|
Name |
Accession |
Description |
Interval |
E-value |
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
5-786 |
0e+00 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 889.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 5 ENALEKLGFTEIKQLIKNHCISQMGHNMVDKIGFISNYDQILKFLQQTAEFKNILTSQEALPIQSFYDIKILADKARvEG 84
Cdd:COG1193 3 EKTLEKLEFDKILELLAEYAVSELGKELARKLRPSTDLEEVERLLAETAEARRLLRLEGGLPLGGIPDIRPLLKRAE-EG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 85 VFLSEDEFYQVHTSLLTVFAVISYFEQRKGVYPTLEALFENLAIEKAILKNIETVIDEKGKIKPNASKQLADLIGAIAKA 164
Cdd:COG1193 82 GVLSPEELLDIARTLRAARRLKRFLEELEEEYPALKELAERLPPLPELEKEIDRAIDEDGEVKDSASPELRRIRREIRSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 165 ENEARKKIDQIYKNAQSNNWLADGSLTVREGRICIPLLSENKRKIKGFIHDESASGQTVYIEPEEVFSLNNLVRDLEFDK 244
Cdd:COG1193 162 EQRIREKLESILRSASYQKYLQDAIITIRNGRYVIPVKAEYKGKIPGIVHDQSASGQTLFIEPMAVVELNNELRELEAEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 245 RREIIRILTNLTDKLRPYVPILIAYHCFLTKLDFVRAKALFAIVIAAEMPILSKQPIIKLFNAQHPLLFLahkkagKLVV 324
Cdd:COG1193 242 RREIERILRELSALVREYAEELLENLEILAELDFIFAKARYALELKAVKPELNDEGYIKLKKARHPLLDL------KKVV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 325 PLNILINDGSRIVLISGPNAGGKSVAMKTIGLLQIMVQAGLLIPAASQSEVGVFKQLFADIGDDQSIESDLSTYSAHLSK 404
Cdd:COG1193 316 PIDIELGEDFRTLVITGPNTGGKTVTLKTVGLLTLMAQSGLPIPAAEGSELPVFDNIFADIGDEQSIEQSLSTFSSHMTN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 405 MKHFTTFANDKTLLLIDEFGTGTDPLFGGPIAEAVLEVVNKKKAYGVITTHYSNLKLFANNTPGLENASMVFDNLNLQPM 484
Cdd:COG1193 396 IVEILEKADENSLVLLDELGAGTDPQEGAALAIAILEELLERGARVVATTHYSELKAYAYNTEGVENASVEFDVETLSPT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 485 YMLEMGKPGSSYAFEIAQKIGLSQHIIDLAKNKIGVQQRKMDTMLIDLERDKKEIIDKKISLDKQQRLYKELLEANEKQK 564
Cdd:COG1193 476 YRLLIGVPGRSNAFEIARRLGLPEEIIERARELLGEESIDVEKLIEELERERRELEEEREEAERLREELEKLREELEEKL 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 565 LYYAENKRNLIRDAKLEAQTIIKNANKLVENTIAEIKETKADKQTTQTLRANL---SAELRNNEIKP-ETAKPAPAENDF 640
Cdd:COG1193 556 EELEEEKEEILEKAREEAEEILREARKEAEELIRELREAQAEEEELKEARKKLeelKQELEEKLEKPkKKAKPAKPPEEL 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 641 KEGDWVKMIDTGNIAQVLEV-AKNNVVLAFGDLRSVVKLNRIQKIANNEVPKEVKRFAKMG-HTESAASFSVEIDLRGQR 718
Cdd:COG1193 636 KVGDRVRVLSLGQKGEVLEIpKGGEAEVQVGILKMTVKLSDLEKVEKKKPKKPKKRPAGVSvSVSKASTVSPELDLRGMR 715
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1579668503 719 GDDAIYELEKYFDKALMFGISNFKIIHGKGDGILRKLIRNYLKNYIQVQRLEDEHADRGGDGITYVYL 786
Cdd:COG1193 716 VEEALPELDKYLDDALLAGLPEVRIIHGKGTGALRKGVREYLKRHPYVKSFRLGEPGEGGDGVTVVEL 783
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
5-786 |
3.91e-178 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 530.55 E-value: 3.91e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 5 ENALEKLGFTEIKQLIKNHCISQMGHNMVDKIGFISNYDQILKFLQQTAEFKNILTSQEALPIQSFYDIKILADKARVEG 84
Cdd:PRK00409 3 EKTLRVLEFNKIKEQLKTFAASELGKEKVLQLDPETDFEEVEELLEETDEAAKLLRLKGLPPFEGVKDIDDALKRAEKGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 85 VfLSEDEFYQVHTslltvfaVISYFEQRKGV---------YPTLEALFENLAIEKAILKNIETVIDEKGKIKPNASKQLA 155
Cdd:PRK00409 83 V-LSGDELLEIAK-------TLRYFRQLKRFiedleeeeeLPILEEWVAKIRTLPELEQEIHNCIDEEGEVKDSASEKLR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 156 DLIGAIAKAENEARKKIDQIYKNAQSNNWLADGSLTVREGRICIPLLSENKRKIKGFIHDESASGQTVYIEPEEVFSLNN 235
Cdd:PRK00409 155 GIRRQLRRKKSRIREKLESIIRSKSLQKYLQDTIITIRNDRYVLPVKAEYKHAIKGIVHDQSSSGATLYIEPQSVVELNN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 236 LVRDLEFDKRREIIRILTNLTDKLRPYVPILIAYHCFLTKLDFVRAKALFAIVIAAEMPILSKQPIIKLFNAQHPLLfla 315
Cdd:PRK00409 235 EIRELRNKEEQEIERILKELSAKVAKNLDFLKFLNKIFDELDFIFARARYAKALKATFPLFNDEGKIDLRQARHPLL--- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 316 hkkAGKLVVPLNILINDGSRIVLISGPNAGGKSVAMKTIGLLQIMVQAGLLIPAASQSEVGVFKQLFADIGDDQSIESDL 395
Cdd:PRK00409 312 ---DGEKVVPKDISLGFDKTVLVITGPNTGGKTVTLKTLGLAALMAKSGLPIPANEPSEIPVFKEIFADIGDEQSIEQSL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 396 STYSAHlskMKHFTTF---ANDKTLLLIDEFGTGTDPLFGGPIAEAVLEVVNKKKAYGVITTHYSNLKLFANNTPGLENA 472
Cdd:PRK00409 389 STFSGH---MTNIVRIlekADKNSLVLFDELGAGTDPDEGAALAISILEYLRKRGAKIIATTHYKELKALMYNREGVENA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 473 SMVFDNLNLQPMYMLEMGKPGSSYAFEIAQKIGLSQHIIDLAKNKIGVQQRKMDTM---LIDLERD-KKEIIDKKISLDK 548
Cdd:PRK00409 466 SVEFDEETLRPTYRLLIGIPGKSNAFEIAKRLGLPENIIEEAKKLIGEDKEKLNELiasLEELERElEQKAEEAEALLKE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 549 QQRLYKELLEANEKQKlyyaENKRNLIRDAKLEAQTIIKNANKLVENTIAEIKETKADKQTTQTLRaNLSAELR----NN 624
Cdd:PRK00409 546 AEKLKEELEEKKEKLQ----EEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVKAH-ELIEARKrlnkAN 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 625 EIKPETAKPAPAEND-FKEGDWVKMIDTGNIAQVLEVAKNN-VVLAFGDLRSVVKLNRIQKIANNEVPKEVKRFAKMGHT 702
Cdd:PRK00409 621 EKKEKKKKKQKEKQEeLKVGDEVKYLSLGQKGEVLSIPDDKeAIVQAGIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKP 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 703 ESAasfSVEIDLRGQRGDDAIYELEKYFDKALMFGISNFKIIHGKGDGILRKLIRNYLKNYIQVQRLEDEHADRGGDGIT 782
Cdd:PRK00409 701 RTV---SLELDLRGMRYEEALERLDKYLDDALLAGYGEVLIIHGKGTGKLRKGVQEFLKKHPSVKSFRDAPPNEGGFGVT 777
|
....
