|
Name |
Accession |
Description |
Interval |
E-value |
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1-770 |
0e+00 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 666.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 1 MEQNFRNELnqaiDFSSVLTQVSAFSSFSCTKEKILNALPVFDKLEIQEQLNYAKEAIQFEQAGGLLSLSGANDISLPVS 80
Cdd:COG1193 1 MNEKTLEKL----EFDKILELLAEYAVSELGKELARKLRPSTDLEEVERLLAETAEARRLLRLEGGLPLGGIPDIRPLLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 81 KASKQMTLTSKELISIYHFLMAVKQAKQSLD--ESDYPKLTNLAQSMDGCTRLMDSIISKIDLTGSVKEDATPALKSMHK 158
Cdd:COG1193 77 RAEEGGVLSPEELLDIARTLRAARRLKRFLEelEEEYPALKELAERLPPLPELEKEIDRAIDEDGEVKDSASPELRRIRR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 159 ALVDTRLALQSKSRQFLKKNSLK--LMENMTTTVSGRVVVLVRAQDKNAFGGMIHGQSSSGLAYYVEPSSFVADNNEISS 236
Cdd:COG1193 157 EIRSLEQRIREKLESILRSASYQkyLQDAIITIRNGRYVIPVKAEYKGKIPGIVHDQSASGQTLFIEPMAVVELNNELRE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 237 LMIRIEEEKKRICKELSMQVKKNALSLTSALETLTVIDVAFTKAKWAVRYDGCIPSLqSRDHSMYLEHAKHPLIDEKKVV 316
Cdd:COG1193 237 LEAEERREIERILRELSALVREYAEELLENLEILAELDFIFAKARYALELKAVKPEL-NDEGYIKLKKARHPLLDLKKVV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 317 CNTYELNDKQACLMISGPNMGGKTVTLKTIGLFVALAHAAFPVLCHK-AILPFYQSMYFDIGDHQSIENNLSTFSSHISR 395
Cdd:COG1193 316 PIDIELGEDFRTLVITGPNTGGKTVTLKTVGLLTLMAQSGLPIPAAEgSELPVFDNIFADIGDEQSIEQSLSTFSSHMTN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 396 LSHICQKSDENSFILLDEIGNGTDPLEGASLAVAILEYLISKRSTIITSTHYSQVKTYGKANDSVLVSSVEFNPETLKPT 475
Cdd:COG1193 396 IVEILEKADENSLVLLDELGAGTDPQEGAALAIAILEELLERGARVVATTHYSELKAYAYNTEGVENASVEFDVETLSPT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 476 YKYIPGVSGASYAFHIAREYNLEESILERA-DFLKNENEKqtekelekleklQNDVL----KQKERFNQLIEDAHRVQKE 550
Cdd:COG1193 476 YRLLIGVPGRSNAFEIARRLGLPEEIIERArELLGEESID------------VEKLIeeleRERRELEEEREEAERLREE 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 551 ACEKEKEIEKRKAQLD-------ASYQEQLNEMLEKKKAEAKEILTVLRKEKTgKQHKQIEKMHELD-LLNEHVEEIEDD 622
Cdd:COG1193 544 LEKLREELEEKLEELEeekeeilEKAREEAEEILREARKEAEELIRELREAQA-EEEELKEARKKLEeLKQELEEKLEKP 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 623 K---------KEFKVGDYVKITGLNSHGEIVDIRR-NEATVLTNGMKMKVKISKLEPMHKPQIKKATYKAHVESVSSR-- 690
Cdd:COG1193 623 KkkakpakppEELKVGDRVRVLSLGQKGEVLEIPKgGEAEVQVGILKMTVKLSDLEKVEKKKPKKPKKRPAGVSVSVSka 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 691 --FPLELNLIGMRVEEGVAALDKYLDQAVVKHIKQVRIIHGMGTGALRTAVWKDLKKQPNVSKFNSAGPSEGGLGATIVI 768
Cdd:COG1193 703 stVSPELDLRGMRVEEALPELDKYLDDALLAGLPEVRIIHGKGTGALRKGVREYLKRHPYVKSFRLGEPGEGGDGVTVVE 782
|
..
gi 2125643774 769 LK 770
Cdd:COG1193 783 LK 784
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
14-770 |
0e+00 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 552.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 14 DFSSVLTQVSAFSSFSCTKEKILNALPVFDKLEIQEQLNYAKEAIQFEQAGGLLSLSGANDISLPVSKASKQMTLTSKEL 93
Cdd:PRK00409 10 EFNKIKEQLKTFAASELGKEKVLQLDPETDFEEVEELLEETDEAAKLLRLKGLPPFEGVKDIDDALKRAEKGGVLSGDEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 94 ISIYHFLMAVKQAK----QSLDESDYPKLTNLAQSMDGCTRLMDSIISKIDLTGSVKEDATPALKSMHKALVDTRLALQS 169
Cdd:PRK00409 90 LEIAKTLRYFRQLKrfieDLEEEEELPILEEWVAKIRTLPELEQEIHNCIDEEGEVKDSASEKLRGIRRQLRRKKSRIRE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 170 KSRQFLKKNSL--KLMENMTTTVSGRVVVLVRAQDKNAFGGMIHGQSSSGLAYYVEPSSFVADNNEISSLMIRIEEEKKR 247
Cdd:PRK00409 170 KLESIIRSKSLqkYLQDTIITIRNDRYVLPVKAEYKHAIKGIVHDQSSSGATLYIEPQSVVELNNEIRELRNKEEQEIER 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 248 ICKELSMQVKKNALSLTSALETLTVIDVAFTKAKWAVRYDGCIPsLQSRDHSMYLEHAKHPLIDEKKVVCNTYELNDKQA 327
Cdd:PRK00409 250 ILKELSAKVAKNLDFLKFLNKIFDELDFIFARARYAKALKATFP-LFNDEGKIDLRQARHPLLDGEKVVPKDISLGFDKT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 328 CLMISGPNMGGKTVTLKTIGLFVALAHAAFPVLC-HKAILPFYQSMYFDIGDHQSIENNLSTFSSHISRLSHICQKSDEN 406
Cdd:PRK00409 329 VLVITGPNTGGKTVTLKTLGLAALMAKSGLPIPAnEPSEIPVFKEIFADIGDEQSIEQSLSTFSGHMTNIVRILEKADKN 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 407 SFILLDEIGNGTDPLEGASLAVAILEYLISKRSTIITSTHYSQVKTYGKANDSVLVSSVEFNPETLKPTYKYIPGVSGAS 486
Cdd:PRK00409 409 SLVLFDELGAGTDPDEGAALAISILEYLRKRGAKIIATTHYKELKALMYNREGVENASVEFDEETLRPTYRLLIGIPGKS 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 487 YAFHIAREYNLEESILERA-DFLKNENEKqtekelekleklQNDV----------LKQKERF-NQLIEDAHRVQKEACEK 554
Cdd:PRK00409 489 NAFEIAKRLGLPENIIEEAkKLIGEDKEK------------LNELiasleelereLEQKAEEaEALLKEAEKLKEELEEK 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 555 EKEIEKRKAQLDASYQEQLNEMLEKKKAEAKEILTVLRKEKTGKQ-----------HKQIEKMHEldLLNEHVEEIEDDK 623
Cdd:PRK00409 557 KEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYasvkahelieaRKRLNKANE--KKEKKKKKQKEKQ 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 624 KEFKVGDYVKITGLNSHGEIVDIR-RNEATVLTNGMKMKVKISKLEPMHKPQIKKATYKAHVESVSSRFPLELNLIGMRV 702
