|
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 ... |
2-1196 |
4.14e-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: 414.37 E-value: 4.14e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 2 YIKQVIIQGFRSYRdQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSD-EFSHLRPEQRLALLHEGTGPRVISAFVEI 80
Cdd:pfam02463 1 YLKRIEIEGFKSYA-KTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGErSAKSLRSERLSDLIHSKSGAFVNSAEVEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 81 IFDNSDNRLPIDKEEVSLRRVIGAKKD-QYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKLL 159
Cdd:pfam02463 80 TFDNEDHELPIDKEEVSIRRRVYRGGDsEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 160 REVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKL 239
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 240 DELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGN 319
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 320 SEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKEL 399
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 400 KSL----DQAINDKKRQIAAIHKDLEDTEANKEKNLEQYKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREE 475
Cdd:pfam02463 400 KSEeekeAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 476 NAEQQALaaKREDLEKKQQLLRAATGKAILNGIDSINKVLEHFRRKGINQHVQNGYHGIVMNNFECEPAFYTCVEVTAGN 555
Cdd:pfam02463 480 VKLQEQL--ELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATA 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 556 RLFYHIVDSDEVSTKILMEFNKMNLPGEVTFLPLNKLDVrdtaypetndaipmisklryNPRFDKAFKHVFGKTLICRSM 635
Cdd:pfam02463 558 DEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV--------------------LEIDPILNLAQLDKATLEADE 617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 636 EVSTQLARAFTMDCITLEGDQVSHRGALTGGYYDTRKSRLELQKDVRKAEEELGELEAKLNENLRRNIERINNEIDQLMN 715
Cdd:pfam02463 618 DDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRR 697
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 716 QMQQIETQQRKFKASRDSILSEMKMlKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKR 795
Cdd:pfam02463 698 QLEIKKKEQREKEELKKLKLEAEEL-LADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKEL 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 796 VDALNDEIRQLQQEnrqllneriKLEGIITRVETYLNENLRKRLDQVEQELNELRETEGGTVLTATTSELEAINKRVKDT 875
Cdd:pfam02463 777 AEEREKTEKLKVEE---------EKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQK 847
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 876 MARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEAFEK 955
Cdd:pfam02463 848 LEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEA 927
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 956 --------YQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGYKSIMELMNVLELRKYEA 1027
Cdd:pfam02463 928 eillkyeeEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKL 1007
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 1028 IQLTFKQVSKNFSEVFQKLVPggkatlvMKKGDVEGSQSQDEGEGSGEsergsgsqsSVPSVDQFTGVGIRVSFTGKQGE 1107
Cdd:pfam02463 1008 IRAIIEETCQRLKEFLELFVS-------INKGWNKVFFYLELGGSAEL---------RLEDPDDPFSGGIEISARPPGKG 1071
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 1108 MREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYG 1187
Cdd:pfam02463 1072 VKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVG 1151
|
1210
....*....|
gi 38566257 1188 VKF-RNKVSH 1196
Cdd:pfam02463 1152 VTMvENGVST 1161
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-1191 |
8.63e-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: 349.75 E-value: 8.63e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 2 YIKQVIIQGFRSYRDQTIVdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSH-LRPEQRLALLHEG-TGPRVISAFVE 79
Cdd:TIGR02169 1 YIERIELENFKSFGKKKVI-PFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKaMRAERLSDLISNGkNGQSGNEAYVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 80 IIFDNSDNRLPiDKEEVSLRRVIG--AKKDQYFLDKKMVTKNDVMNLLESAGFSrSNPYYIVKQGKINQMATAPDSQRLK 157
Cdd:TIGR02169 80 VTFKNDDGKFP-DELEVVRRLKVTddGKYSYYYLNGQRVRLSEIHDFLAAAGIY-PEGYNVVLQGDVTDFISMSPVERRK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 158 LLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRA 237
Cdd:TIGR02169 158 IIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALER 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 238 KLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAM--------KEEKEQLSAERQEQIKQRTKLELKA 309
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERSIAEKEREL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 310 KDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQE----RTDLYAKQGRGSQF 385
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEfaetRDELKDYREKLEKL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 386 TSK-----EERDKWIkKELKSLDQAINDKKRQIAAIHKDLEDTEANKE-KNLEQYKLDQDLNEVKARVEELDRKYYEVKN 459
Cdd:TIGR02169 398 KREinelkRELDRLQ-EELQRLSEELADLNAAIAGIEAKINELEEEKEdKALEIKKQEWKLEQLAADLSKYEQELYDLKE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 460 KKDELQSERNYLWRE-ENAEQQALAAKREdlekkqQLLRAATGKAILNGIDsinkvlehfrrkginqhvqnGYHGIVMNN 538
Cdd:TIGR02169 477 EYDRVEKELSKLQRElAEAEAQARASEER------VRGGRAVEEVLKASIQ--------------------GVHGTVAQL 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 539 FECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLpGEVTFLPLNKLDV--RDTAYPETNDAIPM-ISKLRYN 615
Cdd:TIGR02169 531 GSVGERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKA-GRATFLPLNKMRDerRDLSILSEDGVIGFaVDLVEFD 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 616 PRFDKAFKHVFGKTLICRSMEVSTQLARAFTMdcITLEGDQVSHRGALTGGYYDTRKSRLELQKDVRKAEEELGELEAKL 695
Cdd:TIGR02169 610 PKYEPAFKYVFGDTLVVEDIEAARRLMGKYRM--VTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLK 687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 696 NE--NLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTR 773
Cdd:TIGR02169 688 RElsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARI 767
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 774 ESLKAELGTdllSQLSLEDQKRVDAlNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRL---DQVEQELNELR 850
Cdd:TIGR02169 768 EELEEDLHK---LEEALNDLEARLS-HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEyleKEIQELQEQRI 843
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 851 ETEGGTVltATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGM 930
Cdd:TIGR02169 844 DLKEQIK--SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 931 LLKKKEECMKKIRELGSLPQEAFE-KYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRG 1009
Cdd:TIGR02169 922 LKAKLEALEEELSEIEDPKGEDEEiPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 1010 YKSIMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKLvPGGKATLVMKKGDvegsqsqdegegsgesergsgsqssvpsv 1089
Cdd:TIGR02169 1002 RKAILERIEEYEKKKREVFMEAFEAINENFNEIFAEL-SGGTGELILENPD----------------------------- 1051
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 1090 DQFTGvGIRVSFTGKQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQF 1169
Cdd:TIGR02169 1052 DPFAG-GLELSAKPKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQF 1130
|
1210 1220
....*....|....*....|..
gi 38566257 1170 ITTTFRPELLESADKFYGVKFR 1191
Cdd:TIGR02169 1131 IVVSLRSPMIEYADRAIGVTMR 1152
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
3-158 |
6.07e-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: 6.07e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 3 IKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPRVISAFVEIIF 82
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEPFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALLHEGSGPSVMSAYVEIIF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38566257 83 DNSDNRLPIDKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKL 158
Cdd:cd03272 81 DNSDNRFPIDKEEVRLRRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMKQDEQQEM 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-1197 |
5.15e-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: 325.09 E-value: 5.15e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 2 YIKQVIIQGFRSYRDQTIVDpFSSKHNVIVGRNGSGKSNFFYAIQFVLSdefshlrpEQRLALLHEGTGPRVI------- 74
Cdd:TIGR02168 1 RLKKLELAGFKSFADPTTIN-FDKGITGIVGPNGCGKSNIVDAIRWVLG--------EQSAKALRGGKMEDVIfngsetr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 75 ----SAFVEIIFDNSDNRLP-IDKEEVSLRRVIGAKKD-QYFLDKKMVTKNDVMNLLESAGFSRSNpYYIVKQGKINQMA 148
Cdd:TIGR02168 72 kplsLAEVELVFDNSDGLLPgADYSEISITRRLYRDGEsEYFINGQPCRLKDIQDLFLDTGLGKRS-YSIIEQGKISEII 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 149 TAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIY 228
Cdd:TIGR02168 151 EAKPEERRAIFEEAAGISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 229 NQELNETRAKLDELSAKREtsgEKSRQLRDAQQDARDKMEDIErqvrELKTKISAMKEEKEQLSAERQEQIKQRTKLELK 308
Cdd:TIGR02168 231 VLRLEELREELEELQEELK---EAEEELEELTAELQELEEKLE----ELRLEVSELEEEIEELQKELYALANEISRLEQQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 309 AKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLyakqgrgsqftsk 388
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL------------- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 389 EERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEK-NLEQYKLDQDLNEVKARVEELDRKyyEVKNKKDELQSE 467
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERlEDRRERLQQEIEELLKKLEEAELK--ELQAELEELEEE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 468 RNYLWREENAEQQALAAKREDLEKKQQLLRAATGKA--ILNGIDSINKVLEHFRRKGI-------NQHVQNGYHGIVMNN 538
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELaqLQARLDSLERLQENLEGFSEgvkallkNQSGLSGILGVLSEL 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 539 FECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILmEFNKMNLPGEVTFLPLNKLDVRDTAYPETNDAIPMISKLR----- 613
Cdd:TIGR02168 529 ISVDEGYEAAIEAALGGRLQAVVVENLNAAKKAI-AFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGvakdl 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 614 --YNPRFDKAFKHVFGKTLICRSMEVSTQLARA--FTMDCITLEGDQVSHRGALTGGYYDTRKSRL-------ELQKDVR 682
Cdd:TIGR02168 608 vkFDPKLRKALSYLLGGVLVVDDLDNALELAKKlrPGYRIVTLDGDLVRPGGVITGGSAKTNSSILerrreieELEEKIE 687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 683 KAEEELGELEAKLNEnLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTF-------MPK 755
Cdd:TIGR02168 688 ELEEKIAELEKALAE-LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELteleaeiEEL 766
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 756 QRSLQSLEASLHAMESTRESLKAELgTDLLSQLSLEDqKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLnENL 835
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQI-EQLKEELKALR-EALDELRAELTLLNEEAANLRERLESLERRIAATERRL-EDL 843
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 836 RKRLDQVEQELNELRE--TEGGTVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKsmerwKNMEKEHmdA 913
Cdd:TIGR02168 844 EEQIEELSEDIESLAAeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES-----KRSELRR--E 916
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 914 INHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQE---AFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFV 990
Cdd:TIGR02168 917 LEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeaeALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYE 996
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 991 NFSEQKEKLIKRQEELDRGYKSIMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKLVPGGKATLVMKKGDvegsqsqDEG 1070
Cdd:TIGR02168 997 ELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRVFPKLFGGGEAELRLTDPE-------DLL 1069
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 1071 EgsgesergsgsqssvpsvdqfTGVGIRVSFTGKQgeMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDA 1150
Cdd:TIGR02168 1070 E---------------------AGIEIFAQPPGKK--NQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDD 1126
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....*...
gi 38566257 1151 QHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYGVKFRNK-VSHI 1197
Cdd:TIGR02168 1127 ANVERFANLLKEFSKNTQFIVITHNKGTMEVADQLYGVTMQEKgVSKI 1174
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-1188 |
9.10e-72 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 259.87 E-value: 9.10e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 1 MYIKQVIIQGFRSYRDQTIVdPFSSKHNVIVGRNGSGKSNFFYAIQFVL---SdeFSHLRPEQRLALLHEGTGPR--VIS 75
Cdd:COG1196 1 MRLKRLELAGFKSFADPTTI-PFEPGITAIVGPNGSGKSNIVDAIRWVLgeqS--AKSLRGGKMEDVIFAGSSSRkpLGR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 76 AFVEIIFDNSDNRLPIDKEEVSLRRVIGAKKD-QYFLDKKMVTKNDVMNLLESAGFSRsNPYYIVKQGKINQMATAPDSQ 154
Cdd:COG1196 78 AEVSLTFDNSDGTLPIDYDEVTITRRLYRSGEsEYYINGKPCRLKDIQDLFLDTGLGP-ESYSIIGQGMIDRIIEAKPEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 155 RLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNE 234
Cdd:COG1196 157 RRAIIEEAAGISKYKERKEEAERKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 235 TRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQD 314
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 315 ELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLyakqgrgsqftsKEERDKW 394
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA------------EEELEEL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 395 IKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWRE 474
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 475 ENAEQQALAAKREDLEKKQQLLRAAtgKAILNGIDSINKVLEHFRRKGINQHV---QNGYHGIVMNNFECEPAFYTCVEV 551
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEA--AARLLLLLEAEADYEGFLEGVKAALLlagLRGLAGAVAVLIGVEAAYEAALEA 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 552 TAGNRLFYHIVDSDEVSTKILmEFNKMNLPGEVTFLPLNKLDVRDTAYPETNDA--IPMISKLRYNPRFDKAFKHVFGKT 629
Cdd:COG1196 543 ALAAALQNIVVEDDEVAAAAI-EYLKAAKAGRATFLPLDKIRARAALAAALARGaiGAAVDLVASDLREADARYYVLGDT 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 630 LICRSMEVSTQLARAFTMDciTLEGDQVSHRGALTGGyydtrksrlelqkdvrkaeeelgeleaklnenlrrnierinne 709
Cdd:COG1196 622 LLGRTLVAARLEAALRRAV--TLAGRLREVTLEGEGG------------------------------------------- 656
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 710 idqlmNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKtfmpkqrsLQSLEASLHAMESTRESLKAELGTDLLSQLS 789
Cdd:COG1196 657 -----SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE--------LELEEALLAEEEEERELAEAEEERLEEELEE 723
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 790 LEDQKRVDALNDEIRQLQQENRQLLNEriklEGIITRVETYLNENLRKRLDQVEQELNELretegGTV-LTAtTSELEAI 868
Cdd:COG1196 724 EALEEQLEAEREELLEELLEEEELLEE----EALEELPEPPDLEELERELERLEREIEAL-----GPVnLLA-IEEYEEL 793
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 869 NKRVKDTMARSEDLDNSIDKTEAGIKElqksmerwknmekehmdaINHDTKELekmtnrqgmllkkkeecmkkirelgsl 948
Cdd:COG1196 794 EERYDFLSEQREDLEEARETLEEAIEE------------------IDRETRER--------------------------- 828
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 949 pqeafekyqtlslkqlfrkleqcntelkkyshvnkkaldqfvnFSEqkeklikrqeeldrgyksimelmnvlelrkyeai 1028
Cdd:COG1196 829 -------------------------------------------FLE---------------------------------- 831
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 1029 qlTFKQVSKNFSEVFQKLVPGGKATLVMKKGDvegsqsqdegegsgesergsgsqssvpsvDQF-TGVGIRVSFTGKqgE 1107
Cdd:COG1196 832 --TFDAVNENFQELFPRLFGGGEAELLLTDPD-----------------------------DPLeTGIEIMAQPPGK--K 878
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 1108 MREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQ--HRkaVSDMIMELAVHAQFITTTFRPELLESADKF 1185
Cdd:COG1196 879 LQRLSLLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDAnvER--FAELLKEMSEDTQFIVITHNKRTMEAADRL 956
|
...
gi 38566257 1186 YGV 1188
Cdd:COG1196 957 YGV 959
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1104-1198 |
3.60e-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: 3.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 1104 KQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESAD 1183
Cdd:cd03272 149 KQDEQQEMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVAD 228
|
90
....*....|....*
gi 38566257 1184 KFYGVKFRNKVSHID 1198
Cdd:cd03272 229 KFYGVKFRNKVSTID 243
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1061-1196 |
7.40e-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: 7.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 1061 VEGSQSQDEGEGSGESERGSGSQSSVPSVDqftgVGI----RVSFTgKQGEMREMqqLSGGQKSLVALALIFAIQKCDPA 1136
Cdd:cd03239 45 VLGGKAAKLRRGSLLFLAGGGVKAGINSAS----VEItfdkSYFLV-LQGKVEQI--LSGGEKSLSALALIFALQEIKPS 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38566257 1137 PFYLFDEIDQALDAQHRKAVSDMIMELAVH-AQFITTTFRPELLESADKFYGVKFRNKVSH 1196
Cdd:cd03239 118 PFYVLDEIDAALDPTNRRRVSDMIKEMAKHtSQFIVITLKKEMFENADKLIGVLFVHGVST 178
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-85 |
1.00e-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: 119.72 E-value: 1.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 3 IKQVIIQGFRSYRDQTIVdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPRVISAFVEIIF 82
Cdd:cd03239 1 IKQITLKNFKSYRDETVV-GGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAGGGVKAGINSASVEITF 79
|
...
gi 38566257 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 ... |
529-641 |
3.44e-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: 3.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 529 NGYHGIVMNNFECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILmEFNKMNLPGEVTFLPLNKLD--------VRDTAYP 600
Cdd:smart00968 1 PGVLGRVADLISVDPKYETALEAALGGRLQAVVVDTEETAKKAI-EFLKKNRLGRATFLPLDKIKprspagskLREALLP 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 38566257 601 ETNDAIPMISKLRYNPRFDKAFKHVFGKTLICRSMEVSTQL 641
Cdd:smart00968 80 EPGFVGPAIDLVEYDPELRPALEYLLGNTLVVDDLETARRL 120
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1113-1192 |
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 38566257 1113 QLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVH-AQFITTTFRPELLESADKFYGVKFR 1191
Cdd:cd03227 77 QLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKgAQVIVITHLPELAELADKLIHIKKV 156
|
.
gi 38566257 1192 N 1192
Cdd:cd03227 157 I 157
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-144 |
5.14e-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: 5.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 1 MYIKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLS-DEFSHLRPEQRLALLHEGTGPRVISAFVE 79
Cdd:cd03273 1 MHIKEIILDGFKSYATRTVISGFDPQFNAITGLNGSGKSNILDAICFVLGiTNLSTVRASNLQDLIYKRGQAGITKASVT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 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 ... |
1103-1195 |
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 38566257 1103 GKQgeMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESA 1182
Cdd:cd03278 105 GKK--VQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAA 182
|
90
....*....|....
gi 38566257 1183 DKFYGVKFRNK-VS 1195
Cdd:cd03278 183 DRLYGVTMQESgVS 196
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
529-642 |
1.97e-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: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 529 NGYHGIVMNNFECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLpGEVTFLPLNKLDVRDTAYPET--NDAI 606
Cdd:pfam06470 2 KGVLGRLADLIEVDEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKL-GRATFLPLDRLKPRPRRPGADlkGGAG 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 38566257 607 PMISKLRYNPRFDKAFKHVFGKTLICRSMEVSTQLA 642
Cdd:pfam06470 81 PLLDLVEYDDEYRKALRYLLGNTLVVDDLDEALELA 116
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1113-1198 |
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 38566257 1113 QLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYGVKFRN 1192
Cdd:cd03273 166 ELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNANVLFRTRFVD 245
|
....*.
gi 38566257 1193 KVSHID 1198
Cdd:cd03273 246 GTSTVT 251
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1109-1197 |
9.41e-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: 9.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 1109 REMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAV-HAQFITTTFRPELLESADKFYG 1187
Cdd:cd03275 151 RDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGpNFQFIVISLKEEFFSKADALVG 230
|
90
....*....|...
