLS----QLSLEDQKR--------VDALNDEIRQLQQENRQL------LNERI-KLEGIITRVETYL----- 832
Cdd:TIGR04523 466 LETQLKVLSRSinkiKQNLEQKQKelkskekeLKKLNEEKKELEEKVKDLtkkissLKEKIeKLESEKKEKESKIsdled 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 833 ----------NENLRKRLDQVEQELNELRETEggTVLTATTSELEainKRVKDTMARSEDLDNSIDKTEAGIKELQKSME 902
Cdd:TIGR04523 546 elnkddfelkKENLEKEIDEKNKEIEELKQTQ--KSLKKKQEEKQ---ELIDQKEKEKKDLIKEIEEKEKKISSLEKELE 620
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 36031035 903 rwkNMEKEHMDaINHDTKELEKMTNRQGMLLKKKEECMKKIRE 945
Cdd:TIGR04523 621 ---KAKKENEK-LSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
185-504 |
2.83e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 185 KREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDAR 264
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 265 DKMEDIERQVRELKtKISAmkeekeqlsAERQEQIKQRTKLElKAKDlqdelAGNSEQRKRLLKERqklleKIEEKQKel 344
Cdd:PTZ00121 1163 ARKAEEARKAEDAK-KAEA---------ARKAEEVRKAEELR-KAED-----ARKAEAARKAEEER-----KAEEARK-- 1219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 345 AETEPKFNSVKEKEE--RGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKElksldqaindKKRQIAAIHKDLED 422
Cdd:PTZ00121 1220 AEDAKKAEAVKKAEEakKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE----------EARKADELKKAEEK 1289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 423 TEANKEKNLEQYNKLDQ--DLNEVKARVEELDRKYYEVKNKKDELQSernylwREENAEQQALAAKREDlEKKQQLLRAA 500
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEakKKAEEAKKADEAKKKAEEAKKKADAAKK------KAEEAKKAAEAAKAEA-EAAADEAEAA 1362
|
....
gi 36031035 501 TGKA 504
Cdd:PTZ00121 1363 EEKA 1366
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1114-1185 |
2.93e-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: 2.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 36031035 1114 QLSGGQKSLVALALIFAIqkcDPApFYLFDEIDQALDAQHRKAVSDMIMELavHAQF-ITTTF----RPELLESADK 1185
Cdd:cd03296 136 QLSGGQRQRVALARALAV---EPK-VLLLDEPFGALDAKVRKELRRWLRRL--HDELhVTTVFvthdQEEALEVADR 206
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
183-503 |
3.12e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 183 EGKREKINELLKyiEERLHTLE-EEKEELAQYQKWDKMRRALEYTiynQELNETRAKLDELSAKRETSGEKSRQLRDAQQ 261
Cdd:pfam01576 600 EKKQKKFDQMLA--EEKAISARyAEERDRAEAEAREKETRALSLA---RALEEALEAKEELERTNKQLRAEMEDLVSSKD 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 262 DARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLE-----LKA---KDLQDELAGNSEQRKRLLKERQKL 333
Cdd:pfam01576 675 DVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEvnmqaLKAqfeRDLQARDEQGEEKRRQLVKQVREL 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 334 LEKIEEKQK--------------ELAETEPKFNSVKEKEERGIARLAQATQERTDLY-----AKQGRGSQFTSKEERDKW 394
Cdd:pfam01576 755 EAELEDERKqraqavaakkklelDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQreleeARASRDEILAQSKESEKK 834
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 395 IKKELKSLDQAIND------KKRQIAAIHKDLEDTEAN--KEKNLEQYNK---------LDQDLNEVKARVEELDRKY-- 455
Cdd:pfam01576 835 LKNLEAELLQLQEDlaaserARRQAQQERDELADEIASgaSGKSALQDEKrrleariaqLEEELEEEQSNTELLNDRLrk 914
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 36031035 456 --YEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQLLRAATGK 503
Cdd:pfam01576 915 stLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSK 964
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1110-1186 |
3.28e-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: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1110 REMQQLSGGQKSLVALALIFAIqkcdPAPFYLFDEIDQALDAQHRKAVSDMIMElavHAQ----FITTTFRPELLESADK 1185
Cdd:COG4133 127 LPVRQLSAGQKRRVALARLLLS----PAPLWLLDEPFTALDAAGVALLAELIAA---HLArggaVLLTTHQPLELAAARV 199
|
.