Cdd:PRK00409 635 EELKVGDEVKYLSLGQKGEVLSIPdDKEAIVQAGIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPRTVSLELDLRGMRY 714
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2125643774 703 EEGVAALDKYLDQAVVKHIKQVRIIHGMGTGALRTAVWKDLKKQPNVSKFNSAGPSEGGLGATIVILK 770
Cdd:PRK00409 715 EEALERLDKYLDDALLAGYGEVLIIHGKGTGKLRKGVQEFLKKHPSVKSFRDAPPNEGGFGVTIVELK 782
|
|
| mutS2 |
TIGR01069 |
MutS2 family protein; Function of MutS2 is unknown. It should not be considered a DNA mismatch ... |
12-770 |
6.27e-134 |
|
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: 415.37 E-value: 6.27e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 12 AIDFSSVLTQVSAFSSFSCTKEKILNALPVFDKLEIQEQLNYAKEAIQFEQAgglLSLSGANDISLPVSKASKQMTLT-S 90
Cdd:TIGR01069 8 KLEFDKVKENLLKQTFTPLGKEDAIGLKPPKSVEESKEIIIKLTALGSIENN---VRFFGFEDIRELLKRAELGGIVKgL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 91 KELISIYHFLMAVKQAKQ-SLDESDYPKLTNLAQSMDGCTRLMDSIISKIDLTGSVKEDATPALKSMHKALVDTRLALQS 169
Cdd:TIGR01069 85 EYILVIQNALKTVKHLKVlSEHVLDLEILFHLRLNLITLPPLENDIIACIDDDGKVKDGASEELDAIRESLKALEEEVVK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 170 KSRQFLKKNSLK--LMENMTTTVSGRVVVLVRAQDKNAFGGMIHGQSSSGLAYYVEPSSFVADNNEISSLMIRIEEEKKR 247
Cdd:TIGR01069 165 RLHKIIRSKELAkyLSDTIVTIRNGRYVLPLKSGFKGKIKGIVHDTSSSGETFYIEPQAIVKLNNKLAQLKNEEECEIEK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 248 ICKELSMQVKKNALSLTSALETLTVIDVAFTKAKWAVRYDGCIPSLqSRDHSMYLEHAKHPLIDEKKVVCNTYELNDKQA 327
Cdd:TIGR01069 245 ILRTLSEKVQEYLLELKFLFKEFDFLDSLQARARYAKAVKGEFPMP-SFTGKIILENARHPLLKEPKVVPFTLNLKFEKR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 328 CLMISGPNMGGKTVTLKTIGLFVALAHAAFPVLCHK-AILPFYQSMYFDIGDHQSIENNLSTFSSHISRLSHICQKSDEN 406
Cdd:TIGR01069 324 VLAITGPNTGGKTVTLKTLGLLALMFQSGIPIPANEhSEIPYFEEIFADIGDEQSIEQNLSTFSGHMKNISAILSKTTEN 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 407 SFILLDEIGNGTDPLEGASLAVAILEYLISKRSTIITSTHYSQVKTYGKANDSVLVSSVEFNPETLKPTYKYIPGVSGAS 486
Cdd:TIGR01069 404 SLVLFDELGAGTDPDEGSALAISILEYLLKQNAQVLITTHYKELKALMYNNEGVENASVLFDEETLSPTYKLLKGIPGES 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 487 YAFHIAREYNLEESILERA-DFLKNENEKQTEKELEKLEKLQndvlKQKERFNQLIEDAHRVQKEACEKEKEIEKRKAQL 565
Cdd:TIGR01069 484 YAFEIAQRYGIPHFIIEQAkTFYGEFKEEINVLIEKLSALEK----ELEQKNEHLEKLLKEQEKLKKELEQEMEELKERE 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 566 DASYQEQLNEMLEKKKAEAKEILTVLRKEKTGKQHKQIEKMHELDL--LNEHVEEIEDDKKEF---KVGDYVKITGLNSH 640
Cdd:TIGR01069 560 RNKKLELEKEAQEALKALKKEVESIIRELKEKKIHKAKEIKSIEDLvkLKETKQKIPQKPTNFqadKIGDKVRIRYFGQK 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 641 GEIVDIR-RNEATVLTNGMKMKVKISKLEPMHKPQIKKA-----TYKAHVESVSsrfpLELNLIGMRVEEGVAALDKYLD 714
Cdd:TIGR01069 640 GKIVQILgGNKWNVTVGGMRMKVHGSELEKINKAPPPKKfkvpkTTKPEPKEAS----LTLDLRGQRSEEALDRLEKFLN 715
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 2125643774 715 QAVVKHIKQVRIIHGMGTGALRTAVWKDLKKQPNVSKFNSAGPSEGGLGATIVILK 770
Cdd:TIGR01069 716 DALLAGYEVVLIIHGKGSGKLRKGVQELLKNHPKVKSFRDAPPNDGGSGVTIVYLE 771
|
|
| ABC_MutS2 |
cd03280 |
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ... |
301-497 |
5.38e-79 |
|
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: 252.17 E-value: 5.38e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 301 YLEHAKHPLI--DEKKVVCNTYELNDKQACLMISGPNMGGKTVTLKTIGLFVALAHAAFPVLC-HKAILPFYQSMYFDIG 377
Cdd:cd03280 1 RLREARHPLLplQGEKVVPLDIQLGENKRVLVITGPNAGGKTVTLKTLGLLTLMAQSGLPIPAaEGSSLPVFENIFADIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 378 DHQSIENNLSTFSSHISRLSHICQKSDENSFILLDEIGNGTDPLEGASLAVAILEYLISKRSTIITSTHYSQVKTYGKAN 457
Cdd:cd03280 81 DEQSIEQSLSTFSSHMKNIARILQHADPDSLVLLDELGSGTDPVEGAALAIAILEELLERGALVIATTHYGELKAYAYKR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2125643774 458 DSVLVSSVEFNPETLKPTYKYIPGVSGASYAFHIAREYNL 497
Cdd:cd03280 161 EGVENASMEFDPETLKPTYRLLIGVPGRSNALEIARRLGL 200
|
|
| MUTSac |
smart00534 |
ATPase domain of DNA mismatch repair MUTS family; |
328-505 |
2.90e-56 |
|
ATPase domain of DNA mismatch repair MUTS family;
Pssm-ID: 197777 [Multi-domain] Cd Length: 185 Bit Score: 190.46 E-value: 2.90e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 328 CLMISGPNMGGKTVTLKTIGLFVALAHAAFPVLCHKAILPFYQSMYFDIGDHQSIENNLSTFSSHISRLSHICQKSDENS 407
Cdd:smart00534 1 VVIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPVFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATKNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 408 FILLDEIGNGTDPLEGASLAVAILEYLISK-RSTIITSTHYSQVKTYGKANDSVLVSSVEF--NPETLKPTYKYIPGVSG 484
Cdd:smart00534 81 LVLLDELGRGTSTYDGLAIAAAILEYLLEKiGARTLFATHYHELTKLADNHPGVRNLHMSAleETENITFLYKLKPGVAG 160
|
170 180
....*....|....*....|.
