|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
93-1328 |
1.09e-95 |
|
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: 335.40 E-value: 1.09e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 93 ILNIYVENFKSYAgKHILGPFHKNLTMILGPNGSGKSNVIDALLFVFGFKAGK-IRTKKLSALINSGG--NYESCSVTIM 169
Cdd:pfam02463 2 LKRIEIEGFKSYA-KTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKsLRSERLSDLIHSKSgaFVNSAEVEIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 170 FQmvkdmpveNYDKYEVLTDNCVCITRTINRENNSKYRIDDKDASQKDVQELLLRAGIDMTHNRFLILQGEVEAIALMKP 249
Cdd:pfam02463 81 FD--------NEDHELPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 250 TSKNPNEEGMLEYIEDIVGTNRFVAPISKLMHRVSLLEHKSS---QYGASVRRHEGHLKVFEKAMVIGMAYLN-TFNNLN 325
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEElklQELKLKEQAKKALEYYQLKEKLELEEEYlLYLDYL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 326 YLRGIRVKHNLCRYAETMRDAKMSLVTRTGELEENKDIMLEAKDEVRKKETHERSLNSIVTELENKRIDWQSKKNDwHAR 405
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERR-KVD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 406 DAKRKQGLKSctqDLGKLMKERDEARREKFEIETAPENARISKQNMQLEWDQLKEQENVCQRTATENLIKYDQKSSADRA 485
Cdd:pfam02463 312 DEEKLKESEK---EKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 486 KHDDLEKKLSDELLQSMRAKAELDVSESELKDMTIMMEQGQKRVDELKGTLQTMMAENIRDNTELNAVTTELQDRKLKFD 565
Cdd:pfam02463 389 AAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 566 KAVEKLPHLKSTEQLLRSKKYELDQEVIEASNTQ-EVTYRHQATAKLHELKEAGLFPGFKGRLGDLASIPIKFDTAISTV 644
Cdd:pfam02463 469 KSEDLLKETQLVKLQEQLELLLSRQKLEERSQKEsKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTA 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 645 FFAQLDYHVVQTSDECRIGIGFCHEYKLPRTTFVFLDHLKDTDTSgmDSTMKFPAERLFDKIHCVNPEIRREFYFLIHDI 724
Cdd:pfam02463 549 VIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKS--IAVLEIDPILNLAQLDKATLEADEDDKRAKVVE 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 725 LVVDSLEEATRIDKKYP---GRHRYCTLNGSILNRSGALTGGGKPTTGRIRNDnnpnmsgVKKVDLSKLRAAQEKHNHAL 801
Cdd:pfam02463 627 GILKDTELTKLKESAKAkesGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQ-------ELQEKAESELAKEEILRRQL 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 802 EAHLKLQLKQEEIRADNGPIIKQLEIRKRELimsTKEQKTRIAELKSSIAAHERRMVNYREVTVEDLDEKRAQIADLKRQ 881
Cdd:pfam02463 700 EIKKKEQREKEELKKLKLEAEELLADRVQEA---QDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKEL 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 882 -VEESQKSSAKIKQQIEQYKRKMDRMFMELVQKNKDSIEQAKDRMGQLEQDIARQTAIIENNPSHLEQAEKKLSELEHMC 960
Cdd:pfam02463 777 aEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEEL 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 961 LEKRSEADALAQLEVGEDVKGIDIINAQLQTSTASIDAQRARYTEAVAARREADAAYQTTVDNYNMVKQTYDELMRIIDD 1040
Cdd:pfam02463 857 ERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEE 936
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 1041 LENKTMADNAELDIIESawmqpeklyppgkfvryndpdiaakmtdghvvlpyecismiepHREAYEEHEARMLEddvfed 1120
Cdd:pfam02463 937 PEELLLEEADEKEKEEN-------------------------------------------NKEEEEERNKRLLL------ 967
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 1121 tanKICKLEKDVDKFRREFDNKGVRDYAmiVSLLMNEVTSAKKfsDKLKAHREKLNElrmaRFNEFSEALAFLGTTTQML 1200
Cdd:pfam02463 968 ---AKEELGKVNLMAIEEFEEKEERYNK--DELEKERLEEEKK--KLIRAIIEETCQ----RLKEFLELFVSINKGWNKV 1036
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 1201 YQLITNGGDASLKFVEEGkstDPFDGGIKFSVRPAKKSWKLIENLSGGEKTLASLCFVFAMHHYRPTPLYVMDEIDAALD 1280
Cdd:pfam02463 1037 FFYLELGGSAELRLEDPD---DPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALD 1113
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....*...
gi 17552844 1281 LNNVSLIANYIKhsERTRNAQFIIISLRNQMFEVGNRLLGIYKIDGKT 1328
Cdd:pfam02463 1114 DQNVSRVANLLK--ELSKNAQFIVISLREEMLEKADKLVGVTMVENGV 1159
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
93-1321 |
5.32e-75 |
|
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: 273.48 E-value: 5.32e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 93 ILNIYVENFKSYAGKHILgPFHKNLTMILGPNGSGKSNVIDALLFVFGFKAGK-IRTKKLSALINSGGNYES---CSVTI 168
Cdd:TIGR02169 2 IERIELENFKSFGKKKVI-PFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKaMRAERLSDLISNGKNGQSgneAYVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 169 MFqmvkdmpveNYDKYEVLTDNCVCITRTINREN-NSKYRIDDKDASQKDVQELLLRAGIDMTHNRFlILQGEVEAIALM 247
Cdd:TIGR02169 81 TF---------KNDDGKFPDELEVVRRLKVTDDGkYSYYYLNGQRVRLSEIHDFLAAAGIYPEGYNV-VLQGDVTDFISM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 248 KPTSKNpneegmlEYIEDIVGTNRFVAPISKLMHRVSLLEHKSSQYGASVRRHEGHLKVFEKAMVIGMAYLNTFNNLNYL 327
Cdd:TIGR02169 151 SPVERR-------KIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 328 RGIRVKHNLcryaETMRDAKMSLVTRTGELEENKDIMLEAKDEVRKK-ETHERSLNSIVTEL----ENKRIDWQSKKNDW 402
Cdd:TIGR02169 224 EGYELLKEK----EALERQKEAIERQLASLEEELEKLTEEISELEKRlEEIEQLLEELNKKIkdlgEEEQLRVKEKIGEL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 403 HARDAKRKQGLKSCTQDLGKLMK-------ERDEARREKFEIETAPENARISKQNMQLEWDQLKEQENVCQRTATEnlik 475
Cdd:TIGR02169 300 EAEIASLERSIAEKERELEDAEErlakleaEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE---- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 476 YDQKSSADRAKHDDLEKKLSD------ELLQSM-RAKAELDVSESELKDMTIMMEQGQKRVDELKGTLQTMMAEnirdnt 548
Cdd:TIGR02169 376 VDKEFAETRDELKDYREKLEKlkreinELKRELdRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE------ 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 549 eLNAVTTELQDRKLKFDKAVEKLPHLKSTEQLLRSKKYELDQEVIEASNTQEVTYRHQATAK-LHELKEAGLfPGFKGRL 627
Cdd:TIGR02169 450 -IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRaVEEVLKASI-QGVHGTV 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 628 GDLASIPIKFDTAISTVFFAQLDYHVVQTSDECRIGIGFCHEYKLPRTTFVFLDHLKDTDTSGMDSTMKFPAERLFDKIH 707
Cdd:TIGR02169 528 AQLGSVGERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVE 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 708 CvNPEIRREFYFLIHDILVVDSLEEAtridKKYPGRHRYCTLNGSILNRSGALTGGGKPTTGRIrndnnpnmsgvkkvdl 787
Cdd:TIGR02169 608 F-DPKYEPAFKYVFGDTLVVEDIEAA----RRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGI---------------- 666
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 788 skLRAAQEKHnhaleahlklqlKQEEIRADngpiIKQLEIRKRELIMSTKEQKTRIAELKSSIAAHERRMVNyREVTVED 867
Cdd:TIGR02169 667 --LFSRSEPA------------ELQRLRER----LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGE-IEKEIEQ 727
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 868 LDEKRAQiadLKRQVEESQKSSAKIKQQIEQYKRKMDRMFMELVQKNKDsIEQAKDRMGQLEQDIARQtaIIENNPSHLE 947
Cdd:TIGR02169 728 LEQEEEK---LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED-LHKLEEALNDLEARLSHS--RIPEIQAELS 801
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 948 QAEKKLSELEHMC------LEKRSEADALAQLEVGEDVKGIDIINAQLQTSTASIDAQRARYTEAVAARREADAAYQTTV 1021
Cdd:TIGR02169 802 KLEEEVSRIEARLreieqkLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE 881
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 1022 DNYNMVKQTYDELMRIIDDLENKTMADNAELDIIESawmqpeklyppgkfvryNDPDIAAKMTdghvVLPYECISMIEPH 1101
Cdd:TIGR02169 882 SRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK-----------------RLSELKAKLE----ALEEELSEIEDPK 940
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 1102 REAYEEHEARMLEDDVFEdtanKICKLEKDVDKFRrEFDNKGVRDYAmIVSLLMNEVTSAKkfsDKLKAHREKLnELRMA 1181
Cdd:TIGR02169 941 GEDEEIPEEELSLEDVQA----ELQRVEEEIRALE-PVNMLAIQEYE-EVLKRLDELKEKR---AKLEEERKAI-LERIE 1010