gi 36031035 1186 F 1186
Cdd:COG4133 200 L 200
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1113-1185 |
3.42e-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: 3.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 36031035 1113 QQLSGGQKSLVALA--LIfaiqkCDPaPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADK 1185
Cdd:COG2274 610 SNLSGGQRQRLAIAraLL-----RNP-RILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADR 678
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
169-499 |
3.53e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.86 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 169 DERKEESISLMKETEGKREKINE---LLKYIEERLHTLEEEKEELAQ-YQKW-DKMRRALEYTIYNQELNETRAKLDELS 243
Cdd:COG3096 281 RELSERALELRRELFGARRQLAEeqyRLVEMARELEELSARESDLEQdYQAAsDHLNLVQTALRQQEKIERYQEDLEELT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 244 AKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTkisamkeekeQLsAERQEqikqrtklelkAKDLQDELAGNSEQR 323
Cdd:COG3096 361 ERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKS----------QL-ADYQQ-----------ALDVQQTRAIQYQQA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 324 KRLLKERQKLLekieekqkELAETEPKfnSVKEKEERGIARLAQATQERTDLYAK----QGRGSQF-------------T 386
Cdd:COG3096 419 VQALEKARALC--------GLPDLTPE--NAEDYLAAFRAKEQQATEEVLELEQKlsvaDAARRQFekayelvckiageV 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 387 SKEERDKWIKKELKSL--DQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDE 464
Cdd:COG3096 489 ERSQAWQTARELLRRYrsQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEE 568
|
330 340 350
....*....|....*....|....*....|....*
gi 36031035 465 LQSERnylwREENAEQQALAAKREDLEKKQQLLRA 499
Cdd:COG3096 569 LEEQA----AEAVEQRSELRQQLEQLRARIKELAA 599
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1110-1164 |
3.68e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 40.74 E-value: 3.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 36031035 1110 REMQQLSGGQKSLVALALIFAIqkcDPApFYLFDEIDQALDAQHRKAVSDMIMEL 1164
Cdd:PRK13632 138 KEPQNLSGGQKQRVAIASVLAL---NPE-IIIFDESTSMLDPKGKREIKKIMVDL 188
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
278-482 |
3.72e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 278 KTKISAMKEEKEQLSAERQEQIKQRTKLELkakdlqdelagnSEQRKRLLKERQKLLEKIEEKQKELAETEpkfNSVKEK 357
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEAL------------LEAKEEIHKLRNEFEKELRERRNELQKLE---KRLLQK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 358 EErgiarlaqatqertdlyakqgrgsQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKL 437
Cdd:PRK12704 95 EE------------------------NLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 36031035 438 DQDlnEVKARVeeldrkyyeVKNKKDELQSERNYLWR--EENAEQQA 482
Cdd:PRK12704 151 TAE--EAKEIL---------LEKVEEEARHEAAVLIKeiEEEAKEEA 186
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
270-414 |
3.81e-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: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 270 IERQVRELKTKISAMKEEKEQLSAERQEQikQRTKLELKAKDLQDELagnseqrKRLLKERQKLLEKIEEKQKELAETEP 349
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEER--ELTEEEEEIRRLEEQV-------ERLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 36031035 350 KFNSVKEKEERGIARlaqatqERtdlyakqgrgsQFTSKEERDKWIKKELKSLDQAINDKKRQIA 414
Cdd:COG2433 449 ELSEARSEERREIRK------DR-----------EISRLDREIERLERELEEERERIEELKRKLE 496
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
171-360 |
3.82e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 171 RKEESISLMKETEGKREKINELLKYIEERlhtlEEEKEELAQYQKWDKMrraleytiynQELNETRAKLDELSAKRETSG 250
Cdd:COG5022 912 KKSLSSDLIENLEFKTELIARLKKLLNNI----DLEEGPSIEYVKLPEL----------NKLHEVESKLKETSEEYEDLL 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 251 EKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQE---------QIKQRTKLELKAKDLQdELAGNSE 321
Cdd:COG5022 978 KKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEvaelqsaskIISSESTELSILKPLQ-KLKGLLL 1056
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 36031035 322 QRKRLLKER------QKLLEKIEEKQKELAE-TEPKFNSVKEKEER 360
Cdd:COG5022 1057 LENNQLQARykalklRRENSLLDDKQLYQLEsTENLLKTINVKDLE 1102