gi 38566257 1188 VkFRNK---VSHI 1197
Cdd:cd03275 231 V-YRDQecnSSKV 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-469 |
3.20e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 84.35 E-value: 3.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFVL-SDEFSHLRPEQRLALLHEGTGPRVISAFVE 79
Cdd:PRK03918 1 MKIEELKIKNFRSHKSSVV--EFDDGINLIIGQNGSGKSSILEAILVGLyWGHGSKPKGLKKDDFTRIGGSGTEIELKFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 80 iiFDNSDNRL--PIDKEEVSLRRVIGAKKDqyfLDKKMVTKNDVMNLLESAGFsrSNPYYIvKQGKINQMATApDSQRLK 157
Cdd:PRK03918 79 --KNGRKYRIvrSFNRGESYLKYLDGSEVL---EEGDSSVREWVERLIPYHVF--LNAIYI-RQGEIDAILES-DESREK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 158 LLREVAGTRVYDERKEESISLMKETEGKREKINELLKY---IEERLHTLEEEKEELAQ------------YQKWDKMRRA 222
Cdd:PRK03918 150 VVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRtenIEELIKEKEKELEEVLReineisselpelREELEKLEKE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 223 L-EYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKtKISAMKEEKEQLSAERQEQIKQ 301
Cdd:PRK03918 230 VkELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 302 RTKLELKAKDLQDELAGNSEQRKRL------LKERQKLLEKIEEKQKELAETEPKFNSVKEKE---ERGIARLAQATQER 372
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELeekeerLEELKKKLKELEKRLEELEERHELYEEAKAKKeelERLKKRLTGLTPEK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 373 TDLYAKQGRGSQFTSKEERDKwIKKELKSLDQAINDKKRQIAAIHK--------DLEDTEANKEKNLEQYKLdqDLNEVK 444
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISK-ITARIGELKKEIKELKKAIEELKKakgkcpvcGRELTEEHRKELLEEYTA--ELKRIE 465
|
490 500
....*....|....*....|....*
gi 38566257 445 ARVEELDRKYYEVKNKKDELQSERN 469
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLK 490
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
3-129 |
7.58e-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: 78.77 E-value: 7.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 3 IKQVIIQGFRSYRDQTIVDPFSSkHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEG--TGPRVISAFVEI 80
Cdd:cd03275 1 LKRLELENFKSYKGRHVIGPFDR-FTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYRArvGKPDSNSAYVTA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 38566257 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 38566257 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 ... |
1109-1188 |
2.80e-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: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 1109 REMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYGV 1188
Cdd:cd03274 123 KNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELADRLVGI 202
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
3-205 |
1.36e-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: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 3 IKQVIIQGFRSYRDQTIVDpFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHlRPEQRLALLHEGTGprviSAFVEIIF 82
Cdd:COG0419 2 LLRLRLENFRSYRDTETID-FDDGLNLIVGPNGAGKSTILEAIRYALYGKARS-RSKLRSDLINVGSE----EASVELEF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 83 DNSDNRlpidkeevslrrvigakkdqyfldkkmvtkndvmnllesagfsrsnpYYIVK-QGKINQMATAPDSQRLKLLRE 161
Cdd:COG0419 76 EHGGKR-----------------------------------------------YRIERrQGEFAEFLEAKPSERKEALKR 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 38566257 162 VAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEE 205
Cdd:COG0419 109 LLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQLSG 152
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1113-1189 |
4.34e-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: 4.34e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38566257 1113 QLSGGQKSLVALALIFAIQkcdpAPFYLFDEIDQALDAQHRKAVSDMIMELAVH-AQFITTTFRPELLE-SADKFYGVK 1189
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 38566257 3 IKQVIIQGFRSYRDQTIVdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSH-LRPEQRLALLHEGTGPR--VISAFVE 79
Cdd:cd03278 1 LKKLELKGFKSFADKTTI-PFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKsLRGEKMSDVIFAGSETRkpANFAEVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 80 IIFDNSDNRlpidkeevslrrvigakkdqyfldkkmvtkndvmnllesagfsrsnpYYIVKQGKINQMATAPD--SQRLK 157
Cdd:cd03278 80 LTFDNSDGR-----------------------------------------------YSIISQGDVSEIIEAPGkkVQRLS 112
|
..
gi 38566257 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 38566257 1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFS-HLRPEQrlalLHEGTGPRVISAFVE 79
Cdd:COG3593 1 MKLEKIKIKNFRSIKDLSI--ELSDDLTVLVGENNSGKSSILEALRLLLGPSSSrKFDEED----FYLGDDPDLPEIEIE 74
|
90
....*....|
gi 38566257 80 IIFDNSDNRL 89
Cdd:COG3593 75 LTFGSLLSRL 84
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
113-480 |
1.84e-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: 71.69 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 113 KKMVTKNDVMNLLESagFSRSNPYYIVKqgkINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINEL 192
Cdd:pfam17380 234 EKMERRKESFNLAED--VTTMTPEYTVR---YNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEK 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 193 LKYIEERLHTLEEEKEELAQYQKwdkmrralEYTIYnqelnetrAKLDELSAKRETSGEKSRQlrdaqQDARDKMEDIER 272
Cdd:pfam17380 309 AREVERRRKLEEAEKARQAEMDR--------QAAIY--------AEQERMAMERERELERIRQ-----EERKRELERIRQ 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 273 QvrELKTKISAMKEeKEQLSAERQEQiKQRTKLELKAKDLQDELagnSEQRKRLLKERQKLLEKIEEKQKELAETEpkFN 352
Cdd:pfam17380 368 E--EIAMEISRMRE-LERLQMERQQK-NERVRQELEAARKVKIL---EEERQRKIQQQKVEMEQIRAEQEEARQRE--VR 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 353 SVKEKEERGIARLAQATQERTD----------------LYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAI 416
Cdd:pfam17380 439 RLEEERAREMERVRLEEQERQQqverlrqqeeerkrkkLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLL 518
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38566257 417 HKDLED-----TEANKEKNLEQYKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQ 480
Cdd:pfam17380 519 EKEMEErqkaiYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKA 587
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
170-509 |
2.27e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.10 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 170 ERKEESISLMKETEGKReKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRETS 249
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEEAK-KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE 1532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 250 GEKSRQLRDAQQ----DARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQ--RTKLELKAKDLQDELAGNSEQR 323
Cdd:PTZ00121 1533 AKKADEAKKAEEkkkaDELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeEARIEEVMKLYEEEKKMKAEEA 1612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 324 KRLLKERQKLLE-KIEEKQKELAETEPKfnsvKEKEERGIARLAQATQERTDLyakqgRGSQFTSKEERDKWIKKELKSL 402
Cdd:PTZ00121 1613 KKAEEAKIKAEElKKAEEEKKKVEQLKK----KEAEEKKKAEELKKAEEENKI-----KAAEEAKKAEEDKKKAEEAKKA 1683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 403 DQainDKKRQIAAIHKDLED---------TEANKEKNLEQYKLDQDLNEVKarVEELDRKYYEVKNKKDELqsernylwR 473
Cdd:PTZ00121 1684 EE---DEKKAAEALKKEAEEakkaeelkkKEAEEKKKAEELKKAEEENKIK--AEEAKKEAEEDKKKAEEA--------K 1750
|
330 340 350
....*....|....*....|....*....|....*.
gi 38566257 474 EENAEQQALAAKREDLEKKQQLLRAATGKAILNGID 509
Cdd:PTZ00121 1751 KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-494 |
2.19e-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: 68.46 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 1 MYIKQVIIQGFRSYRDQTIVDPFSSKHN-VIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPRVISAFVE 79
Cdd:TIGR00618 1 MKPLRLTLKNFGSYKGTHTIDFTALGPIfLICGKTGAGKTTLLDAITYALYGKLPRRSEVIRSLNSLYAAPSEAAFAELE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 80 IIFDNSDNRLPI---------DKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATA 150
Cdd:TIGR00618 81 FSLGTKIYRVHRtlrctrshrKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 151 PDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINE----LLKYIEERLHTLEEEKEELAQYQKwdkmrralEYT 226
Cdd:TIGR00618 161 KSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLrsqlLTLCTPCMPDTYHERKQVLEKELK--------HLR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 227 IYNQELNETRAKLDELSAKRETSGEKSRQLRDAQqdardkmedieRQVRELKTKISAMKEEKEQLSAERQ-----EQIKQ 301
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLR-----------ARIEELRAQEAVLEETQERINRARKaaplaAHIKA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 302 RTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEK---IEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAK 378
Cdd:TIGR00618 302 VTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQqssIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 379 QGRGSQFTSKEERDKWIKKELKSLD----------QAINDKKRQIAAIHKDLEDTEanKEKNLEQYKLDQDLNEVKARVE 448
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQSLCKELDILQreqatidtrtSAFRDLQGQLAHAKKQQELQQ--RYAELCAAAITCTAQCEKLEKI 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 38566257 449 ELDRKYYEVKNKKDELQSERNYLWREEnaEQQALAAKREDLEKKQQ 494
Cdd:TIGR00618 460 HLQESAQSLKEREQQLQTKEQIHLQET--RKKAVVLARLLELQEEP 503
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
169-493 |
3.26e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 68.24 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 169 DERKEESISLMKETEGKReKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELN---ETRAKLDELSAK 245
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKK-KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKkkaEEAKKADEAKKK 1452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 246 RETSgEKSRQLRDAQQDARdKMEDIERQVRELKTKISAMKEEKEqlSAERQEQIKQRTKLELKAKDLQ--DELAGNSEQR 323
Cdd:PTZ00121 1453 AEEA-KKAEEAKKKAEEAK-KADEAKKKAEEAKKADEAKKKAEE--AKKKADEAKKAAEAKKKADEAKkaEEAKKADEAK 1528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 324 KRLLKERQKLLEKIEEKQKelAETEPKFNSVKEKEERGIARLAQATQERTDLY---------AKQGRGSQFTSKEERDKW 394
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKK--ADELKKAEELKKAEEKKKAEEAKKAEEDKNMAlrkaeeakkAEEARIEEVMKLYEEEKK 1606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 395 IKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYKLDQDL----NEVKARVEELDRKYYEVKNKKDELQSErny 470
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELkkaeEENKIKAAEEAKKAEEDKKKAEEAKKA--- 1683
|
330 340
....*....|....*....|...
gi 38566257 471 lwrEENAEQQALAAKREDLEKKQ 493
Cdd:PTZ00121 1684 ---EEDEKKAAEALKKEAEEAKK 1703
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
168-502 |
4.52e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.40 E-value: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 168 YDERKEESISLMKETEGKREKINELLKYIEErlhtLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRE 247
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERLEELKKKLKE----LEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 248 TSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEK-------EQLSAERQEQIKQRTKLELkaKDLQDELAgNS 320
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgRELTEEHRKELLEEYTAEL--KRIEKELK-EI 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 321 EQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEER----GIARLAQATQERTDLYAK----QGRGSQFTSKEERD 392
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKlkkyNLEELEKKAEEYEKLKEKliklKGEIKSLKKELEKL 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 393 KWIKKELKSLDQAINDKKRQIAAIHKDLEDteankeknlEQYKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLW 472
Cdd:PRK03918 552 EELKKKLAELEKKLDELEEELAELLKELEE---------LGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK 622
|
330 340 350
....*....|....*....|....*....|
gi 38566257 473 REENaeqqALAAKREDLEKKQQLLRAATGK 502
Cdd:PRK03918 623 KLEE----ELDKAFEELAETEKRLEELRKE 648
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
3-181 |
1.69e-10 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 64.18 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 3 IKQVIIQGFRSYRDQTI-VDPFsskhNVIVGRNGSGKSNFFYAIQF---------------------VLSDEFSHLRPEQ 60
Cdd:COG4637 2 ITRIRIKNFKSLRDLELpLGPL----TVLIGANGSGKSNLLDALRFlsdaargglqdalarrggleeLLWRGPRTITEPI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 61 RLALLHEGTGPRVISAFVEIIFDNSDNRLPIDKEEVSLRRviGAKKDQYFLDKKMVTknDVMNLLESAGFSRSnpyyivk 140
Cdd:COG4637 78 RLELEFAEEDERDLRYELELGLPEPGGRPEVKEERLWLKR--GSGGRPFLDFRPKGR--AVGGEPERLDSPES------- 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 38566257 141 qgKINQMATAPDSQRLKLLRE-VAGTRVYDERkeesISLMKE 181
Cdd:COG4637 147 --LLSQLGDPERFPELRALREaLRSWRFYDFH----PAPLRQ 182
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
258-487 |
1.86e-10 |
|
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: 64.40 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 258 DAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKI 337
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 338 EEKQKELAetepkfnsvkekeERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIH 417
Cdd:COG4942 100 EAQKEELA-------------ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38566257 418 KDLEDTEANKEKNL-----EQYKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKRE 487
Cdd:COG4942 167 AELEAERAELEALLaeleeERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1-151 |
2.54e-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: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 1 MYIKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTG-PRVISAFVE 79
Cdd:cd03274 1 LIITKLVLENFKSYAGEQVIGPFHKSFSAIVGPNGSGKSNVIDSMLFVFGFRASKMRQKKLSDLIHNSAGhPNLDSCSVE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38566257 80 IIFdnsdnrlpidkeevslrrvigakkdQYFLDKKmvtkndvmnLLESAGFSRSNPYYIVKQGKINQMATAP 151
Cdd:cd03274 81 VHF-------------------------QEIIDKP---------LLKSKGIDLDHNRFLILQGEVEQIAQMP 118
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
232-498 |
2.96e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 232 LNETRAKLDELSAKRETSGEKSRQLRDAQQDA----------RDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQ 301
Cdd:PRK02224 208 LNGLESELAELDEEIERYEEQREQARETRDEAdevleeheerREELETLEAEIEDLRETIAETEREREELAEEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 302 RTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERgiarlaqATQERTDLyakqgr 381
Cdd:PRK02224 288 LEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAES-------LREDADDL------ 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 382 gsqftskEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDteankeknleqykLDQDLNEVKARVEELDRKYYEVKNKK 461
Cdd:PRK02224 355 -------EERAEELREEAAELESELEEAREAVEDRREEIEE-------------LEEEIEELRERFGDAPVDLGNAEDFL 414
|
250 260 270
....*....|....*....|....*....|....*...
gi 38566257 462 DELQSERNYLwREENAEQQA-LAAKREDLEKKQQLLRA 498
Cdd:PRK02224 415 EELREERDEL-REREAELEAtLRTARERVEEAEALLEA 451
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
169-494 |
3.80e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.78 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 169 DERKEESISLMKETEGKReKINELLKYIEERlHTLEEEKEELAQYQKWDKMRRALEYTIYNQELN---ETRAKLDELSAK 245
Cdd:PTZ00121 1414 AAAKKKADEAKKKAEEKK-KADEAKKKAEEA-KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKkkaEEAKKADEAKKK 1491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 246 RETSGEKSRQLRDAQQdARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQD-------ELAG 318
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAE-AKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKaeekkkaEEAK 1570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 319 NSEQRKRLLKERQKLLEKIEEKQKE----LAETEPKFNS---VKEKEERGIA-RLAQATQERTDLY------AKQGRGSQ 384
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEevmkLYEEEKKMKAeeaKKAEEAKIKAeELKKAEEEKKKVEqlkkkeAEEKKKAE 1650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 385 FTSKEERDKWIKKElKSLDQAINDKKRQiaaihKDLEDTEANKEKNLEQYKLDQdlnEVKARVEELDRKYYEVKNKKDEL 464
Cdd:PTZ00121 1651 ELKKAEEENKIKAA-EEAKKAEEDKKKA-----EEAKKAEEDEKKAAEALKKEA---EEAKKAEELKKKEAEEKKKAEEL 1721
|
330 340 350
....*....|....*....|....*....|
gi 38566257 465 QSErnylwrEENAEQQALAAKREDLEKKQQ 494
Cdd:PTZ00121 1722 KKA------EEENKIKAEEAKKEAEEDKKK 1745
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-499 |
4.46e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFshlrpEQRLALLHEGTGPRVISAFVEI 80
Cdd:COG4717 1 MKIKELEIYGFGKFRDRTI--EFSPGLNVIYGPNEAGKSTLLAFIRAMLLERL-----EKEADELFKPQGRKPELNLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 81 ifdnsdnrlpidKEEVSLRRVIGAKKDQYfldkkmvtkndvmnllesagfsrsnpyyivkQGKINQMATApDSQRLKLLR 160
Cdd:COG4717 74 ------------KELEEELKEAEEKEEEY-------------------------------AELQEELEEL-EEELEELEA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 161 EVAGTRVYDERKEESISLmKETEGKREKINELLKYIEERLHTLEEEKEELAQYQ-KWDKMRRALE------YTIYNQELN 233
Cdd:COG4717 110 ELEELREELEKLEKLLQL-LPLYQELEALEAELAELPERLEELEERLEELRELEeELEELEAELAelqeelEELLEQLSL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 234 ETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAmKEEKEQLSAERQ----------------- 296
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA-AALEERLKEARLllliaaallallglggs 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 297 ------------------------EQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKL-------LEKIEEKQKELA 345
Cdd:COG4717 268 llsliltiagvlflvlgllallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppdlsPEELLELLDRIE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 346 ETEPKFNSVKEKEERgiARLAQATQERTDLYAKQGrgsqFTSKEERDKWIK--KELKSLDQAINDKKRQIAAIHKDL-ED 422
Cdd:COG4717 348 ELQELLREAEELEEE--LQLEELEQEIAALLAEAG----VEDEEELRAALEqaEEYQELKEELEELEEQLEELLGELeEL 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38566257 423 TEANKEKNLEQ--YKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYlwREENAEQQALAAKREDLEKKQQLLRAA 499
Cdd:COG4717 422 LEALDEEELEEelEELEEELEELEEELEELREELAELEAELEQLEEDGEL--AELLQELEELKAELRELAEEWAALKLA 498
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
262-902 |
6.01e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.78 E-value: 6.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 262 DARDKMEDIERQVRELkTKISAMKEEKEQLSAERQEQIKQRTKLELKAkdlqdelagnSEQRKRLLKERqkllekIEEKQ 341
Cdd:COG4913 239 RAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWF----------AQRRLELLEAE------LEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 342 KELAETEpkfnsvkEKEERGIARLAQATQERTDLYAKQgRGSQFTSKEErdkwIKKELKSLDQAINDKKR-------QIA 414
Cdd:COG4913 302 AELARLE-------AELERLEARLDALREELDELEAQI-RGNGGDRLEQ----LEREIERLERELEERERrrarleaLLA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 415 AIHKDLEDTEANKEKNLEQykLDQDLNEVKARVEELDRKYYEVKNKKDELQSERnylwREENAEQQALAAKREDLEKKQQ 494
Cdd:COG4913 370 ALGLPLPASAEEFAALRAE--AAALLEALEEELEALEEALAEAEAALRDLRREL----RELEAEIASLERRKSNIPARLL 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 495 LLRAATGKAIlnGIDSIN--------KVLEHFRRkginqhvqngyhgivmnnfeCEPAfytcVEVTAGNRLFYHIVDS-- 564
Cdd:COG4913 444 ALRDALAEAL--GLDEAElpfvgeliEVRPEEER--------------------WRGA----IERVLGGFALTLLVPPeh 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 565 -DEVSTKIlmefNKMNLPGEVTFLPLNKLDVRDTAYPETNDAIPmiSKLRYNPrfdkafkHVFGktlicrsMEVSTQLAR 643
Cdd:COG4913 498 yAAALRWV----NRLHLRGRLVYERVRTGLPDPERPRLDPDSLA--GKLDFKP-------HPFR-------AWLEAELGR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 644 AFTMDC-------------ITLEGdQVSHRGALtgGYYDTRK---SRLELQKDVRKAEeelgeleaklnENLRRNIERIN 707
Cdd:COG4913 558 RFDYVCvdspeelrrhpraITRAG-QVKGNGTR--HEKDDRRrirSRYVLGFDNRAKL-----------AALEAELAELE 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 708 NEIDQLMNQMQQIETQQRKFKASRDSIlsemkmlkekRQQSEKTFMpkQRSLQSLEASLHAMESTRESLKAelgtdllsq 787
Cdd:COG4913 624 EELAEAEERLEALEAELDALQERREAL----------QRLAEYSWD--EIDVASAEREIAELEAELERLDA--------- 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 788 lsleDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVEtylnenlrKRLDQVEQELNELRETEGGTVLTATTSELEA 867
Cdd:COG4913 683 ----SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE--------KELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 38566257 868 INKRVKDTMAR------SEDLDNSIDKTEAGIKELQKSMER 902
Cdd:COG4913 751 LEERFAAALGDaverelRENLEERIDALRARLNRAEEELER 791
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-191 |
6.43e-10 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 59.82 E-value: 6.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 6 VIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLH---EGTGPRVISAFVEIIF 82
Cdd:pfam13476 1 LTIENFRSFRDQTI--DFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKgdiRIGLEGKGKAYVEITF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 83 DNSDNR-LPIDKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYI-VKQGKINQMATAPDSQRLKLLR 160
Cdd:pfam13476 79 ENNDGRyTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVfLGQEREEEFERKEKKERLEELE 158
|
170 180 190
....*....|....*....|....*....|.