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 1182 RFNE-----FSEALAFLGTTTQMLYQLItNGGDASLkfVEEGKStDPFDGGIKFSVRPAKKSWKLIENLSGGEKTLASLC 1256
Cdd:TIGR02169 1011 EYEKkkrevFMEAFEAINENFNEIFAEL-SGGTGEL--ILENPD-DPFAGGLELSAKPKGKPVQRLEAMSGGEKSLTALS 1086
|
1210 1220 1230 1240 1250 1260
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17552844 1257 FVFAMHHYRPTPLYVMDEIDAALDLNNVSLIANYIKhsERTRNAQFIIISLRNQMFEVGNRLLGI 1321
Cdd:TIGR02169 1087 FIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIR--EKAGEAQFIVVSLRSPMIEYADRAIGV 1149
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
95-1321 |
3.57e-67 |
|
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: 249.20 E-value: 3.57e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 95 NIYVENFKSYAGKHILgPFHKNLTMILGPNGSGKSNVIDALLFVFG-FKAGKIRTKKLSALINSGGN----YESCSVTIM 169
Cdd:TIGR02168 4 KLELAGFKSFADPTTI-NFDKGITGIVGPNGCGKSNIVDAIRWVLGeQSAKALRGGKMEDVIFNGSEtrkpLSLAEVELV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 170 FqmvkdmpvENYDKYEVLTDNC-VCITRTINRENNSKYRIDDKDASQKDVQELLLRAGIdmTHNRF-LILQGEVEAIALM 247
Cdd:TIGR02168 83 F--------DNSDGLLPGADYSeISITRRLYRDGESEYFINGQPCRLKDIQDLFLDTGL--GKRSYsIIEQGKISEIIEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 248 KPtsknpneEGMLEYIEDIVGtnrfvapISKLmhrvsllehkssqygaSVRRHEGHLKVFEkamvigmaylnTFNNLNYL 327
Cdd:TIGR02168 153 KP-------EERRAIFEEAAG-------ISKY----------------KERRKETERKLER-----------TRENLDRL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 328 RGI-----RVKHNLCRYAET----------MRDAKMSL-VTRTGELEENKD-IMLEAKDEVRKKETHERSLNSIVTELEN 390
Cdd:TIGR02168 192 EDIlneleRQLKSLERQAEKaerykelkaeLRELELALlVLRLEELREELEeLQEELKEAEEELEELTAELQELEEKLEE 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 391 KRIDWQSKKNDWHARDAK--RKQGLKS-CTQDLGKLMKERDEARREKFEIETAPENARISKQNMQLEWDQLKEQENVCQ- 466
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKElyALANEISrLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKe 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 467 -RTATENLIK--------YDQKSSADRAKHDDLEKKLSDELLQSMRAKAELDVSESELKDMTIMMEQGQKRVDELKGTLQ 537
Cdd:TIGR02168 352 eLESLEAELEeleaeleeLESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 538 TMMAENIRdnTELNAVTTELQDRKLKFDKAVEKLPHLKSTEQLLRSKKYELDQEVIEASNTQEVTYRHQ------ATAKL 611
Cdd:TIGR02168 432 EAELKELQ--AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQenlegfSEGVK 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 612 HELKEAGLFPGFKGRLGDLASIPIKFDTAISTVFFAQLDYHVVQTSDECRIGIGFCHEYKLPRTTFVFLDHLKDTD--TS 689
Cdd:TIGR02168 510 ALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEiqGN 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 690 GMDSTMKFPAERLFDKIHC-VNPEIRREFYFLIHDILVVDSLEEATRIDKKYPGRHRYCTLNGSILNRSGALTGGGKPTT 768
Cdd:TIGR02168 590 DREILKNIEGFLGVAKDLVkFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTN 669
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 769 GRIRNDNNpnmsgvKKVDLSKLRAAQEKHNHALEAHLK-LQLKQEEIRADngpiIKQLEIRKRELIMSTKEQKTRIAELK 847
Cdd:TIGR02168 670 SSILERRR------EIEELEEKIEELEEKIAELEKALAeLRKELEELEEE----LEQLRKELEELSRQISALRKDLARLE 739
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 848 SSIAAHERRmVNYREVTVEDLDEKRAQIADlkrQVEESQKSSAKIKQQIEQYKRKMDRmFMELVQKNKDSIEQAKDRMGQ 927
Cdd:TIGR02168 740 AEVEQLEER-IAQLSKELTELEAEIEELEE---RLEEAEEELAEAEAEIEELEAQIEQ-LKEELKALREALDELRAELTL 814
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 928 LEQDIARQTAIIENNPSHLEQAEKKLSELEHMcLEKRSEADALAQLEVGEDVKGIDIINAQLQtstaSIDAQRARYTEAV 1007
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQ-IEELSEDIESLAAEIEELEELIEELESELE----ALLNERASLEEAL 889
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 1008 AARREAdaayqttvdnynmvkqtYDELMRIIDDLENKTMADNAEL----DIIESAWMQPEKLyppgKFVRYNdpdIAAKM 1083
Cdd:TIGR02168 890 ALLRSE-----------------LEELSEELRELESKRSELRRELeelrEKLAQLELRLEGL----EVRIDN---LQERL 945
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 1084 TDGHVVLpyecismiephreaYEEHEARMLEDDVFEDtankicKLEKDVDKFRREFDNKGVrdyamiVSLL-MNEVTSAK 1162
Cdd:TIGR02168 946 SEEYSLT--------------LEEAEALENKIEDDEE------EARRRLKRLENKIKELGP------VNLAaIEEYEELK 999
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 1163 KFSDKLKAHREKLNELR------MARFNE-----FSEALAFLGTTTQMLYQLITNGGDASLKFVEEgksTDPFDGGIKFS 1231
Cdd:TIGR02168 1000 ERYDFLTAQKEDLTEAKetleeaIEEIDRearerFKDTFDQVNENFQRVFPKLFGGGEAELRLTDP---EDLLEAGIEIF 1076
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 1232 VRPAKKSWKLIENLSGGEKTLASLCFVFAMHHYRPTPLYVMDEIDAALDLNNVSLIANYIKH-SERTrnaQFIIISLRNQ 1310
Cdd:TIGR02168 1077 AQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFANLLKEfSKNT---QFIVITHNKG 1153
|
1290
....*....|.
gi 17552844 1311 MFEVGNRLLGI 1321
Cdd:TIGR02168 1154 TMEVADQLYGV 1164
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1235-1331 |
9.71e-53 |
|
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: 184.42 E-value: 9.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 1235 AKKSWKLIENLSGGEKTLASLCFVFAMHHYRPTPLYVMDEIDAALDLNNVSLIANYIKhsERTRNAQFIIISLRNQMFEV 1314
Cdd:cd03274 118 PKKSWKNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIK--ERTKNAQFIVISLRNNMFEL 195
|
90
....*....|....*..
gi 17552844 1315 GNRLLGIYKIDGKTYNI 1331
Cdd:cd03274 196 ADRLVGIYKTNNCTKSV 212
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
91-1321 |
1.73e-47 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 185.53 E-value: 1.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 91 MIILNIYVENFKSYAGKHILgPFHKNLTMILGPNGSGKSNVIDALLFVFG---FKAgkIRTKKLSALINSGGNY----ES 163
Cdd:COG1196 1 MRLKRLELAGFKSFADPTTI-PFEPGITAIVGPNGSGKSNIVDAIRWVLGeqsAKS--LRGGKMEDVIFAGSSSrkplGR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 164 CSVTIMFqmvkdmpvENYDKYEVLTDNCVCITRTINRENNSKYRIDDKDASQKDVQELLLRAGI--DMtHNrfLILQGEV 241
Cdd:COG1196 78 AEVSLTF--------DNSDGTLPIDYDEVTITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLgpES-YS--IIGQGMI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 242 EAIALMKPtsknpnEEgMLEYIEDIVGtnrfvapISKL-----------------MHRVSLLEHkssqygaSVRRHEGHL 304
Cdd:COG1196 147 DRIIEAKP------EE-RRAIIEEAAG-------ISKYkerkeeaerkleateenLERLEDILG-------ELERQLEPL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 305 K----VFEKAMVI--------GMAYLNTFNNLNyLRGIRVKHNLCRYAETMRDAKMSLVTRTGELEENKDIMLEAKDEVR 372
Cdd:COG1196 206 ErqaeKAERYRELkeelkeleAELLLLKLRELE-AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 373 KKETHERSLNSIVTELENKRIDWQSKKNDWHARDAKRKQGLKSCTQDLGKLMKERDEARREKFEIETAPENARISKQNMQ 452
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 453 LEWDQLKEQENVCQRTATENLIKY---DQKSSADRAKHDDLEKKLSDELLQSMRAKAELDVSESELkdmtimmEQGQKRV 529
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELleaLRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL-------AELEEEE 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 530 DELKGTLQTMMAENIRDNTELNAVTTELQDRKLKFDKAVEKLPHLKSTEQLLRSKKYELDQevieasntQEVTYRHQATA 609
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE--------AEADYEGFLEG 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 610 KLHELKEAGLfPGFKGRLGDLASIPIKFDTAISTVFFAQLDYHVVQTSDECRIGIGFCHEYKLPRTTFVFLDHLKDTDTS 689
Cdd:COG1196 510 VKAALLLAGL-RGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAAL 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 690 GmDSTMKFPAERLFDKIHCVnPEIRREFYFLIHDILVVDSLEEATRIDkkypGRHRYCTLNGSILNRSGALTGGgkpttg 769
Cdd:COG1196 589 A-AALARGAIGAAVDLVASD-LREADARYYVLGDTLLGRTLVAARLEA----ALRRAVTLAGRLREVTLEGEGG------ 656
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 770 rirndnnpNMSGVKKVDLSKLRAAQEKHNHALEAHLKLQLKQEEIRAdngpiiKQLEIRKRELIMSTKEQKTRIAELKSS 849
