|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05399 |
PRK05399 |
DNA mismatch repair protein MutS; Provisional |
188-1017 |
9.32e-179 |
|
DNA mismatch repair protein MutS; Provisional
Pssm-ID: 235444 [Multi-domain] Cd Length: 854 Bit Score: 545.07 E-value: 9.32e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 188 YLNWK-RFPDCILLTRVGKFYESYFEPARYLASILSLSLAEKKYGANEakrSYPFAGFPVPTLDKYLKILVqDLGHTVVL 266
Cdd:PRK05399 15 YLEIKaQYPDALLFFRMGDFYELFFEDAKKASRLLDITLTKRGKSAGE---PIPMAGVPYHAAEGYLAKLV-KKGYKVAI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 267 VEEYDTEGavahTGKkltagsGPKERRVYRVVTPGTMVDESWVDTDQSRYLLAIAvgnkgQNGQELSLAYTDASTGEFFT 346
Cdd:PRK05399 91 CEQVEDPA----TAK------GPVKREVVRIVTPGTVTDEALLDEKQNNYLAAIA-----QDGGGYGLAYLDLSTGEFRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 347 KDTTVSQMEDELARITPREVVLDNSLYES----WRKHYNCSEMKPKDASQVEELLalLRVLGVKVSFADPCRPPLLYTSA 422
Cdd:PRK05399 156 TELDEEELLAELARLNPAEILVPEDFSEDelllLRRGLRRRPPWEFDLDTAEKRL--LEQFGVASLDGFGVDLPLAIRAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 423 ssptlhpttpeenaAALLqHHLQYALRESMPALRQPHKQSNSAFMQIDAATLQALEIRHAFRPGgliatgetqinsspls 502
Cdd:PRK05399 234 --------------GALL-QYLKETQKRSLPHLRSPKRYEESDYLILDAATRRNLELTENLRGG---------------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 503 TKGTLLSVVSKTITSSGHRLLIRTLTAPSTSPDIINSRLALVQAFVDREDLKTELRHELKELGDIMRIIQRFRGQRGTRR 582
Cdd:PRK05399 283 RKNSLLSVLDRTVTAMGGRLLRRWLHRPLRDREAIEARLDAVEELLEDPLLREDLRELLKGVYDLERLLSRIALGRANPR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 583 DIwdvgRWIRGAQRILETIKGEIKievgrnnvevvrkSEGITRLKEFVDSFRDLDRVASKIESS-VDESAIMFRSGDdks 661
Cdd:PRK05399 363 DL----AALRDSLEALPELKELLA-------------ELDSPLLAELAEQLDPLEELADLLERAiVEEPPLLIRDGG--- 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 662 iideqeagdallrsqasskeseaeekqrikrerderemsewWIRPQFSPALqlrhDELIALKAEAQ----KLQASLIKKY 737
Cdd:PRK05399 423 -----------------------------------------VIADGYDAEL----DELRALSDNGKdwlaELEARERERT 457
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 738 DTPTLTIEKNHRFSYHIQMSAKDAEKV----------AKArslERigsttgktayFAYAPLAELGTRIeimieyLGAAQR 807
Cdd:PRK05399 458 GISSLKVGYNKVFGYYIEVTKANLDKVpedyirrqtlKNA---ER----------YITPELKELEDKI------LSAEEK 518
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 808 RAARELQ------NMVVEQSDIIQQNSELVDELDLSLSFAQNAVEMNWVRPILDNSTELQIINGRHPSVESSLLSASrnF 881
Cdd:PRK05399 519 ALALEYElfeelrEEVAEHIERLQKLAKALAELDVLASLAEVAEENNYVRPEFTDDPGIDIEEGRHPVVEQVLGGEP--F 596
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 882 TPNSTHMASDTHLHVITGPNQGGKSTLLRQTAVIAILAQSGSFVPAEYVKMGIVDRVFSRVGARDDLWRDRSTFMLEMVE 961
Cdd:PRK05399 597 VPNDCDLDEERRLLLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAESARIGIVDRIFTRIGASDDLASGRSTFMVEMTE 676
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 1216338624 962 TAGILRHATERSLVIMDEIGRGTTLQAGVSIAYATLDYILENIKCRTLFATHYHEL 1017
Cdd:PRK05399 677 TANILNNATERSLVLLDEIGRGTSTYDGLSIAWAVAEYLHDKIGAKTLFATHYHEL 732
|
|
| MutS |
COG0249 |
DNA mismatch repair ATPase MutS [Replication, recombination and repair]; |
188-1020 |
1.15e-177 |
|
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
Pssm-ID: 440019 [Multi-domain] Cd Length: 861 Bit Score: 542.73 E-value: 1.15e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 188 YLNWK-RFPDCILLTRVGKFYESYFEPARYLASILSLSLAEKKYGANEakrSYPFAGFPVPTLDKYLKILVqDLGHTVVL 266
Cdd:COG0249 14 YLEIKaQYPDALLFFRMGDFYELFFEDAEKASRLLDITLTKRGKGAGE---PIPMAGVPYHAAEGYLAKLV-KAGYKVAI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 267 VEEYDTEGavahTGKkltagsGPKERRVYRVVTPGTMVDESWVDTDQSRYLLAIAvgnkgQNGQELSLAYTDASTGEFFT 346
Cdd:COG0249 90 CEQVEDPA----EAK------GLVKREVVRVVTPGTLTEDALLDAKRNNYLAAVA-----RDKGRYGLAWLDISTGEFLV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 347 KDTT-VSQMEDELARITPREVVLdnslyeswrkhyncsemkPKDASQVEELLALLRVLGVKVSFadpcRPPLLYTSASS- 424
Cdd:COG0249 155 TELDgEEALLDELARLAPAEILV------------------PEDLPDPEELLELLRERGAAVTR----LPDWAFDPDAAr 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 425 ---------PTL-----HPTTPEENAAALLQHHLQYALRESMPALRQPHKQSNSAFMQIDAATLQALEIRHAFRPGglia 490
Cdd:COG0249 213 rrlleqfgvASLdgfglEDLPAAIAAAGALLAYLEETQKGALPHLRRLRRYEEDDYLILDAATRRNLELTETLRGG---- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 491 tgetqinssplsTKGTLLSVVSKTITSSGHRLLIRTLTAPSTSPDIINSRLALVQAFVDREDLKTELRHELKELGDIMRI 570
Cdd:COG0249 289 ------------RKGSLLSVLDRTVTAMGSRLLRRWLLRPLRDRAAIEARLDAVEELLEDPLLREELRELLKGVYDLERL 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 571 IQRFRGQRGTRRDIwdvgRWIRGAQRILETIKGEIKievgrnnvevvrkSEGITRLKEFVDSFRDLDRVASKIESS-VDE 649
Cdd:COG0249 357 LSRIALGRANPRDL----AALRDSLAALPELKELLA-------------ELDSPLLAELAEALDPLEDLAELLERAiVDE 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 650 SAIMFRSGDdksiideqeagdallrsqasskeseaeekqrikrerderemsewWIRPQFSPALqlrhDELIALKAEAQK- 728
Cdd:COG0249 420 PPLLIRDGG--------------------------------------------VIREGYDAEL----DELRELSENGKEw 451
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 729 ---LQASLIKKYDTPTLTIEKNHRFSYHIQMSAKDAEKV----------AKArslERIgsTTgktayfayaP-LAELGTR 794
Cdd:COG0249 452 laeLEARERERTGIKSLKVGYNKVFGYYIEVTKANADKVpddyirkqtlKNA---ERY--IT---------PeLKELEDK 517
