|
Name |
Accession |
Description |
Interval |
E-value |
| MutS |
COG0249 |
DNA mismatch repair ATPase MutS [Replication, recombination and repair]; |
156-863 |
8.79e-126 |
|
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
Pssm-ID: 440019 [Multi-domain] Cd Length: 861 Bit Score: 401.36 E-value: 8.79e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 156 IVAVVEGRGlargEIGMASIDLKNPQIILSQFADnttYAKVITKLKILSPLEIImsntacaVGNSTKLFTLITENFKNVN 235
Cdd:COG0249 130 LAAVARDKG----RYGLAWLDISTGEFLVTELDG---EEALLDELARLAPAEIL-------VPEDLPDPEELLELLRERG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 236 F--TTIQRKYFNETKGLEYI-EQLCIAEFSTvlMEVQSKYYCLAAVAALLKYVEFIQNSvyAPKSLK-ICFQGSEQTAMI 311
Cdd:COG0249 196 AavTRLPDWAFDPDAARRRLlEQFGVASLDG--FGLEDLPAAIAAAGALLAYLEETQKG--ALPHLRrLRRYEEDDYLIL 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 312 DSSSAQNLELLINNQDcRNNHTLFGVLNYTKTPGGSRRLRSNILEPLIDVETINMRLDCVQELLQDEELFFGLQSVISRF 391
Cdd:COG0249 272 DAATRRNLELTETLRG-GRKGSLLSVLDRTVTAMGSRLLRRWLLRPLRDRAAIEARLDAVEELLEDPLLREELRELLKGV 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 392 LDTEQLLSVLVQipkqDTVNAAEskitnLIYLKHTLELVDPLKIAMKNCNTPLLRAYYGSLEDkrFGIILEKIKTVINDD 471
Cdd:COG0249 351 YDLERLLSRIAL----GRANPRD-----LAALRDSLAALPELKELLAELDSPLLAELAEALDP--LEDLAELLERAIVDE 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 472 --ARYMKGclNMrtqkcyaVRSNINEFLDIARRTYTEIVDDIAGMISQLGEKYSLP-LRTSFSSARGFFIQMTTdclalP 548
Cdd:COG0249 420 ppLLIRDG--GV-------IREGYDAELDELRELSENGKEWLAELEARERERTGIKsLKVGYNKVFGYYIEVTK-----A 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 549 N-DQLPSEFIKISKVKNSYSFTSADLIKMNER---CQESLREIyhmTYMIVCKLLSEIYEHIHCLYKLSDTVSMLDMLLS 624
Cdd:COG0249 486 NaDKVPDDYIRKQTLKNAERYITPELKELEDKilsAEERALAL---EYELFEELREEVAAHIERLQALARALAELDVLAS 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 625 FA-HACTLsDYVRPEFTD--TLAIKQGWHPILEKISAEKP-IANNTYITEGSNFLIITGPNMSGKSTYLKQIALCQIMAQ 700
Cdd:COG0249 563 LAeVAVEN-NYVRPELDDspGIEIEGGRHPVVEQALPGEPfVPNDCDLDPDRRILLITGPNMAGKSTYMRQVALIVLLAQ 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 701 IGSYVPAEYSSFRIAKQIFTRLSTDDDIETNSSTFMKEMKEIAYILHNANDKSLILIDELGRGTNTEEGIGICYAVCEYL 780
Cdd:COG0249 642 IGSFVPAESARIGIVDRIFTRVGASDDLARGQSTFMVEMTETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAVAEYL 721
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 781 LS-LKAFTLFATHFLELCHIDALYLNVENMHFEVQHVKNTsrnkeaILYTYKLSKGLTeEKNYGLKAAEVSSLPPSIVLD 859
Cdd:COG0249 722 HDkIRARTLFATHYHELTELAEKLPGVKNYHVAVKEWGGD------IVFLHKVVPGPA-DRSYGIHVAKLAGLPASVIER 794
|
....
gi 966918317 860 AKEI 863
Cdd:COG0249 795 AREI 798
|
|
| PRK05399 |
PRK05399 |
DNA mismatch repair protein MutS; Provisional |
275-921 |
5.04e-120 |
|
DNA mismatch repair protein MutS; Provisional
Pssm-ID: 235444 [Multi-domain] Cd Length: 854 Bit Score: 385.99 E-value: 5.04e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 275 LAAVAALLKYVEFIQNSvyAPKSL-KICFQGSEQTAMIDSSSAQNLELLINNQDcRNNHTLFGVLNYTKTPGGSRRLRSN 353
Cdd:PRK05399 230 IRAAGALLQYLKETQKR--SLPHLrSPKRYEESDYLILDAATRRNLELTENLRG-GRKNSLLSVLDRTVTAMGGRLLRRW 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 354 ILEPLIDVETINMRLDCVQELLQDEELFFGLQSVISRFLDTEQLLSVLVQipkqDTVNAAEskitnLIYLKHTLELVDPL 433
Cdd:PRK05399 307 LHRPLRDREAIEARLDAVEELLEDPLLREDLRELLKGVYDLERLLSRIAL----GRANPRD-----LAALRDSLEALPEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 434 KIAMKNCNTPLLRAYYGSLEDkrFGIILEKIKTVINDDARymkgcLNMRtqKCYAVRSNINEFLDIARrtytEIVDDIAG 513
Cdd:PRK05399 378 KELLAELDSPLLAELAEQLDP--LEELADLLERAIVEEPP-----LLIR--DGGVIADGYDAELDELR----ALSDNGKD 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 514 MISQLGEKY-------SLPLRtsFSSARGFFIQMTTdclalPN-DQLPSEFIKISKVKNSYSFTSADLIKM-------NE 578
Cdd:PRK05399 445 WLAELEARErertgisSLKVG--YNKVFGYYIEVTK-----ANlDKVPEDYIRRQTLKNAERYITPELKELedkilsaEE 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 579 RCQEslREiyhmtYMIVCKLLSEIYEHIHCLYKLSDTVSMLDMLLSFAHACTLSDYVRPEFTD--TLAIKQGWHPILEKI 656
Cdd:PRK05399 518 KALA--LE-----YELFEELREEVAEHIERLQKLAKALAELDVLASLAEVAEENNYVRPEFTDdpGIDIEEGRHPVVEQV 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 657 SAEKP-IANNTYITEGSNFLIITGPNMSGKSTYLKQIALCQIMAQIGSYVPAEYSSFRIAKQIFTRLSTDDDIETNSSTF 735
Cdd:PRK05399 591 LGGEPfVPNDCDLDEERRLLLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAESARIGIVDRIFTRIGASDDLASGRSTF 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 736 MKEMKEIAYILHNANDKSLILIDELGRGTNTEEGIGICYAVCEYLLS-LKAFTLFATHFLELCHIDALYLNVENMHFEVQ 814
Cdd:PRK05399 671 MVEMTETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAVAEYLHDkIGAKTLFATHYHELTELEEKLPGVKNVHVAVK 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 815 HVKNTsrnkeaILYTYKLSKGLTeEKNYGLKAAEVSSLPPSIVLDAKEITTQITRQILQNQRSTPEMERQRAVYHLATRL 894
Cdd:PRK05399 751 EHGGD------IVFLHKVVPGAA-DKSYGIHVAKLAGLPASVIKRAREILAQLESASEKAKAASAEEDQLSLFAEPEESP 823
|
650 660 670
....*....|....*....|....*....|..
