|
Name |
Accession |
Description |
Interval |
E-value |
| mutL |
PRK00095 |
DNA mismatch repair endonuclease MutL; |
5-632 |
0e+00 |
|
DNA mismatch repair endonuclease MutL;
Pssm-ID: 234630 [Multi-domain] Cd Length: 617 Bit Score: 927.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 5 PRIQLLSPRLANQIAAGEVVERPASVAKELLENSLDAGSRRIDVEVEQGGIKLLRVRDDGRGIPADDLPLALARHATSKI 84
Cdd:PRK00095 1 MPIQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 85 RELEDLERVMSLGFRGEALASISSVARLTMTSRTADAGEAWQVETEGrDMQPRVQPAAHPVGTSVEVRDLFFNTPARRKF 164
Cdd:PRK00095 81 ASLDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADAAEGWQIVYEG-GEIVEVKPAAHPVGTTIEVRDLFFNTPARRKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 165 LRAEKTEFDHLQEVIKRLALARFDVAFHLRHNGKTIFALHEARDelaRARRVGAVCGQAFLEQALPIEVERNGLHLWGWV 244
Cdd:PRK00095 160 LKSEKTELGHIDDVVNRLALAHPDVAFTLTHNGKLVLQTRGAGQ---LLQRLAAILGREFAENALPIDAEHGDLRLSGYV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 245 GLPTFSRSQPDLQYFYVNGRMVRDKLVAHAVRQAYRDVLYNGRHPTFVLFFEVDPAVVDVNVHPTKHEVRFRDSRMVHDF 324
Cdd:PRK00095 237 GLPTLSRANRDYQYLFVNGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLVHDL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 325 LYGTLHRALGEVRPDDqLAPPGATSLTEPRPTGAAAGEFGPQGEMRLAESVLESPAArvgwSGGSSASGGSSGYSAYTRP 404
Cdd:PRK00095 317 IVQAIQEALAQSGLIP-AAAGANQVLEPAEPEPLPLQQTPLYASGSSPPASSPSSAP----PEQSEESQEESSAEKNPLQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 405 EAPPSLAEAGGAYKAYFAPLPAGEAPAALPESAQDIPPLGYALAQLKGIYILAENAHGLVLVDMHAAHERITYERLKVAM 484
Cdd:PRK00095 392 PNASQSEAAAAASAEAAAAAPAAAPEPAEAAEEADSFPLGYALGQLHGTYILAENEDGLYLVDQHAAHERLLYEQLKDKL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 485 ASEGLRGQPLLVPESIAVSEREADCAEEHSSWFQRLGFELQRLGPESLAIRQIPALLKQAEATQLVRDVIADLLEYGTSD 564
Cdd:PRK00095 472 AEVGLASQPLLIPLVLELSEDEADRLEEHKELLARLGLELEPFGPNSFAVREVPALLGQQELEELIRDLLDELAEEGDSD 551
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600139 565 RIQAHlnELLGTMACHGAVRANRRLTLPEMNALLRDMEITERSGQCNHGRPTWTQLGLDELDKLFLRG 632
Cdd:PRK00095 552 TLKER--ELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIELSLSDLEKLFKRI 617
|
|
| MutL |
COG0323 |
DNA mismatch repair ATPase MutL [Replication, recombination and repair]; |
5-631 |
0e+00 |
|
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
Pssm-ID: 440092 [Multi-domain] Cd Length: 515 Bit Score: 835.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 5 PRIQLLSPRLANQIAAGEVVERPASVAKELLENSLDAGSRRIDVEVEQGGIKLLRVRDDGRGIPADDLPLALARHATSKI 84
Cdd:COG0323 2 PKIRLLPDELANQIAAGEVVERPASVVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLPLAFERHATSKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 85 RELEDLERVMSLGFRGEALASISSVARLTMTSRTADAGEAWQVETEGRDMQPrVQPAAHPVGTSVEVRDLFFNTPARRKF 164
Cdd:COG0323 82 RSAEDLFRIRTLGFRGEALASIASVSRLTLTTRTAGAELGTRIEVEGGKVVE-VEPAAAPKGTTVEVRDLFFNTPARRKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 165 LRAEKTEFDHLQEVIKRLALARFDVAFHLRHNGKTIFALHEARDelaRARRVGAVCGQAFLEQALPIEVERNGLHLWGWV 244
