|
Name |
Accession |
Description |
Interval |
E-value |
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
4-766 |
0e+00 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 825.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 4 DARALSALDFPRVLDALAERSATSLGAERARALRPSDDPERIARELDEVEDAL----FGVSLSLGGIHDIRDLHARAAEG 79
Cdd:COG1193 2 NEKTLEKLEFDKILELLAEYAVSELGKELARKLRPSTDLEEVERLLAETAEARrllrLEGGLPLGGIPDIRPLLKRAEEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 80 RVLSGSELLSAAYSLDGAMTVKRAIGVNSRG--PLREVAVGLGDHSELVRRVLSALDRDGAVRDDASPRLRDLRKRIEPL 157
Cdd:COG1193 82 GVLSPEELLDIARTLRAARRLKRFLEELEEEypALKELAERLPPLPELEKEIDRAIDEDGEVKDSASPELRRIRREIRSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 158 RGRIRERLTATL--EKWSDVLQEHIVTIRRDRYVLPVQASRVGQVQGIIVDASATGQTYFVEPAAVTQLNNELTRLILDE 235
Cdd:COG1193 162 EQRIREKLESILrsASYQKYLQDAIITIRNGRYVIPVKAEYKGKIPGIVHDQSASGQTLFIEPMAVVELNNELRELEAEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 236 EAEVRRILTELSGLLAGDAD-VPMTLVTVGELDLIASKARLARDWRLNRPEQVEGGRYDLREVRHPLI--ENPVANDLSL 312
Cdd:COG1193 242 RREIERILRELSALVREYAEeLLENLEILAELDFIFAKARYALELKAVKPELNDEGYIKLKKARHPLLdlKKVVPIDIEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 313 GET-KLLLITGPNMGGKTATIKTLGLAVLMHQCGLYV-AAASARLPVVRDVLVDIGDEQSIEASLSTFASHLKHLRYVLR 390
Cdd:COG1193 322 GEDfRTLVITGPNTGGKTVTLKTVGLLTLMAQSGLPIpAAEGSELPVFDNIFADIGDEQSIEQSLSTFSSHMTNIVEILE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 391 HAAPDTLVLVDELGSGTDPNEGAALAQALIECLLTQDARGVITSHLSPLKLFALETPGLKNASMGFDVDTLAPTYVLQVG 470
Cdd:COG1193 402 KADENSLVLLDELGAGTDPQEGAALAIAILEELLERGARVVATTHYSELKAYAYNTEGVENASVEFDVETLSPTYRLLIG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 471 QPGRSFALAIAQRMGLPADVLRRAEDLLGPDAGLMERMLEGLEREREDLRAQLEGTAAARRDAEAELGRVRQERETLELR 550
Cdd:COG1193 482 VPGRSNAFEIARRLGLPEEIIERARELLGEESIDVEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEE 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 551 RNEMLAEASQKAESLYADAIERVRTLRARAQEDSARPRVMQELR-ELRVSAQKARP------APIVREERGDPIRVGSRV 623
Cdd:COG1193 562 KEEILEKAREEAEEILREARKEAEELIRELREAQAEEEELKEARkKLEELKQELEEklekpkKKAKPAKPPEELKVGDRV 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 624 DVPAYNATGQVLEL-RGDDLVVQLGVMKVGVKRRDVRLKQEPKVTAPRTRGPRTAFAGAVaASTFQNELQLRGMGVEEAV 702
Cdd:COG1193 642 RVLSLGQKGEVLEIpKGGEAEVQVGILKMTVKLSDLEKVEKKKPKKPKKRPAGVSVSVSK-ASTVSPELDLRGMRVEEAL 720
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906333145 703 EELRTAILEAHALKESPLRVVHGKGQGVLRRLLRDYLKSDKKVESFHDAEANQGGHGVTIVNIR 766
Cdd:COG1193 721 PELDKYLDDALLAGLPEVRIIHGKGTGALRKGVREYLKRHPYVKSFRLGEPGEGGDGVTVVELK 784
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
6-763 |
0e+00 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 581.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 6 RALSALDFPRVLDALAERSATSLGAERARALRPSDDPERIARELDEVEDALFGVSL----SLGGIHDIRDLHARAAEGRV 81
Cdd:PRK00409 4 KTLRVLEFNKIKEQLKTFAASELGKEKVLQLDPETDFEEVEELLEETDEAAKLLRLkglpPFEGVKDIDDALKRAEKGGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 82 LSGSELLSAAYSLDGAMTVKRAIGVNSRGP----LREVAVGLGDHSELVRRVLSALDRDGAVRDDASPRLRDLRKRIEPL 157
Cdd:PRK00409 84 LSGDELLEIAKTLRYFRQLKRFIEDLEEEEelpiLEEWVAKIRTLPELEQEIHNCIDEEGEVKDSASEKLRGIRRQLRRK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 158 RGRIRERLTATL--EKWSDVLQEHIVTIRRDRYVLPVQASRVGQVQGIIVDASATGQTYFVEPAAVTQLNNELTRLILDE 235
Cdd:PRK00409 164 KSRIREKLESIIrsKSLQKYLQDTIITIRNDRYVLPVKAEYKHAIKGIVHDQSSSGATLYIEPQSVVELNNEIRELRNKE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 236 EAEVRRILTELSGLLAGDADVPMTLVTV-GELDLIASKARLARDWRLNRPEQVEGGRYDLREVRHPLIENP--VANDLSL 312
Cdd:PRK00409 244 EQEIERILKELSAKVAKNLDFLKFLNKIfDELDFIFARARYAKALKATFPLFNDEGKIDLRQARHPLLDGEkvVPKDISL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 313 G-ETKLLLITGPNMGGKTATIKTLGLAVLMHQCGLYVAAAS-ARLPVVRDVLVDIGDEQSIEASLSTFASHLKHLRYVLR 390
Cdd:PRK00409 324 GfDKTVLVITGPNTGGKTVTLKTLGLAALMAKSGLPIPANEpSEIPVFKEIFADIGDEQSIEQSLSTFSGHMTNIVRILE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 391 HAAPDTLVLVDELGSGTDPNEGAALAQALIECLLTQDARGVITSHLSPLKLFALETPGLKNASMGFDVDTLAPTYVLQVG 470
Cdd:PRK00409 404 KADKNSLVLFDELGAGTDPDEGAALAISILEYLRKRGAKIIATTHYKELKALMYNREGVENASVEFDEETLRPTYRLLIG 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 471 QPGRSFALAIAQRMGLPADVLRRAEDLLGPDAGLMERMLEGLEREREDLRAQLEGTAAARRDAEAELGRVRQERETLELR 550
Cdd:PRK00409 484 IPGKSNAFEIAKRLGLPENIIEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEE 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 551 RNEMLAEASQKAESLYADA-------IERVRTLRARAQEDSARPRVMQELRELRVSAQKARPAPIVREERGDPIRVGSRV 623
Cdd:PRK00409 564 EDKLLEEAEKEAQQAIKEAkkeadeiIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEV 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 624 DVPAYNATGQVLELRGD-DLVVQLGVMKVGVKRRDVRLKQEPKVTaPRTRGPRTafagAVAASTFQNELQLRGMGVEEAV 702
Cdd:PRK00409 644 KYLSLGQKGEVLSIPDDkEAIVQAGIMKMKVPLSDLEKIQKPKKK-KKKKPKTV----KPKPRTVSLELDLRGMRYEEAL 718
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906333145 703 EELRTAILEAHALKESPLRVVHGKGQGVLRRLLRDYLKSDKKVESFHDAEANQGGHGVTIV 763
Cdd:PRK00409 719 ERLDKYLDDALLAGYGEVLIIHGKGTGKLRKGVQEFLKKHPSVKSFRDAPPNEGGFGVTIV 779