gi 966918317 895 VQTArNSQLDPDSLR-----IYLSNLKKKYKE 921
Cdd:PRK05399 824 LLEA-LKALDPDNLTprealNLLYELKKLLKK 854
|
|
| mutS1 |
TIGR01070 |
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair] |
275-908 |
9.39e-95 |
|
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273427 [Multi-domain] Cd Length: 840 Bit Score: 317.87 E-value: 9.39e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 275 LAAVAALLKYVEFIQNSVYaPKSLKICFQGSEQTAMIDSSSAQNLELLINNQDCRNNhTLFGVLNYTKTPGGSRRLRSNI 354
Cdd:TIGR01070 216 LTAAGCLLQYAKRTQRTAL-PHLQPVRLYELQDFMQLDAATRRNLELTENLRGGKQN-TLFSVLDETKTAMGSRLLKRWL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 355 LEPLIDVETINMRLDCVQELLQDEELFFGLQSVISRFLDTEQLLSVLvqipkqdTVNAAESKitNLIYLKHTLELVDPLK 434
Cdd:TIGR01070 294 HRPLRDREVLEARQDTVEVLLRHFFLREGLRPLLKEVGDLERLAARV-------ALGNARPR--DLARLRTSLEQLPELR 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 435 IAMKNCNTPLLRAYYGSLEDkrFGIILEKIKTVINDDARYM--KGCLnmrtqkcyaVRSNINEFLDIARRTYTEIVDDIA 512
Cdd:TIGR01070 365 ALLEELEGPTLQALAAQIDD--FSELLELLEAALIENPPLVvrDGGL---------IREGYDEELDELRAASREGTDYLA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 513 GMISQLGEKYSLP-LRTSFSSARGFFIQMTTDCLalpnDQLPSEFIKISKVKNSYSFTSADLIKMNERCQESLREIYHMT 591
Cdd:TIGR01070 434 RLEARERERTGIPtLKVGYNAVFGYYIEVTRGQL----HLVPAHYRRRQTLKNAERYITPELKEKEDKVLEAEGKILALE 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 592 YMIVCKLLSEIYEHIHCLYKLSDTVSMLDMLLSFAHACTLSDYVRPEFTD--TLAIKQGWHPILEKISAEKPIANNTYIT 669
Cdd:TIGR01070 510 KELFEELRELLKKYLEALQEAARALAELDVLANLAEVAETLHYTRPRFGDdpQLRIREGRHPVVEQVLRTPFVPNDLEMA 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 670 EGSNFLIITGPNMSGKSTYLKQIALCQIMAQIGSYVPAEYSSFRIAKQIFTRLSTDDDIETNSSTFMKEMKEIAYILHNA 749
Cdd:TIGR01070 590 HNRRMLLITGPNMGGKSTYMRQTALIALLAQIGSFVPAESAELPLFDRIFTRIGASDDLASGRSTFMVEMTEAANILHNA 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 750 NDKSLILIDELGRGTNTEEGIGICYAVCEYLL-SLKAFTLFATHFLELCHIDALYLNVENMHFEVQHVKNTsrnkeaILY 828
Cdd:TIGR01070 670 TENSLVLFDEIGRGTSTYDGLALAWAIAEYLHeHIRAKTLFATHYFELTALEESLPGLKNVHVAALEHNGT------IVF 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 829 TYKLSKGlTEEKNYGLKAAEVSSLPPSIVLDAKEITTQITRQilQNQRSTPEMERQRAVYHLATRLVQ------TARNSQ 902
Cdd:TIGR01070 744 LHQVLPG-PASKSYGLAVAALAGLPKEVIARARQILTQLEAR--STESEAPQRKAQTSAPEQISLFDEaethplLEELAK 820
|
....*.
gi 966918317 903 LDPDSL 908
Cdd:TIGR01070 821 LDPDDL 826
|
|
| MutS_V |
pfam00488 |
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
675-867 |
1.22e-91 |
|
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with pfam01624, pfam05188, pfam05192 and pfam05190. The mutS family of proteins is named after the Salmonella typhimurium MutS protein involved in mismatch repair; other members of the family included the eukaryotic MSH 1,2,3, 4,5 and 6 proteins. These have various roles in DNA repair and recombination. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein. The aligned region corresponds with domain V of Thermus aquaticus MutS as characterized in, which contains a Walker A motif, and is structurally similar to the ATPase domain of ABC transporters.
Pssm-ID: 425714 [Multi-domain] Cd Length: 188 Bit Score: 288.32 E-value: 1.22e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 675 LIITGPNMSGKSTYLKQIALCQIMAQIGSYVPAEYSSFRIAKQIFTRLSTDDDIETNSSTFMKEMKEIAYILHNANDKSL 754
Cdd:pfam00488 1 LIITGPNMGGKSTYLRQVALIVLMAQIGSFVPAESAEIGIVDRIFTRIGASDDLAKGRSTFMVEMLETANILHNATDKSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 755 ILIDELGRGTNTEEGIGICYAVCEYLLS-LKAFTLFATHFLELCHIDALYLNVENMHFEVQHVKNTsrnkeaILYTYKLS 833
Cdd:pfam00488 81 VILDELGRGTSTYDGLAIAWAVAEHLAEkIKARTLFATHYHELTKLAEKLPAVKNLHMAAVEDDDD------IVFLYKVQ 154
|
170 180 190
....*....|....*....|....*....|....
gi 966918317 834 KGLTeEKNYGLKAAEVSSLPPSIVLDAKEITTQI 867
Cdd:pfam00488 155 PGAA-DKSYGIHVAELAGLPESVVERAREILAEL 187
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
644-848 |
3.13e-76 |
|
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213210 [Multi-domain] Cd Length: 202 Bit Score: 247.55 E-value: 3.13e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 644 AIKQGWHPILEKI-SAEKPIANNTYITEGSnFLIITGPNMSGKSTYLKQIALCQIMAQIGSYVPAEYSSFRIAKQIFTRL 722
Cdd:cd03243 1 EIKGGRHPVLLALtKGETFVPNDINLGSGR-LLLITGPNMGGKSTYLRSIGLAVLLAQIGCFVPAESASIPLVDRIFTRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 723 STDDDIETNSSTFMKEMKEIAYILHNANDKSLILIDELGRGTNTEEGIGICYAVCEYLLSLKAFTLFATHFLELCHIDAL 802
Cdd:cd03243 80 GAEDSISDGRSTFMAELLELKEILSLATPRSLVLIDELGRGTSTAEGLAIAYAVLEHLLEKGCRTLFATHFHELADLPEQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 966918317 803 YLNVENMHFEVQHVKNTsrnkeaILYTYKLSKGLTEEKnYGLKAAE 848
Cdd:cd03243 160 VPGVKNLHMEELITTGG------LTFTYKLIDGICDPS-YALQIAE 198
|
|
| MUTSac |
smart00534 |
ATPase domain of DNA mismatch repair MUTS family; |
674-863 |
1.71e-72 |
|
ATPase domain of DNA mismatch repair MUTS family;
Pssm-ID: 197777 [Multi-domain] Cd Length: 185 Bit Score: 236.68 E-value: 1.71e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 674 FLIITGPNMSGKSTYLKQIALCQIMAQIGSYVPAEYSSFRIAKQIFTRLSTDDDIETNSSTFMKEMKEIAYILHNANDKS 753
Cdd:smart00534 1 VVIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPVFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATKNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 754 LILIDELGRGTNTEEGIGICYAVCEYLLS-LKAFTLFATHFLELCHIDALYLNVENMHFEVQhvkntsRNKEAILYTYKL 832
Cdd:smart00534 81 LVLLDELGRGTSTYDGLAIAAAILEYLLEkIGARTLFATHYHELTKLADNHPGVRNLHMSAL------EETENITFLYKL 154
|
170 180 190
....*....|....*....|....*....|.
