|
Name |
Accession |
Description |
Interval |
E-value |
| mutL |
PRK00095 |
DNA mismatch repair endonuclease MutL; |
5-653 |
0e+00 |
|
DNA mismatch repair endonuclease MutL;
Pssm-ID: 234630 [Multi-domain] Cd Length: 617 Bit Score: 722.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 5 INILDDLTINKIAAGEVVERPSSVVKELIENSIDAGANKISIDIIDGGKSLIKITDNGMGIPSSEVEKSFLRHATSKIKK 84
Cdd:PRK00095 3 IQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKIAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 85 IDDLYDLYSLGFRGEALASISAVSKLEMTTKTKDEIIGTKIYVEGGKIISKEPIGSTNGTTIIIRDIFFNTPARQKFLKS 164
Cdd:PRK00095 83 LDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADAAEGWQIVYEGGEIVEVKPAAHPVGTTIEVRDLFFNTPARRKFLKS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 165 THAETINISDLINKLAIGNPNIQFKYTNNNKQMLNTPGDGKLVNTIRSIYGKEITENIIDVEFKCNHFKMNGYIGNNNIY 244
Cdd:PRK00095 163 EKTELGHIDDVVNRLALAHPDVAFTLTHNGKLVLQTRGAGQLLQRLAAILGREFAENALPIDAEHGDLRLSGYVGLPTLS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 245 RSNKNLQHIYINKRFVKSKIIIDAITESYKSIIPIGKHAVCFLNIEVDPSCIDVNIHPNKLEIKFEKEQEVyielRDFLk 324
Cdd:PRK00095 243 RANRDYQYLFVNGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLV----HDLI- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 325 VKLIHSNLigkyatysdkKTQPRIAINSREKSTDYKLRNDNLLESTPKNSNTTKSKDevievvtlSSEKPINEFQSVSEV 404
Cdd:PRK00095 318 VQAIQEAL----------AQSGLIPAAAGANQVLEPAEPEPLPLQQTPLYASGSSPP--------ASSPSSAPPEQSEES 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 405 LNASEDEVNNINYLSEDSANDNIQEEFqvdgirnEGNYYLGDSIKDSEEEylcSSKRKFSLyGYsVIGVVFNTYIILSKN 484
Cdd:PRK00095 380 QEESSAEKNPLQPNASQSEAAAAASAE-------AAAAAPAAAPEPAEAA---EEADSFPL-GY-ALGQLHGTYILAENE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 485 DSMYLLDQHAAHERILYERYMEKFYRQDINMQILLDPVIIEVSNVDMLQIENNLELFMKFGFELEIFGNNHIMVRCVPTI 564
Cdd:PRK00095 448 DGLYLVDQHAAHERLLYEQLKDKLAEVGLASQPLLIPLVLELSEDEADRLEEHKELLARLGLELEPFGPNSFAVREVPAL 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 565 FGVPETEKFILQIIDNIEEITSNYDLKG-ERFASMACRSAIKANDKIYDIEIKSLLEQLEKCENPFTCPHGRPIMVEISK 643
Cdd:PRK00095 528 LGQQELEELIRDLLDELAEEGDSDTLKErELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIELSL 607
|
650
....*....|
gi 489519339 644 TEIEKMFKRI 653
Cdd:PRK00095 608 SDLEKLFKRI 617
|
|
| MutL |
COG0323 |
DNA mismatch repair ATPase MutL [Replication, recombination and repair]; |
3-652 |
0e+00 |
|
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
Pssm-ID: 440092 [Multi-domain] Cd Length: 515 Bit Score: 707.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 3 NIINILDDLTINKIAAGEVVERPSSVVKELIENSIDAGANKISIDIIDGGKSLIKITDNGMGIPSSEVEKSFLRHATSKI 82
Cdd:COG0323 2 PKIRLLPDELANQIAAGEVVERPASVVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLPLAFERHATSKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 83 KKIDDLYDLYSLGFRGEALASISAVSKLEMTTKTKDEIIGTKIYVEGGKIISKEPIGSTNGTTIIIRDIFFNTPARQKFL 162
Cdd:COG0323 82 RSAEDLFRIRTLGFRGEALASIASVSRLTLTTRTAGAELGTRIEVEGGKVVEVEPAAAPKGTTVEVRDLFFNTPARRKFL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 163 KSTHAETINISDLINKLAIGNPNIQFKYTNNNKQMLNTPGDGKLVNTIRSIYGKEITENIIDVEFKCNHFKMNGYIGNNN 242
Cdd:COG0323 162 KSDATELAHITDVVRRLALAHPDIAFTLIHNGREVFQLPGAGDLLQRIAAIYGREFAENLLPVEAEREGLRLSGYIGKPE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 243 IYRSNKNLQHIYINKRFVKSKIIIDAITESYKSIIPIGKHAVCFLNIEVDPSCIDVNIHPNKLEIKFEKEQEVYielrDF 322
Cdd:COG0323 242 FSRSNRDYQYFFVNGRPVRDKLLSHAVREAYRDLLPKGRYPVAVLFLELDPELVDVNVHPTKTEVRFRDEREVY----DL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 323 LkvklihsnligkyatysdkktqpriainsrekstdyklrndnllestpknsnttkskdevievvtlssekpineFQSVS 402
Cdd:COG0323 318 V--------------------------------------------------------------------------RSAVR 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 403 EVLNAsedevnninylsedsandniqeefqvdgirnegnyylgdsikdseeeylcsskrkfslygySVIGVVFNTYIILS 482
Cdd:COG0323 324 EALAQ-------------------------------------------------------------AALGQLHGTYILAE 342
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 483 KNDSMYLLDQHAAHERILYERYMEKFYRQDINMQILLDPVIIEVSNVDMLQIENNLELFMKFGFELEIFGNNHIMVRCVP 562
Cdd:COG0323 343 NEDGLVLIDQHAAHERILYERLKKALAEGGVASQPLLIPETLELSPAEAALLEEHLEELARLGFEIEPFGPNTVAVRAVP 422
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 563 TIFGVPETEKFILQIIDNIEE---ITSNYDLKGERFASMACRSAIKANDKIYDIEIKSLLEQLEKCENPFTCPHGRPIMV 639
Cdd:COG0323 423 ALLGEGDAEELLRDLLDELAEegsSESLEELREELLATMACHGAIKAGRRLSLEEMNALLRDLEATENPYTCPHGRPTWI 502
|
650
....*....|...