|
|
| mutS2 |
TIGR01069 |
MutS2 family protein; Function of MutS2 is unknown. It should not be considered a DNA mismatch ... |
8-766 |
3.56e-159 |
|
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: 480.47 E-value: 3.56e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 8 LSALDFPRVLDALAERSATSLGAERARALRPSDDPERIARELDEvEDALFGVSLS--LGGIHDIRDLHARAAEGRVLSGS 85
Cdd:TIGR01069 6 LIKLEFDKVKENLLKQTFTPLGKEDAIGLKPPKSVEESKEIIIK-LTALGSIENNvrFFGFEDIRELLKRAELGGIVKGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 86 E-LLSAAYSLDGAMTVKRAIGVNSR-GPLREVAVGLGDHSELVRRVLSALDRDGAVRDDASPRLRDLRKRIEPLRGRIRE 163
Cdd:TIGR01069 85 EyILVIQNALKTVKHLKVLSEHVLDlEILFHLRLNLITLPPLENDIIACIDDDGKVKDGASEELDAIRESLKALEEEVVK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 164 RL--TATLEKWSDVLQEHIVTIRRDRYVLPVQASRVGQVQGIIVDASATGQTYFVEPAAVTQLNNELTRLILDEEAEVRR 241
Cdd:TIGR01069 165 RLhkIIRSKELAKYLSDTIVTIRNGRYVLPLKSGFKGKIKGIVHDTSSSGETFYIEPQAIVKLNNKLAQLKNEEECEIEK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 242 ILTELSGLLAGDA-DVPMTLVTVGELDLIASKARLARDWRLNRPEQVEGGRYDLREVRHPLIENP--VANDLSLG-ETKL 317
Cdd:TIGR01069 245 ILRTLSEKVQEYLlELKFLFKEFDFLDSLQARARYAKAVKGEFPMPSFTGKIILENARHPLLKEPkvVPFTLNLKfEKRV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 318 LLITGPNMGGKTATIKTLGLAVLMHQCGLYV-AAASARLPVVRDVLVDIGDEQSIEASLSTFASHLKHLRYVLRHAAPDT 396
Cdd:TIGR01069 325 LAITGPNTGGKTVTLKTLGLLALMFQSGIPIpANEHSEIPYFEEIFADIGDEQSIEQNLSTFSGHMKNISAILSKTTENS 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 397 LVLVDELGSGTDPNEGAALAQALIECLLTQDARGVITSHLSPLKLFALETPGLKNASMGFDVDTLAPTYVLQVGQPGRSF 476
Cdd:TIGR01069 405 LVLFDELGAGTDPDEGSALAISILEYLLKQNAQVLITTHYKELKALMYNNEGVENASVLFDEETLSPTYKLLKGIPGESY 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 477 ALAIAQRMGLPADVLRRAEDLLGPDAGLMERMLEGLEREREDLRAQLEGTAAARRDAEAELGRVRQERETLELRRNEMLA 556
Cdd:TIGR01069 485 AFEIAQRYGIPHFIIEQAKTFYGEFKEEINVLIEKLSALEKELEQKNEHLEKLLKEQEKLKKELEQEMEELKERERNKKL 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 557 EASQ-------KAESLYADAIERVRTLRARAQEDSARPRVMQELRElrvsaQKARPAPIVREERGDpiRVGSRVDVPAYN 629
Cdd:TIGR01069 565 ELEKeaqealkALKKEVESIIRELKEKKIHKAKEIKSIEDLVKLKE-----TKQKIPQKPTNFQAD--KIGDKVRIRYFG 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 630 ATGQVLE-LRGDDLVVQLGVMKVGVKRRDVRL---KQEPKVTAPRTRGPrtafagaVAASTFQNELQLRGMGVEEAVEEL 705
Cdd:TIGR01069 638 QKGKIVQiLGGNKWNVTVGGMRMKVHGSELEKinkAPPPKKFKVPKTTK-------PEPKEASLTLDLRGQRSEEALDRL 710
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906333145 706 RTAILEAHALKESPLRVVHGKGQGVLRRLLRDYLKSDKKVESFHDAEANQGGHGVTIVNIR 766
Cdd:TIGR01069 711 EKFLNDALLAGYEVVLIIHGKGSGKLRKGVQELLKNHPKVKSFRDAPPNDGGSGVTIVYLE 771
|
|
| ABC_MutS2 |
cd03280 |
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ... |
293-486 |
2.60e-103 |
|
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: 315.73 E-value: 2.60e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 293 DLREVRHPLI----ENPVANDLSLGETK-LLLITGPNMGGKTATIKTLGLAVLMHQCGLYV-AAASARLPVVRDVLVDIG 366
Cdd:cd03280 1 RLREARHPLLplqgEKVVPLDIQLGENKrVLVITGPNAGGKTVTLKTLGLLTLMAQSGLPIpAAEGSSLPVFENIFADIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 367 DEQSIEASLSTFASHLKHLRYVLRHAAPDTLVLVDELGSGTDPNEGAALAQALIECLLTQDARGVITSHLSPLKLFALET 446
Cdd:cd03280 81 DEQSIEQSLSTFSSHMKNIARILQHADPDSLVLLDELGSGTDPVEGAALAIAILEELLERGALVIATTHYGELKAYAYKR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1906333145 447 PGLKNASMGFDVDTLAPTYVLQVGQPGRSFALAIAQRMGL 486
Cdd:cd03280 161 EGVENASMEFDPETLKPTYRLLIGVPGRSNALEIARRLGL 200
|
|
| MUTSac |
smart00534 |
ATPase domain of DNA mismatch repair MUTS family; |
317-498 |
5.38e-62 |
|
ATPase domain of DNA mismatch repair MUTS family;
Pssm-ID: 197777 [Multi-domain] Cd Length: 185 Bit Score: 206.25 E-value: 5.38e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 317 LLLITGPNMGGKTATIKTLGLAVLMHQCGLYVAAASARLPVVRDVLVDIGDEQSIEASLSTFASHLKHLRYVLRHAAPDT 396
Cdd:smart00534 1 VVIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPVFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATKNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 397 LVLVDELGSGTDPNEGAALAQALIECLLTQD-ARGVITSHLSPLKLFALETPGLKNASMGFDVDT--LAPTYVLQVGQPG 473
Cdd:smart00534 81 LVLLDELGRGTSTYDGLAIAAAILEYLLEKIgARTLFATHYHELTKLADNHPGVRNLHMSALEETenITFLYKLKPGVAG 160
|
170 180
....*....|....*....|....*
gi 1906333145 474 RSFALAIAQRMGLPADVLRRAEDLL 498
Cdd:smart00534 161 KSYGIEVAKLAGLPKEVIERAKRIL 185
|
|
| MutS_V |
pfam00488 |
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
318-498 |
4.26e-34 |
|
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: 128.85 E-value: 4.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 318 LLITGPNMGGKTATIKTLGLAVLMHQCGLYVAAASARLPVVRDVLVDIGDEQSIEASLSTFASHLKHLRYVLRHAAPDTL 397
Cdd:pfam00488 1 LIITGPNMGGKSTYLRQVALIVLMAQIGSFVPAESAEIGIVDRIFTRIGASDDLAKGRSTFMVEMLETANILHNATDKSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 398 VLVDELGSGTDPNEGAALAQALIECLLTQ-DARGVITSHLSPLKLFALETPGLKNASMgfDV----DTLAPTYVLQVGQP 472
Cdd:pfam00488 81 VILDELGRGTSTYDGLAIAWAVAEHLAEKiKARTLFATHYHELTKLAEKLPAVKNLHM--AAveddDDIVFLYKVQPGAA 158
|
170 180
....*....|....*....|....*.