gi 2125643774 485 ASYAFHIAREYNLEESILERA 505
Cdd:smart00534 161 KSYGIEVAKLAGLPKEVIERA 181
|
|
| MutS_V |
pfam00488 |
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
329-505 |
3.10e-27 |
|
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: 109.21 E-value: 3.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 329 LMISGPNMGGKTVTLKTIGLFVALAHAAFPVLCHKAILPFYQSMYFDIGDHQSIENNLSTFSSHISRLSHICQKSDENSF 408
Cdd:pfam00488 1 LIITGPNMGGKSTYLRQVALIVLMAQIGSFVPAESAEIGIVDRIFTRIGASDDLAKGRSTFMVEMLETANILHNATDKSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 409 ILLDEIGNGTDPLEGASLAVAILEYLISK-RSTIITSTHYSQVKTYGKANDSV--LVSSVEFNPETLKPTYKYIPGVSGA 485
Cdd:pfam00488 81 VILDELGRGTSTYDGLAIAWAVAEHLAEKiKARTLFATHYHELTKLAEKLPAVknLHMAAVEDDDDIVFLYKVQPGAADK 160
|
170 180
....*....|....*....|
gi 2125643774 486 SYAFHIAREYNLEESILERA 505
Cdd:pfam00488 161 SYGIHVAELAGLPESVVERA 180
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1-770 |
0e+00 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 666.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 1 MEQNFRNELnqaiDFSSVLTQVSAFSSFSCTKEKILNALPVFDKLEIQEQLNYAKEAIQFEQAGGLLSLSGANDISLPVS 80
Cdd:COG1193 1 MNEKTLEKL----EFDKILELLAEYAVSELGKELARKLRPSTDLEEVERLLAETAEARRLLRLEGGLPLGGIPDIRPLLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 81 KASKQMTLTSKELISIYHFLMAVKQAKQSLD--ESDYPKLTNLAQSMDGCTRLMDSIISKIDLTGSVKEDATPALKSMHK 158
Cdd:COG1193 77 RAEEGGVLSPEELLDIARTLRAARRLKRFLEelEEEYPALKELAERLPPLPELEKEIDRAIDEDGEVKDSASPELRRIRR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 159 ALVDTRLALQSKSRQFLKKNSLK--LMENMTTTVSGRVVVLVRAQDKNAFGGMIHGQSSSGLAYYVEPSSFVADNNEISS 236
Cdd:COG1193 157 EIRSLEQRIREKLESILRSASYQkyLQDAIITIRNGRYVIPVKAEYKGKIPGIVHDQSASGQTLFIEPMAVVELNNELRE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 237 LMIRIEEEKKRICKELSMQVKKNALSLTSALETLTVIDVAFTKAKWAVRYDGCIPSLqSRDHSMYLEHAKHPLIDEKKVV 316
Cdd:COG1193 237 LEAEERREIERILRELSALVREYAEELLENLEILAELDFIFAKARYALELKAVKPEL-NDEGYIKLKKARHPLLDLKKVV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 317 CNTYELNDKQACLMISGPNMGGKTVTLKTIGLFVALAHAAFPVLCHK-AILPFYQSMYFDIGDHQSIENNLSTFSSHISR 395
Cdd:COG1193 316 PIDIELGEDFRTLVITGPNTGGKTVTLKTVGLLTLMAQSGLPIPAAEgSELPVFDNIFADIGDEQSIEQSLSTFSSHMTN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 396 LSHICQKSDENSFILLDEIGNGTDPLEGASLAVAILEYLISKRSTIITSTHYSQVKTYGKANDSVLVSSVEFNPETLKPT 475
Cdd:COG1193 396 IVEILEKADENSLVLLDELGAGTDPQEGAALAIAILEELLERGARVVATTHYSELKAYAYNTEGVENASVEFDVETLSPT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 476 YKYIPGVSGASYAFHIAREYNLEESILERA-DFLKNENEKqtekelekleklQNDVL----KQKERFNQLIEDAHRVQKE 550
Cdd:COG1193 476 YRLLIGVPGRSNAFEIARRLGLPEEIIERArELLGEESID------------VEKLIeeleRERRELEEEREEAERLREE 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 551 ACEKEKEIEKRKAQLD-------ASYQEQLNEMLEKKKAEAKEILTVLRKEKTgKQHKQIEKMHELD-LLNEHVEEIEDD 622
Cdd:COG1193 544 LEKLREELEEKLEELEeekeeilEKAREEAEEILREARKEAEELIRELREAQA-EEEELKEARKKLEeLKQELEEKLEKP 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 623 K---------KEFKVGDYVKITGLNSHGEIVDIRR-NEATVLTNGMKMKVKISKLEPMHKPQIKKATYKAHVESVSSR-- 690
Cdd:COG1193 623 KkkakpakppEELKVGDRVRVLSLGQKGEVLEIPKgGEAEVQVGILKMTVKLSDLEKVEKKKPKKPKKRPAGVSVSVSka 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 691 --FPLELNLIGMRVEEGVAALDKYLDQAVVKHIKQVRIIHGMGTGALRTAVWKDLKKQPNVSKFNSAGPSEGGLGATIVI 768
Cdd:COG1193 703 stVSPELDLRGMRVEEALPELDKYLDDALLAGLPEVRIIHGKGTGALRKGVREYLKRHPYVKSFRLGEPGEGGDGVTVVE 782
|
..