gi 1579668503 783 YVYL 786
Cdd:PRK00409 778 IVEL 781
|
|
| mutS2 |
TIGR01069 |
MutS2 family protein; Function of MutS2 is unknown. It should not be considered a DNA mismatch ... |
5-786 |
1.13e-147 |
|
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: 451.58 E-value: 1.13e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 5 ENALEKLGFTEIKQLIKNHCISQMGHNMVDKIGFISNYDQILKFLQQTAEFKNIltsQEALPIQSFYDIKILADKARVEG 84
Cdd:TIGR01069 3 EKDLIKLEFDKVKENLLKQTFTPLGKEDAIGLKPPKSVEESKEIIIKLTALGSI---ENNVRFFGFEDIRELLKRAELGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 85 VFLSEDEFYQVHTSLLTVFAVISYFEQRKGVyPTLEALFENLAIEKAILKNIETVIDEKGKIKPNASKQLADLIGAIAKA 164
Cdd:TIGR01069 80 IVKGLEYILVIQNALKTVKHLKVLSEHVLDL-EILFHLRLNLITLPPLENDIIACIDDDGKVKDGASEELDAIRESLKAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 165 ENEARKKIDQIYKNAQSNNWLADGSLTVREGRICIPLLSENKRKIKGFIHDESASGQTVYIEPEEVFSLNNLVRDLEFDK 244
Cdd:TIGR01069 159 EEEVVKRLHKIIRSKELAKYLSDTIVTIRNGRYVLPLKSGFKGKIKGIVHDTSSSGETFYIEPQAIVKLNNKLAQLKNEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 245 RREIIRILTNLTDKLRPYVPILIAYHCFLTKLDFVRAKALFAIVIAAEMPILSKQPIIKLFNAQHPLLFLAHkkagklVV 324
Cdd:TIGR01069 239 ECEIEKILRTLSEKVQEYLLELKFLFKEFDFLDSLQARARYAKAVKGEFPMPSFTGKIILENARHPLLKEPK------VV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 325 PLNILINDGSRIVLISGPNAGGKSVAMKTIGLLQIMVQAGLLIPAASQSEVGVFKQLFADIGDDQSIESDLSTYSAHLSK 404
Cdd:TIGR01069 313 PFTLNLKFEKRVLAITGPNTGGKTVTLKTLGLLALMFQSGIPIPANEHSEIPYFEEIFADIGDEQSIEQNLSTFSGHMKN 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 405 MKHFTTFANDKTLLLIDEFGTGTDPLFGGPIAEAVLEVVNKKKAYGVITTHYSNLKLFANNTPGLENASMVFDNLNLQPM 484
Cdd:TIGR01069 393 ISAILSKTTENSLVLFDELGAGTDPDEGSALAISILEYLLKQNAQVLITTHYKELKALMYNNEGVENASVLFDEETLSPT 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 485 YMLEMGKPGSSYAFEIAQKIGLSQHIIDLAKNKIGVQQRKMDTMLIDLERDKKEIIDKKISLDK----QQRLYKELLEAN 560
Cdd:TIGR01069 473 YKLLKGIPGESYAFEIAQRYGIPHFIIEQAKTFYGEFKEEINVLIEKLSALEKELEQKNEHLEKllkeQEKLKKELEQEM 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 561 EKQKlyyaENKRNLIRDAKLEAQTIIKNANKLVENTIAEIKETKADKQTTQTLRANLSAELRNNEIKPEtaKPAPAENDf 640
Cdd:TIGR01069 553 EELK----ERERNKKLELEKEAQEALKALKKEVESIIRELKEKKIHKAKEIKSIEDLVKLKETKQKIPQ--KPTNFQAD- 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 641 KEGDWVKMIDTGNIAQVLEVAKNNVVLA-FGDLRSVVKLNRIQKIANNEVPKEVKRFAKMGHTESAASFsvEIDLRGQRG 719
Cdd:TIGR01069 626 KIGDKVRIRYFGQKGKIVQILGGNKWNVtVGGMRMKVHGSELEKINKAPPPKKFKVPKTTKPEPKEASL--TLDLRGQRS 703
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1579668503 720 DDAIYELEKYFDKALMFGISNFKIIHGKGDGILRKLIRNYLKNYIQVQRLEDEHADRGGDGITYVYL 786
Cdd:TIGR01069 704 EEALDRLEKFLNDALLAGYEVVLIIHGKGSGKLRKGVQELLKNHPKVKSFRDAPPNDGGSGVTIVYL 770
|
|
| ABC_MutS2 |
cd03280 |
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ... |
303-506 |
6.46e-88 |
|
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: 276.05 E-value: 6.46e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 303 KLFNAQHPLLFLAHKKagklVVPLNILINDGSRIVLISGPNAGGKSVAMKTIGLLQIMVQAGLLIPAASQSEVGVFKQLF 382
Cdd:cd03280 1 RLREARHPLLPLQGEK----VVPLDIQLGENKRVLVITGPNAGGKTVTLKTLGLLTLMAQSGLPIPAAEGSSLPVFENIF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 383 ADIGDDQSIESDLSTYSAHLSKMKHFTTFANDKTLLLIDEFGTGTDPLFGGPIAEAVLEVVNKKKAYGVITTHYSNLKLF 462
Cdd:cd03280 77 ADIGDEQSIEQSLSTFSSHMKNIARILQHADPDSLVLLDELGSGTDPVEGAALAIAILEELLERGALVIATTHYGELKAY 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1579668503 463 ANNTPGLENASMVFDNLNLQPMYMLEMGKPGSSYAFEIAQKIGL 506
Cdd:cd03280 157 AYKREGVENASMEFDPETLKPTYRLLIGVPGRSNALEIARRLGL 200
|
|
| MUTSac |
smart00534 |
ATPase domain of DNA mismatch repair MUTS family; |
336-517 |
5.21e-55 |
|
ATPase domain of DNA mismatch repair MUTS family;
Pssm-ID: 197777 [Multi-domain] Cd Length: 185 Bit Score: 187.38 E-value: 5.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 336 IVLISGPNAGGKSVAMKTIGLLQIMVQAGLLIPAaSQSEVGVFKQLFADIGDDQSIESDLSTYSAHLSKMKHFTTFANDK 415
Cdd:smart00534 1 VVIITGPNMGGKSTYLRQVALIVIMAQIGSFVPA-ESAELPVFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATKN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 416 TLLLIDEFGTGTDPLFGGPIAEAVLE-VVNKKKAYGVITTHYSNLKLFANNTPGLENASMVFD--NLNLQPMYMLEMGKP 492