Cdd:COG0323 161 LKSDATELAHITDVVRRLALAHPDIAFTLIHNGREVFQLPGAGD---LLQRIAAIYGREFAENLLPVEAEREGLRLSGYI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 245 GLPTFSRSQPDLQYFYVNGRMVRDKLVAHAVRQAYRDVLYNGRHPTFVLFFEVDPAVVDVNVHPTKHEVRFRDSRMVHDF 324
Cdd:COG0323 238 GKPEFSRSNRDYQYFFVNGRPVRDKLLSHAVREAYRDLLPKGRYPVAVLFLELDPELVDVNVHPTKTEVRFRDEREVYDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 325 LYGTLHRALGEvrpddqlappgatslteprptgaaagefgpqgemrlaesvlespaarvgwsggssasggssgysaytrp 404
Cdd:COG0323 318 VRSAVREALAQ--------------------------------------------------------------------- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 405 eappslaeaggaykayfaplpageapaalpesaqdipplgYALAQLKGIYILAENAHGLVLVDMHAAHERITYERLKVAM 484
Cdd:COG0323 329 ----------------------------------------AALGQLHGTYILAENEDGLVLIDQHAAHERILYERLKKAL 368
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 485 ASEGLRGQPLLVPESIAVSEREADCAEEHSSWFQRLGFELQRLGPESLAIRQIPALLKQAEATQLVRDVIADLLEYGTSD 564
Cdd:COG0323 369 AEGGVASQPLLIPETLELSPAEAALLEEHLEELARLGFEIEPFGPNTVAVRAVPALLGEGDAEELLRDLLDELAEEGSSE 448
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600139 565 RIQAHLNELLGTMACHGAVRANRRLTLPEMNALLRDMEITERSGQCNHGRPTWTQLGLDELDKLFLR 631
Cdd:COG0323 449 SLEELREELLATMACHGAIKAGRRLSLEEMNALLRDLEATENPYTCPHGRPTWIELSLEELEKLFKR 515
|
|
| mutl |
TIGR00585 |
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ... |
6-314 |
1.89e-130 |
|
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: 385.84 E-value: 1.89e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 6 RIQLLSPRLANQIAAGEVVERPASVAKELLENSLDAGSRRIDVEVEQGGIKLLRVRDDGRGIPADDLPLALARHATSKIR 85
Cdd:TIGR00585 2 TIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKIQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 86 ELEDLERVMSLGFRGEALASISSVARLTMTSRT-ADAGEAWQVETEGRDMQPRvQPAAHPVGTSVEVRDLFFNTPARRKF 164
Cdd:TIGR00585 82 SFEDLERIETLGFRGEALASISSVSRLTITTKTsAADGLAYQALLEGGMIESI-KPAPRPVGTTVEVRDLFYNLPVRRKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 165 LRAEKTEFDHLQEVIKRLALARFDVAFHLRHNGKTIFALHEARDELARARRVGAVCGQAFLEQALPI-EVERNGLHLWGW 243
Cdd:TIGR00585 161 LKSPKKEFRKILDVLQRYALIHPDISFSLTHDGKKVLQLSTKPNQSTKENRIRSVFGTAVLRKLIPLdEWEDLDLQLEGF 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600139 244 VGLPTFSRSQPDL-QYFYVNGRMVRDKLVAHAVRQAYRDVLYNGRHPTFVLFFEVDPAVVDVNVHPTKHEVR 314
Cdd:TIGR00585 241 ISQPNVTRSRRSGwQFLFINGRPVELKLLLKAIREVYHEYLPKGQYPVFVLNLEIDPELVDVNVHPDKKEVR 312
|
|
| HATPase_MutL-MLH-PMS-like |
cd16926 |
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ... |
14-201 |
4.09e-108 |
|
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: 323.62 E-value: 4.09e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 14 LANQIAAGEVVERPASVAKELLENSLDAGSRRIDVEVEQGGIKLLRVRDDGRGIPADDLPLALARHATSKIRELEDLERV 93
Cdd:cd16926 1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 94 MSLGFRGEALASISSVARLTMTSRTADAGEAWQVETEGRDMQPRVQPAAHPVGTSVEVRDLFFNTPARRKFLRAEKTEFD 173
Cdd:cd16926 81 TTLGFRGEALASIASVSRLTITTRTADDDVGTRLVVDGGGIIEEVKPAAAPVGTTVTVRDLFYNTPARRKFLKSPKTELS 160
|
170 180
....*....|....*....|....*...