Cdd:COG1196 657 --------SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL------EEALLAEEEEERELAEAEEERLEEELE 722
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 850 IAAHERRMVNYREVTVEDLDEKRAQIADLKRQVEESQKSSAKIKQQIEQYKRKMDRMfmELVqkNKDSIEQakdrmgqle 929
Cdd:COG1196 723 EEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL--GPV--NLLAIEE--------- 789
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 930 qdiarqtaiiennpshLEQAEKKLSELehmclekrseadalaqlevgedvkgidiinaqlqtstasiDAQRARYTEAVaa 1009
Cdd:COG1196 790 ----------------YEELEERYDFL----------------------------------------SEQREDLEEAR-- 811
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 1010 rreadaayqttvdnynmvkqtyDELMRIIDDLENKTmadnaeldiiesawmqpeklyppgkfvryndpdiaakmtdghvv 1089
Cdd:COG1196 812 ----------------------ETLEEAIEEIDRET-------------------------------------------- 825
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 1090 lpyecismiephREayeehearmleddVFEDTANKIcklekdvdkfRREFdnkgvrdyamivsllmnevtsakkfsdklk 1169
Cdd:COG1196 826 ------------RE-------------RFLETFDAV----------NENF------------------------------ 840
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 1170 ahreklnelrmarfnefsealaflgtttQMLYQLITNGGDASLKFVEEGkstDPFDGGIKFSVRPAKKSWKLIENLSGGE 1249
Cdd:COG1196 841 ----------------------------QELFPRLFGGGEAELLLTDPD---DPLETGIEIMAQPPGKKLQRLSLLSGGE 889
|
1210 1220 1230 1240 1250 1260 1270
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17552844 1250 KTLASLCFVFAMHHYRPTPLYVMDEIDAALDLNNVSLIANYIKhsERTRNAQFIIISLRNQMFEVGNRLLGI 1321
Cdd:COG1196 890 KALTALALLFAIFRLNPSPFCVLDEVDAPLDDANVERFAELLK--EMSEDTQFIVITHNKRTMEAADRLYGV 959
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
91-247 |
3.22e-47 |
|
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: 168.24 E-value: 3.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 91 MIILNIYVENFKSYAGKHILGPFHKNLTMILGPNGSGKSNVIDALLFVFGFKAGKIRTKKLSALINSGGNY---ESCSVT 167
Cdd:cd03274 1 LIITKLVLENFKSYAGEQVIGPFHKSFSAIVGPNGSGKSNVIDSMLFVFGFRASKMRQKKLSDLIHNSAGHpnlDSCSVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 168 IMFQMVKDMPvenydkyevltdncvcitrtinrennskyriddkdasqkdvqeLLLRAGIDMTHNRFLILQGEVEAIALM 247
Cdd:cd03274 81 VHFQEIIDKP-------------------------------------------LLKSKGIDLDHNRFLILQGEVEQIAQM 117
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
93-252 |
7.52e-34 |
|
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: 131.16 E-value: 7.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 93 ILNIYVENFKSYAGKHILGPFHKnLTMILGPNGSGKSNVIDALLFVFGFKAGKIRTKKLSALINSG----GNYESCSVTI 168
Cdd:cd03275 1 LKRLELENFKSYKGRHVIGPFDR-FTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYRArvgkPDSNSAYVTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 169 MFQmvkdmpvenYDKYEVLTdncvcITRTInRENNSKYRIDDKDASQKDVQELLLRAGIDMTHNRFLILQGEVEAIALMK 248
Cdd:cd03275 80 VYE---------DDDGEEKT-----FRRII-TGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESIASKN 144
|
....
gi 17552844 249 PTSK 252
Cdd:cd03275 145 PPGK 148
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1234-1323 |
1.02e-29 |
|
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: 119.21 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 1234 PAKKSWKLIENLSGGEKTLASLCFVFAMHHYRPTPLYVMDEIDAALDLNNVSLIANYIKHSeRTRNAQFIIISLRNQMFE 1313
Cdd:cd03275 145 PPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQ-AGPNFQFIVISLKEEFFS 223
|
90
....*....|
gi 17552844 1314 VGNRLLGIYK 1323
Cdd:cd03275 224 KADALVGVYR 233
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1245-1328 |
1.10e-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: 111.25 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 1245 LSGGEKTLASLCFVFAMHHYRPTPLYVMDEIDAALDLNNVSLIANYIKhSERTRNAQFIIISLRNQMFEVGNRLLGIYKI 1324
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIK-EMAKHTSQFIVITLKKEMFENADKLIGVLFV 173
|
....
gi 17552844 1325 DGKT 1328
Cdd:cd03239 174 HGVS 177
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1234-1321 |
1.70e-25 |
|
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: 105.24 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 1234 PAKKSwKLIENLSGGEKTLASLCFVFAMHHYRPTPLYVMDEIDAALDLNNVSLIANYIKhsERTRNAQFIIISLRNQMFE 1313
Cdd:cd03278 104 PGKKV-QRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLK--EFSKETQFIVITHRKGTME 180
|
....*...
gi 17552844 1314 VGNRLLGI 1321
Cdd:cd03278 181 AADRLYGV 188
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
620-736 |
2.48e-25 |
|
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: 101.95 E-value: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 620 FPGFKGRLGDLASIPIKFDTAISTVFFAQLDYHVVQTSDECRIGIGFCHEYKLPRTTFVFLDHLKDTDTSGMDSTMKFpA 699
Cdd:pfam06470 1 LKGVLGRLADLIEVDEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRLKPRPRRPGADLKGG-A 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 17552844 700 ERLFDKIHCvNPEIRREFYFLIHDILVVDSLEEATRI 736
Cdd:pfam06470 80 GPLLDLVEY-DDEYRKALRYLLGNTLVVDDLDEALEL 115
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
621-736 |
2.57e-22 |
|
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: 93.45 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 621 PGFKGRLGDLASIPIKFDTAISTVFFAQLDYHVVQTSDECRIGIGFCHEYKLPRTTFVFLDHLKDTDTSG-----MDSTM 695
Cdd:smart00968 1 PGVLGRVADLISVDPKYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPRSPAGsklreALLPE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 17552844 696 KFPAERLFDKIHCvNPEIRREFYFLIHDILVVDSLEEATRI 736
Cdd:smart00968 81 PGFVGPAIDLVEY-DPELRPALEYLLGNTLVVDDLETARRL 120
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1239-1328 |
2.99e-21 |
|
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: 94.67 E-value: 2.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 1239 WK--LIEnLSGGEKTLASLCFVFAMHHYRPTPLYVMDEIDAALDLNNVSLIANYIKhsERTRNAQFIIISLRNQMFEVGN 1316
Cdd:cd03273 160 WKesLTE-LSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIK--THFKGSQFIVVSLKEGMFNNAN 236
|
90
....*....|..
gi 17552844 1317 RLLGIYKIDGKT 1328
Cdd:cd03273 237 VLFRTRFVDGTS 248
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
93-171 |
1.16e-19 |
|
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: 88.13 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 93 ILNIYVENFKSYAGKHILGPFHKnLTMILGPNGSGKSNVIDALLFVFGFKAGKIRTKKLSALINSGG--NYESCSVTIMF 170
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSNS-FNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAGGGVkaGINSASVEITF 79
|
.
gi 17552844 171 Q 171
Cdd:cd03239 80 D 80
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
91-241 |
1.15e-18 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 87.35 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 91 MIILNIYVENFKSYAGKHILGPFHKNLTMILGPNGSGKSNVIDALLFVFGF-KAGKIRTKKLSALINSGGN--YESCSVT 167
Cdd:cd03273 1 MHIKEIILDGFKSYATRTVISGFDPQFNAITGLNGSGKSNILDAICFVLGItNLSTVRASNLQDLIYKRGQagITKASVT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17552844 168 IMFqmvkdmpvENYDK--YEVLTDNC--VCITRTINRENNSKYRIDDKDASQKDVQELLLRAGIDMTHNRFLILQGEV 241
Cdd:cd03273 81 IVF--------DNSDKsqSPIGFENYpeITVTRQIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRI 150
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1245-1330 |
2.32e-18 |
|
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: 83.95 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 1245 LSGGEKTLASLCFVFAMHHYRPTPLYVMDEIDAALDLNNVSLIANYIKHSeRTRNAQFIIISLRNQMFEVGNRLLGIYKI 1324
Cdd:cd03227 78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEH-LVKGAQVIVITHLPELAELADKLIHIKKV 156
|
....*.