Cdd:smart00534 80 SLVLLDELGRGTSTYDGLAIAAAILEyLLEKIGARTLFATHYHELTKLADNHPGVRNLHMSALeeTENITFLYKLKPGVA 159
|
170 180
....*....|....*....|....*
gi 1579668503 493 GSSYAFEIAQKIGLSQHIIDLAKNK 517
Cdd:smart00534 160 GKSYGIEVAKLAGLPKEVIERAKRI 184
|
|
| MutS_V |
pfam00488 |
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
337-517 |
4.69e-32 |
|
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: 123.07 E-value: 4.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 337 VLISGPNAGGKSVAMKTIGLLQIMVQAGLLIPAASqSEVGVFKQLFADIGDDQSIESDLSTYSAHLSKMKHFTTFANDKT 416
Cdd:pfam00488 1 LIITGPNMGGKSTYLRQVALIVLMAQIGSFVPAES-AEIGIVDRIFTRIGASDDLAKGRSTFMVEMLETANILHNATDKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 417 LLLIDEFGTGTDPLFGGPIAEAVLE-VVNKKKAYGVITTHYSNLKLFANNTPGLENASMVFDNLNLQP--MYMLEMGKPG 493
Cdd:pfam00488 80 LVILDELGRGTSTYDGLAIAWAVAEhLAEKIKARTLFATHYHELTKLAEKLPAVKNLHMAAVEDDDDIvfLYKVQPGAAD 159
|
170 180
....*....|....*....|....
gi 1579668503 494 SSYAFEIAQKIGLSQHIIDLAKNK 517
Cdd:pfam00488 160 KSYGIHVAELAGLPESVVERAREI 183
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
5-786 |
0e+00 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 889.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 5 ENALEKLGFTEIKQLIKNHCISQMGHNMVDKIGFISNYDQILKFLQQTAEFKNILTSQEALPIQSFYDIKILADKARvEG 84
Cdd:COG1193 3 EKTLEKLEFDKILELLAEYAVSELGKELARKLRPSTDLEEVERLLAETAEARRLLRLEGGLPLGGIPDIRPLLKRAE-EG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 85 VFLSEDEFYQVHTSLLTVFAVISYFEQRKGVYPTLEALFENLAIEKAILKNIETVIDEKGKIKPNASKQLADLIGAIAKA 164
Cdd:COG1193 82 GVLSPEELLDIARTLRAARRLKRFLEELEEEYPALKELAERLPPLPELEKEIDRAIDEDGEVKDSASPELRRIRREIRSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 165 ENEARKKIDQIYKNAQSNNWLADGSLTVREGRICIPLLSENKRKIKGFIHDESASGQTVYIEPEEVFSLNNLVRDLEFDK 244
Cdd:COG1193 162 EQRIREKLESILRSASYQKYLQDAIITIRNGRYVIPVKAEYKGKIPGIVHDQSASGQTLFIEPMAVVELNNELRELEAEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 245 RREIIRILTNLTDKLRPYVPILIAYHCFLTKLDFVRAKALFAIVIAAEMPILSKQPIIKLFNAQHPLLFLahkkagKLVV 324
Cdd:COG1193 242 RREIERILRELSALVREYAEELLENLEILAELDFIFAKARYALELKAVKPELNDEGYIKLKKARHPLLDL------KKVV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 325 PLNILINDGSRIVLISGPNAGGKSVAMKTIGLLQIMVQAGLLIPAASQSEVGVFKQLFADIGDDQSIESDLSTYSAHLSK 404
Cdd:COG1193 316 PIDIELGEDFRTLVITGPNTGGKTVTLKTVGLLTLMAQSGLPIPAAEGSELPVFDNIFADIGDEQSIEQSLSTFSSHMTN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 405 MKHFTTFANDKTLLLIDEFGTGTDPLFGGPIAEAVLEVVNKKKAYGVITTHYSNLKLFANNTPGLENASMVFDNLNLQPM 484
Cdd:COG1193 396 IVEILEKADENSLVLLDELGAGTDPQEGAALAIAILEELLERGARVVATTHYSELKAYAYNTEGVENASVEFDVETLSPT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 485 YMLEMGKPGSSYAFEIAQKIGLSQHIIDLAKNKIGVQQRKMDTMLIDLERDKKEIIDKKISLDKQQRLYKELLEANEKQK 564
Cdd:COG1193 476 YRLLIGVPGRSNAFEIARRLGLPEEIIERARELLGEESIDVEKLIEELERERRELEEEREEAERLREELEKLREELEEKL 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 565 LYYAENKRNLIRDAKLEAQTIIKNANKLVENTIAEIKETKADKQTTQTLRANL---SAELRNNEIKP-ETAKPAPAENDF 640
Cdd:COG1193 556 EELEEEKEEILEKAREEAEEILREARKEAEELIRELREAQAEEEELKEARKKLeelKQELEEKLEKPkKKAKPAKPPEEL 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 641 KEGDWVKMIDTGNIAQVLEV-AKNNVVLAFGDLRSVVKLNRIQKIANNEVPKEVKRFAKMG-HTESAASFSVEIDLRGQR 718
Cdd:COG1193 636 KVGDRVRVLSLGQKGEVLEIpKGGEAEVQVGILKMTVKLSDLEKVEKKKPKKPKKRPAGVSvSVSKASTVSPELDLRGMR 715
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1579668503 719 GDDAIYELEKYFDKALMFGISNFKIIHGKGDGILRKLIRNYLKNYIQVQRLEDEHADRGGDGITYVYL 786
Cdd:COG1193 716 VEEALPELDKYLDDALLAGLPEVRIIHGKGTGALRKGVREYLKRHPYVKSFRLGEPGEGGDGVTVVEL 783
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
5-786 |
3.91e-178 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 530.55 E-value: 3.91e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 5 ENALEKLGFTEIKQLIKNHCISQMGHNMVDKIGFISNYDQILKFLQQTAEFKNILTSQEALPIQSFYDIKILADKARVEG 84
