|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-1219 |
3.96e-103 |
|
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: 353.99 E-value: 3.96e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 3 LKRLEIENFKSYRGHQVVGPFNAFTAVIGPNGSGKSNLMDAISFVLGVRSA-QLRSSQLKDLIFRGRkmgraddqdddda 81
Cdd:TIGR02169 2 IERIELENFKSFGKKKVIPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSkAMRAERLSDLISNGK------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 82 sgsddddlGEGTASKASVTAIY--EDGK-GYEHRFQRSITIAGNSEYRY---NGRAIQYAQYNTKLEQFNILVKAKNFlV 155
Cdd:TIGR02169 69 --------NGQSGNEAYVTVTFknDDGKfPDELEVVRRLKVTDDGKYSYyylNGQRVRLSEIHDFLAAAGIYPEGYNV-V 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 156 FQGDVEAVASQGAKELSRLIDQISGSLELKDDYERAKQAQERATDNSTFNFNKRRGINSELKQFREQKSEAEKFERLQQE 235
Cdd:TIGR02169 140 LQGDVTDFISMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 236 RvqhilnhilwrlfhinQDIElntdfVKTQAKNMRPLRTEHKKAEDAVLRARRDQGQTQTEILQVEKSIKSKQRDVEDLr 315
Cdd:TIGR02169 220 K----------------REYE-----GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 316 ptldayEEKIaisRKKLDNGARmteQVERDLAKQQANLAKLERDRETVQRAADRAAQEQQRALESAGLTLSEAD-----L 390
Cdd:TIGR02169 278 ------NKKI---KDLGEEEQL---RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEelereI 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 391 GEYHNLKAQ-----ANLEAVAE--RQELDGLKRDARIKADAVKDFQDKSEQFSKQKDKLKDEESTLSERHSALEAKRNQI 463
Cdd:TIGR02169 346 EEERKRRDKlteeyAELKEELEdlRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADL 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 464 DTDLQAARDELK----RTQAKQTAINQRETKLNDTLQV----------CYNKLLQAGNDLKEVEREAAMKETIAK----- 524
Cdd:TIGR02169 426 NAAIAGIEAKINeleeEKEDKALEIKKQEWKLEQLAADlskyeqelydLKEEYDRVEKELSKLQRELAEAEAQARaseer 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 525 ----------LQRIFPGVRGRVVDLCKpVQRKYDTAISTVLGRNTDAIIVDQEKTAIDCIEYLRNTRSGQATFLPLDRIQ 594
Cdd:TIGR02169 506 vrggraveevLKASIQGVHGTVAQLGS-VGERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMR 584
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 595 AKPINDRLRSIARGARLAVDVIHFDASIERAIHHACGNALVCDTMDIARSVVydkkVEAKAVTLEGTIIHKSGLIT---G 671
Cdd:TIGR02169 585 DERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVEDIEAARRLM----GKYRMVTLEGELFEKSGAMTggsR 660
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 672 GQSSSSGGKRWEEREVQ-------GLTTQRDKCLAELKELQKE-KRAFVSDDEMVAKITRLEADLRSAQDELAAVNTRLT 743
Cdd:TIGR02169 661 APRGGILFSRSEPAELQrlrerleGLKRELSSLQSELRRIENRlDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 744 GIRDELKNIDKQTKEIQPKLRTAKNELNQLQRQMSTLETVVNRAEDRIFATFCRRIGvDNIREYEERQVRLMERQSDArl 823
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQ-AELSKLEEEVSRIEARLREI-- 817
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 824 qfESQLARLNHQANFERQQIESTQERLETIRQAIARENEKLRSWQAQKQGKQEELEgmleevsELQAQLSELqtqnEAKK 903
Cdd:TIGR02169 818 --EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE-------ELEAALRDL----ESRL 884
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 904 VTLEEKRVELQKAARLLDSLSKEIAARNDEIEGLGSERasiyrrcrleEITLPLLKGSLAKVGLEETIDVDAPMDIdddd 983
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL----------KAKLEALEEELSEIEDPKGEDEEIPEEE---- 950
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 984 ntqkpLSAPDfgiqvdfsslddeakedggasmgneLQTRIESITAEIEKMSP-NMKAVERLDDTEAKLAETEKEFDRSRR 1062
Cdd:TIGR02169 951 -----LSLED-------------------------VQAELQRVEEEIRALEPvNMLAIQEYEEVLKRLDELKEKRAKLEE 1000
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1063 QAKEARDEFNRIKKRRCDLFNSAFNHISKMIDPTYKDLSrskaapmGGSAYLSIENTEEPYLGGITYSVVPPMKRFRDIT 1142
Cdd:TIGR02169 1001 ERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAELS-------GGTGELILENPDDPFAGGLELSAKPKGKPVQRLE 1073
|
1210 1220 1230 1240 1250 1260 1270
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2528757163 1143 ALSGGEKTMAALALLFAIHSFQPAPFFVLDEVDAALDSQNVAKVSNYIRQHASDQfQFIVISLKASLYERSQSLVGI 1219
Cdd:TIGR02169 1074 AMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEA-QFIVVSLRSPMIEYADRAIGV 1149
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
3-1224 |
2.19e-94 |
|
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: 328.85 E-value: 2.19e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 3 LKRLEIENFKSYrGHQVVGPFN-AFTAVIGPNGSGKSNLMDAISFVLGVRSA-QLRSSQLKDLIFRGrkmgraddqdddd 80
Cdd:pfam02463 2 LKRIEIEGFKSY-AKTVILPFSpGFTAIVGPNGSGKSNILDAILFVLGERSAkSLRSERLSDLIHSK------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 81 asgsddddlGEGTASKASVTAIYEDGKGYEHRFQRSITIA------GNSEYRYNGRAIQYAQYNTKLEQFNILVKAKNFL 154
Cdd:pfam02463 68 ---------SGAFVNSAEVEITFDNEDHELPIDKEEVSIRrrvyrgGDSEYYINGKNVTKKEVAELLESQGISPEAYNFL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 155 VFQGDVEAVASQGAKELSRLIDQISGSLELKDDYERAKQAQERATDNSTFNFNKRRGINSELKQFREQKSEAEKFERLQQ 234
Cdd:pfam02463 139 VQGGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 235 ERVQHILNHILWRLFH-INQDIELNTDFVKTQAKNMRPLRTEHKKAEDAVLR------ARRDQGQTQTEILQVEKSIKSK 307
Cdd:pfam02463 219 LELEEEYLLYLDYLKLnEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVlkenkeEEKEKKLQEEELKLLAKEEEEL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 308 QRDVEDLRPTLDAYEEKIAISRKKLDNGARMTEQVERDLAKQQANLAKLERDRETVQRAADRAAQEQQRALESAGLTLSE 387
Cdd:pfam02463 299 KSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 388 ADLGEYHNLKAQANLEAVAERQELDGLKRDARIKADAVKDFQDKSEQFSKQKDKLKDEESTLSERHSALEAKRNQidtDL 467
Cdd:pfam02463 379 KKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEEL---EK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 468 QAARDELKRTQAKQTAINQRETKLNdTLQVCYNKLLQAGNDLKEVEREAAMKETIAKLQRIFPGVRGRVVDLCKPVQRKY 547
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQLV-KLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDL 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 548 DTAISTVLGRNTDAIIVDQEKTAIDCIEYLRNTRSGQATFLPLDRIQAKPINDRLRSIARGARLAVDVIHFDASIERAIH 627
Cdd:pfam02463 535 GVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLE 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 628 HACGNALVCDTMDIARSVVYDKKVEAKAVTLEGTIIHKSGLItggqssssggkrwEEREVQGLTTQRDKCLAELKELQKE 707
Cdd:pfam02463 615 ADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEE-------------GLAEKSEVKASLSELTKELLEIQEL 681
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 708 KRAFVSDdEMVAKITRLEADLRSAQDELAAVNTRLTGIRDELKNIDKQTKEIQPKLRTAKNELNQLQRQMstletvvnra 787
Cdd:pfam02463 682 QEKAESE-LAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEE---------- 750
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 788 edrifatfcrrigvdnirEYEERQVRLMERQSDARLQFESQLARLNHQANFERQQIESTQERLETIRQAIARENEKLRSW 867
Cdd:pfam02463 751 ------------------EEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKE 812
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 868 QAQKQGKQEELEGMLEEVSELQAQLSELQTQNEAKKVTLEEKRVELQKAARLLDSLSKEIAARNDEIEGLGSERASIYRR 947
Cdd:pfam02463 813 EAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKE 892
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 948 CRLEEITLPLLKGSLAKVGLEETIDVDAPMDIDDDDNTQKPLSAPdfgiqVDFSSLDDEAKEDGGASMGNELQTRIESIT 1027
Cdd:pfam02463 893 EKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEP-----EELLLEEADEKEKEENNKEEEEERNKRLLL 967
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1028 AEIEKMSPNMKAVERLDDTEAKLAETEKEFDRSRRQAKEARDEFNRIKKRRCDLFNSAFNHISKMIDPTYKDLSrskaap 1107
Cdd:pfam02463 968 AKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLE------ 1041
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1108 MGGSAYLSIENTEEPYLGGITYSVVPPMKRFRDITALSGGEKTMAALALLFAIHSFQPAPFFVLDEVDAALDSQNVAKVS 1187
Cdd:pfam02463 1042 LGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVA 1121
|
1210 1220 1230
....*....|....*....|....*....|....*..
gi 2528757163 1188 NYIRQHaSDQFQFIVISLKASLYERSQSLVGIYRDQD 1224
Cdd:pfam02463 1122 NLLKEL-SKNAQFIVISLREEMLEKADKLVGVTMVEN 1157
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-1219 |
3.02e-91 |
|
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: 320.08 E-value: 3.02e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 3 LKRLEIENFKSYrGHQVVGPFNA-FTAVIGPNGSGKSNLMDAISFVLGVRSA-QLRSSQLKDLIFRGRKMGRAddqdddd 80
Cdd:TIGR02168 2 LKKLELAGFKSF-ADPTTINFDKgITGIVGPNGCGKSNIVDAIRWVLGEQSAkALRGGKMEDVIFNGSETRKP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 81 asgsddddlgegtASKASVTAIYEDGKGYEHRFQ-------RSITIAGNSEYRYNG-----RAIQYAQYNTKLEqfnilv 148
Cdd:TIGR02168 74 -------------LSLAEVELVFDNSDGLLPGADyseisitRRLYRDGESEYFINGqpcrlKDIQDLFLDTGLG------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 149 kaKNFL--VFQGDVEAVASQGAKELSRLIDQISGSLELKddyERAKQAQ---ERATDNSTFNFNKRRGINSELKQFREQK 223
Cdd:TIGR02168 135 --KRSYsiIEQGKISEIIEAKPEERRAIFEEAAGISKYK---ERRKETErklERTRENLDRLEDILNELERQLKSLERQA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 224 SEAEKFERLQQERVQHilnhilwrlfhinqDIELNTDFVKTQAKNMRPLRTEHKKAEDAVLRARRDQGQTQTEILQVEKS 303
Cdd:TIGR02168 210 EKAERYKELKAELREL--------------ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 304 IKSKQRDVEDLRPTLDAYEEKIAISRKKLDNGARMTEQVERDLAKQQANLAKLERDRETVQRAADRAAQEQQRALESagL 383
Cdd:TIGR02168 276 VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE--L 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 384 TLSEADLGEYHNLKAQANLEAVAERQELDGLKRDARIKADAVKDFQDKSEQFSKQKDKLKDEESTLSERHSAL-----EA 458
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELlkkleEA 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 459 KRNQIDTDLQAARDELKRTQAKQTAINQRETKLNDTLQVCYNKLLQAGNDLKEVEREAAMKETI--------------AK 524
Cdd:TIGR02168 434 ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLqenlegfsegvkalLK 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 525 LQRIFPGVRGRVVDLCKpVQRKYDTAISTVLGRNTDAIIVDQEKTAIDCIEYLRNTRSGQATFLPLDRIQAKPIN----D 600
Cdd:TIGR02168 514 NQSGLSGILGVLSELIS-VDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQgndrE 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 601 RLRSIARGARLAVDVIHFDASIERAIHHACGNALVCDTMDIARSVVYDKKVEAKAVTLEGTIIHKSGLITGgqssssggk 680
Cdd:TIGR02168 593 ILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITG--------- 663
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 681 rwEEREVQGLTTQRDKclaELKELQKEKRAFVSD-DEMVAKITRLEADLRSAQDELAAVNTRLTGIRDELKNIDKQTKEI 759
Cdd:TIGR02168 664 --GSAKTNSSILERRR---EIEELEEKIEELEEKiAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 760 QPKLRTAKNELNQLQRQMSTLETVVNRAEDRIFATFCRRIGVDNIREYEERQVrlmERQSDARLQFESQLARLNHQANFE 839
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI---EQLKEELKALREALDELRAELTLL 815
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 840 RQQIESTQERLETIRQAIARENEKLRSWQAQKQGKQEELEGMLEEVSELQAQLSELQTQneakkvtLEEKRVELQKAARL 919
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE-------LEALLNERASLEEA 888
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 920 LDSLSKEIAARNDEIEGLGSERASIYRrcRLEEITLPLLKGSLAKVGLEETIDvdapmdiddddNTQKPLSApDFGIQVD 999
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRR--ELEELREKLAQLELRLEGLEVRID-----------NLQERLSE-EYSLTLE 954
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1000 fsslDDEAKEDGGASMGNELQTRIESITAEIEKMSP-NMKAVERLDDTEAKLAETEKEFD---RSRRQAKEARDEFNRIK 1075
Cdd:TIGR02168 955 ----EAEALENKIEDDEEEARRRLKRLENKIKELGPvNLAAIEEYEELKERYDFLTAQKEdltEAKETLEEAIEEIDREA 1030
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1076 KRRcdlFNSAFNHISKMIDPTYKDLSRskaapmGGSAYLSIENTEEPYLGGITYSVVPPMKRFRDITALSGGEKTMAALA 1155
Cdd:TIGR02168 1031 RER---FKDTFDQVNENFQRVFPKLFG------GGEAELRLTDPEDLLEAGIEIFAQPPGKKNQNLSLLSGGEKALTALA 1101
|
1210 1220 1230 1240 1250 1260
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2528757163 1156 LLFAIHSFQPAPFFVLDEVDAALDSQNVAKVSNYIRqHASDQFQFIVISLKASLYERSQSLVGI 1219
Cdd:TIGR02168 1102 LLFAIFKVKPAPFCILDEVDAPLDDANVERFANLLK-EFSKNTQFIVITHNKGTMEVADQLYGV 1164
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
3-180 |
1.72e-70 |
|
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: 235.93 E-value: 1.72e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 3 LKRLEIENFKSYRGHQVVGPFNAFTAVIGPNGSGKSNLMDAISFVLGVRSAQLRSSQLKDLIFRGRkmgraddqddddas 82
Cdd:cd03275 1 LKRLELENFKSYKGRHVIGPFDRFTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYRAR-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 83 gsddddLGEGTASKASVTAIYEDGKGYEHRFQRSITIAGnSEYRYNGRAIQYAQYNTKLEQFNILVKAKNFLVFQGDVEA 162
Cdd:cd03275 67 ------VGKPDSNSAYVTAVYEDDDGEEKTFRRIITGGS-SSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVES 139
|
170 180
....*....|....*....|
gi 2528757163 163 VASQGA--KELsRLIDQISG 180
Cdd:cd03275 140 IASKNPpgKRF-RDMDNLSG 158
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1133-1235 |
1.84e-62 |
|
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: 213.20 E-value: 1.84e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1133 PPMKRFRDITALSGGEKTMAALALLFAIHSFQPAPFFVLDEVDAALDSQNVAKVSNYIRQHASDQFQFIVISLKASLYER 1212
Cdd:cd03275 145 PPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGPNFQFIVISLKEEFFSK 224
|
90 100
....*....|....*....|...