gi 38566257 161 EVAGTRVYDERKEESISLMKETEGKREKINE 191
Cdd:pfam13476 159 KALEEKEDEKKLLEKLLQLKEKKKELEELKE 189
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
180-387 |
1.06e-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: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 180 KETEGKREKINELLKYIEERLHTLEEEKEELA-QYQKWDKMRRALEYTI--YNQELNETRAKLDELSAKRETSGEK---- 252
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLkQLAALERRIAALARRIraLEQELAALEAELAELEKEIAELRAEleaq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 253 ----SRQLRDAQQDAR----------DKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAG 318
Cdd:COG4942 103 keelAELLRALYRLGRqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38566257 319 NSEQRKRL---LKERQKLLEKIE----EKQKELAEtepkfnsvKEKEERGIARLAQATQERTDLYAKQGRGSQFTS 387
Cdd:COG4942 183 LEEERAALealKAERQKLLARLEkelaELAAELAE--------LQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
170-489 |
2.61e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.59 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 170 ERKEESISLMKETEGKREKINELLKYIEERLHTLEE---EKEELAQyQKWDKMRRALEYtiyNQELNETRAK-------- 238
Cdd:PRK02224 234 ETRDEADEVLEEHEERREELETLEAEIEDLRETIAEterEREELAE-EVRDLRERLEEL---EEERDDLLAEaglddada 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 239 ------LDELSAKRETSGEKSRQLRDAQQDA-------RDKMEDIE---------------------RQVRELKTKISAM 284
Cdd:PRK02224 310 eavearREELEDRDEELRDRLEECRVAAQAHneeaeslREDADDLEeraeelreeaaeleseleearEAVEDRREEIEEL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 285 KEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELA-----------ETEPKFNS 353
Cdd:PRK02224 390 EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecgqpvEGSPHVET 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 354 VKEKEERG---IARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKK-------RQIAAIHKDLEDT 423
Cdd:PRK02224 470 IEEDRERVeelEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRetieekrERAEELRERAAEL 549
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38566257 424 EAN-KEKNLEQYKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQ--QALAAKREDL 489
Cdd:PRK02224 550 EAEaEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDeiERLREKREAL 618
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
169-463 |
3.01e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 169 DERKEESISLMKETEGKREKINELLKYiEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELsakrET 248
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKKESELIKL-KELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSL----KK 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 249 SGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELagnseqrKRLLK 328
Cdd:PRK03918 547 ELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKEL-------EREEK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 329 ERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERtdlyakqgrgsqftsKEERDKWIKKELKSLDQAIND 408
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEE---------------LREEYLELSRELAGLRAELEE 684
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 38566257 409 KKRQIAAIHKDLEDTEANKEKNLEQYKLDQDLNEVKARVEELDRKYYEVKNKKDE 463
Cdd:PRK03918 685 LEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKE 739
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
169-498 |
3.17e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.59 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 169 DERKEESISLMKETEGKREKINELlkyiEERLHTLEEEKEEL-AQYQKWDKMRRALEY--TIYNQELNETRAKLDELSAK 245
Cdd:PRK02224 359 EELREEAAELESELEEAREAVEDR----REEIEELEEEIEELrERFGDAPVDLGNAEDflEELREERDELREREAELEAT 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 246 RET---SGEKSRQLRDAQQ------------------DARDKMEDIERQVRELKTKISAMKEEKEQLSaERQEQIKQRTK 304
Cdd:PRK02224 435 LRTareRVEEAEALLEAGKcpecgqpvegsphvetieEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIER 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 305 LELKAKDLQDELAgnsEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERG------IARLAQATQE------- 371
Cdd:PRK02224 514 LEERREDLEELIA---ERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAeeareeVAELNSKLAElkeries 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 372 ----RTDLYAKQGRGSQFTS-KEERDKWIKKELKSLD--QAINDKKRQIAAIHKD--LEDTEANKEkNLEQYkldqdlne 442
Cdd:PRK02224 591 leriRTLLAAIADAEDEIERlREKREALAELNDERRErlAEKRERKRELEAEFDEarIEEAREDKE-RAEEY-------- 661
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 38566257 443 vkarVEELDRKYYEVKNKKDELQSERNYLwREENAEQQALAAKREDLEKKQQLLRA 498
Cdd:PRK02224 662 ----LEQVEEKLDELREERDDLQAEIGAV-ENELEELEELRERREALENRVEALEA 712
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
229-418 |
3.56e-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: 60.16 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 229 NQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELK 308
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 309 AKDLQDELAGN-----------------------------------SEQRKRLLKERQKLLEKIEEKQKELAETEPKFNS 353
Cdd:COG4942 99 LEAQKEELAELlralyrlgrqpplalllspedfldavrrlqylkylAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38566257 354 VKEKEERGIARLAQATQERTDLYAKqgRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHK 418
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLAR--LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
8-523 |
3.99e-09 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 60.91 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 8 IQGFRSYRDQTIVDPFSSKhNVIVGRNGSGK---SNFFYAIQfvLSDEFSHLRPEQRLALLHEGTGPRVI---SAFVEII 81
Cdd:COG4694 8 LKNVGAFKDFGWLAFFKKL-NLIYGENGSGKstlSRILRSLE--LGDTSSEVIAEFEIEAGGSAPNPSVRvfnRDFVEEN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 82 FDNSDNRLPI---DKEEVSLRRVIGAKKDQyfLDKKMVTKNDVMNLLESAgfsrsnpyyivkqgkinqmatapDSQRLKL 158
Cdd:COG4694 85 LRSGEEIKGIftlGEENIELEEEIEELEKE--IEDLKKELDKLEKELKEA-----------------------KKALEKL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 159 LREVAGTRVyderkeESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAK 238
Cdd:COG4694 140 LEDLAKSIK------DDLKKLFASSGRNYRKANLEKKLSALKSSSEDELKEKLKLLKEEEPEPIAPITPLPDLKALLSEA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 239 LDELSAKRETSGEKsrQLRDAQQDardkmEDIERQVRELKTKISAMKEEK----EQ-LSAERQEQIKQRtklelkakdLQ 313
Cdd:COG4694 214 ETLLEKSAVSSAIE--ELAALIQN-----PGNSDWVEQGLAYHKEEEDDTcpfcQQeLAAERIEALEAY---------FD 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 314 DELAGNSEQRKRLLKERQKLLEKIEEkqKELAETEPKFNSVKEKEERGIARLAQATQE-RTDLYAKQGRGSQFTSKEERD 392
Cdd:COG4694 278 DEYEKLLAALKDLLEELESAINALSA--LLLEILRTLLPSAKEDLKAALEALNALLETlLAALEEKIANPSTSIDLDDQE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 393 KW--IKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNlEQYKLDQDLNEVKARVEELDRKYYEVKNKKDELQSerny 470
Cdd:COG4694 356 LLdeLNDLIAALNALIEEHNAKIANLKAEKEEARKKLEAH-ELAELKEDLSRYKAEVEELIEELKTIKALKKALED---- 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 38566257 471 lwreenaeqqaLAAKREDLEKKQqllraatgKAILNGIDSINKVLEHFRRKGI 523
Cdd:COG4694 431 -----------LKTEISELEAEL--------SSVDEAADEINEELKALGFDEF 464
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1100-1170 |
6.22e-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: 6.22e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38566257 1100 SF-TGKQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELA---VHAQFI 1170
Cdd:cd03276 95 SFlTSNKAAVRDVKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAkkqPGRQFI 169
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
261-519 |
1.06e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 261 QDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKL---------ELKAKDLQDELAGNSEQRKRLLK--- 328
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdEIDVASAEREIAELEAELERLDAssd 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 329 ERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEER---DKWIKKELksLDQA 405
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRallEERFAAAL--GDAV 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 406 INDKKRQIAAIHKDLEDTEANKEKNLEQyKLDQDLNEVKARVEELDrkyyevknkkDELQSERNYLWREENAEQQALAAK 485
Cdd:COG4913 764 ERELRENLEERIDALRARLNRAEEELER-AMRAFNREWPAETADLD----------ADLESLPEYLALLDRLEEDGLPEY 832
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 38566257 486 REDLekKQQLLRAATG-------------KAILNGIDSINKVLEHFR 519
Cdd:COG4913 833 EERF--KELLNENSIEfvadllsklrraiREIKERIDPLNDSLKRIP 877
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-336 |
1.18e-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: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPrvisafVEI 80
Cdd:pfam13175 1 MKIKSIIIKNFRCLKDTEI--DLDEDLTVLIGKNNSGKSSILEALDIFLNNKEKFFEDDFLVLYLKDVIKI------DKE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 81 IFDNSDNRLPIDKEEVSLrrvigakkdqYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKInqmATAPDSQRLKLLR 160
Cdd:pfam13175 73 DLNIFENISFSIDIEIDV----------EFLLILFGYLEIKKKYLCLASKGKAKEYEKTLHPKG---ANKADLLLELKIS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 161 EVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQE--LNETRAK 238
Cdd:pfam13175 140 DLKKYLKQFKIYIYNNYYLDEKKNVFDKKSKYELPSLKEEFLNSEKEEIKVDKEDLKKLINELEKSINYHEnvLENLQIK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 239 LDELSAKRETSGEKSRQLRDA-----QQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKlelkaKDLQ 313
Cdd:pfam13175 220 KLLISADRNASDEDSEKINSLlgalkQRIFEEALQEELELTEKLKETQNKLKEIDKTLAEELKNILFKKID-----KLKD 294
|
330 340
....*....|....*....|...
gi 38566257 314 DELAGNSEQRKRLLKERQKLLEK 336
Cdd:pfam13175 295 FGYPPFLNPEIEIKKDDEDLPLN 317
|
|
| 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 38566257 180 KETEGKREKINELLKYIEERLHTLEEEKEELAQyqKWDKMRRALEYTiyNQELNETRAKLDELSAKRETSGEK-SRQLRD 258
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNE--EYNELQAELEAL--QAEIDKLQAEIAEAEAEIEERREElGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 259 AQQ------------------DARDKMEDIER-------QVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQ 313
Cdd:COG3883 95 LYRsggsvsyldvllgsesfsDFLDRLSALSKiadadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38566257 314 DELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTS 387
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-65 |
2.81e-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: 2.81e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38566257 1 MYIKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALL 65
Cdd:COG3950 1 MRIKSLTIENFRGFEDLEIDFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLL 65
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
166-468 |
2.89e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 166 RVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKE----------ELAQYQKWDKMRRaleytiYNQELNET 235
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrELTEEHRKELLEE------YTAELKRI 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 236 RAKLDELSAKRETSGEKSRQLRDAQQDARD--KMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRT-KLELKAKDL 312
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiKLKGEIKSL 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 313 QDELagnsEQRKRLLKERQKLLEKIEEKQKELAETEPK-----FNSVKEKEERgIARLAQATQERTDLyakQGRGSQFTS 387
Cdd:PRK03918 545 KKEL----EKLEELKKKLAELEKKLDELEEELAELLKEleelgFESVEELEER-LKELEPFYNEYLEL---KDAEKELER 616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 388 KEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEAN------KEKNLEQYKLDQDLNEVKARVEELDRKYYEVKNKK 461
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeyEELREEYLELSRELAGLRAELEELEKRREEIKKTL 696
|
....*..
gi 38566257 462 DELQSER 468
Cdd:PRK03918 697 EKLKEEL 703
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
150-443 |
3.90e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 150 APDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEytiyn 229
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE----- 1657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 230 qelnETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQ------VRELKTKISAMKEEKEQLSAERQE---QIK 300
Cdd:PTZ00121 1658 ----ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEaeeakkAEELKKKEAEEKKKAEELKKAEEEnkiKAE 1733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 301 QRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKfnSVKEKEERGIARLAQATQERTDLYA--- 377
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE--ELDEEDEKRRMEVDKKIKDIFDNFAnii 1811
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38566257 378 ---KQGRGSQFTSKEERDKWIKKELKSLDQAIND----KKRQIAAIHKDLEDTEANKEKNLEQYKLDQDLNEV 443
Cdd:PTZ00121 1812 eggKEGNLVINDSKEMEDSAIKEVADSKNMQLEEadafEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEI 1884
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
186-496 |
3.94e-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: 57.82 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 186 REKINELLKYIEERLHTLEEeKEELAQYQKwDKMRRALEyTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARD 265
Cdd:pfam15921 266 QDRIEQLISEHEVEITGLTE-KASSARSQA-NSIQSQLE-IIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYED 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 266 KMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKER-------QKLLEKIE 338
Cdd:pfam15921 343 KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDtgnsitiDHLRRELD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 339 EKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAK-QGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAaih 417
Cdd:pfam15921 423 DRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKvSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVS--- 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 418 kDLEDTEANKEKNLEqyKLDQDLNEVKARVEELDRKYYEVKNKKDEL---QSERNYLWREENAEQQALAAKREDLEKKQQ 494
Cdd:pfam15921 500 -DLTASLQEKERAIE--ATNAEITKLRSRVDLKLQELQHLKNEGDHLrnvQTECEALKLQMAEKDKVIEILRQQIENMTQ 576
|
..
gi 38566257 495 LL 496
Cdd:pfam15921 577 LV 578
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
143-504 |
4.28e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 143 KINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRA 222
Cdd:PTZ00121 1213 KAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 223 LEYTIYNQELN--------ETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAE 294
Cdd:PTZ00121 1293 DEAKKAEEKKKadeakkkaEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK 1372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 295 RQEQIKQRTKLELKAKDLQ--DELAGNSEQRKRLLKERQKLLE---KIEEKQKELAETEPKFNSVKEKEERGIARLAQAT 369
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKkaDEAKKKAEEDKKKADELKKAAAakkKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKK 1452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 370 QERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQ----AINDKKRQIAAIHKDLEDTEANKEKNLEQYKLDQDLNEVKA 445
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEakkkAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE 1532
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 38566257 446 RVEELDRKYYEVKNKKDELQSERNYLWREEnaEQQALAAKREDLEKKQQLLRAATGKAI 504
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAEELKKAEE--KKKAEEAKKAEEDKNMALRKAEEAKKA 1589
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
152-490 |
5.08e-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: 57.44 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 152 DSQRLKLLREVagtrvydERKEESISLMKETE--------GKREKINELLKYIEERlhTLEEEK-EELAQYQKWDKMRRA 222
Cdd:pfam15921 376 DDQLQKLLADL-------HKREKELSLEKEQNkrlwdrdtGNSITIDHLRRELDDR--NMEVQRlEALLKAMKSECQGQM 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 223 LEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTkisAMKEEKEQLSAERQEQIKQR 302
Cdd:pfam15921 447 ERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTA---SLQEKERAIEATNAEITKLR 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 303 TKLELKAKDLQdELAGNSEQRKRLLKERQKLLEKIEEKQKElaetepkfnsvkekeergIARLAQATQERTDLYAKQGR- 381
Cdd:pfam15921 524 SRVDLKLQELQ-HLKNEGDHLRNVQTECEALKLQMAEKDKV------------------IEILRQQIENMTQLVGQHGRt 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 382 -GSQFTSKEERDKWIK------KELKSLDQAINDKKRQIAAIHKDLEDTE-----ANKE-----KNLEQYKlDQDLNEVK 444
Cdd:pfam15921 585 aGAMQVEKAQLEKEINdrrlelQEFKILKDKKDAKIRELEARVSDLELEKvklvnAGSErlravKDIKQER-DQLLNEVK 663
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 38566257 445 ARVEELDR--KYYEV-----KNKKDELQSERNYLWREENAEQQALAAKREDLE 490
Cdd:pfam15921 664 TSRNELNSlsEDYEVlkrnfRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLK 716
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
230-371 |
5.47e-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: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 230 QELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKIsamkEEKEQLSAERQEQIKQ-RTKLELK 308
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI----EEVEARIKKYEEQLGNvRNNKEYE 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38566257 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 38566257 1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFvlsdeFSHLR 57
Cdd:PRK00064 1 MYLTRLSLTDFRNYEELDL--ELSPGVNVLVGENGQGKTNLLEAIYL-----LAPGR 50
|
|
| 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 38566257 186 REKInELLKYIEERLHTLEEEKEELAQyqkWDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARD 265
Cdd:COG4913 248 REQI-ELLEPIRELAERYAAARERLAE---LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALRE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 266 KMEDIERQVR--------ELKTKISAMKEEKEQLSAERQEQIKQRTKLELKA------------------KDLQDELAGN 319
Cdd:COG4913 324 ELDELEAQIRgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLpasaeefaalraeaaallEALEEELEAL 403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 38566257 320 SEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTD 374
Cdd:COG4913 404 EEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEA 458
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-471 |
1.74e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 55.68 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 1 MYIKQVIIQGFRSYRDQTIVdpFSSKHNVIVGRNGSGKSNFFYAIQFVLsdeFSHLRPEQRLALLHEGTGPRVISAFVEI 80
Cdd:PRK01156 1 MIIKRIRLKNFLSHDDSEIE--FDTGINIITGKNGAGKSSIVDAIRFAL---FTDKRTEKIEDMIKKGKNNLEVELEFRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 81 IFDNSDNRLPIDKEEVSLRRVIGAKKDQYFLDKKMvtkNDVMNLLESAGFSRSNPYYI----VKQGKINQMATAPDSQRL 156
Cdd:PRK01156 76 GGHVYQIRRSIERRGKGSRREAYIKKDGSIIAEGF---DDTTKYIEKNILGISKDVFLnsifVGQGEMDSLISGDPAQRK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 157 KLLREVAG----TRVYDERKEESISLMKETEGKREKINELLKYIEErlhtLEEEKEELAQYQKW------DKMRRALEYT 226
Cdd:PRK01156 153 KILDEILEinslERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLE----LENIKKQIADDEKShsitlkEIERLSIEYN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 227 IYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDardkMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLE 306
Cdd:PRK01156 229 NAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESD----LSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 307 lkakdlqdelaGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEErgiaRLAQATQERTDLYAKQGR-GSQF 385
Cdd:PRK01156 305 -----------NDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKS----RYDDLNNQILELEGYEMDyNSYL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 386 TSKEERDKWIKKELKsldqainDKKRQIAAIHKDLEDTEANKEK-NLEQYKLDQDLNEVKARVEELDRKYYEVKNKKDEL 464
Cdd:PRK01156 370 KSIESLKKKIEEYSK-------NIERMSAFISEILKIQEIDPDAiKKELNEINVKLQDISSKVSSLNQRIRALRENLDEL 442
|
....*..
gi 38566257 465 QSERNYL 471
Cdd:PRK01156 443 SRNMEML 449
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
3-214 |
2.10e-07 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 54.28 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 3 IKQVIIQGFRSYRDQTIVDPFSSKH-----NVIVGRNGSGKSNFFYAIQFVLS-DEFSHLRPEQRLALLHEGTGPRVISA 76
Cdd:COG1106 2 LISFSIENFRSFKDELTLSMVASGLrllrvNLIYGANASGKSNLLEALYFLRNlVLNSSQPGDKLVEPFLLDSESKNEPS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 77 FVEIIFDNSDNRLPI----DKEEVSLRRVigakkdqYFLdkkmvtkndvmnlleSAGFSRSNPYYIvkqgkinqmatapd 152
Cdd:COG1106 82 EFEILFLLDGVRYEYgfelDKERIISEWL-------YFL---------------STAAQLNVPLLS-------------- 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38566257 153 sqrlKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIE---ERLHTLEEEKEELAQYQ 214
Cdd:COG1106 126 ----PLYDWFDNNISLDTSSDGLTLLLKEDESLKEELLELLKIADpgiEDIEVEEEEIEDLVERK 186
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
186-440 |
3.25e-07 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 54.55 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 186 REKINELLKYIEER--LHtLEEEKEELAQyqkwDKMRRALEYTIynqELNETRAKLDELSAKRETSGE-----KSRQLRD 258
Cdd:PRK05771 15 KSYKDEVLEALHELgvVH-IEDLKEELSN----ERLRKLRSLLT---KLSEALDKLRSYLPKLNPLREekkkvSVKSLEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 259 AQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERqEQIKQRTKLELKAKDLQDElaGNSEQRKRLLKERQKLLEKIE 338
Cdd:PRK05771 87 LIKDVEEELEKIEKEIKELEEEISELENEIKELEQEI-ERLEPWGNFDLDLSLLLGF--KYVSVFVGTVPEDKLEELKLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 339 EKQKELAETEPKFNSV-------KEKEERGIARLAQATQERTDLYAKQgrgsqfTSKEERDKwIKKELKSLDQAINDKKR 411
Cdd:PRK05771 164 SDVENVEYISTDKGYVyvvvvvlKELSDEVEEELKKLGFERLELEEEG------TPSELIRE-IKEELEEIEKERESLLE 236
|
250 260
....*....|....*....|....*....
gi 38566257 412 QIAAIHKDLEDTEANKEKNLEQYKLDQDL 440
Cdd:PRK05771 237 ELKELAKKYLEELLALYEYLEIELERAEA 265
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
183-375 |
3.36e-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: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 183 EGKREKINELLKYIEERLHTLEEEKEE----LAQY-QKWDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLR 257
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEaeaaLEEFrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 258 DAQQDARDKMEDIERQVRelktkISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAgnsEQRKRLLKERQKLLEKI 337
Cdd:COG3206 247 AQLGSGPDALPELLQSPV-----IQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIA---ALRAQLQQEAQRILASL 318
|
170 180 190
....*....|....*....|....*....|....*...