gi 17552844 1325 DGKTYN 1330
Cdd:cd03227 157 ITGVYK 162
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
96-170 |
6.28e-17 |
|
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: 80.59 E-value: 6.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 96 IYVENFKSYAGKHILgPFHKNLTMILGPNGSGKSNVIDALLFVFGFKAGK-IRTKKLSALINSGGNYES----CSVTIMF 170
Cdd:cd03278 4 LELKGFKSFADKTTI-PFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKsLRGEKMSDVIFAGSETRKpanfAEVTLTF 82
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
93-248 |
1.15e-15 |
|
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: 78.07 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 93 ILNIYVENFKSYAGKHILGPFHKNLTMILGPNGSGKSNVIDALLFVFGFKAGKIRTKKLSALIN--SGGNYESCSVTIMF 170
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEPFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALLHegSGPSVMSAYVEIIF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17552844 171 qmvkdmpvENYDKYEVLTDNCVCITRTINRENNsKYRIDDKDASQKDVQELLLRAGIDMTHNRFLILQGEVEAIALMK 248
Cdd:cd03272 81 --------DNSDNRFPIDKEEVRLRRTIGLKKD-EYFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMK 149
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1242-1321 |
1.38e-15 |
|
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: 78.07 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 1242 IENLSGGEKTLASLCFVFAMHHYRPTPLYVMDEIDAALDLNNVSLIANYIKhsERTRNAQFIIISLRNQMFEVGNRLLGI 1321
Cdd:cd03272 156 MQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIK--ELSDGAQFITTTFRPELLEVADKFYGV 233
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
92-171 |
7.40e-13 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 68.88 E-value: 7.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 92 IILNIYVENFKSYAGKHILgPFHKNLTMILGPNGSGKSNVIDALLFVFGFKAGKiRTKKLSALINSGGnyESCSVTIMFQ 171
Cdd:COG0419 1 KLLRLRLENFRSYRDTETI-DFDDGLNLIVGPNGAGKSTILEAIRYALYGKARS-RSKLRSDLINVGS--EEASVELEFE 76
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
96-171 |
1.51e-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: 64.30 E-value: 1.51e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17552844 96 IYVENFKSYAGKHILGPFHKNLTMILGPNGSGKSNVIDALLFVFGFKAGKIRTKKLSALinsggNYESCSVTIMFQ 171
Cdd:cd03227 2 IVLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKA-----GCIVAAVSAELI 72
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
96-252 |
1.01e-09 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 59.43 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 96 IYVENFKSYAGKHIlgPFHKNLTMILGPNGSGKSNVIDALLFVFGFKAGKIRTKKLSALINS-----GGNYESCSVTIMF 170
Cdd:pfam13476 1 LTIENFRSFRDQTI--DFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGdirigLEGKGKAYVEITF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 171 QMVKDMPVENydkyevltdncVCITRTINRENNSKYR-----IDDKDASQKDVQELLLRAGIDMthNRFLILQGEVEAIA 245
Cdd:pfam13476 79 ENNDGRYTYA-----------IERSRELSKKKGKTKKkeileILEIDELQQFISELLKSDKIIL--PLLVFLGQEREEEF 145
|
....*..
gi 17552844 246 LMKPTSK 252
Cdd:pfam13476 146 ERKEKKE 152
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
824-1039 |
8.87e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 60.03 E-value: 8.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 824 QLEIRKRELIMSTKEQKTRIAELKSSIAAHERRMVNYREVT-VEDLDEKR----AQIADLKRQVEESQKSSAKIKQQIEQ 898
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNgLVDLSEEAklllQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 899 YKRKMDRMFMELVQKNKDS-IEQAKDRMGQLEQDIARQTAII-ENNPShLEQAEKKLSELEHMcLEKRSEAdALAQLEVg 976
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPvIQQLRAQLAELEAELAELSARYtPNHPD-VIALRAQIAALRAQ-LQQEAQR-ILASLEA- 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17552844 977 edvkGIDIINAQLQTSTASIDAQRARYTEAVAARREADAA---YQTTVDNYNMVKQTYDELM----------RIID 1039
Cdd:COG3206 321 ----ELEALQAREASLQAQLAQLEARLAELPELEAELRRLereVEVARELYESLLQRLEEARlaealtvgnvRVID 392
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
113-249 |
1.07e-08 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (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 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 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: 213208 [Multi-domain] Cd Length: 276 Bit Score: 57.98 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 113 FHKNLTMILGPNGSGKSNVIDALLFVFGFKAGK--IRTKKLSALIN---SGGNYEscsvtimfqMVKDMPVENYDkyevL 187
Cdd:cd03241 19 FEEGLTVLTGETGAGKSILLDALSLLLGGRASAdlIRSGAEKAVVEgvfDISDEE---------EAKALLLELGI----E 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17552844 188 TDNCVCITRTINRENNSKYRIDDKDASQKDVQELLlragidmthNRFLILQGEVEAIALMKP 249
Cdd:cd03241 86 DDDDLIIRREISRKGRSRYFINGQSVTLKLLRELG---------SLLVDIHGQHDHQNLLNP 138
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
837-1018 |
4.43e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.15 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 837 KEQKTRIAELKSSIAAHERRMVNYR---EVTVEDLDEKRAQIADLKRQVEESQKSSAKIKQQIEQYKRKMDRMfMELVQK 913
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQaelEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER-ARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 914 NK------------DSIEQAKDRMGQLEQDIARQTAIIENnpshLEQAEKKLSELEHMCLEKRSEADALAQlEVGEDVKG 981
Cdd:COG3883 98 SGgsvsyldvllgsESFSDFLDRLSALSKIADADADLLEE----LKADKAELEAKKAELEAKLAELEALKA-ELEAAKAE 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 17552844 982 IDIINAQLQTSTASIDAQRARYTEAVAARREADAAYQ 1018
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
822-1016 |
4.63e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 55.70 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 822 IKQLEIRKRELimstkeqKTRIAELKSSIAAHERRMVNYRevtvEDLDEKRAQIADLKRQVEESQkssakikQQIEQYKR 901
Cdd:COG1579 19 LDRLEHRLKEL-------PAELAELEDELAALEARLEAAK----TELEDLEKEIKRLELEIEEVE-------ARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 902 KMDRmfmelVQKNKDS------IEQAKDRMGQLEQDIARQTAIIENNPSHLEQAEKKLSELEHMCLEKRSEADAlaqlEV 975
Cdd:COG1579 81 QLGN-----VRNNKEYealqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE----EL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17552844 976 GEDVKGIDIINAQLQTSTASIDAQ-RARYtEAVAARREADAA 1016
Cdd:COG1579 152 AELEAELEELEAEREELAAKIPPElLALY-ERIRKRKNGLAV 192
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
806-1043 |
6.10e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 6.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 806 KLQLKQEEIRadngpiikQLEIRKRELIMSTKEQKTRIAELKSSIAAHER-RMVNYREVTVEDLDEKRAQIADLKRQVEE 884
Cdd:COG4913 611 KLAALEAELA--------ELEEELAEAEERLEALEAELDALQERREALQRlAEYSWDEIDVASAEREIAELEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 885 SQKSSAKIKQQIEQYKRKMDRmfmelvqkNKDSIEQAKDRMGQLEQDIARQTAIIENNPSHLEQAEKKLSELEHMCLEKR 964
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEE--------LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 965 SEADALAQLEvgedvkgiDIINAQLQTSTASIDAQRAR-YTEAVAARREADAAYQTTVDNYNMVKQTYDELMRIIDDLEN 1043
Cdd:COG4913 755 FAAALGDAVE--------RELRENLEERIDALRARLNRaEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEE 826
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
91-170 |
7.70e-08 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 55.39 E-value: 7.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 91 MIILNIYVENFKSYAGKHILGPFHKNLTMILGPNGSGKSNVIDALLFVFGFKAGKIRTKKLSALINSGGNYESCSVTIMF 170
Cdd:COG3950 1 MRIKSLTIENFRGFEDLEIDFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNGEFGDSAKLILY 80
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
788-1015 |
1.04e-07 |
|
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: 56.44 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 788 SKLRAAQEKHNHALEAHLKLQLKQEEIRADNGPIIKQleirKRELIMSTKEQKTRIAELKSSIAAHERRMVNyREVTVED 867
Cdd:pfam07888 80 SRVAELKEELRQSREKHEELEEKYKELSASSEELSEE----KDALLAQRAAHEARIRELEEDIKTLTQRVLE-RETELER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 868 LDEKRAQIADLKRQVEESQKSSAKIKQQIEQYKRKMDRMFmelvQKNKDSIEQAKDRMGQLEQDIARQTaiiennpSHLE 947
Cdd:pfam07888 155 MKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF----QELRNSLAQRDTQVLQLQDTITTLT-------QKLT 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17552844 948 QAEKKLSELEHMCLEKRSEADALAQLEVGEDVKGIDIINAQLQTSTASIDAQRARYTEAVAARREADA 1015
Cdd:pfam07888 224 TAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADA 291
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
93-138 |
1.49e-07 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 55.32 E-value: 1.49e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 17552844 93 ILNIYVENFKSYAGKHI-LGPfhknLTMILGPNGSGKSNVIDALLFV 138
Cdd:COG4637 2 ITRIRIKNFKSLRDLELpLGP----LTVLIGANGSGKSNLLDALRFL 44
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
93-192 |
3.33e-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: 52.61 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 93 ILNIYVENFKSYAGKHILgPFHKNLTMILGPNGSGKSNVIDALLFV-FGFKA-GKIRTKKLSALINSGGNyeSCSVTIMF 170
Cdd:cd03240 1 IDKLSIRNIRSFHERSEI-EFFSPLTLIVGQNGAGKTTIIEALKYAlTGELPpNSKGGAHDPKLIREGEV--RAQVKLAF 77
|
90 100
....*....|....*....|..