gi 489519339 640 EISKTEIEKMFKR 652
Cdd:COG0323 503 ELSLEELEKLFKR 515
|
|
| mutl |
TIGR00585 |
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ... |
5-307 |
7.56e-104 |
|
DNA mismatch repair protein MutL; All proteins in this family for which the functions are known are involved in the process of generalized mismatch repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273155 [Multi-domain] Cd Length: 312 Bit Score: 318.05 E-value: 7.56e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 5 INILDDLTINKIAAGEVVERPSSVVKELIENSIDAGANKISIDIIDGGKSLIKITDNGMGIPSSEVEKSFLRHATSKIKK 84
Cdd:TIGR00585 3 IKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKIQS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 85 IDDLYDLYSLGFRGEALASISAVSKLEMTTKT-KDEIIGTKIYVEGGKIISKEPIGSTNGTTIIIRDIFFNTPARQKFLK 163
Cdd:TIGR00585 83 FEDLERIETLGFRGEALASISSVSRLTITTKTsAADGLAYQALLEGGMIESIKPAPRPVGTTVEVRDLFYNLPVRRKFLK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 164 STHAETINISDLINKLAIGNPNIQFKYTNNNKQMLNTPGDGK---LVNTIRSIYGKEITEN-IIDVEFKCNHFKMNGYIG 239
Cdd:TIGR00585 163 SPKKEFRKILDVLQRYALIHPDISFSLTHDGKKVLQLSTKPNqstKENRIRSVFGTAVLRKlIPLDEWEDLDLQLEGFIS 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489519339 240 NNNIYRSNKNL-QHIYINKRFVKSKIIIDAITESYKSIIPIGKHAVCFLNIEVDPSCIDVNIHPNKLEI 307
Cdd:TIGR00585 243 QPNVTRSRRSGwQFLFINGRPVELKLLLKAIREVYHEYLPKGQYPVFVLNLEIDPELVDVNVHPDKKEV 311
|
|
| HATPase_MutL-MLH-PMS-like |
cd16926 |
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ... |
12-198 |
4.31e-98 |
|
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, human MutL homologs (MLH/ PMS), and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of Escherichia coli MutL, human MLH1 (mutL homolog 1), human PMS1 (PMS1 homolog 1, mismatch repair system component), human MLH3 (mutL homolog 3), and human PMS2 (PMS1 homolog 2, mismatch repair system component). MutL homologs (MLH/PMS) participate in MMR (DNA mismatch repair), and in addition have role(s) in DNA damage signaling and suppression of homologous recombination (recombination between partially homologous parental DNAs). The primary role of MutL in MMR is to mediate protein-protein interactions during mismatch recognition and strand removal; a ternary complex is formed between MutS, MutL, and the mismatched DNA, which activates the MutH endonuclease.
Pssm-ID: 340403 [Multi-domain] Cd Length: 188 Bit Score: 298.58 E-value: 4.31e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 12 TINKIAAGEVVERPSSVVKELIENSIDAGANKISIDIIDGGKSLIKITDNGMGIPSSEVEKSFLRHATSKIKKIDDLYDL 91
Cdd:cd16926 1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 92 YSLGFRGEALASISAVSKLEMTTKTKDEIIGTKIYV-EGGKIISKEPIGSTNGTTIIIRDIFFNTPARQKFLKSTHAETI 170
Cdd:cd16926 81 TTLGFRGEALASIASVSRLTITTRTADDDVGTRLVVdGGGIIEEVKPAAAPVGTTVTVRDLFYNTPARRKFLKSPKTELS 160
|
170 180
....*....|....*....|....*...
gi 489519339 171 NISDLINKLAIGNPNIQFKYTNNNKQML 198
Cdd:cd16926 161 KILDLVQRLALAHPDVSFSLTHDGKLVL 188
|
|
| MutL_C |
smart00853 |
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ... |
470-609 |
4.52e-47 |
|
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair machinery that corrects replication errors. MutS recognises mispaired or unpaired bases in a DNA duplex and in the presence of ATP, recruits MutL to form a DNA signaling complex for repair. The N terminal region of MutL contains the ATPase domain and the C terminal is involved in dimerisation.
Pssm-ID: 214857 [Multi-domain] Cd Length: 140 Bit Score: 162.52 E-value: 4.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 470 VIGVVFNTYIILSKNDSMYLLDQHAAHERILYERYMEKfyRQDINMQILLDPVIIEVSNVDMLQIENNLELFMKFGFELE 549
Cdd:smart00853 1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQ--AGGLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELE 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489519339 550 IFGNNHIMVRCVPTIFGVPETEKFILQIIDNIEEITSNYDLKGER--FASMACRSAIKANDK 609
Cdd:smart00853 79 IFGPQSLILRSVPALLRQQNLQKLIPELLDLLSDEEENARPSRLEalLASLACRSAIRAGDA 140
|
|
| MutL_C |
pfam08676 |
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ... |
471-608 |
2.26e-44 |
|
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair machinery that corrects replication errors. MutS recognizes mispaired or unpaired bases in a DNA duplex and in the presence of ATP, recruits MutL to form a DNA signaling complex for repair. The N terminal region of MutL contains the ATPase domain and the C terminal is involved in dimerization.