gi 2125643774 769 LK 770
Cdd:COG1193 783 LK 784
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
14-770 |
0e+00 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 552.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 14 DFSSVLTQVSAFSSFSCTKEKILNALPVFDKLEIQEQLNYAKEAIQFEQAGGLLSLSGANDISLPVSKASKQMTLTSKEL 93
Cdd:PRK00409 10 EFNKIKEQLKTFAASELGKEKVLQLDPETDFEEVEELLEETDEAAKLLRLKGLPPFEGVKDIDDALKRAEKGGVLSGDEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 94 ISIYHFLMAVKQAK----QSLDESDYPKLTNLAQSMDGCTRLMDSIISKIDLTGSVKEDATPALKSMHKALVDTRLALQS 169
Cdd:PRK00409 90 LEIAKTLRYFRQLKrfieDLEEEEELPILEEWVAKIRTLPELEQEIHNCIDEEGEVKDSASEKLRGIRRQLRRKKSRIRE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 170 KSRQFLKKNSL--KLMENMTTTVSGRVVVLVRAQDKNAFGGMIHGQSSSGLAYYVEPSSFVADNNEISSLMIRIEEEKKR 247
Cdd:PRK00409 170 KLESIIRSKSLqkYLQDTIITIRNDRYVLPVKAEYKHAIKGIVHDQSSSGATLYIEPQSVVELNNEIRELRNKEEQEIER 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 248 ICKELSMQVKKNALSLTSALETLTVIDVAFTKAKWAVRYDGCIPsLQSRDHSMYLEHAKHPLIDEKKVVCNTYELNDKQA 327
Cdd:PRK00409 250 ILKELSAKVAKNLDFLKFLNKIFDELDFIFARARYAKALKATFP-LFNDEGKIDLRQARHPLLDGEKVVPKDISLGFDKT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 328 CLMISGPNMGGKTVTLKTIGLFVALAHAAFPVLC-HKAILPFYQSMYFDIGDHQSIENNLSTFSSHISRLSHICQKSDEN 406
Cdd:PRK00409 329 VLVITGPNTGGKTVTLKTLGLAALMAKSGLPIPAnEPSEIPVFKEIFADIGDEQSIEQSLSTFSGHMTNIVRILEKADKN 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 407 SFILLDEIGNGTDPLEGASLAVAILEYLISKRSTIITSTHYSQVKTYGKANDSVLVSSVEFNPETLKPTYKYIPGVSGAS 486
Cdd:PRK00409 409 SLVLFDELGAGTDPDEGAALAISILEYLRKRGAKIIATTHYKELKALMYNREGVENASVEFDEETLRPTYRLLIGIPGKS 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 487 YAFHIAREYNLEESILERA-DFLKNENEKqtekelekleklQNDV----------LKQKERF-NQLIEDAHRVQKEACEK 554
Cdd:PRK00409 489 NAFEIAKRLGLPENIIEEAkKLIGEDKEK------------LNELiasleelereLEQKAEEaEALLKEAEKLKEELEEK 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 555 EKEIEKRKAQLDASYQEQLNEMLEKKKAEAKEILTVLRKEKTGKQ-----------HKQIEKMHEldLLNEHVEEIEDDK 623
Cdd:PRK00409 557 KEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYasvkahelieaRKRLNKANE--KKEKKKKKQKEKQ 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 624 KEFKVGDYVKITGLNSHGEIVDIR-RNEATVLTNGMKMKVKISKLEPMHKPQIKKATYKAHVESVSSRFPLELNLIGMRV 702
Cdd:PRK00409 635 EELKVGDEVKYLSLGQKGEVLSIPdDKEAIVQAGIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPRTVSLELDLRGMRY 714
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2125643774 703 EEGVAALDKYLDQAVVKHIKQVRIIHGMGTGALRTAVWKDLKKQPNVSKFNSAGPSEGGLGATIVILK 770
Cdd:PRK00409 715 EEALERLDKYLDDALLAGYGEVLIIHGKGTGKLRKGVQEFLKKHPSVKSFRDAPPNEGGFGVTIVELK 782
|
|
| mutS2 |
TIGR01069 |
MutS2 family protein; Function of MutS2 is unknown. It should not be considered a DNA mismatch ... |
12-770 |
6.27e-134 |
|
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: 415.37 E-value: 6.27e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 12 AIDFSSVLTQVSAFSSFSCTKEKILNALPVFDKLEIQEQLNYAKEAIQFEQAgglLSLSGANDISLPVSKASKQMTLT-S 90
Cdd:TIGR01069 8 KLEFDKVKENLLKQTFTPLGKEDAIGLKPPKSVEESKEIIIKLTALGSIENN---VRFFGFEDIRELLKRAELGGIVKgL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 91 KELISIYHFLMAVKQAKQ-SLDESDYPKLTNLAQSMDGCTRLMDSIISKIDLTGSVKEDATPALKSMHKALVDTRLALQS 169
Cdd:TIGR01069 85 EYILVIQNALKTVKHLKVlSEHVLDLEILFHLRLNLITLPPLENDIIACIDDDGKVKDGASEELDAIRESLKALEEEVVK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 170 KSRQFLKKNSLK--LMENMTTTVSGRVVVLVRAQDKNAFGGMIHGQSSSGLAYYVEPSSFVADNNEISSLMIRIEEEKKR 247
Cdd:TIGR01069 165 RLHKIIRSKELAkyLSDTIVTIRNGRYVLPLKSGFKGKIKGIVHDTSSSGETFYIEPQAIVKLNNKLAQLKNEEECEIEK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 248 ICKELSMQVKKNALSLTSALETLTVIDVAFTKAKWAVRYDGCIPSLqSRDHSMYLEHAKHPLIDEKKVVCNTYELNDKQA 327
Cdd:TIGR01069 245 ILRTLSEKVQEYLLELKFLFKEFDFLDSLQARARYAKAVKGEFPMP-SFTGKIILENARHPLLKEPKVVPFTLNLKFEKR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 328 CLMISGPNMGGKTVTLKTIGLFVALAHAAFPVLCHK-AILPFYQSMYFDIGDHQSIENNLSTFSSHISRLSHICQKSDEN 406
Cdd:TIGR01069 324 VLAITGPNTGGKTVTLKTLGLLALMFQSGIPIPANEhSEIPYFEEIFADIGDEQSIEQNLSTFSGHMKNISAILSKTTEN 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 407 SFILLDEIGNGTDPLEGASLAVAILEYLISKRSTIITSTHYSQVKTYGKANDSVLVSSVEFNPETLKPTYKYIPGVSGAS 486
Cdd:TIGR01069 404 SLVLFDELGAGTDPDEGSALAISILEYLLKQNAQVLITTHYKELKALMYNNEGVENASVLFDEETLSPTYKLLKGIPGES 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 487 YAFHIAREYNLEESILERA-DFLKNENEKQTEKELEKLEKLQndvlKQKERFNQLIEDAHRVQKEACEKEKEIEKRKAQL 565
Cdd:TIGR01069 484 YAFEIAQRYGIPHFIIEQAkTFYGEFKEEINVLIEKLSALEK----ELEQKNEHLEKLLKEQEKLKKELEQEMEELKERE 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 566 DASYQEQLNEMLEKKKAEAKEILTVLRKEKTGKQHKQIEKMHELDL--LNEHVEEIEDDKKEF---KVGDYVKITGLNSH 640
Cdd:TIGR01069 560 RNKKLELEKEAQEALKALKKEVESIIRELKEKKIHKAKEIKSIEDLvkLKETKQKIPQKPTNFqadKIGDKVRIRYFGQK 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 641 GEIVDIR-RNEATVLTNGMKMKVKISKLEPMHKPQIKKA-----TYKAHVESVSsrfpLELNLIGMRVEEGVAALDKYLD 714
Cdd:TIGR01069 640 GKIVQILgGNKWNVTVGGMRMKVHGSELEKINKAPPPKKfkvpkTTKPEPKEAS----LTLDLRGQRSEEALDRLEKFLN 715