gi 2528757163 1213 SQSLVGIYRDQDVNSSSSLTLDL 1235
Cdd:cd03275 225 ADALVGVYRDQECNSSKVLTLDL 247
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-1219 |
2.44e-56 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 212.87 E-value: 2.44e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1 MPLKRLEIENFKSYRGHQVVgPFNA-FTAVIGPNGSGKSNLMDAISFVLGVRSA-QLRSSQLKDLIFRG---RKmgradd 75
Cdd:COG1196 1 MRLKRLELAGFKSFADPTTI-PFEPgITAIVGPNGSGKSNIVDAIRWVLGEQSAkSLRGGKMEDVIFAGsssRK------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 76 qddddasgsddddlgegTASKASVTAIYEDGKGYEHRFQRSITIA------GNSEYRYNGRA-----IQ--YAQYNTKLE 142
Cdd:COG1196 74 -----------------PLGRAEVSLTFDNSDGTLPIDYDEVTITrrlyrsGESEYYINGKPcrlkdIQdlFLDTGLGPE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 143 QFNIlvkaknflVFQGDVEAVASQGAKELSRLIDQISGSLELKddyERAKQAQ----------ERATDnstfnfnKRRGI 212
Cdd:COG1196 137 SYSI--------IGQGMIDRIIEAKPEERRAIIEEAAGISKYK---ERKEEAErkleateenlERLED-------ILGEL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 213 NSELKQFREQKSEAEKFERLQQERVQHILNHILWRLFHINQDI--------ELNTDFVKTQA------KNMRPLRTEHKK 278
Cdd:COG1196 199 ERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELeeleaeleELEAELEELEAelaeleAELEELRLELEE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 279 AEDAVLRARRDQGQTQTEILQVEKSIKSKQRDVEDLRPTLDAYEEKIAISRKKLDNGARMTEQVERDLAKQQANLAKLER 358
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 359 DRETVQRAADRAAQEQQRALESAgLTLSEADLGEYHNLKAQANLEAVAERQELDGLKRDARIKAdAVKDFQDKSEQFSKQ 438
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEEL-EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE-ELEELEEALAELEEE 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 439 KDKLKDEESTLSERHSALEAKRNQIDTDLQAARDELKRTQAKQTAINQREtklndtlqvcyNKLLQAGNDLKEVEREAAM 518
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL-----------AEAAARLLLLLEAEADYEG 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 519 KETIAKLQRIFPGVRG--RVVDLCKPVQRKYDTAISTVLGRNTDAIIVDQEKTAIDCIEYLRNTRSGQATFLPLDRIQAK 596
Cdd:COG1196 506 FLEGVKAALLLAGLRGlaGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRAR 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 597 PINDRLRSIARGARlAVDVIHFDASIERAIHHACGNALVCDTMDIARsvvydkkveakavtlegtiihksglitggqsss 676
Cdd:COG1196 586 AALAAALARGAIGA-AVDLVASDLREADARYYVLGDTLLGRTLVAAR--------------------------------- 631
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 677 sggkrweerevqglttqrdkclaelkelqkekrafvsDDEMVAKITRLEADLRSAQDELAAVNTRLTGIRDELKNIDKQt 756
Cdd:COG1196 632 -------------------------------------LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA- 673
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 757 keiqpklrtaknelnqlqrqmstletvvnraedrifatfcrrigvdnireyEERQVRLMERQSDARLQfesqlarlnhqa 836
Cdd:COG1196 674 ---------------------------------------------------LLEAEAELEELAERLAE------------ 690
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 837 nfERQQIESTQERLETIRQAIARENEKLRSWQAQKQGKQEELEGMLEEVSELQAQLSELQTQNEAKKVTLEEKRvelqka 916
Cdd:COG1196 691 --EELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL------ 762
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 917 arlldslskeiaarndeieglgserasiyrrcrleeitlpllkgslakvgleetidvdapmdiddddntqkplsapdfgi 996
Cdd:COG1196 --------------------------------------------------------------------------------
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 997 qvdfsslddeakedggasmgNELQTRIESITAEIEKMSP-NMKAVERLDDTEAKLAETEKEFD---RSRRQAKEARDEFN 1072
Cdd:COG1196 763 --------------------EELERELERLEREIEALGPvNLLAIEEYEELEERYDFLSEQREdleEARETLEEAIEEID 822
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1073 RIKKRRcdlFNSAFNHISKMIDPTYKDLSRskaapmGGSAYLSIENTEEPYLGGITYSVVPPMKRFRDITALSGGEKTMA 1152
Cdd:COG1196 823 RETRER---FLETFDAVNENFQELFPRLFG------GGEAELLLTDPDDPLETGIEIMAQPPGKKLQRLSLLSGGEKALT 893
|
1210 1220 1230 1240 1250 1260
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2528757163 1153 ALALLFAIHSFQPAPFFVLDEVDAALDSQNVAKVSNYIRQHaSDQFQFIVISLKASLYERSQSLVGI 1219
Cdd:COG1196 894 ALALLFAIFRLNPSPFCVLDEVDAPLDDANVERFAELLKEM-SEDTQFIVITHNKRTMEAADRLYGV 959
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
530-645 |
1.71e-33 |
|
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: 125.42 E-value: 1.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 530 PGVRGRVVDLCKpVQRKYDTAISTVLGRNTDAIIVDQEKTAIDCIEYLRNTRSGQATFLPLDRIQAKPI-----NDRLRS 604
Cdd:smart00968 1 PGVLGRVADLIS-VDPKYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPRSPagsklREALLP 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2528757163 605 IARGARLAVDVIHFDASIERAIHHACGNALVCDTMDIARSV 645
Cdd:smart00968 80 EPGFVGPAIDLVEYDPELRPALEYLLGNTLVVDDLETARRL 120
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
529-646 |
1.07e-30 |
|
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: 117.36 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 529 FPGVRGRVVDLCKpVQRKYDTAISTVLGRNTDAIIVDQEKTAIDCIEYLRNTRSGQATFLPLDRIQAKPINDRLRSIArG 608
Cdd:pfam06470 1 LKGVLGRLADLIE-VDEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRLKPRPRRPGADLKG-G 78
|
90 100 110
....*....|....*....|....*....|....*...
gi 2528757163 609 ARLAVDVIHFDASIERAIHHACGNALVCDTMDIARSVV 646
Cdd:pfam06470 79 AGPLLDLVEYDDEYRKALRYLLGNTLVVDDLDEALELA 116
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1134-1228 |
1.95e-30 |
|
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: 120.09 E-value: 1.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1134 PMKRFRDITALSGGEKTMAALALLFAIHSFQPAPFFVLDEVDAALDSQNVAKVSNYIRQHASDQfQFIVISLKASLYERS 1213
Cdd:cd03274 118 PKKSWKNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNA-QFIVISLRNNMFELA 196
|
90
....*....|....*
gi 2528757163 1214 QSLVGIYRDQDVNSS 1228
Cdd:cd03274 197 DRLVGIYKTNNCTKS 211
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1134-1219 |
3.06e-29 |
|
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: 116.03 E-value: 3.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1134 PMKRFRDITALSGGEKTMAALALLFAIHSFQPAPFFVLDEVDAALDSQNVAKVSNYIRQhASDQFQFIVISLKASLYERS 1213
Cdd:cd03278 104 PGKKVQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKE-FSKETQFIVITHRKGTMEAA 182
|
....*.
gi 2528757163 1214 QSLVGI 1219
Cdd:cd03278 183 DRLYGV 188
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1098-1225 |
5.26e-27 |
|
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: 108.93 E-value: 5.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1098 KDLSRSKAAPMGGSAYLSIENTEepylggiTYSVVPP--MKRFrditaLSGGEKTMAALALLFAIHSFQPAPFFVLDEVD 1175
Cdd:cd03239 59 LFLAGGGVKAGINSASVEITFDK-------SYFLVLQgkVEQI-----LSGGEKSLSALALIFALQEIKPSPFYVLDEID 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1176 AALDSQNVAKVSNYIRQHASDQFQFIVISLKASLYERSQSLVGIYRDQDV 1225
Cdd:cd03239 127 AALDPTNRRRVSDMIKEMAKHTSQFIVITLKKEMFENADKLIGVLFVHGV 176
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
3-64 |
3.33e-22 |
|
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: 96.21 E-value: 3.33e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2528757163 3 LKRLEIENFKSYRGHQVVGPFNA-FTAVIGPNGSGKSNLMDAISFVLGVRSAQLRSSQLKDLI 64
Cdd:cd03274 3 ITKLVLENFKSYAGEQVIGPFHKsFSAIVGPNGSGKSNVIDSMLFVFGFRASKMRQKKLSDLI 65
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-63 |
1.05e-21 |
|
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: 93.53 E-value: 1.05e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2528757163 3 LKRLEIENFKSYRGHQVVGPFNAFTAVIGPNGSGKSNLMDAISFVLGVRSAQLRSSQLKDL 63
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFL 61
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
3-69 |
4.07e-21 |
|
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: 92.53 E-value: 4.07e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2528757163 3 LKRLEIENFKSYRGHQVVgPFNA-FTAVIGPNGSGKSNLMDAISFVLGVRSA-QLRSSQLKDLIFRGRK 69
Cdd:cd03278 1 LKKLELKGFKSFADKTTI-PFPPgLTAIVGPNGSGKSNIIDAIRWVLGEQSAkSLRGEKMSDVIFAGSE 68
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1144-1221 |
9.38e-21 |
|
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: 90.50 E-value: 9.38e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2528757163 1144 LSGGEKTMAALALLFAIHSFQPAPFFVLDEVDAALDSQNVAKVSNYIRQHASDQFQFIVISLKASLYERSQSLVGIYR 1221
Cdd:cd03227 78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIKK 155
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-172 |
2.01e-20 |
|
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: 91.98 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1 MPLKRLEIENFKSYRGHQVVGPFNA-FTAVIGPNGSGKSNLMDAISFVLGVRS-AQLRSSQLKDLIFRGRKMGRaddqdd 78
Cdd:cd03273 1 MHIKEIILDGFKSYATRTVISGFDPqFNAITGLNGSGKSNILDAICFVLGITNlSTVRASNLQDLIYKRGQAGI------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 79 ddasgsddddlgegtaSKASVTAIY--EDGKGYEHRFQ--------RSITIAGNSEYRYNGRAIQyaqyNTKLEQF---- 144
Cdd:cd03273 75 ----------------TKASVTIVFdnSDKSQSPIGFEnypeitvtRQIVLGGTNKYLINGHRAQ----QQRVQDLfqsv 134
|
170 180 190
....*....|....*....|....*....|....
gi 2528757163 145 NILVKAKNFLVFQGDVEAVASQGAK------ELS 172
Cdd:cd03273 135 QLNVNNPHFLIMQGRITKVLNMGGVwkesltELS 168
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
262-947 |
5.61e-18 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 89.97 E-value: 5.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 262 VKTQAKNMRPLRTEHKKAEDAVLRARR-DQGQTQTEILQVEKSIKSKQRDVEDLRPTLDAYEEKIAISRKKLDNGARMTE 340
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAElEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 341 QVERDLAKQQ-ANLAKLERDRETVQRAAD---RAAQEQQRALESAGLTLsEADLGEYHNLKAQANLEAVAERQELDGLkR 416
Cdd:COG4913 327 ELEAQIRGNGgDRLEQLEREIERLERELEereRRRARLEALLAALGLPL-PASAEEFAALRAEAAALLEALEEELEAL-E 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 417 DARIKADAvkdfqdkseqfskQKDKLKDEESTLSERHSALEAKRNQIDTDLQAARDELKRtqakqtAINQRETKLN---D 493
Cdd:COG4913 405 EALAEAEA-------------ALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAE------ALGLDEAELPfvgE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 494 TLQVcynkllqagndlkevereaamketiaklqrifpgvrgrvvdlcKPVQRKYDTAISTVLGRNTDAIIVDQEKTAiDC 573
Cdd:COG4913 466 LIEV-------------------------------------------RPEEERWRGAIERVLGGFALTLLVPPEHYA-AA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 574 IEYLRNTR-SGQATFLPLDRIQAKPINDRL--RSIARgaRLAVDVIHF----DASIERAIHHACgnalvCDTMDiarsvv 646
Cdd:COG4913 502 LRWVNRLHlRGRLVYERVRTGLPDPERPRLdpDSLAG--KLDFKPHPFrawlEAELGRRFDYVC-----VDSPE------ 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 647 yDKKVEAKAVTLEGTiIHKSGLITGGQSSSSGGKRW------------EEREVQGLTTQRDKCLAELKELQKEKRAFVSD 714
Cdd:COG4913 569 -ELRRHPRAITRAGQ-VKGNGTRHEKDDRRRIRSRYvlgfdnraklaaLEAELAELEEELAEAEERLEALEAELDALQER 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 715 DEMVAKITRL---EADLRSAQDELAAVNTRLTGIR---DELKNIDKQTKEIQPKLRTAKNELNQLQRQMSTLETVVNRAE 788
Cdd:COG4913 647 REALQRLAEYswdEIDVASAEREIAELEAELERLDassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 789 DRifatfcrrigvdnIREYEERQVRLMERQSDA-RLQFESQLARLNhQANFERQQIESTQERLETIRQAIARENEKLRsw 867
Cdd:COG4913 727 EE-------------LDELQDRLEAAEDLARLElRALLEERFAAAL-GDAVERELRENLEERIDALRARLNRAEEELE-- 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 868 QAQKQGKQE------ELEGMLEEVSELQAQLSELQTQNeakkvtLEEKRvelQKAARLLDSLSKE-IAARNDEIEglgSE 940
Cdd:COG4913 791 RAMRAFNREwpaetaDLDADLESLPEYLALLDRLEEDG------LPEYE---ERFKELLNENSIEfVADLLSKLR---RA 858
|
....*..
gi 2528757163 941 RASIYRR 947
Cdd:COG4913 859 IREIKER 865
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1139-1202 |
5.88e-16 |
|
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: 78.84 E-value: 5.88e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2528757163 1139 RDITALSGGEKTMAALALLFAIHSFQPAPFFVLDEVDAALDSQNVAKVSNYIRQhASDQFQFIV 1202
Cdd:cd03272 154 QEMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKE-LSDGAQFIT 216
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1141-1232 |
1.65e-15 |
|
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: 77.72 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1141 ITALSGGEKTMAALALLFAIHSFQPAPFFVLDEVDAALDSQNVAKVSNYIRQHASDQfQFIVISLKASLYERSQSLvgiY 1220
Cdd:cd03273 164 LTELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGS-QFIVVSLKEGMFNNANVL---F 239
|
90
....*....|..
gi 2528757163 1221 RDQDVNSSSSLT 1232
Cdd:cd03273 240 RTRFVDGTSTVT 251
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
719-943 |
1.54e-13 |
|
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: 74.03 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 719 AKITRLEADLRSAQDELAAVNTRLTGIRDELKNIDKQTKEIQPKLRTAKNELNQLQRQMSTLETVVNRAEDRIFATfcrR 798
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL---R 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 799 IGVDNIREYEERQVRLMERQ-----------SDARLQFESQLARLNHQANFERQQIE---STQERLETIRQAIARENEKL 864
Cdd:COG4942 97 AELEAQKEELAELLRALYRLgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEelrADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2528757163 865 RSWQAQKQGKQEELEgmlEEVSELQAQLSELQTQNEAKKVTLEEKRVELQKAARLLDSLSKEIAARNDEIEGLGSERAS 943
Cdd:COG4942 177 EALLAELEEERAALE---ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
3-69 |
8.20e-12 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 68.42 E-value: 8.20e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2528757163 3 LKRLEIENFKSYRghQVVGPFNAFTAVIGPNGSGKSNLMDAISFV-----LGVRSAQLRSSQLKDLIFRGRK 69
Cdd:COG4637 2 ITRIRIKNFKSLR--DLELPLGPLTVLIGANGSGKSNLLDALRFLsdaarGGLQDALARRGGLEELLWRGPR 71
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
5-58 |
1.60e-11 |
|
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: 63.92 E-value: 1.60e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2528757163 5 RLEIENFKSYRGHQVVGPFNA-FTAVIGPNGSGKSNLMDAISFVLGVRSAQLRSS 58
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTFGEGsLTIITGPNGSGKSTILDAIGLALGGAQSATRRR 55
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-67 |
4.70e-10 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 62.87 E-value: 4.70e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2528757163 1 MPLKRLEIENFKSYRgHQVVGPFNAFTAVIGPNGSGKSNLMDAISFV-LGvRSaqLRSSQLKDLIFRG 67
Cdd:PRK00064 1 MYLTRLSLTDFRNYE-ELDLELSPGVNVLVGENGQGKTNLLEAIYLLaPG-RS--HRTARDKELIRFG 64
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1121-1222 |
1.06e-09 |
|
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: 58.41 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1121 EPYLGGITYSVVPPMKRFRDITA---LSGGEKTMAALALLFAihsfQPAPFFVLDEVDAALDSQNVAKVSNYIRQHASDQ 1197
Cdd:cd00267 55 EILIDGKDIAKLPLEELRRRIGYvpqLSGGQRQRVALARALL----LNPDLLLLDEPTSGLDPASRERLLELLRELAEEG 130
|
90 100
....*....|....*....|....*
gi 2528757163 1198 FQFIVISLKASLYERSQSLVGIYRD 1222
Cdd:cd00267 131 RTVIIVTHDPELAELAADRVIVLKD 155
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
3-67 |
1.97e-09 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 60.94 E-value: 1.97e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2528757163 3 LKRLEIENFKSYRgHQVVGPFNAFTAVIGPNGSGKSNLMDAISFVLGVRSaqLRSSQLKDLIFRG 67
Cdd:COG1195 2 LKRLSLTNFRNYE-SLELEFSPGINVLVGPNGQGKTNLLEAIYLLATGRS--FRTARDAELIRFG 63
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
3-72 |
2.42e-09 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 58.48 E-value: 2.42e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2528757163 3 LKRLEIENFKSYRGHQVVgPFNA-FTAVIGPNGSGKSNLMDAISFVLGVRSAQlRSSQLKDLIFRGRKMGR 72
Cdd:COG0419 2 LLRLRLENFRSYRDTETI-DFDDgLNLIVGPNGAGKSTILEAIRYALYGKARS-RSKLRSDLINVGSEEAS 70
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-923 |
3.54e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 61.52 E-value: 3.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1 MPLKRLEIENFKSYRGHQVV--GPFNAFTAVIGPNGSGKSNLMDAISFVLGvrsaqlrssqlkdlifrgRKMGRaddqdd 78
Cdd:TIGR00618 1 MKPLRLTLKNFGSYKGTHTIdfTALGPIFLICGKTGAGKTTLLDAITYALY------------------GKLPR------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 79 ddasgsddddLGEGTASKASVTAIYEDGKGYEHRFqrsitIAGNSEYRYNgRAIQYAQYNTKL-EQFNILVKAKNFLvfq 157
Cdd:TIGR00618 57 ----------RSEVIRSLNSLYAAPSEAAFAELEF-----SLGTKIYRVH-RTLRCTRSHRKTeQPEQLYLEQKKGR--- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 158 gdvEAVASQGAKELSRLIDQISGsLELK-------------DDYERAKQAQERATDNSTFNFNKRRGINSELkqfREQKS 224
Cdd:TIGR00618 118 ---GRILAAKKSETEEVIHDLLK-LDYKtftrvvllpqgefAQFLKAKSKEKKELLMNLFPLDQYTQLALME---FAKKK 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 225 EAEKFERLQQERVQhILNHILwrlfhiNQDIELNTDFVKTQAKNMRPLRTEHKKAEDAVLRARRDQgQTQTEILQVEKSI 304
Cdd:TIGR00618 191 SLHGKAELLTLRSQ-LLTLCT------PCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR-EAQEEQLKKQQLL 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 305 KSKQRDVEDLRPTLDAYE---EKIAISRKK---LDNGARMTE---QVERDLAKQQANLAKLERDRETVQR-AADRAAQEQ 374
Cdd:TIGR00618 263 KQLRARIEELRAQEAVLEetqERINRARKAaplAAHIKAVTQieqQAQRIHTELQSKMRSRAKLLMKRAAhVKQQSSIEE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 375 QRALESAgltlseadLGEYHNLKAQANLEAVAERQELDGLKRDA-RIKADA--VKDFQDKSEQFSKQKDKLKDEESTLSE 451
Cdd:TIGR00618 343 QRRLLQT--------LHSQEIHIRDAHEVATSIREISCQQHTLTqHIHTLQqqKTTLTQKLQSLCKELDILQREQATIDT 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 452 RHSAleakRNQIDTDLQAARDELKRTQAKQTAINQRETKLNDTLQVCYNKLLQAGNDLKEVEREAAMKETIAKLQRIFPG 531
Cdd:TIGR00618 415 RTSA----FRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKA 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 532 VRGRVVDLCKPVQRKYDTAISTVLGRNTDAIIVDQEKTAIDCIEYlrnTRSGQATFLPLDRIQAKPINDRLRSIARGARL 611
Cdd:TIGR00618 491 VVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQ---TYAQLETSEEDVYHQLTSERKQRASLKEQMQE 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 612 AVDVIHFDASieraihhaCGNALVCDtMDIARSVV------YDKKVEAKAVTLEGTIIHKSGL--ITGGQSSSSGGKRWE 683
Cdd:TIGR00618 568 IQQSFSILTQ--------CDNRSKED-IPNLQNITvrlqdlTEKLSEAEDMLACEQHALLRKLqpEQDLQDVRLHLQQCS 638
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 684 EREVQGLTTQRDKCLAELKELQKEKRAFVSDDEMvAKITRLEADLRSAQ----------DELAAVNTRLTGIRDELKNID 753
Cdd:TIGR00618 639 QELALKLTALHALQLTLTQERVREHALSIRVLPK-ELLASRQLALQKMQsekeqltywkEMLAQCQTLLRELETHIEEYD 717
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 754 KQTKEIQPKLRTAKNELNQlqrQMSTLETVVNRAEdRIFATFCRRIGVDNIREYEERQVRLMerqsdaRLQFESQLARLN 833
Cdd:TIGR00618 718 REFNEIENASSSLGSDLAA---REDALNQSLKELM-HQARTVLKARTEAHFNNNEEVTAALQ------TGAELSHLAAEI 787
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 834 HQANFERQQ-IESTQERLETIRQAIARENEKLRSWQAQKQGKQEELEGMLEEVSELQAQLSELQTQNEAKKVTLEEKRVE 912
Cdd:TIGR00618 788 QFFNRLREEdTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQE 867
|
970
....*....|.