gi 1906333145 473 GRSFALAIAQRMGLPADVLRRAEDLL 498
Cdd:pfam00488 159 DKSYGIHVAELAGLPESVVERAREIL 184
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
4-766 |
0e+00 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 825.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 4 DARALSALDFPRVLDALAERSATSLGAERARALRPSDDPERIARELDEVEDAL----FGVSLSLGGIHDIRDLHARAAEG 79
Cdd:COG1193 2 NEKTLEKLEFDKILELLAEYAVSELGKELARKLRPSTDLEEVERLLAETAEARrllrLEGGLPLGGIPDIRPLLKRAEEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 80 RVLSGSELLSAAYSLDGAMTVKRAIGVNSRG--PLREVAVGLGDHSELVRRVLSALDRDGAVRDDASPRLRDLRKRIEPL 157
Cdd:COG1193 82 GVLSPEELLDIARTLRAARRLKRFLEELEEEypALKELAERLPPLPELEKEIDRAIDEDGEVKDSASPELRRIRREIRSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 158 RGRIRERLTATL--EKWSDVLQEHIVTIRRDRYVLPVQASRVGQVQGIIVDASATGQTYFVEPAAVTQLNNELTRLILDE 235
Cdd:COG1193 162 EQRIREKLESILrsASYQKYLQDAIITIRNGRYVIPVKAEYKGKIPGIVHDQSASGQTLFIEPMAVVELNNELRELEAEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 236 EAEVRRILTELSGLLAGDAD-VPMTLVTVGELDLIASKARLARDWRLNRPEQVEGGRYDLREVRHPLI--ENPVANDLSL 312
Cdd:COG1193 242 RREIERILRELSALVREYAEeLLENLEILAELDFIFAKARYALELKAVKPELNDEGYIKLKKARHPLLdlKKVVPIDIEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 313 GET-KLLLITGPNMGGKTATIKTLGLAVLMHQCGLYV-AAASARLPVVRDVLVDIGDEQSIEASLSTFASHLKHLRYVLR 390
Cdd:COG1193 322 GEDfRTLVITGPNTGGKTVTLKTVGLLTLMAQSGLPIpAAEGSELPVFDNIFADIGDEQSIEQSLSTFSSHMTNIVEILE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 391 HAAPDTLVLVDELGSGTDPNEGAALAQALIECLLTQDARGVITSHLSPLKLFALETPGLKNASMGFDVDTLAPTYVLQVG 470
Cdd:COG1193 402 KADENSLVLLDELGAGTDPQEGAALAIAILEELLERGARVVATTHYSELKAYAYNTEGVENASVEFDVETLSPTYRLLIG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 471 QPGRSFALAIAQRMGLPADVLRRAEDLLGPDAGLMERMLEGLEREREDLRAQLEGTAAARRDAEAELGRVRQERETLELR 550
Cdd:COG1193 482 VPGRSNAFEIARRLGLPEEIIERARELLGEESIDVEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEE 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 551 RNEMLAEASQKAESLYADAIERVRTLRARAQEDSARPRVMQELR-ELRVSAQKARP------APIVREERGDPIRVGSRV 623
Cdd:COG1193 562 KEEILEKAREEAEEILREARKEAEELIRELREAQAEEEELKEARkKLEELKQELEEklekpkKKAKPAKPPEELKVGDRV 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 624 DVPAYNATGQVLEL-RGDDLVVQLGVMKVGVKRRDVRLKQEPKVTAPRTRGPRTAFAGAVaASTFQNELQLRGMGVEEAV 702
Cdd:COG1193 642 RVLSLGQKGEVLEIpKGGEAEVQVGILKMTVKLSDLEKVEKKKPKKPKKRPAGVSVSVSK-ASTVSPELDLRGMRVEEAL 720
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906333145 703 EELRTAILEAHALKESPLRVVHGKGQGVLRRLLRDYLKSDKKVESFHDAEANQGGHGVTIVNIR 766
Cdd:COG1193 721 PELDKYLDDALLAGLPEVRIIHGKGTGALRKGVREYLKRHPYVKSFRLGEPGEGGDGVTVVELK 784
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
6-763 |
0e+00 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 581.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 6 RALSALDFPRVLDALAERSATSLGAERARALRPSDDPERIARELDEVEDALFGVSL----SLGGIHDIRDLHARAAEGRV 81
Cdd:PRK00409 4 KTLRVLEFNKIKEQLKTFAASELGKEKVLQLDPETDFEEVEELLEETDEAAKLLRLkglpPFEGVKDIDDALKRAEKGGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 82 LSGSELLSAAYSLDGAMTVKRAIGVNSRGP----LREVAVGLGDHSELVRRVLSALDRDGAVRDDASPRLRDLRKRIEPL 157
Cdd:PRK00409 84 LSGDELLEIAKTLRYFRQLKRFIEDLEEEEelpiLEEWVAKIRTLPELEQEIHNCIDEEGEVKDSASEKLRGIRRQLRRK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 158 RGRIRERLTATL--EKWSDVLQEHIVTIRRDRYVLPVQASRVGQVQGIIVDASATGQTYFVEPAAVTQLNNELTRLILDE 235
Cdd:PRK00409 164 KSRIREKLESIIrsKSLQKYLQDTIITIRNDRYVLPVKAEYKHAIKGIVHDQSSSGATLYIEPQSVVELNNEIRELRNKE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 236 EAEVRRILTELSGLLAGDADVPMTLVTV-GELDLIASKARLARDWRLNRPEQVEGGRYDLREVRHPLIENP--VANDLSL 312
Cdd:PRK00409 244 EQEIERILKELSAKVAKNLDFLKFLNKIfDELDFIFARARYAKALKATFPLFNDEGKIDLRQARHPLLDGEkvVPKDISL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 313 G-ETKLLLITGPNMGGKTATIKTLGLAVLMHQCGLYVAAAS-ARLPVVRDVLVDIGDEQSIEASLSTFASHLKHLRYVLR 390
Cdd:PRK00409 324 GfDKTVLVITGPNTGGKTVTLKTLGLAALMAKSGLPIPANEpSEIPVFKEIFADIGDEQSIEQSLSTFSGHMTNIVRILE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 391 HAAPDTLVLVDELGSGTDPNEGAALAQALIECLLTQDARGVITSHLSPLKLFALETPGLKNASMGFDVDTLAPTYVLQVG 470
Cdd:PRK00409 404 KADKNSLVLFDELGAGTDPDEGAALAISILEYLRKRGAKIIATTHYKELKALMYNREGVENASVEFDEETLRPTYRLLIG 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 471 QPGRSFALAIAQRMGLPADVLRRAEDLLGPDAGLMERMLEGLEREREDLRAQLEGTAAARRDAEAELGRVRQERETLELR 550
Cdd:PRK00409 484 IPGKSNAFEIAKRLGLPENIIEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEE 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 551 RNEMLAEASQKAESLYADA-------IERVRTLRARAQEDSARPRVMQELRELRVSAQKARPAPIVREERGDPIRVGSRV 623