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1115-1187 |
4.04e-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: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 1115 LSGGQKSLVALALifAI-QKCDpapFYLFDEIDQALDAQhrkaVSDMIME------LAVHAQFITTTFRPELLESADKFY 1187
Cdd:cd03250 128 LSGGQKQRISLAR--AVySDAD---IYLLDDPLSAVDAH----VGRHIFEncilglLLNNKTRILVTHQLQLLPHADQIV 198
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
735-969 |
4.14e-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: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 735 ILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELG----TDLLSQLSLEDQKRVDALNDEIRQLQQE 810
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKArqaeMDRQAAIYAEQERMAMERERELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 811 NRQLLNERIKLEGIITRVETY-----LNENLRKRLDQVEQELNELR-----ETEGGTVLTATTSELEAInkRVKDTMARS 880
Cdd:pfam17380 357 ERKRELERIRQEEIAMEISRMrelerLQMERQQKNERVRQELEAARkvkilEEERQRKIQQQKVEMEQI--RAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 881 EDLDNSIDKTEAGIKEL-QKSMERWKNMEKEHMDAINHDTKELEKmtNRQGMLLKKKEECMKKIRElgslpQEAFEKYQT 959
Cdd:pfam17380 435 REVRRLEEERAREMERVrLEEQERQQQVERLRQQEEERKRKKLEL--EKEKRDRKRAEEQRRKILE-----KELEERKQA 507
|
250
....*....|
gi 36031035 960 LSLKQLFRKL 969
Cdd:pfam17380 508 MIEEERKRKL 517
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
275-516 |
4.46e-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: 41.30 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 275 RELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELA-----GNSEQRKRLLKERQKLLEKIEEKQKELaetEP 349
Cdd:pfam18971 559 RNLENKLTAKGLSLQEANKLIKDFLSSNKELAGKALNFNKAVAeakstGNYDEVKKAQKDLEKSLRKREHLEKEV---EK 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 350 KFNSVKEKEERGIARlAQATQERTDLYAKQGRGSqftSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDT--EANK 427
Cdd:pfam18971 636 KLESKSGNKNKMEAK-AQANSQKDEIFALINKEA---NRDARAIAYTQNLKGIKRELSDKLEKISKDLKDFSKSfdEFKN 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 428 EKNlEQYNKLDQDLNEVKARVEELDRKyYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQllRAATGKAILN 507
Cdd:pfam18971 712 GKN-KDFSKAEETLKALKGSVKDLGIN-PEWISKVENLNAALNEFKNGKNKDFSKVTQAKSDLENSVK--DVIINQKVTD 787
|
....*....
gi 36031035 508 GIDSINKVL 516
Cdd:pfam18971 788 KVDNLNQAV 796
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
698-1047 |
4.86e-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: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 698 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKasrdSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTresl 777
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK----SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQ---- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 778 kaelgtdlLSQLSLEDQKRVDALNDEIRQLQQENRQLlneriklegiitrvetylnENLRKRLDQVEQELNELRETEGGT 857
Cdd:TIGR04523 255 --------LNQLKDEQNKIKKQLSEKQKELEQNNKKI-------------------KELEKQLNQLKSEISDLNNQKEQD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 858 VLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKKKE 937
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 938 ECMKKIRELGSLPQEAFEKYQTL-----SLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKrqeELDRGYK 1012
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKdeqikKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK---NLDNTRE 464
|
330 340 350
....*....|....*....|....*....|....*
gi 36031035 1013 SIMELMNVLElRKYEAIQLTFKQVSKNFSEVFQKL 1047
Cdd:TIGR04523 465 SLETQLKVLS-RSINKIKQNLEQKQKELKSKEKEL 498
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
268-433 |
5.08e-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: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 268 EDIERQVrELKTKISAMKEEKEQLSAERQEQIKQrtklELKAKdlQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAET 347
Cdd:pfam05262 188 EDNEKGV-NFRRDMTDLKERESQEDAKRAQQLKE----ELDKK--QIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 348 EPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKrqiAAIHKDLEDTEANK 427
Cdd:pfam05262 261 PKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKE---LEAQKKREPVAEDL 337
|
....*.