Cdd:PRK00409 3 EKTLRVLEFNKIKEQLKTFAASELGKEKVLQLDPETDFEEVEELLEETDEAAKLLRLKGLPPFEGVKDIDDALKRAEKGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 85 VfLSEDEFYQVHTslltvfaVISYFEQRKGV---------YPTLEALFENLAIEKAILKNIETVIDEKGKIKPNASKQLA 155
Cdd:PRK00409 83 V-LSGDELLEIAK-------TLRYFRQLKRFiedleeeeeLPILEEWVAKIRTLPELEQEIHNCIDEEGEVKDSASEKLR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 156 DLIGAIAKAENEARKKIDQIYKNAQSNNWLADGSLTVREGRICIPLLSENKRKIKGFIHDESASGQTVYIEPEEVFSLNN 235
Cdd:PRK00409 155 GIRRQLRRKKSRIREKLESIIRSKSLQKYLQDTIITIRNDRYVLPVKAEYKHAIKGIVHDQSSSGATLYIEPQSVVELNN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 236 LVRDLEFDKRREIIRILTNLTDKLRPYVPILIAYHCFLTKLDFVRAKALFAIVIAAEMPILSKQPIIKLFNAQHPLLfla 315
Cdd:PRK00409 235 EIRELRNKEEQEIERILKELSAKVAKNLDFLKFLNKIFDELDFIFARARYAKALKATFPLFNDEGKIDLRQARHPLL--- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 316 hkkAGKLVVPLNILINDGSRIVLISGPNAGGKSVAMKTIGLLQIMVQAGLLIPAASQSEVGVFKQLFADIGDDQSIESDL 395
Cdd:PRK00409 312 ---DGEKVVPKDISLGFDKTVLVITGPNTGGKTVTLKTLGLAALMAKSGLPIPANEPSEIPVFKEIFADIGDEQSIEQSL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 396 STYSAHlskMKHFTTF---ANDKTLLLIDEFGTGTDPLFGGPIAEAVLEVVNKKKAYGVITTHYSNLKLFANNTPGLENA 472
Cdd:PRK00409 389 STFSGH---MTNIVRIlekADKNSLVLFDELGAGTDPDEGAALAISILEYLRKRGAKIIATTHYKELKALMYNREGVENA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 473 SMVFDNLNLQPMYMLEMGKPGSSYAFEIAQKIGLSQHIIDLAKNKIGVQQRKMDTM---LIDLERD-KKEIIDKKISLDK 548
Cdd:PRK00409 466 SVEFDEETLRPTYRLLIGIPGKSNAFEIAKRLGLPENIIEEAKKLIGEDKEKLNELiasLEELERElEQKAEEAEALLKE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 549 QQRLYKELLEANEKQKlyyaENKRNLIRDAKLEAQTIIKNANKLVENTIAEIKETKADKQTTQTLRaNLSAELR----NN 624
Cdd:PRK00409 546 AEKLKEELEEKKEKLQ----EEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVKAH-ELIEARKrlnkAN 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 625 EIKPETAKPAPAEND-FKEGDWVKMIDTGNIAQVLEVAKNN-VVLAFGDLRSVVKLNRIQKIANNEVPKEVKRFAKMGHT 702
Cdd:PRK00409 621 EKKEKKKKKQKEKQEeLKVGDEVKYLSLGQKGEVLSIPDDKeAIVQAGIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKP 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 703 ESAasfSVEIDLRGQRGDDAIYELEKYFDKALMFGISNFKIIHGKGDGILRKLIRNYLKNYIQVQRLEDEHADRGGDGIT 782
Cdd:PRK00409 701 RTV---SLELDLRGMRYEEALERLDKYLDDALLAGYGEVLIIHGKGTGKLRKGVQEFLKKHPSVKSFRDAPPNEGGFGVT 777
|
....
gi 1579668503 783 YVYL 786
Cdd:PRK00409 778 IVEL 781
|
|
| mutS2 |
TIGR01069 |
MutS2 family protein; Function of MutS2 is unknown. It should not be considered a DNA mismatch ... |
5-786 |
1.13e-147 |
|
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: 451.58 E-value: 1.13e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 5 ENALEKLGFTEIKQLIKNHCISQMGHNMVDKIGFISNYDQILKFLQQTAEFKNIltsQEALPIQSFYDIKILADKARVEG 84
Cdd:TIGR01069 3 EKDLIKLEFDKVKENLLKQTFTPLGKEDAIGLKPPKSVEESKEIIIKLTALGSI---ENNVRFFGFEDIRELLKRAELGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 85 VFLSEDEFYQVHTSLLTVFAVISYFEQRKGVyPTLEALFENLAIEKAILKNIETVIDEKGKIKPNASKQLADLIGAIAKA 164
Cdd:TIGR01069 80 IVKGLEYILVIQNALKTVKHLKVLSEHVLDL-EILFHLRLNLITLPPLENDIIACIDDDGKVKDGASEELDAIRESLKAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 165 ENEARKKIDQIYKNAQSNNWLADGSLTVREGRICIPLLSENKRKIKGFIHDESASGQTVYIEPEEVFSLNNLVRDLEFDK 244
Cdd:TIGR01069 159 EEEVVKRLHKIIRSKELAKYLSDTIVTIRNGRYVLPLKSGFKGKIKGIVHDTSSSGETFYIEPQAIVKLNNKLAQLKNEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 245 RREIIRILTNLTDKLRPYVPILIAYHCFLTKLDFVRAKALFAIVIAAEMPILSKQPIIKLFNAQHPLLFLAHkkagklVV 324
Cdd:TIGR01069 239 ECEIEKILRTLSEKVQEYLLELKFLFKEFDFLDSLQARARYAKAVKGEFPMPSFTGKIILENARHPLLKEPK------VV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 325 PLNILINDGSRIVLISGPNAGGKSVAMKTIGLLQIMVQAGLLIPAASQSEVGVFKQLFADIGDDQSIESDLSTYSAHLSK 404
Cdd:TIGR01069 313 PFTLNLKFEKRVLAITGPNTGGKTVTLKTLGLLALMFQSGIPIPANEHSEIPYFEEIFADIGDEQSIEQNLSTFSGHMKN 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 405 MKHFTTFANDKTLLLIDEFGTGTDPLFGGPIAEAVLEVVNKKKAYGVITTHYSNLKLFANNTPGLENASMVFDNLNLQPM 484
Cdd:TIGR01069 393 ISAILSKTTENSLVLFDELGAGTDPDEGSALAISILEYLLKQNAQVLITTHYKELKALMYNNEGVENASVLFDEETLSPT 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 485 YMLEMGKPGSSYAFEIAQKIGLSQHIIDLAKNKIGVQQRKMDTMLIDLERDKKEIIDKKISLDK----QQRLYKELLEAN 560