Pssm-ID: 430147 Cd Length: 145 Bit Score: 155.45 E-value: 2.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 471 IGVVFNTYIILSKNDSMYLLDQHAAHERILYERYMEKFYRQDINMQILLDPVIIEVSNVDMLQIENNLELFMKFGFELEI 550
Cdd:pfam08676 4 LGQVHGTYILAENEDGLYLIDQHAAHERILYEKLKRALAEGGLAAQPLLIPLVLELSPEEAALLEEHKEELAQLGFELEE 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 551 FGNNHIMVRCVPTIFGVPETEKFILQIIDNIEEITSNY--DLKGERFASMACRSAIKAND 608
Cdd:pfam08676 84 FGPNSVIVRSVPALLRQQNLQELIRELLDELAEKGGSSleESLEELLATMACHSAVRAGR 143
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| mutL |
PRK00095 |
DNA mismatch repair endonuclease MutL; |
5-653 |
0e+00 |
|
DNA mismatch repair endonuclease MutL;
Pssm-ID: 234630 [Multi-domain] Cd Length: 617 Bit Score: 722.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 5 INILDDLTINKIAAGEVVERPSSVVKELIENSIDAGANKISIDIIDGGKSLIKITDNGMGIPSSEVEKSFLRHATSKIKK 84
Cdd:PRK00095 3 IQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKIAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 85 IDDLYDLYSLGFRGEALASISAVSKLEMTTKTKDEIIGTKIYVEGGKIISKEPIGSTNGTTIIIRDIFFNTPARQKFLKS 164
Cdd:PRK00095 83 LDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADAAEGWQIVYEGGEIVEVKPAAHPVGTTIEVRDLFFNTPARRKFLKS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 165 THAETINISDLINKLAIGNPNIQFKYTNNNKQMLNTPGDGKLVNTIRSIYGKEITENIIDVEFKCNHFKMNGYIGNNNIY 244
Cdd:PRK00095 163 EKTELGHIDDVVNRLALAHPDVAFTLTHNGKLVLQTRGAGQLLQRLAAILGREFAENALPIDAEHGDLRLSGYVGLPTLS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 245 RSNKNLQHIYINKRFVKSKIIIDAITESYKSIIPIGKHAVCFLNIEVDPSCIDVNIHPNKLEIKFEKEQEVyielRDFLk 324
Cdd:PRK00095 243 RANRDYQYLFVNGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLV----HDLI- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 325 VKLIHSNLigkyatysdkKTQPRIAINSREKSTDYKLRNDNLLESTPKNSNTTKSKDevievvtlSSEKPINEFQSVSEV 404
Cdd:PRK00095 318 VQAIQEAL----------AQSGLIPAAAGANQVLEPAEPEPLPLQQTPLYASGSSPP--------ASSPSSAPPEQSEES 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 405 LNASEDEVNNINYLSEDSANDNIQEEFqvdgirnEGNYYLGDSIKDSEEEylcSSKRKFSLyGYsVIGVVFNTYIILSKN 484
Cdd:PRK00095 380 QEESSAEKNPLQPNASQSEAAAAASAE-------AAAAAPAAAPEPAEAA---EEADSFPL-GY-ALGQLHGTYILAENE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 485 DSMYLLDQHAAHERILYERYMEKFYRQDINMQILLDPVIIEVSNVDMLQIENNLELFMKFGFELEIFGNNHIMVRCVPTI 564
Cdd:PRK00095 448 DGLYLVDQHAAHERLLYEQLKDKLAEVGLASQPLLIPLVLELSEDEADRLEEHKELLARLGLELEPFGPNSFAVREVPAL 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 565 FGVPETEKFILQIIDNIEEITSNYDLKG-ERFASMACRSAIKANDKIYDIEIKSLLEQLEKCENPFTCPHGRPIMVEISK 643
Cdd:PRK00095 528 LGQQELEELIRDLLDELAEEGDSDTLKErELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIELSL 607
|
650
....*....|
gi 489519339 644 TEIEKMFKRI 653
Cdd:PRK00095 608 SDLEKLFKRI 617
|
|
| MutL |
COG0323 |
DNA mismatch repair ATPase MutL [Replication, recombination and repair]; |
3-652 |
0e+00 |
|
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
Pssm-ID: 440092 [Multi-domain] Cd Length: 515 Bit Score: 707.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 3 NIINILDDLTINKIAAGEVVERPSSVVKELIENSIDAGANKISIDIIDGGKSLIKITDNGMGIPSSEVEKSFLRHATSKI 82
Cdd:COG0323 2 PKIRLLPDELANQIAAGEVVERPASVVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLPLAFERHATSKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 83 KKIDDLYDLYSLGFRGEALASISAVSKLEMTTKTKDEIIGTKIYVEGGKIISKEPIGSTNGTTIIIRDIFFNTPARQKFL 162
Cdd:COG0323 82 RSAEDLFRIRTLGFRGEALASIASVSRLTLTTRTAGAELGTRIEVEGGKVVEVEPAAAPKGTTVEVRDLFFNTPARRKFL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 163 KSTHAETINISDLINKLAIGNPNIQFKYTNNNKQMLNTPGDGKLVNTIRSIYGKEITENIIDVEFKCNHFKMNGYIGNNN 242
Cdd:COG0323 162 KSDATELAHITDVVRRLALAHPDIAFTLIHNGREVFQLPGAGDLLQRIAAIYGREFAENLLPVEAEREGLRLSGYIGKPE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 243 IYRSNKNLQHIYINKRFVKSKIIIDAITESYKSIIPIGKHAVCFLNIEVDPSCIDVNIHPNKLEIKFEKEQEVYielrDF 322
Cdd:COG0323 242 FSRSNRDYQYFFVNGRPVRDKLLSHAVREAYRDLLPKGRYPVAVLFLELDPELVDVNVHPTKTEVRFRDEREVY----DL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 323 LkvklihsnligkyatysdkktqpriainsrekstdyklrndnllestpknsnttkskdevievvtlssekpineFQSVS 402
Cdd:COG0323 318 V--------------------------------------------------------------------------RSAVR 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 403 EVLNAsedevnninylsedsandniqeefqvdgirnegnyylgdsikdseeeylcsskrkfslygySVIGVVFNTYIILS 482
Cdd:COG0323 324 EALAQ-------------------------------------------------------------AALGQLHGTYILAE 342
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 483 KNDSMYLLDQHAAHERILYERYMEKFYRQDINMQILLDPVIIEVSNVDMLQIENNLELFMKFGFELEIFGNNHIMVRCVP 562
Cdd:COG0323 343 NEDGLVLIDQHAAHERILYERLKKALAEGGVASQPLLIPETLELSPAEAALLEEHLEELARLGFEIEPFGPNTVAVRAVP 422
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 563 TIFGVPETEKFILQIIDNIEE---ITSNYDLKGERFASMACRSAIKANDKIYDIEIKSLLEQLEKCENPFTCPHGRPIMV 639
Cdd:COG0323 423 ALLGEGDAEELLRDLLDELAEegsSESLEELREELLATMACHGAIKAGRRLSLEEMNALLRDLEATENPYTCPHGRPTWI 502
|
650
....*....|...