gi 966918317 833 SKGLTeEKNYGLKAAEVSSLPPSIVLDAKEI 863
Cdd:smart00534 155 KPGVA-GKSYGIEVAKLAGLPKEVIERAKRI 184
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
7-79 |
2.00e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.08 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 7 SSASPSAPAVS--PSSGETRSPQGPRYNFRLQETPQRRPSGQVASA-------STPPGTSGAAGDRSSSSSLPCPAPGSR 77
Cdd:PHA03307 332 SSESSRGAAVSpgPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSpaasagrPTRRRARAAVAGRARRRDATGRFPAGR 411
|
..
gi 966918317 78 PA 79
Cdd:PHA03307 412 PR 413
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MutS |
COG0249 |
DNA mismatch repair ATPase MutS [Replication, recombination and repair]; |
156-863 |
8.79e-126 |
|
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
Pssm-ID: 440019 [Multi-domain] Cd Length: 861 Bit Score: 401.36 E-value: 8.79e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 156 IVAVVEGRGlargEIGMASIDLKNPQIILSQFADnttYAKVITKLKILSPLEIImsntacaVGNSTKLFTLITENFKNVN 235
Cdd:COG0249 130 LAAVARDKG----RYGLAWLDISTGEFLVTELDG---EEALLDELARLAPAEIL-------VPEDLPDPEELLELLRERG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 236 F--TTIQRKYFNETKGLEYI-EQLCIAEFSTvlMEVQSKYYCLAAVAALLKYVEFIQNSvyAPKSLK-ICFQGSEQTAMI 311
Cdd:COG0249 196 AavTRLPDWAFDPDAARRRLlEQFGVASLDG--FGLEDLPAAIAAAGALLAYLEETQKG--ALPHLRrLRRYEEDDYLIL 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 312 DSSSAQNLELLINNQDcRNNHTLFGVLNYTKTPGGSRRLRSNILEPLIDVETINMRLDCVQELLQDEELFFGLQSVISRF 391
Cdd:COG0249 272 DAATRRNLELTETLRG-GRKGSLLSVLDRTVTAMGSRLLRRWLLRPLRDRAAIEARLDAVEELLEDPLLREELRELLKGV 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 392 LDTEQLLSVLVQipkqDTVNAAEskitnLIYLKHTLELVDPLKIAMKNCNTPLLRAYYGSLEDkrFGIILEKIKTVINDD 471
Cdd:COG0249 351 YDLERLLSRIAL----GRANPRD-----LAALRDSLAALPELKELLAELDSPLLAELAEALDP--LEDLAELLERAIVDE 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 472 --ARYMKGclNMrtqkcyaVRSNINEFLDIARRTYTEIVDDIAGMISQLGEKYSLP-LRTSFSSARGFFIQMTTdclalP 548
Cdd:COG0249 420 ppLLIRDG--GV-------IREGYDAELDELRELSENGKEWLAELEARERERTGIKsLKVGYNKVFGYYIEVTK-----A 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 549 N-DQLPSEFIKISKVKNSYSFTSADLIKMNER---CQESLREIyhmTYMIVCKLLSEIYEHIHCLYKLSDTVSMLDMLLS 624
Cdd:COG0249 486 NaDKVPDDYIRKQTLKNAERYITPELKELEDKilsAEERALAL---EYELFEELREEVAAHIERLQALARALAELDVLAS 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 625 FA-HACTLsDYVRPEFTD--TLAIKQGWHPILEKISAEKP-IANNTYITEGSNFLIITGPNMSGKSTYLKQIALCQIMAQ 700
Cdd:COG0249 563 LAeVAVEN-NYVRPELDDspGIEIEGGRHPVVEQALPGEPfVPNDCDLDPDRRILLITGPNMAGKSTYMRQVALIVLLAQ 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 701 IGSYVPAEYSSFRIAKQIFTRLSTDDDIETNSSTFMKEMKEIAYILHNANDKSLILIDELGRGTNTEEGIGICYAVCEYL 780
Cdd:COG0249 642 IGSFVPAESARIGIVDRIFTRVGASDDLARGQSTFMVEMTETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAVAEYL 721
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 781 LS-LKAFTLFATHFLELCHIDALYLNVENMHFEVQHVKNTsrnkeaILYTYKLSKGLTeEKNYGLKAAEVSSLPPSIVLD 859
Cdd:COG0249 722 HDkIRARTLFATHYHELTELAEKLPGVKNYHVAVKEWGGD------IVFLHKVVPGPA-DRSYGIHVAKLAGLPASVIER 794
|
....
gi 966918317 860 AKEI 863
Cdd:COG0249 795 AREI 798
|
|
| PRK05399 |
PRK05399 |
DNA mismatch repair protein MutS; Provisional |
275-921 |
5.04e-120 |
|
DNA mismatch repair protein MutS; Provisional
Pssm-ID: 235444 [Multi-domain] Cd Length: 854 Bit Score: 385.99 E-value: 5.04e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 275 LAAVAALLKYVEFIQNSvyAPKSL-KICFQGSEQTAMIDSSSAQNLELLINNQDcRNNHTLFGVLNYTKTPGGSRRLRSN 353
Cdd:PRK05399 230 IRAAGALLQYLKETQKR--SLPHLrSPKRYEESDYLILDAATRRNLELTENLRG-GRKNSLLSVLDRTVTAMGGRLLRRW 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 354 ILEPLIDVETINMRLDCVQELLQDEELFFGLQSVISRFLDTEQLLSVLVQipkqDTVNAAEskitnLIYLKHTLELVDPL 433
Cdd:PRK05399 307 LHRPLRDREAIEARLDAVEELLEDPLLREDLRELLKGVYDLERLLSRIAL----GRANPRD-----LAALRDSLEALPEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 434 KIAMKNCNTPLLRAYYGSLEDkrFGIILEKIKTVINDDARymkgcLNMRtqKCYAVRSNINEFLDIARrtytEIVDDIAG 513
Cdd:PRK05399 378 KELLAELDSPLLAELAEQLDP--LEELADLLERAIVEEPP-----LLIR--DGGVIADGYDAELDELR----ALSDNGKD 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 514 MISQLGEKY-------SLPLRtsFSSARGFFIQMTTdclalPN-DQLPSEFIKISKVKNSYSFTSADLIKM-------NE 578
Cdd:PRK05399 445 WLAELEARErertgisSLKVG--YNKVFGYYIEVTK-----ANlDKVPEDYIRRQTLKNAERYITPELKELedkilsaEE 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 579 RCQEslREiyhmtYMIVCKLLSEIYEHIHCLYKLSDTVSMLDMLLSFAHACTLSDYVRPEFTD--TLAIKQGWHPILEKI 656
Cdd:PRK05399 518 KALA--LE-----YELFEELREEVAEHIERLQKLAKALAELDVLASLAEVAEENNYVRPEFTDdpGIDIEEGRHPVVEQV 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 657 SAEKP-IANNTYITEGSNFLIITGPNMSGKSTYLKQIALCQIMAQIGSYVPAEYSSFRIAKQIFTRLSTDDDIETNSSTF 735
Cdd:PRK05399 591 LGGEPfVPNDCDLDEERRLLLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAESARIGIVDRIFTRIGASDDLASGRSTF 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 736 MKEMKEIAYILHNANDKSLILIDELGRGTNTEEGIGICYAVCEYLLS-LKAFTLFATHFLELCHIDALYLNVENMHFEVQ 814
Cdd:PRK05399 671 MVEMTETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAVAEYLHDkIGAKTLFATHYHELTELEEKLPGVKNVHVAVK 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 815 HVKNTsrnkeaILYTYKLSKGLTeEKNYGLKAAEVSSLPPSIVLDAKEITTQITRQILQNQRSTPEMERQRAVYHLATRL 894
Cdd:PRK05399 751 EHGGD------IVFLHKVVPGAA-DKSYGIHVAKLAGLPASVIKRAREILAQLESASEKAKAASAEEDQLSLFAEPEESP 823
|
650 660 670
....*....|....*....|....*....|..