Cdd:PRK00409 564 EDKLLEEAEKEAQQAIKEAkkeadeiIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEV 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 624 DVPAYNATGQVLELRGD-DLVVQLGVMKVGVKRRDVRLKQEPKVTaPRTRGPRTafagAVAASTFQNELQLRGMGVEEAV 702
Cdd:PRK00409 644 KYLSLGQKGEVLSIPDDkEAIVQAGIMKMKVPLSDLEKIQKPKKK-KKKKPKTV----KPKPRTVSLELDLRGMRYEEAL 718
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906333145 703 EELRTAILEAHALKESPLRVVHGKGQGVLRRLLRDYLKSDKKVESFHDAEANQGGHGVTIV 763
Cdd:PRK00409 719 ERLDKYLDDALLAGYGEVLIIHGKGTGKLRKGVQEFLKKHPSVKSFRDAPPNEGGFGVTIV 779
|
|
| mutS2 |
TIGR01069 |
MutS2 family protein; Function of MutS2 is unknown. It should not be considered a DNA mismatch ... |
8-766 |
3.56e-159 |
|
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: 480.47 E-value: 3.56e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 8 LSALDFPRVLDALAERSATSLGAERARALRPSDDPERIARELDEvEDALFGVSLS--LGGIHDIRDLHARAAEGRVLSGS 85
Cdd:TIGR01069 6 LIKLEFDKVKENLLKQTFTPLGKEDAIGLKPPKSVEESKEIIIK-LTALGSIENNvrFFGFEDIRELLKRAELGGIVKGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 86 E-LLSAAYSLDGAMTVKRAIGVNSR-GPLREVAVGLGDHSELVRRVLSALDRDGAVRDDASPRLRDLRKRIEPLRGRIRE 163
Cdd:TIGR01069 85 EyILVIQNALKTVKHLKVLSEHVLDlEILFHLRLNLITLPPLENDIIACIDDDGKVKDGASEELDAIRESLKALEEEVVK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 164 RL--TATLEKWSDVLQEHIVTIRRDRYVLPVQASRVGQVQGIIVDASATGQTYFVEPAAVTQLNNELTRLILDEEAEVRR 241
Cdd:TIGR01069 165 RLhkIIRSKELAKYLSDTIVTIRNGRYVLPLKSGFKGKIKGIVHDTSSSGETFYIEPQAIVKLNNKLAQLKNEEECEIEK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 242 ILTELSGLLAGDA-DVPMTLVTVGELDLIASKARLARDWRLNRPEQVEGGRYDLREVRHPLIENP--VANDLSLG-ETKL 317
Cdd:TIGR01069 245 ILRTLSEKVQEYLlELKFLFKEFDFLDSLQARARYAKAVKGEFPMPSFTGKIILENARHPLLKEPkvVPFTLNLKfEKRV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 318 LLITGPNMGGKTATIKTLGLAVLMHQCGLYV-AAASARLPVVRDVLVDIGDEQSIEASLSTFASHLKHLRYVLRHAAPDT 396
Cdd:TIGR01069 325 LAITGPNTGGKTVTLKTLGLLALMFQSGIPIpANEHSEIPYFEEIFADIGDEQSIEQNLSTFSGHMKNISAILSKTTENS 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 397 LVLVDELGSGTDPNEGAALAQALIECLLTQDARGVITSHLSPLKLFALETPGLKNASMGFDVDTLAPTYVLQVGQPGRSF 476
Cdd:TIGR01069 405 LVLFDELGAGTDPDEGSALAISILEYLLKQNAQVLITTHYKELKALMYNNEGVENASVLFDEETLSPTYKLLKGIPGESY 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 477 ALAIAQRMGLPADVLRRAEDLLGPDAGLMERMLEGLEREREDLRAQLEGTAAARRDAEAELGRVRQERETLELRRNEMLA 556
Cdd:TIGR01069 485 AFEIAQRYGIPHFIIEQAKTFYGEFKEEINVLIEKLSALEKELEQKNEHLEKLLKEQEKLKKELEQEMEELKERERNKKL 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 557 EASQ-------KAESLYADAIERVRTLRARAQEDSARPRVMQELRElrvsaQKARPAPIVREERGDpiRVGSRVDVPAYN 629
Cdd:TIGR01069 565 ELEKeaqealkALKKEVESIIRELKEKKIHKAKEIKSIEDLVKLKE-----TKQKIPQKPTNFQAD--KIGDKVRIRYFG 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 630 ATGQVLE-LRGDDLVVQLGVMKVGVKRRDVRL---KQEPKVTAPRTRGPrtafagaVAASTFQNELQLRGMGVEEAVEEL 705
Cdd:TIGR01069 638 QKGKIVQiLGGNKWNVTVGGMRMKVHGSELEKinkAPPPKKFKVPKTTK-------PEPKEASLTLDLRGQRSEEALDRL 710
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906333145 706 RTAILEAHALKESPLRVVHGKGQGVLRRLLRDYLKSDKKVESFHDAEANQGGHGVTIVNIR 766
Cdd:TIGR01069 711 EKFLNDALLAGYEVVLIIHGKGSGKLRKGVQELLKNHPKVKSFRDAPPNDGGSGVTIVYLE 771
|
|
| ABC_MutS2 |
cd03280 |
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ... |
293-486 |
2.60e-103 |
|
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: 315.73 E-value: 2.60e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 293 DLREVRHPLI----ENPVANDLSLGETK-LLLITGPNMGGKTATIKTLGLAVLMHQCGLYV-AAASARLPVVRDVLVDIG 366
Cdd:cd03280 1 RLREARHPLLplqgEKVVPLDIQLGENKrVLVITGPNAGGKTVTLKTLGLLTLMAQSGLPIpAAEGSSLPVFENIFADIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 367 DEQSIEASLSTFASHLKHLRYVLRHAAPDTLVLVDELGSGTDPNEGAALAQALIECLLTQDARGVITSHLSPLKLFALET 446
Cdd:cd03280 81 DEQSIEQSLSTFSSHMKNIARILQHADPDSLVLLDELGSGTDPVEGAALAIAILEELLERGALVIATTHYGELKAYAYKR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1906333145 447 PGLKNASMGFDVDTLAPTYVLQVGQPGRSFALAIAQRMGL 486
Cdd:cd03280 161 EGVENASMEFDPETLKPTYRLLIGVPGRSNALEIARRLGL 200
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
293-486 |
1.58e-69 |
|
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: 226.75 E-value: 1.58e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 293 DLREVRHPLI------ENPVANDLSLGETKLLLITGPNMGGKTATIKTLGLAVLMHQCGLYVAAASARLPVVRDVLVDIG 366
Cdd:cd03243 1 EIKGGRHPVLlaltkgETFVPNDINLGSGRLLLITGPNMGGKSTYLRSIGLAVLLAQIGCFVPAESASIPLVDRIFTRIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 367 DEQSIEASLSTFASHLKHLRYVLRHAAPDTLVLVDELGSGTDPNEGAALAQALIECLLTQDARGVITSHLSPLKLFALET 446