gi 2528757163 913 LQKAARLLDSL 923
Cdd:TIGR00618 868 QAKIIQLSDKL 878
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
3-68 |
3.69e-09 |
|
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: 58.81 E-value: 3.69e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2528757163 3 LKRLEIENFKSYRGHQVVGPFNAFTAVI-GPNGSGKSNLMDAISFVLGVRSAQLRSSQLKDLIFRGR 68
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEPFSPKHNVVvGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALLHEGS 67
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-52 |
3.71e-09 |
|
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: 60.02 E-value: 3.71e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2528757163 1 MPLKRLEIENFKSYRGHQVvgPFNA-FTAVIGPNGSGKSNLMDAISFVLGVRS 52
Cdd:COG3593 1 MKLEKIKIKNFRSIKDLSI--ELSDdLTVLVGENNSGKSSILEALRLLLGPSS 51
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
279-537 |
5.31e-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: 59.78 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 279 AEDAVLRARRDQGQTQTEILQVEKSIKSKQRDVEDLRPTLDAYEEKIAISRKKLDNGARMTEQVERDLAKQQANLAKLER 358
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 359 DRETVQRAADRAAQEQQRALESAGLTLSEADLGEYHNLKAQANLEAVAE--RQELDGLKRDArikadavKDFQDKSEQFS 436
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAParREQAEELRADL-------AELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 437 KQKDKLKDEESTLSERHSALEAKRNQIDTDLQAARDELKRTQAKQTAINQRETKLNDTLQvcynKLLQAGNDLKEVEREA 516
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA----RLEAEAAAAAERTPAA 246
|
250 260
....*....|....*....|.
gi 2528757163 517 AMKETIAKLqrIFPgVRGRVV 537
Cdd:COG4942 247 GFAALKGKL--PWP-VSGRVV 264
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-71 |
5.42e-09 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 58.86 E-value: 5.42e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2528757163 1 MPLKRLEIENFKSYRGHQVvgPFNA---FTAVIGPNGSGKSNLMDAISFVLGVRSAQLRSSQLKDLIFRGRKMG 71
Cdd:COG3950 1 MRIKSLTIENFRGFEDLEI--DFDNpprLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNGEFG 72
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
3-48 |
1.58e-08 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 52.22 E-value: 1.58e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2528757163 3 LKRLEIENFKSYRGHQVVGPFNAFTAVIGPNGSGKSNLMDAISFVL 48
Cdd:pfam13555 1 LTRLQLINWGTFDGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLL 46
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
699-952 |
1.82e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 699 AELKELQKEKRAFVSDDEMVAKITRLEADLRSAQ-----DELAAVNTRLTGIRDELKNIDKQTKEIQPKLRTAKNELNQL 773
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEAREAVEDRREEieeleEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 774 QRQMSTLETVVNRAEDRIFATFCRRIG--------VDNIREYEERQVRLMERQSDARLQ---FESQLARLNHQANFERQq 842
Cdd:PRK02224 432 EATLRTARERVEEAEALLEAGKCPECGqpvegsphVETIEEDRERVEELEAELEDLEEEveeVEERLERAEDLVEAEDR- 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 843 IESTQERLETIRQAIAReneklrswqaqkqgKQEELEGMLEEVSELQAQLSELQTQNEAKKVTLEEKRVELQKAARLLDS 922
Cdd:PRK02224 511 IERLEERREDLEELIAE--------------RRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
250 260 270
....*....|....*....|....*....|
gi 2528757163 923 LSKEIAARNDEIEGLGSERASIYRRCRLEE 952
Cdd:PRK02224 577 LNSKLAELKERIESLERIRTLLAAIADAED 606
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
720-945 |
1.96e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.92 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 720 KITRLEADLRSAQDELAAVNTRLTGIRDELKNIDKQTKEIQPKLRTAKNELNQLQRQMSTLETVVNRAEDRIfatfcrri 799
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 800 gvdnireyeERQVRLMERQSDARLQFE---------------SQLARLNHQANFERQQIESTQERLETIRQAIARENEKL 864
Cdd:COG3883 89 ---------GERARALYRSGGSVSYLDvllgsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 865 RSWQAQKQGKQEELEGMLEEVSELQAQLSELQTQNEAKKVTLEEKRVELQKAARLLDSLSKEIAARNDEIEGLGSERASI 944
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
.
gi 2528757163 945 Y 945
Cdd:COG3883 240 A 240
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
725-947 |
2.20e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.92 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 725 EADLRSAQDELAAVNTRLTGIRDELKNIDKQTKEIQPKLRTAKNELNQLQRQMSTLETVVNRAEDRIfatfcrrigvdni 804
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 805 reyEERQVRLMERqsdARLQFESQLARLNHQANFERQQIESTQERLETIRQAIARENEKLRSWQAQKqgkqEELEGMLEE 884
Cdd:COG3883 82 ---EERREELGER---ARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADK----AELEAKKAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2528757163 885 VSELQAQLSELQTQNEAKKVTLEEKRVELQKaarLLDSLSKEIAARNDEIEGLGSERASIYRR 947
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEA---LLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
3-65 |
4.82e-08 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 56.21 E-value: 4.82e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2528757163 3 LKRLEIENFKSYRGHQV---------VGPFNAftaVIGPNGSGKSNLMDAISFvlgVRSAQLRSSQLKDLIF 65
Cdd:COG1106 2 LISFSIENFRSFKDELTlsmvasglrLLRVNL---IYGANASGKSNLLEALYF---LRNLVLNSSQPGDKLV 67
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-913 |
1.91e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1 MPLKRLEIENFKSYRGHQVvgPFN-AFTAVIGPNGSGKSNLMDAISFVL-GVRSAQLRSSQLKDLIFRGrkmgraddqdd 78
Cdd:PRK03918 1 MKIEELKIKNFRSHKSSVV--EFDdGINLIIGQNGSGKSSILEAILVGLyWGHGSKPKGLKKDDFTRIG----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 79 ddasgsddddlgegtASKASVTAIYE-DGKGYehRFQRSITiAGNSEYRYNGRAI-------QYAQYNTKLEQFNILVKA 150
Cdd:PRK03918 68 ---------------GSGTEIELKFEkNGRKY--RIVRSFN-RGESYLKYLDGSEvleegdsSVREWVERLIPYHVFLNA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 151 knFLVFQGDVEA-VASQGAKElsRLIDQISGSlelkDDYERA-KQAQERATdnstfNFNKRRginSELKQFREQKSEAEK 228
Cdd:PRK03918 130 --IYIRQGEIDAiLESDESRE--KVVRQILGL----DDYENAyKNLGEVIK-----EIKRRI---ERLEKFIKRTENIEE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 229 FERLQQERVQHILNHILwRLFHINQDIELNTDFVKTQAKNMRPLRTEHKKAEDAVLRARRDQGQTQTEILQVEKSIKSKQ 308
Cdd:PRK03918 194 LIKEKEKELEEVLREIN-EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 309 RDVEDLR------PTLDAYEEKIAISRKKLDNgarmTEQVERDLAKQqanLAKLERDRETVQRAADRAAQEQQRALESAG 382
Cdd:PRK03918 273 KEIEELEekvkelKELKEKAEEYIKLSEFYEE----YLDELREIEKR---LSRLEEEINGIEERIKELEEKEERLEELKK 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 383 LTlsEADLGEYHNLKAQANL--EAVAERQELDGLKrdARIKADAVKDFQDKSEQFSKQKDKLKDEESTLSERHSALEAKR 460
Cdd:PRK03918 346 KL--KELEKRLEELEERHELyeEAKAKKEELERLK--KRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEI 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 461 NqidtDLQAARDELKRTQAKqtainqretklndtLQVCynkllqaGNDLKEVEREAAMKETIAKLQRIfpgvrgrvvdlc 540
Cdd:PRK03918 422 K----ELKKAIEELKKAKGK--------------CPVC-------GRELTEEHRKELLEEYTAELKRI------------ 464
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 541 kpvqrkydtaistvlgRNTDAIIVDQEKTAIDCIEYLRNTRSGQATFLPLDRI--QAKPINDRLRSIargarlavdvihf 618
Cdd:PRK03918 465 ----------------EKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKELEEKLKKY------------- 515
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 619 dasieraihhacgnalvcDTMDIARSVVYDKKVEAKAVTLEGTIihkSGLITGGQSSSSGGKRWEErevqgLTTQRDKCL 698
Cdd:PRK03918 516 ------------------NLEELEKKAEEYEKLKEKLIKLKGEI---KSLKKELEKLEELKKKLAE-----LEKKLDELE 569
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 699 AELKELQKE--KRAFVSDDEMVAKITRLEA------DLRSAQDELAAVNTRLTGIRDELKNIDKQTKEIQPKLRTAKNEL 770
Cdd:PRK03918 570 EELAELLKEleELGFESVEELEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL 649
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 771 NQLQRQMStletvvnraedrifatfcrrigVDNIREYEERQVRLMERQSDARLQFES------QLARLNHQANFERQQIE 844
Cdd:PRK03918 650 EELEKKYS----------------------EEEYEELREEYLELSRELAGLRAELEElekrreEIKKTLEKLKEELEERE 707
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2528757163 845 STQERLETIRQAIAREnEKLRswQAQKQGKQEELEGMLEEVSELQAQLSELQTQNEAKKVTL--EEKRVEL 913
Cdd:PRK03918 708 KAKKELEKLEKALERV-EELR--EKVKKYKALLKERALSKVGEIASEIFEELTEGKYSGVRVkaEENKVKL 775
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
684-1076 |
3.11e-07 |
|
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: 55.03 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 684 EREVQGLTTQRDKCLAELKELQKEKrafvsdDEMVAKITRLEADLRSAQDELAAVNTR-----LTGIRDELKNIDKQTKE 758
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLSEKQKEL------EQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEE 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 759 IQPKLRTAKNELNQLQRQMSTLETVVNRAEDrifatfcrrigvdnirEYEERQVRLMERQSDARlqfesQLARLNHQANF 838
Cdd:TIGR04523 326 IQNQISQNNKIISQLNEQISQLKKELTNSES----------------ENSEKQRELEEKQNEIE-----KLKKENQSYKQ 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 839 ERQQIESTQERLETIRQAIAREN----EKLRSWQAQKQGKQEELEGMLEEVSELQAQLSELQTQNEAKKVT---LEEKRV 911
Cdd:TIGR04523 385 EIKNLESQINDLESKIQNQEKLNqqkdEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIiknLDNTRE 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 912 ELQKAarlLDSLSKEIAARNDEIEGLGSErasiyrrcrLEEITLPLLKGSLAKVGLEETIDvDAPMDIDDDDNTQKPLSA 991
Cdd:TIGR04523 465 SLETQ---LKVLSRSINKIKQNLEQKQKE---------LKSKEKELKKLNEEKKELEEKVK-DLTKKISSLKEKIEKLES 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 992 PDFGIQVDFSSLDDEAKEDGGASMGNELQTRIESITAEIEKM--------SPNMKAVERLDDTEAKLAETEKEFDRSRRQ 1063
Cdd:TIGR04523 532 EKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELkqtqkslkKKQEEKQELIDQKEKEKKDLIKEIEEKEKK 611
|
410
....*....|...
gi 2528757163 1064 AKEARDEFNRIKK 1076
Cdd:TIGR04523 612 ISSLEKELEKAKK 624
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
721-914 |
3.44e-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: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 721 ITRLEADLRSAQDELAA--VNTRLTGIRDELKNIDKQTKEIQPKLRTAKNELNQLQRQMSTLETVVNRAEDRIFATfcrr 798
Cdd:COG3206 184 LPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL---- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 799 IGVDNIREYEERQVRLMERQSDARLQFES---QLARLNHQANFERQQIestQERLETIRQAIARENEKLRSWQAQKQGKQ 875
Cdd:COG3206 260 LQSPVIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQIAALRAQL---QQEAQRILASLEAELEALQAREASLQAQL 336
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2528757163 876 EELEGMLEEVSELQAQLSELQTQNEAKK---VTLEEKRVELQ 914
Cdd:COG3206 337 AQLEARLAELPELEAELRRLEREVEVARelyESLLQRLEEAR 378
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
403-937 |
3.85e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 403 EAVAERQELDGLKR---DARIKADAVKDFQDKSEQFSKQKDKLKDEESTLSE-RHSALEAKRNQIDTDLQAARDELKRTQ 478
Cdd:COG4913 229 ALVEHFDDLERAHEaleDAREQIELLEPIRELAERYAAARERLAELEYLRAAlRLWFAQRRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 479 AKQTAINQRETKLNDTLQVCYNKLLQAGND-LKEVERE-AAMKETIAKLQRifpgVRGRVVDLCKPVQRKYDTAISTVLG 556
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRGNGGDrLEQLEREiERLERELEERER----RRARLEALLAALGLPLPASAEEFAA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 557 RNTDAiivDQEKTAIDCI-EYLRNTRSGQATFLPLDRIQAKPINDRLRSIARG------------ARLA----------- 612
Cdd:COG4913 385 LRAEA---AALLEALEEElEALEEALAEAEAALRDLRRELRELEAEIASLERRksniparllalrDALAealgldeaelp 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 613 -----VDVIHFDA----SIERAIHhacGNAL--------------VCDTMDIARSVVYDkKVEAKAVTLEGTIIHKSGLI 669
Cdd:COG4913 462 fvgelIEVRPEEErwrgAIERVLG---GFALtllvppehyaaalrWVNRLHLRGRLVYE-RVRTGLPDPERPRLDPDSLA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 670 TGGQSSSSGGKRWEEREVQGlttQRD-KCLAELKELQKEKRAfVSDDEMVAKI-TRLEADLR-----------SAQDELA 736
Cdd:COG4913 538 GKLDFKPHPFRAWLEAELGR---RFDyVCVDSPEELRRHPRA-ITRAGQVKGNgTRHEKDDRrrirsryvlgfDNRAKLA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 737 AVNTRLTGIRDELKNIDKQtkeiqpkLRTAKNELNQLQRQMSTLETVVNRAEDRIfatfcrrigvdNIREYEERQVRLME 816
Cdd:COG4913 614 ALEAELAELEEELAEAEER-------LEALEAELDALQERREALQRLAEYSWDEI-----------DVASAEREIAELEA 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 817 RQSDARlQFESQLARLNHQANFERQQIESTQERLETIRQAIARENEKLRSWQAQKQGKQEELEGMLEEVSELQAQLSELQ 896
Cdd:COG4913 676 ELERLD-ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER 754
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2528757163 897 TQNEAKKVTLEEKRVELQKAarlLDSLSKEIAARNDEIEGL 937
Cdd:COG4913 755 FAAALGDAVERELRENLEER---IDALRARLNRAEEELERA 792
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
1-64 |
4.69e-07 |
|
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: 53.51 E-value: 4.69e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2528757163 1 MPLKRLEIENFKSYRghQVVGPFNA-FTAVIGPNGSGKSNLMDAISFVLGVRSaqLRSSQLKDLI 64
Cdd:TIGR00611 1 MYLSRLELTDFRNYD--AVDLELSPgVNVIVGPNGQGKTNLLEAIYYLALGRS--HRTSRDKPLI 61
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-48 |
6.35e-07 |
|
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: 51.45 E-value: 6.35e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2528757163 3 LKRLEIENFKSYRGHQVVGPFNAFTAVIGPNGSGKSNLMDAISFVL 48
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYAL 46
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
26-222 |
8.58e-07 |
|
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: 52.39 E-value: 8.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 26 FTAVIGPNGSGKSNLMDAISFVlgvrsAQLRSSQLKDLIFRGRKMGRADDQDDDDASGSDDddlgegtASKASVTAIYED 105
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFL-----ADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKE-------PIEFEISEFLED 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 106 GKGYEHRFQRSITIAGNSEYRYNgRAIQYAQYNTKLEQFNILVKAKNFLVFqGDVEAVASQGAKELSRLIDQISGSLELK 185
Cdd:pfam13304 69 GVRYRYGLDLEREDVEEKLSSKP-TLLEKRLLLREDSEEREPKFPPEAEEL-RLGLDVEERIELSLSELSDLISGLLLLS 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2528757163 186 DDYERAKQAQE----RATDNSTFNFNKRRGINSELKQFREQ 222
Cdd:pfam13304 147 IISPLSFLLLLdeglLLEDWAVLDLAADLALFPDLKELLQR 187
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
698-891 |
9.11e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 9.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 698 LAELKELQKEKRAFvsdDEMVAKITRLEADLRSAQDELAAVNTRLTGIRDELKNIDKQTkeiqpKLRTAKNELNQLQRQM 777
Cdd:COG4717 70 LKELKELEEELKEA---EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 778 STLETVVNRAEDRifatfcrrigvdnIREYEERQVRLmERQSDARLQFESQLARLNHQANFE-RQQIESTQERLETIRQA 856
Cdd:COG4717 142 AELPERLEELEER-------------LEELRELEEEL-EELEAELAELQEELEELLEQLSLAtEEELQDLAEELEELQQR 207
|
170 180 190
....*....|....*....|....*....|....*
gi 2528757163 857 IARENEKLRSWQAQKQGKQEELEGMLEEVSELQAQ 891
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
734-921 |
9.76e-07 |
|
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: 51.46 E-value: 9.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 734 ELAAVNTRLTGIRDELKNIDKQTKEIQPKLRTAKNELNQLQRQMSTLETVVNRAEDrifatfcrrigvdNIREYEERQVR 813
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLEL-------------EIEEVEARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 814 LMERQSDARLQFEsqLARLNHQanferqqIESTQERLETIRQAIARENEKLRSWQAQKQGKQEELEGMLEEVSELQAQLS 893
Cdd:COG1579 78 YEEQLGNVRNNKE--YEALQKE-------IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
170 180 190
....*....|....*....|....*....|
gi 2528757163 894 ELQTQNEAKKVTLEEKRVELQKA--ARLLD 921
Cdd:COG1579 149 EELAELEAELEELEAEREELAAKipPELLA 178
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-197 |
1.23e-06 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 50.19 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 6 LEIENFKSYRGHQVvgPFNA-FTAVIGPNGSGKSNLMDAISFVLGVRSAQLRSSQLKDLifrgrkmgraddqddddasGS 84
Cdd:pfam13476 1 LTIENFRSFRDQTI--DFSKgLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGF-------------------VK 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 85 DDDDLGEGTASKASVTAIYEDGKG-YEHRFQRSITIAGNSEYRYNGRAIQYAQYNTKLEQFNILVKAK----NFLVFQGD 159
Cdd:pfam13476 60 GDIRIGLEGKGKAYVEITFENNDGrYTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDkiilPLLVFLGQ 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2528757163 160 ------VEAVASQGAKELSRLIDQISGSLELKDDYERAKQAQER 197
Cdd:pfam13476 140 ereeefERKEKKERLEELEKALEEKEDEKKLLEKLLQLKEKKKE 183
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-497 |
1.29e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.98 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1 MPLKRLEIENFKSYRGHQVVGPfNAFTAVIGPNGSGKSNLMDAISFVLgvrSAQLRSSQLKDLIFRGRKmgraddqdddd 80
Cdd:PRK01156 1 MIIKRIRLKNFLSHDDSEIEFD-TGINIITGKNGAGKSSIVDAIRFAL---FTDKRTEKIEDMIKKGKN----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 81 asgsddddlgegtasKASVTAIYEDGkGYEHRFQRSIT-----IAGNSEYRYNGRAI-QYAQYNTKLEQFNILVKAKN-- 152
Cdd:PRK01156 66 ---------------NLEVELEFRIG-GHVYQIRRSIErrgkgSRREAYIKKDGSIIaEGFDDTTKYIEKNILGISKDvf 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 153 ---FLVFQGDVEAVASQGAKELSRLIDQISGSLELKDDYERAKQAQERATDN-STFNF--NKRRGINSELKQFREQKSEA 226
Cdd:PRK01156 130 lnsIFVGQGEMDSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEiSNIDYleEKLKSSNLELENIKKQIADD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 227 EKFERLQQERVQhilnhilwRLFHINQDIELNTDFVKTQAKNMRPLRTEHKKAEDAVlraRRDQGQTQTEILQVEKSIKS 306
Cdd:PRK01156 210 EKSHSITLKEIE--------RLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI---KTAESDLSMELEKNNYYKEL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 307 KQRDVEDLRPTLDAYEEKIA---ISRKKLDNGARMTEQVERDLAKQQANLAKLErdretvqraadraaqeqqralesagl 383
Cdd:PRK01156 279 EERHMKIINDPVYKNRNYINdyfKYKNDIENKKQILSNIDAEINKYHAIIKKLS-------------------------- 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 384 tLSEADLGEYHNLKAQANlEAVAERQELDGLKRDARIKADAVKDFQDKSEQFSKQKDKLKDEESTLSERH----SALEAK 459
Cdd:PRK01156 333 -VLQKDYNDYIKKKSRYD-DLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQeidpDAIKKE 410
|
490 500 510
....*....|....*....|....*....|....*...