gi 36031035 428 EKNLEQ 433
Cdd:pfam05262 338 QKTKPQ 343
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
792-1006 |
5.38e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 792 EDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNEnLRKRLDQVEQELNELRETeggtvLTATTSELEAINK 871
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-LARRIRALEQELAALEAE-----LAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 872 RVKDTMARSEDLDNSIDKT-EAGIKELQKSMERWKNMEK--EHMDAIN-HDTKELEKMTNRQGMLLKKKEECMKKIRELG 947
Cdd:COG4942 98 ELEAQKEELAELLRALYRLgRQPPLALLLSPEDFLDAVRrlQYLKYLApARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 36031035 948 SLPQEAFEKYQTLSLKQLFRK--LEQCNTELKKYshvnKKALDQFVNFSEQKEKLIKRQEE 1006
Cdd:COG4942 178 ALLAELEEERAALEALKAERQklLARLEKELAEL----AAELAELQQEAEELEALIARLEA 234
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
155-373 |
5.42e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 155 RLKLLREVAGTRVYDE---RKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELaqyqkwDKMRRALEYtiynqe 231
Cdd:PRK05771 61 KLRSYLPKLNPLREEKkkvSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKEL------EQEIERLEP------ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 232 LNETRAKLDELSAKRETSGEKSRqlRDAQQDARDKMEDIERQVRELKTK-------ISAMKEEKEQLSAERQEQIKQRTK 304
Cdd:PRK05771 129 WGNFDLDLSLLLGFKYVSVFVGT--VPEDKLEELKLESDVENVEYISTDkgyvyvvVVVLKELSDEVEEELKKLGFERLE 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 36031035 305 LELKaKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAE----TEPKFNSVKEKEErgiARLAQATQERT 373
Cdd:PRK05771 207 LEEE-GTPSELIREIKEELEEIEKERESLLEELKELAKKYLEellaLYEYLEIELERAE---ALSKFLKTDKT 275
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
167-364 |
5.44e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 167 VYDERKEESISLMKETEGKREKINELLKYIEERLHTLEE-------EKEELAQYQKWDKM-RRALEYTIYNQELNETRAK 238
Cdd:PHA02562 221 KYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKlntaaakIKSKIEQFQKVIKMyEKGGVCPTCTQQISEGPDR 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 239 LDELSAKRETSGEKSRQLrdaqQDARDKMEDIERQVRELKTKISAMkeeKEQLSAERQeqikQRTKLELKAKDLQDELag 318
Cdd:PHA02562 301 ITKIKDKLKELQHSLEKL----DTAIDELEEIMDEFNEQSKKLLEL---KNKISTNKQ----SLITLVDKAKKVKAAI-- 367
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 36031035 319 nseqrKRLLKERQKLLEKIEEKQKELAET-EPKFNSVKEKEERGIAR 364
Cdd:PHA02562 368 -----EELQAEFVDNAEELAKLQDELDKIvKTKSELVKEKYHRGIVT 409
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
173-504 |
5.47e-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: 41.19 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 173 EESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALeytiyNQELNETRAKLdelsakretsgek 252
Cdd:TIGR00606 234 ESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKD-----NSELELKMEKV------------- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 253 srqLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQK 332
Cdd:TIGR00606 296 ---FQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQS 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 333 LLEKIEEKQKE---LAETEPKfNSVKEKEERGIARLAQATQERTDLYAKQG-RGSQFTSKEERDKWIKKELKSLDQAIND 408
Cdd:TIGR00606 373 LATRLELDGFErgpFSERQIK-NFHTLVIERQEDEAKTAAQLCADLQSKERlKQEQADEIRDEKKGLGRTIELKKEILEK 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 409 KKRQIAAIHKDLEDTEANKEKNLEqynkLDQDLNEVKARVEELDRKYYEVKNKKDE--LQSERNYLWREENAEQQALAAK 486
Cdd:TIGR00606 452 KQEELKFVIKELQQLEGSSDRILE----LDQELRKAERELSKAEKNSLTETLKKEVksLQNEKADLDRKLRKLDQEMEQL 527
|
330
....*....|....*...