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 795 IeimieyLGAAQRRAARELQ------NMVVEQSDIIQQNSELVDELDLSLSFAQNAVEMNWVRPILDNSTELQIINGRHP 868
Cdd:COG0249 518 I------LSAEERALALEYElfeelrEEVAAHIERLQALARALAELDVLASLAEVAVENNYVRPELDDSPGIEIEGGRHP 591
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 869 SVESSLlsASRNFTPNSTHMASDTHLHVITGPNQGGKSTLLRQTAVIAILAQSGSFVPAEYVKMGIVDRVFSRVGARDDL 948
Cdd:COG0249 592 VVEQAL--PGEPFVPNDCDLDPDRRILLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAESARIGIVDRIFTRVGASDDL 669
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1216338624 949 WRDRSTFMLEMVETAGILRHATERSLVIMDEIGRGTTLQAGVSIAYATLDYILENIKCRTLFATHYHELGQM 1020
Cdd:COG0249 670 ARGQSTFMVEMTETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAVAEYLHDKIRARTLFATHYHELTEL 741
|
|
| mutS1 |
TIGR01070 |
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair] |
181-1020 |
1.69e-118 |
|
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273427 [Multi-domain] Cd Length: 840 Bit Score: 386.05 E-value: 1.69e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 181 TPLAHEvYLNWK-RFPDCILLTRVGKFYESYFEPARYLASILSLSLAEKKYGANEakrSYPFAGFPVPTLDKYLKILVQd 259
Cdd:TIGR01070 2 TPMMQQ-YLKLKaEHPDALLFFRMGDFYELFYEDAKKAAQLLDISLTSRGQSADE---PIPMAGIPYHAVEAYLEKLVK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 260 LGHTVVLVEEydTEGAvahtgkklTAGSGPKERRVYRVVTPGTMVDESWVDTDQSRYLLAIAVGNKGqngqeLSLAYTDA 339
Cdd:TIGR01070 77 QGESVAICEQ--IEDP--------KTAKGPVEREVVQLITPGTVSDEALLPERQDNLLAAIAQESNG-----FGLATLDL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 340 STGEFF-TKDTTVSQMEDELARITPREVVLDNSLyeswrkhyncSEMKPKDASQVEELLAllrVLGVKVSFADPCRPPLl 418
Cdd:TIGR01070 142 TTGEFKvTELADKETLYAELQRLNPAEVLLAEDL----------SEMEAIELREFRKDTA---VMSLEAQFGTEDLGGL- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 419 ytsasspTLHPTTPEENAAALLqhhLQYALRESMPALrqPHKQS-----NSAFMQIDAATLQALEIRHAFRPGgliatge 493
Cdd:TIGR01070 208 -------GLRNAPLGLTAAGCL---LQYAKRTQRTAL--PHLQPvrlyeLQDFMQLDAATRRNLELTENLRGG------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 494 tqinssplsTKGTLLSVVSKTITSSGHRLLIRTLTAPSTSPDIINSRLALVQAFVDREDLKTELRHELKELGDIMRIIQR 573
Cdd:TIGR01070 269 ---------KQNTLFSVLDETKTAMGSRLLKRWLHRPLRDREVLEARQDTVEVLLRHFFLREGLRPLLKEVGDLERLAAR 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 574 FRGQRGTRRDIwdvGRwIRGAQRILETIKGEIKIEVGrnnvevvrksegiTRLKEFVDSFRDLDRVASKIESS-VDESAI 652
Cdd:TIGR01070 340 VALGNARPRDL---AR-LRTSLEQLPELRALLEELEG-------------PTLQALAAQIDDFSELLELLEAAlIENPPL 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 653 MFRSGddkSIIDE--QEAGDALLRSQASSKESEAEEKQRikrerdEREMSewwirpqfspalqlrhdelialkaeaqklq 730
Cdd:TIGR01070 403 VVRDG---GLIREgyDEELDELRAASREGTDYLARLEAR------ERERT------------------------------ 443
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 731 aslikkyDTPTLTIEKNHRFSYHIQMSAKDAEKVAKarSLERIGSTTGKTAYFayapLAELGTRIEIMIEYLGAAQRRAA 810
Cdd:TIGR01070 444 -------GIPTLKVGYNAVFGYYIEVTRGQLHLVPA--HYRRRQTLKNAERYI----TPELKEKEDKVLEAEGKILALEK 510
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 811 R---ELQNMVVEQSDIIQQNSELVDELDLSLSFAQNAVEMNWVRPILDNSTELQIINGRHPSVESSLlsaSRNFTPNSTH 887
Cdd:TIGR01070 511 ElfeELRELLKKYLEALQEAARALAELDVLANLAEVAETLHYTRPRFGDDPQLRIREGRHPVVEQVL---RTPFVPNDLE 587
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 888 MASDTHLHVITGPNQGGKSTLLRQTAVIAILAQSGSFVPAEYVKMGIVDRVFSRVGARDDLWRDRSTFMLEMVETAGILR 967
Cdd:TIGR01070 588 MAHNRRMLLITGPNMGGKSTYMRQTALIALLAQIGSFVPAESAELPLFDRIFTRIGASDDLASGRSTFMVEMTEAANILH 667
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 1216338624 968 HATERSLVIMDEIGRGTTLQAGVSIAYATLDYILENIKCRTLFATHYHELGQM 1020
Cdd:TIGR01070 668 NATENSLVLFDEIGRGTSTYDGLALAWAIAEYLHEHIRAKTLFATHYFELTAL 720
|
|
| ABC_MutS1 |
cd03284 |
ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair ... |
861-1074 |
1.52e-78 |
|
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: 256.42 E-value: 1.52e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 861 QIINGRHPSVESSLlsASRNFTPNSTHMASDTHLHVITGPNQGGKSTLLRQTAVIAILAQSGSFVPAEYVKMGIVDRVFS 940
Cdd:cd03284 1 EIEGGRHPVVEQVL--DNEPFVPNDTELDPERQILLITGPNMAGKSTYLRQVALIALLAQIGSFVPASKAEIGVVDRIFT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 941 RVGARDDLWRDRSTFMLEMVETAGILRHATERSLVIMDEIGRGTTLQAGVSIAYATLDYILENIKCRTLFATHYHELGQM 1020
Cdd:cd03284 79 RIGASDDLAGGRSTFMVEMVETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAIVEYLHEKIGAKTLFATHYHELTEL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1216338624 1021 LGYNPKRAGGEVikgrsgitfwctDVDEADGVFSYSYKLRPGINYNSHAI--VRLA 1074
Cdd:cd03284 159 EGKLPRVKNFHV------------AVKEKGGGVVFLHKIVEGAADKSYGIevARLA 202
|
|
| MutS_V |
pfam00488 |
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
895-1074 |
8.66e-71 |
|
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: 234.01 E-value: 8.66e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 895 HVITGPNQGGKSTLLRQTAVIAILAQSGSFVPAEYVKMGIVDRVFSRVGARDDLWRDRSTFMLEMVETAGILRHATERSL 974
Cdd:pfam00488 1 LIITGPNMGGKSTYLRQVALIVLMAQIGSFVPAESAEIGIVDRIFTRIGASDDLAKGRSTFMVEMLETANILHNATDKSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 975 VIMDEIGRGTTLQAGVSIAYATLDYILENIKCRTLFATHYHELGQMlgynpkragGEVIKGRSGITFwctDVDEADGVFS 1054
Cdd:pfam00488 81 VILDELGRGTSTYDGLAIAWAVAEHLAEKIKARTLFATHYHELTKL---------AEKLPAVKNLHM---AAVEDDDDIV 148
|
170 180
....*....|....*....|..