gi 489519339 640 EISKTEIEKMFKR 652
Cdd:COG0323 503 ELSLEELEKLFKR 515
|
|
| mutl |
TIGR00585 |
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ... |
5-307 |
7.56e-104 |
|
DNA mismatch repair protein MutL; All proteins in this family for which the functions are known are involved in the process of generalized mismatch repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273155 [Multi-domain] Cd Length: 312 Bit Score: 318.05 E-value: 7.56e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 5 INILDDLTINKIAAGEVVERPSSVVKELIENSIDAGANKISIDIIDGGKSLIKITDNGMGIPSSEVEKSFLRHATSKIKK 84
Cdd:TIGR00585 3 IKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKIQS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 85 IDDLYDLYSLGFRGEALASISAVSKLEMTTKT-KDEIIGTKIYVEGGKIISKEPIGSTNGTTIIIRDIFFNTPARQKFLK 163
Cdd:TIGR00585 83 FEDLERIETLGFRGEALASISSVSRLTITTKTsAADGLAYQALLEGGMIESIKPAPRPVGTTVEVRDLFYNLPVRRKFLK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 164 STHAETINISDLINKLAIGNPNIQFKYTNNNKQMLNTPGDGK---LVNTIRSIYGKEITEN-IIDVEFKCNHFKMNGYIG 239
Cdd:TIGR00585 163 SPKKEFRKILDVLQRYALIHPDISFSLTHDGKKVLQLSTKPNqstKENRIRSVFGTAVLRKlIPLDEWEDLDLQLEGFIS 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489519339 240 NNNIYRSNKNL-QHIYINKRFVKSKIIIDAITESYKSIIPIGKHAVCFLNIEVDPSCIDVNIHPNKLEI 307
Cdd:TIGR00585 243 QPNVTRSRRSGwQFLFINGRPVELKLLLKAIREVYHEYLPKGQYPVFVLNLEIDPELVDVNVHPDKKEV 311
|
|
| HATPase_MutL-MLH-PMS-like |
cd16926 |
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ... |
12-198 |
4.31e-98 |
|
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, human MutL homologs (MLH/ PMS), and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of Escherichia coli MutL, human MLH1 (mutL homolog 1), human PMS1 (PMS1 homolog 1, mismatch repair system component), human MLH3 (mutL homolog 3), and human PMS2 (PMS1 homolog 2, mismatch repair system component). MutL homologs (MLH/PMS) participate in MMR (DNA mismatch repair), and in addition have role(s) in DNA damage signaling and suppression of homologous recombination (recombination between partially homologous parental DNAs). The primary role of MutL in MMR is to mediate protein-protein interactions during mismatch recognition and strand removal; a ternary complex is formed between MutS, MutL, and the mismatched DNA, which activates the MutH endonuclease.
Pssm-ID: 340403 [Multi-domain] Cd Length: 188 Bit Score: 298.58 E-value: 4.31e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 12 TINKIAAGEVVERPSSVVKELIENSIDAGANKISIDIIDGGKSLIKITDNGMGIPSSEVEKSFLRHATSKIKKIDDLYDL 91
Cdd:cd16926 1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 92 YSLGFRGEALASISAVSKLEMTTKTKDEIIGTKIYV-EGGKIISKEPIGSTNGTTIIIRDIFFNTPARQKFLKSTHAETI 170
Cdd:cd16926 81 TTLGFRGEALASIASVSRLTITTRTADDDVGTRLVVdGGGIIEEVKPAAAPVGTTVTVRDLFYNTPARRKFLKSPKTELS 160
|
170 180
....*....|....*....|....*...
gi 489519339 171 NISDLINKLAIGNPNIQFKYTNNNKQML 198
Cdd:cd16926 161 KILDLVQRLALAHPDVSFSLTHDGKLVL 188
|
|
| MutL_C |
smart00853 |
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ... |
470-609 |
4.52e-47 |
|
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair machinery that corrects replication errors. MutS recognises mispaired or unpaired bases in a DNA duplex and in the presence of ATP, recruits MutL to form a DNA signaling complex for repair. The N terminal region of MutL contains the ATPase domain and the C terminal is involved in dimerisation.
Pssm-ID: 214857 [Multi-domain] Cd Length: 140 Bit Score: 162.52 E-value: 4.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 470 VIGVVFNTYIILSKNDSMYLLDQHAAHERILYERYMEKfyRQDINMQILLDPVIIEVSNVDMLQIENNLELFMKFGFELE 549
Cdd:smart00853 1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQ--AGGLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELE 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489519339 550 IFGNNHIMVRCVPTIFGVPETEKFILQIIDNIEEITSNYDLKGER--FASMACRSAIKANDK 609
Cdd:smart00853 79 IFGPQSLILRSVPALLRQQNLQKLIPELLDLLSDEEENARPSRLEalLASLACRSAIRAGDA 140
|
|
| MutL_C |
pfam08676 |
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ... |
471-608 |
2.26e-44 |
|
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair machinery that corrects replication errors. MutS recognizes mispaired or unpaired bases in a DNA duplex and in the presence of ATP, recruits MutL to form a DNA signaling complex for repair. The N terminal region of MutL contains the ATPase domain and the C terminal is involved in dimerization.