gi 17552844 171 QMVKDMPVENYDKYEVLtDNCV 192
Cdd:cd03240 78 ENANGKKYTITRSLAIL-ENVI 98
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
93-158 |
5.34e-07 |
|
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: 51.83 E-value: 5.34e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17552844 93 ILNIYVENFKSYagKHILGPFHKNLTMILGPNGSGKSNVIDALLFVFGFKAGKI-RTKKLSALINSG 158
Cdd:cd03277 3 IVRIKLENFVTY--DETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLGGKPKLLgRAKKVGEFVKRG 67
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
91-140 |
6.45e-07 |
|
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: 53.47 E-value: 6.45e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 17552844 91 MIILNIYVENFKSYAGKHIlgPFHKNLTMILGPNGSGKSNVIDALLFVFG 140
Cdd:COG3593 1 MKLEKIKIKNFRSIKDLSI--ELSDDLTVLVGENNSGKSSILEALRLLLG 48
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
822-1016 |
1.06e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 822 IKQLEIRKRELIMSTKEQKTRIAELKSSIAAHERRMVNYRE---VTVEDLDEKRAQIADLKRQVEESQKSSAKIKQQIEQ 898
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARrirALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 899 YKRKMDRM---------------------------FMELVQKNKDSIEQAKDRMGQLEQDIARQTAIIENNPSHLEQAEK 951
Cdd:COG4942 109 LLRALYRLgrqpplalllspedfldavrrlqylkyLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17552844 952 KLSElehmclEKRSEADALAQLEvgEDVKGIDIINAQLQTSTASIDAQRARYTEAVAARREADAA 1016
Cdd:COG4942 189 ALEA------LKAERQKLLARLE--KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
794-1039 |
1.35e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 53.30 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 794 QEKHNHALEAHLKLQLKQEEIRADNGPIIKQLEIR-------KRELIMSTKEQKTRIAELKSSIAAHERRMVNYR-EVTV 865
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERqetsaelNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRsELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 866 EDLDEKRAQIADLKR-------------QVEESQKSSAKIKQQIEQYKRKMDRMFMELVQKNKDSIEQAKDRMGQLEQDI 932
Cdd:pfam12128 327 LEDQHGAFLDADIETaaadqeqlpswqsELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 933 ARQTAIIENnpsHLEQAEKKL-SELEHMCLEKRSEA---------------------DALAQLEVGEDVkgIDIINAQLQ 990
Cdd:pfam12128 407 DRQLAVAED---DLQALESELrEQLEAGKLEFNEEEyrlksrlgelklrlnqatatpELLLQLENFDER--IERAREEQE 481
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 17552844 991 TSTASI-DAQRARyTEAVAARREADAAYQTTVDNYNMVKQTYDELMRIID 1039
Cdd:pfam12128 482 AANAEVeRLQSEL-RQARKRRDQASEALRQASRRLEERQSALDELELQLF 530
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
91-247 |
1.47e-06 |
|
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: 52.22 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 91 MIILNIYVENFKSYAGKHIlgPFHKNLTMILGPNGSGKSNVIDALLFVFGFKAGKIRTKKLSALINSGGNYESCSVTIMF 170
Cdd:pfam13175 1 MKIKSIIIKNFRCLKDTEI--DLDEDLTVLIGKNNSGKSSILEALDIFLNNKEKFFEDDFLVLYLKDVIKIDKEDLNIFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 171 QMVKDMPVENYDKYEVLTDNCVCITRTINRE---NNSKYRIDDKDASQKDVQELLLRAGIDMTHNRFLILQGEVEAIALM 247
Cdd:pfam13175 79 NISFSIDIEIDVEFLLILFGYLEIKKKYLCLaskGKAKEYEKTLHPKGANKADLLLELKISDLKKYLKQFKIYIYNNYYL 158
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
93-168 |
1.60e-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: 1.60e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17552844 93 ILNIYVENFKSYAGKHI-LGPfhkNLTMILGPNGSGKSNVIDALLFVFGFKAGKI-RTKKLSALINSGGNYESCSVTI 168
Cdd:cd03276 1 IESITLKNFMCHRHLQIeFGP---RVNFIVGNNGSGKSAILTALTIGLGGKASDTnRGSSLKDLIKDGESSAKITVTL 75
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
788-957 |
2.15e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 788 SKLRAAQEKHNHALEAHLKLQLKQEEIRAdngpiiKQLEIRKRELIMSTKEQKTRIAELKSSIAAHERRMVNYREVtVED 867
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEE------LEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPER-LEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 868 LDEKRAQIADLKRQVEEsqkssakIKQQIEQYKRKMDRMFMELVQKNKDSIEQAKDRMGQLEQDIARQTAIIENNPSHLE 947
Cdd:COG4717 151 LEERLEELRELEEELEE-------LEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|
gi 17552844 948 QAEKKLSELE 957
Cdd:COG4717 224 ELEEELEQLE 233
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1218-1306 |
2.49e-06 |
|
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: 48.78 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 1218 GKST---------DPFDGGIKFS-VRPAKKSWKLIEN-------LSGGEKTLASLCFVFAmhhYRPtPLYVMDEIDAALD 1280
Cdd:cd00267 37 GKSTllraiagllKPTSGEILIDgKDIAKLPLEELRRrigyvpqLSGGQRQRVALARALL---LNP-DLLLLDEPTSGLD 112
|
90 100
....*....|....*....|....*.
gi 17552844 1281 LNNVSLIANYIKHsERTRNAQFIIIS 1306
Cdd:cd00267 113 PASRERLLELLRE-LAEEGRTVIIVT 137
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
92-222 |
5.36e-06 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 50.54 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 92 IILNIYVENFKSYAGKHIlgPFHKNLTMILGPNGSGKSNVIDAlLFVFGFkaGK-IRTKKLSALINSGGnyESCSVTIMF 170
Cdd:COG1195 1 RLKRLSLTNFRNYESLEL--EFSPGINVLVGPNGQGKTNLLEA-IYLLAT--GRsFRTARDAELIRFGA--DGFRVRAEV 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 17552844 171 QmvkdmpvENYDKYEVLTdncvcitrTINRENNSKYRIDDKDA-SQKDVQELL 222
Cdd:COG1195 74 E-------RDGREVRLGL--------GLSRGGKKRVRINGKPVrRLSDLAGLL 111
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1245-1338 |
6.02e-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: 48.75 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 1245 LSGGEKTLASLCFVFAMHHYRPTPLYVMDEIDAALD-LNNVSLIANYIKHSERTRNAQFIIISLRNqMFEVGNrllgiyk 1323
Cdd:cd03276 110 LSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDmVNRKISTDLLVKEAKKQPGRQFIFITPQD-ISGLAS------- 181
|
90
....*....|....*
gi 17552844 1324 IDGKTYNIMVDPIAV 1338
Cdd:cd03276 182 SDDVKVFRMKDPRGP 196
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
866-1074 |
7.69e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 7.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 866 EDLDEKRAQIADLKRQVEESQKSSAKIKQQIEQYKRKMDRMFMEL------VQKNKDSIEQAKDRMGQLEQDIARQTAII 939
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIraleqeLAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 940 EN------------------NPSHLEQAEKKLSELEHMCLEKRSEADALAQL--EVGEDVKGIDIINAQLQTSTASIDAQ 999
Cdd:COG4942 107 AEllralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADlaELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17552844 1000 RARYTEAVAARREADAAYQTTVDNYnmvKQTYDELMRIIDDLEnktmadnAELDIIESAWMQPEKLYPPGKFVRY 1074
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAEL---AAELAELQQEAEELE-------ALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
865-1012 |
1.07e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 865 VEDLDEKRAQIADLKRQVEEsqkssakIKQQIEQYKRKMDRMfmELVQKNKDSIEQAKDRMGQLEQDIARQTAIIENNPS 944
Cdd:PRK02224 467 VETIEEDRERVEELEAELED-------LEEEVEEVEERLERA--EDLVEAEDRIERLEERREDLEELIAERRETIEEKRE 537
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17552844 945 HLEQAEKKLSELEHMCLEKRSEADAlAQLEVGEDVKGIDIINAQLQTSTASID---------AQRARYTEAVAARRE 1012
Cdd:PRK02224 538 RAEELRERAAELEAEAEEKREAAAE-AEEEAEEAREEVAELNSKLAELKERIEslerirtllAAIADAEDEIERLRE 613
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
772-1064 |
1.39e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 772 RNDNNPNMSGVKKVDLSKLRAAQEKHNHALEAHLKlQLKQEEIRADNGPIIKQLEIRKRElimstkEQKTRIAELKSSIA 851
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK-KMKAEEAKKAEEAKIKAEELKKAE------EEKKKVEQLKKKEA 1643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 852 AHERRMVNYREVTvedlDEKRAQIADLKRQVEESQKSSAKIKQQIEQYKRKMDRMFMELVQKNKdsIEQAKDRMGQLEQD 931
Cdd:PTZ00121 1644 EEKKKAEELKKAE----EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK--AEELKKKEAEEKKK 1717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 932 IARQTAIIENNPSHLEQAEKKLSELEHMCLEKR---SEADALAQLEVGEDVKGIDIINAQLQTSTASIDaqraryTEAVA 1008
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKkdeEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD------EEDEK 1791
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17552844 1009 ARREADAAYQTTVDNYNMVKQTYDELMRIIDDleNKTMADNAELDIIESAWMQPEK 1064
Cdd:PTZ00121 1792 RRMEVDKKIKDIFDNFANIIEGGKEGNLVIND--SKEMEDSAIKEVADSKNMQLEE 1845
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
787-956 |
1.89e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 787 LSKLRAAQEKHNHALEAHLKLQLKQEEIRADngpiIKQLEIRKRELIMSTKEQKTRIAEL------------------KS 848
Cdd:COG4942 54 LKQLAALERRIAALARRIRALEQELAALEAE----LAELEKEIAELRAELEAQKEELAELlralyrlgrqpplalllsPE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 849 SIAAHERRMVNYREVTVEDldekRAQIADLKRQVEESQKSSAKIKQQIEQYKRKMDRMfmelvQKNKDSIEQAKDRMGQL 928
Cdd:COG4942 130 DFLDAVRRLQYLKYLAPAR----REQAEELRADLAELAALRAELEAERAELEALLAEL-----EEERAALEALKAERQKL 200
|
170 180
....*....|....*....|....*...