gi 966918317 895 VQTArNSQLDPDSLR-----IYLSNLKKKYKE 921
Cdd:PRK05399 824 LLEA-LKALDPDNLTprealNLLYELKKLLKK 854
|
|
| mutS1 |
TIGR01070 |
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair] |
275-908 |
9.39e-95 |
|
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273427 [Multi-domain] Cd Length: 840 Bit Score: 317.87 E-value: 9.39e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 275 LAAVAALLKYVEFIQNSVYaPKSLKICFQGSEQTAMIDSSSAQNLELLINNQDCRNNhTLFGVLNYTKTPGGSRRLRSNI 354
Cdd:TIGR01070 216 LTAAGCLLQYAKRTQRTAL-PHLQPVRLYELQDFMQLDAATRRNLELTENLRGGKQN-TLFSVLDETKTAMGSRLLKRWL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 355 LEPLIDVETINMRLDCVQELLQDEELFFGLQSVISRFLDTEQLLSVLvqipkqdTVNAAESKitNLIYLKHTLELVDPLK 434
Cdd:TIGR01070 294 HRPLRDREVLEARQDTVEVLLRHFFLREGLRPLLKEVGDLERLAARV-------ALGNARPR--DLARLRTSLEQLPELR 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 435 IAMKNCNTPLLRAYYGSLEDkrFGIILEKIKTVINDDARYM--KGCLnmrtqkcyaVRSNINEFLDIARRTYTEIVDDIA 512
Cdd:TIGR01070 365 ALLEELEGPTLQALAAQIDD--FSELLELLEAALIENPPLVvrDGGL---------IREGYDEELDELRAASREGTDYLA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 513 GMISQLGEKYSLP-LRTSFSSARGFFIQMTTDCLalpnDQLPSEFIKISKVKNSYSFTSADLIKMNERCQESLREIYHMT 591
Cdd:TIGR01070 434 RLEARERERTGIPtLKVGYNAVFGYYIEVTRGQL----HLVPAHYRRRQTLKNAERYITPELKEKEDKVLEAEGKILALE 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 592 YMIVCKLLSEIYEHIHCLYKLSDTVSMLDMLLSFAHACTLSDYVRPEFTD--TLAIKQGWHPILEKISAEKPIANNTYIT 669
Cdd:TIGR01070 510 KELFEELRELLKKYLEALQEAARALAELDVLANLAEVAETLHYTRPRFGDdpQLRIREGRHPVVEQVLRTPFVPNDLEMA 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 670 EGSNFLIITGPNMSGKSTYLKQIALCQIMAQIGSYVPAEYSSFRIAKQIFTRLSTDDDIETNSSTFMKEMKEIAYILHNA 749
Cdd:TIGR01070 590 HNRRMLLITGPNMGGKSTYMRQTALIALLAQIGSFVPAESAELPLFDRIFTRIGASDDLASGRSTFMVEMTEAANILHNA 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 750 NDKSLILIDELGRGTNTEEGIGICYAVCEYLL-SLKAFTLFATHFLELCHIDALYLNVENMHFEVQHVKNTsrnkeaILY 828
Cdd:TIGR01070 670 TENSLVLFDEIGRGTSTYDGLALAWAIAEYLHeHIRAKTLFATHYFELTALEESLPGLKNVHVAALEHNGT------IVF 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 829 TYKLSKGlTEEKNYGLKAAEVSSLPPSIVLDAKEITTQITRQilQNQRSTPEMERQRAVYHLATRLVQ------TARNSQ 902
Cdd:TIGR01070 744 LHQVLPG-PASKSYGLAVAALAGLPKEVIARARQILTQLEAR--STESEAPQRKAQTSAPEQISLFDEaethplLEELAK 820
|
....*.
gi 966918317 903 LDPDSL 908
Cdd:TIGR01070 821 LDPDDL 826
|
|
| MutS_V |
pfam00488 |
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
675-867 |
1.22e-91 |
|
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with pfam01624, pfam05188, pfam05192 and pfam05190. The mutS family of proteins is named after the Salmonella typhimurium MutS protein involved in mismatch repair; other members of the family included the eukaryotic MSH 1,2,3, 4,5 and 6 proteins. These have various roles in DNA repair and recombination. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein. The aligned region corresponds with domain V of Thermus aquaticus MutS as characterized in, which contains a Walker A motif, and is structurally similar to the ATPase domain of ABC transporters.