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 2125643774 715 QAVVKHIKQVRIIHGMGTGALRTAVWKDLKKQPNVSKFNSAGPSEGGLGATIVILK 770
Cdd:TIGR01069 716 DALLAGYEVVLIIHGKGSGKLRKGVQELLKNHPKVKSFRDAPPNDGGSGVTIVYLE 771
|
|
| ABC_MutS2 |
cd03280 |
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ... |
301-497 |
5.38e-79 |
|
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: 252.17 E-value: 5.38e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 301 YLEHAKHPLI--DEKKVVCNTYELNDKQACLMISGPNMGGKTVTLKTIGLFVALAHAAFPVLC-HKAILPFYQSMYFDIG 377
Cdd:cd03280 1 RLREARHPLLplQGEKVVPLDIQLGENKRVLVITGPNAGGKTVTLKTLGLLTLMAQSGLPIPAaEGSSLPVFENIFADIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 378 DHQSIENNLSTFSSHISRLSHICQKSDENSFILLDEIGNGTDPLEGASLAVAILEYLISKRSTIITSTHYSQVKTYGKAN 457
Cdd:cd03280 81 DEQSIEQSLSTFSSHMKNIARILQHADPDSLVLLDELGSGTDPVEGAALAIAILEELLERGALVIATTHYGELKAYAYKR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2125643774 458 DSVLVSSVEFNPETLKPTYKYIPGVSGASYAFHIAREYNL 497
Cdd:cd03280 161 EGVENASMEFDPETLKPTYRLLIGVPGRSNALEIARRLGL 200
|
|
| MUTSac |
smart00534 |
ATPase domain of DNA mismatch repair MUTS family; |
328-505 |
2.90e-56 |
|
ATPase domain of DNA mismatch repair MUTS family;
Pssm-ID: 197777 [Multi-domain] Cd Length: 185 Bit Score: 190.46 E-value: 2.90e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 328 CLMISGPNMGGKTVTLKTIGLFVALAHAAFPVLCHKAILPFYQSMYFDIGDHQSIENNLSTFSSHISRLSHICQKSDENS 407
Cdd:smart00534 1 VVIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPVFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATKNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 408 FILLDEIGNGTDPLEGASLAVAILEYLISK-RSTIITSTHYSQVKTYGKANDSVLVSSVEF--NPETLKPTYKYIPGVSG 484
Cdd:smart00534 81 LVLLDELGRGTSTYDGLAIAAAILEYLLEKiGARTLFATHYHELTKLADNHPGVRNLHMSAleETENITFLYKLKPGVAG 160
|
170 180
....*....|....*....|.
gi 2125643774 485 ASYAFHIAREYNLEESILERA 505
Cdd:smart00534 161 KSYGIEVAKLAGLPKEVIERA 181
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
305-497 |
4.60e-48 |
|
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: 168.58 E-value: 4.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 305 AKHPLI----DEKKVVCNTYELNDkQACLMISGPNMGGKTVTLKTIGLFVALAHAAFPVLCHKAILPFYQSMYFDIGDHQ 380
Cdd:cd03243 5 GRHPVLlaltKGETFVPNDINLGS-GRLLLITGPNMGGKSTYLRSIGLAVLLAQIGCFVPAESASIPLVDRIFTRIGAED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 381 SIENNLSTFSSHISRLSHICQKSDENSFILLDEIGNGTDPLEGASLAVAILEYLISKRSTIITSTHYSQVKTYGKANDSV 460
Cdd:cd03243 84 SISDGRSTFMAELLELKEILSLATPRSLVLIDELGRGTSTAEGLAIAYAVLEHLLEKGCRTLFATHFHELADLPEQVPGV 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 2125643774 461 LVSSVEF--NPETLKPTYKYIPGVSGASYAFHIAREYNL 497
Cdd:cd03243 164 KNLHMEEliTTGGLTFTYKLIDGICDPSYALQIAELAGL 202
|
|
| mutS1 |
TIGR01070 |
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair] |
91-544 |
2.17e-32 |
|
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273427 [Multi-domain] Cd Length: 840 Bit Score: 134.90 E-value: 2.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 91 KELISIYHFLMAVKQAKQSLDESDYPKLTNLAQSMDGCTRLMD----SIIS----KIDLTGSVKEDATP---ALKSMHKA 159
Cdd:TIGR01070 348 RDLARLRTSLEQLPELRALLEELEGPTLQALAAQIDDFSELLElleaALIEnpplVVRDGGLIREGYDEeldELRAASRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 160 LVDTRLALQSKSRQFLKKNSLKLMENmttTVSGRVVVLVRAQDKNAFGGMIHGQSSSGLAYYVEPssfvaDNNEISSLMI 239
Cdd:TIGR01070 428 GTDYLARLEARERERTGIPTLKVGYN---AVFGYYIEVTRGQLHLVPAHYRRRQTLKNAERYITP-----ELKEKEDKVL 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 240 RIEEEKKRICKELSMQ----VKKNALSLTSALETLTVIDVAFTKAKWAVRYDGCIPSLqSRDHSMYLEHAKHPLIDE--- 312
Cdd:TIGR01070 500 EAEGKILALEKELFEElrelLKKYLEALQEAARALAELDVLANLAEVAETLHYTRPRF-GDDPQLRIREGRHPVVEQvlr 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 313 KKVVCNTYELNDKQACLMISGPNMGGKTVTLKTIGLFVALAHAAFPVLCHKAILPFYQSMYFDIGDHQSIENNLSTFSSH 392
Cdd:TIGR01070 579 TPFVPNDLEMAHNRRMLLITGPNMGGKSTYMRQTALIALLAQIGSFVPAESAELPLFDRIFTRIGASDDLASGRSTFMVE 658
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 393 ISRLSHICQKSDENSFILLDEIGNGTDPLEGASLAVAILEYLISK-RSTIITSTHYSQV-----KTYGKANdsVLVSSVE 466
Cdd:TIGR01070 659 MTEAANILHNATENSLVLFDEIGRGTSTYDGLALAWAIAEYLHEHiRAKTLFATHYFELtaleeSLPGLKN--VHVAALE 736
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2125643774 467 FNpETLKPTYKYIPGVSGASYAFHIAREYNLEESILERADFLKNENEKQTEKELEKLEKLQNDVLKQKERFNQLIEDA 544
Cdd:TIGR01070 737 HN-GTIVFLHQVLPGPASKSYGLAVAALAGLPKEVIARARQILTQLEARSTESEAPQRKAQTSAPEQISLFDEAETHP 813
|
|
| ABC_MutS-like |
cd03283 |
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ... |
307-491 |
3.30e-29 |
|
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: 115.09 E-value: 3.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 307 HPLIDEKKVVCNTYELNDKQACLmISGPNMGGKTVTLKTIGLFVALAHAAFPVLCHKAILPF---YQSMyfDIGDhqSIE 383
Cdd:cd03283 7 HPLIGREKRVANDIDMEKKNGIL-ITGSNMSGKSTFLRTIGVNVILAQAGAPVCASSFELPPvkiFTSI--RVSD--DLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 384 NNLSTFSSHISRLSHICQ--KSDENSFILLDEIGNGTDPLEGASLAVAILEYLISKRSTIITSTHYSQVKTYGKANDSV- 460
Cdd:cd03283 82 DGISYFYAELRRLKEIVEkaKKGEPVLFLLDEIFKGTNSRERQAASAAVLKFLKNKNTIGIISTHDLELADLLDLDSAVr 161
|
170 180 190
....*....|....*....|....*....|..