gi 15600139 174 HLQEVIKRLALARFDVAFHLRHNGKTIF 201
Cdd:cd16926 161 KILDLVQRLALAHPDVSFSLTHDGKLVL 188
|
|
| DNA_mis_repair |
pfam01119 |
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ... |
218-333 |
2.40e-57 |
|
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: 188.86 E-value: 2.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 218 AVCGQAFLEQALPIEVERNGLHLWGWVGLPTFSRSQPDLQYFYVNGRMVRDKLVAHAVRQAYRDVLYNGRHPTFVLFFEV 297
Cdd:pfam01119 2 AIYGKEFAENLLPIEKEDDGLRLSGYISKPTLSRSNRDYQYLFVNGRPVRDKLLSHAIREAYRDLLPKGRYPVAVLFLEI 81
|
90 100 110
....*....|....*....|....*....|....*.
gi 15600139 298 DPAVVDVNVHPTKHEVRFRDSRMVHDFLYGTLHRAL 333
Cdd:pfam01119 82 DPELVDVNVHPTKREVRFRDEREVYDFIKEALREAL 117
|
|
| MutL_C |
smart00853 |
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ... |
446-588 |
1.99e-46 |
|
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: 160.60 E-value: 1.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 446 ALAQLKGIYILAENAHGLVLVDMHAAHERITYERLKVAmaSEGLRGQPLLVPESIAVSEREADCAEEHSSWFQRLGFELQ 525
Cdd:smart00853 1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQ--AGGLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELE 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600139 526 RLGPESLAIRQIPALLKQAEATQLVRDVIADLLEYGTSDrIQAHLNELLGTMACHGAVRANRR 588
Cdd:smart00853 79 IFGPQSLILRSVPALLRQQNLQKLIPELLDLLSDEEENA-RPSRLEALLASLACRSAIRAGDA 140
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| mutL |
PRK00095 |
DNA mismatch repair endonuclease MutL; |
5-632 |
0e+00 |
|
DNA mismatch repair endonuclease MutL;
Pssm-ID: 234630 [Multi-domain] Cd Length: 617 Bit Score: 927.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 5 PRIQLLSPRLANQIAAGEVVERPASVAKELLENSLDAGSRRIDVEVEQGGIKLLRVRDDGRGIPADDLPLALARHATSKI 84
Cdd:PRK00095 1 MPIQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 85 RELEDLERVMSLGFRGEALASISSVARLTMTSRTADAGEAWQVETEGrDMQPRVQPAAHPVGTSVEVRDLFFNTPARRKF 164
Cdd:PRK00095 81 ASLDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADAAEGWQIVYEG-GEIVEVKPAAHPVGTTIEVRDLFFNTPARRKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 165 LRAEKTEFDHLQEVIKRLALARFDVAFHLRHNGKTIFALHEARDelaRARRVGAVCGQAFLEQALPIEVERNGLHLWGWV 244
Cdd:PRK00095 160 LKSEKTELGHIDDVVNRLALAHPDVAFTLTHNGKLVLQTRGAGQ---LLQRLAAILGREFAENALPIDAEHGDLRLSGYV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 245 GLPTFSRSQPDLQYFYVNGRMVRDKLVAHAVRQAYRDVLYNGRHPTFVLFFEVDPAVVDVNVHPTKHEVRFRDSRMVHDF 324
Cdd:PRK00095 237 GLPTLSRANRDYQYLFVNGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLVHDL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 325 LYGTLHRALGEVRPDDqLAPPGATSLTEPRPTGAAAGEFGPQGEMRLAESVLESPAArvgwSGGSSASGGSSGYSAYTRP 404
Cdd:PRK00095 317 IVQAIQEALAQSGLIP-AAAGANQVLEPAEPEPLPLQQTPLYASGSSPPASSPSSAP----PEQSEESQEESSAEKNPLQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 405 EAPPSLAEAGGAYKAYFAPLPAGEAPAALPESAQDIPPLGYALAQLKGIYILAENAHGLVLVDMHAAHERITYERLKVAM 484