Pssm-ID: 425714 [Multi-domain] Cd Length: 188 Bit Score: 288.32 E-value: 1.22e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 675 LIITGPNMSGKSTYLKQIALCQIMAQIGSYVPAEYSSFRIAKQIFTRLSTDDDIETNSSTFMKEMKEIAYILHNANDKSL 754
Cdd:pfam00488 1 LIITGPNMGGKSTYLRQVALIVLMAQIGSFVPAESAEIGIVDRIFTRIGASDDLAKGRSTFMVEMLETANILHNATDKSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 755 ILIDELGRGTNTEEGIGICYAVCEYLLS-LKAFTLFATHFLELCHIDALYLNVENMHFEVQHVKNTsrnkeaILYTYKLS 833
Cdd:pfam00488 81 VILDELGRGTSTYDGLAIAWAVAEHLAEkIKARTLFATHYHELTKLAEKLPAVKNLHMAAVEDDDD------IVFLYKVQ 154
|
170 180 190
....*....|....*....|....*....|....
gi 966918317 834 KGLTeEKNYGLKAAEVSSLPPSIVLDAKEITTQI 867
Cdd:pfam00488 155 PGAA-DKSYGIHVAELAGLPESVVERAREILAEL 187
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
644-848 |
3.13e-76 |
|
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213210 [Multi-domain] Cd Length: 202 Bit Score: 247.55 E-value: 3.13e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 644 AIKQGWHPILEKI-SAEKPIANNTYITEGSnFLIITGPNMSGKSTYLKQIALCQIMAQIGSYVPAEYSSFRIAKQIFTRL 722
Cdd:cd03243 1 EIKGGRHPVLLALtKGETFVPNDINLGSGR-LLLITGPNMGGKSTYLRSIGLAVLLAQIGCFVPAESASIPLVDRIFTRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 723 STDDDIETNSSTFMKEMKEIAYILHNANDKSLILIDELGRGTNTEEGIGICYAVCEYLLSLKAFTLFATHFLELCHIDAL 802
Cdd:cd03243 80 GAEDSISDGRSTFMAELLELKEILSLATPRSLVLIDELGRGTSTAEGLAIAYAVLEHLLEKGCRTLFATHFHELADLPEQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 966918317 803 YLNVENMHFEVQHVKNTsrnkeaILYTYKLSKGLTEEKnYGLKAAE 848
Cdd:cd03243 160 VPGVKNLHMEELITTGG------LTFTYKLIDGICDPS-YALQIAE 198
|
|
| MUTSac |
smart00534 |
ATPase domain of DNA mismatch repair MUTS family; |
674-863 |
1.71e-72 |
|
ATPase domain of DNA mismatch repair MUTS family;
Pssm-ID: 197777 [Multi-domain] Cd Length: 185 Bit Score: 236.68 E-value: 1.71e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 674 FLIITGPNMSGKSTYLKQIALCQIMAQIGSYVPAEYSSFRIAKQIFTRLSTDDDIETNSSTFMKEMKEIAYILHNANDKS 753
Cdd:smart00534 1 VVIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPVFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATKNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 754 LILIDELGRGTNTEEGIGICYAVCEYLLS-LKAFTLFATHFLELCHIDALYLNVENMHFEVQhvkntsRNKEAILYTYKL 832
Cdd:smart00534 81 LVLLDELGRGTSTYDGLAIAAAILEYLLEkIGARTLFATHYHELTKLADNHPGVRNLHMSAL------EETENITFLYKL 154
|
170 180 190
....*....|....*....|....*....|.
gi 966918317 833 SKGLTeEKNYGLKAAEVSSLPPSIVLDAKEI 863
Cdd:smart00534 155 KPGVA-GKSYGIEVAKLAGLPKEVIERAKRI 184
|
|
| ABC_MutS1 |
cd03284 |
ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair ... |
645-863 |
1.22e-70 |
|
ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213251 [Multi-domain] Cd Length: 216 Bit Score: 232.93 E-value: 1.22e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 645 IKQGWHPILEKISAEKP-IANNTYITEGSNFLIITGPNMSGKSTYLKQIALCQIMAQIGSYVPAEYSSFRIAKQIFTRLS 723
Cdd:cd03284 2 IEGGRHPVVEQVLDNEPfVPNDTELDPERQILLITGPNMAGKSTYLRQVALIALLAQIGSFVPASKAEIGVVDRIFTRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 724 TDDDIETNSSTFMKEMKEIAYILHNANDKSLILIDELGRGTNTEEGIGICYAVCEYLLS-LKAFTLFATHFLELCHIDAL 802
Cdd:cd03284 82 ASDDLAGGRSTFMVEMVETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAIVEYLHEkIGAKTLFATHYHELTELEGK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966918317 803 YLNVENMHFEVQHVKNTsrnkeaILYTYKLSKGLTeEKNYGLKAAEVSSLPPSIVLDAKEI 863
Cdd:cd03284 162 LPRVKNFHVAVKEKGGG------VVFLHKIVEGAA-DKSYGIEVARLAGLPEEVIERAREI 215
|
|
| ABC_MSH4_euk |
cd03282 |
ATP-binding cassette domain of eukaryotic MutS4 homolog; The MutS protein initiates DNA ... |
644-852 |
3.09e-70 |
|
ATP-binding cassette domain of eukaryotic MutS4 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213249 [Multi-domain] Cd Length: 204 Bit Score: 231.51 E-value: 3.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 644 AIKQGWHPILEKISaEKPIANNTYITEG-SNFLIITGPNMSGKSTYLKQIALCQIMAQIGSYVPAEYSSFRIAKQIFTRL 722
Cdd:cd03282 1 IIRDSRHPILDRDK-KNFIPNDIYLTRGsSRFHIITGPNMSGKSTYLKQIALLAIMAQIGCFVPAEYATLPIFNRLLSRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 723 STDDDIETNSSTFMKEMKEIAYILHNANDKSLILIDELGRGTNTEEGIGICYAVCEYLLSLKAFTLFATHFLELCHIDAL 802
Cdd:cd03282 80 SNDDSMERNLSTFASEMSETAYILDYADGDSLVLIDELGRGTSSADGFAISLAILECLIKKESTVFFATHFRDIAAILGN 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 966918317 803 YLNVENMHFEVQHVkntsrNKEAILYTYKLSKGLTEEKNYGLKAAEVSSL 852
Cdd:cd03282 160 KSCVVHLHMKAQSI-----NSNGIEMAYKLVLGLYRIVDDGIRFVRVLAL 204
|
|
| ABC_MSH2_euk |
cd03285 |
ATP-binding cassette domain of eukaryotic MutS2 homolog; The MutS protein initiates DNA ... |
645-862 |
1.12e-63 |
|
ATP-binding cassette domain of eukaryotic MutS2 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213252 [Multi-domain] Cd Length: 222 Bit Score: 214.16 E-value: 1.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 645 IKQGWHPILEKISAEKPIANNTYITEG-SNFLIITGPNMSGKSTYLKQIALCQIMAQIGSYVPAEYSSFRIAKQIFTRLS 723
Cdd:cd03285 2 LKEARHPCVEAQDDVAFIPNDVTLTRGkSRFLIITGPNMGGKSTYIRQIGVIVLMAQIGCFVPCDSADIPIVDCILARVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 724 TDDDIETNSSTFMKEMKEIAYILHNANDKSLILIDELGRGTNTEEGIGICYAVCEYLLS-LKAFTLFATHFLELCHIDAL 802
Cdd:cd03285 82 ASDSQLKGVSTFMAEMLETAAILKSATENSLIIIDELGRGTSTYDGFGLAWAIAEYIATqIKCFCLFATHFHELTALADE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 803 YLNVENMHFEVqHVKNTSRNkeaILYTYKLSKGLTeEKNYGLKAAEVSSLPPSIVLDAKE 862
Cdd:cd03285 162 VPNVKNLHVTA-LTDDASRT---LTMLYKVEKGAC-DQSFGIHVAELANFPKEVIEMAKQ 216
|
|
| ABC_MSH3_euk |
cd03287 |
ATP-binding cassette domain of eukaryotic MutS3 homolog; The MutS protein initiates DNA ... |
643-857 |
2.31e-57 |
|