gi 2125643774 461 -LVSSVEFNPETLKPTYKYIPGVSGASYAFHI 491
Cdd:cd03283 162 nYHFREDIDDNKLIFDYKLKPGVSPTRNALRL 193
|
|
| ABC_MSH4_euk |
cd03282 |
ATP-binding cassette domain of eukaryotic MutS4 homolog; The MutS protein initiates DNA ... |
305-447 |
2.03e-28 |
|
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: 113.25 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 305 AKHPLIDE--KKVVCNTYELNDKQACL-MISGPNMGGKTVTLKTIGLFVALAHAAFPVLCHKAILPFYQSMYFDIGDHQS 381
Cdd:cd03282 5 SRHPILDRdkKNFIPNDIYLTRGSSRFhIITGPNMSGKSTYLKQIALLAIMAQIGCFVPAEYATLPIFNRLLSRLSNDDS 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2125643774 382 IENNLSTFSSHISRLSHICQKSDENSFILLDEIGNGTDPLEGASLAVAILEYLISKRSTIITSTHY 447
Cdd:cd03282 85 MERNLSTFASEMSETAYILDYADGDSLVLIDELGRGTSSADGFAISLAILECLIKKESTVFFATHF 150
|
|
| ABC_MSH3_euk |
cd03287 |
ATP-binding cassette domain of eukaryotic MutS3 homolog; The MutS protein initiates DNA ... |
305-505 |
1.30e-27 |
|
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: 111.43 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 305 AKHPLI---DEKKVVCNTYELN-DKQACLMISGPNMGGKTVTLKTIGLFVALAHAAFPVLCHKAILPFYQSMYFDIGDHQ 380
Cdd:cd03287 6 GRHPMIeslLDKSFVPNDIHLSaEGGYCQIITGPNMGGKSSYIRQVALITIMAQIGSFVPASSATLSIFDSVLTRMGASD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 381 SIENNLSTFSSHISRLSHICQKSDENSFILLDEIGNGTDPLEGASLAVAILEYLIS-KRSTIITSTHY-----------S 448
Cdd:cd03287 86 SIQHGMSTFMVELSETSHILSNCTSRSLVILDELGRGTSTHDGIAIAYATLHYLLEeKKCLVLFVTHYpslgeilrrfeG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2125643774 449 QVKTYGKANDSVLVSSVEFNPETLKPTYKYIPGVSGASYAFHIAREYNLEESILERA 505
Cdd:cd03287 166 SIRNYHMSYLESQKDFETSDSQSITFLYKLVRGLASRSFGLNVARLAGLPKSIISRA 222
|
|
| MutS_V |
pfam00488 |
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
329-505 |
3.10e-27 |
|
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: 109.21 E-value: 3.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 329 LMISGPNMGGKTVTLKTIGLFVALAHAAFPVLCHKAILPFYQSMYFDIGDHQSIENNLSTFSSHISRLSHICQKSDENSF 408
Cdd:pfam00488 1 LIITGPNMGGKSTYLRQVALIVLMAQIGSFVPAESAEIGIVDRIFTRIGASDDLAKGRSTFMVEMLETANILHNATDKSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 409 ILLDEIGNGTDPLEGASLAVAILEYLISK-RSTIITSTHYSQVKTYGKANDSV--LVSSVEFNPETLKPTYKYIPGVSGA 485
Cdd:pfam00488 81 VILDELGRGTSTYDGLAIAWAVAEHLAEKiKARTLFATHYHELTKLAEKLPAVknLHMAAVEDDDDIVFLYKVQPGAADK 160
|
170 180
....*....|....*....|
gi 2125643774 486 SYAFHIAREYNLEESILERA 505
Cdd:pfam00488 161 SYGIHVAELAGLPESVVERA 180
|
|
| Smr |
pfam01713 |
Smr domain; This family includes the Smr (Small MutS Related) proteins, and the C-terminal ... |
696-770 |
2.23e-26 |
|
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: 102.93 E-value: 2.23e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2125643774 696 NLIGMRVEEGVAALDKYLDQAVVKHIKQVRIIHGMGT-GALRTAVWKDLKKQPNVSKFNSAGPSEGGLGATIVILK 770
Cdd:pfam01713 1 DLHGMTVEEAREALDKFLDDALLAGLRCVLIIHGKGThGVLRKAVREWLKQHPLVLAFRSAPPGEGGDGATYVLLK 76
|
|
| ABC_MSH2_euk |
cd03285 |
ATP-binding cassette domain of eukaryotic MutS2 homolog; The MutS protein initiates DNA ... |
301-505 |
4.01e-26 |
|
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: 107.08 E-value: 4.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 301 YLEHAKHPLI---DEKKVVCNTYEL-NDKQACLMISGPNMGGKTVTLKTIGLFVALAHAAFPVLCHKAILPFYQSMYFDI 376
Cdd:cd03285 1 VLKEARHPCVeaqDDVAFIPNDVTLtRGKSRFLIITGPNMGGKSTYIRQIGVIVLMAQIGCFVPCDSADIPIVDCILARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 377 GDHQSIENNLSTFSSHISRLSHICQKSDENSFILLDEIGNGTDPLEGASLAVAILEYLISK-RSTIITSTHYSQV----- 450
Cdd:cd03285 81 GASDSQLKGVSTFMAEMLETAAILKSATENSLIIIDELGRGTSTYDGFGLAWAIAEYIATQiKCFCLFATHFHELtalad 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2125643774 451 KTYGKANDSVlVSSVEFNPETLKPTYKYIPGVSGASYAFHIAREYNLEESILERA 505
Cdd:cd03285 161 EVPNVKNLHV-TALTDDASRTLTMLYKVEKGACDQSFGIHVAELANFPKEVIEMA 214
|
|
| ABC_MutS1 |
cd03284 |
ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair ... |