Cdd:cd03243 81 AEDSISDGRSTFMAELLELKEILSLATPRSLVLIDELGRGTSTAEGLAIAYAVLEHLLEKGCRTLFATHFHELADLPEQV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1906333145 447 PGLKNASMGFDV--DTLAPTYVLQVGQPGRSFALAIAQRMGL 486
Cdd:cd03243 161 PGVKNLHMEELIttGGLTFTYKLIDGICDPSYALQIAELAGL 202
|
|
| MUTSac |
smart00534 |
ATPase domain of DNA mismatch repair MUTS family; |
317-498 |
5.38e-62 |
|
ATPase domain of DNA mismatch repair MUTS family;
Pssm-ID: 197777 [Multi-domain] Cd Length: 185 Bit Score: 206.25 E-value: 5.38e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 317 LLLITGPNMGGKTATIKTLGLAVLMHQCGLYVAAASARLPVVRDVLVDIGDEQSIEASLSTFASHLKHLRYVLRHAAPDT 396
Cdd:smart00534 1 VVIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPVFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATKNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 397 LVLVDELGSGTDPNEGAALAQALIECLLTQD-ARGVITSHLSPLKLFALETPGLKNASMGFDVDT--LAPTYVLQVGQPG 473
Cdd:smart00534 81 LVLLDELGRGTSTYDGLAIAAAILEYLLEKIgARTLFATHYHELTKLADNHPGVRNLHMSALEETenITFLYKLKPGVAG 160
|
170 180
....*....|....*....|....*
gi 1906333145 474 RSFALAIAQRMGLPADVLRRAEDLL 498
Cdd:smart00534 161 KSYGIEVAKLAGLPKEVIERAKRIL 185
|
|
| ABC_MSH2_euk |
cd03285 |
ATP-binding cassette domain of eukaryotic MutS2 homolog; The MutS protein initiates DNA ... |
294-494 |
4.57e-37 |
|
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: 138.66 E-value: 4.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 294 LREVRHPLIE-----NPVANDLSL--GETKLLLITGPNMGGKTATIKTLGLAVLMHQCGLYVAAASARLPVVRDVLVDIG 366
Cdd:cd03285 2 LKEARHPCVEaqddvAFIPNDVTLtrGKSRFLIITGPNMGGKSTYIRQIGVIVLMAQIGCFVPCDSADIPIVDCILARVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 367 DEQSIEASLSTFASHLKHLRYVLRHAAPDTLVLVDELGSGTDPNEGAALAQALIECLLTQ-DARGVITSHLSPLKLFALE 445
Cdd:cd03285 82 ASDSQLKGVSTFMAEMLETAAILKSATENSLIIIDELGRGTSTYDGFGLAWAIAEYIATQiKCFCLFATHFHELTALADE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1906333145 446 TPGLKNASMGFDVDTLAPT----YVLQVGQPGRSFALAIAQRMGLPADVLRRA 494
Cdd:cd03285 162 VPNVKNLHVTALTDDASRTltmlYKVEKGACDQSFGIHVAELANFPKEVIEMA 214
|
|
| ABC_MSH6_euk |
cd03286 |
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA ... |
294-494 |
2.34e-36 |
|
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: 136.40 E-value: 2.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 294 LREVRHPLI-----ENPVANDLSLGET--KLLLITGPNMGGKTATIKTLGLAVLMHQCGLYVAAASARLPVVRDVLVDIG 366
Cdd:cd03286 2 FEELRHPCLnastaSSFVPNDVDLGATspRILVLTGPNMGGKSTLLRTVCLAVIMAQMGMDVPAKSMRLSLVDRIFTRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 367 DEQSIEASLSTFASHLKHLRYVLRHAAPDTLVLVDELGSGTDPNEGAALAQALIECLLTQDA-RGVITSHLSPLKLFALE 445
Cdd:cd03286 82 ARDDIMKGESTFMVELSETANILRHATPDSLVILDELGRGTSTHDGYAIAHAVLEYLVKKVKcLTLFSTHYHSLCDEFHE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1906333145 446 TPGLKNASMGFDVD--------TLAPTYVLQVGQPGRSFALAIAQRMGLPADVLRRA 494
Cdd:cd03286 162 HGGVRLGHMACAVKnesdptirDITFLYKLVAGICPKSYGLYVALMAGIPDGVVERA 218
|
|
| ABC_MutS1 |
cd03284 |
ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair ... |
293-498 |
2.24e-34 |
|
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: 130.46 E-value: 2.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 293 DLREVRHPLIE------NPVANDLSLG-ETKLLLITGPNMGGKTATIKTLGLAVLMHQCGLYVAAASARLPVVRDVLVDI 365
Cdd:cd03284 1 EIEGGRHPVVEqvldnePFVPNDTELDpERQILLITGPNMAGKSTYLRQVALIALLAQIGSFVPASKAEIGVVDRIFTRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 366 GDEQSIEASLSTFASHLKHLRYVLRHAAPDTLVLVDELGSGTDPNEGAALAQALIECLLTQD-ARGVITSHLSPLKLFAL 444
Cdd:cd03284 81 GASDDLAGGRSTFMVEMVETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAIVEYLHEKIgAKTLFATHYHELTELEG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1906333145 445 ETPGLKNASMGF--DVDTLAPTYVLQVGQPGRSFALAIAQRMGLPADVLRRAEDLL 498
Cdd:cd03284 161 KLPRVKNFHVAVkeKGGGVVFLHKIVEGAADKSYGIEVARLAGLPEEVIERAREIL 216
|
|
| ABC_MSH3_euk |
cd03287 |
ATP-binding cassette domain of eukaryotic MutS3 homolog; The MutS protein initiates DNA ... |
294-494 |
2.85e-34 |
|
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: 130.69 E-value: 2.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 294 LREVRHPLIE-----NPVAND--LSLGETKLLLITGPNMGGKTATIKTLGLAVLMHQCGLYVAAASARLPVVRDVLVDIG 366
Cdd:cd03287 3 IKEGRHPMIEslldkSFVPNDihLSAEGGYCQIITGPNMGGKSSYIRQVALITIMAQIGSFVPASSATLSIFDSVLTRMG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 367 DEQSIEASLSTFASHLKHLRYVLRHAAPDTLVLVDELGSGTDPNEGAALAQALIECLLTQDARGVI-TSHLSPLKLFALE 445
Cdd:cd03287 83 ASDSIQHGMSTFMVELSETSHILSNCTSRSLVILDELGRGTSTHDGIAIAYATLHYLLEEKKCLVLfVTHYPSLGEILRR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 446 TPG-LKNASMGF----------DVDTLAPTYVLQVGQPGRSFALAIAQRMGLPADVLRRA 494
Cdd:cd03287 163 FEGsIRNYHMSYlesqkdfetsDSQSITFLYKLVRGLASRSFGLNVARLAGLPKSIISRA 222