gi 1216338624 1055 YSYKLRPGINYNSHAI--VRLA 1074
Cdd:pfam00488 149 FLYKVQPGAADKSYGIhvAELA 170
|
|
| MUTSac |
smart00534 |
ATPase domain of DNA mismatch repair MUTS family; |
894-1070 |
2.42e-70 |
|
ATPase domain of DNA mismatch repair MUTS family;
Pssm-ID: 197777 [Multi-domain] Cd Length: 185 Bit Score: 232.45 E-value: 2.42e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 894 LHVITGPNQGGKSTLLRQTAVIAILAQSGSFVPAEYVKMGIVDRVFSRVGARDDLWRDRSTFMLEMVETAGILRHATERS 973
Cdd:smart00534 1 VVIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPVFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATKNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 974 LVIMDEIGRGTTLQAGVSIAYATLDYILENIKCRTLFATHYHELGQMLGYNPkraggevikgrsGITFWCTDVDEADGVF 1053
Cdd:smart00534 81 LVLLDELGRGTSTYDGLAIAAAILEYLLEKIGARTLFATHYHELTKLADNHP------------GVRNLHMSALEETENI 148
|
170
....*....|....*..
gi 1216338624 1054 SYSYKLRPGINYNSHAI 1070
Cdd:smart00534 149 TFLYKLKPGVAGKSYGI 165
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05399 |
PRK05399 |
DNA mismatch repair protein MutS; Provisional |
188-1017 |
9.32e-179 |
|
DNA mismatch repair protein MutS; Provisional
Pssm-ID: 235444 [Multi-domain] Cd Length: 854 Bit Score: 545.07 E-value: 9.32e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 188 YLNWK-RFPDCILLTRVGKFYESYFEPARYLASILSLSLAEKKYGANEakrSYPFAGFPVPTLDKYLKILVqDLGHTVVL 266
Cdd:PRK05399 15 YLEIKaQYPDALLFFRMGDFYELFFEDAKKASRLLDITLTKRGKSAGE---PIPMAGVPYHAAEGYLAKLV-KKGYKVAI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 267 VEEYDTEGavahTGKkltagsGPKERRVYRVVTPGTMVDESWVDTDQSRYLLAIAvgnkgQNGQELSLAYTDASTGEFFT 346
Cdd:PRK05399 91 CEQVEDPA----TAK------GPVKREVVRIVTPGTVTDEALLDEKQNNYLAAIA-----QDGGGYGLAYLDLSTGEFRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 347 KDTTVSQMEDELARITPREVVLDNSLYES----WRKHYNCSEMKPKDASQVEELLalLRVLGVKVSFADPCRPPLLYTSA 422
Cdd:PRK05399 156 TELDEEELLAELARLNPAEILVPEDFSEDelllLRRGLRRRPPWEFDLDTAEKRL--LEQFGVASLDGFGVDLPLAIRAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 423 ssptlhpttpeenaAALLqHHLQYALRESMPALRQPHKQSNSAFMQIDAATLQALEIRHAFRPGgliatgetqinsspls 502
Cdd:PRK05399 234 --------------GALL-QYLKETQKRSLPHLRSPKRYEESDYLILDAATRRNLELTENLRGG---------------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 503 TKGTLLSVVSKTITSSGHRLLIRTLTAPSTSPDIINSRLALVQAFVDREDLKTELRHELKELGDIMRIIQRFRGQRGTRR 582
Cdd:PRK05399 283 RKNSLLSVLDRTVTAMGGRLLRRWLHRPLRDREAIEARLDAVEELLEDPLLREDLRELLKGVYDLERLLSRIALGRANPR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 583 DIwdvgRWIRGAQRILETIKGEIKievgrnnvevvrkSEGITRLKEFVDSFRDLDRVASKIESS-VDESAIMFRSGDdks 661
Cdd:PRK05399 363 DL----AALRDSLEALPELKELLA-------------ELDSPLLAELAEQLDPLEELADLLERAiVEEPPLLIRDGG--- 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 662 iideqeagdallrsqasskeseaeekqrikrerderemsewWIRPQFSPALqlrhDELIALKAEAQ----KLQASLIKKY 737
Cdd:PRK05399 423 -----------------------------------------VIADGYDAEL----DELRALSDNGKdwlaELEARERERT 457
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 738 DTPTLTIEKNHRFSYHIQMSAKDAEKV----------AKArslERigsttgktayFAYAPLAELGTRIeimieyLGAAQR 807
Cdd:PRK05399 458 GISSLKVGYNKVFGYYIEVTKANLDKVpedyirrqtlKNA---ER----------YITPELKELEDKI------LSAEEK 518
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 808 RAARELQ------NMVVEQSDIIQQNSELVDELDLSLSFAQNAVEMNWVRPILDNSTELQIINGRHPSVESSLLSASrnF 881
Cdd:PRK05399 519 ALALEYElfeelrEEVAEHIERLQKLAKALAELDVLASLAEVAEENNYVRPEFTDDPGIDIEEGRHPVVEQVLGGEP--F 596
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 882 TPNSTHMASDTHLHVITGPNQGGKSTLLRQTAVIAILAQSGSFVPAEYVKMGIVDRVFSRVGARDDLWRDRSTFMLEMVE 961
Cdd:PRK05399 597 VPNDCDLDEERRLLLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAESARIGIVDRIFTRIGASDDLASGRSTFMVEMTE 676
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 1216338624 962 TAGILRHATERSLVIMDEIGRGTTLQAGVSIAYATLDYILENIKCRTLFATHYHEL 1017
Cdd:PRK05399 677 TANILNNATERSLVLLDEIGRGTSTYDGLSIAWAVAEYLHDKIGAKTLFATHYHEL 732
|
|
| MutS |
COG0249 |
DNA mismatch repair ATPase MutS [Replication, recombination and repair]; |
188-1020 |
1.15e-177 |
|
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
Pssm-ID: 440019 [Multi-domain] Cd Length: 861 Bit Score: 542.73 E-value: 1.15e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 188 YLNWK-RFPDCILLTRVGKFYESYFEPARYLASILSLSLAEKKYGANEakrSYPFAGFPVPTLDKYLKILVqDLGHTVVL 266
Cdd:COG0249 14 YLEIKaQYPDALLFFRMGDFYELFFEDAEKASRLLDITLTKRGKGAGE---PIPMAGVPYHAAEGYLAKLV-KAGYKVAI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 267 VEEYDTEGavahTGKkltagsGPKERRVYRVVTPGTMVDESWVDTDQSRYLLAIAvgnkgQNGQELSLAYTDASTGEFFT 346
Cdd:COG0249 90 CEQVEDPA----EAK------GLVKREVVRVVTPGTLTEDALLDAKRNNYLAAVA-----RDKGRYGLAWLDISTGEFLV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 347 KDTT-VSQMEDELARITPREVVLdnslyeswrkhyncsemkPKDASQVEELLALLRVLGVKVSFadpcRPPLLYTSASS- 424
Cdd:COG0249 155 TELDgEEALLDELARLAPAEILV------------------PEDLPDPEELLELLRERGAAVTR----LPDWAFDPDAAr 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 425 ---------PTL-----HPTTPEENAAALLQHHLQYALRESMPALRQPHKQSNSAFMQIDAATLQALEIRHAFRPGglia 490