gi 38566257 338 EEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDL 375
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRL 356
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
224-521 |
4.87e-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: 54.46 E-value: 4.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 224 EYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKE-------------- 289
Cdd:pfam12128 577 ELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETfartalknarldlr 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 290 QLSAE-RQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELaeTEPKFNSVKEKEERGIARLAQA 368
Cdd:pfam12128 657 RLFDEkQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREA--RTEKQAYWQVVEGALDAQLALL 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 369 TQERTDLYAKQGRgsqftSKEERDKWIKKELKSLD---QAINDKKRQIAAIHKDLEDTEANKEKNL-------EQYKLDQ 438
Cdd:pfam12128 735 KAAIAARRSGAKA-----ELKALETWYKRDLASLGvdpDVIAKLKREIRTLERKIERIAVRRQEVLryfdwyqETWLQRR 809
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 439 D-----LNEVKARVEELD----RKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQLLRAATGKAILNGID 509
Cdd:pfam12128 810 PrlatqLSNIERAISELQqqlaRLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIG 889
|
330
....*....|..
gi 38566257 510 SINKVLEHFRRK 521
Cdd:pfam12128 890 ERLAQLEDLKLK 901
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
186-432 |
6.21e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 6.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 186 REKINEL---LKYIEERLHTLEEEKEEL-AQYQKWDKMRRAL----EYTIYNQELNETRAKLDELSAKR---ETSGEKSR 254
Cdd:COG4913 609 RAKLAALeaeLAELEEELAEAEERLEALeAELDALQERREALqrlaEYSWDEIDVASAEREIAELEAELerlDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 255 QLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQE---------QIKQRTKLELKAKDLQDELAGNSEQ--R 323
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDElqdrleaaeDLARLELRALLEERFAAALGDAVERelR 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 324 KRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERG-----------IARLAQatQERTDLYAKQGR-GSQFTSKEER 391
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAMRAFNREWPAETADldadleslpeyLALLDR--LEEDGLPEYEERfKELLNENSIE 846
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 38566257 392 DkwiKKELKS-LDQAINDKKRQIAAIHKDLEDTEANKEKNLE 432
Cdd:COG4913 847 F---VADLLSkLRRAIREIKERIDPLNDSLKRIPFGPGRYLR 885
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
287-503 |
6.22e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 6.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 287 EKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEpkfNSVKEKEERgIARLA 366
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREE-LGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 367 QATQER----------------TDLYAKQGRGSQFTskeERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKN 430
Cdd:COG3883 93 RALYRSggsvsyldvllgsesfSDFLDRLSALSKIA---DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38566257 431 LEQykLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQLLRAATGKA 503
Cdd:COG3883 170 KAE--LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
169-428 |
6.29e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 169 DERKEESISLMKETEGKREKINELlkyiEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQE---------LNETRAKL 239
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEV----EERLERAEDLVEAEDRIERLEERREDLEELIAERRetieekrerAEELRERA 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 240 DELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLsAERQEQIKQRTKLELKAKDLQDElagN 319
Cdd:PRK02224 547 AELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLL-AAIADAEDEIERLREKREALAEL---N 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 320 SEQRKRL--LKERQKLLE------KIEEKQKELAETEPKFNSVKEKeergiarLAQATQERTDLYAKQGRgsqftskeer 391
Cdd:PRK02224 623 DERRERLaeKRERKRELEaefdeaRIEEAREDKERAEEYLEQVEEK-------LDELREERDDLQAEIGA---------- 685
|
250 260 270
....*....|....*....|....*....|....*..
gi 38566257 392 dkwIKKELKSLDqAINDKKRQIAAIHKDLEDTEANKE 428
Cdd:PRK02224 686 ---VENELEELE-ELRERREALENRVEALEALYDEAE 718
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
166-411 |
9.26e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 53.30 E-value: 9.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 166 RVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETR-AKLDELSA 244
Cdd:pfam12128 657 RLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALdAQLALLKA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 245 KREtsgeKSRQLRDAQQDA---------------RDKMEDIERQVRELKTKISAMKEEK-----------EQLSAERQEQ 298
Cdd:pfam12128 737 AIA----ARRSGAKAELKAletwykrdlaslgvdPDVIAKLKREIRTLERKIERIAVRRqevlryfdwyqETWLQRRPRL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 299 IKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSvkekEERGIARL---AQATQERTDL 375
Cdd:pfam12128 813 ATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRC----EMSKLATLkedANSEQAQGSI 888
|
250 260 270
....*....|....*....|....*....|....*..
gi 38566257 376 YAKQGRGSQFTSKEERDKW-IKKELKSLDQAINDKKR 411
Cdd:pfam12128 889 GERLAQLEDLKLKRDYLSEsVKKYVEHFKNVIADHSG 925
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
143-493 |
9.88e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 9.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 143 KINQMATAPDSQRLKLLREVAGTRVYDE-RKEESISLMKETEGKRE--------KINELLKYIEERLHTLEEEKEELAQY 213
Cdd:PTZ00121 1141 KAEEARKAEDAKRVEIARKAEDARKAEEaRKAEDAKKAEAARKAEEvrkaeelrKAEDARKAEAARKAEEERKAEEARKA 1220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 214 Q---KWDKMRRALEytiynqelnetrAKLDELSAKRetsGEKSRQLRDAQQDARDKMEDIERqvRELKTKISAMKEEKEQ 290
Cdd:PTZ00121 1221 EdakKAEAVKKAEE------------AKKDAEEAKK---AEEERNNEEIRKFEEARMAHFAR--RQAAIKAEEARKADEL 1283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 291 LSAERQEQIKQRTKLELKAKdlQDELAGNSEQRKRL--LKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQA 368
Cdd:PTZ00121 1284 KKAEEKKKADEAKKAEEKKK--ADEAKKKAEEAKKAdeAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 369 TQERTDlyAKQGRGSQFTSKEERDKWIKKELKSLDQAiNDKKRQIAAIHKDLEDTEANKEKNLEQYKldqdLNEVKARVE 448
Cdd:PTZ00121 1362 AEEKAE--AAEKKKEEAKKKADAAKKKAEEKKKADEA-KKKAEEDKKKADELKKAAAAKKKADEAKK----KAEEKKKAD 1434
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 38566257 449 ELDRKYYEvKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQ 493
Cdd:PTZ00121 1435 EAKKKAEE-AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK 1478
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
179-357 |
1.04e-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: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 179 MKETEGKREKINELLKYIEERLHTLEEEKEEL-AQYQKWDKMRRALEYTIY-------------NQELNETRAKLDELSA 244
Cdd:COG4942 64 IAALARRIRALEQELAALEAELAELEKEIAELrAELEAQKEELAELLRALYrlgrqpplalllsPEDFLDAVRRLQYLKY 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 245 KRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRK 324
Cdd:COG4942 144 LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
170 180 190
....*....|....*....|....*....|...
gi 38566257 325 RLlkerQKLLEKIEEKQKELAETEPKFNSVKEK 357
Cdd:COG4942 224 EL----EALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
181-343 |
1.15e-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: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 181 ETEGKREKINELLKYIEERLHTLEEEKEELAQYQKwdkmRRALEYTIYNQELNETRAKLDELSAKRetsgekSRQLRDAQ 260
Cdd:pfam15709 349 EVERKRREQEEQRRLQQEQLERAEKMREELELEQQ----RRFEEIRLRKQRLEEERQRQEEEERKQ------RLQLQAAQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 261 QDARDKMEDIERQVRELKTKisamkeeKEQLSAERQEQIKQRTK-LELKAKDLQDELAGNSE------QRKRLLKERQKL 333
Cdd:pfam15709 419 ERARQQQEEFRRKLQELQRK-------KQQEEAERAEAEKQRQKeLEMQLAEEQKRLMEMAEeerleyQRQKQEAEEKAR 491
|
170
....*....|
gi 38566257 334 LEKIEEKQKE 343
Cdd:pfam15709 492 LEAEERRQKE 501
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
170-460 |
1.21e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.84 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 170 ERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQyqkwdkMRRALeytiyNQELNETRAKLDELSAKRETS 249
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAE------KRDEL-----NAQVKELREEAQELREKRDEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 250 GEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDE--LAGNSEQRKRLL 327
Cdd:COG1340 70 NEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEkeLVEKIKELEKEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 328 KERQKLLEKIEEKQKELAETEPKFNSVKEKEERgIARLAQATQERTDLYAKQgrgsqftsKEERDKwIKKELKSLDQAIN 407
Cdd:COG1340 150 EKAKKALEKNEKLKELRAELKELRKEAEEIHKK-IKELAEEAQELHEEMIEL--------YKEADE-LRKEADELHKEIV 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 38566257 408 DKKRQIAAIHKDLEDTEA---NKEKNLEQYKLDQDLNEVKARVEELDRKYYEVKNK 460
Cdd:COG1340 220 EAQEKADELHEEIIELQKelrELRKELKKLRKKQRALKREKEKEELEEKAEEIFEK 275
|
|
| 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 38566257 146 QMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKRE--KINELlkyieerlhtleeEKEELAQYQKWDKMRRAL 223
Cdd:pfam17380 332 QAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEisRMREL-------------ERLQMERQQKNERVRQEL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 224 EYTIYNQELNETRAKldelsaKRETSGEKSRQLRDAQQDARdkmediERQVRELKTKISAMKEEKEQLSAERQEQIKQRT 303
Cdd:pfam17380 399 EAARKVKILEEERQR------KIQQQKVEMEQIRAEQEEAR------QREVRRLEEERAREMERVRLEEQERQQQVERLR 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 304 KLELKAKDLQDELAGNSEQRKRLLKERQKLLEK---------IEEKQKEL---AETEPKFNSVKEKEERGIA----RLAQ 367
Cdd:pfam17380 467 QQEEERKRKKLELEKEKRDRKRAEEQRRKILEKeleerkqamIEEERKRKlleKEMEERQKAIYEEERRREAeeerRKQQ 546
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 38566257 368 ATQERTDLyakQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQ 412
Cdd:pfam17380 547 EMEERRRI---QEQMRKATEERSRLEAMEREREMMRQIVESEKAR 588
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
2-47 |
1.53e-06 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 51.69 E-value: 1.53e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 38566257 2 YIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQF 47
Cdd:COG1195 1 RLKRLSLTNFRNYESLEL--EFSPGINVLVGPNGQGKTNLLEAIYL 44
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
267-359 |
1.64e-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: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 267 MEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRtklELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAE 346
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASFERLAELRDE---LAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPE 489
|
90
....*....|...
gi 38566257 347 TEPKFNSVKEKEE 359
Cdd:COG0542 490 LEKELAELEEELA 502
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
168-467 |
1.82e-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: 52.33 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 168 YDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRAleytiynqELNETRAKLDELSAKRE 247
Cdd:TIGR04523 382 YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII--------KNNSEIKDLTNQDSVKE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 248 TSGEKSRQLRDAQQDardKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLL 327
Cdd:TIGR04523 454 LIIKNLDNTRESLET---QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 328 KERQKLLEKIEEKQKELAE--TEPKFNSVKEKEERGIARLAQATQERTDLYAKQgrgsqfTSKEERDKWIKKELKSLDQA 405
Cdd:TIGR04523 531 SEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQ------EEKQELIDQKEKEKKDLIKE 604
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38566257 406 INDKKRQIAAIHKDLEDTEANKEK-NLEQYKLDQDLNEVKARVEELDRKYYEVKNKKDELQSE 467
Cdd:TIGR04523 605 IEEKEKKISSLEKELEKAKKENEKlSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKK 667
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
172-497 |
1.92e-06 |
|
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: 52.48 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 172 KEESISLMKEtegKREKINELLKYIEERLHTLEEEKEELAQ--------YQKWDKMRRALEYTiyNQELNETrakLDELS 243
Cdd:pfam01576 10 KEEELQKVKE---RQQKAESELKELEKKHQQLCEEKNALQEqlqaetelCAEAEEMRARLAAR--KQELEEI---LHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 244 AKRETSGEKSRQLRDAQQDARDKMEDIERQVRElktkisamkEEkeqlsAERQEQIKQRTKLELKAKDLQDELAGNSEQR 323
Cdd:pfam01576 82 SRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE---------EE-----AARQKLQLEKVTTEAKIKKLEEDILLLEDQN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 324 KRLLKERQKLLEKIEEKQKELAETEPK---FNSVKEKEERGIARLaqatQERTDLYAKqgrgsqftSKEERDKWIKKelk 400
Cdd:pfam01576 148 SKLSKERKLLEERISEFTSNLAEEEEKaksLSKLKNKHEAMISDL----EERLKKEEK--------GRQELEKAKRK--- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 401 sLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYKLDQD-LNEVKARVEELDRKYYEVKNKKDELQSErnyLWREENAEQ 479
Cdd:pfam01576 213 -LEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALArLEEETAQKNNALKKIRELEAQISELQED---LESERAARN 288
|
330
....*....|....*...
gi 38566257 480 QALAAKReDLEKKQQLLR 497
Cdd:pfam01576 289 KAEKQRR-DLGEELEALK 305
|
|
| recN |
TIGR00634 |
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ... |
794-1212 |
2.72e-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: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 794 KRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNEnlrkrLDQVEQELNELRETEGGTVLTattSELEAINKRVK 873
Cdd:TIGR00634 161 KAYRELYQAWLKARQQLKDRQQKEQELAQRLDFLQFQLEE-----LEEADLQPGEDEALEAEQQRL---SNLEKLRELSQ 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 874 DTMAR-SEDLDNSIDKTEAGIKELQKSMErwknmekehmdaiNHDTKELEKMTNRQGMLLKKKEECMKKIRELGS----L 948
Cdd:TIGR00634 233 NALAAlRGDVDVQEGSLLEGLGEAQLALA-------------SVIDGSLRELAEQVGNALTEVEEATRELQNYLDelefD 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 949 PQEAFEKYQTLS-LKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGYksIMELMNVLELRKYEA 1027
Cdd:TIGR00634 300 PERLNEIEERLAqIKRLKRKYGASVEEVLEYAEKIKEELDQLDDSDESLEALEEEVDKLEEEL--DKAAVALSLIRRKAA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 1028 iqltfKQVSKNFSEVFQKLvpggkaTLVMKKGDVEGSQSQDEGEGSGESERGsgsqssvpsVDQftgvgIRVSFTGKQGE 1107
Cdd:TIGR00634 378 -----ERLAKRVEQELKAL------AMEKAEFTVEIKTSLPSGAKARAGAYG---------ADQ-----VEFLFSANTGE 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 1108 mrEMQQL----SGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESAD 1183
Cdd:TIGR00634 433 --PVKPLakvaSGGELSRVMLALKVVLSSSAAVTTLIFDEVDVGVSGETAQAIAKKLAQLSERHQVLCVTHLPQVAAHAD 510
|
410 420
....*....|....*....|....*....
gi 38566257 1184 KFYGVKfrnKVShIDVITAEMAKDFVEDD 1212
Cdd:TIGR00634 511 AHFKVE---KEG-LDGRTATRVRPLSGEE 535
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-58 |
3.16e-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: 3.16e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 38566257 3 IKQVIIQGFRSYRDQTIVDpFSSKHNVIVGRNGSGKSNFFYAIQFVLsdeFSHLRP 58
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIE-FFSPLTLIVGQNGAGKTTIIEALKYAL---TGELPP 52
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
698-1028 |
4.44e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 698 NLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEktfmpkqRSLQSLEASLHAMESTRE--- 774
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELR-------EELEKLEKEVKELEELKEeie 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 775 SLKAELGTDLLSQLSLEDQKRvdALNDEIRQLQQENRQLLNERIKLEGIITRVETYlnENLRKRLDQVEQELNELRETEG 854
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIR--ELEERIEELKKEIEELEEKVKELKELKEKAEEY--IKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 855 G-----TVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRqg 929
Cdd:PRK03918 318 RleeeiNGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEE-- 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 930 mLLKKKEECMKKIREL----GSLPQEAFEKYQTLS-LKQLFRKLEQCNTEL---------KKYSHVNKKALDQFVNFSEQ 995
Cdd:PRK03918 396 -LEKAKEEIEEEISKItariGELKKEIKELKKAIEeLKKAKGKCPVCGRELteehrkellEEYTAELKRIEKELKEIEEK 474
|
330 340 350
....*....|....*....|....*....|...
gi 38566257 996 KEKLIKRQEELDrgyksiMELMNVLELRKYEAI 1028
Cdd:PRK03918 475 ERKLRKELRELE------KVLKKESELIKLKEL 501
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
143-469 |
4.74e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 143 KINQMATAPDSQRLKLLREVAGTRVYDE-RKEESISLMKETEGKREKINEllkyiEERLHTLEEEKEELAQYQKwdkmRR 221
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADElKKAEELKKAEEKKKAEEAKKA-----EEDKNMALRKAEEAKKAEE----AR 1593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 222 ALEYTIYNQELNETRAkldELSAKRETSGEKSRQLRDAQQDaRDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQ 301
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKA---EEAKKAEEAKIKAEELKKAEEE-KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 302 RTKLELKAKDLQDELAGNSEQRKRLLKERQKLlEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQErtdlyakqgr 381
Cdd:PTZ00121 1670 AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE---------- 1738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 382 gsqftskEERDKWIKKELKSLDQaindKKRQIAAIHKDLEDTEANKEKNLEQYKLDQDLNEVKARVEELDRKYYEVKNKK 461
Cdd:PTZ00121 1739 -------AEEDKKKAEEAKKDEE----EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNF 1807
|
....*...
gi 38566257 462 DELQSERN 469
Cdd:PTZ00121 1808 ANIIEGGK 1815
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
168-488 |
4.81e-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: 51.11 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 168 YDERKEESISLMKETEGKREKINELLKYIEERLHTLEEE----KEELAQYQKWDKM--RRALEYTIYNQELNETRA--KL 239
Cdd:COG3096 352 YQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEvdslKSQLADYQQALDVqqTRAIQYQQAVQALEKARAlcGL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 240 DELSAKretsgeksrQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSA------------ERQEQIKQRTKLEL 307
Cdd:COG3096 432 PDLTPE---------NAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKayelvckiagevERSQAWQTARELLR 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 308 KAKDLQdELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSqfts 387
Cdd:COG3096 503 RYRSQQ-ALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAV---- 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 388 keERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYkldQDLNEVKARVEELDRKYYEVKNKKDELQSE 467
Cdd:COG3096 578 --EQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEAL---ADSQEVTAAMQQLLEREREATVERDELAAR 652
|
330 340
....*....|....*....|.
gi 38566257 468 RNYLwrEENAEQQALAAKRED 488
Cdd:COG3096 653 KQAL--ESQIERLSQPGGAED 671
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
668-986 |
5.91e-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: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 668 YDTRKSRLELQKDVRKAEEELGELEAKLNENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQ 747
Cdd:TIGR00606 205 HQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKD 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 748 SEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLsqlslEDQKRVDALNDEIRQLQQENRQLLNERIKL------- 820
Cdd:TIGR00606 285 NSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELV-----DCQRELEKLNKERRLLNQEKTELLVEQGRLqlqadrh 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 821 -EGIITRVETYLNENLRKRLDQVEQELNELRETEGGTVLTATTSELEA--INKRVKDTMARSEDLDNSIDKTEAGIKELQ 897
Cdd:TIGR00606 360 qEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAktAAQLCADLQSKERLKQEQADEIRDEKKGLG 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 898 KSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEA----------FEKYQTLSLKQLFRK 967
Cdd:TIGR00606 440 RTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSltetlkkevkSLQNEKADLDRKLRK 519
|
330
....*....|....*....
gi 38566257 968 LEQCNTELKKYSHVNKKAL 986
Cdd:TIGR00606 520 LDQEMEQLNHHTTTRTQME 538
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
231-434 |
6.17e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 6.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 231 ELNETRAKLDELSAKRETSGEksrQLRDAQQDARDKMEDIER---QVRELKTKISAMKEE---KEQLSAERQEQIKQR-- 302
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQA---ELDALQAELEELNEEYNElqaELEALQAEIDKLQAEiaeAEAEIEERREELGERar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 303 ---------TKLE--LKAKDLQDeLAGNSEQRKRLLKERQKLLEKIEEKQKELAETEpkfNSVKEKEERGIARLAQATQE 371
Cdd:COG3883 94 alyrsggsvSYLDvlLGSESFSD-FLDRLSALSKIADADADLLEELKADKAELEAKK---AELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38566257 372 RTDLYAKQgrgsqfTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQY 434
Cdd:COG3883 170 KAELEAQQ------AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
181-350 |
7.07e-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: 7.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 181 ETEGKREKINELLKYIEERLHTLEEEKEELAQyqkwdkmrralEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQ 260
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEA-----------RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 261 QDARD--KMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIE 338
Cdd:COG1579 83 GNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|..