gi 17552844 929 EQDIARQTAIIENNPSHLEQAEKKLSEL 956
Cdd:COG4942 201 LARLEKELAELAAELAELQQEAEELEAL 228
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
91-172 |
2.06e-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: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 91 MIILNIYVENFKSYAGKHIL---GPFHKNLTMILGPNGSGKSNVIDALLF-VFGFKAGKIRTKKLSALINSGGNyeSCSV 166
Cdd:cd03279 1 MKPLKLELKNFGPFREEQVIdftGLDNNGLFLICGPTGAGKSTILDAITYaLYGKTPRYGRQENLRSVFAPGED--TAEV 78
|
....*.
gi 17552844 167 TIMFQM 172
Cdd:cd03279 79 SFTFQL 84
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
783-967 |
2.45e-05 |
|
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: 48.97 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 783 KKVDLSKLRaaQEKHNHALEAHLKLQLKQEEIRADNGPIIKQLEIRKRELIMStKEQKTRIAELKSSIAAHERRMVNYRE 862
Cdd:pfam17380 358 RKRELERIR--QEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILE-EERQRKIQQQKVEMEQIRAEQEEARQ 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 863 VTVEDLDEKRAQIADLKRQVE-ESQKSSAKIKQQIEQYKRKmdRMFMELVQKNKDSIEQAKDRMgqLEQDI-ARQTAIIE 940
Cdd:pfam17380 435 REVRRLEEERAREMERVRLEEqERQQQVERLRQQEEERKRK--KLELEKEKRDRKRAEEQRRKI--LEKELeERKQAMIE 510
|
170 180
....*....|....*....|....*..
gi 17552844 941 nnpshlEQAEKKLSELEhmcLEKRSEA 967
Cdd:pfam17380 511 ------EERKRKLLEKE---MEERQKA 528
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
117-326 |
3.62e-05 |
|
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: 47.38 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 117 LTMILGPNGSGKSNVIDALLFVFGFKAGKIRTKKLSALINSGGNYESCSVTIMfqmvKDMPVEnydkyevltdncVCITR 196
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLNGID----PKEPIE------------FEISE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 197 TINRENNSKYRIDDKDasqKDVQELLLRAGIDMTHNRFLILQGEVEAIAlmkptsKNPNEEGMLEYIEDIVGTNRFVAPI 276
Cdd:pfam13304 65 FLEDGVRYRYGLDLER---EDVEEKLSSKPTLLEKRLLLREDSEEREPK------FPPEAEELRLGLDVEERIELSLSEL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17552844 277 SKlmhrvsllEHKSSQYGASVRRHEGHLKVFEKAMVIGMAYLNTFNNLNY 326
Cdd:pfam13304 136 SD--------LISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLAL 177
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
91-161 |
1.31e-04 |
|
recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273173 [Multi-domain] Cd Length: 365 Bit Score: 46.19 E-value: 1.31e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17552844 91 MIILNIYVENFKSYAgkHILGPFHKNLTMILGPNGSGKSNVIDALLFVfgFKAGKIRTKKLSALINSGGNY 161
Cdd:TIGR00611 1 MYLSRLELTDFRNYD--AVDLELSPGVNVIVGPNGQGKTNLLEAIYYL--ALGRSHRTSRDKPLIRFGAEA 67
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
837-1304 |
1.93e-04 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 45.88 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 837 KEQKTRIAELKSSIAAHERRMVNYREvtveDLDEKRAQIADLKRQVEESQKSSAKIKQQIEQYKRKMDRMFMELVQKNKD 916
Cdd:COG4694 102 IELEEEIEELEKEIEDLKKELDKLEK----ELKEAKKALEKLLEDLAKSIKDDLKKLFASSGRNYRKANLEKKLSALKSS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 917 SIEQAKDRMGQLEQDIARQTAIIENNPShLEQAEKKLSELehmcLEKRSEADALAQLEvgEDVKGIDI------------ 984
Cdd:COG4694 178 SEDELKEKLKLLKEEEPEPIAPITPLPD-LKALLSEAETL----LEKSAVSSAIEELA--ALIQNPGNsdwveqglayhk 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 985 -------------INAQLQTS-TASIDAQrarYTEAVAARREADAAYQTTVDNYNMVKQT--YDELMRIIDDLENKTMAD 1048
Cdd:COG4694 251 eeeddtcpfcqqeLAAERIEAlEAYFDDE---YEKLLAALKDLLEELESAINALSALLLEilRTLLPSAKEDLKAALEAL 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 1049 NAELDIIESAWmqPEKLYPPGKFVRYNDPDIAAKMTDghvvlpyecisMIEPHREAYEEHEARmleddvFEDTANKICKL 1128
Cdd:COG4694 328 NALLETLLAAL--EEKIANPSTSIDLDDQELLDELND-----------LIAALNALIEEHNAK------IANLKAEKEEA 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 1129 EKDVDKFRREFDNKGVRDYAMIVSLLMNEVTSAKKFSDKLKAHREKLNELRmarfNEFSEALAFLGTTTQMLYQLitngG 1208
Cdd:COG4694 389 RKKLEAHELAELKEDLSRYKAEVEELIEELKTIKALKKALEDLKTEISELE----AELSSVDEAADEINEELKAL----G 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 1209 DASLKFVEEGkstdpfDGGIKFSV-RPAKKSWKLIENLSGGEKTLASLCFVFAM-----HHYRPTPLYVMDEIdAALDLN 1282
Cdd:COG4694 461 FDEFSLEAVE------DGRSSYRLkRNGENDAKPAKTLSEGEKTAIALAYFLAElegdeNDLKKKIVVIDDPV-SSLDSN 533
|
490 500
....*....|....*....|..
gi 17552844 1283 NVSLIANYIKhSERTRNAQFII 1304
Cdd:COG4694 534 HRFAVASLLK-ELSKKAKQVIV 554
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
783-967 |
1.96e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 783 KKVDLSKLRAAQEKHNHALEAHLKLQLKQEEIRADNGPIiKQLEIRKRELIMSTKEQKTRIAELK--------SSIAAHE 854
Cdd:PRK03918 513 KKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL-EELKKKLAELEKKLDELEEELAELLkeleelgfESVEELE 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 855 RRMVNYREV---------TVEDLDEKRAQIADLKRQVEESQKSSAKIKQQIEQYKRKMDrmfmELVQK-NKDSIEQAKDR 924
Cdd:PRK03918 592 ERLKELEPFyneylelkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE----ELEKKySEEEYEELREE 667
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17552844 925 MGQLEQDIARQTAIIENNPSHLEQAEKKLSELEHMcLEKRSEA 967
Cdd:PRK03918 668 YLELSRELAGLRAELEELEKRREEIKKTLEKLKEE-LEEREKA 709
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1243-1313 |
2.14e-04 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 44.05 E-value: 2.14e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17552844 1243 ENLSGGEKTLASLCFVFAMhhyRPTpLYVMDEIDAALDLNNVSLIANYIKHSeRTRNAQFIIISLRNQMFE 1313
Cdd:cd03217 103 EGFSGGEKKRNEILQLLLL---EPD-LAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLD 168
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
93-137 |
2.89e-04 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 44.60 E-value: 2.89e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 17552844 93 ILNIYVENFKSYAgkHILGPFHKNLTMILGPNGSGKSNVIDALLF 137
Cdd:cd03242 1 LKSLELRNFRNYA--ELELEFEPGVTVLVGENAQGKTNLLEAISL 43
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
91-141 |
2.90e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 44.65 E-value: 2.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 17552844 91 MIIlNIYVENFKSYAGKHIL-----GPFHKNLTMILGPNGSGKSNVIDALLFVFGF 141
Cdd:COG1106 1 MLI-SFSIENFRSFKDELTLsmvasGLRLLRVNLIYGANASGKSNLLEALYFLRNL 55
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
787-955 |
3.72e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 787 LSKLRAAQEKHNHALEAHLKLQLKQEEIR---------ADNGPIIKQLEIRKRELimstKEQKTRIAELKSSIAAHERRM 857
Cdd:COG4717 343 LDRIEELQELLREAEELEEELQLEELEQEiaallaeagVEDEEELRAALEQAEEY----QELKEELEELEEQLEELLGEL 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 858 VNYREVTVED-----LDEKRAQIADLKRQVEESQKSSAKIKQQIEQYKRKmdrmfmELVQKNKDSIEQAKDRMGQLEQDI 932
Cdd:COG4717 419 EELLEALDEEeleeeLEELEEELEELEEELEELREELAELEAELEQLEED------GELAELLQELEELKAELRELAEEW 492
|
170 180
....*....|....*....|...
gi 17552844 933 ARQTAIIEnnpsHLEQAEKKLSE 955
Cdd:COG4717 493 AALKLALE----LLEEAREEYRE 511
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
102-147 |
4.97e-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: 42.23 E-value: 4.97e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 17552844 102 KSYAGKHILGPFHKNL-----TMILGPNGSGKSNVIDALLFVFGFKAGKIR 147
Cdd:cd00267 7 FRYGGRTALDNVSLTLkageiVALVGPNGSGKSTLLRAIAGLLKPTSGEIL 57
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
367-617 |
5.41e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 367 AKDEVRKKETHERSlNSIVTELENKRIDWQSKKndwhARDAKRKQGLKSCTQDLGKLMKERDEARREKFEIETAPENARI 446
Cdd:PTZ00121 1355 AADEAEAAEEKAEA-AEKKKEEAKKKADAAKKK----AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEE 1429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 447 SKQNMQLEwdqlKEQENvcQRTATENLIKYDQKSSADRAKHDDLEKKLSDELLQSMRAKAELDVSESELKDMTIMMEQGQ 526
Cdd:PTZ00121 1430 KKKADEAK----KKAEE--AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK 1503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 527 KRVDELKGTLQTMMAENIRDNTELNAVTTELQDRKLKFDKAVEKLPHLKSTEQLlrsKKYELDQEVIEASNTQEvtYRHQ 606
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL---KKAEEKKKAEEAKKAEE--DKNM 1578
|
250
....*....|.