Cdd:COG0249 213 rrlleqfgvASLdgfglEDLPAAIAAAGALLAYLEETQKGALPHLRRLRRYEEDDYLILDAATRRNLELTETLRGG---- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 491 tgetqinssplsTKGTLLSVVSKTITSSGHRLLIRTLTAPSTSPDIINSRLALVQAFVDREDLKTELRHELKELGDIMRI 570
Cdd:COG0249 289 ------------RKGSLLSVLDRTVTAMGSRLLRRWLLRPLRDRAAIEARLDAVEELLEDPLLREELRELLKGVYDLERL 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 571 IQRFRGQRGTRRDIwdvgRWIRGAQRILETIKGEIKievgrnnvevvrkSEGITRLKEFVDSFRDLDRVASKIESS-VDE 649
Cdd:COG0249 357 LSRIALGRANPRDL----AALRDSLAALPELKELLA-------------ELDSPLLAELAEALDPLEDLAELLERAiVDE 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 650 SAIMFRSGDdksiideqeagdallrsqasskeseaeekqrikrerderemsewWIRPQFSPALqlrhDELIALKAEAQK- 728
Cdd:COG0249 420 PPLLIRDGG--------------------------------------------VIREGYDAEL----DELRELSENGKEw 451
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 729 ---LQASLIKKYDTPTLTIEKNHRFSYHIQMSAKDAEKV----------AKArslERIgsTTgktayfayaP-LAELGTR 794
Cdd:COG0249 452 laeLEARERERTGIKSLKVGYNKVFGYYIEVTKANADKVpddyirkqtlKNA---ERY--IT---------PeLKELEDK 517
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 795 IeimieyLGAAQRRAARELQ------NMVVEQSDIIQQNSELVDELDLSLSFAQNAVEMNWVRPILDNSTELQIINGRHP 868
Cdd:COG0249 518 I------LSAEERALALEYElfeelrEEVAAHIERLQALARALAELDVLASLAEVAVENNYVRPELDDSPGIEIEGGRHP 591
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 869 SVESSLlsASRNFTPNSTHMASDTHLHVITGPNQGGKSTLLRQTAVIAILAQSGSFVPAEYVKMGIVDRVFSRVGARDDL 948
Cdd:COG0249 592 VVEQAL--PGEPFVPNDCDLDPDRRILLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAESARIGIVDRIFTRVGASDDL 669
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1216338624 949 WRDRSTFMLEMVETAGILRHATERSLVIMDEIGRGTTLQAGVSIAYATLDYILENIKCRTLFATHYHELGQM 1020
Cdd:COG0249 670 ARGQSTFMVEMTETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAVAEYLHDKIRARTLFATHYHELTEL 741
|
|
| mutS1 |
TIGR01070 |
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair] |
181-1020 |
1.69e-118 |
|
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273427 [Multi-domain] Cd Length: 840 Bit Score: 386.05 E-value: 1.69e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 181 TPLAHEvYLNWK-RFPDCILLTRVGKFYESYFEPARYLASILSLSLAEKKYGANEakrSYPFAGFPVPTLDKYLKILVQd 259
Cdd:TIGR01070 2 TPMMQQ-YLKLKaEHPDALLFFRMGDFYELFYEDAKKAAQLLDISLTSRGQSADE---PIPMAGIPYHAVEAYLEKLVK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 260 LGHTVVLVEEydTEGAvahtgkklTAGSGPKERRVYRVVTPGTMVDESWVDTDQSRYLLAIAVGNKGqngqeLSLAYTDA 339
Cdd:TIGR01070 77 QGESVAICEQ--IEDP--------KTAKGPVEREVVQLITPGTVSDEALLPERQDNLLAAIAQESNG-----FGLATLDL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 340 STGEFF-TKDTTVSQMEDELARITPREVVLDNSLyeswrkhyncSEMKPKDASQVEELLAllrVLGVKVSFADPCRPPLl 418
Cdd:TIGR01070 142 TTGEFKvTELADKETLYAELQRLNPAEVLLAEDL----------SEMEAIELREFRKDTA---VMSLEAQFGTEDLGGL- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 419 ytsasspTLHPTTPEENAAALLqhhLQYALRESMPALrqPHKQS-----NSAFMQIDAATLQALEIRHAFRPGgliatge 493
Cdd:TIGR01070 208 -------GLRNAPLGLTAAGCL---LQYAKRTQRTAL--PHLQPvrlyeLQDFMQLDAATRRNLELTENLRGG------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 494 tqinssplsTKGTLLSVVSKTITSSGHRLLIRTLTAPSTSPDIINSRLALVQAFVDREDLKTELRHELKELGDIMRIIQR 573
Cdd:TIGR01070 269 ---------KQNTLFSVLDETKTAMGSRLLKRWLHRPLRDREVLEARQDTVEVLLRHFFLREGLRPLLKEVGDLERLAAR 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 574 FRGQRGTRRDIwdvGRwIRGAQRILETIKGEIKIEVGrnnvevvrksegiTRLKEFVDSFRDLDRVASKIESS-VDESAI 652
Cdd:TIGR01070 340 VALGNARPRDL---AR-LRTSLEQLPELRALLEELEG-------------PTLQALAAQIDDFSELLELLEAAlIENPPL 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 653 MFRSGddkSIIDE--QEAGDALLRSQASSKESEAEEKQRikrerdEREMSewwirpqfspalqlrhdelialkaeaqklq 730
Cdd:TIGR01070 403 VVRDG---GLIREgyDEELDELRAASREGTDYLARLEAR------ERERT------------------------------ 443
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 731 aslikkyDTPTLTIEKNHRFSYHIQMSAKDAEKVAKarSLERIGSTTGKTAYFayapLAELGTRIEIMIEYLGAAQRRAA 810
Cdd:TIGR01070 444 -------GIPTLKVGYNAVFGYYIEVTRGQLHLVPA--HYRRRQTLKNAERYI----TPELKEKEDKVLEAEGKILALEK 510
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 811 R---ELQNMVVEQSDIIQQNSELVDELDLSLSFAQNAVEMNWVRPILDNSTELQIINGRHPSVESSLlsaSRNFTPNSTH 887
Cdd:TIGR01070 511 ElfeELRELLKKYLEALQEAARALAELDVLANLAEVAETLHYTRPRFGDDPQLRIREGRHPVVEQVL---RTPFVPNDLE 587
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 888 MASDTHLHVITGPNQGGKSTLLRQTAVIAILAQSGSFVPAEYVKMGIVDRVFSRVGARDDLWRDRSTFMLEMVETAGILR 967
Cdd:TIGR01070 588 MAHNRRMLLITGPNMGGKSTYMRQTALIALLAQIGSFVPAESAELPLFDRIFTRIGASDDLASGRSTFMVEMTEAANILH 667
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 1216338624 968 HATERSLVIMDEIGRGTTLQAGVSIAYATLDYILENIKCRTLFATHYHELGQM 1020
Cdd:TIGR01070 668 NATENSLVLFDEIGRGTSTYDGLALAWAIAEYLHEHIRAKTLFATHYFELTAL 720
|
|
| ABC_MutS1 |
cd03284 |
ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair ... |
861-1074 |
1.52e-78 |
|
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: 256.42 E-value: 1.52e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 861 QIINGRHPSVESSLlsASRNFTPNSTHMASDTHLHVITGPNQGGKSTLLRQTAVIAILAQSGSFVPAEYVKMGIVDRVFS 940