Pssm-ID: 430147 Cd Length: 145 Bit Score: 155.45 E-value: 2.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 471 IGVVFNTYIILSKNDSMYLLDQHAAHERILYERYMEKFYRQDINMQILLDPVIIEVSNVDMLQIENNLELFMKFGFELEI 550
Cdd:pfam08676 4 LGQVHGTYILAENEDGLYLIDQHAAHERILYEKLKRALAEGGLAAQPLLIPLVLELSPEEAALLEEHKEELAQLGFELEE 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 551 FGNNHIMVRCVPTIFGVPETEKFILQIIDNIEEITSNY--DLKGERFASMACRSAIKAND 608
Cdd:pfam08676 84 FGPNSVIVRSVPALLRQQNLQELIRELLDELAEKGGSSleESLEELLATMACHSAVRAGR 143
|
|
| DNA_mis_repair |
pfam01119 |
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ... |
211-321 |
5.53e-41 |
|
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain of the mutL/hexB/PMS1 family. This domain has a ribosomal S5 domain 2-like fold.
Pssm-ID: 426060 [Multi-domain] Cd Length: 117 Bit Score: 144.95 E-value: 5.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 211 RSIYGKEITENIIDVEFKCNHFKMNGYIGNNNIYRSNKNLQHIYINKRFVKSKIIIDAITESYKSIIPIGKHAVCFLNIE 290
Cdd:pfam01119 1 AAIYGKEFAENLLPIEKEDDGLRLSGYISKPTLSRSNRDYQYLFVNGRPVRDKLLSHAIREAYRDLLPKGRYPVAVLFLE 80
|
90 100 110
....*....|....*....|....*....|.
gi 489519339 291 VDPSCIDVNIHPNKLEIKFEKEQEVYIELRD 321
Cdd:pfam01119 81 IDPELVDVNVHPTKREVRFRDEREVYDFIKE 111
|
|
| MutL_Trans |
cd00782 |
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ... |
206-327 |
4.54e-38 |
|
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the C-terminal domain of DNA mismatch repair (MutL/MLH1/PMS2) family. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. Included in this group are proteins similar to human MLH1, hPMS2, hPMS1, hMLH3 and E. coli MutL, MLH1 forms heterodimers with PMS2, PMS1 and MLH3. These three complexes have distinct functions in meiosis. hMLH1-hPMS2 also participates in the repair of all DNA mismatch repair (MMR) substrates. Roles for hMLH1-hPMS1 or hMLH1-hMLH3 in MMR have not been established. Cells lacking either hMLH1 or hPMS2 have a strong mutator phenotype and display microsatellite instability (MSI). Mutation in hMLH1 causes predisposition to HNPCC, Muir-Torre syndrome and Turcot syndrome (HNPCC variant). Mutation in hPMS2 causes predisposition to HPNCC and Turcot syndrome. Mutation in hMLH1 accounts for a large fraction of HNPCC families. There is no convincing evidence to support hPMS1 having a role in HNPCC predisposition. It has been suggested that hMLH3 may be a low risk gene for colorectal cancer; however there is little evidence to support it having a role in classical HNPCC. It has been suggested that during initiation of DNA mismatch repair in E. coli, the mismatch recognition protein MutS recruits MutL in the presence of ATP. The MutS(ATP)-MutL ternary complex formed, then recruits the latent endonuclease MutH.
Pssm-ID: 238405 [Multi-domain] Cd Length: 122 Bit Score: 136.90 E-value: 4.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 206 LVNTIRSIYGKEITENIIDVEFKCNHFKMNGYIGNNNIYRSNKNLQHIYINKRFVKSKIIIDAITESYKSIIPIGKHAVC 285
Cdd:cd00782 1 LKDRIAQVYGKEVAKNLIEVELESGDFRISGYISKPDFGRSSKDRQFLFVNGRPVRDKLLSKAINEAYRSYLPKGRYPVF 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 489519339 286 FLNIEVDPSCIDVNIHPNKLEIKFEKEQEVYIELRDFLKVKL 327
Cdd:cd00782 81 VLNLELPPELVDVNVHPTKREVRFSDEEEVLELIREALRSAL 122
|
|
| MutL_Trans_MutL |
cd03482 |
MutL_Trans_MutL: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
210-323 |
1.82e-22 |
|
MutL_Trans_MutL: transducer domain, having a ribosomal S5 domain 2-like fold, found in proteins similar to Escherichia coli MutL. EcMutL belongs to the DNA mismatch repair (MutL/MLH1/PMS2) family. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from the ATP-binding site to the DNA breakage/reunion regions of the enzymes. It has been suggested that during initiation of DNA mismatch repair in E. coli, the mismatch recognition protein MutS recruits MutL in the presence of ATP. The MutS(ATP)-MutL ternary complex formed, then recruits the latent endonuclease MutH. Prokaryotic MutS and MutL are homodimers.
Pssm-ID: 239564 [Multi-domain] Cd Length: 123 Bit Score: 93.03 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 210 IRSIYGKEITENIIDVEFKCNHFKMNGYIGNNNIYRSNKNLQHIYINKRFVKSKIIIDAITESYKSIIPIGKHAVCFLNI 289
Cdd:cd03482 5 LADILGEDFAEQALAIDEEAGGLRLSGWIALPTFARSQADIQYFYVNGRMVRDKLISHAVRQAYSDVLHGGRHPAYVLYL 84
|
90 100 110
....*....|....*....|....*....|....
gi 489519339 290 EVDPSCIDVNIHPNKLEIKFEKEQEVYielrDFL 323
Cdd:cd03482 85 ELDPAQVDVNVHPAKHEVRFRDSRLVH----DFI 114
|
|
| TopoII_MutL_Trans |
cd00329 |
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ... |
210-308 |
5.18e-22 |
|
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the C-terminal domain of type II DNA topoisomerases (Topo II) and DNA mismatch repair (MutL/MLH1/PMS2) proteins. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. The GyrB dimerizes in response to ATP binding, and is homologous to the N-terminal half of eukaryotic Topo II and the ATPase fragment of MutL. Type II DNA topoisomerases catalyze the ATP-dependent transport of one DNA duplex through another, in the process generating transient double strand breaks via covalent attachments to both DNA strands at the 5' positions. Included in this group are proteins similar to human MLH1 and PMS2. MLH1 forms a heterodimer with PMS2 which functions in meiosis and in DNA mismatch repair (MMR). Cells lacking either hMLH1 or hPMS2 have a strong mutator phenotype and display microsatellite instability (MSI). Mutation in hMLH1 accounts for a large fraction of Lynch syndrome (HNPCC) families.