gi 36031035 487 REDLEKKQQLLRAATGKA 504
Cdd:TIGR00606 528 NHHTTTRTQMEMLTKDKM 545
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
697-1007 |
5.71e-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: 40.77 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 697 NENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILsemKMLKEKRQQSEKTfmpkQRSLQSLEASLHAMESTRES 776
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIK---KQLSEKQKELEQN----NKKIKELEKQLNQLKSEISD 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 777 LKAELGTDLLSQlsledqkrvdaLNDEIRQLQQENRQLLNERIKLEGIITRVETYLNeNLRKRLDQVEQELNELRETegg 856
Cdd:TIGR04523 300 LNNQKEQDWNKE-----------LKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS-QLKKELTNSESENSEKQRE--- 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 857 tvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSM----ERWKNMEKEHmDAINHDTKELEKMTNRQGM- 931
Cdd:TIGR04523 365 --LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNqqkdEQIKKLQQEK-ELLEKEIERLKETIIKNNSe 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 932 ---LLKKKEECMKKIRELGSLPQEAFEKYQTLS---------LKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEK 999
Cdd:TIGR04523 442 ikdLTNQDSVKELIIKNLDNTRESLETQLKVLSrsinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
....*...
gi 36031035 1000 LIKRQEEL 1007
Cdd:TIGR04523 522 LKEKIEKL 529
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
254-335 |
5.90e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 40.74 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 254 RQLRDAQQDARDKMED------IERQVRELKtkiSAMKEEKEQLsAERQEQIKQRTK-------LELKAKDLQD------ 314
Cdd:pfam13779 489 RRLRAAQERLSEALERgasdeeIAKLMQELR---EALDDYMQAL-AEQAQQNPQDLQqpddpnaQEMTQQDLQRmldrie 564
|
90 100
....*....|....*....|...
gi 36031035 315 ELA--GNSEQRKRLLKERQKLLE 335
Cdd:pfam13779 565 ELArsGRRAEAQQMLSQLQQMLE 587
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1113-1165 |
6.04e-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: 6.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 36031035 1113 QQLSGGQKSLVALALIFAIQKcdpaPFYLFDEIDQALDAQHRKAVSDMIMELA 1165
Cdd:cd03226 125 LSLSGGQKQRLAIAAALLSGK----DLLIFDEPTSGLDYKNMERVGELIRELA 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1113-1164 |
6.12e-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: 6.12e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 36031035 1113 QQLSGGQKSLVALALIFAiqkCDPApFYLFDEIDQALDAQHRKAVSDMIMEL 1164
Cdd:COG1123 141 HQLSGGQRQRVAIAMALA---LDPD-LLIADEPTTALDVTTQAEILDLLREL 188
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
215-406 |
6.15e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 40.62 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 215 KWDKMRRALEYTIYNQELN--------ETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVR----ELKTKIS 282
Cdd:PRK00106 25 KMKSAKEAAELTLLNAEQEavnlrgkaERDAEHIKKTAKRESKALKKELLLEAKEEARKYREEIEQEFKserqELKQIES 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 283 AMKEEKEQLSAERQEQIKQRTKLELKAKDLQDelagnseqRKRLLKERQKLLEKIEEKQKELAEtepKFNSVKEKEERGI 362
Cdd:PRK00106 105 RLTERATSLDRKDENLSSKEKTLESKEQSLTD--------KSKHIDEREEQVEKLEEQKKAELE---RVAALSQAEAREI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 36031035 363 ArLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAI 406
Cdd:PRK00106 174 I-LAETENKLTHEIATRIREAEREVKDRSDKMAKDLLAQAMQRL 216
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
139-463 |
6.52e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 139 VKQGKINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINEllKYIEERLHTLEEEKEELAQYQKWDK 218
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE--KKAAEALKKEAEEAKKAEELKKKEA 1712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 219 mrraleytiynqelnETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRElKTKISAMKEEKEQLSAERQEQ 298
Cdd:PTZ00121 1713 ---------------EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKIAHLKKEEEKKAEEIRKE 1776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 299 IKQRTKLELKAKDLQDELagnseQRKRLLKERQKLLEKIEEKQKelaETEPKFNSVKEKEERGIARLAQATQ---ERTDL 375
Cdd:PTZ00121 1777 KEAVIEEELDEEDEKRRM-----EVDKKIKDIFDNFANIIEGGK---EGNLVINDSKEMEDSAIKEVADSKNmqlEEADA 1848
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 376 YAKQGRGSQFTSKE----ERDKWIKKELKSLDQAINDKKRQIAAIHK-DLEDTEAN---KEKNLEQ-YNKLDQDlnEVKA 446
Cdd:PTZ00121 1849 FEKHKFNKNNENGEdgnkEADFNKEKDLKEDDEEEIEEADEIEKIDKdDIEREIPNnnmAGKNNDIiDDKLDKD--EYIK 1926
|
330
....*....|....*..