Cdd:cd03284 1 EIEGGRHPVVEQVL--DNEPFVPNDTELDPERQILLITGPNMAGKSTYLRQVALIALLAQIGSFVPASKAEIGVVDRIFT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 941 RVGARDDLWRDRSTFMLEMVETAGILRHATERSLVIMDEIGRGTTLQAGVSIAYATLDYILENIKCRTLFATHYHELGQM 1020
Cdd:cd03284 79 RIGASDDLAGGRSTFMVEMVETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAIVEYLHEKIGAKTLFATHYHELTEL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1216338624 1021 LGYNPKRAGGEVikgrsgitfwctDVDEADGVFSYSYKLRPGINYNSHAI--VRLA 1074
Cdd:cd03284 159 EGKLPRVKNFHV------------AVKEKGGGVVFLHKIVEGAADKSYGIevARLA 202
|
|
| MutS_V |
pfam00488 |
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
895-1074 |
8.66e-71 |
|
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: 234.01 E-value: 8.66e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 895 HVITGPNQGGKSTLLRQTAVIAILAQSGSFVPAEYVKMGIVDRVFSRVGARDDLWRDRSTFMLEMVETAGILRHATERSL 974
Cdd:pfam00488 1 LIITGPNMGGKSTYLRQVALIVLMAQIGSFVPAESAEIGIVDRIFTRIGASDDLAKGRSTFMVEMLETANILHNATDKSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 975 VIMDEIGRGTTLQAGVSIAYATLDYILENIKCRTLFATHYHELGQMlgynpkragGEVIKGRSGITFwctDVDEADGVFS 1054
Cdd:pfam00488 81 VILDELGRGTSTYDGLAIAWAVAEHLAEKIKARTLFATHYHELTKL---------AEKLPAVKNLHM---AAVEDDDDIV 148
|
170 180
....*....|....*....|..
gi 1216338624 1055 YSYKLRPGINYNSHAI--VRLA 1074
Cdd:pfam00488 149 FLYKVQPGAADKSYGIhvAELA 170
|
|
| MUTSac |
smart00534 |
ATPase domain of DNA mismatch repair MUTS family; |
894-1070 |
2.42e-70 |
|
ATPase domain of DNA mismatch repair MUTS family;
Pssm-ID: 197777 [Multi-domain] Cd Length: 185 Bit Score: 232.45 E-value: 2.42e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 894 LHVITGPNQGGKSTLLRQTAVIAILAQSGSFVPAEYVKMGIVDRVFSRVGARDDLWRDRSTFMLEMVETAGILRHATERS 973
Cdd:smart00534 1 VVIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPVFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATKNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 974 LVIMDEIGRGTTLQAGVSIAYATLDYILENIKCRTLFATHYHELGQMLGYNPkraggevikgrsGITFWCTDVDEADGVF 1053
Cdd:smart00534 81 LVLLDELGRGTSTYDGLAIAAAILEYLLEKIGARTLFATHYHELTKLADNHP------------GVRNLHMSALEETENI 148
|
170
....*....|....*..
gi 1216338624 1054 SYSYKLRPGINYNSHAI 1070
Cdd:smart00534 149 TFLYKLKPGVAGKSYGI 165
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
861-1070 |
2.78e-66 |
|
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: 221.74 E-value: 2.78e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 861 QIINGRHPSVESSLLSasRNFTPNSTHMaSDTHLHVITGPNQGGKSTLLRQTAVIAILAQSGSFVPAEYVKMGIVDRVFS 940
Cdd:cd03243 1 EIKGGRHPVLLALTKG--ETFVPNDINL-GSGRLLLITGPNMGGKSTYLRSIGLAVLLAQIGCFVPAESASIPLVDRIFT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 941 RVGARDDLWRDRSTFMLEMVETAGILRHATERSLVIMDEIGRGTTLQAGVSIAYATLDYILEnIKCRTLFATHYHELGQM 1020
Cdd:cd03243 78 RIGAEDSISDGRSTFMAELLELKEILSLATPRSLVLIDELGRGTSTAEGLAIAYAVLEHLLE-KGCRTLFATHFHELADL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1216338624 1021 LgynpkraggeviKGRSGITFWCTDVDEADGVFSYSYKLRPGINYNSHAI 1070
Cdd:cd03243 157 P------------EQVPGVKNLHMEELITTGGLTFTYKLIDGICDPSYAL 194
|
|
| ABC_MSH3_euk |
cd03287 |
ATP-binding cassette domain of eukaryotic MutS3 homolog; The MutS protein initiates DNA ... |
860-1074 |
3.85e-60 |
|
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: 205.41 E-value: 3.85e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 860 LQIINGRHPSVESSLlsaSRNFTPNSTHMASDT-HLHVITGPNQGGKSTLLRQTAVIAILAQSGSFVPAEYVKMGIVDRV 938
Cdd:cd03287 1 ILIKEGRHPMIESLL---DKSFVPNDIHLSAEGgYCQIITGPNMGGKSSYIRQVALITIMAQIGSFVPASSATLSIFDSV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 939 FSRVGARDDLWRDRSTFMLEMVETAGILRHATERSLVIMDEIGRGTTLQAGVSIAYATLDYILENIKCRTLFATHYHELG 1018
Cdd:cd03287 78 LTRMGASDSIQHGMSTFMVELSETSHILSNCTSRSLVILDELGRGTSTHDGIAIAYATLHYLLEEKKCLVLFVTHYPSLG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1216338624 1019 QML-GYNPKRAGGEVIKGRSGITFWCTDVDEadgvFSYSYKLRPGINYNSHA--IVRLA 1074
Cdd:cd03287 158 EILrRFEGSIRNYHMSYLESQKDFETSDSQS----ITFLYKLVRGLASRSFGlnVARLA 212
|
|
| ABC_MSH2_euk |
cd03285 |
ATP-binding cassette domain of eukaryotic MutS2 homolog; The MutS protein initiates DNA ... |
862-1070 |
2.86e-58 |
|
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: 199.91 E-value: 2.86e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 862 IINGRHPSVESSLLSasrNFTPNSTHMASD-THLHVITGPNQGGKSTLLRQTAVIAILAQSGSFVPAEYVKMGIVDRVFS 940
Cdd:cd03285 2 LKEARHPCVEAQDDV---AFIPNDVTLTRGkSRFLIITGPNMGGKSTYIRQIGVIVLMAQIGCFVPCDSADIPIVDCILA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 941 RVGARDDLWRDRSTFMLEMVETAGILRHATERSLVIMDEIGRGTTLQAGVSIAYATLDYILENIKCRTLFATHYHELGQM 1020
Cdd:cd03285 79 RVGASDSQLKGVSTFMAEMLETAAILKSATENSLIIIDELGRGTSTYDGFGLAWAIAEYIATQIKCFCLFATHFHELTAL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1216338624 1021 lgynpkragGEVIKGRSGITFWCtDVDEADGVFSYSYKLRPGINYNSHAI 1070
Cdd:cd03285 159 ---------ADEVPNVKNLHVTA-LTDDASRTLTMLYKVEKGACDQSFGI 198
|
|
| ABC_MSH6_euk |
cd03286 |
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA ... |
865-1068 |
9.43e-56 |
|
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: 192.64 E-value: 9.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 865 GRHPSVESSLLSAsrnFTPNSTHM-ASDTHLHVITGPNQGGKSTLLRQTAVIAILAQSGSFVPAEYVKMGIVDRVFSRVG 943