Pssm-ID: 238202 [Multi-domain] Cd Length: 107 Bit Score: 91.17 E-value: 5.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 210 IRSIYGKEITENIIDVEFKCNHFKMNGYIGNNNIYRSNKNLQHIYINKRFV-KSKIIIDAITESYKSII---PIGKHAVC 285
Cdd:cd00329 5 LAEILGDKVADKLIYVEGESDGFRVEGAISYPDSGRSSKDRQFSFVNGRPVrEGGTHVKAVREAYTRALngdDVRRYPVA 84
|
90 100
....*....|....*....|...
gi 489519339 286 FLNIEVDPSCIDVNIHPNKLEIK 308
Cdd:cd00329 85 VLSLKIPPSLVDVNVHPTKEEVR 107
|
|
| MutL_Trans_MLH1 |
cd03483 |
MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
210-327 |
1.22e-16 |
|
MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in proteins similar to yeast and human MLH1 (MutL homologue 1). This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. MLH1 forms heterodimers with PMS2, PMS1 and MLH3. These three complexes have distinct functions in meiosis. hMLH1-hPMS2 also participates in the repair of all DNA mismatch repair (MMR) substrates. Roles for hMLH1-hPMS1 or hMLH1-hMLH3 in MMR have not been established. Cells lacking hMLH1 have a strong mutator phenotype and display microsatellite instability (MSI). Mutation in hMLH1 causes predisposition to HNPCC, Muir-Torre syndrome and Turcot syndrome (HNPCC variant). Mutation in hMLH1 accounts for a large fraction of HNPCC families.
Pssm-ID: 239565 [Multi-domain] Cd Length: 127 Bit Score: 76.50 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 210 IRSIYGKEITENIIDVEFKCNH----FKMNGYIGNNNiYRSNKNLQHIYINKRFVKSKIIIDAITESYKSIIPIGKHAVC 285
Cdd:cd03483 6 IRSVYGAAVANELIEVEISDDDddlgFKVKGLISNAN-YSKKKIIFILFINNRLVECSALRRAIENVYANYLPKGAHPFV 84
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 489519339 286 FLNIEVDPSCIDVNIHPNKLEIKFEKEQEVYIELRDFLKVKL 327
Cdd:cd03483 85 YLSLEIPPENVDVNVHPTKREVHFLNEEEIIERIQKLVEDKL 126
|
|
| MutL_Trans_hPMS_2_like |
cd03484 |
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
218-324 |
6.04e-09 |
|
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in proteins similar to human PSM2 (hPSM2). hPSM2 belongs to the DNA mismatch repair (MutL/MLH1/PMS2) family. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. Included in this group are proteins similar to yeast PMS1. The yeast MLH1-PMS1 and the human MLH1-PMS2 heterodimers play a role in meiosis. hMLH1-hPMS2 also participates in the repair of all DNA mismatch repair (MMR) substrates. Cells lacking hPMS2 have a strong mutator phenotype and display microsatellite instability (MSI). Mutation in hPMS2 causes predisposition to HPNCC and Turcot syndrome.
Pssm-ID: 239566 [Multi-domain] Cd Length: 142 Bit Score: 54.97 E-value: 6.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 218 ITENIIDVEFKCNHFKMNGYIGNNNIY--RSNKNLQHIYINKRFVKSKIIIDAITESYKSIiPIGKHAVCFLNIEVDPSC 295
Cdd:cd03484 31 KEELDSDEDLADSEVKITGYISKPSHGcgRSSSDRQFFYINGRPVDLKKVAKLINEVYKSF-NSRQYPFFILNISLPTSL 109
|
90 100
....*....|....*....|....*....
gi 489519339 296 IDVNIHPNKLEIKFEKEQEVYIELRDFLK 324
Cdd:cd03484 110 YDVNVTPDKRTVLLHDEDRLIDTLKTSLS 138
|
|
| HATPase_c_3 |
pfam13589 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ... |
27-138 |
1.07e-08 |
|
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.
Pssm-ID: 433332 [Multi-domain] Cd Length: 135 Bit Score: 54.26 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 27 SVVKELIENSIDAGANKISIDIID--GGKSLIKITDNGMGIPSSEVEKSFLRHATSKIKKID-DLYDLYSLGFRgeaLAS 103
Cdd:pfam13589 3 GALAELIDNSIDADATNIKIEVNKnrGGGTEIVIEDDGHGMSPEELINALRLATSAKEAKRGsTDLGRYGIGLK---LAS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489519339 104 ISAVSKLEMTTKTKDE-----IIGTKIYVEGGKIISKEPI 138
Cdd:pfam13589 80 LSLGAKLTVTSKKEGKsstltLDRDKISNENDWLLPLLTP 119
|
|
| MutL_Trans_hPMS_1_like |
cd03485 |
MutL_Trans_hPMS1_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
212-324 |
4.25e-08 |
|
MutL_Trans_hPMS1_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in proteins similar to human PSM1 (hPSM1) and yeast MLH2. hPSM1 and yMLH2 are members of the DNA mismatch repair (MutL/MLH1/PMS2) family. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. PMS1 forms a heterodimer with MLH1. The MLH1-PMS1 complex functions in meiosis. Loss of yMLH2 results in a small but significant decrease in spore viability and a significant increase in gene conversion frequencies. A role for hMLH1-hPMS1 in DNA mismatch repair has not been established. Mutation in hMLH1 accounts for a large fraction of Lynch syndrome (HNPCC) families, however there is no convincing evidence to support hPMS1 having a role in HNPCC predisposition.