gi 2528757163 460 RNQIDTDLQAARDELKRTQAKQTAINQRETKLNDTLQV 497
Cdd:PRK01156 411 LNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEM 448
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1136-1204 |
1.31e-06 |
|
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: 50.29 E-value: 1.31e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2528757163 1136 KRFRDITALSGGEKTMAALALLFAIHSFQPAPFFVLDEVDAALDSQNVAKVSNYIRQHASDQ--FQFIVIS 1204
Cdd:cd03276 102 AAVRDVKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAKKQpgRQFIFIT 172
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
723-929 |
1.71e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 723 RLEADLRSAQDELaavnTRLTGIRDELKNIDKQTKEIQPkLRTAKNELNQLQRQMSTLETVVNRAEDRiFATFCRRIGVD 802
Cdd:COG4913 222 DTFEAADALVEHF----DDLERAHEALEDAREQIELLEP-IRELAERYAAARERLAELEYLRAALRLW-FAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 803 NIREYEERQVRLMERQSDARLQFESQLARLNH------QANFER-----QQIESTQERLETIRQAIARENEKLRSWQAQK 871
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDEleaqirGNGGDRleqleREIERLERELEERERRRARLEALLAALGLPL 375
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2528757163 872 QGKQEELEGMLEEVSELQAQLSELQTQNEAKKVTLEEKRVELQKAarlLDSLSKEIAA 929
Cdd:COG4913 376 PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE---LRELEAEIAS 430
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
770-953 |
1.75e-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: 52.43 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 770 LNQLQRQMSTLETVVNRAEDRIFatfcRRIGVDNIREYEERQVRLMERQsdaRLQFESQLARlnhQANFERQ-QIESTQE 848
Cdd:pfam17380 271 LNQLLHIVQHQKAVSERQQQEKF----EKMEQERLRQEKEEKAREVERR---RKLEEAEKAR---QAEMDRQaAIYAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 849 RLETIRQaiaRENEKLRSWQAQK---QGKQEELEGMLEEVSELQAQLSELQTQNE--------AKKVTL--EEKRVELQK 915
Cdd:pfam17380 341 RMAMERE---RELERIRQEERKReleRIRQEEIAMEISRMRELERLQMERQQKNErvrqeleaARKVKIleEERQRKIQQ 417
|
170 180 190
....*....|....*....|....*....|....*....
gi 2528757163 916 AARLLDSLSKEIA-ARNDEIEGLGSERASIYRRCRLEEI 953
Cdd:pfam17380 418 QKVEMEQIRAEQEeARQREVRRLEEERAREMERVRLEEQ 456
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
5-71 |
3.23e-06 |
|
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: 49.52 E-value: 3.23e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2528757163 5 RLEIENFKSYrGHQVVGPFNAFTAVIGPNGSGKSNLMDAISFVLGVRSAQL-RSSQLKDLIFRGRKMG 71
Cdd:cd03277 5 RIKLENFVTY-DETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLGGKPKLLgRAKKVGEFVKRGCDEG 71
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
187-482 |
3.74e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.66 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 187 DYERAKQAQERATDNSTFNFNKRRG-INSELKQFREQKSEAEKFERLQQErvqhiLNHILWRLFHINQDIELntdfVKTQ 265
Cdd:pfam15921 500 DLTASLQEKERAIEATNAEITKLRSrVDLKLQELQHLKNEGDHLRNVQTE-----CEALKLQMAEKDKVIEI----LRQQ 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 266 AKNMRPLRTEHKkaedavlrarRDQGQTQTEILQVEKSIKSKQRDVEDLRPTLDAYEEKI----------AISRKKLDNG 335
Cdd:pfam15921 571 IENMTQLVGQHG----------RTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIrelearvsdlELEKVKLVNA 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 336 ARMTEQVERDLAKQQ-----------ANLAKLERDRETVQRAADRAAQEQ--------------QRALESAGLTLSEADL 390
Cdd:pfam15921 641 GSERLRAVKDIKQERdqllnevktsrNELNSLSEDYEVLKRNFRNKSEEMetttnklkmqlksaQSELEQTRNTLKSMEG 720
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 391 GEYHNLKAQANLEA--VAERQELDGLKRDARIKADAVKDFqdkseqfSKQKDKLKDEESTLSERHSALEAKRNQIDTDLQ 468
Cdd:pfam15921 721 SDGHAMKVAMGMQKqiTAKRGQIDALQSKIQFLEEAMTNA-------NKEKHFLKEEKNKLSQELSTVATEKNKMAGELE 793
|
330
....*....|....
gi 2528757163 469 AARDELKRTQAKQT 482
Cdd:pfam15921 794 VLRSQERRLKEKVA 807
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
353-516 |
4.02e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 50.86 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 353 LAKLERDRETVQRAADRAAQEQQRALESAGLTLSEADLGEYHnlkaQANLEAVAERQELdglKRDARIKADAVKDFQDKS 432
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERN----QQRQEARREREEL---QREEERLVQKEEQLDARA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 433 EQFSKQKDKLKDEESTLSERHSALEAKRNQIDTDLQAArDELKRTQAKQTAINQRETKLNDTLQVCYNKLLQAGNDlkEV 512
Cdd:PRK12705 98 EKLDNLENQLEEREKALSARELELEELEKQLDNELYRV-AGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADL--EA 174
|
....
gi 2528757163 513 EREA 516
Cdd:PRK12705 175 ERKA 178
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
724-940 |
4.29e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.78 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 724 LEADLRSAQDELAAVNTRLTGIRDELK-------NIDKQTKEIQPKLRtakNELNQLQRQMSTLETVVNRAEDRIFATfc 796
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQIKtynknieEQRKKNGENIARKQ---NKYDELVEEAKTIKAEIEELTDELLNL-- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 797 rrigVDNIREYEERQVRLmerqSDARLQFESQLARLNHQANFER---------QQIESTQERLETIRQAIARENEKLRsw 867
Cdd:PHA02562 247 ----VMDIEDPSAALNKL----NTAAAKIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRITKIKDKLKELQHSLE-- 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2528757163 868 qaQKQGKQEELEGMLEEVSELQAQLSELQTQNEAKKVTLEEKRVELQKAARLLDSLSKEIAARNDEIEGLGSE 940
Cdd:PHA02562 317 --KLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDE 387
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
748-937 |
5.29e-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: 49.15 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 748 ELKNIDKQTKEIQPKLRTAKNELNQLQRQMSTLETVVNRAEDRIfatfcrrigvdnireyeerqvrlmerqsdarLQFES 827
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTEL-------------------------------EDLEK 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 828 QLARLNHQANFERQQIESTQERLETIR-----QAIARENEKLRswQAQKQGKQEELEGMlEEVSELQAQLSELQTQNEAK 902
Cdd:COG1579 60 EIKRLELEIEEVEARIKKYEEQLGNVRnnkeyEALQKEIESLK--RRISDLEDEILELM-ERIEELEEELAELEAELAEL 136
|
170 180 190
....*....|....*....|....*....|....*
gi 2528757163 903 KVTLEEKRVELQKAarlLDSLSKEIAARNDEIEGL 937
Cdd:COG1579 137 EAELEEKKAELDEE---LAELEAELEELEAEREEL 168
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
720-943 |
6.60e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.40 E-value: 6.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 720 KITRLEADLRSAQDELAAVNTRLTGIRDELKNIDKQTKEIQPKLRTAKNELNQLQRQMSTLETVVNRAEDRIFATFCRRI 799
Cdd:TIGR04523 240 EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQ 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 800 gvdnireyeERQVRLMERQSDarlQFESQLARLNHQANFERQQIESTQERLETIRQAIARENEKLRSWQAQKQGKQEELE 879
Cdd:TIGR04523 320 ---------EKKLEEIQNQIS---QNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2528757163 880 GMLEEVSELQAQLSELQTQNEAKKVTLEEKRVELQKAARLLDSLSKEIAARNDEIEGLGSERAS 943
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV 451
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
215-927 |
1.17e-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: 50.05 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 215 ELKQFREQKSEAEKFERLQQERVQHILNHILWRLFHINQDIELNTDFVKTQAKNMRPLRTEHKKAEdavlrarrdqgQTQ 294
Cdd:TIGR00606 193 QVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIE-----------HNL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 295 TEILQVE---KSIKSKQRDVEDLRPTLDAYEEKIAISRKK-----LDNGARMTEQVERDLAKQQANLAKLERDRETVQra 366
Cdd:TIGR00606 262 SKIMKLDneiKALKSRKKQMEKDNSELELKMEKVFQGTDEqlndlYHNHQRTVREKERELVDCQRELEKLNKERRLLN-- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 367 adraaQEQQRALESAGLTLSEADLGEYHNLKAQANLEAVAERQELDGLKRDARIKADaVKDF--------QDKSEQFSKQ 438
Cdd:TIGR00606 340 -----QEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQ-IKNFhtlvierqEDEAKTAAQL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 439 KDKLKDEESTLSERHSALEAKRNQIDTDLQAARDELKRTQA----KQTAINQRETKLNDTLQVcYNKLLQAGNDLKEVER 514
Cdd:TIGR00606 414 CADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEelkfVIKELQQLEGSSDRILEL-DQELRKAERELSKAEK 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 515 EAAMKETIAKLQRIFPGVRGRVVDLCKPVQRKYDTAISTVLGRNTDAIIVDQektaIDCIEYLRNTRS-------GQATF 587
Cdd:TIGR00606 493 NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDK----MDKDEQIRKIKSrhsdeltSLLGY 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 588 LPLDRIQAKPINDRLRSIARGARLAVDVIHFDASIERAIHHACGNalvcdtmdiarsvvyDKKVEAKAVTLEGTIIHKSG 667
Cdd:TIGR00606 569 FPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNE---------------LESKEEQLSSYEDKLFDVCG 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 668 LITGGQSSSSGGKRWEEREVQ-----GLTTQRDKCLAELKELQKE-----KRAFVSDDEMVAKITRLEADLRSAQDELAA 737
Cdd:TIGR00606 634 SQDEESDLERLKEEIEKSSKQramlaGATAVYSQFITQLTDENQSccpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKS 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 738 VNTRLT--------------GIRDELKNIDKQTKEIQPKLRTAKNELNQLQRQMSTLETVVNRAEDRIFATFCRRIGVDN 803
Cdd:TIGR00606 714 TESELKkkekrrdemlglapGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTI 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 804 IREYEErQVRLMERQSdARLQFESQLARLNHQANFERQQIESTQERLETIRQAIarenEKLRSWQAQKQGKQEELEGMLE 883
Cdd:TIGR00606 794 MERFQM-ELKDVERKI-AQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKI----ELNRKLIQDQQEQIQHLKSKTN 867
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 2528757163 884 EVSELQAQLSELQTQNEAKKVTLEEKRVELQKAARLLDSLSKEI 927
Cdd:TIGR00606 868 ELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQD 911
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
696-942 |
1.20e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 49.30 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 696 KCLAELKELQKEKRAFVSDDEMVAKitrlEAD-LRSAQDELAAVN------TRLTGIRDELKNIDKqtkeIQPKLRTAKN 768
Cdd:COG0497 162 EAYRAWRALKKELEELRADEAERAR----ELDlLRFQLEELEAAAlqpgeeEELEEERRRLSNAEK----LREALQEALE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 769 ELNQLQrqmSTLETVVNRAEDRIfatfcrrigvDNIREYEERQVRLMERQSDARLQFE---SQLARLNHQANFERQQIES 845
Cdd:COG0497 234 ALSGGE---GGALDLLGQALRAL----------ERLAEYDPSLAELAERLESALIELEeaaSELRRYLDSLEFDPERLEE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 846 TQERLETIRQaIAR----ENEKLRSWQAQKQGKQEELEGMLEEVSELQAQLSELQTQ--NEAKKVTleEKRvelQKAARl 919
Cdd:COG0497 301 VEERLALLRR-LARkygvTVEELLAYAEELRAELAELENSDERLEELEAELAEAEAEllEAAEKLS--AAR---KKAAK- 373
|
250 260
....*....|....*....|...
gi 2528757163 920 ldSLSKEIAArndEIEGLGSERA 942
Cdd:COG0497 374 --KLEKAVTA---ELADLGMPNA 391
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
681-1072 |
1.20e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 681 RWEER--EVQGLTTQRDKCLAELKELQKEKRAFVSDDEMVAKITRLEADLRSAQDELAAVNTRLTG-----IRDELKNID 753
Cdd:PRK03918 318 RLEEEinGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGltpekLEKELEELE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 754 KQTKEIQPKLRTAKNELNQLQRQMSTLETVVNRAED-RIFATFCRRigvdniREYEERQVRLMERQSDARLQFESQLARL 832
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKKAIEELKKaKGKCPVCGR------ELTEEHRKELLEEYTAELKRIEKELKEI 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 833 NhqanferQQIESTQERLETIRQAIARENEKLRswqaqkqgkqeeLEGMLEEVSELQAQLSELQTQNeakkvtLEEKRVE 912
Cdd:PRK03918 472 E-------EKERKLRKELRELEKVLKKESELIK------------LKELAEQLKELEEKLKKYNLEE------LEKKAEE 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 913 LQKAARLLDSLSKEIAARNDEIE---GLGSERASIYRRCRLEEITLPLLKGSLAKVGLEETIDVDAPMDIDDDdntqkpl 989
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEkleELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEP------- 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 990 sapdfgIQVDFSSLDDEAKEdggasmgnelqtrIESITAEIEKMSpnmkavERLDDTEAKLAETEKEFDRSRRQAKEARD 1069
Cdd:PRK03918 600 ------FYNEYLELKDAEKE-------------LEREEKELKKLE------EELDKAFEELAETEKRLEELRKELEELEK 654
|
...