Cdd:cd03286 5 LRHPCLNASTASS---FVPNDVDLgATSPRILVLTGPNMGGKSTLLRTVCLAVIMAQMGMDVPAKSMRLSLVDRIFTRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 944 ARDDLWRDRSTFMLEMVETAGILRHATERSLVIMDEIGRGTTLQAGVSIAYATLDYILENIKCRTLFATHYHELGQMLGY 1023
Cdd:cd03286 82 ARDDIMKGESTFMVELSETANILRHATPDSLVILDELGRGTSTHDGYAIAHAVLEYLVKKVKCLTLFSTHYHSLCDEFHE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1216338624 1024 NPKRAGGE---VIKGRSgitfwctDVDEADGVFsySYKLRPGINYNSH 1068
Cdd:cd03286 162 HGGVRLGHmacAVKNES-------DPTIRDITF--LYKLVAGICPKSY 200
|
|
| ABC_MSH5_euk |
cd03281 |
ATP-binding cassette domain of eukaryotic MutS5 homolog; The MutS protein initiates DNA ... |
861-1070 |
4.14e-54 |
|
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: 187.89 E-value: 4.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 861 QIINGRHPSVESsllsASRNFTPNSTHMASDTH-LHVITGPNQGGKSTLLRQTAVIAILAQSGSFVPAEYVKMGIVDRVF 939
Cdd:cd03281 1 EIQGGRHPLLEL----FVDSFVPNDTEIGGGGPsIMVITGPNSSGKSVYLKQVALIVFLAHIGSFVPADSATIGLVDKIF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 940 SRVGARDDLWRDRSTFMLEMVETAGILRHATERSLVIMDEIGRGTTLQAGVSIAYATLDYILE-NIKC-RTLFATHYHEL 1017
Cdd:cd03281 77 TRMSSRESVSSGQSAFMIDLYQVSKALRLATRRSLVLIDEFGKGTDTEDGAGLLIATIEHLLKrGPECpRVIVSTHFHEL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 1018 GQMlgynpkraggEVIKGRSGITFWCTDV-------DEADGVfSYSYKLRPGINYNSHAI 1070
Cdd:cd03281 157 FNR----------SLLPERLKIKFLTMEVllnptstSPNEDI-TYLYRLVPGLADTSFAI 205
|
|
| ABC_MSH4_euk |
cd03282 |
ATP-binding cassette domain of eukaryotic MutS4 homolog; The MutS protein initiates DNA ... |
862-1025 |
1.02e-43 |
|
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: 157.55 E-value: 1.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 862 IINGRHPSVESSllsaSRNFTPNSTHMASD-THLHVITGPNQGGKSTLLRQTAVIAILAQSGSFVPAEYVKMGIVDRVFS 940
Cdd:cd03282 2 IRDSRHPILDRD----KKNFIPNDIYLTRGsSRFHIITGPNMSGKSTYLKQIALLAIMAQIGCFVPAEYATLPIFNRLLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 941 RVGARDDLWRDRSTFMLEMVETAGILRHATERSLVIMDEIGRGTTLQAGVSIAYAtldyILENIKCR---TLFATHYHEL 1017
Cdd:cd03282 78 RLSNDDSMERNLSTFASEMSETAYILDYADGDSLVLIDELGRGTSSADGFAISLA----ILECLIKKestVFFATHFRDI 153
|
....*...
gi 1216338624 1018 GQMLGYNP 1025
Cdd:cd03282 154 AAILGNKS 161
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
510-1017 |
4.56e-41 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 163.00 E-value: 4.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 510 VVSKTITSSGhRLLIRTLTaPSTSPDIINSRLALVQAFVDREDLKTELrhELKELGDIMRIIQRFRgqRGTR---RDIWD 586
Cdd:COG1193 18 LAEYAVSELG-KELARKLR-PSTDLEEVERLLAETAEARRLLRLEGGL--PLGGIPDIRPLLKRAE--EGGVlspEELLD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 587 VGRWIRGAQRILETIKgeikievgrnnvevvRKSEGITRLKEFVDSFRDLDRVASKIESSVDEsaimfrsgdDKSIIDEq 666
Cdd:COG1193 92 IARTLRAARRLKRFLE---------------ELEEEYPALKELAERLPPLPELEKEIDRAIDE---------DGEVKDS- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 667 eAGDAL--LRSQASSKESEAEEK-QRIKRerderemsewwiRPQFSPALQ-----LRHDEL-IALKAEAqklqaslikky 737
Cdd:COG1193 147 -ASPELrrIRREIRSLEQRIREKlESILR------------SASYQKYLQdaiitIRNGRYvIPVKAEY----------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 738 dtptltieKNhrfsyhiqmsakdaekvakarsleRIG------STTGKTAYFAYAPLAELGTRIEimiEYLGAAQR---R 808
Cdd:COG1193 203 --------KG------------------------KIPgivhdqSASGQTLFIEPMAVVELNNELR---ELEAEERReieR 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 809 AARELQNMVVEQSDIIQQNSELVDELDLSLSFAQNAVEMNWVRPILDNSTELQIINGRHPsvessLLsASRNFTPNSTHM 888
Cdd:COG1193 248 ILRELSALVREYAEELLENLEILAELDFIFAKARYALELKAVKPELNDEGYIKLKKARHP-----LL-DLKKVVPIDIEL 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 889 ASDTHLHVITGPNQGGKSTLLRQTAVIAILAQSGSFVPA-EYVKMGIVDRVFSRVGARDDLWRDRSTF---MLEMVEtag 964
Cdd:COG1193 322 GEDFRTLVITGPNTGGKTVTLKTVGLLTLMAQSGLPIPAaEGSELPVFDNIFADIGDEQSIEQSLSTFsshMTNIVE--- 398
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1216338624 965 ILRHATERSLVIMDEIGRGTTLQAGVSIAYATLDYILEnIKCRTLFATHYHEL 1017
Cdd:COG1193 399 ILEKADENSLVLLDELGAGTDPQEGAALAIAILEELLE-RGARVVATTHYSEL 450
|
|
| MUTSd |
smart00533 |
DNA-binding domain of DNA mismatch repair MUTS family; |
504-871 |
2.16e-36 |
|
DNA-binding domain of DNA mismatch repair MUTS family;
Pssm-ID: 214710 [Multi-domain] Cd Length: 308 Bit Score: 140.13 E-value: 2.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 504 KGTLLSVVSKTITSSGHRLLIRTLTAPSTSPDIINSRLALVQAFVDREDLKTELRHELKELGDIMRIIQRFRGQRGTRRD 583
Cdd:smart00533 1 KGSLFELLNHTKTPMGKRLLRRWLLQPLLDLKEINERLDAVEELVENPELRQKLRQLLKRIPDLERLLSRIERGRASPRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 584 IwdvgrwirgaqriletikgeikievgrnnvevvrksegiTRLKEFVDSFRDLDRVASKIESSVDesaimfrsGDDKSII 663
Cdd:smart00533 81 L---------------------------------------LRLYDSLEGLKEIRQLLESLDGPLL--------GLLLKVI 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 664 DEQEAG--DALLRSQASSKESEAEEKQRIKRErderemsewwirpqFSPALQLRHDELIALKAEAQKLQASLIKKYDTPT 741