ATP-binding cassette domain of eukaryotic MutS3 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213254 [Multi-domain] Cd Length: 222 Bit Score: 196.55 E-value: 2.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 643 LAIKQGWHPILEKISAEKPIANNTYIT-EGSNFLIITGPNMSGKSTYLKQIALCQIMAQIGSYVPAEYSSFRIAKQIFTR 721
Cdd:cd03287 1 ILIKEGRHPMIESLLDKSFVPNDIHLSaEGGYCQIITGPNMGGKSSYIRQVALITIMAQIGSFVPASSATLSIFDSVLTR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 722 LSTDDDIETNSSTFMKEMKEIAYILHNANDKSLILIDELGRGTNTEEGIGICYAVCEYLLSL-KAFTLFATHFLELCHID 800
Cdd:cd03287 81 MGASDSIQHGMSTFMVELSETSHILSNCTSRSLVILDELGRGTSTHDGIAIAYATLHYLLEEkKCLVLFVTHYPSLGEIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966918317 801 ALYLN-VENMHF---EVQHVKNTSRNKEaILYTYKLSKGLTeEKNYGLKAAEVSSLPPSIV 857
Cdd:cd03287 161 RRFEGsIRNYHMsylESQKDFETSDSQS-ITFLYKLVRGLA-SRSFGLNVARLAGLPKSII 219
|
|
| ABC_MSH6_euk |
cd03286 |
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA ... |
645-857 |
4.41e-54 |
|
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213253 [Multi-domain] Cd Length: 218 Bit Score: 187.25 E-value: 4.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 645 IKQGWHPILEKISAEKPIANNTYI-TEGSNFLIITGPNMSGKSTYLKQIALCQIMAQIGSYVPAEYSSFRIAKQIFTRLS 723
Cdd:cd03286 2 FEELRHPCLNASTASSFVPNDVDLgATSPRILVLTGPNMGGKSTLLRTVCLAVIMAQMGMDVPAKSMRLSLVDRIFTRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 724 TDDDIETNSSTFMKEMKEIAYILHNANDKSLILIDELGRGTNTEEGIGICYAVCEYLLS-LKAFTLFATHFLELCHIDAL 802
Cdd:cd03286 82 ARDDIMKGESTFMVELSETANILRHATPDSLVILDELGRGTSTHDGYAIAHAVLEYLVKkVKCLTLFSTHYHSLCDEFHE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 966918317 803 YLNVENMHFEVQHVKNTSRNKEAILYTYKLSKGLTeEKNYGLKAAEVSSLPPSIV 857
Cdd:cd03286 162 HGGVRLGHMACAVKNESDPTIRDITFLYKLVAGIC-PKSYGLYVALMAGIPDGVV 215
|
|
| ABC_MSH5_euk |
cd03281 |
ATP-binding cassette domain of eukaryotic MutS5 homolog; The MutS protein initiates DNA ... |
645-849 |
1.67e-49 |
|
ATP-binding cassette domain of eukaryotic MutS5 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213248 [Multi-domain] Cd Length: 213 Bit Score: 174.03 E-value: 1.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 645 IKQGWHPILEKISaEKPIANNTYITEGSN-FLIITGPNMSGKSTYLKQIALCQIMAQIGSYVPAEYSSFRIAKQIFTRLS 723
Cdd:cd03281 2 IQGGRHPLLELFV-DSFVPNDTEIGGGGPsIMVITGPNSSGKSVYLKQVALIVFLAHIGSFVPADSATIGLVDKIFTRMS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 724 TDDDIETNSSTFMKEMKEIAYILHNANDKSLILIDELGRGTNTEEGIGICYAVCEYLLSLKA---FTLFATHFLELCHID 800
Cdd:cd03281 81 SRESVSSGQSAFMIDLYQVSKALRLATRRSLVLIDEFGKGTDTEDGAGLLIATIEHLLKRGPecpRVIVSTHFHELFNRS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 966918317 801 ALY--LNVENMHFEVQHVKNTSRNKEAILYTYKLSKGLTeEKNYGLKAAEV 849
Cdd:cd03281 161 LLPerLKIKFLTMEVLLNPTSTSPNEDITYLYRLVPGLA-DTSFAIHCAKL 210
|
|
| MutS_III |
pfam05192 |
MutS domain III; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
314-626 |
2.51e-47 |
|
MutS domain III; This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with pfam00488, pfam05188, pfam01624 and pfam05190. The MutS family of proteins is named after the Salmonella typhimurium MutS protein involved in mismatch repair; other members of the family included the eukaryotic MSH 1,2,3, 4,5 and 6 proteins. These have various roles in DNA repair and recombination. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein. The aligned region corresponds with domain III, which is central to the structure of Thermus aquaticus MutS as characterized in.
Pssm-ID: 461579 [Multi-domain] Cd Length: 291 Bit Score: 170.66 E-value: 2.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 314 SSAQNLELLINNQDcRNNHTLFGVLNYTKTPGGSRRLRSNILEPLIDVETINMRLDCVQELLQDEELFFGLQSVISRFLD 393
Cdd:pfam05192 1 ATLRNLELTENLRG-GKEGSLLGLLDRTKTPMGSRLLRQWLLQPLTDLEEINERLDAVEELLENSELREDLRELLRRLPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 394 TEQLLSvlvqipkqdTVNAAESKITNLIYLKHTLELVDPLKIAMKNCNTPLLRAYYgSLEDKrfgiiLEkiKTVINDDAR 473
Cdd:pfam05192 80 LERLLS---------RIALGKATPRDLLALLDSLEKLPLLKELLLEEKSALLGELA-SLAEL-----LE--EAIDEEPPA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 474 YMKGCLNMRTQKCYAVRSNINEFLDIARRTYTEIVDDIAGMISQLGEKYSLPLRTSFSSARGFFIQMTTDCLalpnDQLP 553
Cdd:pfam05192 143 LLRDGGVIRDGYDEELDELRDLLLDGKRLLAKLEARERERTGIKSLKVLYNKVFGYYLLLVEYYIEVSKSQK----DKVP 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966918317 554 SEFIKISKVKNSYSFTSADLIKMNERCQESLREIYHMTYMIVCKLLSEIYEHIHCLYKLSDTVSMLDMLLSFA 626
Cdd:pfam05192 219 DDYIRIQTTKNAERYITPELKELERKILQAEERLLALEKELFEELLEEVLEYIEVLRRAAEALAELDVLLSLA 291
|
|
| MUTSd |
smart00533 |
DNA-binding domain of DNA mismatch repair MUTS family; |
333-655 |
3.40e-44 |
|
DNA-binding domain of DNA mismatch repair MUTS family;
Pssm-ID: 214710 [Multi-domain] Cd Length: 308 Bit Score: 162.47 E-value: 3.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 333 TLFGVLNYTKTPGGSRRLRSNILEPLIDVETINMRLDCVQELLQDEELFFGLQSVISRFLDTEQLLSvlvqipkqdTVNA 412
Cdd:smart00533 3 SLFELLNHTKTPMGKRLLRRWLLQPLLDLKEINERLDAVEELVENPELRQKLRQLLKRIPDLERLLS---------RIER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 413 AESKITNLIYLKHTLELVDPLKIAMKNCNTPLLRAYYGSLEDKRFGIILEKIKTVINDDArymkgclnMRTQKCYAVRSN 492
Cdd:smart00533 74 GRASPRDLLRLYDSLEGLKEIRQLLESLDGPLLGLLLKVILEPLLELLELLLELLNDDDP--------LEVNDGGLIKDG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 493 INEFLDIARRTYTEIVDDIAGMISQLGEKYSLP-LRTSFSSARGFFIQMTTDclalPNDQLPSEFIKISKVKNSYSFTSA 571
Cdd:smart00533 146 FDPELDELREKLEELEEELEELLKKEREELGIDsLKLGYNKVHGYYIEVTKS----EAKKVPKDFIRRSSLKNTERFTTP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 572 DLIKMNERCQESLREIYHMTYMIVCKLLSEIYEHIHCLYKLSDTVSMLDMLLSFAHACTLSDYVRPEFTDT--LAIKQGW 649
Cdd:smart00533 222 ELKELENELLEAKEEIERLEKEILRELLEKVLEYLEELRALAEALAELDVLLSLATLAAEGNYVRPEFVDSgeLEIKNGR 301
|
....*.