302-505 |
5.22e-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: 106.58 E-value: 5.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 302 LEHAKHP----LIDEKKVVCNTYELNDKQACLMISGPNMGGKTVTLKTIGLFVALAHAAFPVLCHKAILPFYQSMYFDIG 377
Cdd:cd03284 2 IEGGRHPvveqVLDNEPFVPNDTELDPERQILLITGPNMAGKSTYLRQVALIALLAQIGSFVPASKAEIGVVDRIFTRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 378 DHQSIENNLSTFSSHISRLSHICQKSDENSFILLDEIGNGTDPLEGASLAVAILEYLISK-RSTIITSTHYSQVKTYGKA 456
Cdd:cd03284 82 ASDDLAGGRSTFMVEMVETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAIVEYLHEKiGAKTLFATHYHELTELEGK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2125643774 457 NDSV--LVSSVEFNPETLKPTYKYIPGVSGASYAFHIAREYNLEESILERA 505
Cdd:cd03284 162 LPRVknFHVAVKEKGGGVVFLHKIVEGAADKSYGIEVARLAGLPEEVIERA 212
|
|
| ABC_MSH6_euk |
cd03286 |
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA ... |
301-505 |
3.28e-25 |
|
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: 104.43 E-value: 3.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 301 YLEHAKHPLI---DEKKVVCNTYELNDKQACLMI-SGPNMGGKTVTLKTIGLFVALAHAAFPVLCHKAILPFYQSMYFDI 376
Cdd:cd03286 1 CFEELRHPCLnasTASSFVPNDVDLGATSPRILVlTGPNMGGKSTLLRTVCLAVIMAQMGMDVPAKSMRLSLVDRIFTRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 377 GDHQSIENNLSTFSSHISRLSHICQKSDENSFILLDEIGNGTDPLEGASLAVAILEYLISK-RSTIITSTHYSQ----VK 451
Cdd:cd03286 81 GARDDIMKGESTFMVELSETANILRHATPDSLVILDELGRGTSTHDGYAIAHAVLEYLVKKvKCLTLFSTHYHSlcdeFH 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2125643774 452 TYGKAN----DSVLVSSVEFNPETLKPTYKYIPGVSGASYAFHIAREYNLEESILERA 505
Cdd:cd03286 161 EHGGVRlghmACAVKNESDPTIRDITFLYKLVAGICPKSYGLYVALMAGIPDGVVERA 218
|
|
| ABC_MSH5_euk |
cd03281 |
ATP-binding cassette domain of eukaryotic MutS5 homolog; The MutS protein initiates DNA ... |
329-494 |
2.00e-22 |
|
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: 96.22 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 329 LMISGPNMGGKTVTLKTIGLFVALAHAAFPVLCHKAILPFYQSMYFDIGDHQSIENNLSTFSSHISRLSHICQKSDENSF 408
Cdd:cd03281 32 MVITGPNSSGKSVYLKQVALIVFLAHIGSFVPADSATIGLVDKIFTRMSSRESVSSGQSAFMIDLYQVSKALRLATRRSL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 409 ILLDEIGNGTDPLEGASLAVAILEYLISKRST---IITSTHYSQVKTYGKANDSVLVS----SVEFNP------ETLKPT 475
Cdd:cd03281 112 VLIDEFGKGTDTEDGAGLLIATIEHLLKRGPEcprVIVSTHFHELFNRSLLPERLKIKfltmEVLLNPtstspnEDITYL 191
|
170
....*....|....*....
gi 2125643774 476 YKYIPGVSGASYAFHIARE 494
Cdd:cd03281 192 YRLVPGLADTSFAIHCAKL 210
|
|
| PRK05399 |
PRK05399 |
DNA mismatch repair protein MutS; Provisional |
91-447 |
2.20e-16 |
|
DNA mismatch repair protein MutS; Provisional
Pssm-ID: 235444 [Multi-domain] Cd Length: 854 Bit Score: 83.61 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 91 KELISIYHFLMAVKQAKQSLDESDYPKLTNLAQSMDGCTRLMDSIISKI--DLTGSVKE--------DATpalksmhkal 160
Cdd:PRK05399 362 RDLAALRDSLEALPELKELLAELDSPLLAELAEQLDPLEELADLLERAIveEPPLLIRDggviadgyDAE---------- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 161 VDTRLALQSKSRQFLKK-----------NSLKLMENmtttvsgrvvvlvraqdkNAFGgmihgqsssglaYYVE------ 223
Cdd:PRK05399 432 LDELRALSDNGKDWLAElearerertgiSSLKVGYN------------------KVFG------------YYIEvtkanl 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 224 ---PSSFV-----AdNNE--ISSLMIRIE------EEK-----KRICKELSMQVKKNALSLTSALETLTVIDVAFTKAKW 282
Cdd:PRK05399 482 dkvPEDYIrrqtlK-NAEryITPELKELEdkilsaEEKalaleYELFEELREEVAEHIERLQKLAKALAELDVLASLAEV 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 283 AVRYDGCIPSLqSRDHSMYLEHAKHP----LIDEKKVVCNTYELNDKQACLMISGPNMGGKTVTLKTIGLFVALAHAAFP 358
Cdd:PRK05399 561 AEENNYVRPEF-TDDPGIDIEEGRHPvveqVLGGEPFVPNDCDLDEERRLLLITGPNMAGKSTYMRQVALIVLLAQIGSF 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 359 VLCHKAILPfyqsmYFD-----IG--DhqsienNL----STFSSHISRLSHICQKSDENSFILLDEIGNGTDPLEGASLA 427
Cdd:PRK05399 640 VPAESARIG-----IVDriftrIGasD------DLasgrSTFMVEMTETANILNNATERSLVLLDEIGRGTSTYDGLSIA 708
|
410 420
....*....|....*....|.