Cdd:PRK00095 392 PNASQSEAAAAASAEAAAAAPAAAPEPAEAAEEADSFPLGYALGQLHGTYILAENEDGLYLVDQHAAHERLLYEQLKDKL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 485 ASEGLRGQPLLVPESIAVSEREADCAEEHSSWFQRLGFELQRLGPESLAIRQIPALLKQAEATQLVRDVIADLLEYGTSD 564
Cdd:PRK00095 472 AEVGLASQPLLIPLVLELSEDEADRLEEHKELLARLGLELEPFGPNSFAVREVPALLGQQELEELIRDLLDELAEEGDSD 551
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600139 565 RIQAHlnELLGTMACHGAVRANRRLTLPEMNALLRDMEITERSGQCNHGRPTWTQLGLDELDKLFLRG 632
Cdd:PRK00095 552 TLKER--ELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIELSLSDLEKLFKRI 617
|
|
| MutL |
COG0323 |
DNA mismatch repair ATPase MutL [Replication, recombination and repair]; |
5-631 |
0e+00 |
|
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
Pssm-ID: 440092 [Multi-domain] Cd Length: 515 Bit Score: 835.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 5 PRIQLLSPRLANQIAAGEVVERPASVAKELLENSLDAGSRRIDVEVEQGGIKLLRVRDDGRGIPADDLPLALARHATSKI 84
Cdd:COG0323 2 PKIRLLPDELANQIAAGEVVERPASVVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLPLAFERHATSKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 85 RELEDLERVMSLGFRGEALASISSVARLTMTSRTADAGEAWQVETEGRDMQPrVQPAAHPVGTSVEVRDLFFNTPARRKF 164
Cdd:COG0323 82 RSAEDLFRIRTLGFRGEALASIASVSRLTLTTRTAGAELGTRIEVEGGKVVE-VEPAAAPKGTTVEVRDLFFNTPARRKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 165 LRAEKTEFDHLQEVIKRLALARFDVAFHLRHNGKTIFALHEARDelaRARRVGAVCGQAFLEQALPIEVERNGLHLWGWV 244
Cdd:COG0323 161 LKSDATELAHITDVVRRLALAHPDIAFTLIHNGREVFQLPGAGD---LLQRIAAIYGREFAENLLPVEAEREGLRLSGYI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 245 GLPTFSRSQPDLQYFYVNGRMVRDKLVAHAVRQAYRDVLYNGRHPTFVLFFEVDPAVVDVNVHPTKHEVRFRDSRMVHDF 324
Cdd:COG0323 238 GKPEFSRSNRDYQYFFVNGRPVRDKLLSHAVREAYRDLLPKGRYPVAVLFLELDPELVDVNVHPTKTEVRFRDEREVYDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 325 LYGTLHRALGEvrpddqlappgatslteprptgaaagefgpqgemrlaesvlespaarvgwsggssasggssgysaytrp 404
Cdd:COG0323 318 VRSAVREALAQ--------------------------------------------------------------------- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 405 eappslaeaggaykayfaplpageapaalpesaqdipplgYALAQLKGIYILAENAHGLVLVDMHAAHERITYERLKVAM 484
Cdd:COG0323 329 ----------------------------------------AALGQLHGTYILAENEDGLVLIDQHAAHERILYERLKKAL 368
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 485 ASEGLRGQPLLVPESIAVSEREADCAEEHSSWFQRLGFELQRLGPESLAIRQIPALLKQAEATQLVRDVIADLLEYGTSD 564
Cdd:COG0323 369 AEGGVASQPLLIPETLELSPAEAALLEEHLEELARLGFEIEPFGPNTVAVRAVPALLGEGDAEELLRDLLDELAEEGSSE 448
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600139 565 RIQAHLNELLGTMACHGAVRANRRLTLPEMNALLRDMEITERSGQCNHGRPTWTQLGLDELDKLFLR 631
Cdd:COG0323 449 SLEELREELLATMACHGAIKAGRRLSLEEMNALLRDLEATENPYTCPHGRPTWIELSLEELEKLFKR 515
|
|
| mutl |
TIGR00585 |
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ... |
6-314 |