gi 38566257 339 EKQKELAETEPK 350
Cdd:COG1579 163 AEREELAAKIPP 174
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
289-509 |
7.09e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 7.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 289 EQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERgIARLAQA 368
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK-LEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 369 TQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLE----DTEANKEKNLEQykLDQDLNEVK 444
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEelleQLSLATEEELQD--LAEELEELQ 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38566257 445 ARVEELDRKYYEVKNKKDELQSErnylwREENAEQQALAAKREDLEKKQQLLRAATGKAILNGID 509
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEE-----LEQLENELEAAALEERLKEARLLLLIAAALLALLGLG 265
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
183-491 |
7.74e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.89 E-value: 7.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 183 EGKREKINELLKYIEERLHTLEEEKEELAQY-QKWDKMRRALEYTI--YNQELNETRAKLDELSAKR---ETSGEKSRQL 256
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKEKERYKRDrEQWERQRRELESRVaeLKEELRQSREKHEELEEKYkelSASSEELSEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 257 RDAQQDARdkmEDIERQVRELKTKISAMKEEKEQLSAErQEQIKQRTKLELKakdlqdelagnseQRKRLLKERQKLLEK 336
Cdd:pfam07888 117 KDALLAQR---AAHEARIRELEEDIKTLTQRVLERETE-LERMKERAKKAGA-------------QRKEEEAERKQLQAK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 337 IEEKQKELAETEPKFNSVKEKEERgiaRLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAI 416
Cdd:pfam07888 180 LQQTEEELRSLSKEFQELRNSLAQ---RDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGL 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38566257 417 HKDLEDTEANKEKNLeqykldQDLNEVKARVEELDRKYYEVKNKkdeLQSERNYLWREENAEQQALAAKREDLEK 491
Cdd:pfam07888 257 GEELSSMAAQRDRTQ------AELHQARLQAAQLTLQLADASLA---LREGRARWAQERETLQQSAEADKDRIEK 322
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
171-498 |
9.00e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.29 E-value: 9.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 171 RKEESISLMKETEGKREKINELLKYIEERLHTLEEEK---EELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRE 247
Cdd:PRK01156 347 RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSkniERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVS 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 248 TSGEKSRQLRDAQQDARDKM------------------EDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKA 309
Cdd:PRK01156 427 SLNQRIRALRENLDELSRNMemlngqsvcpvcgttlgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRK 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 310 KDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEK---------EERGIARL-AQATQERTDLYAKQ 379
Cdd:PRK01156 507 EYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRykslkledlDSKRTSWLnALAVISLIDIETNR 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 380 GRGSQFTSK----EER---------------DKWIKK---ELKSLDQAIN---DKKRQIAAIHKDLEDTeanKEKNLEQY 434
Cdd:PRK01156 587 SRSNEIKKQlndlESRlqeieigfpddksyiDKSIREienEANNLNNKYNeiqENKILIEKLRGKIDNY---KKQIAEID 663
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38566257 435 KLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYL------WREENAE-QQALAAKREDLEKKQQLLRA 498
Cdd:PRK01156 664 SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLestieiLRTRINElSDRINDINETLESMKKIKKA 734
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
200-494 |
1.23e-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: 49.66 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 200 LHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKretsGEKSRQLRDAQQDARDKMEDIERQVRELKT 279
Cdd:TIGR00606 799 MELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSK----IELNRKLIQDQQEQIQHLKSKTNELKSEKL 874
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 280 KISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKelaETEPKFNSVKEKEE 359
Cdd:TIGR00606 875 QIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNK---KAQDKVNDIKEKVK 951
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 360 RGIAR---LAQATQERTDLYAKQ------GRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKN 430
Cdd:TIGR00606 952 NIHGYmkdIENKIQDGKDDYLKQketelnTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELK 1031
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38566257 431 LEQYKLDQDLNEV-KARVEELDRKYYEVKNKKDELQSERNYLW-REENAEQQALAAKREDLEKKQQ 494
Cdd:TIGR00606 1032 EVEEELKQHLKEMgQMQVLQMKQEHQKLEENIDLIKRNHVLALgRQKGYEKEIKHFKKELREPQFR 1097
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1103-1184 |
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 38566257 1103 GKQGEMremqqLSGGQKSLVALALIFaiqkCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESA 1182
Cdd:TIGR02857 453 GEGGAG-----LSGGQAQRLALARAF----LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALA 523
|
..
gi 38566257 1183 DK 1184
Cdd:TIGR02857 524 DR 525
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
178-491 |
1.47e-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: 49.25 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 178 LMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKwDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLR 257
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK-ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 258 DAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKI 337
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 338 EEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGR-GSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAI 416
Cdd:TIGR04523 471 KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDlTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD 550
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38566257 417 HKDLEDTEANKEKNleqyKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEK 491
Cdd:TIGR04523 551 DFELKKENLEKEID----EKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
170-502 |
1.53e-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: 49.40 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 170 ERKEESISLMKETEGKREKINELlkyiEERLHTLEEEKEELAQYQ--------KWDKMRRALEytiynQELNETRAKLDE 241
Cdd:pfam01576 633 EKETRALSLARALEEALEAKEEL----ERTNKQLRAEMEDLVSSKddvgknvhELERSKRALE-----QQVEEMKTQLEE 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 242 LSAKRETSGEKSRQLRDAQQDARDKMEdierqvRELKTKISAMKEEKEQLS-------AERQEQIKQRT-------KLEL 307
Cdd:pfam01576 704 LEDELQATEDAKLRLEVNMQALKAQFE------RDLQARDEQGEEKRRQLVkqvreleAELEDERKQRAqavaakkKLEL 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 308 KAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAET----EPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGS 383
Cdd:pfam01576 778 DLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEArasrDEILAQSKESEKKLKNLEAELLQLQEDLAASERARR 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 384 QftSKEERDKwIKKELK---SLDQAINDKKRQIAAIHKDLEDteankeknleqyKLDQDLNEVKARVEELDRKYYEVKNK 460
Cdd:pfam01576 858 Q--AQQERDE-LADEIAsgaSGKSALQDEKRRLEARIAQLEE------------ELEEEQSNTELLNDRLRKSTLQVEQL 922
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 38566257 461 KDELQSERNYLWREENAEQQALAAKREDLEKKQQLLRAATGK 502
Cdd:pfam01576 923 TTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSK 964
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
1099-1164 |
1.62e-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: 1.62e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38566257 1099 VSFtgKQGEmrEMQQL-----SGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELA 1164
Cdd:cd03277 111 VKF--REGE--QLQELdphhqSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVETA 177
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1104-1189 |
2.33e-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: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 1104 KQGE-----MREMQQLSGGQKSLVALALIFAIQK--CDPAPFYLFDEIDQALDAQHRKAVSDMIMELA---VHAQFITTT 1173
Cdd:cd03240 101 HQGEsnwplLDMRGRCSGGEKVLASLIIRLALAEtfGSNCGILALDEPTTNLDEENIEESLAEIIEERksqKNFQLIVIT 180
|
90
....*....|....*.
gi 38566257 1174 FRPELLESADKFYGVK 1189
Cdd:cd03240 181 HDEELVDAADHIYRVE 196
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
251-503 |
3.11e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 251 EKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKakdlQDELAGNSEQRKRLLKER 330
Cdd:PTZ00121 1137 EDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELR----KAEDARKAEAARKAEEER 1212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 331 qklleKIEEKQKelAETEPKFNSVKEKEE--RGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKElksldqaind 408
Cdd:PTZ00121 1213 -----KAEEARK--AEDAKKAEAVKKAEEakKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE---------- 1275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 409 KKRQIAAIHKDLEDTEANKEKNLEQYKLDQDLN---EVKARVEELDRKYYEVKNKKDELQSernylwREENAEQQALAAK 485
Cdd:PTZ00121 1276 EARKADELKKAEEKKKADEAKKAEEKKKADEAKkkaEEAKKADEAKKKAEEAKKKADAAKK------KAEEAKKAAEAAK 1349
|
250
....*....|....*...
gi 38566257 486 REDlEKKQQLLRAATGKA 503
Cdd:PTZ00121 1350 AEA-EAAADEAEAAEEKA 1366
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
180-370 |
3.99e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 180 KETEGKREKInelLKYIEERLHTLEEEKEeLAQYQKWDKMRRALEytiynQELNETRAKLDE-----------LSAKRET 248
Cdd:PRK12704 34 KEAEEEAKRI---LEEAKKEAEAIKKEAL-LEAKEEIHKLRNEFE-----KELRERRNELQKlekrllqkeenLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 249 SGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQR--TKLELKAKdlqdelagnseqrkrl 326
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEIllEKVEEEAR---------------- 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 38566257 327 lKERQKLLEKIEEKQKELAetepkfnsvkEKEERGIarLAQATQ 370
Cdd:PRK12704 169 -HEAAVLIKEIEEEAKEEA----------DKKAKEI--LAQAIQ 199
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
170-467 |
4.83e-05 |
|
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: 47.79 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 170 ERKEESISLMK-ETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIynQELNETRAKLDELSAKRET 248
Cdd:pfam05483 373 EKNEDQLKIITmELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIA--EELKGKEQELIFLLQAREK 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 249 SGE----KSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRK 324
Cdd:pfam05483 451 EIHdleiQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEE 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 325 RLLKErqklLEKIEEKQKELAEtepKFNSVKEkeergiarlaQATQERTDLYAKQGRGSQFTSKEERDKWIK-KELKSLD 403
Cdd:pfam05483 531 RMLKQ----IENLEEKEMNLRD---ELESVRE----------EFIQKGDEVKCKLDKSEENARSIEYEVLKKeKQMKILE 593
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38566257 404 QAINDKKRQIAaihkdledteaNKEKNLEQYKLDQDLNEVKARVEELDRKYYEVKNKKDELQSE 467
Cdd:pfam05483 594 NKCNNLKKQIE-----------NKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELA 646
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
697-1045 |
4.91e-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: 48.12 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 697 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEmkmlkeKRQQSEKTFmpKQRSLQSLEASLHAMESTRESL 776
Cdd:TIGR01612 934 EKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLID------KINELDKAF--KDASLNDYEAKNNELIKYFNDL 1005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 777 KAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERI-----------KLEGIITRVETYLNENLRKRLDQVEQE 845
Cdd:TIGR01612 1006 KANLGKNKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIaihtsiyniidEIEKEIGKNIELLNKEILEEAEINITN 1085
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 846 LNELRETEGGTVLTATTSE-----LEAINKrVKDTMarsEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAI------ 914
Cdd:TIGR01612 1086 FNEIKEKLKHYNFDDFGKEenikyADEINK-IKDDI---KNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLedvadk 1161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 915 ---NHDTKELE-KMTNRQGMLLKKK---EECMKKIRELGSLP--QEAFEKYQTL------SLKQLFrkLEQCNTELKKYS 979
Cdd:TIGR01612 1162 aisNDDPEEIEkKIENIVTKIDKKKniyDEIKKLLNEIAEIEkdKTSLEEVKGInlsygkNLGKLF--LEKIDEEKKKSE 1239
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38566257 980 HVNKKALDQFVNFSEQKEK--LIKRQEELDRGYKSIMELMNVLElRKYEAIQLTFKQVSKNFSEVFQK 1045
Cdd:TIGR01612 1240 HMIKAMEAYIEDLDEIKEKspEIENEMGIEMDIKAEMETFNISH-DDDKDHHIISKKHDENISDIREK 1306
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
148-415 |
4.99e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.74 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 148 ATAPDSQRLKL-LREVAGTRVYDERK-----EESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQyqKWDKMRR 221
Cdd:PRK10929 20 ATAPDEKQITQeLEQAKAAKTPAQAEivealQSALNWLEERKGSLERAKQYQQVIDNFPKLSAELRQQLNN--ERDEPRS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 222 A---LEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDA-------QQDARDKMEDIERQVRELKTKISAmkEEKEQL 291
Cdd:PRK10929 98 VppnMSTDALEQEILQVSSQLLEKSRQAQQEQDRAREISDSlsqlpqqQTEARRQLNEIERRLQTLGTPNTP--LAQAQL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 292 SAERQEQIKQRTKLElkakdlQDELAGNS-EQRKRLLKERQKLLEK-IEEKQKELAETEPKFNSVKEKEergiarlAQAT 369
Cdd:PRK10929 176 TALQAESAALKALVD------ELELAQLSaNNRQELARLRSELAKKrSQQLDAYLQALRNQLNSQRQRE-------AERA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 38566257 370 QERTDLYAKQGRG------SQFTSKEERDKWIKKELKSLDQaINDKKRQIAA 415
Cdd:PRK10929 243 LESTELLAEQSGDlpksivAQFKINRELSQALNQQAQRMDL-IASQQRQAAS 293
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
251-428 |
6.23e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 251 EKSRQlRDAQQDARDKMEDI----ERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRL 326
Cdd:PRK09510 78 EEQRK-KKEQQQAEELQQKQaaeqERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 327 LKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAI 406
Cdd:PRK09510 157 AAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKA 236
|
170 180
....*....|....*....|..
gi 38566257 407 NDKKrqiAAIHKDLEDTEANKE 428
Cdd:PRK09510 237 AAEK---AAAAKAAEKAAAAKA 255
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
242-447 |
6.73e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 6.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 242 LSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTK----------------ISAMKEEKEQLSAERQEQIKQRTKL 305
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKnglvdlseeaklllqqLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 306 ELKAKDLQDELA--GNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQErtdlyAKQGRGS 383
Cdd:COG3206 246 RAQLGSGPDALPelLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQR-----ILASLEA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 384 QFTSKEERDKWIKKELKSLDQAI---NDKKRQIAAIHKDLEDTEANKE---KNLEQYKLDQDLNEVKARV 447
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLaelPELEAELRRLEREVEVARELYEsllQRLEEARLAEALTVGNVRV 390
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
283-492 |
7.52e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 283 AMKEEKEQLsAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGI 362
Cdd:COG1579 1 AMPEDLRAL-LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 363 ARLAQATQErtdlyakqgrgsqftskeerdkwikKELKSLDQAINDKKRQIAaihkDLEDTEANKEKNLEQykLDQDLNE 442
Cdd:COG1579 80 EQLGNVRNN-------------------------KEYEALQKEIESLKRRIS----DLEDEILELMERIEE--LEEELAE 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 38566257 443 VKARVEELDRkyyEVKNKKDELQSERNylwrEENAEQQALAAKREDLEKK 492
Cdd:COG1579 129 LEAELAELEA---ELEEKKAELDEELA----ELEAELEELEAEREELAAK 171
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
238-359 |
7.64e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 7.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 238 KLDELSAKREtsgEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKlELKA------KD 311
Cdd:PRK00409 517 KLNELIASLE---ELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIK-EAKKeadeiiKE 592
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 38566257 312 L-QDELAGNSEQRKRLLKERQKLL-EKIEEKQKELAETEPKFNSVKEKEE 359
Cdd:PRK00409 593 LrQLQKGGYASVKAHELIEARKRLnKANEKKEKKKKKQKEKQEELKVGDE 642
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
316-502 |
7.86e-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: 46.30 E-value: 7.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 316 LAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLyakqgrgsqftskeerdkwi 395
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL-------------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 396 KKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNL-EQYK-------------------------LDQDLNEVKARVEE 449
Cdd:COG4942 75 EQELAALEAELAELEKEIAELRAELEAQKEELAELLrALYRlgrqpplalllspedfldavrrlqyLKYLAPARREQAEE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 38566257 450 LDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQLLRAATGK 502
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
183-481 |
1.03e-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: 46.71 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 183 EGKREKINELLKYIEERLHTLEEEKEELAQYQKwdkMRRALEYtiynqELNETRAKLDELSAKREtsgEKSRQLRDAQ-- 260
Cdd:pfam01576 738 EQGEEKRRQLVKQVRELEAELEDERKQRAQAVA---AKKKLEL-----DLKELEAQIDAANKGRE---EAVKQLKKLQaq 806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 261 --------QDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQK 332
Cdd:pfam01576 807 mkdlqrelEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRR 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 333 LLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQE-RTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDK-K 410
Cdd:pfam01576 887 LEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTElAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKfK 966
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 411 RQIAAihkdLEDTEANKEKNLEQ------------YKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWRE-ENA 477
Cdd:pfam01576 967 SSIAA----LEAKIAQLEEQLEQesrerqaanklvRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQlEEA 1042
|
....
gi 38566257 478 EQQA 481
Cdd:pfam01576 1043 EEEA 1046
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
229-498 |
1.39e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 229 NQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELK 308
Cdd:COG4372 51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 309 AKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSK 388
Cdd:COG4372 131 RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 389 EERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYKLDQDLNEVKARVEELDRKYYEVKNKKDELQSER 468
Cdd:COG4372 211 SLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
250 260 270
....*....|....*....|....*....|
gi 38566257 469 NYLWREENAEQQALAAKREDLEKKQQLLRA 498
Cdd:COG4372 291 AALELKLLALLLNLAALSLIGALEDALLAA 320
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1114-1186 |
1.47e-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: 1.47e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38566257 1114 LSGGQKSLVALALIFaIQKcdpAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFY 1186
Cdd:cd03228 97 LSGGQRQRIAIARAL-LRD---PPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRII 165
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
226-490 |
1.54e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.66 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 226 TIYNQELNETRAKLDELSAKRETSgekSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEkeqLSAERQEQikqrTKL 305
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAA---NRQREKEKERYKRDREQWERQRRELESRVAELKEE---LRQSREKH----EEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 306 ELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKqkelaetepkfnsvkekeERGIARLAQATQER-TDLYAKQGRGSQ 384
Cdd:pfam07888 100 EEKYKELSASSEELSEEKDALLAQRAAHEARIREL------------------EEDIKTLTQRVLEReTELERMKERAKK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 385 FTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQykLDQDLNEVKARVEELDRKYYEVKNKKDEL 464
Cdd:pfam07888 162 AGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQ--LQDTITTLTQKLTTAHRKEAENEALLEEL 239
|
250 260
....*....|....*....|....*.
gi 38566257 465 QSERNYLwreeNAEQQALAAKREDLE 490
Cdd:pfam07888 240 RSLQERL----NASERKVEGLGEELS 261
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
254-490 |
1.56e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 254 RQLRDAQQDARDKMEDIERQVRELKTKISAmkeekeqlsAERQ-EQIKQRTK---LELKAKDLQDELAGNSEQRKRLLKE 329
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEE---------AEAAlEEFRQKNGlvdLSEEAKLLLQQLSELESQLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 330 RQKLLEKIEEKQKELAETEPKFNSVKEKEE--RGIARLAQATQERTDLYAKQGRGSQftskeerdkwikkELKSLDQAIN 407
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDALPELLQSPViqQLRAQLAELEAELAELSARYTPNHP-------------DVIALRAQIA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 408 DKKRQIAA-IHKDLEDTEANKEknleqyKLDQDLNEVKARVEELDRKYYEVKNKKDELQS-ERNYlwreENAEQ--QALA 483
Cdd:COG3206 302 ALRAQLQQeAQRILASLEAELE------ALQAREASLQAQLAQLEARLAELPELEAELRRlEREV----EVARElyESLL 371
|
....*..