Pssm-ID: 239567 [Multi-domain] Cd Length: 132 Bit Score: 52.27 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 212 SIYGKEITENIIDVEFKCNH--FKMNGYI---GNNNIYRSNKNlQHIYINKRFVKS-KIIIDAITESYKSIIPIG---KH 282
Cdd:cd03485 8 RVLGTAVAANMVPVQSTDEDpqISLEGFLpkpGSDVSKTKSDG-KFISVNSRPVSLgKDIGKLLRQYYSSAYRKSslrRY 86
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 489519339 283 AVCFLNIEVDPSCIDVNIHPNKLEIKFEKEQEVYIELRDFLK 324
Cdd:cd03485 87 PVFFLNILCPPGLVDVNIEPDKDDVLLQNKEAVLQAVENLLE 128
|
|
| MutL_Trans_MLH3 |
cd03486 |
MutL_Trans_MLH3: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
206-310 |
1.92e-07 |
|
MutL_Trans_MLH3: transducer domain, having a ribosomal S5 domain 2-like fold, found in proteins similar to yeast and human MLH3 (MutL homologue 3). MLH3 belongs to the DNA mismatch repair (MutL/MLH1/PMS2) family. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. MLH1 forms heterodimers with MLH3. The MLH1-MLH3 complex plays a role in meiosis. A role for hMLH1-hMLH3 in DNA mismatch repair (MMR) has not been established. It has been suggested that hMLH3 may be a low risk gene for colorectal cancer; however there is little evidence to support it having a role in classical HNPCC.
Pssm-ID: 239568 [Multi-domain] Cd Length: 141 Bit Score: 50.78 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 206 LVNTIRSIYGKEITENIIDVEFKCNHFKMNGYIGNNNIYrsNKNLQHIYINKR--------------FVKSKII-----I 266
Cdd:cd03486 2 ILSVFKQIYGLVLAQKLKEVSAKFQEYEVSGYISSEGHY--SKSFQFIYVNGRlylktrfhklinklFRKTSAVaknksS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 489519339 267 DAITESYKSIIPIGKHAVCFLNIEVDPSCIDVNIHPNKLEIKFE 310
Cdd:cd03486 80 PQSKSSRRGKRSQESYPVFVLNITCPASEYDLSQEPSKTIIEFK 123
|
|
| HATPase_c |
pfam02518 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
28-84 |
1.37e-06 |
|
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.
Pssm-ID: 460579 [Multi-domain] Cd Length: 109 Bit Score: 47.36 E-value: 1.37e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 489519339 28 VVKELIENSID--AGANKISIDIIDGGKSLIKITDNGMGIPSSEVEKSFLRHATSKIKK 84
Cdd:pfam02518 9 VLSNLLDNALKhaAKAGEITVTLSEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRG 67
|
|
| top6b |
TIGR01052 |
DNA topoisomerase VI, B subunit; This model describes DNA topoisomerase VI, an archaeal type ... |
28-146 |
1.66e-06 |
|
DNA topoisomerase VI, B subunit; This model describes DNA topoisomerase VI, an archaeal type II DNA topoisomerase (DNA gyrase). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273417 [Multi-domain] Cd Length: 488 Bit Score: 50.98 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 28 VVKELIENSIDAGAN-------KISIDIIDGGKSLIKITDNGMGIPSSEVEKSFLRH-ATSKIKKIDDLYDLYSLGFRGE 99
Cdd:TIGR01052 32 VIHELVTNSLDACEEagilpdiKVEIEKIGKDHYKVTVEDNGPGIPEEYIPKVFGKMlAGSKFHRIIQSRGQQGIGISGA 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 489519339 100 AL-ASISAVSKLEMTTKTKDEIIGTKIYVE------GGKIISKE--PIGSTNGTTI 146
Cdd:TIGR01052 112 VLySQMTTGKPVKVISSTGGEIYVYKMKLKidvqknEGEIVEKGewNKPGWRGTRI 167
|
|
| PRK04184 |
PRK04184 |
DNA topoisomerase VI subunit B; Validated |
28-74 |
6.65e-05 |
|
DNA topoisomerase VI subunit B; Validated
Pssm-ID: 235246 [Multi-domain] Cd Length: 535 Bit Score: 46.04 E-value: 6.65e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 489519339 28 VVKELIENSIDAGAN-------KISIDIIDGGKSLIKIT--DNGMGIPSSEVEKSF 74
Cdd:PRK04184 40 TVKELVDNSLDACEEagilpdiKIEIKRVDEGKDHYRVTveDNGPGIPPEEIPKVF 95
|
|
| HATPase |
cd00075 |
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ... |
28-81 |
8.23e-05 |
|
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains.
Pssm-ID: 340391 [Multi-domain] Cd Length: 102 Bit Score: 42.20 E-value: 8.23e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 489519339 28 VVKELIENSIDAGAN--KISIDII-DGGKSLIKITDNGMGIPSSEVEKSFLRHATSK 81
Cdd:cd00075 4 VLSNLLDNALKYSPPggTIEISLRqEGDGVVLEVEDNGPGIPEEDLERIFERFYRGD 60
|
|
| HATPase_c |
smart00387 |
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
28-76 |
8.65e-05 |
|
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 42.25 E-value: 8.65e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 489519339 28 VVKELIENSIDAGANKISIDII---DGGKSLIKITDNGMGIPSSEVEKSFLR 76
Cdd:smart00387 9 VLSNLLDNAIKYTPEGGRITVTlerDGDHVEITVEDNGPGIPPEDLEKIFEP 60
|
|
| HATPase_MORC-like |
cd16931 |
Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger ... |
25-103 |
2.29e-04 |
|
Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger proteins MORC1-4, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of human microrchidia (MORC) family CW-type zinc finger proteins MORC1-4, and related domains. In addition to the HATPase domain, MORC family proteins have a CW-type zinc finger domain containing four conserved cysteines and two conserved tryptophans, and coiled-coil domains at the carboxy-terminus. MORC1 has cross-species differential methylation in association with early life stress, and genome-wide association with major depressive disorder (MDD). MORC2 is involved in several nuclear processes, including transcription modulation and DNA damage repair, and exhibits a cytosolic function in lipogenesis, adipogenic differentiation, and lipid homeostasis by increasing the activity of ACLY. MORC3 regulates p53, and is an antiviral factor which plays an important role during HSV-1 and HCMV infection, and is a positive regulator of influenza virus transcription. MORC4 is highly expressed in a subset of diffuse large B-cell lymphomas and has potential as a lymphoma biomarker.