gi 2528757163 1070 EFN 1072
Cdd:PRK03918 655 KYS 657
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
275-484 |
1.27e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 275 EHKKAEDAVLRARRDQGQTQTEILQVEKSIKSKQRDVEDLRPTLDAYEEKiaisRKKLdngarmtEQVERDLAKQQANLA 354
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER----REEL-------ETLEAEIEDLRETIA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 355 KLERDREtvqrAADRAAQEQQRALESAGL----TLSEADLGEyhnlkaqANLEAVAERQE-LDGLKRDARikaDAVKDFQ 429
Cdd:PRK02224 269 ETERERE----ELAEEVRDLRERLEELEEerddLLAEAGLDD-------ADAEAVEARREeLEDRDEELR---DRLEECR 334
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2528757163 430 DKSEQFSKQKDKLKDEESTLSERHSALEAKRNQIDTDLQAARDELKRTQAKQTAI 484
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL 389
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
5-48 |
1.59e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 47.26 E-value: 1.59e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2528757163 5 RLEIENFKSYRGHQVV----GPFNAFTAVIGPNGSGKSNLMDAISFVL 48
Cdd:cd03279 5 KLELKNFGPFREEQVIdftgLDNNGLFLICGPTGAGKSTILDAITYAL 52
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-67 |
2.00e-05 |
|
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: 47.68 E-value: 2.00e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2528757163 3 LKRLEIENFKSYRGHQVvgPFNA-FTAVIGPNGSGKSNLMDAISFVLGVRSaqLRSSQLKDLIFRG 67
Cdd:cd03242 1 LKSLELRNFRNYAELEL--EFEPgVTVLVGENAQGKTNLLEAISLLATGKS--HRTSRDKELIRWG 62
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1144-1194 |
2.55e-05 |
|
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: 46.70 E-value: 2.55e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2528757163 1144 LSGGEKTMAALALLFAihsfQPAPFFVLDEVDAALDSQNVAKVSNYIRQHA 1194
Cdd:COG4133 132 LSAGQKRRVALARLLL----SPAPLWLLDEPFTALDAAGVALLAELIAAHL 178
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
3-64 |
3.05e-05 |
|
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: 46.44 E-value: 3.05e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2528757163 3 LKRLEIENFKSYRGHQV-VGPFNAFtaVIGPNGSGKSNLMDAISFVLGVR-SAQLRSSQLKDLI 64
Cdd:cd03276 1 IESITLKNFMCHRHLQIeFGPRVNF--IVGNNGSGKSAILTALTIGLGGKaSDTNRGSSLKDLI 62
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
723-1065 |
3.09e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 723 RLEADLRSAQDELAA---------VNTRLTGIRDELKNIDKQTKEIQPKLRTAKNELNQL----------QRQMSTLETV 783
Cdd:PRK02224 180 RVLSDQRGSLDQLKAqieekeekdLHERLNGLESELAELDEEIERYEEQREQARETRDEAdevleeheerREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 784 VNRAEDRIFATFCRRIGV-DNIREYEERQVRLMERQSDARLQFE----SQLARLNHQANFERQqIESTQERLETIRQAIA 858
Cdd:PRK02224 260 IEDLRETIAETEREREELaEEVRDLRERLEELEEERDDLLAEAGlddaDAEAVEARREELEDR-DEELRDRLEECRVAAQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 859 RENEklrswqaQKQGKQEELEGMLEEVSELQAQLSELQTQNEAKKVTLEEKRVELQKAARLLDSLSKEIAARNDEIEGLG 938
Cdd:PRK02224 339 AHNE-------EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 939 SERASIyrRCRLEEITlpllkgslakvGLEETIDVDAPMDIDDDDNTQKPLSA---PDFGIQVDFSSLDDEAKEDggasm 1015
Cdd:PRK02224 412 DFLEEL--REERDELR-----------EREAELEATLRTARERVEEAEALLEAgkcPECGQPVEGSPHVETIEED----- 473
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1016 gnelQTRIESITAEIEKMSPNMKAVERLDDTEAKLAETEKEFDRSRRQAK 1065
Cdd:PRK02224 474 ----RERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERRE 519
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
683-1212 |
3.63e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 683 EEREVQGLTTQRDKCLAELKELQKEKRAFVSDDEMVAKITR---LEADLRSAQDELAAVNTRLTGIRDELKNIdkqtKEI 759
Cdd:COG4717 86 KEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllpLYQELEALEAELAELPERLEELEERLEEL----REL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 760 QPKLRTAKNELNQLQRQMSTLETVVNRAEDRIFATFCRRIGV--DNIREYEERQVRLMERQSDARLQFESQLARLNHQAN 837
Cdd:COG4717 162 EEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEElqQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 838 FERQQIESTQERLETIRQAIARENEKLRSWQAQKQG---------------KQEELEGMLEEVSELQAQLSELQTQNEAK 902
Cdd:COG4717 242 EERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEEL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 903 KVTLEEKRVELQKAARLLDSLSKEIAARNDEIEGLGSERASIYRRCRLEEITlPLLKgsLAKVGLEETIDVDAPMDIDDD 982
Cdd:COG4717 322 EELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA-ALLA--EAGVEDEEELRAALEQAEEYQ 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 983 DNTQKPLSapdfgIQVDFSSLDDEAKEDGGASMGNELQTRIESITAEIEKMSPNMKAV-ERLDDTEAKL--AETEKEFDR 1059
Cdd:COG4717 399 ELKEELEE-----LEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELrEELAELEAELeqLEEDGELAE 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1060 SRRQAKEARDEFNRIKKRRcdlfnSAFNHISKMIDPTYKDLSRSKAAP-----------MGGSAYLSIENTEEPYLggit 1128
Cdd:COG4717 474 LLQELEELKAELRELAEEW-----AALKLALELLEEAREEYREERLPPvleraseyfsrLTDGRYRLIRIDEDLSL---- 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1129 ySVVPPMKRFRDITALSGGEKTMAALALLFA-IHSFQPAPF-FVLDEVDAALDSQNVAKVSNYIRQHASDQfQFIVISLK 1206
Cdd:COG4717 545 -KVDTEDGRTRPVEELSRGTREQLYLALRLAlAELLAGEPLpLILDDAFVNFDDERLRAALELLAELAKGR-QVIYFTCH 622
|
....*.
gi 2528757163 1207 ASLYER 1212
Cdd:COG4717 623 EELVEL 628
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
170-483 |
3.73e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 170 ELSRLIDQISGSLELKDDYERAKQAQERATDNSTFNFNKRRGINSELKQFREQKSEAEKFERLQQERVQHILNHILwrlf 249
Cdd:PTZ00121 1221 EDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK---- 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 250 hiNQDIELNTDFVKTQAKNMRPLRTEHKKAEDA-----VLRARRDQGQTQTEILQVEKsiKSKQRDVEDLRPTLDAYEEK 324
Cdd:PTZ00121 1297 --KAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkkadAAKKKAEEAKKAAEAAKAEA--EAAADEAEAAEEKAEAAEKK 1372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 325 IAISRKKLDNGARMTEQVER-DLAKQQANLAKLERD----RETVQRAADRAAQ--EQQRALESAGLTLSEADLGEYHNLK 397
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKaDEAKKKAEEDKKKADelkkAAAAKKKADEAKKkaEEKKKADEAKKKAEEAKKADEAKKK 1452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 398 AQANLEA------VAERQELDGLKRDARIKADAvKDFQDKSEQFSKQKDKLK---DEESTLSERHSALEAKRNQIDTDLQ 468
Cdd:PTZ00121 1453 AEEAKKAeeakkkAEEAKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADEAKkaaEAKKKADEAKKAEEAKKADEAKKAE 1531
|
330
....*....|....*..
gi 2528757163 469 AAR--DELKRTQAKQTA 483
Cdd:PTZ00121 1532 EAKkaDEAKKAEEKKKA 1548
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
227-917 |
4.17e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 227 EKFERLQQErVQHILNHILWRLFHINQDIELNTDFVKTQAKNMRPLRTEHKKAEDAVLRARRDQGQTQ------------ 294
Cdd:pfam15921 74 EHIERVLEE-YSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQedlrnqlqntvh 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 295 -----------------TEILQVEKSIKSKQRDVEDLRPTLDAYEEKiaiSRKKLDNGARMTEQVERDLAKQQANLAKlE 357
Cdd:pfam15921 153 eleaakclkedmledsnTQIEQLRKMMLSHEGVLQEIRSILVDFEEA---SGKKIYEHDSMSTMHFRSLGSAISKILR-E 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 358 RDRE-TVQRAADRAAQEQQRALESAGLTLSEADLGEYHNLKAQANLEAVAERQELDGLKRDARIKADAVKD----FQDKS 432
Cdd:pfam15921 229 LDTEiSYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSqleiIQEQA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 433 E-QFSKQKDKLKDEESTLSERHSAL-EAKR------NQIDTDLQAARDELKRTQAKQTAINQRETKLNDTLQvcynKLLQ 504
Cdd:pfam15921 309 RnQNSMYMRQLSDLESTVSQLRSELrEAKRmyedkiEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQ----KLLA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 505 agnDLKEVEREAAM-KETIAKLQRIFPG-------VRGRVVDLCKPVQRK---YDTAISTVLGRNTDAIIVDQEKTaiDC 573
Cdd:pfam15921 385 ---DLHKREKELSLeKEQNKRLWDRDTGnsitidhLRRELDDRNMEVQRLealLKAMKSECQGQMERQMAAIQGKN--ES 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 574 IEYLRNTRSGQATFLPLDRIQAKPINDRLRSIARGARLAVDVIHFDASIERAIHHAcgNALVCDTmdiaRSVVYDKKVEA 653
Cdd:pfam15921 460 LEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAT--NAEITKL----RSRVDLKLQEL 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 654 KAVTLEGTIIHKSGLITGGQSSSSGGK-------RWEEREVQGLTTQRDKC----LAELKELQKE--------KRAFVSD 714
Cdd:pfam15921 534 QHLKNEGDHLRNVQTECEALKLQMAEKdkvieilRQQIENMTQLVGQHGRTagamQVEKAQLEKEindrrlelQEFKILK 613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 715 DEMVAKITRLEADLRSAQDE----LAAVNTRLTGIRDelknIDKQTKEIQPKLRTAKNELNQLQRQMSTLE-TVVNRAED 789
Cdd:pfam15921 614 DKKDAKIRELEARVSDLELEkvklVNAGSERLRAVKD----IKQERDQLLNEVKTSRNELNSLSEDYEVLKrNFRNKSEE 689
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 790 RIFATFCRRIGVDNIREYEERQVRLMERQSDARLQFESQLARLNHQANFERQQIESTQERLETIRQAIARENEKLRSWQA 869
Cdd:pfam15921 690 METTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKE 769
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 2528757163 870 QKQGKQEELEGMLEEVSELQAQLSELQTQNEAKKVTLEEKRVELQKAA 917
Cdd:pfam15921 770 EKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKAS 817
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
277-907 |
4.44e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 277 KKAEDAVLRARRDQGQTQTEILQVEKSIKSKQ------------RDVEDLRPTLDAYEEKIAISRKKLDNGARMTEQ--- 341
Cdd:PRK02224 169 ERASDARLGVERVLSDQRGSLDQLKAQIEEKEekdlherlngleSELAELDEEIERYEEQREQARETRDEADEVLEEhee 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 342 -------VERDLAKQQANLAKLERDREtvqrAADRAAQEQQRALESAGL----TLSEADLGEyhnlkaqANLEAVAERQE 410
Cdd:PRK02224 249 rreeletLEAEIEDLRETIAETERERE----ELAEEVRDLRERLEELEEerddLLAEAGLDD-------ADAEAVEARRE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 411 -LDGLKRDARikaDAVKDFQDKSEQFSKQKDKLKDEESTLSERHSALEAKRNQIDTDLQAARDELKRTQAKQTAINQRET 489
Cdd:PRK02224 318 eLEDRDEELR---DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 490 KLNDTLQvcynkllQAGNDLKEVEREAAMketiakLQRIFPGVRGRVVDLckpvqrkyDTAISTVLGRNTDAIIVDQEKT 569
Cdd:PRK02224 395 ELRERFG-------DAPVDLGNAEDFLEE------LREERDELREREAEL--------EATLRTARERVEEAEALLEAGK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 570 AIDCIEYLRNtrSGQATFLPLDRIQAKPINDRLrsiargARLAVDVIHFDASIERAihhacgNALVcdtmdiarsvvydk 649
Cdd:PRK02224 454 CPECGQPVEG--SPHVETIEEDRERVEELEAEL------EDLEEEVEEVEERLERA------EDLV-------------- 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 650 KVEAKAVTLEgtiihksglitggQSSSSGGKRWEEREvQGLTTQRDKClAELKELQKEKRAFVSDDEMVAKITRLEADlr 729
Cdd:PRK02224 506 EAEDRIERLE-------------ERREDLEELIAERR-ETIEEKRERA-EELRERAAELEAEAEEKREAAAEAEEEAE-- 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 730 SAQDELAAVNTRLTGIRDELKNIDKqTKEIQPKLRTAKNELNQLQRQMSTLETVVNRAEDRIFAtfcRRigvDNIREYEE 809
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERLREKREALAELNDERRERLAE---KR---ERKRELEA 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 810 R--QVRLMERQSDaRLQFESQLARLNHQANFERQQIESTQERLETIRQAIARENEkLRSWQAQKQGKQEELEGMLEEVSE 887
Cdd:PRK02224 642 EfdEARIEEARED-KERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE-LRERREALENRVEALEALYDEAEE 719
|
650 660
....*....|....*....|.
gi 2528757163 888 LQAQLSELQTQNEAKKV-TLE 907
Cdd:PRK02224 720 LESMYGDLRAELRQRNVeTLE 740
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
831-942 |
5.10e-05 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 47.15 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 831 RLNHQA-----NFERQQIESTQERLETIRQAiarenekLRSWQAQKQ--GKQEELEGMLEEVSELQAQLSELQTQNEAKK 903
Cdd:COG3524 169 QLSERAredavRFAEEEVERAEERLRDAREA-------LLAFRNRNGilDPEATAEALLQLIATLEGQLAELEAELAALR 241
|
90 100 110
....*....|....*....|....*....|....*....
gi 2528757163 904 VTLEEKRVELQKAARLLDSLSKEIAARNDEIEGLGSERA 942
Cdd:COG3524 242 SYLSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDS 280
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
684-952 |
5.68e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 684 EREVQGLTTQRDKCLAELKELQKEKrafvsdDEMVAKITRLEADLRSAQDELAAVNT----------------------- 740
Cdd:PRK02224 397 RERFGDAPVDLGNAEDFLEELREER------DELREREAELEATLRTARERVEEAEAlleagkcpecgqpvegsphveti 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 741 -----RLTGIRDELKNIDKQTKEIQPKLRTAKnELNQLQRQMSTLETVVNRAEDRIFAtfcRRIGVDNIRE-YEERQVRL 814
Cdd:PRK02224 471 eedreRVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAE---RRETIEEKRErAEELRERA 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 815 MERQSDARLQFES-QLARLNHQA--------NFERQQIESTQERLETIR----------QAIARENEKLRSWQAQKQGKQ 875
Cdd:PRK02224 547 AELEAEAEEKREAaAEAEEEAEEareevaelNSKLAELKERIESLERIRtllaaiadaeDEIERLREKREALAELNDERR 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 876 EELEGMLEEVSELQAQ-----LSELQTQNEAKKVTLEEKRVELQKAARLLDSLSKEIAARNDEIEGLGSERAsiyRRCRL 950
Cdd:PRK02224 627 ERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRE---RREAL 703
|
..
gi 2528757163 951 EE 952
Cdd:PRK02224 704 EN 705
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
273-956 |
1.00e-04 |
|
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: 46.76 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 273 RTEHKKAEDAVLRARRDQGQTQTEILQVEKS-----IKSKQRDVEDLRPTLDAYEeKIAISRKKLDngARMTEQVERDLA 347
Cdd:pfam12128 281 RQETSAELNQLLRTLDDQWKEKRDELNGELSaadaaVAKDRSELEALEDQHGAFL-DADIETAAAD--QEQLPSWQSELE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 348 KQQANLAKLERDRETVQRAADR--AAQEQQRALESAGLTLSEAdlgeyhNLKAQANLEAVAERQELDGLKRDARIKADAV 425
Cdd:pfam12128 358 NLEERLKALTGKHQDVTAKYNRrrSKIKEQNNRDIAGIKDKLA------KIREARDRQLAVAEDDLQALESELREQLEAG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 426 K-DFQDKSEQFSKQKDKLK---DEESTLSERHSALEAKRNQI---DTDLQAARDELKRTQAKQTAINQRETKLNDTLQVC 498
Cdd:pfam12128 432 KlEFNEEEYRLKSRLGELKlrlNQATATPELLLQLENFDERIeraREEQEAANAEVERLQSELRQARKRRDQASEALRQA 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 499 YNKLLQAGNDLKEVERE--AAMKETIAKLQRIFPGVR---GRVVDlckpvqrkydtaiSTVLGRnTDaiiVDQEKTAidc 573
Cdd:pfam12128 512 SRRLEERQSALDELELQlfPQAGTLLHFLRKEAPDWEqsiGKVIS-------------PELLHR-TD---LDPEVWD--- 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 574 ieylrNTRSGQATF----LPLDRIQAKP---INDRLRSIARGARLAVDVihfdasiERAIHHACGNALVCDTMDIARSvv 646
Cdd:pfam12128 572 -----GSVGGELNLygvkLDLKRIDVPEwaaSEEELRERLDKAEEALQS-------AREKQAAAEEQLVQANGELEKA-- 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 647 yDKKVEAKAVTLEGTIIHKSGLITGGQSSSSGGKRWEEREVQGLTTQRDKCLAELKELQKEKRAFVSD---------DEM 717
Cdd:pfam12128 638 -SREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEqkeqkrearTEK 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 718 VAKITRLEADLRSAQDEL-AAVNTRLTGIRDELKNIDKQTKEIQPKLRTAKNELNQLQRQMSTLETVVNRAEDRIFAtfc 796
Cdd:pfam12128 717 QAYWQVVEGALDAQLALLkAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQE--- 793
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 797 rrigvdnIREYEerqVRLMERQSDARLQFESQLARLNHQANFERQQIESTQERLETIRQAIARENEKLRswqAQKQGKQE 876
Cdd:pfam12128 794 -------VLRYF---DWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASE---KQQVRLSE 860
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 877 ELEGMLEEVSELqAQLSELQTQNEAkKVTLEEKRVELQKAARLLDSLSKEIAARNDEIEGL-----GSERASIYRRCRLE 951
Cdd:pfam12128 861 NLRGLRCEMSKL-ATLKEDANSEQA-QGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNViadhsGSGLAETWESLREE 938
|
....*
gi 2528757163 952 EITLP 956
Cdd:pfam12128 939 DHYQN 943
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-44 |
1.15e-04 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 44.83 E-value: 1.15e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2528757163 7 EIENFK-SYRGHQVVGPFN------AFTAVIGPNGSGKSNLMDAI 44
Cdd:cd03235 1 EVEDLTvSYGGHPVLEDVSfevkpgEFLAIVGPNGAGKSTLLKAI 45
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-48 |
1.39e-04 |
|
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: 45.67 E-value: 1.39e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2528757163 1 MPLKRLEIENFKSYRghQVVGPF-NAFTAVIGPNGSGKSNLMDAISFVL 48
Cdd:pfam13175 1 MKIKSIIIKNFRCLK--DTEIDLdEDLTVLIGKNNSGKSSILEALDIFL 47
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-45 |
1.49e-04 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 45.03 E-value: 1.49e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2528757163 5 RLEIENFK-SYRGHQVVGPFNA------FTAVIGPNGSGKSNLMDAIS 45
Cdd:COG1120 1 MLEAENLSvGYGGRPVLDDVSLslppgeVTALLGPNGSGKSTLLRALA 48
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
3-48 |
1.54e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 44.96 E-value: 1.54e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2528757163 3 LKRLEIENFKSYRGHQVvgPFNAFTAVIGPNGSGKSNLMDAISFVL 48
Cdd:COG4938 1 IKSISIKNFGPFKEAEL--ELKPLTLLIGPNGSGKSTLIQALLLLL 44
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-56 |
1.81e-04 |
|
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: 43.39 E-value: 1.81e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2528757163 7 EIENF-KSYRGHQVVGPFN------AFTAVIGPNGSGKSNLMDAISFVLGVRSAQLR 56
Cdd:cd00267 1 EIENLsFRYGGRTALDNVSltlkagEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL 57
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
699-865 |
1.85e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 699 AELKELQKEKRAFVSDDEM---VAKITRLEADLRSAQDELAAVNTRLTGIRDELKNIDKQTKEIQ--PKLRTAKNELNQ- 772
Cdd:COG3206 196 AALEEFRQKNGLVDLSEEAkllLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLqsPVIQQLRAQLAEl 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 773 --------------------LQRQMSTLETVVNRAEDRIFATFCRRIGVDNIREYE-ERQVRLMERQSDARLQFESQLAR 831
Cdd:COG3206 276 eaelaelsarytpnhpdviaLRAQIAALRAQLQQEAQRILASLEAELEALQAREASlQAQLAQLEARLAELPELEAELRR 355
|
170 180 190
....*....|....*....|....*....|....