1.89e-130 |
|
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: 385.84 E-value: 1.89e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 6 RIQLLSPRLANQIAAGEVVERPASVAKELLENSLDAGSRRIDVEVEQGGIKLLRVRDDGRGIPADDLPLALARHATSKIR 85
Cdd:TIGR00585 2 TIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKIQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 86 ELEDLERVMSLGFRGEALASISSVARLTMTSRT-ADAGEAWQVETEGRDMQPRvQPAAHPVGTSVEVRDLFFNTPARRKF 164
Cdd:TIGR00585 82 SFEDLERIETLGFRGEALASISSVSRLTITTKTsAADGLAYQALLEGGMIESI-KPAPRPVGTTVEVRDLFYNLPVRRKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 165 LRAEKTEFDHLQEVIKRLALARFDVAFHLRHNGKTIFALHEARDELARARRVGAVCGQAFLEQALPI-EVERNGLHLWGW 243
Cdd:TIGR00585 161 LKSPKKEFRKILDVLQRYALIHPDISFSLTHDGKKVLQLSTKPNQSTKENRIRSVFGTAVLRKLIPLdEWEDLDLQLEGF 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600139 244 VGLPTFSRSQPDL-QYFYVNGRMVRDKLVAHAVRQAYRDVLYNGRHPTFVLFFEVDPAVVDVNVHPTKHEVR 314
Cdd:TIGR00585 241 ISQPNVTRSRRSGwQFLFINGRPVELKLLLKAIREVYHEYLPKGQYPVFVLNLEIDPELVDVNVHPDKKEVR 312
|
|
| HATPase_MutL-MLH-PMS-like |
cd16926 |
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ... |
14-201 |
4.09e-108 |
|
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: 323.62 E-value: 4.09e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 14 LANQIAAGEVVERPASVAKELLENSLDAGSRRIDVEVEQGGIKLLRVRDDGRGIPADDLPLALARHATSKIRELEDLERV 93
Cdd:cd16926 1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 94 MSLGFRGEALASISSVARLTMTSRTADAGEAWQVETEGRDMQPRVQPAAHPVGTSVEVRDLFFNTPARRKFLRAEKTEFD 173
Cdd:cd16926 81 TTLGFRGEALASIASVSRLTITTRTADDDVGTRLVVDGGGIIEEVKPAAAPVGTTVTVRDLFYNTPARRKFLKSPKTELS 160
|
170 180
....*....|....*....|....*...
gi 15600139 174 HLQEVIKRLALARFDVAFHLRHNGKTIF 201
Cdd:cd16926 161 KILDLVQRLALAHPDVSFSLTHDGKLVL 188
|
|
| MutL_Trans_MutL |
cd03482 |
MutL_Trans_MutL: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
212-333 |
5.88e-72 |
|
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: 227.47 E-value: 5.88e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 212 RARRVGAVCGQAFLEQALPIEVERNGLHLWGWVGLPTFSRSQPDLQYFYVNGRMVRDKLVAHAVRQAYRDVLYNGRHPTF 291
Cdd:cd03482 1 KLQRLADILGEDFAEQALAIDEEAGGLRLSGWIALPTFARSQADIQYFYVNGRMVRDKLISHAVRQAYSDVLHGGRHPAY 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 15600139 292 VLFFEVDPAVVDVNVHPTKHEVRFRDSRMVHDFLYGTLHRAL 333
Cdd:cd03482 81 VLYLELDPAQVDVNVHPAKHEVRFRDSRLVHDFIYHAVKKAL 122
|
|
| DNA_mis_repair |
pfam01119 |
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ... |
218-333 |
2.40e-57 |
|
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: 188.86 E-value: 2.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 218 AVCGQAFLEQALPIEVERNGLHLWGWVGLPTFSRSQPDLQYFYVNGRMVRDKLVAHAVRQAYRDVLYNGRHPTFVLFFEV 297
Cdd:pfam01119 2 AIYGKEFAENLLPIEKEDDGLRLSGYISKPTLSRSNRDYQYLFVNGRPVRDKLLSHAIREAYRDLLPKGRYPVAVLFLEI 81
|
90 100 110
....*....|....*....|....*....|....*.