gi 36031035 447 RVEELDRKYYEVKNKKD 463
Cdd:PTZ00121 1927 RDAEETREEIIKISKKD 1943
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
191-299 |
6.59e-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: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 191 ELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEytiYNQELNETRAKLDELSAKretsGEKSRQLRDAQQDARDKMEDI 270
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEASFERLAE---LRDELAELEEELEALKAR----WEAEKELIEEIQELKEELEQR 483
|
90 100
....*....|....*....|....*....
gi 36031035 271 ERQVRELKTKISAMKEEKEQLSAERQEQI 299
Cdd:COG0542 484 YGKIPELEKELAELEEELAELAPLLREEV 512
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
179-531 |
6.75e-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: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 179 MKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEytiynQELNETRAKLDELSAKRETSGEKSRQLRD 258
Cdd:TIGR00606 600 LASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLK-----EEIEKSSKQRAMLAGATAVYSQFITQLTD 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 259 --------AQQDARDKMEdIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKER 330
Cdd:TIGR00606 675 enqsccpvCQRVFQTEAE-LQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKL 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 331 QKLLEKIEEKQKELAETEPKFNSVKEKEERG---------IARLAQATQERTDLYAKQGRGSQFTSkeerdkwIKKELKS 401
Cdd:TIGR00606 754 QKVNRDIQRLKNDIEEQETLLGTIMPEEESAkvcltdvtiMERFQMELKDVERKIAQQAAKLQGSD-------LDRTVQQ 826
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 402 LDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVK--------------ARVEELDRKYYEVKNKKDELQS 467
Cdd:TIGR00606 827 VNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKseklqigtnlqrrqQFEEQLVELSTEVQSLIREIKD 906
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 36031035 468 ERNYLWREENAEQQALAAKREDLEKKQQLLRAATGKailngIDSINKVLE--HFRRKGINQHVQNG 531
Cdd:TIGR00606 907 AKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDK-----VNDIKEKVKniHGYMKDIENKIQDG 967
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1112-1161 |
6.77e-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: 6.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 36031035 1112 MQQLSGGQKSLVALALIFaIQKCDpapFYLFDEIDQALDAQHRKAVSDMI 1161
Cdd:cd03221 68 FEQLSGGEKMRLALAKLL-LENPN---LLLLDEPTNHLDLESIEALEEAL 113
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
192-370 |
6.89e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.46 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 192 LLKYIEERLHTLEEEKEELAQYQK-WDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQL--RDAQQDAR-DKM 267
Cdd:PRK12705 21 LVVLLKKRQRLAKEAERILQEAQKeAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLvqKEEQLDARaEKL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 268 EDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLElkakdlqdelagNSEQRKRLLKERQKLLEkiEEKQKELAET 347
Cdd:PRK12705 101 DNLENQLEEREKALSARELELEELEKQLDNELYRVAGLT------------PEQARKLLLKLLDAELE--EEKAQRVKKI 166
|
170 180
....*....|....*....|...
gi 36031035 348 EPKFNSVKEKEERGIarLAQATQ 370
Cdd:PRK12705 167 EEEADLEAERKAQNI--LAQAMQ 187
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1110-1165 |
7.01e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.56 E-value: 7.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 36031035 1110 REMQQLSGG--QKSLVALALIfaiqkcDPAPFYLFDEIDQALDAQHRKAVSDMIMELA 1165
Cdd:PRK13409 208 RDISELSGGelQRVAIAAALL------RDADFYFFDEPTSYLDIRQRLNVARLIRELA 259
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
178-500 |
7.10e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 40.29 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 178 LMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIynqELNETRAKLDELSAKRETSGEKSRQLR 257
Cdd:pfam13868 33 RIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQI---EEREQKRQEEYEEKLQEREQMDEIVER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 258 DAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKI 337
Cdd:pfam13868 110 IQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 338 EEKQKELAETepkfnsvKEKEERGIARLAQATQERtdlyakqgrgsqftskeerdKWIKKELksldQAINDKKRQIAAIH 417
Cdd:pfam13868 190 RAQQEKAQDE-------KAERDELRAKLYQEEQER--------------------KERQKER----EEAEKKARQRQELQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 418 KDLEDTEANKEKNLEQYNKLDQDLNE-VKARVEELDRKYYEVKNKKDELQSE--RNYLWREENAEQQALAAKREDLEKKQ 494
Cdd:pfam13868 239 QAREEQIELKERRLAEEAEREEEEFErMLRKQAEDEEIEQEEAEKRRMKRLEhrRELEKQIEEREEQRAAEREEELEEGE 318
|
....*.