gi 2528757163 832 LNHQANFERQQIESTQERLETIRQAIARENEKLR 865
Cdd:COG3206 356 LEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
289-489 |
2.57e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.20 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 289 DQGQTQTEILQVEKSikSKQRDVEDLRPTLDAYEEKIAISRKKLDNgarMTEQVeRDLAKQQANLaklerdRETVQraad 368
Cdd:pfam10174 362 NKKTKQLQDLTEEKS--TLAGEIRDLKDMLDVKERKINVLQKKIEN---LQEQL-RDKDKQLAGL------KERVK---- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 369 rAAQEQQRALESAGLTLSEAdLGE----YHNLKAQANLEAVAERQELDGLKRDARIKADAVKDFQ-DKSEQFSKQKDkLK 443
Cdd:pfam10174 426 -SLQTDSSNTDTALTTLEEA-LSEkeriIERLKEQREREDRERLEELESLKKENKDLKEKVSALQpELTEKESSLID-LK 502
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2528757163 444 DEESTLSERHSALEAKRNQIDTDLQAARDELKRTQAK-QTAINQRET 489
Cdd:pfam10174 503 EHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQlKKAHNAEEA 549
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
684-966 |
2.60e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 684 EREVQGLTTQRDKCLAELKELQKE---KRAFVSDDEMVAKITRLEADLRS--------AQDELAAVNTRLTGIRDELKNI 752
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVlkkESELIKLKELAEQLKELEEKLKKynleelekKAEEYEKLKEKLIKLKGEIKSL 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 753 DKQTKEIQP---KLRTAKNELNQLQRQMSTLETVVnraedrifatfcRRIGVDNIREYEERQVRLME------RQSDARL 823
Cdd:PRK03918 545 KKELEKLEElkkKLAELEKKLDELEEELAELLKEL------------EELGFESVEELEERLKELEPfyneylELKDAEK 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 824 QFESQLARLnhqanferqqiESTQERLETIRQAIARENEKLRSW-----QAQKQGKQEELEGMLEEVSELQAQLSELQTQ 898
Cdd:PRK03918 613 ELEREEKEL-----------KKLEEELDKAFEELAETEKRLEELrkeleELEKKYSEEEYEELREEYLELSRELAGLRAE 681
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2528757163 899 NEakkvTLEEKRVELQKAARLLDSLSKEIAARNDEIEGLGSERASIYR-RCRLEEITLPLLKGSLAKVG 966
Cdd:PRK03918 682 LE----ELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEElREKVKKYKALLKERALSKVG 746
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
684-926 |
3.41e-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: 44.89 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 684 EREVQGLTTQRDKCLAELKELQKEKRAfvsddemvakitrLEADLRSAQDELAAVNTRLTGIRDELKNIDKQTKEIQPKL 763
Cdd:pfam07888 149 ETELERMKERAKKAGAQRKEEEAERKQ-------------LQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTI 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 764 RTAKNELNQLQR----------QMSTLETVVNRAEDRIFATFCRRIGVDNIREY---EERQVRLMERQSDARLQfESQLA 830
Cdd:pfam07888 216 TTLTQKLTTAHRkeaenealleELRSLQERLNASERKVEGLGEELSSMAAQRDRtqaELHQARLQAAQLTLQLA-DASLA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 831 RLNHQANFerqqiesTQERlETIRQAIARENEKLRSWQAQKQGKQEELEgmlEEVSELQAQLSELQTQNEAKKVTLEEKR 910
Cdd:pfam07888 295 LREGRARW-------AQER-ETLQQSAEADKDRIEKLSAELQRLEERLQ---EERMEREKLEVELGREKDCNRVQLSESR 363
|
250
....*....|....*.
gi 2528757163 911 VELQKAARLLDSLSKE 926
Cdd:pfam07888 364 RELQELKASLRVAQKE 379
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
1137-1206 |
3.55e-04 |
|
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: 43.35 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1137 RFRDITAL--------SGGEKTMAALALLFAIHSFQPAPFFVLDEVDAALDSQNVAKVSNYIRQHASDQF--QFIVISLK 1206
Cdd:cd03277 112 KFREGEQLqeldphhqSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVETACKEGtsQYFLITPK 191
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-44 |
4.14e-04 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 43.54 E-value: 4.14e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2528757163 1 MPLKRLEIENFK-SYRGHQVVGPFN------AFTAVIGPNGSGKSNLMDAI 44
Cdd:COG1121 2 MMMPAIELENLTvSYGGRPVLEDVSltippgEFVAIVGPNGAGKSTLLKAI 52
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
684-858 |
4.16e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 684 EREVQGLTTQRDKCLAELKELQKEkrafvsddemvakITRLEADLRSAQDELAAVNTRLTGIRDELKNIDKQTKEIQPKL 763
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDE-------------LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 764 RTAKN--ELNQLQRQMSTLETVVNRAEDRIFATFcrrigvDNIREYEERQVRLMERQSDARLQFESQLARLNHqanfERQ 841
Cdd:COG1579 83 GNVRNnkEYEALQKEIESLKRRISDLEDEILELM------ERIEELEEELAELEAELAELEAELEEKKAELDE----ELA 152
|
170
....*....|....*..
gi 2528757163 842 QIESTQERLETIRQAIA 858
Cdd:COG1579 153 ELEAELEELEAEREELA 169
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
162-524 |
4.26e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 162 AVASQGAKELSRLIDQISGSLELKDDYERAKQAQEratdnstfnfnkrrginseLKQFREQKSEAEKFERLQQERVQhil 241
Cdd:PTZ00121 1414 AAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADE-------------------AKKKAEEAKKAEEAKKKAEEAKK--- 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 242 nhilwrlfhinqdielnTDFVKTQAKNMRPLRTEHKKAEDAVLRARRDQGQTQTEILQVEKSIKSKQRDVEDLRPTLD-- 319
Cdd:PTZ00121 1472 -----------------ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEak 1534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 320 -AYEEKIAISRKKLDNgARMTEQVERDLAKQQANLAK-LERDRETVQRAADRAAQ-EQQRALESAGLTLSEAdlgeyhNL 396
Cdd:PTZ00121 1535 kADEAKKAEEKKKADE-LKKAEELKKAEEKKKAEEAKkAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEK------KM 1607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 397 KAQANLEAVAERQELDGLKRDARIKaDAVKDFQDKSEQFSKQKDKLKDEESTLSERHSALEAKRNQIDTDLQAAR--DEL 474
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKAEELKKAEEEK-KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKkaEED 1686
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2528757163 475 KRTQAKQTAINQRETKLNDTLQVCYNKLLQAGNDLKEVEREAAMKETIAK 524
Cdd:PTZ00121 1687 EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1139-1205 |
5.36e-04 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 42.42 E-value: 5.36e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2528757163 1139 RDITALSGGEKTMAALALLFAihsfQPAPFFVLDEVDAALDSQNVAKVSNYIRQHASDQFQFIVISL 1205
Cdd:cd03214 93 RPFNELSGGERQRVLLARALA----QEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVL 155
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-45 |
6.66e-04 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 42.76 E-value: 6.66e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2528757163 7 EIEN-FKSYRGHQVVGPFNA------FTAVIGPNGSGKSNLMDAIS 45
Cdd:COG4604 3 EIKNvSKRYGGKVVLDDVSLtipkggITALIGPNGAGKSTLLSMIS 48
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
684-1105 |
6.71e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 684 EREVQGLTTQRDKCLAELKELQKEKRAFvsdDEMVAKITRLEADLRSAQDELAAVNTRLTGIRD----------ELKNID 753
Cdd:PRK03918 206 LREINEISSELPELREELEKLEKEVKEL---EELKEEIEELEKELESLEGSKRKLEEKIRELEErieelkkeieELEEKV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 754 KQTKEIQPK----------LRTAKNELNQLQRQMSTLETVVNRAEDRIFATFCRRIGVDNIRE-YEERQVRLMERQSDAR 822
Cdd:PRK03918 283 KELKELKEKaeeyiklsefYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKkLKELEKRLEELEERHE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 823 L-----QFESQLARLNHQ-ANFERQQIESTQERLETIRQAIARENEKLRSWQAQKQGKQEELEGMLEEVSELQ------- 889
Cdd:PRK03918 363 LyeeakAKKEELERLKKRlTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcg 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 890 AQLSELQTQNEAKKVTLEEKRVELQKAArlLDSLSKEIAARNDEIEG-LGSERASIYRRCRLEEITlpLLKGSLAKVGLE 968
Cdd:PRK03918 443 RELTEEHRKELLEEYTAELKRIEKELKE--IEEKERKLRKELRELEKvLKKESELIKLKELAEQLK--ELEEKLKKYNLE 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 969 EtidvdAPMDIDDDDNTQKPLSapdfGIQVDFSSLDDEAKEdggasmGNELQTRIESITAEIEKMSPNMKAVER------ 1042
Cdd:PRK03918 519 E-----LEKKAEEYEKLKEKLI----KLKGEIKSLKKELEK------LEELKKKLAELEKKLDELEEELAELLKeleelg 583
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2528757163 1043 ---LDDTEAKLAETEKEFDRSRRqAKEARDEFNRIKKRRCDLFNSAfNHISKMIDPTYKDLSRSKA 1105
Cdd:PRK03918 584 fesVEELEERLKELEPFYNEYLE-LKDAEKELEREEKELKKLEEEL-DKAFEELAETEKRLEELRK 647
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
345-522 |
6.81e-04 |
|
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: 43.99 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 345 DLAKQQANLAKLERDRETVQRAADRAAQEQ---QRALESAGLTLSEAD-LGEYHNLKAQANLEAVAERQELDGLKRDARI 420
Cdd:pfam18971 611 EVKKAQKDLEKSLRKREHLEKEVEKKLESKsgnKNKMEAKAQANSQKDeIFALINKEANRDARAIAYTQNLKGIKRELSD 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 421 KADAV-KDFQDkseqFSKQKDKLKD-EESTLSERHSALEAKRNQIdTDLQAARDELKRTQAKQTAINQRETKLNDTlqvc 498
Cdd:pfam18971 691 KLEKIsKDLKD----FSKSFDEFKNgKNKDFSKAEETLKALKGSV-KDLGINPEWISKVENLNAALNEFKNGKNKD---- 761
|
170 180
....*....|....*....|....
gi 2528757163 499 YNKLLQAGNDLKEVEREAAMKETI 522
Cdd:pfam18971 762 FSKVTQAKSDLENSVKDVIINQKV 785
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-45 |
6.90e-04 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 42.04 E-value: 6.90e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2528757163 7 EIEN-FKSYRGHQVVGPFNA------FTAVIGPNGSGKSNLMDAIS 45
Cdd:cd03214 1 EVENlSVGYGGRTVLDDLSLsieageIVGILGPNGAGKSTLLKTLA 46
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
684-939 |
7.47e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.95 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 684 EREVQGLT-------TQRDKCLAELKELQKEKRAFVSD-----DEMVAKITRLEADLRSA-----------QDELAAVNT 740
Cdd:pfam15921 277 EVEITGLTekassarSQANSIQSQLEIIQEQARNQNSMymrqlSDLESTVSQLRSELREAkrmyedkieelEKQLVLANS 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 741 RLTGIRDELKNIDKQTKEIQPKLRTAKNELNQLQRQMSTLETVVNRAEDRIFATfcrRIGVDNIREyeERQVRLMERQsd 820
Cdd:pfam15921 357 ELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGN---SITIDHLRR--ELDDRNMEVQ-- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 821 aRLQFESQLARLNHQANFERQqIESTQERLETIrqaiarenEKLRSWQAQKQGKQEELEGMLEEVSelqaqlselqtqne 900
Cdd:pfam15921 430 -RLEALLKAMKSECQGQMERQ-MAAIQGKNESL--------EKVSSLTAQLESTKEMLRKVVEELT-------------- 485
|
250 260 270
....*....|....*....|....*....|....*....
gi 2528757163 901 AKKVTLEEKRVELQKAARLLDSLSKEIAARNDEIEGLGS 939
Cdd:pfam15921 486 AKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRS 524
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
352-791 |
8.66e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 8.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 352 NLAKLERDRETVQRAADRAAQ--EQQRALESAGLTLSEADLGEYHNLKAQANLEAVAERQELDGLKRDARIKadaVKDFQ 429
Cdd:COG4717 69 NLKELKELEEELKEAEEKEEEyaELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAE---LAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 430 DKSEQFSKQKDKLKDEESTLSERHSALEAKRNQIDTDLQ----AARDELKRTQAKQTAINQRETKLNDTLQVCYNKLLQA 505
Cdd:COG4717 146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEqlslATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 506 GNDLKEVEREAAMKETIAKLQ--RIFPGVRGRVVDLCKPVQRKYDTaISTVLGRNTDAIivdqektAIDCIEYLRNTRSG 583
Cdd:COG4717 226 EEELEQLENELEAAALEERLKeaRLLLLIAAALLALLGLGGSLLSL-ILTIAGVLFLVL-------GLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 584 QATFLPLDRIQAKPINDRLRSIARGARLAVDVIHFDASIERAIHHACGNALVCDTMDIARSvvYDKKVEAKAVTLEGTII 663
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE--LEEELQLEELEQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 664 HKSGLITGGQSSSSGGKRWEER-EVQGLTTQRDKCLAELKELQKEKRAFVSDDEMVAKITRLEADLRSAQDELAAVNTRL 742
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEYqELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREEL 455
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2528757163 743 TGIRDELKNIDKQTK--EIQPKLRTAKNELNQLQRQ---MSTLETVVNRAEDRI 791
Cdd:COG4717 456 AELEAELEQLEEDGElaELLQELEELKAELRELAEEwaaLKLALELLEEAREEY 509
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
694-933 |
1.02e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 694 RDKCLAELK-ELQKEKRAFVSDDEMVAKITRLEADLRSA-------------QDELAAVNTRLTGIRDELKNIDKQTKEI 759
Cdd:PRK04863 784 REKRIEQLRaEREELAERYATLSFDVQKLQRLHQAFSRFigshlavafeadpEAELRQLNRRRVELERALADHESQEQQQ 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 760 QPKLRTAKNELNQLQRqmstLETVVNRAEDRIFAtfcrrigvDNIREYEERQVRLMERQSDARlQFESQLARLNHQANFE 839
Cdd:PRK04863 864 RSQLEQAKEGLSALNR----LLPRLNLLADETLA--------DRVEEIREQLDEAEEAKRFVQ-QHGNALAQLEPIVSVL 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 840 R---QQIESTQERLETIRQAIARENEKLRSW----QAQKQGKQEELEGMLEEVSELQAQLSELQTQNEAK----KVTLEE 908
Cdd:PRK04863 931 QsdpEQFEQLKQDYQQAQQTQRDAKQQAFALtevvQRRAHFSYEDAAEMLAKNSDLNEKLRQRLEQAEQErtraREQLRQ 1010
|
250 260
....*....|....*....|....*
gi 2528757163 909 KRVELQKAARLLDSLSKEIAARNDE 933
Cdd:PRK04863 1011 AQAQLAQYNQVLASLKSSYDAKRQM 1035
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
397-496 |
1.07e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 397 KAQANLEAVAERQELDGLKRDARIKADAVKDFQDKSEQFSKQKDKLKDEESTLSERHSALEAKRNQIDTDLQAARDELKR 476
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQE 125
|
90 100
....*....|....*....|
gi 2528757163 477 TQAKQTAINQRETKLNDTLQ 496
Cdd:PRK12704 126 LEKKEEELEELIEEQLQELE 145
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
818-944 |
1.15e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 818 QSDARLQFESQLARLNHQANFERQQIESTQERLETIRQAIARENEKLRSWQAQKQGKQEELEGMLEEVSELQAQLSELQT 897
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2528757163 898 QNEAKKVTLEEKRVELQK------------------AARLLDSLSKEIAARNDEIEGLGSERASI 944
Cdd:COG4942 98 ELEAQKEELAELLRALYRlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
700-1070 |
1.23e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.17 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 700 ELKELQKEKRAFVSDDE-----MVAKITRLEADLRSAQDELAAVNTRLTGIRDELKNIDKQTKEIQPKLRTAKNELN--- 771
Cdd:pfam05483 223 KIQHLEEEYKKEINDKEkqvslLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEdik 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 772 -QLQRQMSTLETVvnrAEDRIFATfcrrigvDNIREYEERQVRLMERQSDAR-------LQFESQLARLNHQANFERQQI 843
Cdd:pfam05483 303 mSLQRSMSTQKAL---EEDLQIAT-------KTICQLTEEKEAQMEELNKAKaahsfvvTEFEATTCSLEELLRTEQQRL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 844 ESTQERLETIRQAIARENEKLRSWQAQKQGKQEELEgmleevsELQAQLSELQTQNEAKKvTLEEKRVELQKAARLLDSL 923
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELE-------ELKKILAEDEKLLDEKK-QFEKIAEELKGKEQELIFL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 924 skeIAARNDEIEGLgserasiyrrcrleEITLPLLKGSlAKVGLEETIDVDAPMDIDDDDNTQkpLSApdfgiQVDFSSL 1003
Cdd:pfam05483 445 ---LQAREKEIHDL--------------EIQLTAIKTS-EEHYLKEVEDLKTELEKEKLKNIE--LTA-----HCDKLLL 499
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2528757163 1004 DDEAKEDGGASMGNELQTRIESITAEIEKMSPNMKAVERLDDTEAKLaetEKEFDRSRRQAKEARDE 1070
Cdd:pfam05483 500 ENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNL---RDELESVREEFIQKGDE 563
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
724-933 |
1.33e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 724 LEADLRSAQDELAAVNTRLTGIR-DELKNIDKQTKEIQPK---LRTAKNELNQLQRQMSTLETVVNRAEDRIFATFCRRI 799
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNlKELKELEEELKEAEEKeeeYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 800 GVDNIREYEERQVRLMErqsdarlqFESQLARLNHQanfeRQQIESTQERLETIRQAIARENEKLRSWQAQKQgkqeelE 879
Cdd:COG4717 127 LLPLYQELEALEAELAE--------LPERLEELEER----LEELRELEEELEELEAELAELQEELEELLEQLS------L 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2528757163 880 GMLEEVSELQAQLSELQTQNEAKKVTLEEKRVELQKAARLLDSLSKEIAARNDE 933
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
684-918 |
1.50e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 684 EREVQGLTTQRDKCLAELKELQKEKrafvsdDEMVAKITRLEADLRSAQDELAAVntrltgIRDELKNidkqtkeiqpkl 763
Cdd:COG3883 43 QAELEELNEEYNELQAELEALQAEI------DKLQAEIAEAEAEIEERREELGER------ARALYRS------------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 764 rtaknelnqlQRQMSTLETVVNrAEDriFATFCRRigVDNIREYEERQVRLMERQSDARLQFESQLARLNHQANFERQQI 843
Cdd:COG3883 99 ----------GGSVSYLDVLLG-SES--FSDFLDR--LSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2528757163 844 ESTQERLETIRQAIARENEKLRSWQAQKQGKQEELEGMLEEVSELQAQLSELQTQNEAKKVTLEEKRVELQKAAR 918
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
840-939 |
1.54e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 840 RQQIESTQERLETIRQAIAR-ENEKLRSWQAQKQGKQEELEGMLEEVSELQAQLSELQTQNEAKKVTLEE---KRVELQK 915
Cdd:COG0542 403 RMEIDSKPEELDELERRLEQlEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEiqeLKEELEQ 482
|
90 100
....*....|....*....|....