gi 15600139 298 DPAVVDVNVHPTKHEVRFRDSRMVHDFLYGTLHRAL 333
Cdd:pfam01119 82 DPELVDVNVHPTKREVRFRDEREVYDFIKEALREAL 117
|
|
| MutL_C |
pfam08676 |
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ... |
442-589 |
1.53e-56 |
|
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: 187.81 E-value: 1.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 442 PLGyaLAQLKGIYILAENAHGLVLVDMHAAHERITYERLKVAMASEGLRGQPLLVPESIAVSEREADCAEEHSSWFQRLG 521
Cdd:pfam08676 1 PLG--LGQVHGTYILAENEDGLYLIDQHAAHERILYEKLKRALAEGGLAAQPLLIPLVLELSPEEAALLEEHKEELAQLG 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600139 522 FELQRLGPESLAIRQIPALLKQAEATQLVRDVIADLLEYGTsDRIQAHLNELLGTMACHGAVRANRRL 589
Cdd:pfam08676 79 FELEEFGPNSVIVRSVPALLRQQNLQELIRELLDELAEKGG-SSLEESLEELLATMACHSAVRAGRRL 145
|
|
| MutL_Trans |
cd00782 |
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ... |
214-333 |
1.31e-54 |
|
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: 181.59 E-value: 1.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 214 RRVGAVCGQAFLEQALPIEVERNGLHLWGWVGLPTFSRSQPDLQYFYVNGRMVRDKLVAHAVRQAYRDVLYNGRHPTFVL 293
Cdd:cd00782 3 DRIAQVYGKEVAKNLIEVELESGDFRISGYISKPDFGRSSKDRQFLFVNGRPVRDKLLSKAINEAYRSYLPKGRYPVFVL 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15600139 294 FFEVDPAVVDVNVHPTKHEVRFRDSRMVHDFLYGTLHRAL 333
Cdd:cd00782 83 NLELPPELVDVNVHPTKREVRFSDEEEVLELIREALRSAL 122
|
|
| MutL_C |
smart00853 |
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ... |
446-588 |
1.99e-46 |
|
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: 160.60 E-value: 1.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 446 ALAQLKGIYILAENAHGLVLVDMHAAHERITYERLKVAmaSEGLRGQPLLVPESIAVSEREADCAEEHSSWFQRLGFELQ 525
Cdd:smart00853 1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQ--AGGLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELE 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600139 526 RLGPESLAIRQIPALLKQAEATQLVRDVIADLLEYGTSDrIQAHLNELLGTMACHGAVRANRR 588
Cdd:smart00853 79 IFGPQSLILRSVPALLRQQNLQKLIPELLDLLSDEEENA-RPSRLEALLASLACRSAIRAGDA 140
|
|
| TopoII_MutL_Trans |
cd00329 |
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ... |
215-314 |
3.02e-32 |
|
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: 120.06 E-value: 3.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 215 RVGAVCGQAFLEQALPIEVERNGLHLWGWVGLPTFSRSQPDLQYFYVNGRMVR-DKLVAHAVRQAYRDVLY---NGRHPT 290
Cdd:cd00329 4 RLAEILGDKVADKLIYVEGESDGFRVEGAISYPDSGRSSKDRQFSFVNGRPVReGGTHVKAVREAYTRALNgddVRRYPV 83
|
90 100
....*....|....*....|....
gi 15600139 291 FVLFFEVDPAVVDVNVHPTKHEVR 314
Cdd:cd00329 84 AVLSLKIPPSLVDVNVHPTKEEVR 107
|
|
| MutL_Trans_MLH1 |
cd03483 |
MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
231-315 |
7.61e-13 |
|
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: 65.72 E-value: 7.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 231 IEVE------RNGLHLWGWVGLPTFSrSQPDLQYFYVNGRMVRDKLVAHAVRQAYRDVLYNGRHPTFVLFFEVDPAVVDV 304
Cdd:cd03483 19 IEVEisddddDLGFKVKGLISNANYS-KKKIIFILFINNRLVECSALRRAIENVYANYLPKGAHPFVYLSLEIPPENVDV 97
|
90
....*....|.