Cdd:TIGR01069 473 YKLLKGIPGESYAFEIAQRYGIPHFIIEQAKTFYGEFKEEINVLIEKLSALEKELEQKNEHLEKllkeQEKLKKELEQEM 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 561 EKQKlyyaENKRNLIRDAKLEAQTIIKNANKLVENTIAEIKETKADKQTTQTLRANLSAELRNNEIKPEtaKPAPAENDf 640
Cdd:TIGR01069 553 EELK----ERERNKKLELEKEAQEALKALKKEVESIIRELKEKKIHKAKEIKSIEDLVKLKETKQKIPQ--KPTNFQAD- 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 641 KEGDWVKMIDTGNIAQVLEVAKNNVVLA-FGDLRSVVKLNRIQKIANNEVPKEVKRFAKMGHTESAASFsvEIDLRGQRG 719
Cdd:TIGR01069 626 KIGDKVRIRYFGQKGKIVQILGGNKWNVtVGGMRMKVHGSELEKINKAPPPKKFKVPKTTKPEPKEASL--TLDLRGQRS 703
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1579668503 720 DDAIYELEKYFDKALMFGISNFKIIHGKGDGILRKLIRNYLKNYIQVQRLEDEHADRGGDGITYVYL 786
Cdd:TIGR01069 704 EEALDRLEKFLNDALLAGYEVVLIIHGKGSGKLRKGVQELLKNHPKVKSFRDAPPNDGGSGVTIVYL 770
|
|
| ABC_MutS2 |
cd03280 |
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ... |
303-506 |
6.46e-88 |
|
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: 276.05 E-value: 6.46e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 303 KLFNAQHPLLFLAHKKagklVVPLNILINDGSRIVLISGPNAGGKSVAMKTIGLLQIMVQAGLLIPAASQSEVGVFKQLF 382
Cdd:cd03280 1 RLREARHPLLPLQGEK----VVPLDIQLGENKRVLVITGPNAGGKTVTLKTLGLLTLMAQSGLPIPAAEGSSLPVFENIF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 383 ADIGDDQSIESDLSTYSAHLSKMKHFTTFANDKTLLLIDEFGTGTDPLFGGPIAEAVLEVVNKKKAYGVITTHYSNLKLF 462
Cdd:cd03280 77 ADIGDEQSIEQSLSTFSSHMKNIARILQHADPDSLVLLDELGSGTDPVEGAALAIAILEELLERGALVIATTHYGELKAY 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1579668503 463 ANNTPGLENASMVFDNLNLQPMYMLEMGKPGSSYAFEIAQKIGL 506
Cdd:cd03280 157 AYKREGVENASMEFDPETLKPTYRLLIGVPGRSNALEIARRLGL 200
|
|
| MUTSac |
smart00534 |
ATPase domain of DNA mismatch repair MUTS family; |
336-517 |
5.21e-55 |
|
ATPase domain of DNA mismatch repair MUTS family;
Pssm-ID: 197777 [Multi-domain] Cd Length: 185 Bit Score: 187.38 E-value: 5.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 336 IVLISGPNAGGKSVAMKTIGLLQIMVQAGLLIPAaSQSEVGVFKQLFADIGDDQSIESDLSTYSAHLSKMKHFTTFANDK 415
Cdd:smart00534 1 VVIITGPNMGGKSTYLRQVALIVIMAQIGSFVPA-ESAELPVFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATKN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 416 TLLLIDEFGTGTDPLFGGPIAEAVLE-VVNKKKAYGVITTHYSNLKLFANNTPGLENASMVFD--NLNLQPMYMLEMGKP 492
Cdd:smart00534 80 SLVLLDELGRGTSTYDGLAIAAAILEyLLEKIGARTLFATHYHELTKLADNHPGVRNLHMSALeeTENITFLYKLKPGVA 159
|
170 180
....*....|....*....|....*
gi 1579668503 493 GSSYAFEIAQKIGLSQHIIDLAKNK 517
Cdd:smart00534 160 GKSYGIEVAKLAGLPKEVIERAKRI 184
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
307-506 |
5.43e-46 |
|
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: 163.19 E-value: 5.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 307 AQHPLLFLAHKkaGKLVVPLNILINDGsRIVLISGPNAGGKSVAMKTIGLLQIMVQAGLLIPAASqSEVGVFKQLFADIG 386
Cdd:cd03243 5 GRHPVLLALTK--GETFVPNDINLGSG-RLLLITGPNMGGKSTYLRSIGLAVLLAQIGCFVPAES-ASIPLVDRIFTRIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 387 DDQSIESDLSTYSAHLSKMKHFTTFANDKTLLLIDEFGTGTDPLFGGPIAEAVLEVVNKKKAYGVITTHYSNLKLFANNT 466
Cdd:cd03243 81 AEDSISDGRSTFMAELLELKEILSLATPRSLVLIDELGRGTSTAEGLAIAYAVLEHLLEKGCRTLFATHFHELADLPEQV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1579668503 467 PGLENASMVFD--NLNLQPMYMLEMGKPGSSYAFEIAQKIGL 506
Cdd:cd03243 161 PGVKNLHMEELitTGGLTFTYKLIDGICDPSYALQIAELAGL 202
|
|
| MutS_V |
pfam00488 |
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
337-517 |
4.69e-32 |
|
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: 123.07 E-value: 4.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 337 VLISGPNAGGKSVAMKTIGLLQIMVQAGLLIPAASqSEVGVFKQLFADIGDDQSIESDLSTYSAHLSKMKHFTTFANDKT 416
Cdd:pfam00488 1 LIITGPNMGGKSTYLRQVALIVLMAQIGSFVPAES-AEIGIVDRIFTRIGASDDLAKGRSTFMVEMLETANILHNATDKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 417 LLLIDEFGTGTDPLFGGPIAEAVLE-VVNKKKAYGVITTHYSNLKLFANNTPGLENASMVFDNLNLQP--MYMLEMGKPG 493
Cdd:pfam00488 80 LVILDELGRGTSTYDGLAIAWAVAEhLAEKIKARTLFATHYHELTKLAEKLPAVKNLHMAAVEDDDDIvfLYKVQPGAAD 159
|
170 180
....*....|....*....|....