gi 38566257 484 AKREDLE 490
Cdd:COG3206 372 QRLEEAR 378
|
|
| 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 38566257 1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIqFVLSDEFSHlRPEQRLALLHEGTgPRvisAFVEI 80
Cdd:TIGR00611 1 MYLSRLELTDFRNYDAVDL--ELSPGVNVIVGPNGQGKTNLLEAI-YYLALGRSH-RTSRDKPLIRFGA-EA---FVIEG 72
|
90 100
....*....|....*....|
gi 38566257 81 IFDNSDNRLPIDKEEVSLRR 100
Cdd:TIGR00611 73 RVSKGDREVTIPLEGLLKKK 92
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
669-898 |
1.84e-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: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 669 DTRKSRLELQKDVRKAEEELGELEAKLNEnLRRNIERINNEIDQLMnqmQQIETQQRKFKASRDSILSEMKMLKEKRQQS 748
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRIRA-LEQELAALEAELAELE---KEIAELRAELEAQKEELAELLRALYRLGRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 749 EKTFMPKQRSLQSLEASLHamestreslkaelgtdLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVE 828
Cdd:COG4942 121 PLALLLSPEDFLDAVRRLQ----------------YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 829 TylnenLRKRLDQVEQELNELreteggtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQK 898
Cdd:COG4942 185 E-----ERAALEALKAERQKL--------LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
180-481 |
2.10e-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: 45.33 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 180 KETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETraKLDELSAKRETSGEKSRQLRDA 259
Cdd:COG5185 156 VETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESE--TGNLGSESTLLEKAKEIINIEE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 260 QQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTK-LELKAKDLQDELAgNSEQRKRLLKERQKLLEKIE 338
Cdd:COG5185 234 ALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKrLNENANNLIKQFE-NTKEKIAEYTKSIDIKKATE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 339 EKQKELAETEP--KFNSVKEKEERGIARL-AQATQERTDLYAKQ-----GRGSQFTSKEERDKwiKKELKSLDQAINDKK 410
Cdd:COG5185 313 SLEEQLAAAEAeqELEESKRETETGIQNLtAEIEQGQESLTENLeaikeEIENIVGEVELSKS--SEELDSFKDTIESTK 390
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38566257 411 RQIAAIHKDLEDTEANKEKNLEQYK--LDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQA 481
Cdd:COG5185 391 ESLDEIPQNQRGYAQEILATLEDTLkaADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQS 463
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
157-348 |
2.24e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 157 KLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETR 236
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELK 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 237 AKLDELSAKRetsgEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMK-----EEKEQLSAE----RQEQIKQRTKLEl 307
Cdd:PRK03918 609 DAEKELEREE----KELKKLEEELDKAFEELAETEKRLEELRKELEELEkkyseEEYEELREEylelSRELAGLRAELE- 683
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 38566257 308 KAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETE 348
Cdd:PRK03918 684 ELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
11-79 |
2.38e-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: 44.21 E-value: 2.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38566257 11 FRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFvLSDEFSHLRPEQRlALLHEGTGPRVISAFVE 79
Cdd:cd03242 9 FRNYAELEL--EFEPGVTVLVGENAQGKTNLLEAISL-LATGKSHRTSRDK-ELIRWGAEEAKISAVLE 73
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
697-1018 |
2.39e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.45 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 697 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEM--KMLKEKRQQSEKtfmPKQRSLQSLEASLHAMESTRE 774
Cdd:COG5022 810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFgrSLKAKKRFSLLK---KETIYLQSAQRVELAERQLQE 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 775 sLKAELGT-DLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERI-KLEGIITRVETylnENLRKRLDQVEQELNELRET 852
Cdd:COG5022 887 -LKIDVKSiSSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIaRLKKLLNNIDL---EEGPSIEYVKLPELNKLHEV 962
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 853 EGGtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEH-------------MDAINHDTK 919
Cdd:COG5022 963 ESK--LKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLkelpvevaelqsaSKIISSEST 1040
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 920 ELEKMTNRQ---GMLLKKKEECMKKIRELG----SLPQEAFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNF 992
Cdd:COG5022 1041 ELSILKPLQklkGLLLLENNQLQARYKALKlrreNSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVA 1120
|
330 340
....*....|....*....|....*.
gi 38566257 993 SEQKEKLIKRQEELDRGYKSIMELMN 1018
Cdd:COG5022 1121 QMIKLNLLQEISKFLSQLVNTLEPVF 1146
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1109-1171 |
2.96e-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: 2.96e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38566257 1109 REMQQLSGGQKSLVALALIFAIQkcdpAPFYLFDEIDQALDAQHRKAVSDMIMELavHAQFIT 1171
Cdd:cd03225 130 RSPFTLSGGQKQRVAIAGVLAMD----PDILLLDEPTAGLDPAGRRELLELLKKL--KAEGKT 186
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
173-521 |
3.77e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 44.68 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 173 EESISLMKETEGKREKINEL-----------LKYIEERlHTLEEEKEELAQYQKW-DKMR--------RALEYTIYNQEL 232
Cdd:pfam05622 28 EEKNSLQQENKKLQERLDQLesgddsgtpggKKYLLLQ-KQLEQLQEENFRLETArDDYRikceelekEVLELQHRNEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 233 ----NETRAKLDELSAKRETSgEKSRQLRDAQQDARDKME---DIERQVREL------------------------KTKI 281
Cdd:pfam05622 107 tslaEEAQALKDEMDILRESS-DKVKKLEATVETYKKKLEdlgDLRRQVKLLeernaeymqrtlqleeelkkanalRGQL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 282 SAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKqkelaetepKFNSVKEKEERG 361
Cdd:pfam05622 186 ETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRETNEEL---------RCAQLQQAELSQ 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 362 IARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKsLDQAINDKKRqIAAIHKDLEDTEANKEKNLEQYKL-DQDL 440
Cdd:pfam05622 257 ADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLR-LGQEGSYRER-LTELQQLLEDANRRKNELETQNRLaNQRI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 441 NEVKARVEELDRKYYEVKNKKDELQSernyLWREENAEQQALAAKREDLEKKQQLLRAATGKAILNGIDSINKVLEHFRR 520
Cdd:pfam05622 335 LELQQQVEELQKALQEQGSKAEDSSL----LKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQEALRK 410
|
.
gi 38566257 521 K 521
Cdd:pfam05622 411 K 411
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
253-428 |
3.81e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 253 SRQLRDAQQDARDKMEDIERQVrelktkiSAMKEEKEqLSAeRQEQIKQRTKLELKAKDLQDELAGNSE---QRKRLLKE 329
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEA-------EAIKKEAL-LEA-KEEIHKLRNEFEKELRERRNELQKLEKrllQKEENLDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 330 RQKLLEKIEEK-QKELAETEPKFNSVKEKEERgIARLAQATQERTDlyakqgRGSQFTSKEerdkwIKKELksLDQAIND 408
Cdd:PRK12704 101 KLELLEKREEElEKKEKELEQKQQELEKKEEE-LEELIEEQLQELE------RISGLTAEE-----AKEIL--LEKVEEE 166
|
170 180
....*....|....*....|...
gi 38566257 409 KKRQIAAIHKDLED---TEANKE 428
Cdd:PRK12704 167 ARHEAAVLIKEIEEeakEEADKK 189
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
741-902 |
3.86e-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: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 741 LKEKRQQSEKT--FMPKQrsLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERI 818
Cdd:COG3206 166 LELRREEARKAleFLEEQ--LPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 819 KLEGIITRVETYLNE--------NLRKRLDQVEQELNELRE--TEGGTVLTATTSELEAINKRVKDTMARS-EDLDNSID 887
Cdd:COG3206 244 ALRAQLGSGPDALPEllqspviqQLRAQLAELEAELAELSAryTPNHPDVIALRAQIAALRAQLQQEAQRIlASLEAELE 323
|
170
....*....|....*
gi 38566257 888 KTEAGIKELQKSMER 902
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 38566257 28 NVIVGRNGSGKSNFFYAIQFvLSDEFSHLRPEQRLALLHEGTG----------PRVISAFVEIIFDNSDNR----LPIDK 93
Cdd:pfam13304 2 NVLIGPNGSGKSNLLEALRF-LADFDALVIGLTDERSRNGGIGgipsllngidPKEPIEFEISEFLEDGVRyrygLDLER 80
|
90 100
....*....|....*....|....
gi 38566257 94 EEVS--LRRVIGAKKDQYFLDKKM 115
Cdd:pfam13304 81 EDVEekLSSKPTLLEKRLLLREDS 104
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1109-1170 |
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 38566257 1109 REMQQLSGGQKSLVALAlIFAIQKCDpapFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFI 1170
Cdd:cd03236 135 RNIDQLSGGELQRVAIA-AALARDAD---FYFFDEPSSYLDIKQRLNAARLIRELAEDDNYV 192
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
111-463 |
4.82e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 44.65 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 111 LDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKIN 190
Cdd:PTZ00108 1026 LVITNAKKKDLVKELKKLGYVRFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSYDYLLSMPIWSLTKEKVE 1105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 191 ELLKYIEERLhtleeekeelaqyQKWDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDI 270
Cdd:PTZ00108 1106 KLNAELEKKE-------------KELEKLKNTTPKDMWLEDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKP 1172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 271 ERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKD-------LQDELAGNSEQRKRLLKERQKLLEKIEEKQKE 343
Cdd:PTZ00108 1173 KLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPdnkksnsSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSK 1252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 344 LAETEPKFNSVKEKEERGIARL---AQATQERTDLYAKQGRGSQFTSKEERDkwikkELKSLDQAINDKKRQIAAIHKDL 420
Cdd:PTZ00108 1253 SSEDNDEFSSDDLSKEGKPKNApkrVSAVQYSPPPPSKRPDGESNGGSKPSS-----PTKKKVKKRLEGSLAALKKKKKS 1327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 38566257 421 EDTEANKEKNLEQYK--LDQDLNEVKAR---------VEELDRKYYEVKNKKDE 463
Cdd:PTZ00108 1328 EKKTARKKKSKTRVKqaSASQSSRLLRRprkkksdssSEDDDDSEVDDSEDEDD 1381
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
165-494 |
5.39e-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: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 165 TRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAqyqkwDKMRRAleytiyNQELNETRAKLDELSA 244
Cdd:TIGR00606 704 LRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELR-----NKLQKV------NRDIQRLKNDIEEQET 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 245 KRETSGEKSRQLRDAQQDArDKMEDIERQVRELKTKIsamkeekEQLSAERQEqikqrTKLELKAKDLQDELAGNSEQRK 324
Cdd:TIGR00606 773 LLGTIMPEEESAKVCLTDV-TIMERFQMELKDVERKI-------AQQAAKLQG-----SDLDRTVQQVNQEKQEKQHELD 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 325 RLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEergiARLAQATQERTDLyakqgrgsqftskEERDKWIKKELKSLDQ 404
Cdd:TIGR00606 840 TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEK----LQIGTNLQRRQQF-------------EEQLVELSTEVQSLIR 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 405 AINDKKRQIAAIHKDLEDTEANKE-----KNLEQYKLDQDLNEVKarvEELDRKYYEVKNKKDELQSERNYLWREENAEQ 479
Cdd:TIGR00606 903 EIKDAKEQDSPLETFLEKDQQEKEelissKETSNKKAQDKVNDIK---EKVKNIHGYMKDIENKIQDGKDDYLKQKETEL 979
|
330
....*....|....*
gi 38566257 480 QALAAKREDLEKKQQ 494
Cdd:TIGR00606 980 NTVNAQLEECEKHQE 994
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
186-490 |
5.69e-04 |
|
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: 43.90 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 186 REKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRAlEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARD 265
Cdd:pfam19220 26 KADFSQLIEPIEAILRELPQAKSRLLELEALLAQERA-AYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 266 KMEDIERQVRELKTKISA----MKEEKEQLSAERQEQIKQRTKLELKAKDLQD---ELAGNSEQRKRLLKERQKLLEKIE 338
Cdd:pfam19220 105 AKEELRIELRDKTAQAEAlerqLAAETEQNRALEEENKALREEAQAAEKALQRaegELATARERLALLEQENRRLQALSE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 339 EKQKELAETEPKfnsVKEKEERGIARLAQATQERTDLYAKQ-GRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIH 417
Cdd:pfam19220 185 EQAAELAELTRR---LAELETQLDATRARLRALEGQLAAEQaERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 418 KDLEDTEAN-KEKNLEQYKLDQDLNE-------VKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDL 489
Cdd:pfam19220 262 QLLAEARNQlRDRDEAIRAAERRLKEasierdtLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAAL 341
|
.
gi 38566257 490 E 490
Cdd:pfam19220 342 E 342
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
246-447 |
5.69e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 246 RETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAE----RQEQIKQRTKLELKAKDLQ-DELAGNS 320
Cdd:PHA02562 208 RKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAlnklNTAAAKIKSKIEQFQKVIKmYEKGGVC 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 321 EQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAK-QGRGSQFTSKEERDKWIKKEL 399
Cdd:PHA02562 288 PTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKiSTNKQSLITLVDKAKKVKAAI 367
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 38566257 400 KSLDQAINDKKRQIAAIHKDLED---TEANKEKNLEQYKLDQDL---NEVKARV 447
Cdd:PHA02562 368 EELQAEFVDNAEELAKLQDELDKivkTKSELVKEKYHRGIVTDLlkdSGIKASI 421
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
234-379 |
5.89e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 234 ETRAKLDELSAKRETSgeksRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKakdlQ 313
Cdd:PRK12704 52 EAIKKEALLEAKEEIH----KLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK----Q 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38566257 314 DELAGNSEQRKRLLKERQKLLEKI-----EEKQKELAEtepkfnSVKEKEERGIARLAQATQERTDLYAKQ 379
Cdd:PRK12704 124 QELEKKEEELEELIEEQLQELERIsgltaEEAKEILLE------KVEEEARHEAAVLIKEIEEEAKEEADK 188
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
187-511 |
6.60e-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: 44.19 E-value: 6.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 187 EKINELLKYIEERLHTLEEEKEELAQ-----YQKWDKMRRALEytIYNQELNETRAKLDELS-AKRETSGEKSRQLRDAQ 260
Cdd:TIGR00618 545 EDVYHQLTSERKQRASLKEQMQEIQQsfsilTQCDNRSKEDIP--NLQNITVRLQDLTEKLSeAEDMLACEQHALLRKLQ 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 261 --QDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQ------------IKQRTKLELKAKDLQDELAGNSEQRKRL 326
Cdd:TIGR00618 623 peQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREhalsirvlpkelLASRQLALQKMQSEKEQLTYWKEMLAQC 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 327 LKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQE-----RTDLYAKQGRGSQFTSKEERDKWIKKELKS 401
Cdd:TIGR00618 703 QTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKElmhqaRTVLKARTEAHFNNNEEVTAALQTGAELSH 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 402 LDQAINDKKRQIAAIHKDLEDTEAN---------KEKNLEQYKLDQDLNEVKARVEELDRKYYEVKnkkdelqseRNYLW 472
Cdd:TIGR00618 783 LAAEIQFFNRLREEDTHLLKTLEAEigqeipsdeDILNLQCETLVQEEEQFLSRLEEKSATLGEIT---------HQLLK 853
|
330 340 350
....*....|....*....|....*....|....*....
gi 38566257 473 REENAEQQAlaakredlEKKQQLLRAATGKAILNGIDSI 511
Cdd:TIGR00618 854 YEECSKQLA--------QLTQEQAKIIQLSDKLNGINQI 884
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1113-1184 |
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 38566257 1113 QLSGGQKSLVALALIFAIQkcdpAPFYLFDEIDQALDAQHRKAVSDMIMELavHAQF-ITTTF----RPELLESADK 1184
Cdd:PRK10851 136 QLSGGQKQRVALARALAVE----PQILLLDEPFGALDAQVRKELRRWLRQL--HEELkFTSVFvthdQEEAMEVADR 206
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
168-409 |
9.24e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 168 YDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEEL-AQYQKWDKMRRALeytiyNQELNETRAKLDELSAKR 246
Cdd:COG1340 27 LKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELnEKVKELKEERDEL-----NEKLNELREELDELRKEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 247 ETSGEKSRQLRDAQQDARDKMEDIERQV------RELKTKISAMKEEKEQLSAERQEQIKQRTKLE------LKAKDLQD 314
Cdd:COG1340 102 AELNKAGGSIDKLRKEIERLEWRQQTEVlspeeeKELVEKIKELEKELEKAKKALEKNEKLKELRAelkelrKEAEEIHK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 315 ELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERgIARLAQATQERTDLYAKQGRGSQFTSKEERDKW 394
Cdd:COG1340 182 KIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADE-LHEEIIELQKELRELRKELKKLRKKQRALKREK 260
|
250
....*....|....*
gi 38566257 395 IKKELKSLDQAINDK 409
Cdd:COG1340 261 EKEELEEKAEEIFEK 275
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
180-498 |
9.34e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.50 E-value: 9.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 180 KETEGKREKINELLKYIEErLHTLEEEKEELAQYQKWDKMRRALeYTIYNQELNETRAKLdelsAKRETSGEKSRQLRDA 259
Cdd:TIGR00606 169 KALKQKFDEIFSATRYIKA-LETLRQVRQTQGQKVQEHQMELKY-LKQYKEKACEIRDQI----TSKEAQLESSREIVKS 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 260 QQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDL----QDELAGNSEQRKRLLKERQKLLE 335
Cdd:TIGR00606 243 YENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVfqgtDEQLNDLYHNHQRTVREKERELV 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 336 KIEEKQKELAETEPKFNSVKEKEERGIARL---AQATQERTDLYAKQGRGSQFTSKE---ERDKWIKKELKS----LDQA 405
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLqlqADRHQEHIRARDSLIQSLATRLELdgfERGPFSERQIKNfhtlVIER 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 406 INDKKRQIAAIHKDLEDTEANKEKNleqykldqdLNEVKARVEELDRKyyeVKNKKDELQSERNYLWREENAEQQALAAK 485
Cdd:TIGR00606 403 QEDEAKTAAQLCADLQSKERLKQEQ---------ADEIRDEKKGLGRT---IELKKEILEKKQEELKFVIKELQQLEGSS 470
|
330
....*....|...
gi 38566257 486 REDLEKKQQLLRA 498
Cdd:TIGR00606 471 DRILELDQELRKA 483
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
171-342 |
9.92e-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: 9.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 171 RKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKM-RRALEYTIYNQELNETRAKLDELSAK---- 245
Cdd:COG3206 203 QKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSgPDALPELLQSPVIQQLRAQLAELEAElael 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 246 RETSGEKS---RQLRDAQQDARDKMED-IERQVRELKTKISAMKEEKEQLSAERQE---QIKQRTKLELKAKDLQDELAG 318
Cdd:COG3206 283 SARYTPNHpdvIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQleaRLAELPELEAELRRLEREVEV 362
|
170 180
....*....|....*....|....
gi 38566257 319 NSEQRKRLLKERQKLleKIEEKQK 342
Cdd:COG3206 363 ARELYESLLQRLEEA--RLAEALT 384
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
229-357 |
1.08e-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: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 229 NQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSA---ERQEQIKQRTKL 305
Cdd:pfam06008 53 AQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSsdlSRMLAEAQRMLG 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 38566257 306 ELKAKDLQDELAGNSEQrkrlLKERQKLLEKIEEKQKEL-AETEPKFNSVKEK 357
Cdd:pfam06008 133 EIRSRDFGTQLQNAEAE----LKAAQDLLSRIQTWFQSPqEENKALANALRDS 181
|
|
| 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 38566257 158 LLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKW-DKMRRALE------------ 224
Cdd:pfam06160 279 LEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYTLNENELERVRGLEKQlEELEKRYDeiverleekeva 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 225 YTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKIsamkeEKEQLSAERQEQIKQRTK 304
Cdd:pfam06160 359 YSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLV-----EKSNLPGLPESYLDYFFD 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 38566257 305 LELKAKDLQDELAG---NSEQRKRLLKERQKLLEKIEEKQKELAET 347
Cdd:pfam06160 434 VSDEIEDLADELNEvplNMDEVNRLLDEAQDDVDTLYEKTEELIDN 479
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
716-888 |
1.09e-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: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 716 QMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKR 795
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 796 VDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLnENLRKRLDQVEQELNELREteggtvltATTSELEAINKRVKDT 875
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEEL-AELEAELAELEAELEEKKA--------ELDEELAELEAELEEL 161
|
170
....*....|...
gi 38566257 876 MARSEDLDNSIDK 888
Cdd:COG1579 162 EAEREELAAKIPP 174
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
173-494 |
1.31e-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: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 173 EESISLMKETEGKREKINELlkyiEERLHTLEEEKEELAQYQKWDKMrralEYTIYNQELNETRAKLDELSAKRETSGEK 252
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNKL----EVELNKLEKQKKENKKNIDKFLT----EIKKKEKELEKLNNKYNDLKKQKEELENE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 253 SRQLRDAQQDARDKMEDIERQV-----------------RELKTKISAMKEEKEQLSaerqeqiKQRTKLELKAKDLQDE 315
Cdd:TIGR04523 175 LNLLEKEKLNIQKNIDKIKNKLlklelllsnlkkkiqknKSLESQISELKKQNNQLK-------DNIEKKQQEINEKTTE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 316 LAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRgSQFTSKEERDKWI 395
Cdd:TIGR04523 248 ISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELK-SELKNQEKKLEEI 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 396 KKELKSLDQAINDKKRQIAAIHKDLEDTEANKEknleqyKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREE 475
Cdd:TIGR04523 327 QNQISQNNKIISQLNEQISQLKKELTNSESENS------EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI 400
|
330
....*....|....*....
gi 38566257 476 NAEQQALAAKREDLEKKQQ 494
Cdd:TIGR04523 401 QNQEKLNQQKDEQIKKLQQ 419
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
173-504 |
1.35e-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: 43.24 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 173 EESISLMKETEGKREKINELLkyiEERLH----TLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRET 248
Cdd:pfam01576 137 EEDILLLEDQNSKLSKERKLL---EERISeftsNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 249 SGEKSrqlrdaqqDARDKMEDIERQVRELKTKISAMKEE-------KEQLSAERQEQIKQRTKLELKAKDLQDELAGNSE 321
Cdd:pfam01576 214 EGEST--------DLQEQIAELQAQIAELRAQLAKKEEElqaalarLEEETAQKNNALKKIRELEAQISELQEDLESERA 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 322 QRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKE---KEERGIARLAQATQERTDLYA------KQGRGSQFTSKEERD 392
Cdd:pfam01576 286 ARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQElrsKREQEVTELKKALEEETRSHEaqlqemRQKHTQALEELTEQL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 393 KWIKKELKSLDQAINDKKRQIAAIHKDLED-TEANKEKNLEQYKLDQDLNEVKARVEELDRKYYEVKNKKDELQSErnyl 471
Cdd:pfam01576 366 EQAKRNKANLEKAKQALESENAELQAELRTlQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSE---- 441
|
330 340 350
....*....|....*....|....*....|...