gi 2528757163 916 AARLLDSLSKEIAARNDEIEGLGS 939
Cdd:COG0542 483 RYGKIPELEKELAELEEELAELAP 506
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1138-1204 |
1.59e-03 |
|
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: 41.05 E-value: 1.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2528757163 1138 FRDITALSGGEKTMAALALLFAIHSFQPA--PFFVLDEVDAALDSQNVA-KVSNYIRQHASD-QFQFIVIS 1204
Cdd:cd03240 110 LDMRGRCSGGEKVLASLIIRLALAETFGSncGILALDEPTTNLDEENIEeSLAEIIEERKSQkNFQLIVIT 180
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
684-902 |
1.79e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.37 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 684 EREVQGLTTQRDKCLAELKelqkekrafvSDDEMVAKITRleaDLRSAQDELAAVNTRLTGIRDELKNIDKQTKEiQPKL 763
Cdd:PRK11637 60 EKSVRQQQQQRASLLAQLK----------KQEEAISQASR---KLRETQNTLNQLNKQIDELNASIAKLEQQQAA-QERL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 764 RTAKNELNQLQRQMSTLETVVNRAE----DRIFATFcrriGVDNireyeerqvrlmerqsDARLQFESQLARLNHQANFE 839
Cdd:PRK11637 126 LAAQLDAAFRQGEHTGLQLILSGEEsqrgERILAYF----GYLN----------------QARQETIAELKQTREELAAQ 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2528757163 840 RQQIESTQERLETIRQAIARENEKLRSWQAQKQGKQEELEGMLEEVselQAQLSELQtQNEAK 902
Cdd:PRK11637 186 KAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKD---QQQLSELR-ANESR 244
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
685-929 |
1.85e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.52 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 685 REVQGLTTQRDKCLAELKELQKEKRAFVS--DDEMVAKITRLEADLRSAQDELAAVNTRLTGIRDELKNIDK----QTKE 758
Cdd:pfam12128 265 FGYKSDETLIASRQEERQETSAELNQLLRtlDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDadieTAAA 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 759 IQPKLRTAKNELNQLQRQMSTLETVVNRAEdRIFATFCRRIGVDNIREYEERQVRLMERQSDARLQFESQLARLNHQANF 838
Cdd:pfam12128 345 DQEQLPSWQSELENLEERLKALTGKHQDVT-AKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 839 ERQQIESTQERL--ETIRQAIARENEKLRSWQA--------QKQGKQEELEGMLEEVSELQAQLSELQTQNEAKKVTLEE 908
Cdd:pfam12128 424 LREQLEAGKLEFneEEYRLKSRLGELKLRLNQAtatpelllQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQ 503
|
250 260
....*....|....*....|.
gi 2528757163 909 KRVELQKAARLLDSLSKEIAA 929
Cdd:pfam12128 504 ASEALRQASRRLEERQSALDE 524
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
277-388 |
1.88e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 277 KKAEDAVLRARRD-QGQTQTEILQVEKSIKSKQRDVE----DLRPTLDAYEEKIAISRKKLDNGARMTEQVERDLAKQQA 351
Cdd:PRK12704 38 EEAKRILEEAKKEaEAIKKEALLEAKEEIHKLRNEFEkelrERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEK 117
|
90 100 110
....*....|....*....|....*....|....*...
gi 2528757163 352 NLAKLERDRETVQRAADRAAQEQQRALES-AGLTLSEA 388
Cdd:PRK12704 118 ELEQKQQELEKKEEELEELIEEQLQELERiSGLTAEEA 155
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
687-965 |
1.89e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 687 VQGLTTQRDKCLAELKELQKEKRAF-----VSDD--EMVAKITRLEADLRSAQDELAAVNTRLTGIRDELKNIDKQTKEI 759
Cdd:PRK01156 144 ISGDPAQRKKILDEILEINSLERNYdklkdVIDMlrAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 760 QPKLRTAKNELNQLQ---RQMSTLETVVNRAEDRIFATFCRR-IGVDNIREYEERQVRLMERQSDARLQFESqlaRLNHQ 835
Cdd:PRK01156 224 SIEYNNAMDDYNNLKsalNELSSLEDMKNRYESEIKTAESDLsMELEKNNYYKELEERHMKIINDPVYKNRN---YINDY 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 836 ANFeRQQIESTQERLETIRQAIARENEKLRswqaqkqgKQEELEGMLEEVSELQAQLSELQTQneakKVTLEEKRVELQK 915
Cdd:PRK01156 301 FKY-KNDIENKKQILSNIDAEINKYHAIIK--------KLSVLQKDYNDYIKKKSRYDDLNNQ----ILELEGYEMDYNS 367
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2528757163 916 AARLLDSLSKEIAARNDEIEGLGSErasIYRRCRLEEITLPLLKGSLAKV 965
Cdd:PRK01156 368 YLKSIESLKKKIEEYSKNIERMSAF---ISEILKIQEIDPDAIKKELNEI 414
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
724-934 |
2.35e-03 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 42.15 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 724 LEADLRSAQDELAAVNTRLTGIRDELKNIDKQTKEIQPKLRTAKNELNQLQRQmstletvvnraedrifatfcrrigVDN 803
Cdd:COG5283 5 LGAVDKPFKSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTK------------------------YNK 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 804 IREYEERQVRLMERQSDARLQFESQLARLNHQANFERQQIESTQERLETIRQAiareneklrswQAQKQGKQEELEGMLE 883
Cdd:COG5283 61 LRQSLQRLRQALDQAGIDTRQLSAAQRRLRSSLEQTNRQLERQQQRLARLGAR-----------QDRLKAARARLQRLAG 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2528757163 884 EVS-----------------ELQAQLSELQTQNEAKKVTLEEKrvELQKAARlldSLSKEIAARNDEI 934
Cdd:COG5283 130 AGAaaaaigaalaasvkpaiDFEDAMADVAATVDLDKSSEQFK--ALGKQAR---ELSAQTPQSADDI 192
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
728-954 |
2.57e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 41.60 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 728 LRSAQDELAAVNTRLTGIRDELKNIDKQTKEIQPKLRTAKNELNQLQRQMSTLETVVNRAEDRIfatfcRRIGVD-NIRE 806
Cdd:pfam04108 23 LEELVVLLAKIAFLRRGLSVQLANLEKVREGLEKVLNELKKDFKQLLKDLDAALERLEETLDKL-----RNTPVEpALPP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 807 YEERQVRL-----MERQSDARLQFESQLARLN-HQANFErQQIESTQERLETIRQAIARENEKLRSwQAQKQGKQEELEG 880
Cdd:pfam04108 98 GEEKQKTLldfidEDSVEILRDALKELIDELQaAQESLD-SDLKRFDDDLRDLQKELESLSSPSES-ISLIPTLLKELES 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2528757163 881 MLEE-VSELQAQLSELQTQNEAKKVTLEEKRVELQ---KAARLLDSLSKEIAARNDEIEGLgSERASIYRRCRLEEIT 954
Cdd:pfam04108 176 LEEEmASLLESLTNHYDQCVTAVKLTEGGRAEMLEvleNDARELDDVVPELQDRLDEMENN-YERLQKLLEQKNSLID 252
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
824-940 |
2.61e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 824 QFESQLARLNHQANFERQQIESTQERLETIRQAIAR---ENEKLRSWQAQKQGKQEELEGML----EEVSELQAQLSELQ 896
Cdd:PRK09039 57 RLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAaeaERSRLQALLAELAGAGAAAEGRAgelaQELDSEKQVSARAL 136
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2528757163 897 TQNEAKKVTLEEKRVELQKAARLLDSLSKEIAARNDEIEGLGSE 940
Cdd:PRK09039 137 AQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRR 180
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
817-947 |
2.70e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 817 RQSDARLQ-F--ESQLARLNHQANFERQQIESTQERLETIRQAIARENEKLRSWQAQKQGKQEELEGMLE--EVSELQAQ 891
Cdd:COG3206 192 EEAEAALEeFrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQ 271
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2528757163 892 LSELQTQNEAKKVTLEEKRVELQKAARLLDSLSKEIAARNDEI-EGLGSERASIYRR 947
Cdd:COG3206 272 LAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIlASLEAELEALQAR 328
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
824-953 |
2.76e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 824 QFESQLARLNHQANFERQQIESTQERLETIRQAIARENEKLRSWQAQKQGKQEELEGMLEEVSELQAQLSELQTQNEAKK 903
Cdd:COG4372 56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLE 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2528757163 904 VTLEEKRVELQKAARLLDSLSKEIAARNDEIEGLGSERASIYRRCRLEEI 953
Cdd:COG4372 136 AQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
273-526 |
2.77e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 273 RTEHKKAEDAVLRARRDQGQTQTEILQVE----KSIKSKQRDVEDLRPTLDAYEEKIAISRKKLDngarmtEQVERdLAK 348
Cdd:PRK02224 469 TIEEDRERVEELEAELEDLEEEVEEVEERleraEDLVEAEDRIERLEERREDLEELIAERRETIE------EKRER-AEE 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 349 QQANLAKLERDRETVQRAADRAAQEQQRALESAGLTlsEADLGEyhnlkAQANLEAVAERQELDGLKRDARikaDAVKDF 428
Cdd:PRK02224 542 LRERAAELEAEAEEKREAAAEAEEEAEEAREEVAEL--NSKLAE-----LKERIESLERIRTLLAAIADAE---DEIERL 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 429 QDKSEQFSKQKDKLKDEESTLSERHSALEAKRNqiDTDLQAARDELKRTqakQTAINQRETKLN------DTLQvcyNKL 502
Cdd:PRK02224 612 REKREALAELNDERRERLAEKRERKRELEAEFD--EARIEEAREDKERA---EEYLEQVEEKLDelreerDDLQ---AEI 683
|
250 260
....*....|....*....|....*...
gi 2528757163 503 LQAGNDLKEVE----REAAMKETIAKLQ 526
Cdd:PRK02224 684 GAVENELEELEelreRREALENRVEALE 711
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
686-927 |
3.14e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.42 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 686 EVQGLTTQRDKCLAELKELQKEKRAFV-SDDEMVAKITRLEADLRSAQDELAAVNTRLTGIRDELKNIDKQTKEIQPKLR 764
Cdd:pfam07888 95 KHEELEEKYKELSASSEELSEEKDALLaQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 765 TAKNELNQLQRQMSTLETvvnraedrifatfcrrigvdnirEYEERQVRLMERQSDArLQFESQLARLNHQANFE----- 839
Cdd:pfam07888 175 QLQAKLQQTEEELRSLSK-----------------------EFQELRNSLAQRDTQV-LQLQDTITTLTQKLTTAhrkea 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 840 -----RQQIESTQERLETIRQAIARENEKLRSWQAQKQGKQEELEGMLEEVSELQAQLSELQTQNEAKKVTLEEKRVELQ 914
Cdd:pfam07888 231 enealLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQ 310
|
250
....*....|....*..
gi 2528757163 915 KAARL----LDSLSKEI 927
Cdd:pfam07888 311 QSAEAdkdrIEKLSAEL 327
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
721-974 |
3.28e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 721 ITRLEADLRSAQDELAAVNTRLTGIRDELKNIDKQTKEIQPKLRTAKNELNQLQRQMSTLETVVNRAEDRIfatfcrrig 800
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL--------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 801 vdnireyeerqvrlmerqsdarLQFESQLARLNHQANFERQQIESTQERLETIRQAIARENEKLRSWQAQKQGKQEELEG 880
Cdd:COG4372 97 ----------------------AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 881 MLEEVSELQAQLSELQTQNEAKKVTLEEKRVELQKAARLLDSLSKEIAARNDEIEGLGSERASIYRRCRLEEITLPLLKG 960
Cdd:COG4372 155 LEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
250
....*....|....
gi 2528757163 961 SLAKVGLEETIDVD 974
Cdd:COG4372 235 LSALLDALELEEDK 248
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-525 |
3.41e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1 MPLKRLEIENFKSYRGHQVVGPfNAFTAVIGPNGSGKSNLMDAISFVLgvrSAQLRSSQLKDLIFRGRKmgradDQDDDD 80
Cdd:COG4717 1 MKIKELEIYGFGKFRDRTIEFS-PGLNVIYGPNEAGKSTLLAFIRAML---LERLEKEADELFKPQGRK-----PELNLK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 81 ASGSDDDDLGEGTASKASVTAIYEDGKGYEHRFQ-------------RSITIAGNSEYRYNGRA---IQYAQYNTKLEQF 144
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEeleaeleelreelEKLEKLLQLLPLYQELEaleAELAELPERLEEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 145 NILVKAKNFLVFQGD-VEAVASQGAKELSRLIDQISGSLE-----LKDDYERAKQAQERATDNSTFNFNKRRGINSELKQ 218
Cdd:COG4717 152 EERLEELRELEEELEeLEAELAELQEELEELLEQLSLATEeelqdLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 219 FREQKSEAEKFERLQQERVQHILNHILWRLFHINQDIELNTDFVKTQAKNMRPLrtehkkAEDAVLRARRDQGQTQTEIL 298
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL------LALLFLLLAREKASLGKEAE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 299 QVEKSIKSKQRDVEDLRPTLDAYEEKIAISRKKLdngarmtEQVERDLAKQQANLAKLERDREtvQRAADRAAQEQQRAL 378
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEEL-------LELLDRIEELQELLREAEELEE--ELQLEELEQEIAALL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 379 ESAGLTlSEADLgeyhnlkaQANLEAVAERQELdglkrdarikadaVKDFQDKSEQFSKQKDKLKDEESTLSErhSALEA 458
Cdd:COG4717 377 AEAGVE-DEEEL--------RAALEQAEEYQEL-------------KEELEELEEQLEELLGELEELLEALDE--EELEE 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2528757163 459 KRNQIDTDLQAARDELKRTQAKQTAINQR--ETKLNDTLQVCYNKLLQAGNDLKEVEREAAMKETIAKL 525
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAEleQLEEDGELAELLQELEELKAELRELAEEWAALKLALEL 501
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1136-1204 |
3.73e-03 |
|
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: 40.14 E-value: 3.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2528757163 1136 KRFRDITALSGGEKTMAALALLFAIhsfQPaPFFVLDEVDAALDSQNVAKVSNYIRQHASDQFQFIVIS 1204
Cdd:cd03225 127 LRDRSPFTLSGGQKQRVAIAGVLAM---DP-DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVT 191
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
824-944 |
3.84e-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: 40.29 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 824 QFESQLARLNHQANFERQQIESTQERLETIRQAIARENEKLRSWQAQKQGKQEELEGMLEEVSELQAQLSELQTQNEAKK 903
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEA 93
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2528757163 904 VTLeekrvELQKAARLLDSLSKEIAARNDEIEGLGSERASI 944
Cdd:COG1579 94 LQK-----EIESLKRRISDLEDEILELMERIEELEEELAEL 129
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
149-473 |
4.15e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 149 KAKNFLVFQGDVEAVASQGAKELS-----RLIDQISGSLELKDDYERAKQAQE-RATDNSTFNFNKRRGINSELKQFREQ 222
Cdd:PTZ00121 1261 RMAHFARRQAAIKAEEARKADELKkaeekKKADEAKKAEEKKKADEAKKKAEEaKKADEAKKKAEEAKKKADAAKKKAEE 1340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 223 KSEAEKFERLQQERVQHILNHILWRlfhiNQDIELNTDFVKTQAKNMRPLRTEHKKAEDAVLRARRDQGQTQteilQVEK 302
Cdd:PTZ00121 1341 AKKAAEAAKAEAEAAADEAEAAEEK----AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD----ELKK 1412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 303 SIKSKQRdVEDLRPTldAYEEKIAISRKKLDNGARMTEQVER--DLAKQQANLAKLERDRETVQRAADRA-----AQEQQ 375
Cdd:PTZ00121 1413 AAAAKKK-ADEAKKK--AEEKKKADEAKKKAEEAKKADEAKKkaEEAKKAEEAKKKAEEAKKADEAKKKAeeakkADEAK 1489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 376 RALESAGLTLSEADLGEYHNLKAQANLEAVAERQELDGLKRDARIKADAVKDFQD--------KSEQFSKQKDKLKDEES 447
Cdd:PTZ00121 1490 KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEkkkadelkKAEELKKAEEKKKAEEA 1569
|
330 340
....*....|....*....|....*.