gi 17552844 607 ATAKLHELKEA 617
Cdd:PTZ00121 1579 ALRKAEEAKKA 1589
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
789-976 |
6.33e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 789 KLRAAQEKHNH-ALEAHLKLQLKQeeiradngpiIKQLEIRKRELIMSTKEQKTRIAELKSSIAAHERRMVNYREVTVed 867
Cdd:COG3206 197 ALEEFRQKNGLvDLSEEAKLLLQQ----------LSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPV-- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 868 LDEKRAQIADLKRQ-VEESQKSSAK------IKQQIEQYKRKMDRMFMELVQKNKDSIEQAKDRMGQLEQDIARQTAIIE 940
Cdd:COG3206 265 IQQLRAQLAELEAElAELSARYTPNhpdviaLRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLA 344
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17552844 941 NNPshleQAEKKLSELEH----------MCLEKRSEADALAQLEVG 976
Cdd:COG3206 345 ELP----ELEAELRRLERevevarelyeSLLQRLEEARLAEALTVG 386
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
784-955 |
6.51e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 784 KVDLSKLRAAQEKHNHaLEAHLKLQLKQEEIRADNGpIIKQLEIRKRELIMSTKEQKTRIAELKSSIAAHE-------RR 856
Cdd:COG4913 268 RERLAELEYLRAALRL-WFAQRRLELLEAELEELRA-ELARLEAELERLEARLDALREELDELEAQIRGNGgdrleqlER 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 857 MVNYREVTVEDLDEKRAQIADLKRQVEESQKSSAK--------IKQQIEQYKRKMDRmFMELVQKNKDSIEQAKDRMGQL 928
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAALGLPLPASAEefaalraeAAALLEALEEELEA-LEEALAEAEAALRDLRRELREL 424
|
170 180
....*....|....*....|....*..
gi 17552844 929 EQDIARQTAIIENNPSHLEQAEKKLSE 955
Cdd:COG4913 425 EAEIASLERRKSNIPARLLALRDALAE 451
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
91-161 |
7.70e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 7.70e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17552844 91 MIILNIYVENFKSYAGKHILgpFHKNLTMILGPNGSGKSNVIDALLF-VFGFKagkiRTKKLSALINSGGNY 161
Cdd:PRK01156 1 MIIKRIRLKNFLSHDDSEIE--FDTGINIITGKNGAGKSSIVDAIRFaLFTDK----RTEKIEDMIKKGKNN 66
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
784-1019 |
8.23e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 43.52 E-value: 8.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 784 KVDLSKLRAAQEKHNHALEA----HLKLQLKQEEIRADNGPIikQLEIRKRELIMSTKEQktRIAELKSSIAAHERRMVN 859
Cdd:pfam19220 26 KADFSQLIEPIEAILRELPQaksrLLELEALLAQERAAYGKL--RRELAGLTRRLSAAEG--ELEELVARLAKLEAALRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 860 YREVTVE---DLDEKRAQIADLKRQVEESqkssakiKQQIEQYKRKMDRMFMELVQKNKDSIE------QAKDRMGQLEQ 930
Cdd:pfam19220 102 AEAAKEElriELRDKTAQAEALERQLAAE-------TEQNRALEEENKALREEAQAAEKALQRaegelaTARERLALLEQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 931 DIARQTAIIENNPSHLEQAEKKLSElehmcLEKRSEAdALAQLEvgedvkgidiinaQLQTSTASIDAQRARyteAVAAR 1010
Cdd:pfam19220 175 ENRRLQALSEEQAAELAELTRRLAE-----LETQLDA-TRARLR-------------ALEGQLAAEQAERER---AEAQL 232
|
....*....
gi 17552844 1011 READAAYQT 1019
Cdd:pfam19220 233 EEAVEAHRA 241
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
783-939 |
1.10e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 783 KKVDLSKLRAAQEKhnhaleahLKLQLKQEEIRADNgpiIKQLEIR--KRELIMSTKEQKTRIAELKSSIAAHERRmVNY 860
Cdd:PRK12704 26 KKIAEAKIKEAEEE--------AKRILEEAKKEAEA---IKKEALLeaKEEIHKLRNEFEKELRERRNELQKLEKR-LLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 861 REvtvEDLDEKRAQIADLKRQVEESQKSSAKIKQQIEQYKRKMDRMFMELVQKNKD----SIEQAKDR-MGQLEQDIARQ 935
Cdd:PRK12704 94 KE---ENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisglTAEEAKEIlLEKVEEEARHE 170
|
....
gi 17552844 936 TAII 939
Cdd:PRK12704 171 AAVL 174
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
91-571 |
1.30e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 91 MIILNIYVENFKSYAGKHIlgPFHKNLTMILGPNGSGKSNVIDALLF-VFGFKAGKIRTKKLSALINSGGNyeSCSVTIM 169
Cdd:PRK03918 1 MKIEELKIKNFRSHKSSVV--EFDDGINLIIGQNGSGKSSILEAILVgLYWGHGSKPKGLKKDDFTRIGGS--GTEIELK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 170 FQmvkdmpvENYDKYEvltdncvcITRTINRENNSKYRIDDKDA---SQKDVQELLLR-AGIDMTHNRFLILQGEVEAIA 245
Cdd:PRK03918 77 FE-------KNGRKYR--------IVRSFNRGESYLKYLDGSEVleeGDSSVREWVERlIPYHVFLNAIYIRQGEIDAIL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 246 lmkptsknPNEEGMLEYIEDIVGTNRFVAPISKLMHRVSLLEHKSSQYGASVRRHEG---HLKVFEKAMVigmAYLNTFN 322
Cdd:PRK03918 142 --------ESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENieeLIKEKEKELE---EVLREIN 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 323 NLNYLRgirvkhnlcryaETMRDAKMSLVTRTGELEENKDIMLEAKDEVRKKETHERSLNSIVTELEnKRIDWQSKKNDW 402
Cdd:PRK03918 211 EISSEL------------PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE-ERIEELKKEIEE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 403 HARDAKRKQGLKSCTQDLGKLMKERDEARREKFEIETAPENARISKQNMQLEWDQLKEQEnvcqrtatENLIKYDQKSSA 482
Cdd:PRK03918 278 LEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE--------ERLEELKKKLKE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 483 DRAKHDDLEKKLsdELLQSMRAK-AELDVSESELKDMTImmEQGQKRVDELKGTLQTMMAENIRDNTELNAVTTELQDRK 561
Cdd:PRK03918 350 LEKRLEELEERH--ELYEEAKAKkEELERLKKRLTGLTP--EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK 425
|
490
....*....|
gi 17552844 562 lkfdKAVEKL 571
Cdd:PRK03918 426 ----KAIEEL 431
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
338-587 |
1.35e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 338 RYAETMRDAKMSLVTRTGELEENKDIMLEAkDEVRKKETHERSLNSIVTELENKRIDWQSKKNDWHARDAKRKQGLKSCT 417
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEEAKIKA-EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 418 QDLGK---LMKERDEARREKFEIETAPENARISKQNMQLEWDQLKEQENVcQRTATENLIKYDQ--------KSSADRAK 486
Cdd:PTZ00121 1672 EDKKKaeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL-KKAEEENKIKAEEakkeaeedKKKAEEAK 1750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 487 HDDLEKKLSDELLQSMRAKAELDVSESELkdmtiMMEQGQKRVDELKGTLQTMMAENIRDNTEL-----NAVTTELQDRK 561
Cdd:PTZ00121 1751 KDEEEKKKIAHLKKEEEKKAEEIRKEKEA-----VIEEELDEEDEKRRMEVDKKIKDIFDNFANiieggKEGNLVINDSK 1825
|
250 260
....*....|....*....|....*.