gi 36031035 495 QLLRAA 500
Cdd:pfam13868 319 RLREEE 324
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
233-496 |
7.45e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.18 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 233 NETRAKLDELSAKRETSGEKSRQLRDAQQDARD----------KMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQR 302
Cdd:pfam15905 52 TARKVKSLELKKKSQKNLKESKDQKELEKEIRAlvqergeqdkRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 303 TKLELKAKDLQDELAGNSEQRK--RLLKERQKLLEKIEEKQKELAEtepkfnsvkekEERGIARLAQATQerTDLYAKQG 380
Cdd:pfam15905 132 LELTRVNELLKAKFSEDGTQKKmsSLSMELMKLRNKLEAKMKEVMA-----------KQEGMEGKLQVTQ--KNLEHSKG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 381 RGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTE---ANKEKNLEQYNKLDQDL-NEVKARVEELDRKYY 456
Cdd:pfam15905 199 KVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKldiAQLEELLKEKNDEIESLkQSLEEKEQELSKQIK 278
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 36031035 457 EVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQL 496
Cdd:pfam15905 279 DLNEKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTL 318
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
173-500 |
7.78e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 173 EESISLMKE---TEGKREKINELLKYIEERLHTLEEEKEELAQ-YQKW-DKMRRALEYTIYNQELNETRAKLDELSAKRE 247
Cdd:PRK04863 286 EEALELRRElytSRRQLAAEQYRLVEMARELAELNEAESDLEQdYQAAsDHLNLVQTALRQQEKIERYQADLEELEERLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 248 TSGEKSRQLRDAQQDARDKMEDIERQVRELKTkisamkeekeQLSAERQeqikqrtklelkAKDLQDELAGNSEQRKRLL 327
Cdd:PRK04863 366 EQNEVVEEADEQQEENEARAEAAEEEVDELKS----------QLADYQQ------------ALDVQQTRAIQYQQAVQAL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 328 KERQKLLekieekqkELAETEPKfnSVKEKEERGIARLAQATQERTDLYAK----QGRGSQFT-------------SKEE 390
Cdd:PRK04863 424 ERAKQLC--------GLPDLTAD--NAEDWLEEFQAKEQEATEELLSLEQKlsvaQAAHSQFEqayqlvrkiagevSRSE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 391 RDKWIKKELKSL--DQAINDKKRQIAAIHKDLE---DTEANKEKNLEQYNK-----------LDQDLNEVKARVEELDrk 454
Cdd:PRK04863 494 AWDVARELLRRLreQRHLAEQLQQLRMRLSELEqrlRQQQRAERLLAEFCKrlgknlddedeLEQLQEELEARLESLS-- 571
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 36031035 455 yyEVKNKKDELQSernylwrEENAEQQALAAKREDLEKKQQLLRAA 500
Cdd:PRK04863 572 --ESVSEARERRM-------ALRQQLEQLQARIQRLAARAPAWLAA 608
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
670-884 |
7.91e-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: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 670 DTRKSRLELQKDVRKAEEELGELEAKLNENLRRN-IERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQ 748
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEFRQKNgLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 749 SEKT--FMPKQRSLQSLEASLHAMESTRESLKAELGtdllsqlslEDQKRVDALNDEI----RQLQQENRQLLNE-RIKL 821
Cdd:COG3206 252 GPDAlpELLQSPVIQQLRAQLAELEAELAELSARYT---------PNHPDVIALRAQIaalrAQLQQEAQRILASlEAEL 322
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 36031035 822 EGIITRVETylnenLRKRLDQVEQELNELRETEggTVLTATTSELEAINKRVKDTMARSEDLD 884
Cdd:COG3206 323 EALQAREAS-----LQAQLAQLEARLAELPELE--AELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
834-1025 |
8.36e-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: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 834 ENLRKRLDQVEQELNELRETEggtvlTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMD 913
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEE-----KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 914 AINHDTKELEKMTNRQG-MLLKKKEECMKKIRELGSLpqeafeKYQTLSLKQLFRKLEQCNTELKKyshVNKKALDQFVN 992
Cdd:COG4942 105 ELAELLRALYRLGRQPPlALLLSPEDFLDAVRRLQYL------KYLAPARREQAEELRADLAELAA---LRAELEAERAE 175
|
170 180 190
....*....|....*....|....*....|...