|
|
| MutS_V |
pfam00488 |
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
318-498 |
4.26e-34 |
|
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: 128.85 E-value: 4.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 318 LLITGPNMGGKTATIKTLGLAVLMHQCGLYVAAASARLPVVRDVLVDIGDEQSIEASLSTFASHLKHLRYVLRHAAPDTL 397
Cdd:pfam00488 1 LIITGPNMGGKSTYLRQVALIVLMAQIGSFVPAESAEIGIVDRIFTRIGASDDLAKGRSTFMVEMLETANILHNATDKSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 398 VLVDELGSGTDPNEGAALAQALIECLLTQ-DARGVITSHLSPLKLFALETPGLKNASMgfDV----DTLAPTYVLQVGQP 472
Cdd:pfam00488 81 VILDELGRGTSTYDGLAIAWAVAEHLAEKiKARTLFATHYHELTKLAEKLPAVKNLHM--AAveddDDIVFLYKVQPGAA 158
|
170 180
....*....|....*....|....*.
gi 1906333145 473 GRSFALAIAQRMGLPADVLRRAEDLL 498
Cdd:pfam00488 159 DKSYGIHVAELAGLPESVVERAREIL 184
|
|
| mutS1 |
TIGR01070 |
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair] |
31-498 |
2.21e-33 |
|
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273427 [Multi-domain] Cd Length: 840 Bit Score: 137.98 E-value: 2.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 31 ERARALRPSDDPERIARELDEVEDalfgVSLSLGGIHDIRDLHARAAEGRVlSGSELLSAAYSLDGAMTVKRAIGVNSRG 110
Cdd:TIGR01070 299 DREVLEARQDTVEVLLRHFFLREG----LRPLLKEVGDLERLAARVALGNA-RPRDLARLRTSLEQLPELRALLEELEGP 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 111 PLREVAVGLGDHSELvrrvLSALDRdgAVRDDASPRLRDlrkrieplRGRIRERLTATLEKWSDVLQEHIVTI----RRD 186
Cdd:TIGR01070 374 TLQALAAQIDDFSEL----LELLEA--ALIENPPLVVRD--------GGLIREGYDEELDELRAASREGTDYLarleARE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 187 RYVLPVQASRVG--QVQGIIVDASaTGQTYFVEPAAV---TQLNNEltRLILDEEAEVRRILTELSGL-LAGDADVPMTL 260
Cdd:TIGR01070 440 RERTGIPTLKVGynAVFGYYIEVT-RGQLHLVPAHYRrrqTLKNAE--RYITPELKEKEDKVLEAEGKiLALEKELFEEL 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 261 ---------------VTVGELDLIASKARLARDWRLNRPEQVEGGRYDLREVRHPLIENP-----VANDLSLGE-TKLLL 319
Cdd:TIGR01070 517 rellkkylealqeaaRALAELDVLANLAEVAETLHYTRPRFGDDPQLRIREGRHPVVEQVlrtpfVPNDLEMAHnRRMLL 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 320 ITGPNMGGKTATIKTLGLAVLMHQCGLYVAAASARLPVVRDVLVDIGDEQSIEASLSTFASHLKHLRYVLRHAAPDTLVL 399
Cdd:TIGR01070 597 ITGPNMGGKSTYMRQTALIALLAQIGSFVPAESAELPLFDRIFTRIGASDDLASGRSTFMVEMTEAANILHNATENSLVL 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 400 VDELGSGTDPNEGAALAQALIECLltQDARGVIT---SHLSPLKLFALETPGLKN---ASMGFDvDTLAPTYVLQVGQPG 473
Cdd:TIGR01070 677 FDEIGRGTSTYDGLALAWAIAEYL--HEHIRAKTlfaTHYFELTALEESLPGLKNvhvAALEHN-GTIVFLHQVLPGPAS 753
|
490 500
....*....|....*....|....*
gi 1906333145 474 RSFALAIAQRMGLPADVLRRAEDLL 498
Cdd:TIGR01070 754 KSYGLAVAALAGLPKEVIARARQIL 778
|
|
| PRK05399 |
PRK05399 |
DNA mismatch repair protein MutS; Provisional |
16-498 |
4.41e-33 |
|
DNA mismatch repair protein MutS; Provisional
Pssm-ID: 235444 [Multi-domain] Cd Length: 854 Bit Score: 136.76 E-value: 4.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 16 VLDalaeRSATSLGAE--RARALRPSDDPERIARELDEVEDALFGVSL------SLGGIHDIRDLHARAAEGRVlSGSEL 87
Cdd:PRK05399 290 VLD----RTVTAMGGRllRRWLHRPLRDREAIEARLDAVEELLEDPLLredlreLLKGVYDLERLLSRIALGRA-NPRDL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 88 LSAAYSLDGAMTVKRAIGVNSRGPLREVAVGLGDHSELVRRVLSALD-------RDGAV-RDDASP---RLRDL----RK 152
Cdd:PRK05399 365 AALRDSLEALPELKELLAELDSPLLAELAEQLDPLEELADLLERAIVeepplliRDGGViADGYDAeldELRALsdngKD 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 153 RIEPLRGRIRERlT--ATLekwsdvlqehivtirrdryvlpvqasRVG--QVQGiivdasatgqtYFVEpaaVTQ----- 223
Cdd:PRK05399 445 WLAELEARERER-TgiSSL--------------------------KVGynKVFG-----------YYIE---VTKanldk 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 224 ----------LNN----------ELTRLILdeEAEVRR------ILTELSGLLAGDAD-VPMTLVTVGELDLIASKARLA 276
Cdd:PRK05399 484 vpedyirrqtLKNaeryitpelkELEDKIL--SAEEKAlaleyeLFEELREEVAEHIErLQKLAKALAELDVLASLAEVA 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 277 RDWRLNRPEQVEGGRYDLREVRHPLIENP------VANDLSLGE-TKLLLITGPNMGGKTATIKTLGLAVLMHQCGLYVA 349
Cdd:PRK05399 562 EENNYVRPEFTDDPGIDIEEGRHPVVEQVlggepfVPNDCDLDEeRRLLLITGPNMAGKSTYMRQVALIVLLAQIGSFVP 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 350 AASARLPVV-----RdvlvdIGdeqsieAS------LSTF------ASHlkhlryVLRHAAPDTLVLVDELGSGTDPNEG 412
Cdd:PRK05399 642 AESARIGIVdriftR-----IG------ASddlasgRSTFmvemteTAN------ILNNATERSLVLLDEIGRGTSTYDG 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 413 AALAQALIECLLTqdargvitsHLSPLKLFA--------LET--PGLKNASMGfdvdtlaptyVLQVG---------QPG 473
Cdd:PRK05399 705 LSIAWAVAEYLHD---------KIGAKTLFAthyhelteLEEklPGVKNVHVA----------VKEHGgdivflhkvVPG 765
|
570 580
....*....|....*....|....*...