gi 17552844 562 LKFDKAVEKLPhLKSTEQLLRSKKYE 587
Cdd:PTZ00121 1826 EMEDSAIKEVA-DSKNMQLEEADAFE 1850
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
823-956 |
1.45e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 41.41 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 823 KQLEIRKRELIMSTKEQ--KTR------IAELKSSIAAHERRMVNyREvtvEDLDEKRAQIADLKRQVEESQKSSAKIKQ 894
Cdd:pfam12072 45 KEAETKKKEALLEAKEEihKLRaeaereLKERRNELQRQERRLLQ-KE---ETLDRKDESLEKKEESLEKKEKELEAQQQ 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17552844 895 QIEQYKRKMDRMFMELVQKNKD----SIEQAKDR-MGQLEQDIARQTAI----IENNPShlEQAEKKLSEL 956
Cdd:pfam12072 121 QLEEKEEELEELIEEQRQELERisglTSEEAKEIlLDEVEEELRHEAAVmikeIEEEAK--EEADKKAKEI 189
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
866-1001 |
1.66e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.59 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 866 EDLDEKRAQIADLKRQVEESQKSSAKIKQQIEQYKrkmDRMFMELVQKNKDSIEQAKDRMGQLEQDIARQTAIIENNPSH 945
Cdd:pfam04012 36 SELVKARQALAQTIARQKQLERRLEQQTEQAKKLE---EKAQAALTKGNEELAREALAEKKSLEKQAEALETQLAQQRSA 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 17552844 946 LEQAEKKLSELEHMCLEKRSEADAL-AQLEVGedvkgidIINAQLQTSTASIDAQRA 1001
Cdd:pfam04012 113 VEQLRKQLAALETKIQQLKAKKNLLkARLKAA-------KAQEAVQTSLGSLSTSSA 162
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
328-617 |
1.85e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 328 RGIRVKHNLCRYAETMRDAKMslVTRTGELEENKDImlEAKDEVRKKETHERSLNSIVTELE--NKRIDWQSKKNDWHAR 405
Cdd:PTZ00121 1268 RQAAIKAEEARKADELKKAEE--KKKADEAKKAEEK--KKADEAKKKAEEAKKADEAKKKAEeaKKKADAAKKKAEEAKK 1343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 406 DAKRKQGLKSCTQDLGKLMKERDEARREKFEIETAPENARISKQNMQLEWDQLKEQENVCQRTATENLIKYDQKSSADRA 485
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA 1423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 486 KHDDLEKKLSDELLQSMRAKAELDVSESELKDMTIMMEQGQKRVDELKGTLQTMMAENIRDNTELNAVTTELQDRKLKFD 565
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK 1503
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 17552844 566 KAVE---KLPHLKSTEQLLRS---KKYELDQEVIEASNTQEVTyRHQATAKLHELKEA 617
Cdd:PTZ00121 1504 KAAEakkKADEAKKAEEAKKAdeaKKAEEAKKADEAKKAEEKK-KADELKKAEELKKA 1560
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
852-1041 |
2.25e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 42.32 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 852 AHERRMVNYREVTVEDLDEKRAQIADLKRQVE--ESQKSSA-----KIKQQIEQYKRKMDRMFMELVQKNKDSiEQAKDR 924
Cdd:pfam05701 28 AHRIQTVERRKLVELELEKVQEEIPEYKKQSEaaEAAKAQVleeleSTKRLIEELKLNLERAQTEEAQAKQDS-ELAKLR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 925 MGQLEQDIARQTAIIENnpSHLEQA----EKKLSEL------------EHMCL-------EKRSEADALAQLEVGEDVKG 981
Cdd:pfam05701 107 VEEMEQGIADEASVAAK--AQLEVAkarhAAAVAELksvkeeleslrkEYASLvserdiaIKRAEEAVSASKEIEKTVEE 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17552844 982 IDIinaQLQTSTASIDAQRARYTEAVAARREADAAYQTTVDNY-NMVKQTYDELMRIIDDL 1041
Cdd:pfam05701 185 LTI---ELIATKESLESAHAAHLEAEEHRIGAALAREQDKLNWeKELKQAEEELQRLNQQL 242
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
118-139 |
2.41e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.58 E-value: 2.41e-03
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
872-1056 |
3.03e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 872 RAQIADLKRQVEESQKSSAKIKQQIEQYKRKMDRM------FMELVQKNKDSI--EQAKDRMGQLEQDIARqtaiIENNP 943
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALqerreaLQRLAEYSWDEIdvASAEREIAELEAELER----LDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 944 SHLEQAEKKLSELEHmclEKRSEADALAQLEVGEDVKGIDIINAQLQTSTASIDAQRARYTEAVAARREADAAYQtTVDN 1023
Cdd:COG4913 685 DDLAALEEQLEELEA---ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFA-AALG 760
|
170 180 190
....*....|....*....|....*....|...
gi 17552844 1024 YNMVKQTYDELMRIIDDLENKtmADNAELDIIE 1056
Cdd:COG4913 761 DAVERELRENLEERIDALRAR--LNRAEEELER 791
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
1246-1306 |
3.54e-03 |
|
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: 40.66 E-value: 3.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17552844 1246 SGGEKTLASLCFVFAMHHYRPTPLYVMDEIDAALDLNNVSLIANYI-KHSERTRNAQFIIIS 1306
Cdd:cd03277 128 SGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLvETACKEGTSQYFLIT 189
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
96-138 |
3.66e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 41.11 E-value: 3.66e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 17552844 96 IYVENFKSYAGKHI-LGPfhknLTMILGPNGSGKSNVIDALLFV 138
Cdd:COG4938 4 ISIKNFGPFKEAELeLKP----LTLLIGPNGSGKSTLIQALLLL 43
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
866-1042 |
3.75e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.86 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 866 EDLDEKRAQIADLKRQVEESQKSSAKIKQQIEQYKRKMD------------------------RMFMELVQKNKDSIEQA 921
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQllnkllpqanlladetladrleelREELDAAQEAQAFIQQH 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 922 KDRMGQLEqdiaRQTAIIENNPSHLEQAEKKLSELEHMCLEKRSEADALAQLEVGEDVKGIDIINAQLQTSTASIDAQRA 1001
Cdd:COG3096 916 GKALAQLE----PLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLLGENSDLNEKLRA 991
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17552844 1002 RYTEAVAARREADAA---YQTTVDNYNMV-----------KQTYDELMRIIDDLE 1042
Cdd:COG3096 992 RLEQAEEARREAREQlrqAQAQYSQYNQVlaslkssrdakQQTLQELEQELEELG 1046
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
339-579 |
4.95e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.26 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 339 YAETMRDAkmslVTRTGELEENKdiMLEAKDEVRKKETHERSLN-SIVTELENKRIDWQSKKNDWH-----ARDAK---- 408
Cdd:pfam17380 336 YAEQERMA----MERERELERIR--QEERKRELERIRQEEIAMEiSRMRELERLQMERQQKNERVRqeleaARKVKilee 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 409 -RKQGLKSCTQDLGKLMKERDEARRE---KFEIETAPENARISKQNM--QLEWDQLKEQENVCQRTATENLIKYDQKSSA 482
Cdd:pfam17380 410 eRQRKIQQQKVEMEQIRAEQEEARQRevrRLEEERAREMERVRLEEQerQQQVERLRQQEEERKRKKLELEKEKRDRKRA 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 483 DRAKHDDLEKKLSDELLQSMRAKAELDVSESELKD-MTIMMEQGQKRVDELKGTLQTMMAENIRDNTELNAVTTElQDRK 561
Cdd:pfam17380 490 EEQRRKILEKELEERKQAMIEEERKRKLLEKEMEErQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEE-RSRL 568
|
250
....*....|....*...
gi 17552844 562 LKFDKAVEKLPHLKSTEQ 579
Cdd:pfam17380 569 EAMEREREMMRQIVESEK 586
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
350-595 |
4.99e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 350 LVTRTGELEENKDIMLEAKDEVRKKETHERSLNSIVTELENKRI------DWQSKK-NDWHARDAKRK-QGLKSCTQDLG 421
Cdd:TIGR00606 250 LKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEkvfqgtDEQLNDlYHNHQRTVREKeRELVDCQRELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 422 KLMKERDEARREKFEIETapenaRISKQNMQLEWDQlkeqenvCQRTATENLIKYDQ-KSSADRAKHD-DLEKKLSDEL- 498
Cdd:TIGR00606 330 KLNKERRLLNQEKTELLV-----EQGRLQLQADRHQ-------EHIRARDSLIQSLAtRLELDGFERGpFSERQIKNFHt 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 499 LQSMRAKAELDVSESELKDMTIMMEQGQKRVDELKgtlqtmmaenirdnTELNAVTTELQDRKLKFDKAVEKLPHLKSTE 578
Cdd:TIGR00606 398 LVIERQEDEAKTAAQLCADLQSKERLKQEQADEIR--------------DEKKGLGRTIELKKEILEKKQEELKFVIKEL 463
|
250 260
....*....|....*....|
gi 17552844 579 QLLRSKK---YELDQEVIEA 595
Cdd:TIGR00606 464 QQLEGSSdriLELDQELRKA 483
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
821-1016 |
6.61e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 821 IIKQLEIRKRELI----MSTKEQKTRIAELKSSIAAHERRMVNYREVTvEDLDEKRAQIADLKRQVEESQKSSAKIKQQI 896
Cdd:COG4717 47 LLERLEKEADELFkpqgRKPELNLKELKELEEELKEAEEKEEEYAELQ-EELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 897 EQY----KRKMDRMFMELVQKNKDSIEQAKDRMGQLEQDIARQTAIIENNPSHLEQAEKKLSELEHMCLEKRSEADALAQ 972
Cdd:COG4717 126 QLLplyqELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17552844 973 LEVGEdvkgidiINAQLQTSTASIDAQRARYTEAVAARREADAA 1016
Cdd:COG4717 206 QRLAE-------LEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
91-161 |
7.02e-03 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 40.53 E-value: 7.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17552844 91 MIILNIYVENFKSYAGKHIlgPFHKNLTMILGPNGSGKSNVIDAlLFVFGfKAGKIRTKKLSALINSGGNY 161
Cdd:PRK00064 1 MYLTRLSLTDFRNYEELDL--ELSPGVNVLVGENGQGKTNLLEA-IYLLA-PGRSHRTARDKELIRFGAEA 67
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
864-1072 |
7.79e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 864 TVEDLDEKRAQIADLKRQVEESQKSSAKIKQQIEQYKRKMDRMFMELVQKNKD------SIEQAKDRMGQLEQD---IAR 934
Cdd:COG4372 36 ALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQlqaaqaELAQAQEELESLQEEaeeLQE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552844 935 QTAIIENNPSHLEQAEKKLSELEHMCLEKRSEADA-LAQLEvgEDVKGIDIINAQLQTSTASIDAQRARyTEAVAARREA 1013
Cdd:COG4372 116 ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEeLKELE--EQLESLQEELAALEQELQALSEAEAE-QALDELLKEA 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17552844 1014 DAAYQTTVDNYNMVKQTYDELMRIIDDLENKTMADNAELDIIESAWMQPEKLYPPGKFV 1072
Cdd:COG4372 193 NRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
|
|
| |