gi 38566257 472 wreenaeqqalaakredLEKKQQLLRAATGKAI 504
Cdd:pfam01576 442 -----------------LESVSSLLNEAEGKNI 457
|
|
| MAT1 |
pfam06391 |
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ... |
227-352 |
1.54e-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: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 227 IYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQ--IKQRTK 304
Cdd:pfam06391 58 TNGIDVEETEKKIEQYEKENKDLILKNKMKLSQEEEELEELLELEKREKEERRKEEKQEEEEEKEKKEKAKQelIDELMT 137
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 38566257 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. ... |
699-1031 |
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 38566257 699 LRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMpkqRSLQSLEASLHAMESTRESLKa 778
Cdd:pfam15921 262 LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYM---RQLSDLESTVSQLRSELREAK- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 779 ELGTDLLSQLsledQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNEnlRKRLDQVEQELNEL---RETEGG 855
Cdd:pfam15921 338 RMYEDKIEEL----EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHK--REKELSLEKEQNKRlwdRDTGNS 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 856 TVLTATTSELEAINKRVKdtmaRSEDLDNSIDkteagiKELQKSMERwknmekeHMDAINHDTKELEKMTNRQGMLLKKK 935
Cdd:pfam15921 412 ITIDHLRRELDDRNMEVQ----RLEALLKAMK------SECQGQMER-------QMAAIQGKNESLEKVSSLTAQLESTK 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 936 EECMKKIRELGS--LPQEAFEKY---QTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGY 1010
Cdd:pfam15921 475 EMLRKVVEELTAkkMTLESSERTvsdLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALK 554
|
330 340
....*....|....*....|.
gi 38566257 1011 KSIMELMNVLELRKYEAIQLT 1031
Cdd:pfam15921 555 LQMAEKDKVIEILRQQIENMT 575
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
281-503 |
1.66e-03 |
|
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: 42.90 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 281 ISAMKEEKEQLSAERqEQIKQRtklELKAKDLQDElAGNSEQRKRLLKERQKLLEKIEEKQKELAETEP-KFNSVKEKEE 359
Cdd:NF012221 1534 VVATSESSQQADAVS-KHAKQD---DAAQNALADK-ERAEADRQRLEQEKQQQLAAISGSQSQLESTDQnALETNGQAQR 1608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 360 RGIARLAQA-TQERTDLyaKQG----RGSQFTSKEERDKW--------IKKELKSLDQA-------INDKKRQIAAIHKD 419
Cdd:NF012221 1609 DAILEESRAvTKELTTL--AQGldalDSQATYAGESGDQWrnpfagglLDRVQEQLDDAkkisgkqLADAKQRHVDNQQK 1686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 420 LEDTEANKEKNL---EQYKLDQDLNEVKARVeeldrkyyEVKNKKDELQSERNylwREENAEQQALAAKREDLEKKQQLL 496
Cdd:NF012221 1687 VKDAVAKSEAGVaqgEQNQANAEQDIDDAKA--------DAEKRKDDALAKQN---EAQQAESDANAAANDAQSRGEQDA 1755
|
....*..
gi 38566257 497 RAATGKA 503
Cdd:NF012221 1756 SAAENKA 1762
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
151-495 |
1.84e-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: 42.65 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 151 PDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQ 230
Cdd:TIGR00618 274 AQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 231 ELNETRAKLDELSAKRETSGEKS--RQLRDAQQD----------ARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQ 298
Cdd:TIGR00618 354 EIHIRDAHEVATSIREISCQQHTltQHIHTLQQQkttltqklqsLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQ 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 299 IKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIE---------EKQKELAETEPKFNSVKEKEERGI-ARLAQA 368
Cdd:TIGR00618 434 ELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQqlqtkeqihLQETRKKAVVLARLLELQEEPCPLcGSCIHP 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 369 TQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAaihkdlEDTEANKEKNLEQYKLDQDLNEVKARVE 448
Cdd:TIGR00618 514 NPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRA------SLKEQMQEIQQSFSILTQCDNRSKEDIP 587
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 38566257 449 ELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQL 495
Cdd:TIGR00618 588 NLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHL 634
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
173-429 |
2.10e-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: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 173 EESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQyqkwdkMRRALEYTI--YNQELNETRAKLDELSAKRETSG 250
Cdd:pfam05483 506 QEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN------LRDELESVReeFIQKGDEVKCKLDKSEENARSIE 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 251 EKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKER 330
Cdd:pfam05483 580 YEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNY 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 331 QK-----------LLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAK--QGRGSQFTSKEERDKWIKK 397
Cdd:pfam05483 660 QKeiedkkiseekLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKiiEERDSELGLYKNKEQEQSS 739
|
250 260 270
....*....|....*....|....*....|..
gi 38566257 398 ELKSLDQAINDKKRQIAAIHKDLEDTEANKEK 429
Cdd:pfam05483 740 AKAALEIELSNIKAELLSLKKQLEIEKEEKEK 771
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
139-891 |
2.15e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 139 VKQGKINQMATAPDSQR------------LKLLREVAGT------RVYDERKEESISLMKETEGKREKinELlkyiEERL 200
Cdd:PRK02224 135 VRQGEVNKLINATPSDRqdmiddllqlgkLEEYRERASDarlgveRVLSDQRGSLDQLKAQIEEKEEK--DL----HERL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 201 HTLEeekeelaqyqkwdkmrraleytiynQELNETRAKLDELSAKRETSGEKSRQLR---DAQQDARDKMEDIERQVREL 277
Cdd:PRK02224 209 NGLE-------------------------SELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 278 KTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEK 357
Cdd:PRK02224 264 RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEE 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 358 EERgiarlaqATQERTDLyakqgrgsqftskEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDteankeknleqykLD 437
Cdd:PRK02224 344 AES-------LREDADDL-------------EERAEELREEAAELESELEEAREAVEDRREEIEE-------------LE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 438 QDLNEVKARVEELDRKYYEVKNKKDELQSERNYLwREENAEQQA-LAAKREDLEKKQQLLRAatGKAILNGidsinkvle 516
Cdd:PRK02224 391 EEIEELRERFGDAPVDLGNAEDFLEELREERDEL-REREAELEAtLRTARERVEEAEALLEA--GKCPECG--------- 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 517 hfrrkginQHVQNGYHgivmnnfecepafytcVEVTAGNRlfyhivdsdevstkilmefnkmnlpGEVTFLPLNKLDVRD 596
Cdd:PRK02224 459 --------QPVEGSPH----------------VETIEEDR-------------------------ERVEELEAELEDLEE 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 597 TaypetndaipmisklrynprfdkafkhvfgktlicrSMEVSTQLARAftMDCITLEgdqvshrgaltggyydtrkSRLE 676
Cdd:PRK02224 490 E------------------------------------VEEVEERLERA--EDLVEAE-------------------DRIE 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 677 LQKDVRKAEEELGELEAKLNENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFmpkq 756
Cdd:PRK02224 513 RLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERI---- 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 757 RSLQSLEASLHAMESTRESLKaELGTDLLSQLSLEDQKR--VDALNDEIRQLQQEnrqLLNERI-KLEGIITRVETYLnE 833
Cdd:PRK02224 589 ESLERIRTLLAAIADAEDEIE-RLREKREALAELNDERRerLAEKRERKRELEAE---FDEARIeEAREDKERAEEYL-E 663
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 38566257 834 NLRKRLDQVEQELNELRETEGGtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEA 891
Cdd:PRK02224 664 QVEEKLDELREERDDLQAEIGA--VENELEELEELRERREALENRVEALEALYDEAEE 719
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
702-947 |
2.19e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 702 NIERINNEIDQLMNQMQQIETQQRKFKAsrdsiLSEMKMLKEKRQQsektfmpkqrsLQSLEASLHAMESTRESLKAELG 781
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDAREQIEL-----LEPIRELAERYAA-----------ARERLAELEYLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 782 TDLLsqlsledQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRLDQVEQELNELREteggtvltat 861
Cdd:COG4913 290 LELL-------EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLER---------- 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 862 tsELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINhdtKELEKMTNRQGMLLKKKEECMKK 941
Cdd:COG4913 353 --ELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE---EALAEAEAALRDLRRELRELEAE 427
|
....*.
gi 38566257 942 IRELGS 947
Cdd:COG4913 428 IASLER 433
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
696-944 |
2.50e-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: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 696 NENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRES 775
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 776 LKAELGTDLLS----QLSLEDQKR--------VDALNDEIRQLQQENRQL------LNERI-KLEGIITRVETYL----- 831
Cdd:TIGR04523 466 LETQLKVLSRSinkiKQNLEQKQKelkskekeLKKLNEEKKELEEKVKDLtkkissLKEKIeKLESEKKEKESKIsdled 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 832 ----------NENLRKRLDQVEQELNELRETEggTVLTATTSELEainKRVKDTMARSEDLDNSIDKTEAGIKELQKSME 901
Cdd:TIGR04523 546 elnkddfelkKENLEKEIDEKNKEIEELKQTQ--KSLKKKQEEKQ---ELIDQKEKEKKDLIKEIEEKEKKISSLEKELE 620
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 38566257 902 rwkNMEKEHMDaINHDTKELEKMTNRQGMLLKKKEECMKKIRE 944
Cdd:TIGR04523 621 ---KAKKENEK-LSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
254-493 |
2.51e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.37 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 254 RQLRDAQQDARdkMEDIERQVRELKTKIsamkeEKEQLSAERQEQIKQRTKLELKAKDLQDELAGN---SEQRKRLLKER 330
Cdd:COG5022 801 PLLSLLGSRKE--YRSYLACIIKLQKTI-----KREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKrfsLLKKETIYLQS 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 331 QKLLEKIEEKQKELAETEPKFNSVKEKeergiarlaqatqertdLYAKQGRGSQFTSKEERDkwIKKELKSLDQAINDKK 410
Cdd:COG5022 874 AQRVELAERQLQELKIDVKSISSLKLV-----------------NLELESEIIELKKSLSSD--LIENLEFKTELIARLK 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 411 RQIAAIhkdleDTEANKEKNLEQYKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLE 490
Cdd:COG5022 935 KLLNNI-----DLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYG 1009
|
...
gi 38566257 491 KKQ 493
Cdd:COG5022 1010 ALQ 1012
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
275-515 |
2.63e-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: 42.07 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 275 RELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELA-----GNSEQRKRLLKERQKLLEKIEEKQKELaetEP 349
Cdd:pfam18971 559 RNLENKLTAKGLSLQEANKLIKDFLSSNKELAGKALNFNKAVAeakstGNYDEVKKAQKDLEKSLRKREHLEKEV---EK 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 350 KFNSVKEKEERGIARlAQATQERTDLYAKQGRGSqftSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDT--EANK 427
Cdd:pfam18971 636 KLESKSGNKNKMEAK-AQANSQKDEIFALINKEA---NRDARAIAYTQNLKGIKRELSDKLEKISKDLKDFSKSfdEFKN 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 428 EKNLEQYKLDQDLNEVKARVEELDRKyYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQllRAATGKAILNG 507
Cdd:pfam18971 712 GKNKDFSKAEETLKALKGSVKDLGIN-PEWISKVENLNAALNEFKNGKNKDFSKVTQAKSDLENSVK--DVIINQKVTDK 788
|
....*...
gi 38566257 508 IDSINKVL 515
Cdd:pfam18971 789 VDNLNQAV 796
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
275-488 |
2.81e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 41.86 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 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 38566257 352 NSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKS---LDQAINDKKRQIAAihkDLEDTEANK- 427
Cdd:PRK05035 486 DAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAekqAAAAADPKKAAVAA---AIARAKAKKa 562
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38566257 428 EKNLEQYKLDQDLNEVKARVEELDRKyyeVKNKKDELQSErnylwREENAEQQALAAKRED 488
Cdd:PRK05035 563 AQQAANAEAEEEVDPKKAAVAAAIAR---AKAKKAAQQAA-----SAEPEEQVAEVDPKKA 615
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1113-1184 |
2.92e-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: 2.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38566257 1113 QLSGGQKSLVALALIFAIqkcDPApFYLFDEIDQALDAQHRKAVSDMIMELavHAQF-ITTTF----RPELLESADK 1184
Cdd:cd03296 136 QLSGGQRQRVALARALAV---EPK-VLLLDEPFGALDAKVRKELRRWLRRL--HDELhVTTVFvthdQEEALEVADR 206
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1109-1185 |
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 38566257 1109 REMQQLSGGQKSLVALALIFAIqkcdPAPFYLFDEIDQALDAQHRKAVSDMIMElavHAQ----FITTTFRPELLESADK 1184
Cdd:COG4133 127 LPVRQLSAGQKRRVALARLLLS----PAPLWLLDEPFTALDAAGVALLAELIAA---HLArggaVLLTTHQPLELAAARV 199
|
.
gi 38566257 1185 F 1185
Cdd:COG4133 200 L 200
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1112-1184 |
3.51e-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: 3.51e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38566257 1112 QQLSGGQKSLVALA--LIfaiqkCDPaPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADK 1184
Cdd:COG2274 610 SNLSGGQRQRLAIAraLL-----RNP-RILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADR 678
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1109-1163 |
3.65e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 40.74 E-value: 3.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 38566257 1109 REMQQLSGGQKSLVALALIFAIqkcDPApFYLFDEIDQALDAQHRKAVSDMIMEL 1163
Cdd:PRK13632 138 KEPQNLSGGQKQRVAIASVLAL---NPE-IIIFDESTSMLDPKGKREIKKIMVDL 188
|
|
| 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 38566257 171 RKEESISLMKETEGKREKINELLKYIEERlhtlEEEKEELAQYQKWDKMrraleytiynQELNETRAKLDELSAKRETSG 250
Cdd:COG5022 912 KKSLSSDLIENLEFKTELIARLKKLLNNI----DLEEGPSIEYVKLPEL----------NKLHEVESKLKETSEEYEDLL 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 251 EKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQE---------QIKQRTKLELKAKDLQdELAGNSE 321
Cdd:COG5022 978 KKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEvaelqsaskIISSESTELSILKPLQ-KLKGLLL 1056
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 38566257 322 QRKRLLKER------QKLLEKIEEKQKELAE-TEPKFNSVKEKEER 360
Cdd:COG5022 1057 LENNQLQARykalklRRENSLLDDKQLYQLEsTENLLKTINVKDLE 1102
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
734-968 |
3.93e-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: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 734 ILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELG----TDLLSQLSLEDQKRVDALNDEIRQLQQE 809
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKArqaeMDRQAAIYAEQERMAMERERELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 810 NRQLLNERIKLEGIITRVETY-----LNENLRKRLDQVEQELNELR-----ETEGGTVLTATTSELEAInkRVKDTMARS 879
Cdd:pfam17380 357 ERKRELERIRQEEIAMEISRMrelerLQMERQQKNERVRQELEAARkvkilEEERQRKIQQQKVEMEQI--RAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 880 EDLDNSIDKTEAGIKEL-QKSMERWKNMEKEHMDAINHDTKELEKmtNRQGMLLKKKEECMKKIRElgslpQEAFEKYQT 958
Cdd:pfam17380 435 REVRRLEEERAREMERVrLEEQERQQQVERLRQQEEERKRKKLEL--EKEKRDRKRAEEQRRKILE-----KELEERKQA 507
|
250
....*....|
gi 38566257 959 LSLKQLFRKL 968
Cdd:pfam17380 508 MIEEERKRKL 517
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
270-414 |
3.94e-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: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 270 IERQVRELKTKISAMKEEKEQLSAERQEQikQRTKLELKAKDLQDELagnseqrKRLLKERQKLLEKIEEKQKELAETEP 349
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEER--ELTEEEEEIRRLEEQV-------ERLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38566257 350 KFNSVKEKEERGIARlaqatqERtdlyakqgrgsQFTSKEERDKWIKKELKSLDQAINDKKRQIA 414
Cdd:COG2433 449 ELSEARSEERREIRK------DR-----------EISRLDREIERLERELEEERERIEELKRKLE 496
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1114-1186 |
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 38566257 1114 LSGGQKSLVALALifAI-QKCDpapFYLFDEIDQALDAQhrkaVSDMIME------LAVHAQFITTTFRPELLESADKFY 1186
Cdd:cd03250 128 LSGGQKQRISLAR--AVySDAD---IYLLDDPLSAVDAH----VGRHIFEncilglLLNNKTRILVTHQLQLLPHADQIV 198
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
268-435 |
4.06e-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: 41.14 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 268 EDIERQVrELKTKISAMKEEKEQLSAERQEQIKQrtklELKAKdlQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAET 347
Cdd:pfam05262 188 EDNEKGV-NFRRDMTDLKERESQEDAKRAQQLKE----ELDKK--QIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 348 EPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKrqiAAIHKDLEDTEANK 427
Cdd:pfam05262 261 PKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKE---LEAQKKREPVAEDL 337
|
....*...
gi 38566257 428 EKNLEQYK 435
Cdd:pfam05262 338 QKTKPQVE 345
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
173-503 |
4.20e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 173 EESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALeytiyNQELNETRAKLdelsakretsgek 252
Cdd:TIGR00606 234 ESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKD-----NSELELKMEKV------------- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 253 srqLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQK 332
Cdd:TIGR00606 296 ---FQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQS 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 333 LLEKIEEKQKE---LAETEPKfNSVKEKEERGIARLAQATQERTDLYAKQG-RGSQFTSKEERDKWIKKELKSLDQAIND 408
Cdd:TIGR00606 373 LATRLELDGFErgpFSERQIK-NFHTLVIERQEDEAKTAAQLCADLQSKERlKQEQADEIRDEKKGLGRTIELKKEILEK 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 409 KKRQIAAIHKDLEDTEANKEKNLEqykLDQDLNEVKARVEELDRKYYEVKNKKDE--LQSERNYLWREENAEQQALAAKR 486
Cdd:TIGR00606 452 KQEELKFVIKELQQLEGSSDRILE---LDQELRKAERELSKAEKNSLTETLKKEVksLQNEKADLDRKLRKLDQEMEQLN 528
|
330
....*....|....*..
gi 38566257 487 EDLEKKQQLLRAATGKA 503
Cdd:TIGR00606 529 HHTTTRTQMEMLTKDKM 545
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
330-500 |
4.32e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 330 RQKLLEKIEEKQKELaetepkFNSVKEKEERGIARLAQATQERTDLYAKQGrgsQFTSKEERDKWIKKELKSLDQAINDK 409
Cdd:COG4717 44 RAMLLERLEKEADEL------FKPQGRKPELNLKELKELEEELKEAEEKEE---EYAELQEELEELEEELEELEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 410 KRQIAAIHKDLEDTEANKEKNleqyKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLwrEENAEQQALAAKREDL 489
Cdd:COG4717 115 REELEKLEKLLQLLPLYQELE----ALEAELAELPERLEELEERLEELRELEEELEELEAEL--AELQEELEELLEQLSL 188
|
170
....*....|.