gi 1579668503 494 SSYAFEIAQKIGLSQHIIDLAKNK 517
Cdd:pfam00488 160 KSYGIHVAELAGLPESVVERAREI 183
|
|
| mutS1 |
TIGR01070 |
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair] |
43-518 |
6.63e-31 |
|
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273427 [Multi-domain] Cd Length: 840 Bit Score: 130.27 E-value: 6.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 43 DQILKFLQQTAEFKNIltsQEALpiQSFYDIKILAdkARVEGVFLSEDEFYQVHTSLLTVFAVISYFEQRKGvyPTLEAL 122
Cdd:TIGR01070 308 DTVEVLLRHFFLREGL---RPLL--KEVGDLERLA--ARVALGNARPRDLARLRTSLEQLPELRALLEELEG--PTLQAL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 123 FENLA--------IEKAILKNIETVIDEKGKIKPNASKQLADLIGAIAKAenearkkidqiyknaqsNNWLADgsLTVRE 194
Cdd:TIGR01070 379 AAQIDdfsellelLEAALIENPPLVVRDGGLIREGYDEELDELRAASREG-----------------TDYLAR--LEARE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 195 -GRICIPLLSENKRKIKGF-IH-----DESASG-----QTV-----YIEPE------EVFSLNNLVRDLEFDkrreiirI 251
Cdd:TIGR01070 440 rERTGIPTLKVGYNAVFGYyIEvtrgqLHLVPAhyrrrQTLknaerYITPElkekedKVLEAEGKILALEKE-------L 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 252 LTNLTDKLRPYVPILIAYHCFLTKLDFVRAKALFAIVIAAEMPILSKQPIIKLFNAQHPLLflaHKKAGKLVVPLNILIN 331
Cdd:TIGR01070 513 FEELRELLKKYLEALQEAARALAELDVLANLAEVAETLHYTRPRFGDDPQLRIREGRHPVV---EQVLRTPFVPNDLEMA 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 332 DGSRIVLISGPNAGGKSVAMKTIGLLQIMVQAGLLIPAASqSEVGVFKQLFADIGDDQSIESDLSTYSAHLSKMKHFTTF 411
Cdd:TIGR01070 590 HNRRMLLITGPNMGGKSTYMRQTALIALLAQIGSFVPAES-AELPLFDRIFTRIGASDDLASGRSTFMVEMTEAANILHN 668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 412 ANDKTLLLIDEFGTGTDPLFGGPIAEAVLEVVNKK-KAYGVITTHYSNLKLFANNTPGL---------ENASMVFdnlnl 481
Cdd:TIGR01070 669 ATENSLVLFDEIGRGTSTYDGLALAWAIAEYLHEHiRAKTLFATHYFELTALEESLPGLknvhvaaleHNGTIVF----- 743
|
490 500 510
....*....|....*....|....*....|....*..
gi 1579668503 482 qpMYMLEMGKPGSSYAFEIAQKIGLSQHIIDLAKNKI 518
Cdd:TIGR01070 744 --LHQVLPGPASKSYGLAVAALAGLPKEVIARARQIL 778
|
|
| ABC_MSH6_euk |
cd03286 |
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA ... |
309-514 |
3.33e-29 |
|
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: 115.99 E-value: 3.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 309 HPLLFLAhkkAGKLVVPLNILINDGS-RIVLISGPNAGGKSVAMKTIGLLQIMVQAGLLIPAASqSEVGVFKQLFADIGD 387
Cdd:cd03286 7 HPCLNAS---TASSFVPNDVDLGATSpRILVLTGPNMGGKSTLLRTVCLAVIMAQMGMDVPAKS-MRLSLVDRIFTRIGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 388 DQSIESDLSTYSAHLSKMKHFTTFANDKTLLLIDEFGTGTDPLFGGPIAEAVLE-VVNKKKAYGVITTHYSNLKLFANNT 466
Cdd:cd03286 83 RDDIMKGESTFMVELSETANILRHATPDSLVILDELGRGTSTHDGYAIAHAVLEyLVKKVKCLTLFSTHYHSLCDEFHEH 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1579668503 467 PGLENASM--VFDNLNLQPM------YMLEMGKPGSSYAFEIAQKIGLSQHIIDLA 514
Cdd:cd03286 163 GGVRLGHMacAVKNESDPTIrditflYKLVAGICPKSYGLYVALMAGIPDGVVERA 218
|
|
| ABC_MSH4_euk |
cd03282 |
ATP-binding cassette domain of eukaryotic MutS4 homolog; The MutS protein initiates DNA ... |
306-474 |
1.82e-27 |
|
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: 110.56 E-value: 1.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 306 NAQHPLLflahKKAGKLVVPLNILINDG-SRIVLISGPNAGGKSVAMKTIGLLQIMVQAGLLIPAaSQSEVGVFKQLFAD 384
Cdd:cd03282 4 DSRHPIL----DRDKKNFIPNDIYLTRGsSRFHIITGPNMSGKSTYLKQIALLAIMAQIGCFVPA-EYATLPIFNRLLSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 385 IGDDQSIESDLSTYSAHLSKMKHFTTFANDKTLLLIDEFGTGTDPLFGGPIAEAVLEVVNKKKAYGVITTHYSNLKLFAN 464
Cdd:cd03282 79 LSNDDSMERNLSTFASEMSETAYILDYADGDSLVLIDELGRGTSSADGFAISLAILECLIKKESTVFFATHFRDIAAILG 158
|
170
....*....|
gi 1579668503 465 NTPGLENASM 474
Cdd:cd03282 159 NKSCVVHLHM 168
|
|
| ABC_MutS1 |
cd03284 |
ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair ... |
324-515 |
3.01e-26 |
|
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: 107.35 E-value: 3.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 324 VPLNILINDGSRIVLISGPNAGGKSVAMKTIGLLQIMVQAGLLIPAASqSEVGVFKQLFADIG--DDQSieSDLSTYSAH 401
Cdd:cd03284 20 VPNDTELDPERQILLITGPNMAGKSTYLRQVALIALLAQIGSFVPASK-AEIGVVDRIFTRIGasDDLA--GGRSTFMVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 402 LSKMKHFTTFANDKTLLLIDEFGTGTDPLFGGPIAEAVLE-VVNKKKAYGVITTHYSNLKLFANNTPGLENASM------ 474
Cdd:cd03284 97 MVETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAIVEyLHEKIGAKTLFATHYHELTELEGKLPRVKNFHVavkekg 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1579668503 475 ---VFdnlnlqpMYMLEMGKPGSSYAFEIAQKIGLSQHIIDLAK 515
Cdd:cd03284 177 ggvVF-------LHKIVEGAADKSYGIEVARLAGLPEEVIERAR 213
|
|
| ABC_MSH3_euk |
cd03287 |
ATP-binding cassette domain of eukaryotic MutS3 homolog; The MutS protein initiates DNA ... |
302-514 |
4.74e-24 |
|
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: 101.02 E-value: 4.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 302 IKLFNAQHPLLFLAhkkAGKLVVPLNILIN-DGSRIVLISGPNAGGKSVAMKTIGLLQIMVQAGLLIPAASqSEVGVFKQ 380
Cdd:cd03287 1 ILIKEGRHPMIESL---LDKSFVPNDIHLSaEGGYCQIITGPNMGGKSSYIRQVALITIMAQIGSFVPASS-ATLSIFDS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 381 LFADIGDDQSIESDLSTYSAHLSKMKHFTTFANDKTLLLIDEFGTGTDPLFGGPIAEAVLEVVNK-KKAYGVITTHYSNL 459
Cdd:cd03287 77 VLTRMGASDSIQHGMSTFMVELSETSHILSNCTSRSLVILDELGRGTSTHDGIAIAYATLHYLLEeKKCLVLFVTHYPSL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1579668503 460 KLFANNTPG-LENASMVFDNL----------NLQPMYMLEMGKPGSSYAFEIAQKIGLSQHIIDLA 514
Cdd:cd03287 157 GEILRRFEGsIRNYHMSYLESqkdfetsdsqSITFLYKLVRGLASRSFGLNVARLAGLPKSIISRA 222
|
|
| Smr |
pfam01713 |
Smr domain; This family includes the Smr (Small MutS Related) proteins, and the C-terminal ... |
713-786 |
5.56e-24 |
|
Smr domain; This family includes the Smr (Small MutS Related) proteins, and the C-terminal region of the MutS2 protein. It has been suggested that this domain interacts with the MutS1 protein in the case of Smr proteins and with the N-terminal MutS related region of MutS2. This domain exhibits nicking endonuclease activity that might have a role in mismatch repair or genetic recombination. It shows no significant double strand cleavage or exonuclease activity. The full-length Swiss:Q86UW6 also has the polynucleotide kinase activity.