Pssm-ID: 340408 [Multi-domain] Cd Length: 118 Bit Score: 41.24 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 25 PSSVVKELIENSIDAGANKISIDIID----GGKSLIKITDNGMGIPSSEveksfLRHATSKIKKIDDLYDLYSLGFRGEA 100
Cdd:cd16931 12 PFGAVAELVDNARDADATRLDIFIDDinllRGGFMLSFLDDGNGMTPEE-----AHHMISFGFSDKRSDDHDHIGRYGNG 86
|
...
gi 489519339 101 LAS 103
Cdd:cd16931 87 FKS 89
|
|
| COG1389 |
COG1389 |
DNA topoisomerase VI, subunit B [Replication, recombination and repair]; |
28-74 |
4.30e-04 |
|
DNA topoisomerase VI, subunit B [Replication, recombination and repair];
Pssm-ID: 440999 [Multi-domain] Cd Length: 530 Bit Score: 43.28 E-value: 4.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 489519339 28 VVKELIENSIDAGAN-------KISIDIIDGgKSLIKIT--DNGMGIPSSEVEKSF 74
Cdd:COG1389 39 TVKEAVDNSLDACEEagilpdiKVSIERVDG-KDIYRVTveDNGPGIPPEQIPKVF 93
|
|
| HATPase_TopVIB-like |
cd16933 |
Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family ... |
28-121 |
7.18e-04 |
|
Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family includes the histidine kinase-like ATPase (HATPase) domain of the B subunit of topoisomerase VI (Topo VIB). Topo VI is a heterotetrameric complex composed of two TopVIA and two TopVIB subunits and is categorized as a type II B DNA topoisomerase. It is found in archaea and also in plants. Type II enzymes cleave both strands of a DNA duplex and pass a second duplex through the resulting break in an ATP-dependent mechanism. DNA cleavage by Topo VI generates two-nucleotide 5'-protruding ends.
Pssm-ID: 340410 [Multi-domain] Cd Length: 203 Bit Score: 41.18 E-value: 7.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 28 VVKELIENSIDAGAN-------KISIDIIDGGKSLIKITDNGMGIPSSEVEKSFLR-HATSKIKKIDDlYDLYSLGFRGE 99
Cdd:cd16933 23 TVRELVENSLDATEEagilpdiKVEIEEIGKDHYKVIVEDNGPGIPEEQIPKVFGKvLYGSKYHNKQS-RGQQGLGISAA 101
|
90 100
....*....|....*....|...
gi 489519339 100 ALAS-ISAVSKLEMTTKTKDEII 121
Cdd:cd16933 102 VLYSqMTTGKPVEIISSTKDSNY 124
|
|
| CitA |
COG3290 |
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ... |
4-84 |
9.08e-04 |
|
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];
Pssm-ID: 442519 [Multi-domain] Cd Length: 389 Bit Score: 42.14 E-value: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 4 IINILDDLTINKIAAGEVVerpsSVVKELIENSIDAGAN------KISIDI-IDGGKSLIKITDNGMGIPSSEVEKSFLR 76
Cdd:COG3290 265 TIDIDSDLPDLPLSDTDLV----TILGNLLDNAIEAVEKlpeeerRVELSIrDDGDELVIEVEDSGPGIPEELLEKIFER 340
|
....*...
gi 489519339 77 HATSKIKK 84
Cdd:COG3290 341 GFSTKLGE 348
|
|
| 39 |
PHA02569 |
DNA topoisomerase II large subunit; Provisional |
28-71 |
1.76e-03 |
|
DNA topoisomerase II large subunit; Provisional
Pssm-ID: 177398 [Multi-domain] Cd Length: 602 Bit Score: 41.28 E-value: 1.76e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 489519339 28 VVKELIENSIDAG-------ANKISIDIIDGgksLIKITDNGMGIPSSEVE 71
Cdd:PHA02569 49 IIDEIIDNSVDEAirtnfkfANKIDVTIKNN---QVTVSDNGRGIPQAMVT 96
|
|
| HATPase_GyrB-like |
cd16928 |
Histidine kinase-like ATPase domain of the B subunit of DNA gyrase; This family includes ... |
29-146 |
3.06e-03 |
|
Histidine kinase-like ATPase domain of the B subunit of DNA gyrase; This family includes histidine kinase-like ATPase domain of the B subunit of DNA gyrase. Bacterial DNA gyrase is a type II topoisomerase (type II as it transiently cleaves both strands of DNA) which catalyzes the introduction of negative supercoils into DNA, possibly by a mechanism in which one segment of the double-stranded DNA substrate is passed through a transient break in a second segment. It consists of GyrA and GyrB subunits in an A2B2 stoichiometry; GyrA subunits catalyze strand-breakage and reunion reactions, and GyrB subunits hydrolyze ATP. DNA gyrase is found in bacteria, plants and archaea, but as it is absent in humans it is a possible drug target for the treatment of bacterial and parasite infections.
Pssm-ID: 340405 [Multi-domain] Cd Length: 180 Bit Score: 39.06 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519339 29 VKELIENSID---AG-ANKISIDIIDGGksLIKITDNGMGIP----------SSEVEKSFLrHATSKIKKidDLYDlYSL 94
Cdd:cd16928 5 VWEIVDNSIDealAGyATEIEVTLHEDN--SITVEDNGRGIPvdihpktgksAVEVVLTVL-HAGGKFDG--GSYK-VSG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 489519339 95 GFRGEALASISAVS-KLEMTTKtKDEIIGTKIYVEGGKIISKEPIGSTN--GTTI 146
Cdd:cd16928 79 GLHGVGVSVVNALSeRLEVEVK-RDGKIYRQEFSRGGPLTPLEVIGETKktGTTV 132
|
|
| |