gi 2528757163 448 TLSERHSALEAKRNQIDTDLQAARDE 473
Cdd:PTZ00121 1570 KKAEEDKNMALRKAEEAKKAEEARIE 1595
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
681-942 |
4.56e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 681 RWEEREVQGLTTQRDKCLAELKELQKEKRAFVSDD--EMVAKITRLEADLRSAQDELAAVNTRLTGIRDELKNIDKQTKE 758
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLslATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 759 IQPKLRTAkNELNQLQRQMSTLET-----VVNRAEDRIFATFCRRIGV-------------------DNIREYEERQVRL 814
Cdd:COG4717 232 LENELEAA-ALEERLKEARLLLLIaaallALLGLGGSLLSLILTIAGVlflvlgllallflllarekASLGKEAEELQAL 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 815 MERQSDARLQFESQLARLNHQANFERQQIESTQERLETIRQAIARENEKLRSWQ-----------------------AQK 871
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQleeleqeiaallaeagvedeeelRAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 872 QGKQEELEGMLEEVSELQAQLSEL---------QTQNEAKKVTLEEKRVELQKAARLLDSLSKEIAARNDEIEGLGSERA 942
Cdd:COG4717 391 LEQAEEYQELKEELEELEEQLEELlgeleelleALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE 470
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1133-1197 |
4.57e-03 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 40.08 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1133 PPMKRFRD---------------ITALSGGEKTMAALallfaIHSFQPAP-FFVLDEVDAALDSQNVAKVSNYIRQHASD 1196
Cdd:PRK10247 112 PDPAIFLDdlerfalpdtiltknIAELSGGEKQRISL-----IRNLQFMPkVLLLDEITSALDESNKHNVNEIIHRYVRE 186
|
.
gi 2528757163 1197 Q 1197
Cdd:PRK10247 187 Q 187
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
684-931 |
4.62e-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: 41.31 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 684 EREVQGLTTQRDKCLAELKELQKEKRAFVSDDEMVAKITRLEADLRSAQDELAAvntRLTGIRDELKNI----DKQTKEI 759
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRA---RLAARKQELEEIlhelESRLEEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 760 QPKLRTAKNELNQLQRQMSTLETVVNRAEDRIFATFCRRIGVDNIREYEERQVRLMERQSDA----RLQFESQLARLNHQ 835
Cdd:pfam01576 88 EERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKlskeRKLLEERISEFTSN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 836 ANFERQQIESTQERLETIRQAIARENEKLRSWQAQKQgKQEELEGMLE-EVSELQAQLSELQTQNEAKKVTLEEKRVELQ 914
Cdd:pfam01576 168 LAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQ-ELEKAKRKLEgESTDLQEQIAELQAQIAELRAQLAKKEEELQ 246
|
250
....*....|....*..
gi 2528757163 915 KAarlLDSLSKEIAARN 931
Cdd:pfam01576 247 AA---LARLEEETAQKN 260
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
774-876 |
4.63e-03 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 40.80 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 774 QRQMS-TLETVVNRAEDRIFAtfcrrigVDNIREYEERQVRLMERQSDARLQFESQLARLNHQANFERQQIESTQERLET 852
Cdd:smart00435 268 QRTVSkTHEKSMEKLQEKIKA-------LKYQLKRLKKMILLFEMISDLKRKLKSKFERDNEKLDAEVKEKKKEKKKEEK 340
|
90 100
....*....|....*....|....
gi 2528757163 853 IRQAIARENEKLRSWQAQKQGKQE 876
Cdd:smart00435 341 KKKQIERLEERIEKLEVQATDKEE 364
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1116-1204 |
4.81e-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: 38.97 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1116 IENTEEPYLGGITysvVPPMKRFRDITALSGGEKTMAALALLFaihsFQPAPFFVLDEVDAALDSQNVAKVSNYIRQHAS 1195
Cdd:cd03221 46 IAGELEPDEGIVT---WGSTVKIGYFEQLSGGEKMRLALAKLL----LENPNLLLLDEPTNHLDLESIEALEEALKEYPG 118
|
....*....
gi 2528757163 1196 DqfqFIVIS 1204
Cdd:cd03221 119 T---VILVS 124
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
295-483 |
5.04e-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: 39.91 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 295 TEILQVEKSIKSKQRDVEDLRPTLDAYEEKIaisrkkldngarmtEQVERDLAKQQANLAKLERDRETVQRAADRaaqeq 374
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARL--------------EAAKTELEDLEKEIKRLELEIEEVEARIKK----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 375 qralesagltlSEADLGEYHNLKAQANLEavaerQELDGLKRDARIKADAVKDFQDKSEQFSKQKDKLKDEESTLSERHS 454
Cdd:COG1579 78 -----------YEEQLGNVRNNKEYEALQ-----KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE 141
|
170 180
....*....|....*....|....*....
gi 2528757163 455 ALEAKRNQIDTDLQAARDELKRTQAKQTA 483
Cdd:COG1579 142 EKKAELDEELAELEAELEELEAEREELAA 170
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
700-922 |
5.55e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 700 ELKELQKEKRAFVSD--DEMVAKITRLEADLRSAQDELAAVNtrltgirdelKNIDKQTKEIQpKLRTAKNelnQLQRQM 777
Cdd:PHA02562 206 EQRKKNGENIARKQNkyDELVEEAKTIKAEIEELTDELLNLV----------MDIEDPSAALN-KLNTAAA---KIKSKI 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 778 STLETVVNRAEDRIFATFCRRigvdNIREYEERQVRLMERQSDARLQFE------SQLARLNHQANFERQQIESTQERLE 851
Cdd:PHA02562 272 EQFQKVIKMYEKGGVCPTCTQ----QISEGPDRITKIKDKLKELQHSLEkldtaiDELEEIMDEFNEQSKKLLELKNKIS 347
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2528757163 852 TIRQAIARENEKLRSWQAQKQGKQEELEGMLEEVSELQAQLSELQTqneaKKVTLEEKRVELQKAARLL-DS 922
Cdd:PHA02562 348 TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVK----TKSELVKEKYHRGIVTDLLkDS 415
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
329-538 |
5.65e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 329 RKKLDNGARMTEQVERDLAKQQANLAKLERDRETVQRAADRAAQEQQRALESAGLTLSEADLgeyhnlkAQANLEAVAER 408
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQL-------AEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 409 QELDGLKRDARIKADAVKD------FQDKSEQFSKQKDKLKDEESTLSERHSALEAKRNQIDT-----------DLQAAR 471
Cdd:COG3206 240 ARLAALRAQLGSGPDALPEllqspvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAAlraqlqqeaqrILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2528757163 472 DELKRTQAKQTAINQRETKLNDTLQvcynKLLQAGNDLKEVEREAAMKETI----------AKLQRIFPGVRGRVVD 538
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLA----ELPELEAELRRLEREVEVARELyesllqrleeARLAEALTVGNVRVID 392
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
824-908 |
6.07e-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: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 824 QFESQLARLNHQAN-FERQQIESTQERLETIRQAIARENEKLRS----WQAQK------QGKQEELEGMLEEVSELQAQL 892
Cdd:COG0542 415 ELERRLEQLEIEKEaLKKEQDEASFERLAELRDELAELEEELEAlkarWEAEKelieeiQELKEELEQRYGKIPELEKEL 494
|
90
....*....|....*.
gi 2528757163 893 SELQTQNEAKKVTLEE 908
Cdd:COG0542 495 AELEEELAELAPLLRE 510
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1144-1194 |
6.58e-03 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 39.40 E-value: 6.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2528757163 1144 LSGGEKTMAALALLFAIHsfqpAPFFVLDEVDAALDSQNVAKVSNYIRQHA 1194
Cdd:cd03231 126 LSAGQQRRVALARLLLSG----RPLWILDEPTTALDKAGVARFAEAMAGHC 172
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-56 |
6.71e-03 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 39.14 E-value: 6.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2528757163 13 SYRGHQVVG------PFNAFTAVIGPNGSGKSNLMDAISFVLGVRSAQLR 56
Cdd:NF040873 1 GYGGRPVLHgvdltiPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR 50
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
288-516 |
6.90e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.45 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 288 RDQGQT-QTEILQVEKSIKSKQRDVEDLRPTLDAYEEKIAISRKKLDNGARMTEQVERDLAKQQANLAKLERDRETVQR- 365
Cdd:PRK11637 46 RDQLKSiQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERl 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 366 ------AADRaaQEQQRALEsagLTLSeadlGEyhnlkaqanleavaERQeldglkRDARIKADavkdFQDKSEQFSKQK 439
Cdd:PRK11637 126 laaqldAAFR--QGEHTGLQ---LILS----GE--------------ESQ------RGERILAY----FGYLNQARQETI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 440 DKLKDEESTLSERHSALEAKRNQIDT----------DLQAARDELKRT-----------QAKQTAINQRETKLNDtlqvc 498
Cdd:PRK11637 173 AELKQTREELAAQKAELEEKQSQQKTllyeqqaqqqKLEQARNERKKTltglesslqkdQQQLSELRANESRLRD----- 247
|
250
....*....|....*....
gi 2528757163 499 ynKLLQAGNDLKE-VEREA 516
Cdd:PRK11637 248 --SIARAEREAKArAEREA 264
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
816-917 |
6.94e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.71 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 816 ERQSDARLQFESQLARLNHQANFERQQIESTQERLEtirqaiaRENEKLRSWQAQKQgkqeELEgmlEEVSELQAQLSEL 895
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAE-------AQQQELVALEGLAA----ELE---EKQQELEAQLEQL 203
|
90 100
....*....|....*....|..
gi 2528757163 896 QTQNEAKKVTLEEKRVELQKAA 917
Cdd:PRK11448 204 QEKAAETSQERKQKRKEITDQA 225
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
1139-1192 |
8.35e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 36.83 E-value: 8.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2528757163 1139 RDITALSGGEK-TMAALALLFAI-------HSFQPAP-FFVLDEVDAALDSQNVAKVSNYIRQ 1192
Cdd:pfam13558 28 RRSGGLSGGEKqLLAYLPLAAALaaqygsaEGRPPAPrLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
745-898 |
8.83e-03 |
|
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: 40.42 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 745 IRDELKN----IDKQTKEIQPKLRTAKNELNQLQRQMSTLETVVNRAedrifatfcrrIGVDNIREYEERQVRLMERQSD 820
Cdd:TIGR01612 1116 IKDDIKNldqkIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKA-----------ISNDDPEEIEKKIENIVTKIDK 1184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 821 ARLQFESQLARLNHQANFERQQieSTQERLETIRQAIARENEKLRSWQAQKQGKQEE-----LEGMLEEVSELQAQLSEL 895
Cdd:TIGR01612 1185 KKNIYDEIKKLLNEIAEIEKDK--TSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEhmikaMEAYIEDLDEIKEKSPEI 1262
|
...
gi 2528757163 896 QTQ 898
Cdd:TIGR01612 1263 ENE 1265
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
813-944 |
9.12e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 813 RLMERQSDARLQFESQLARLNHQANFERQQIESTQERLETIRQAIARENEKLRSWQAQKQGKQEELEGMLEEVSELQAQL 892
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2528757163 893 SELQTQNEAKKVTLEEKRVELQKAARLLDSLSKEIAARNDEIEGLGSERASI 944
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL 134
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
700-1202 |
9.42e-03 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 40.10 E-value: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 700 ELKELQKE-KRAFVSDDEMVAKITRLEADLRSAQDELAAVNTRLTGIRDELKNIDKQTKEIQPKLRTAKNE-LNQLQRQM 777
Cdd:COG4694 107 EIEELEKEiEDLKKELDKLEKELKEAKKALEKLLEDLAKSIKDDLKKLFASSGRNYRKANLEKKLSALKSSsEDELKEKL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 778 STLETVVNRAEDRIFAtfcrrigVDNIREYEERQVRLMERQ--SDARLQFESQLARLNHQA------NFERQQIEST--- 846
Cdd:COG4694 187 KLLKEEEPEPIAPITP-------LPDLKALLSEAETLLEKSavSSAIEELAALIQNPGNSDwveqglAYHKEEEDDTcpf 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 847 ------QERLETIRQAIARENEKLrswqaqkqgkQEELEGMLEEVSELQAQLSELQTQNEAKKvtLEEKRVELQKAARLL 920
Cdd:COG4694 260 cqqelaAERIEALEAYFDDEYEKL----------LAALKDLLEELESAINALSALLLEILRTL--LPSAKEDLKAALEAL 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 921 DSLSKEIAARNDEIEGLGSERASIYRRCRLEEITLPLlkgslakVGLEETIDvdapmdiddDDNTQKplsapdfgiqVDF 1000
Cdd:COG4694 328 NALLETLLAALEEKIANPSTSIDLDDQELLDELNDLI-------AALNALIE---------EHNAKI----------ANL 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1001 SSLDDEAKEDGGASMGNELQTRIESITAEIEKMSPNMKAVERLDDTEAKLAETEKEFDRSRRQAKEARDEFNRIKKRrcd 1080
Cdd:COG4694 382 KAEKEEARKKLEAHELAELKEDLSRYKAEVEELIEELKTIKALKKALEDLKTEISELEAELSSVDEAADEINEELKA--- 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 1081 lfnsaFnhiskmidptykdlsrskaapmgGSAYLSIENTEEpylGGITYSVVPPMKRFRDI-TALSGGEKTmaALALLFA 1159
Cdd:COG4694 459 -----L-----------------------GFDEFSLEAVED---GRSSYRLKRNGENDAKPaKTLSEGEKT--AIALAYF 505
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2528757163 1160 IHSFQPAPFF------VLDEVDAALDSQNVAKVSNYIRQHASDQFQFIV 1202
Cdd:COG4694 506 LAELEGDENDlkkkivVIDDPVSSLDSNHRFAVASLLKELSKKAKQVIV 554
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
717-935 |
9.45e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 40.13 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 717 MVAKITRLEADLRSAQDElAAVNTRLTGIRDELKNIDKQT-KEIQPKLRTAKNELNQLQrqMSTLETVVNRAEDRIFATF 795
Cdd:pfam09731 224 LPEHLDNVEEKVEKAQSL-AKLVDQYKELVASERIVFQQElVSIFPDIIPVLKEDNLLS--NDDLNSLIAHAHREIDQLS 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 796 CRRIGVDnIREYEERQVRLMERQSDARLQFESQLARLNHQANFERQQIESTQER-LETIRQAIareNEKLRswqAQKQGK 874
Cdd:pfam09731 301 KKLAELK-KREEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEReREEIRESY---EEKLR---TELERQ 373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2528757163 875 QEELEGMLEEVSELQAQLSELQTQNEAKKVTLEEKRVELQKAARL---LDSLSKEIAARNDEIE 935
Cdd:pfam09731 374 AEAHEEHLKDVLVEQEIELQREFLQDIKEKVEEERAGRLLKLNELlanLKGLEKATSSHSEVED 437
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
705-954 |
9.46e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 705 QKEKRAFVSDDE----MVAKITRLEaDLRSAQDELAAVNTRLTGIRDELKNIDKQTKEIQPKLRTAKNELNQLQRQMSTL 780
Cdd:PRK03918 134 QGEIDAILESDEsrekVVRQILGLD-DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 781 EtvvnraedrifatfcrrigvDNIREYEErQVRLMERqsdarlqfesqlarlnhqanfERQQIESTQERLETIRQAIARE 860
Cdd:PRK03918 213 S--------------------SELPELRE-ELEKLEK---------------------EVKELEELKEEIEELEKELESL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 861 NEKLRSWQAQKQGKQEELEGMLEEVSELQAQLSELQTQNEAKKV------TLEEKRVELQKAARLLDSLSKEIAARNDEI 934
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiklseFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
250 260
....*....|....*....|
gi 2528757163 935 EGLGSERAsiyrrcRLEEIT 954
Cdd:PRK03918 331 KELEEKEE------RLEELK 344
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
26-45 |
9.94e-03 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 39.33 E-value: 9.94e-03
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
748-917 |
9.98e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 9.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 748 ELKNIDKQTKEIQPKLRTAKNELNQLQRQMSTLETVVNRAEDRifATFCRRIGVDNIREYEERQVRLMERQ-SDARLQFE 826
Cdd:PRK04863 436 TADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQA--YQLVRKIAGEVSRSEAWDVARELLRRlREQRHLAE 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528757163 827 SQLARLNHQANFERQQIEstQERLETIRQAIARENEKLRSWQAQKQGKQEELEGMLEEVSELQAQLSELQTQNEAKKVTL 906
Cdd:PRK04863 514 QLQQLRMRLSELEQRLRQ--QQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQL 591
|
170
....*....|.
gi 2528757163 907 EEKRVELQKAA 917
Cdd:PRK04863 592 QARIQRLAARA 602
|
|
| |