Pssm-ID: 460303 [Multi-domain] Cd Length: 76 Bit Score: 96.00 E-value: 5.56e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1579668503 713 DLRGQRGDDAIYELEKYFDKALMFGISNFKIIHGKGD-GILRKLIRNYLKNYIQVQRLEDEHADRGGDGITYVYL 786
Cdd:pfam01713 1 DLHGMTVEEAREALDKFLDDALLAGLRCVLIIHGKGThGVLRKAVREWLKQHPLVLAFRSAPPGEGGDGATYVLL 75
|
|
| ABC_MSH2_euk |
cd03285 |
ATP-binding cassette domain of eukaryotic MutS2 homolog; The MutS protein initiates DNA ... |
304-517 |
6.03e-24 |
|
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: 100.91 E-value: 6.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 304 LFNAQHPLLFLAHKKAgklVVPLNI-LINDGSRIVLISGPNAGGKSVAMKTIGLLQIMVQAGLLIPaASQSEVGVFKQLF 382
Cdd:cd03285 2 LKEARHPCVEAQDDVA---FIPNDVtLTRGKSRFLIITGPNMGGKSTYIRQIGVIVLMAQIGCFVP-CDSADIPIVDCIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 383 ADIGDDQSIESDLSTYSAHLSKMKHFTTFANDKTLLLIDEFGTGTDPLFGGPIAEAVLE-VVNKKKAYGVITTHYSNLKL 461
Cdd:cd03285 78 ARVGASDSQLKGVSTFMAEMLETAAILKSATENSLIIIDELGRGTSTYDGFGLAWAIAEyIATQIKCFCLFATHFHELTA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 462 FANNTPGLEN----ASMVFDNLNLQPMYMLEMGKPGSSYAFEIAQKIGLSQHIIDLAKNK 517
Cdd:cd03285 158 LADEVPNVKNlhvtALTDDASRTLTMLYKVEKGACDQSFGIHVAELANFPKEVIEMAKQK 217
|
|
| ABC_MSH5_euk |
cd03281 |
ATP-binding cassette domain of eukaryotic MutS5 homolog; The MutS protein initiates DNA ... |
306-506 |
7.66e-21 |
|
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: 91.59 E-value: 7.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 306 NAQHPLLFLAHKKAgklvVPLNILIN-DGSRIVLISGPNAGGKSVAMKTIGLLQIMVQAGLLIPAASqSEVGVFKQLFAD 384
Cdd:cd03281 4 GGRHPLLELFVDSF----VPNDTEIGgGGPSIMVITGPNSSGKSVYLKQVALIVFLAHIGSFVPADS-ATIGLVDKIFTR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 385 IGDDQSIESDLSTYSAHLSKMKHFTTFANDKTLLLIDEFGTGTDPLFGGPIAEAVLEVVNKKKA---YGVITTHYSNL-- 459
Cdd:cd03281 79 MSSRESVSSGQSAFMIDLYQVSKALRLATRRSLVLIDEFGKGTDTEDGAGLLIATIEHLLKRGPecpRVIVSTHFHELfn 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1579668503 460 KLFANNTPG--------LENASMVFDNLNLQPMYMLEMGKPGSSYAFEIAQKIGL 506
Cdd:cd03281 159 RSLLPERLKikfltmevLLNPTSTSPNEDITYLYRLVPGLADTSFAIHCAKLAGI 213
|
|
| MUTSd |
smart00533 |
DNA-binding domain of DNA mismatch repair MUTS family; |
22-312 |
2.11e-18 |
|
DNA-binding domain of DNA mismatch repair MUTS family;
Pssm-ID: 214710 [Multi-domain] Cd Length: 308 Bit Score: 86.58 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 22 NHCISQMGHNMVDKigFIS----NYDQILKFLQQTAEFKNILTSQEAL--PIQSFYDIKILAdkARVEGVFLSEDEFYQV 95
Cdd:smart00533 9 NHTKTPMGKRLLRR--WLLqpllDLKEINERLDAVEELVENPELRQKLrqLLKRIPDLERLL--SRIERGRASPRDLLRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 96 HTSLLTVFAVISYFEQRKGVYPTL-------EALFENLAIEKAILKNIETVIDEKGKIKPNASKQLADLIGAIAKAENEA 168
Cdd:smart00533 85 YDSLEGLKEIRQLLESLDGPLLGLllkvilePLLELLELLLELLNDDDPLEVNDGGLIKDGFDPELDELREKLEELEEEL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 169 RKKIDQIYKNAQSNNwLADGSLTVREgrICIPLLSENKRKIKGFIHDESASGQTVYIEPEEVFSLNNLVRDLEFDKRREI 248
Cdd:smart00533 165 EELLKKEREELGIDS-LKLGYNKVHG--YYIEVTKSEAKKVPKDFIRRSSLKNTERFTTPELKELENELLEAKEEIERLE 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1579668503 249 IRILTNLTDKLRPYVPILIAYHCFLTKLDFVRAKALFAIVIAAEMPILSKQPIIKLFNAQHPLL 312
Cdd:smart00533 242 KEILRELLEKVLEYLEELRALAEALAELDVLLSLATLAAEGNYVRPEFVDSGELEIKNGRHPVL 305
|
|
| ABC_MutS-like |
cd03283 |
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ... |
334-506 |
1.43e-13 |
|
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: 70.02 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 334 SRIVLISGPNAGGKSVAMKTIGLLQIMVQAGLLIPAASQseVGVFKQLFADIGDDQSIESDLSTYSAHLSKMKHFTTFAN 413
Cdd:cd03283 25 KNGILITGSNMSGKSTFLRTIGVNVILAQAGAPVCASSF--ELPPVKIFTSIRVSDDLRDGISYFYAELRRLKEIVEKAK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 414 DKT--LLLIDEFGTGTDPLFGGPIAEAVLEVVNKKKAYGVITTHYSNLKLFANNTPGLENA--SMVFDNLNLQPMYMLEM 489
Cdd:cd03283 103 KGEpvLFLLDEIFKGTNSRERQAASAAVLKFLKNKNTIGIISTHDLELADLLDLDSAVRNYhfREDIDDNKLIFDYKLKP 182
|
170
....*....|....*..