Cdd:smart00533 114 LEPLLEllELLLELLNDDDPLEVNDGGLIKDG--------------FDPELDELREKLEELEEELEELLKKEREELGIDS 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 742 LTIEKNHRFSYHIQMSAKDAEKVAKarSLERIgSTTGKTAYFAYAPLAELGTRIEIMIEYLGAAQRRAARELQNMVVEQS 821
Cdd:smart00533 180 LKLGYNKVHGYYIEVTKSEAKKVPK--DFIRR-SSLKNTERFTTPELKELENELLEAKEEIERLEKEILRELLEKVLEYL 256
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1216338624 822 DIIQQNSELVDELDLSLSFAQNAVEMNWVRPILDNSTELQIINGRHPSVE 871
Cdd:smart00533 257 EELRALAEALAELDVLLSLATLAAEGNYVRPEFVDSGELEIKNGRHPVLE 306
|
|
| MutS_III |
pfam05192 |
MutS domain III; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
472-841 |
3.88e-35 |
|
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: 136.00 E-value: 3.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 472 ATLQALEIRHAFRPGgliatgetqinssplsTKGTLLSVVSKTITSSGHRLLIRTLTAPSTSPDIINSRLALVQAFVDRE 551
Cdd:pfam05192 1 ATLRNLELTENLRGG----------------KEGSLLGLLDRTKTPMGSRLLRQWLLQPLTDLEEINERLDAVEELLENS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 552 DLKTELRHELKELGDIMRIIQRFRGQRGTRRDIwdvgrwirgaQRILETIKGEIKIEvgrnnvevvrksegITRLKEFVD 631
Cdd:pfam05192 65 ELREDLRELLRRLPDLERLLSRIALGKATPRDL----------LALLDSLEKLPLLK--------------ELLLEEKSA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 632 SFRDLDRVASKIESSVDESAIMFRSGDDKsiideqeagdallrsqasskeseaeekqrikrerderemsewwIRPQFSPA 711
Cdd:pfam05192 121 LLGELASLAELLEEAIDEEPPALLRDGGV-------------------------------------------IRDGYDEE 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 712 LQLRHDELIALKAEAQKLQASLIKKYDTPTLTIEKNHRFSYH-------IQMSAKDAEKVAKarSLERIgSTTGKTAYFA 784
Cdd:pfam05192 158 LDELRDLLLDGKRLLAKLEARERERTGIKSLKVLYNKVFGYYlllveyyIEVSKSQKDKVPD--DYIRI-QTTKNAERYI 234
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1216338624 785 YAPLAELGTRIEIMIEYLGAAQRRAARELQNMVVEQSDIIQQNSELVDELDLSLSFA 841
Cdd:pfam05192 235 TPELKELERKILQAEERLLALEKELFEELLEEVLEYIEVLRRAAEALAELDVLLSLA 291
|
|
| ABC_MutS2 |
cd03280 |
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ... |
861-1017 |
3.12e-29 |
|
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: 115.81 E-value: 3.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 861 QIINGRHPSvessLLSASRNFTPNSTHMASDTHLHVITGPNQGGKSTLLRQTAVIAILAQSGSFVPA-EYVKMGIVDRVF 939
Cdd:cd03280 1 RLREARHPL----LPLQGEKVVPLDIQLGENKRVLVITGPNAGGKTVTLKTLGLLTLMAQSGLPIPAaEGSSLPVFENIF 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1216338624 940 SRVGARDDLWRDRSTFMLEMVETAGILRHATERSLVIMDEIGRGTTLQAGVSIAYATLDYILENiKCRTLFATHYHEL 1017
Cdd:cd03280 77 ADIGDEQSIEQSLSTFSSHMKNIARILQHADPDSLVLLDELGSGTDPVEGAALAIAILEELLER-GALVIATTHYGEL 153
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
788-1024 |
3.14e-28 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 122.63 E-value: 3.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 788 LAELGTRIEIMIEylgaaqrRAARELQNMVVEQSDIIQQNSELVDELDLSLSFAQNAVEMNWVRPILDNSTELQIINGRH 867
Cdd:PRK00409 236 IRELRNKEEQEIE-------RILKELSAKVAKNLDFLKFLNKIFDELDFIFARARYAKALKATFPLFNDEGKIDLRQARH 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 868 PsvessLLSASRNfTPNSTHMASDTHLHVITGPNQGGKSTLLRQTAVIAILAQSGSFVPA-EYVKMGIVDRVFSRVGARD 946
Cdd:PRK00409 309 P-----LLDGEKV-VPKDISLGFDKTVLVITGPNTGGKTVTLKTLGLAALMAKSGLPIPAnEPSEIPVFKEIFADIGDEQ 382
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1216338624 947 DLWRDRSTFMLEMVETAGILRHATERSLVIMDEIGRGTTLQAGVSIAYATLDYILENiKCRTLFATHYHELgQMLGYN 1024
Cdd:PRK00409 383 SIEQSLSTFSGHMTNIVRILEKADKNSLVLFDELGAGTDPDEGAALAISILEYLRKR-GAKIIATTHYKEL-KALMYN 458
|
|
| mutS2 |
TIGR01069 |
MutS2 family protein; Function of MutS2 is unknown. It should not be considered a DNA mismatch ... |
615-1027 |
3.76e-26 |
|
MutS2 family protein; Function of MutS2 is unknown. It should not be considered a DNA mismatch repair protein. It is likely a DNA mismatch binding protein of unknown cellular function. [DNA metabolism, Other]
Pssm-ID: 130141 [Multi-domain] Cd Length: 771 Bit Score: 116.07 E-value: 3.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 615 EVVRKSEGITRLKEFVDSFRDLDRVAS-----KIESSVDESAIMFRS--GDDKSIIDEqeagDALLRSQASSKESEAEEK 687
Cdd:TIGR01069 79 GIVKGLEYILVIQNALKTVKHLKVLSEhvldlEILFHLRLNLITLPPleNDIIACIDD----DGKVKDGASEELDAIRES 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 688 QRIKRERDEREMSEWWIRPQFSPALQlrhDELIALKAeaqklqaslikkyDTPTLTIEKNHRFSYhiqmsakdaekvaKA 767
Cdd:TIGR01069 155 LKALEEEVVKRLHKIIRSKELAKYLS---DTIVTIRN-------------GRYVLPLKSGFKGKI-------------KG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 768 RSLERigSTTGKTAYFAYAPLAELGTRieimieyLGAAQRRAARELQNMVVEQSDIIQQNSELVDE-------LDLSLSF 840
Cdd:TIGR01069 206 IVHDT--SSSGETFYIEPQAIVKLNNK-------LAQLKNEEECEIEKILRTLSEKVQEYLLELKFlfkefdfLDSLQAR 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 841 AQNAVEMNWVRPILDNSTELQIINGRHPsvessLLSASRnFTPNSTHMASDTHLHVITGPNQGGKSTLLRQTAVIAILAQ 920
Cdd:TIGR01069 277 ARYAKAVKGEFPMPSFTGKIILENARHP-----LLKEPK-VVPFTLNLKFEKRVLAITGPNTGGKTVTLKTLGLLALMFQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 921 SGSFVPA-EYVKMGIVDRVFSRVGARDDLWRDRSTFMLEMVETAGILRHATERSLVIMDEIGRGTTLQAGVSIAYATLDY 999
Cdd:TIGR01069 351 SGIPIPAnEHSEIPYFEEIFADIGDEQSIEQNLSTFSGHMKNISAILSKTTENSLVLFDELGAGTDPDEGSALAISILEY 430
|
410 420
....*....|....*....|....*...