gi 1906333145 474 ---RSFALAIAQRMGLPADVLRRAEDLL 498
Cdd:PRK05399 766 aadKSYGIHVAKLAGLPASVIKRAREIL 793
|
|
| ABC_MSH5_euk |
cd03281 |
ATP-binding cassette domain of eukaryotic MutS5 homolog; The MutS protein initiates DNA ... |
293-486 |
3.62e-31 |
|
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: 121.25 E-value: 3.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 293 DLREVRHPLIE----NPVANDLSLGET--KLLLITGPNMGGKTATIKTLGLAVLMHQCGLYVAAASARLPVVRDVLVDIG 366
Cdd:cd03281 1 EIQGGRHPLLElfvdSFVPNDTEIGGGgpSIMVITGPNSSGKSVYLKQVALIVFLAHIGSFVPADSATIGLVDKIFTRMS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 367 DEQSIEASLSTFASHLKHLRYVLRHAAPDTLVLVDELGSGTDPNEGAALAQALIECLLTQDA---RGVITSHLSPL--KL 441
Cdd:cd03281 81 SRESVSSGQSAFMIDLYQVSKALRLATRRSLVLIDEFGKGTDTEDGAGLLIATIEHLLKRGPecpRVIVSTHFHELfnRS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1906333145 442 FALETPGLKNASM--------GFDVDTLAPTYVLQVGQPGRSFALAIAQRMGL 486
Cdd:cd03281 161 LLPERLKIKFLTMevllnptsTSPNEDITYLYRLVPGLADTSFAIHCAKLAGI 213
|
|
| ABC_MSH4_euk |
cd03282 |
ATP-binding cassette domain of eukaryotic MutS4 homolog; The MutS protein initiates DNA ... |
293-435 |
2.15e-30 |
|
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: 118.65 E-value: 2.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 293 DLREVRHPLIE----NPVANDLSL--GETKLLLITGPNMGGKTATIKTLGLAVLMHQCGLYVAAASARLPVVRDVLVDIG 366
Cdd:cd03282 1 IIRDSRHPILDrdkkNFIPNDIYLtrGSSRFHIITGPNMSGKSTYLKQIALLAIMAQIGCFVPAEYATLPIFNRLLSRLS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906333145 367 DEQSIEASLSTFASHLKHLRYVLRHAAPDTLVLVDELGSGTDPNEGAALAQALIECLLTQDARGVITSH 435
Cdd:cd03282 81 NDDSMERNLSTFASEMSETAYILDYADGDSLVLIDELGRGTSSADGFAISLAILECLIKKESTVFFATH 149
|
|
| MutS |
COG0249 |
DNA mismatch repair ATPase MutS [Replication, recombination and repair]; |
16-498 |
2.53e-30 |
|
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
Pssm-ID: 440019 [Multi-domain] Cd Length: 861 Bit Score: 128.25 E-value: 2.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 16 VLDalaeRSATSLGAeraRALR-----PSDDPERIARELDEVEDALFGVSL------SLGGIHDIrdlhARAAeGRVLSG 84
Cdd:COG0249 296 VLD----RTVTAMGS---RLLRrwllrPLRDRAAIEARLDAVEELLEDPLLreelreLLKGVYDL----ERLL-SRIALG 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 85 S----ELLSAAYSLDGAMTVKRAIGVNSRGPLREVAVGLGDHSELVRRVLSALD-------RDGAV-RDDASPRLRDLRK 152
Cdd:COG0249 364 RanprDLAALRDSLAALPELKELLAELDSPLLAELAEALDPLEDLAELLERAIVdepplliRDGGViREGYDAELDELRE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 153 riepLRGRIRERLtATLEKwsdvlQEhivtirRDRYVLPvqaS-RVG--QVQGiivdasatgqtYFVEpaaVTQLN---- 225
Cdd:COG0249 444 ----LSENGKEWL-AELEA-----RE------RERTGIK---SlKVGynKVFG-----------YYIE---VTKANadkv 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 226 -----------N----------ELTRLIL--DEEAEVR--RILTELSGLLAGDADVPMTLVT-VGELDLIASKARLARDW 279
Cdd:COG0249 491 pddyirkqtlkNaeryitpelkELEDKILsaEERALALeyELFEELREEVAAHIERLQALARaLAELDVLASLAEVAVEN 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 280 RLNRPEQVEGGRYDLREVRHPLIE-----NP-VANDLSLGETK-LLLITGPNMGGKTATIKTLGLAVLMHQCGLYVAAAS 352
Cdd:COG0249 571 NYVRPELDDSPGIEIEGGRHPVVEqalpgEPfVPNDCDLDPDRrILLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAES 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 353 ARLPVV-----RdvlvdIGdeqsieAS------LSTF-------AShlkhlryVLRHAAPDTLVLVDELGSGTDPNEGAA 414
Cdd:COG0249 651 ARIGIVdriftR-----VG------ASddlargQSTFmvemtetAN-------ILNNATERSLVLLDEIGRGTSTYDGLS 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 415 LAQALIECLLTqdargvitsHLSPLKLFA--------LET--PGLKNASMGfdvdtlaptyVLQVG---------QPG-- 473
Cdd:COG0249 713 IAWAVAEYLHD---------KIRARTLFAthyhelteLAEklPGVKNYHVA----------VKEWGgdivflhkvVPGpa 773
|
570 580
....*....|....*....|....*.