gi 1579668503 490 GKPGSSYAFEIAQKIGL 506
Cdd:cd03283 183 GVSPTRNALRLMKKIGI 199
|
|
| PRK05399 |
PRK05399 |
DNA mismatch repair protein MutS; Provisional |
224-474 |
1.16e-12 |
|
DNA mismatch repair protein MutS; Provisional
Pssm-ID: 235444 [Multi-domain] Cd Length: 854 Bit Score: 71.66 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 224 YIEPE------EVFSLNNLVRDLEFDkrreiirILTNLTDKLRPYVPIL------IAYhcfltkLDFVRAkalFAIViAA 291
Cdd:PRK05399 500 YITPElkeledKILSAEEKALALEYE-------LFEELREEVAEHIERLqklakaLAE------LDVLAS---LAEV-AE 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 292 E----MPILSKQPIIKLFNAQHPLL--FLAHKKagklVVPLNILINDGSRIVLISGPNAGGKSVAMKTIGLLQIMVQAGL 365
Cdd:PRK05399 563 EnnyvRPEFTDDPGIDIEEGRHPVVeqVLGGEP----FVPNDCDLDEERRLLLITGPNMAGKSTYMRQVALIVLLAQIGS 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 366 LIPAASqSEVGVFKQLFADIG--DD----QSiesdlstysahlskmkhftTF-------------ANDKTLLLIDEFGTG 426
Cdd:PRK05399 639 FVPAES-ARIGIVDRIFTRIGasDDlasgRS-------------------TFmvemtetanilnnATERSLVLLDEIGRG 698
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1579668503 427 T---DplfGGPIAEAVLE-VVNKKKAYGVITTHYSNLKLFANNTPGLENASM 474
Cdd:PRK05399 699 TstyD---GLSIAWAVAEyLHDKIGAKTLFATHYHELTELEEKLPGVKNVHV 747
|
|
| MutS |
COG0249 |
DNA mismatch repair ATPase MutS [Replication, recombination and repair]; |
324-515 |
3.68e-12 |
|
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
Pssm-ID: 440019 [Multi-domain] Cd Length: 861 Bit Score: 70.09 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 324 VPLNILINDGSRIVLISGPNAGGKSVAMKTIGLLQIMVQAGLLIPAASqSEVGVFKQLFADIG--DD----QSiesdlst 397
Cdd:COG0249 603 VPNDCDLDPDRRILLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAES-ARIGIVDRIFTRVGasDDlargQS------- 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 398 ysahlskmkhftTF-------------ANDKTLLLIDEFGTGT---DplfGGPIAEAVLE-VVNKKKAYGVITTHYSNLK 460
Cdd:COG0249 675 ------------TFmvemtetanilnnATERSLVLLDEIGRGTstyD---GLSIAWAVAEyLHDKIRARTLFATHYHELT 739
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1579668503 461 LFANNTPGLENASM---------VFdnlnlqpMYMLEMGKPGSSYAFEIAQKIGLSQHIIDLAK 515
Cdd:COG0249 740 ELAEKLPGVKNYHVavkewggdiVF-------LHKVVPGPADRSYGIHVAKLAGLPASVIERAR 796
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
324-464 |
2.77e-11 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 62.38 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 324 VPLNILINDGsRIVLISGPNAGGKSVAMKTIGLLQIM----------VQAGLLIPAASQSEVGVFKQLfadigddQSIES 393
Cdd:cd03227 12 VPNDVTFGEG-SLTIITGPNGSGKSTILDAIGLALGGaqsatrrrsgVKAGCIVAAVSAELIFTRLQL-------SGGEK 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1579668503 394 DLSTYSAHLSKMKHfttfaNDKTLLLIDEFGTGTDPLFGGPIAEAVLEvVNKKKAYGVITTHYSNLKLFAN 464
Cdd:cd03227 84 ELSALALILALASL-----KPRPLYILDEIDRGLDPRDGQALAEAILE-HLVKGAQVIVITHLPELAELAD 148
|
|
| SMR |
smart00463 |
Small MutS-related domain; |
711-786 |
8.06e-10 |
|
Small MutS-related domain;
Pssm-ID: 214676 [Multi-domain] Cd Length: 80 Bit Score: 55.77 E-value: 8.06e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1579668503 711 EIDLRGQRGDDAIYELEKYFDKALMFGI-SNFKIIHGKGDGILR--KLIRNYLKNYIQVQRLEDEHadRGGDGITYVYL 786
Cdd:smart00463 3 SLDLHGLTVEEALTALDKFLNNARLKGLeQKLVIITGKGKHSLGgkSGVKPALKEHLRVESFRFAE--EGNSGVLVVKL 79
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
318-465 |
1.14e-06 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 49.17 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 318 KAGKLVVPLNILINDGsRIVLISGPNAGGKSVAMKTIgllqimvqAGLLIPaaSQSEVGVFKQlfaDIGDDQSIE-SDLS 396
Cdd:cd00267 10 GGRTALDNVSLTLKAG-EIVALVGPNGSGKSTLLRAI--------AGLLKP--TSGEILIDGK---DIAKLPLEElRRRI 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1579668503 397 TYSAHLSK-MKHFTTFA----NDKTLLLIDEFGTGTDPLFGGPIAEAVLEVVNKKKAYgVITTHYSNLKLFANN 465
Cdd:cd00267 76 GYVPQLSGgQRQRVALArallLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTV-IIVTHDPELAELAAD 148
|
|
| SmrA |
COG2840 |
DNA-nicking endonuclease, Smr domain [Replication, recombination and repair]; |
690-786 |
5.13e-06 |
|
DNA-nicking endonuclease, Smr domain [Replication, recombination and repair];
Pssm-ID: 442088 [Multi-domain] Cd Length: 177 Bit Score: 47.60 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579668503 690 PKEVKRFaKMGHTESAAsfsvEIDLRGQRGDDAIYELEKYFDKALMFGISNFKIIHGKG------DGILRKLIRNYLKNY 763
Cdd:COG2840 75 PGVLKKL-RRGKYPPEA----RLDLHGLTVEEAREALAAFLAEAQRRGLRCVLIIHGKGlgspggRPVLKSQVPRWLRQH 149
|
90 100
....*....|....*....|...
gi 1579668503 764 IQVQRLEDEHADRGGDGITYVYL 786
Cdd:COG2840 150 PEVLAFHSAPPRHGGSGALYVLL 172
|
|
| MSSS |
pfam20297 |
MutS2 and Smr-associated SH3 domain; This is a SH3-like domain associated with the MutS-like ... |
642-681 |
8.24e-04 |
|
MutS2 and Smr-associated SH3 domain; This is a SH3-like domain associated with the MutS-like ABC ATPase and Smr domains. It has been predicted to play a role in lesion recognition or alternatively in mediating contacts with RNA primers or misincorporated ribonucleotides during DNA repair or interacting with the ribosome at the intersection between DNA repair and ribosome rescue.
Pssm-ID: 466447 [Multi-domain] Cd Length: 42 Bit Score: 37.78 E-value: 8.24e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1579668503 642 EGDWVKMIDTGNIAQVLEVA--KNNVVLAFGDLRSVVKLNRI 681
Cdd:pfam20297 1 VGDEVRVKSLGQKGEVLEVPgkKGEVEVQVGIMKMTVKLSDL 42
|
|
| |