gi 1216338624 1000 iLENIKCRTLFATHYHELgQMLGYNPKR 1027
Cdd:TIGR01069 431 -LLKQNAQVLITTHYKEL-KALMYNNEG 456
|
|
| ABC_MutS-like |
cd03283 |
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ... |
861-1070 |
4.54e-25 |
|
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: 103.92 E-value: 4.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 861 QIINGRHPSVESSLLSAsrnftpNSTHMaSDTHLHVITGPNQGGKSTLLRQTAVIAILAQSGSFVPAEYVKmGIVDRVFS 940
Cdd:cd03283 1 EAKNLGHPLIGREKRVA------NDIDM-EKKNGILITGSNMSGKSTFLRTIGVNVILAQAGAPVCASSFE-LPPVKIFT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 941 RVGARDDLWRDRSTFMLEMVETAGILRHA--TERSLVIMDEIGRGTTLQAGVSIAYATLDYILENiKCRTLFATHYHELg 1018
Cdd:cd03283 73 SIRVSDDLRDGISYFYAELRRLKEIVEKAkkGEPVLFLLDEIFKGTNSRERQAASAAVLKFLKNK-NTIGIISTHDLEL- 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1216338624 1019 qmlgynpkragGEVIKGRSGITFWCTDVDEADGVFSYSYKLRPGINYNSHAI 1070
Cdd:cd03283 151 -----------ADLLDLDSAVRNYHFREDIDDNKLIFDYKLKPGVSPTRNAL 191
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
861-1021 |
1.60e-21 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 92.42 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 861 QIINGRHPSvessllsasrNFTPNSTHmASDTHLHVITGPNQGGKSTLLRQTAVIAILAQS----------GSFVPAEYv 930
Cdd:cd03227 1 KIVLGRFPS----------YFVPNDVT-FGEGSLTIITGPNGSGKSTILDAIGLALGGAQSatrrrsgvkaGCIVAAVS- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 931 kmgiVDRVFSRVGArddlwrdrSTFMLEMVETAGILRHAT--ERSLVIMDEIGRGTTLQAGVSIAYATLDYILEniKCRT 1008
Cdd:cd03227 69 ----AELIFTRLQL--------SGGEKELSALALILALASlkPRPLYILDEIDRGLDPRDGQALAEAILEHLVK--GAQV 134
|
170
....*....|...
gi 1216338624 1009 LFATHYHELGQML 1021
Cdd:cd03227 135 IVITHLPELAELA 147
|
|
| MutS_I |
pfam01624 |
MutS domain I; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
192-307 |
1.22e-20 |
|
MutS domain I; This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with pfam00488, 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 globular domain I, which is involved in DNA binding, in Thermus aquaticus MutS as characterized in.
Pssm-ID: 426350 [Multi-domain] Cd Length: 113 Bit Score: 88.03 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 192 KRFPDCILLTRVGKFYESYFEPARYLASILSLSLAEKKYGANEakrSYPFAGFPVPTLDKYLKILVQdLGHTVVLVEEyd 271
Cdd:pfam01624 12 SKYPDAVLFFRVGDFYELFGEDAEIAARELGITLTVRKGGSGK---RIPMAGVPEHAFERYARRLVN-KGYKVAICEQ-- 85
|
90 100 110
....*....|....*....|....*....|....*.
gi 1216338624 272 TEGAvahtgkklTAGSGPKERRVYRVVTPGTMVDES 307
Cdd:pfam01624 86 TETP--------AEAKGVVKREVVRVVTPGTLTDDE 113
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
896-1022 |
4.95e-08 |
|
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: 53.40 E-value: 4.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 896 VITGPNQGGKSTLLRQTAVIAILAqSGS-FVPAEYVKMGIVDRVFSRVGARDDLwrdrSTFMLEMVETAGILrhATERSL 974
Cdd:cd00267 29 ALVGPNGSGKSTLLRAIAGLLKPT-SGEiLIDGKDIAKLPLEELRRRIGYVPQL----SGGQRQRVALARAL--LLNPDL 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1216338624 975 VIMDEIGRGTTLQAGVSIAYATLDYILENikCRTLFATHYHELGQMLG 1022
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEG--RTVIIVTHDPELAELAA 147
|
|
| MutS_II |
pfam05188 |
MutS domain II; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
316-375 |
4.98e-07 |
|
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: 50.04 E-value: 4.98e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1216338624 316 YLLAIAVGNKGQNGqelsLAYTDASTGEFFTKDTT-VSQMEDELARITPREVVLDNSLYES 375
Cdd:pfam05188 2 YLAAISRGDGNRYG----LAFLDLSTGEFGVSEFEdFEELLAELSRLSPKELLLPESLSSS 58
|
|
| THEP1 |
COG1618 |
Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism]; |
896-982 |
5.15e-03 |
|
Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];
Pssm-ID: 441225 [Multi-domain] Cd Length: 175 Bit Score: 39.12 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216338624 896 VITGPNQGGKSTLLRQtaVIAILAQSGS----FVPAEYVKMG------IVD------RVFSRVGARDDLWRDRSTFMLEM 959
Cdd:COG1618 4 FITGRPGVGKTTLLLK--VVEELRDEGLrvggFITPEVREGGrrvgfkLVDlatgeeAILASVDIDSGPRVGKYGVDPEA 81
|
90 100
....*....|....*....|....*.
gi 1216338624 960 VETAGI--LRHATERS-LVIMDEIGR 982
Cdd:COG1618 82 LEAIAVeaLERALEEAdLIVIDEIGK 107
|
|
| |