gi 2125643774 428 VAILEYLISK-RSTIITSTHY 447
Cdd:PRK05399 709 WAVAEYLHDKiGAKTLFATHY 729
|
|
| MutS |
COG0249 |
DNA mismatch repair ATPase MutS [Replication, recombination and repair]; |
243-529 |
1.18e-15 |
|
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
Pssm-ID: 440019 [Multi-domain] Cd Length: 861 Bit Score: 81.26 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 243 EEK-----KRICKELSMQVKKNALSLTSALETLTVIDVAFTKAKWAVRYDGCIPSLqSRDHSMYLEHAKHP----LIDEK 313
Cdd:COG0249 522 EERalaleYELFEELREEVAAHIERLQALARALAELDVLASLAEVAVENNYVRPEL-DDSPGIEIEGGRHPvveqALPGE 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 314 KVVCNTYELNDKQACLMISGPNMGGKTVTLKTIGLFVALAHAAFPVLCHKAILPfyqsmYFD-----IG--DhqsienNL 386
Cdd:COG0249 601 PFVPNDCDLDPDRRILLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAESARIG-----IVDriftrVGasD------DL 669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 387 ----STFSSHISRLSHICQKSDENSFILLDEIGNGTDPLEGASLAVAILEYLISK-RSTIITSTHY----------SQVK 451
Cdd:COG0249 670 argqSTFMVEMTETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAVAEYLHDKiRARTLFATHYheltelaeklPGVK 749
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 452 TYgkandSVLV----SSVEFnpetlkpTYKYIPGVSGASYAFHIAREYNLEESILERADFLKNENEKQTEKELEKLEKLQ 527
Cdd:COG0249 750 NY-----HVAVkewgGDIVF-------LHKVVPGPADRSYGIHVAKLAGLPASVIERAREILAELEKGEAAAAGKAAPDQ 817
|
..
gi 2125643774 528 ND 529
Cdd:COG0249 818 LS 819
|
|
| MUTSd |
smart00533 |
DNA-binding domain of DNA mismatch repair MUTS family; |
40-312 |
1.38e-13 |
|
DNA-binding domain of DNA mismatch repair MUTS family;
Pssm-ID: 214710 [Multi-domain] Cd Length: 308 Bit Score: 72.33 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 40 PVFDKLEIQEQLNYAKEAIQ----FEQAGGLLSlsGANDISLPVSKASKQmTLTSKELISIYHFLMAVKQAKQSLDESDY 115
Cdd:smart00533 27 PLLDLKEINERLDAVEELVEnpelRQKLRQLLK--RIPDLERLLSRIERG-RASPRDLLRLYDSLEGLKEIRQLLESLDG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 116 P-----------KLTNLAQSMDGCTRlmDSIISKIDLTGSVKEDATPALKSMHKAL--VDTRLA-LQSKSRQFLKKNSLK 181
Cdd:smart00533 104 PllglllkvilePLLELLELLLELLN--DDDPLEVNDGGLIKDGFDPELDELREKLeeLEEELEeLLKKEREELGIDSLK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 182 LMENmttTVSGRVVVLVRAQDKNAFGGMIHGQSSSGLAYYvEPSSFVADNNEISSLMIRIEEEKKRICKELSMQVKKNAL 261
Cdd:smart00533 182 LGYN---KVHGYYIEVTKSEAKKVPKDFIRRSSLKNTERF-TTPELKELENELLEAKEEIERLEKEILRELLEKVLEYLE 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2125643774 262 SLTSALETLTVIDVAFTKAKWAVRYDGCIPSLQSRDHsMYLEHAKHPLIDE 312
Cdd:smart00533 258 ELRALAEALAELDVLLSLATLAAEGNYVRPEFVDSGE-LEIKNGRHPVLEL 307
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
328-451 |
3.91e-13 |
|
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: 67.77 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 328 CLMISGPNMGGKTVTLKTIGLFVALAHAAFPVlcHKAILPFYQSMYFDIGDHQSIENnLSTFSSHISRLSHICQKSDEN- 406
Cdd:cd03227 23 LTIITGPNGSGKSTILDAIGLALGGAQSATRR--RSGVKAGCIVAAVSAELIFTRLQ-LSGGEKELSALALILALASLKp 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2125643774 407 -SFILLDEIGNGTDPLEGASLAVAILEYLISKRSTIITsTHYSQVK 451
Cdd:cd03227 100 rPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVI-THLPELA 144
|
|
| SMR |
smart00463 |
Small MutS-related domain; |
692-770 |
4.13e-11 |
|
Small MutS-related domain;
Pssm-ID: 214676 [Multi-domain] Cd Length: 80 Bit Score: 59.62 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 692 PLELNLIGMRVEEGVAALDKYLDQAVVKHI-KQVRIIHGMGTGALRT--AVWKDLKKQPNVSKFNSAGPseGGLGATIVI 768
Cdd:smart00463 1 KWSLDLHGLTVEEALTALDKFLNNARLKGLeQKLVIITGKGKHSLGGksGVKPALKEHLRVESFRFAEE--GNSGVLVVK 78
|
..
gi 2125643774 769 LK 770
Cdd:smart00463 79 LK 80
|
|
| MSSS |
pfam20297 |
MutS2 and Smr-associated SH3 domain; This is a SH3-like domain associated with the MutS-like ... |
628-667 |
4.53e-08 |
|
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: 49.72 E-value: 4.53e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2125643774 628 VGDYVKITGLNSHGEIVDI--RRNEATVLTNGMKMKVKISKL 667
Cdd:pfam20297 1 VGDEVRVKSLGQKGEVLEVpgKKGEVEVQVGIMKMTVKLSDL 42
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
328-462 |
1.49e-06 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 48.78 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 328 CLMISGPNMGGKTVTLKTIGLFVAlahaafpvlchkailPFYQSMYFDigDHQSIENNLSTFSSHIS-----------RL 396
Cdd:cd00267 27 IVALVGPNGSGKSTLLRAIAGLLK---------------PTSGEILID--GKDIAKLPLEELRRRIGyvpqlsggqrqRV 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2125643774 397 SHICQKSDENSFILLDEIGNGTDPLEGASLAVAILEyLISKRSTIITSTHYSQVKTYgkANDSVLV 462
Cdd:cd00267 90 ALARALLLNPDLLLLDEPTSGLDPASRERLLELLRE-LAEEGRTVIIVTHDPELAEL--AADRVIV 152
|
|
| PRK04950 |
PRK04950 |
ProP expression regulator; Provisional |
567-663 |
8.82e-03 |
|
ProP expression regulator; Provisional
Pssm-ID: 235322 [Multi-domain] Cd Length: 213 Bit Score: 38.37 E-value: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125643774 567 ASYQEQLNEMLEKKKAEAKEILTVLRKEKTGKQHKQIEKMHELDLLNEHVEEIEDDKKEFKVGDYVKITGLNS--HGEIV 644
Cdd:PRK04950 108 AKVQAQRAEQQAKKREAAGEKEKAPRRERKPKPKAPRKKRKPRAQKPEPQHTPVSDISELTVGQAVKVKAGKSamDATVL 187
|
90 100
....*....|....*....|
gi 2125643774 645 DIRRNEATV-LTNGMKMKVK 663
Cdd:PRK04950 188 EITKDDVRVqLDSGLSMIVR 207
|
|
| |