gi 36031035 993 FSEQKEKLIKRQEELDRGYKSIMELMNVLELRK 1025
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
733-820 |
8.54e-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: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 733 DSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENR 812
Cdd:smart00935 7 QKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQ 86
|
....*...
gi 36031035 813 QLLNERIK 820
Cdd:smart00935 87 KRQQEELQ 94
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
206-467 |
8.68e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.06 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 206 EKEELAQYQKwdKMRRALeytiynqelnetrakLDELSAKRETSGEKSRQLRDAQqdarDKMEDIERQVRELKTKISAMK 285
Cdd:PRK11637 58 AKEKSVRQQQ--QQRASL---------------LAQLKKQEEAISQASRKLRETQ----NTLNQLNKQIDELNASIAKLE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 286 EEK--------EQL-SAERQeqiKQRTKLELKakdlqdeLAGNSEQRK-RLL-------KERQKLLEKIEEKQKELAETE 348
Cdd:PRK11637 117 QQQaaqerllaAQLdAAFRQ---GEHTGLQLI-------LSGEESQRGeRILayfgylnQARQETIAELKQTREELAAQK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 349 pkfnsvKEKEERgiarlaqATQERTDLYAKQGRGSQFT-SKEERdkwiKKELKSLDQAINDKKRQIAAIHKD---LEDTE 424
Cdd:PRK11637 187 ------AELEEK-------QSQQKTLLYEQQAQQQKLEqARNER----KKTLTGLESSLQKDQQQLSELRANesrLRDSI 249
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 36031035 425 ANKEKnleqynkldqdlnEVKARVEELDRKYYEVKNKKDELQS 467
Cdd:PRK11637 250 ARAER-------------EAKARAEREAREAARVRDKQKQAKR 279
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
247-345 |
8.69e-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: 39.03 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 247 ETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKD-------LQDELAGN 319
Cdd:pfam06785 79 ELDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEEqlaekqlLINEYQQT 158
|
90 100
....*....|....*....|....*.
gi 36031035 320 SEQRKRLLKERQKLLEKIEEKQKELA 345
Cdd:pfam06785 159 IEEQRSVLEKRQDQIENLESKVRDLN 184
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
154-385 |
8.73e-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: 40.34 E-value: 8.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 154 QRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQ------------------YQK 215
Cdd:TIGR00618 643 LKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQcqtllrelethieeydreFNE 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 216 WDKMRRALEYTI------YNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIErqvRELKTKISAMkEEKE 289
Cdd:TIGR00618 723 IENASSSLGSDLaaredaLNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLA---AEIQFFNRLR-EEDT 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 290 QLSAERQEQIKQRTKLELKAKDLQDE-LAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEergiarlAQA 368
Cdd:TIGR00618 799 HLLKTLEAEIGQEIPSDEDILNLQCEtLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQ-------AKI 871
|
250
....*....|....*..
gi 36031035 369 TQERTDLYAKQGRGSQF 385
Cdd:TIGR00618 872 IQLSDKLNGINQIKIQF 888
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1110-1172 |
8.75e-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: 8.75e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 36031035 1110 REMQQLSGGQKSLVALALIFAIQkcdpaPFYL-FDEIDQALDAQHRKAVSDMIMELavHAQFIT 1172
Cdd:COG1122 130 RPPHELSGGQKQRVAIAGVLAME-----PEVLvLDEPTAGLDPRGRRELLELLKRL--NKEGKT 186
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
193-297 |
8.78e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 40.05 E-value: 8.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36031035 193 LKYIEERLHTLEE------EKEELAQYQKWDKMRRALEytiynqelnetrAKLDELSAKRETSGEKSRQLRDAQQDARDK 266
Cdd:PRK05431 4 IKLIRENPEAVKEalakrgFPLDVDELLELDEERRELQ------------TELEELQAERNALSKEIGQAKRKGEDAEAL 71
|
90 100 110
....*....|....*....|....*....|.
gi 36031035 267 MEdierQVRELKTKISAMKEEKEQLSAERQE 297
Cdd:PRK05431 72 IA----EVKELKEEIKALEAELDELEAELEE 98
|
|
| |