gi 966918317 650 HPILEK 655
Cdd:smart00533 302 HPVLEL 307
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
339-886 |
2.83e-43 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 169.17 E-value: 2.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 339 NYTKTPGGSRRLRSniLEPLIDVETINMRLDCVQELLQ--DEELFFGLQSV--ISRFLDTEQLLSVLvqipkqdtvNAAE 414
Cdd:COG1193 20 EYAVSELGKELARK--LRPSTDLEEVERLLAETAEARRllRLEGGLPLGGIpdIRPLLKRAEEGGVL---------SPEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 415 skitnLIYLKHTLELVDPLKIAMKNC--NTPLLRAYYGSLEDkrFGIILEKIKTVINDDARYM----KGCLNMRTQKcYA 488
Cdd:COG1193 89 -----LLDIARTLRAARRLKRFLEELeeEYPALKELAERLPP--LPELEKEIDRAIDEDGEVKdsasPELRRIRREI-RS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 489 VRSNINEFLD--IARRTYTEIVDDiaGMISQLGEKYSLPLRTSF----------SSARG--FFIQmttdclalpndqlPS 554
Cdd:COG1193 161 LEQRIREKLEsiLRSASYQKYLQD--AIITIRNGRYVIPVKAEYkgkipgivhdQSASGqtLFIE-------------PM 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 555 EFIKISkvkNSYsftsADLiKMNERcqeslREIYhmtymivcKLLSE----IYEHIHCLYKLSDTVSMLDMLLS---FAH 627
Cdd:COG1193 226 AVVELN---NEL----REL-EAEER-----REIE--------RILRElsalVREYAEELLENLEILAELDFIFAkarYAL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 628 ACtlsDYVRPEFTD--TLAIKQGWHPILEKisaEKPIANNTYITEGSNFLIITGPNMSGKSTYLKQIALCQIMAQIGSYV 705
Cdd:COG1193 285 EL---KAVKPELNDegYIKLKKARHPLLDL---KKVVPIDIELGEDFRTLVITGPNTGGKTVTLKTVGLLTLMAQSGLPI 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 706 PA-EYSSFRIAKQIFTrlstdD-----DIETNSSTFMKEMKEIAYILHNANDKSLILIDELGRGTNTEEGIGICYAVCEY 779
Cdd:COG1193 359 PAaEGSELPVFDNIFA-----DigdeqSIEQSLSTFSSHMTNIVEILEKADENSLVLLDELGAGTDPQEGAALAIAILEE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 780 LLSLKAFTLFATHFLELchiDALYLN---VEN--MHFEVQHVKNtsrnkeailyTYKLSKGLTEEKNyglkAAEVSS--- 851
Cdd:COG1193 434 LLERGARVVATTHYSEL---KAYAYNtegVENasVEFDVETLSP----------TYRLLIGVPGRSN----AFEIARrlg 496
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 966918317 852 LPPSIVLDAKEITTQITRQI------LQNQRSTPEMERQRA 886
Cdd:COG1193 497 LPEEIIERARELLGEESIDVeklieeLERERRELEEEREEA 537
|
|
| ABC_MutS-like |
cd03283 |
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ... |
644-841 |
1.29e-41 |
|
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213250 [Multi-domain] Cd Length: 199 Bit Score: 151.30 E-value: 1.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 644 AIKQGWHPILEKisaEKPIANNTYItEGSNFLIITGPNMSGKSTYLKQIALCQIMAQIGSYVPAEYSSFRIAKqIFTRLS 723
Cdd:cd03283 1 EAKNLGHPLIGR---EKRVANDIDM-EKKNGILITGSNMSGKSTFLRTIGVNVILAQAGAPVCASSFELPPVK-IFTSIR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 724 TDDDIETNSSTFMKEMKEIAYILHNAND--KSLILIDELGRGTNTEEGIGICYAVCEYLLSLKAFTLFATHFLELCHIDA 801
Cdd:cd03283 76 VSDDLRDGISYFYAELRRLKEIVEKAKKgePVLFLLDEIFKGTNSRERQAASAAVLKFLKNKNTIGIISTHDLELADLLD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 966918317 802 LYLNVENMHFEVQHVKNtsrnkeAILYTYKLSKGLTEEKN 841
Cdd:cd03283 156 LDSAVRNYHFREDIDDN------KLIFDYKLKPGVSPTRN 189
|
|
| ABC_MutS2 |
cd03280 |
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ... |
645-796 |
9.40e-36 |
|
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213247 [Multi-domain] Cd Length: 200 Bit Score: 134.30 E-value: 9.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 645 IKQGWHPILeKISAEKPIANNTYITEGSNFLIITGPNMSGKSTYLKQIALCQIMAQIGSYVPA-EYSSFRIAKQIFTRLS 723
Cdd:cd03280 2 LREARHPLL-PLQGEKVVPLDIQLGENKRVLVITGPNAGGKTVTLKTLGLLTLMAQSGLPIPAaEGSSLPVFENIFADIG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966918317 724 TDDDIETNSSTFMKEMKEIAYILHNANDKSLILIDELGRGTNTEEGIGICYAVCEYLLSLKAFTLFATHFLEL 796
Cdd:cd03280 81 DEQSIEQSLSTFSSHMKNIARILQHADPDSLVLLDELGSGTDPVEGAALAIAILEELLERGALVIATTHYGEL 153
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
573-886 |
5.37e-28 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 121.47 E-value: 5.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 573 LIKMNERCQESLREIYHMTYMIvCKLLSE-IYEHIHCLYKLSDTVSMLDMLLSFAH-ACTLsDYVRPEFTD--TLAIKQG 648
Cdd:PRK00409 229 VVELNNEIRELRNKEEQEIERI-LKELSAkVAKNLDFLKFLNKIFDELDFIFARARyAKAL-KATFPLFNDegKIDLRQA 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 649 WHPILEKisaEKPIANNTYITEGSNFLIITGPNMSGKSTYLKQIALCQIMAQIGSYVPA----EYSSFriaKQIFTRLST 724
Cdd:PRK00409 307 RHPLLDG---EKVVPKDISLGFDKTVLVITGPNTGGKTVTLKTLGLAALMAKSGLPIPAnepsEIPVF---KEIFADIGD 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 725 DDDIETNSSTFMKEMKEIAYILHNANDKSLILIDELGRGTNTEEGIGICYAVCEYLLSLKAFTLFATHFLELchiDALYL 804
Cdd:PRK00409 381 EQSIEQSLSTFSGHMTNIVRILEKADKNSLVLFDELGAGTDPDEGAALAISILEYLRKRGAKIIATTHYKEL---KALMY 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 805 N---VENM--HFEVQhvknTSRNkeailyTYKLSKGlTEEKNYGLKAAEVSSLPPSIVLDAKEITTQITRQI------LQ 873
Cdd:PRK00409 458 NregVENAsvEFDEE----TLRP------TYRLLIG-IPGKSNAFEIAKRLGLPENIIEEAKKLIGEDKEKLneliasLE 526
|
330
....*....|...