gi 38566257 490 EKKQQLLRAAT 500
Cdd:COG4717 189 ATEEELQDLAE 199
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
697-1046 |
4.62e-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: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 697 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKasrdSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTresl 776
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK----SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQ---- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 777 kaelgtdlLSQLSLEDQKRVDALNDEIRQLQQENRQLlneriklegiitrvetylnENLRKRLDQVEQELNELRETEGGT 856
Cdd:TIGR04523 255 --------LNQLKDEQNKIKKQLSEKQKELEQNNKKI-------------------KELEKQLNQLKSEISDLNNQKEQD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 857 VLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKKKE 936
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 937 ECMKKIRELGSLPQEAFEKYQTL-----SLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKrqeELDRGYK 1011
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKdeqikKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK---NLDNTRE 464
|
330 340 350
....*....|....*....|....*....|....*
gi 38566257 1012 SIMELMNVLElRKYEAIQLTFKQVSKNFSEVFQKL 1046
Cdd:TIGR04523 465 SLETQLKVLS-RSINKIKQNLEQKQKELKSKEKEL 498
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
232-494 |
5.03e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.25 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 232 LNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKE-------QLSAERQEQIKQRTK 304
Cdd:pfam05483 263 LEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatkticQLTEEKEAQMEELNK 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 305 LELKAKDLQDELAGNSEQRKRLLKERQKLLEKIE--------EKQKELAETE--PKFNSVKEKEERGIARLaqATQERTD 374
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEdqlkiitmELQKKSSELEemTKFKNNKEVELEELKKI--LAEDEKL 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 375 LYAKQgrgsQFTSKEERDKWIKKELKSLDQAindKKRQIAAIHKDLEDTEANKEKNLEQYKldqdlnEVKARVEELDRKY 454
Cdd:pfam05483 421 LDEKK----QFEKIAEELKGKEQELIFLLQA---REKEIHDLEIQLTAIKTSEEHYLKEVE------DLKTELEKEKLKN 487
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 38566257 455 YEVKNKKDELQSERNYLWREENAEQQALAAKREDLE--KKQQ 494
Cdd:pfam05483 488 IELTAHCDKLLLENKELTQEASDMTLELKKHQEDIIncKKQE 529
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
791-1005 |
5.28e-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: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 791 EDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNEnLRKRLDQVEQELNELRETeggtvLTATTSELEAINK 870
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-LARRIRALEQELAALEAE-----LAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 871 RVKDTMARSEDLDNSIDKT-EAGIKELQKSMERWKNMEK--EHMDAIN-HDTKELEKMTNRQGMLLKKKEECMKKIRELG 946
Cdd:COG4942 98 ELEAQKEELAELLRALYRLgRQPPLALLLSPEDFLDAVRrlQYLKYLApARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38566257 947 SLPQEAFEKYQTLSLKQLFRK--LEQCNTELKKYshvnKKALDQFVNFSEQKEKLIKRQEE 1005
Cdd:COG4942 178 ALLAELEEERAALEALKAERQklLARLEKELAEL----AAELAELQQEAEELEALIARLEA 234
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
167-364 |
5.34e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 167 VYDERKEESISLMKETEGKREKINELLKYIEERLHTLEE-------EKEELAQYQKWDKM-RRALEYTIYNQELNETRAK 238
Cdd:PHA02562 221 KYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKlntaaakIKSKIEQFQKVIKMyEKGGVCPTCTQQISEGPDR 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 239 LDELSAKRETSGEKSRQLrdaqQDARDKMEDIERQVRELKTKISAMkeeKEQLSAERQeqikQRTKLELKAKDLQDELag 318
Cdd:PHA02562 301 ITKIKDKLKELQHSLEKL----DTAIDELEEIMDEFNEQSKKLLEL---KNKISTNKQ----SLITLVDKAKKVKAAI-- 367
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 38566257 319 nseqrKRLLKERQKLLEKIEEKQKELAET-EPKFNSVKEKEERGIAR 364
Cdd:PHA02562 368 -----EELQAEFVDNAEELAKLQDELDKIvKTKSELVKEKYHRGIVT 409
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
155-373 |
5.46e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 155 RLKLLREVAGTRVYDE---RKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELaqyqkwDKMRRALEYtiynqe 231
Cdd:PRK05771 61 KLRSYLPKLNPLREEKkkvSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKEL------EQEIERLEP------ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 232 LNETRAKLDELSAKRETSGEKSRqlRDAQQDARDKMEDIERQVRELKTK-------ISAMKEEKEQLSAERQEQIKQRTK 304
Cdd:PRK05771 129 WGNFDLDLSLLLGFKYVSVFVGT--VPEDKLEELKLESDVENVEYISTDkgyvyvvVVVLKELSDEVEEELKKLGFERLE 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38566257 305 LELKaKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAE----TEPKFNSVKEKEErgiARLAQATQERT 373
Cdd:PRK05771 207 LEEE-GTPSELIREIKEELEEIEKERESLLEELKELAKKYLEellaLYEYLEIELERAE---ALSKFLKTDKT 275
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
696-1006 |
5.47e-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: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 696 NENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILsemKMLKEKRQQSEKTfmpkQRSLQSLEASLHAMESTRES 775
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIK---KQLSEKQKELEQN----NKKIKELEKQLNQLKSEISD 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 776 LKAELGTDLLSQlsledqkrvdaLNDEIRQLQQENRQLLNERIKLEGIITRVETYLNeNLRKRLDQVEQELNELRETegg 855
Cdd:TIGR04523 300 LNNQKEQDWNKE-----------LKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS-QLKKELTNSESENSEKQRE--- 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 856 tvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSM----ERWKNMEKEHmDAINHDTKELEKMTNRQGM- 930
Cdd:TIGR04523 365 --LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNqqkdEQIKKLQQEK-ELLEKEIERLKETIIKNNSe 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 931 ---LLKKKEECMKKIRELGSLPQEAFEKYQTLS---------LKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEK 998
Cdd:TIGR04523 442 ikdLTNQDSVKELIIKNLDNTRESLETQLKVLSrsinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
....*...
gi 38566257 999 LIKRQEEL 1006
Cdd:TIGR04523 522 LKEKIEKL 529
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
202-498 |
5.98e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 202 TLEEEKEELAQYQK----WDKMRRALEytiynQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVREL 277
Cdd:pfam01576 357 ALEELTEQLEQAKRnkanLEKAKQALE-----SENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAEL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 278 KTKISAMKEEKEQLSAE----------------------------RQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKE 329
Cdd:pfam01576 432 AEKLSKLQSELESVSSLlneaegkniklskdvsslesqlqdtqelLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEA 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 330 RQKLLEKIEEKQKELAETEPK---FNSVKEKEERGIARLAQATQERTDLYAKqgRGSQFTSKEERDKWIKKELKSLDQAI 406
Cdd:pfam01576 512 KRNVERQLSTLQAQLSDMKKKleeDAGTLEALEEGKKRLQRELEALTQQLEE--KAAAYDKLEKTKNRLQQELDDLLVDL 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 407 nDKKRQIAaihkdledteANKEKnlEQYKLDQDLNEVKA----RVEELDRKYYEVKNKKDELQSernyLWREENAEQQAl 482
Cdd:pfam01576 590 -DHQRQLV----------SNLEK--KQKKFDQMLAEEKAisarYAEERDRAEAEAREKETRALS----LARALEEALEA- 651
|
330
....*....|....*.
gi 38566257 483 aakREDLEKKQQLLRA 498
Cdd:pfam01576 652 ---KEELERTNKQLRA 664
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
254-335 |
6.00e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 40.74 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 254 RQLRDAQQDARDKMED------IERQVRELKtkiSAMKEEKEQLsAERQEQIKQRTK-------LELKAKDLQD------ 314
Cdd:pfam13779 489 RRLRAAQERLSEALERgasdeeIAKLMQELR---EALDDYMQAL-AEQAQQNPQDLQqpddpnaQEMTQQDLQRmldrie 564
|
90 100
....*....|....*....|...
gi 38566257 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 ... |
1112-1164 |
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 38566257 1112 QQLSGGQKSLVALALIFAIQKcdpaPFYLFDEIDQALDAQHRKAVSDMIMELA 1164
Cdd:cd03226 125 LSLSGGQKQRLAIAAALLSGK----DLLIFDEPTSGLDYKNMERVGELIRELA 173
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
215-406 |
6.09e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 40.62 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 215 KWDKMRRALEYTIYNQELN--------ETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVR----ELKTKIS 282
Cdd:PRK00106 25 KMKSAKEAAELTLLNAEQEavnlrgkaERDAEHIKKTAKRESKALKKELLLEAKEEARKYREEIEQEFKserqELKQIES 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 283 AMKEEKEQLSAERQEQIKQRTKLELKAKDLQDelagnseqRKRLLKERQKLLEKIEEKQKELAEtepKFNSVKEKEERGI 362
Cdd:PRK00106 105 RLTERATSLDRKDENLSSKEKTLESKEQSLTD--------KSKHIDEREEQVEKLEEQKKAELE---RVAALSQAEAREI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 38566257 363 ArLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAI 406
Cdd:PRK00106 174 I-LAETENKLTHEIATRIREAEREVKDRSDKMAKDLLAQAMQRL 216
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1112-1163 |
6.27e-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: 6.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 38566257 1112 QQLSGGQKSLVALALIFAiqkCDPApFYLFDEIDQALDAQHRKAVSDMIMEL 1163
Cdd:COG1123 141 HQLSGGQRQRVAIAMALA---LDPD-LLIADEPTTALDVTTQAEILDLLREL 188
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
284-433 |
6.52e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 40.62 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 284 MKEEKEQ-----LSAErQEQIKQRTKLELKAkdlqdELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKE 358
Cdd:PRK00106 26 MKSAKEAaeltlLNAE-QEAVNLRGKAERDA-----EHIKKTAKRESKALKKELLLEAKEEARKYREEIEQEFKSERQEL 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38566257 359 ERGIARLAQ--ATQERTDlyakqgrgSQFTSKEerdkwikKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQ 433
Cdd:PRK00106 100 KQIESRLTEraTSLDRKD--------ENLSSKE-------KTLESKEQSLTDKSKHIDEREEQVEKLEEQKKAELER 161
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
191-299 |
6.58e-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: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 191 ELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEytiYNQELNETRAKLDELSAKretsGEKSRQLRDAQQDARDKMEDI 270
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEASFERLAE---LRDELAELEEELEALKAR----WEAEKELIEEIQELKEELEQR 483
|
90 100
....*....|....*....|....*....
gi 38566257 271 ERQVRELKTKISAMKEEKEQLSAERQEQI 299
Cdd:COG0542 484 YGKIPELEKELAELEEELAELAPLLREEV 512
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
206-466 |
6.64e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.45 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 206 EKEELAQYQKwdKMRRALeytiynqelnetrakLDELSAKRETSGEKSRQLRDAQqdarDKMEDIERQVRELKTKISAMK 285
Cdd:PRK11637 58 AKEKSVRQQQ--QQRASL---------------LAQLKKQEEAISQASRKLRETQ----NTLNQLNKQIDELNASIAKLE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 286 EEK--------EQL-SAERQeqiKQRTKLELKakdlqdeLAGNSEQRK-RLL-------KERQKLLEKIEEKQKELAETE 348
Cdd:PRK11637 117 QQQaaqerllaAQLdAAFRQ---GEHTGLQLI-------LSGEESQRGeRILayfgylnQARQETIAELKQTREELAAQK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 349 pkfnsvKEKEERgiarlaqATQERTDLYAKQGRGSQFT-SKEERdkwiKKELKSLDQAINDKKRQIAAIHKD---LEDTE 424
Cdd:PRK11637 187 ------AELEEK-------QSQQKTLLYEQQAQQQKLEqARNER----KKTLTGLESSLQKDQQQLSELRANesrLRDSI 249
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 38566257 425 ANKEKnleqykldqdlnEVKARVEELDRKYYEVKNKKDELQS 466
Cdd:PRK11637 250 ARAER------------EAKARAEREAREAARVRDKQKQAKR 279
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1111-1160 |
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 38566257 1111 MQQLSGGQKSLVALALIFaIQKCDpapFYLFDEIDQALDAQHRKAVSDMI 1160
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 38566257 192 LLKYIEERLHTLEEEKEELAQYQK-WDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQL--RDAQQDAR-DKM 267
Cdd:PRK12705 21 LVVLLKKRQRLAKEAERILQEAQKeAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLvqKEEQLDARaEKL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 268 EDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLElkakdlqdelagNSEQRKRLLKERQKLLEkiEEKQKELAET 347
Cdd:PRK12705 101 DNLENQLEEREKALSARELELEELEKQLDNELYRVAGLT------------PEQARKLLLKLLDAELE--EEKAQRVKKI 166
|
170 180
....*....|....*....|...
gi 38566257 348 EPKFNSVKEKEERGIarLAQATQ 370
Cdd:PRK12705 167 EEEADLEAERKAQNI--LAQAMQ 187
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
233-494 |
7.01e-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: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 233 NETRAKLDELSAKRETSGEKSRQLRDAQQDARD----------KMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQR 302
Cdd:pfam15905 52 TARKVKSLELKKKSQKNLKESKDQKELEKEIRAlvqergeqdkRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 303 TKLELKAKDLQDELAGNSEQRK--RLLKERQKLLEKIEEKQKELA----ETEPKFNSVKEKEERGIARLAQATQERTDLY 376
Cdd:pfam15905 132 LELTRVNELLKAKFSEDGTQKKmsSLSMELMKLRNKLEAKMKEVMakqeGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 377 AKqgrgsQFTSKEERDKWIK--KELKSLDQAINDKKRQIAAIHKDLEdtEANKEKNLEQYKLDQDLNEVKARVEELDRKY 454
Cdd:pfam15905 212 KE-----KIEEKSETEKLLEyiTELSCVSEQVEKYKLDIAQLEELLK--EKNDEIESLKQSLEEKEQELSKQIKDLNEKC 284
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 38566257 455 YEVKNKKDELQSERNYLWREENAE----QQALAAKREDLEKKQQ 494
Cdd:pfam15905 285 KLLESEKEELLREYEEKEQTLNAEleelKEKLTLEEQEHQKLQQ 328
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1109-1164 |
7.06e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.56 E-value: 7.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 38566257 1109 REMQQLSGG--QKSLVALALIfaiqkcDPAPFYLFDEIDQALDAQHRKAVSDMIMELA 1164
Cdd:PRK13409 208 RDISELSGGelQRVAIAAALL------RDADFYFFDEPTSYLDIRQRLNVARLIRELA 259
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
180-442 |
7.92e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.49 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 180 KETEGKREKInELLKYIEERLHTLEEEKEELAQYQKwdKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDA 259
Cdd:pfam05557 21 MELEHKRARI-ELEKKASALKRQLDRESDRNQELQK--RIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKES 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 260 QQ-DARDKMEDIERQVRELKTKIsamkeEKEQLSAERQEQIKQRTKLELkakDLQDELAGNSEQRKRLLKERQKLLEKIE 338
Cdd:pfam05557 98 QLaDAREVISCLKNELSELRRQI-----QRAELELQSTNSELEELQERL---DLLKAKASEAEQLRQNLEKQQSSLAEAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 339 EKQKELaetepkfnsvkekeERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHK 418
Cdd:pfam05557 170 QRIKEL--------------EFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKR 235
|
250 260
....*....|....*....|....*...
gi 38566257 419 DLEDTEANKEK----NLEQYKLDQDLNE 442
Cdd:pfam05557 236 KLEREEKYREEaatlELEKEKLEQELQS 263
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
669-883 |
8.18e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 8.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 669 DTRKSRLELQKDVRKAEEELGELEAKLNENLRRN-IERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQ 747
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEFRQKNgLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 748 SEKT--FMPKQRSLQSLEASLHAMESTRESLKAELGtdllsqlslEDQKRVDALNDEI----RQLQQENRQLLNE-RIKL 820
Cdd:COG3206 252 GPDAlpELLQSPVIQQLRAQLAELEAELAELSARYT---------PNHPDVIALRAQIaalrAQLQQEAQRILASlEAEL 322
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38566257 821 EGIITRVETylnenLRKRLDQVEQELNELRETEggTVLTATTSELEAINKRVKDTMARSEDLD 883
Cdd:COG3206 323 EALQAREAS-----LQAQLAQLEARLAELPELE--AELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
833-1024 |
8.35e-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: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 833 ENLRKRLDQVEQELNELRETEggtvlTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMD 912
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEE-----KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 913 AINHDTKELEKMTNRQG-MLLKKKEECMKKIRELGSLpqeafeKYQTLSLKQLFRKLEQCNTELKKyshVNKKALDQFVN 991
Cdd:COG4942 105 ELAELLRALYRLGRQPPlALLLSPEDFLDAVRRLQYL------KYLAPARREQAEELRADLAELAA---LRAELEAERAE 175
|
170 180 190
....*....|....*....|....*....|...
gi 38566257 992 FSEQKEKLIKRQEELDRGYKSIMELMNVLELRK 1024
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
732-819 |
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 38566257 732 DSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENR 811
Cdd:smart00935 7 QKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQ 86
|
....*...
gi 38566257 812 QLLNERIK 819
Cdd:smart00935 87 KRQQEELQ 94
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
139-366 |
8.68e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 139 VKQGKINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINEllKYIEERLHTLEEEKEELAQYQKWDK 218
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE--KKAAEALKKEAEEAKKAEELKKKEA 1712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 219 mrraleytiynqelnETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRElKTKISAMKEEKEQLSAERQEQ 298
Cdd:PTZ00121 1713 ---------------EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKIAHLKKEEEKKAEEIRKE 1776
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38566257 299 IKQRTKLELKAKDLQDELagnseQRKRLLKERQKLLEKIEEKQKelaETEPKFNSVKEKEERGIARLA 366
Cdd:PTZ00121 1777 KEAVIEEELDEEDEKRRM-----EVDKKIKDIFDNFANIIEGGK---EGNLVINDSKEMEDSAIKEVA 1836
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
247-345 |
8.68e-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: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 247 ETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKD-------LQDELAGN 319
Cdd:pfam06785 79 ELDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEEqlaekqlLINEYQQT 158
|
90 100
....*....|....*....|....*.
gi 38566257 320 SEQRKRLLKERQKLLEKIEEKQKELA 345
Cdd:pfam06785 159 IEEQRSVLEKRQDQIENLESKVRDLN 184
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
193-297 |
8.70e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 40.05 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 193 LKYIEERLHTLEE------EKEELAQYQKWDKMRRALEytiynqelnetrAKLDELSAKRETSGEKSRQLRDAQQDARDK 266
Cdd:PRK05431 4 IKLIRENPEAVKEalakrgFPLDVDELLELDEERRELQ------------TELEELQAERNALSKEIGQAKRKGEDAEAL 71
|
90 100 110
....*....|....*....|....*....|.
gi 38566257 267 MEdierQVRELKTKISAMKEEKEQLSAERQE 297
Cdd:PRK05431 72 IA----EVKELKEEIKALEAELDELEAELEE 98
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
154-385 |
8.80e-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: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 154 QRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQ------------------YQK 215
Cdd:TIGR00618 643 LKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQcqtllrelethieeydreFNE 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 216 WDKMRRALEYTI------YNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIErqvRELKTKISAMkEEKE 289
Cdd:TIGR00618 723 IENASSSLGSDLaaredaLNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLA---AEIQFFNRLR-EEDT 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 290 QLSAERQEQIKQRTKLELKAKDLQDE-LAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEergiarlAQA 368
Cdd:TIGR00618 799 HLLKTLEAEIGQEIPSDEDILNLQCEtLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQ-------AKI 871
|
250
....*....|....*..
gi 38566257 369 TQERTDLYAKQGRGSQF 385
Cdd:TIGR00618 872 IQLSDKLNGINQIKIQF 888
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1109-1171 |
8.83e-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: 8.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38566257 1109 REMQQLSGGQKSLVALALIFAIQkcdpaPFYL-FDEIDQALDAQHRKAVSDMIMELavHAQFIT 1171
Cdd:COG1122 130 RPPHELSGGQKQRVAIAGVLAME-----PEVLvLDEPTAGLDPRGRRELLELLKRL--NKEGKT 186
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
130-500 |
8.94e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.55 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 130 FSRSnpyYIVKQGKINQMATAPDSQRLKLLREVAGT--------RVYDERKEESISLMK---ETEGKREKINELLKYIEE 198
Cdd:PRK10246 147 FTRS---MLLSQGQFAAFLNAKPKERAELLEELTGTeiygqisaMVFEQHKSARTELEKlqaQASGVALLTPEQVQSLTA 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 199 RLHTL-EEEKEELAQYQkwdkmrraleytIYNQELNE-TRakLDELSAKRETSGEKSRQLRDAQQDARDKMEDIE----- 271
Cdd:PRK10246 224 SLQVLtDEEKQLLTAQQ------------QQQQSLNWlTR--LDELQQEASRRQQALQQALAAEEKAQPQLAALSlaqpa 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 272 RQVRELKTKIsamkEEKEQLSAERQEQIKqrtklELKAKdLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEpKF 351
Cdd:PRK10246 290 RQLRPHWERI----QEQSAALAHTRQQIE-----EVNTR-LQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHD-RF 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38566257 352 NSVKEKEERGIARLAQATQERTDLYAKQGRgsqftskeerdkwikkeLKSLDQaindKKRQIAAIHKDL--EDTEANKEK 429
Cdd:PRK10246 359 RQWNNELAGWRAQFSQQTSDREQLRQWQQQ-----------------LTHAEQ----KLNALPAITLTLtaDEVAAALAQ 417
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38566257 430 NLEQYKLDQDLNEVKARVEELDRKyyevknkKDELQSERNYLWREENAEQQALAAKREDL-EKKQQLLRAAT 500
Cdd:PRK10246 418 HAEQRPLRQRLVALHGQIVPQQKR-------LAQLQVAIQNVTQEQTQRNAALNEMRQRYkEKTQQLADVKT 482
|
|
| |