gi 1906333145 474 -RSFALAIAQRMGLPADVLRRAEDLL 498
Cdd:COG0249 774 dRSYGIHVAKLAGLPASVIERAREIL 799
|
|
| ABC_MutS-like |
cd03283 |
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ... |
296-436 |
2.61e-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: 115.47 E-value: 2.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 296 EVRHPLI--ENPVANDLSLGETKLLLITGPNMGGKTATIKTLGLAVLMHQCGLYVAAASARLPVVRdVLVDIGDEQSIEA 373
Cdd:cd03283 4 NLGHPLIgrEKRVANDIDMEKKNGILITGSNMSGKSTFLRTIGVNVILAQAGAPVCASSFELPPVK-IFTSIRVSDDLRD 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906333145 374 SLSTFASHLKHLRYVLRHAAPDT--LVLVDELGSGTDPNEGAALAQALIECLLTQDARGVITSHL 436
Cdd:cd03283 83 GISYFYAELRRLKEIVEKAKKGEpvLFLLDEIFKGTNSRERQAASAAVLKFLKNKNTIGIISTHD 147
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
298-450 |
8.12e-26 |
|
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: 104.36 E-value: 8.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 298 RHPLieNPVANDLSLGETKLLLITGPNMGGKTATIKTLGLAVLMH----------QCGLYVAAASARLPVVRDvlvdigd 367
Cdd:cd03227 6 RFPS--YFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAqsatrrrsgvKAGCIVAAVSAELIFTRL------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 368 eqsieaSLSTFASHLKHLRYVLRHAA--PDTLVLVDELGSGTDPNEGAALAQALIEcLLTQDARGVITSHLSPLKLFALE 445
Cdd:cd03227 77 ------QLSGGEKELSALALILALASlkPRPLYILDEIDRGLDPRDGQALAEAILE-HLVKGAQVIVITHLPELAELADK 149
|
....*
gi 1906333145 446 TPGLK 450
Cdd:cd03227 150 LIHIK 154
|
|
| MUTSd |
smart00533 |
DNA-binding domain of DNA mismatch repair MUTS family; |
36-303 |
1.11e-23 |
|
DNA-binding domain of DNA mismatch repair MUTS family;
Pssm-ID: 214710 [Multi-domain] Cd Length: 308 Bit Score: 102.38 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 36 LRPSDDPERIARELDEVEDALFGVSL------SLGGIHDIRDLHARAAEGRVlSGSELLSAAYSLDGAMTVKRAIGVNS- 108
Cdd:smart00533 25 LQPLLDLKEINERLDAVEELVENPELrqklrqLLKRIPDLERLLSRIERGRA-SPRDLLRLYDSLEGLKEIRQLLESLDg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 109 --RGPLREV----AVGLGDH-SELVRRVLSALDRDGA-VRDDASPRLRDLRKRIEPLRGRIRERLtATLEKWSDVLQEHI 180
Cdd:smart00533 104 plLGLLLKVilepLLELLELlLELLNDDDPLEVNDGGlIKDGFDPELDELREKLEELEEELEELL-KKEREELGIDSLKL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 181 VTIRRDRYVLPVQASRVGQVQGIIVDASATGQTYFVEPAAVTQLNNELTRLILDEEAEVRRILTELSGLLAGDADVPMTL 260
Cdd:smart00533 183 GYNKVHGYYIEVTKSEAKKVPKDFIRRSSLKNTERFTTPELKELENELLEAKEEIERLEKEILRELLEKVLEYLEELRAL 262
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1906333145 261 VTV-GELDLIASKARLARDWRLNRPEQVEGGRYDLREVRHPLIE 303
Cdd:smart00533 263 AEAlAELDVLLSLATLAAEGNYVRPEFVDSGELEIKNGRHPVLE 306
|
|
| Smr |
pfam01713 |
Smr domain; This family includes the Smr (Small MutS Related) proteins, and the C-terminal ... |
693-766 |
1.01e-21 |
|
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: 89.45 E-value: 1.01e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906333145 693 LRGMGVEEAVEELRTAILEAHALKESPLRVVHGKG-QGVLRRLLRDYLKSDKKVESFHDAEANQGGHGVTIVNIR 766
Cdd:pfam01713 2 LHGMTVEEAREALDKFLDDALLAGLRCVLIIHGKGtHGVLRKAVREWLKQHPLVLAFRSAPPGEGGDGATYVLLK 76
|
|
| SmrA |
COG2840 |
DNA-nicking endonuclease, Smr domain [Replication, recombination and repair]; |
690-767 |
5.55e-10 |
|
DNA-nicking endonuclease, Smr domain [Replication, recombination and repair];
Pssm-ID: 442088 [Multi-domain] Cd Length: 177 Bit Score: 59.16 E-value: 5.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 690 ELQLRGMGVEEAVEELRTAILEAHALKESPLRVVHGKG------QGVLRRLLRDYLKSDKKVESFHDAEANQGGHGVTIV 763
Cdd:COG2840 91 RLDLHGLTVEEAREALAAFLAEAQRRGLRCVLIIHGKGlgspggRPVLKSQVPRWLRQHPEVLAFHSAPPRHGGSGALYV 170
|
....
gi 1906333145 764 NIRR 767
Cdd:COG2840 171 LLRR 174
|
|
| SMR |
smart00463 |
Small MutS-related domain; |
688-766 |
3.02e-09 |
|
Small MutS-related domain;
Pssm-ID: 214676 [Multi-domain] Cd Length: 80 Bit Score: 54.23 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 688 QNELQLRGMGVEEAVEELRTAILEA-HALKESPLRVVHGKGQGVLRR--LLRDYLKSDKKVESFHDAEanQGGHGVTIVN 764
Cdd:smart00463 1 KWSLDLHGLTVEEALTALDKFLNNArLKGLEQKLVIITGKGKHSLGGksGVKPALKEHLRVESFRFAE--EGNSGVLVVK 78
|
..
gi 1906333145 765 IR 766
Cdd:smart00463 79 LK 80
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
294-435 |
2.92e-07 |
|
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: 50.71 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333145 294 LREVRHPLIENPV--ANDLSLGETKLLLITGPNMGGKTATIKTLGLAvlmhqcgLYVAAASARL---PVVRDVLVDIGDE 368
Cdd:cd00267 2 IENLSFRYGGRTAldNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGL-------LKPTSGEILIdgkDIAKLPLEELRRR 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906333145 369 QSIEASLSTFASHLKHLRYVLRHAAPdtLVLVDELGSGTDPNEGAALAQALIEcLLTQDARGVITSH 435
Cdd:cd00267 75 IGYVPQLSGGQRQRVALARALLLNPD--LLLLDEPTSGLDPASRERLLELLRE-LAEEGRTVIIVTH 138
|
|
| MSSS |
pfam20297 |
MutS2 and Smr-associated SH3 domain; This is a SH3-like domain associated with the MutS-like ... |
619-658 |
6.96e-06 |
|
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: 43.56 E-value: 6.96e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1906333145 619 VGSRVDVPAYNATGQVLELRGDD--LVVQLGVMKVGVKRRDV 658
Cdd:pfam20297 1 VGDEVRVKSLGQKGEVLEVPGKKgeVEVQVGIMKMTVKLSDL 42
|
|
| |