gi 966918317 874 NQRSTPEMERQRA 886
Cdd:PRK00409 527 ELERELEQKAEEA 539
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
644-796 |
7.85e-23 |
|
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: 95.89 E-value: 7.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 644 AIKQGWHPILekisaekPIANNTYITEGsNFLIITGPNMSGKSTYLKQIALCQIMA----------QIGSYVPAEYSSFr 713
Cdd:cd03227 1 KIVLGRFPSY-------FVPNDVTFGEG-SLTIITGPNGSGKSTILDAIGLALGGAqsatrrrsgvKAGCIVAAVSAEL- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 714 iakqIFTRLSTdddietnsSTFMKEMKEIAYILHNANDK--SLILIDELGRGTNTEEGIGICYAVCEYLLSlKAFTLFAT 791
Cdd:cd03227 72 ----IFTRLQL--------SGGEKELSALALILALASLKprPLYILDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVIT 138
|
....*
gi 966918317 792 HFLEL 796
Cdd:cd03227 139 HLPEL 143
|
|
| MutS_IV |
pfam05190 |
MutS family domain IV; This domain is found in proteins of the MutS family (DNA mismatch ... |
492-586 |
2.32e-17 |
|
MutS family domain IV; This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with pfam01624, pfam05188, pfam05192 and pfam00488. The mutS family of proteins is named after the Salmonella typhimurium MutS protein involved in mismatch repair; other members of the family included the eukaryotic MSH 1,2,3, 4,5 and 6 proteins. These have various roles in DNA repair and recombination. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein. The aligned region corresponds in part with globular domain IV, which is involved in DNA binding, in Thermus aquaticus MutS as characterized in.
Pssm-ID: 398730 [Multi-domain] Cd Length: 92 Bit Score: 78.03 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 492 NINEFLDIARRTYTEIVDDIAGMISQLGEKYSLP-LRTSFSSARGFFIQMTTDCLalpnDQLPSEFIKISKVKNSYSFTS 570
Cdd:pfam05190 1 GFDEELDELRDLLDELEKELEELEKKEREKLGIKsLKVGYNKVFGYYIEVTRSEA----KKVPSNYIRRQTLKNGVRFTT 76
|
90
....*....|....*.
gi 966918317 571 ADLIKMNERCQESLRE 586
Cdd:pfam05190 77 PELKKLEDELLEAEEE 92
|
|
| MutS_II |
pfam05188 |
MutS domain II; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
154-292 |
7.74e-17 |
|
MutS domain II; This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with pfam00488, pfam01624, pfam05192 and pfam05190. The MutS family of proteins is named after the Salmonella typhimurium MutS protein involved in mismatch repair; other members of the family included the eukaryotic MSH 1,2,3, 4,5 and 6 proteins. These have various roles in DNA repair and recombination. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein. This domain corresponds to domain II in Thermus aquaticus MutS as characterized in, and has similarity resembles RNAse-H-like domains (see pfam00075).
Pssm-ID: 398728 [Multi-domain] Cd Length: 133 Bit Score: 77.78 E-value: 7.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 154 SVIVAVVEGRGlarGEIGMASIDLKNPQIILSQFADnttYAKVITKLKILSPLEIIMSNTACAvGNSTKLFTLITENFKN 233
Cdd:pfam05188 1 NYLAAISRGDG---NRYGLAFLDLSTGEFGVSEFED---FEELLAELSRLSPKELLLPESLSS-STVAESQKLLELRLRV 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 966918317 234 VNFTTIQRKYFNETKGLEyiEQLCIAEFSTvlMEVQSKYYCLAAVAALLKYVEFIQNSV 292
Cdd:pfam05188 74 GRRPTWLFELEHAYEDLN--EDFGVEDLDG--FGLEELPLALCAAGALISYLKETQKEN 128
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
664-796 |
1.11e-09 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 58.03 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 664 NNTYITEGSnFLIITGPNMSGKSTYLKQIAL----CQIMAQIGSYVPAEYSSFRIAKQIFTR--LSTDddietnsstfMK 737
Cdd:cd00267 18 VSLTLKAGE-IVALVGPNGSGKSTLLRAIAGllkpTSGEILIDGKDIAKLPLEELRRRIGYVpqLSGG----------QR 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 966918317 738 EMKEIAYILhnANDKSLILIDELGRGTNTEEGIGICYAVCEyLLSLKAFTLFATHFLEL 796
Cdd:cd00267 87 QRVALARAL--LLNPDLLLLDEPTSGLDPASRERLLELLRE-LAEEGRTVIIVTHDPEL 142
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
7-79 |
2.00e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.08 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 7 SSASPSAPAVS--PSSGETRSPQGPRYNFRLQETPQRRPSGQVASA-------STPPGTSGAAGDRSSSSSLPCPAPGSR 77
Cdd:PHA03307 332 SSESSRGAAVSpgPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSpaasagrPTRRRARAAVAGRARRRDATGRFPAGR 411
|
..
gi 966918317 78 PA 79
Cdd:PHA03307 412 PR 413
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
638-715 |
2.48e-03 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 40.21 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 638 EFTDtLAIKQGWHPILEKISAEkpianntyITEGSnFLIITGPNMSGKSTYLKQIaLCQIMAQIGS----YVPAEYSSFR 713
Cdd:cd03235 1 EVED-LTVSYGGHPVLEDVSFE--------VKPGE-FLAIVGPNGAGKSTLLKAI-LGLLKPTSGSirvfGKPLEKERKR 69
|
..
gi 966918317 714 IA 715
Cdd:cd03235 70 IG 71
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
4-136 |
4.40e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 40.92 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918317 4 PEISSASPSAPAVSPSSGETRSPQGPRynfrlQETPQRRPSGQVASASTPPGTSGAAGDRSSSSSLPCPAPGSRPAQGSY 83
Cdd:PHA03307 155 AGASPAAVASDAASSRQAALPLSSPEE-----TARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAA 229
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 966918317 84 FGNKRAYAentvasnftfGASSSSARDTNYPQTLKTPLSTGNPQRSSYKSWTP 136
Cdd:PHA03307 230 DDAGASSS----------DSSSSESSGCGWGPENECPLPRPAPITLPTRIWEA 272
|
|
| |