gi 15600139 305 NVHPTKHEVRF 315
Cdd:cd03483 98 NVHPTKREVHF 108
|
|
| MutL_Trans_hPMS_2_like |
cd03484 |
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
231-329 |
7.48e-12 |
|
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: 63.44 E-value: 7.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 231 IEVERNGLHLWGWVGL---PTF--SRSQPDLQYFYVNGRMVRDKLVAHAVRQAYRDvlYNGRH-PTFVLFFEVDPAVVDV 304
Cdd:cd03484 35 DSDEDLADSEVKITGYiskPSHgcGRSSSDRQFFYINGRPVDLKKVAKLINEVYKS--FNSRQyPFFILNISLPTSLYDV 112
|
90 100
....*....|....*....|....*
gi 15600139 305 NVHPTKHEVRFRDSRMVHDFLYGTL 329
Cdd:cd03484 113 NVTPDKRTVLLHDEDRLIDTLKTSL 137
|
|
| HATPase_c |
pfam02518 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
22-88 |
4.84e-09 |
|
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: 54.30 E-value: 4.84e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600139 22 EVVERPASVAKELLENSLDAGSR--RIDVEVEQGGIKLLRVRDDGRGIPADDLPLALARHATSKIRELE 88
Cdd:pfam02518 1 GDELRLRQVLSNLLDNALKHAAKagEITVTLSEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGGG 69
|
|
| HATPase_c_3 |
pfam13589 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ... |
27-118 |
2.03e-07 |
|
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: 50.41 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 27 PASVAKELLENSLDAGSRRIDVEVEQ--GGIKLLRVRDDGRGIPADDLPLALARHATSKIRELEdlERVMSLGFRGEALA 104
Cdd:pfam13589 1 LEGALAELIDNSIDADATNIKIEVNKnrGGGTEIVIEDDGHGMSPEELINALRLATSAKEAKRG--STDLGRYGIGLKLA 78
|
90
....*....|....
gi 15600139 105 SISSVARLTMTSRT 118
Cdd:pfam13589 79 SLSLGAKLTVTSKK 92
|
|
| MutL_Trans_hPMS_1_like |
cd03485 |
MutL_Trans_hPMS1_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
209-321 |
1.37e-06 |
|
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: 48.03 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 209 ELARARRVGAVCGQAFLEQALPieVERNGLHLWGWVGLPTFSRS--QPDLQYFYVNGR---MVRD--KLVAHAVRQAYRD 281
Cdd:cd03485 3 KEALARVLGTAVAANMVPVQST--DEDPQISLEGFLPKPGSDVSktKSDGKFISVNSRpvsLGKDigKLLRQYYSSAYRK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15600139 282 vLYNGRHPTFVLFFEVDPAVVDVNVHPTKHEVRFRDSRMV 321
Cdd:cd03485 81 -SSLRRYPVFFLNILCPPGLVDVNIEPDKDDVLLQNKEAV 119
|
|
| HATPase |
cd00075 |
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ... |
33-112 |
2.39e-06 |
|
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: 46.44 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 33 ELLENSLDAGSR--RIDVEVEQGGIKL-LRVRDDGRGIPADDLPLALARHATSKireledleRVMSLGFRGEALASISSV 109
Cdd:cd00075 7 NLLDNALKYSPPggTIEISLRQEGDGVvLEVEDNGPGIPEEDLERIFERFYRGD--------KSREGGGTGLGLAIVRRI 78
|
...
gi 15600139 110 ARL 112
Cdd:cd00075 79 VEA 81
|
|
| HATPase_c |
smart00387 |
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
30-86 |
4.63e-06 |
|
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 45.72 E-value: 4.63e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 30 VAKELLENSLDAGSR--RIDVEVEQGGIKL-LRVRDDGRGIPADDLPLALARHATSKIRE 86
Cdd:smart00387 9 VLSNLLDNAIKYTPEggRITVTLERDGDHVeITVEDNGPGIPPEDLEKIFEPFFRTDKRS 68
|
|
| PRK05559 |
PRK05559 |
DNA topoisomerase IV subunit B; Reviewed |
31-73 |
2.66e-04 |
|
DNA topoisomerase IV subunit B; Reviewed
Pssm-ID: 235501 [Multi-domain] Cd Length: 631 Bit Score: 43.94 E-value: 2.66e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 15600139 31 AKELLENSLD---AGS-RRIDVEVEQGGIklLRVRDDGRGIPADDLP 73
Cdd:PRK05559 42 VQEVIDNSVDealAGHgKRIEVTLHADGS--VSVRDNGRGIPVGIHP 86
|
|
| HATPase_TopVIB-like |
cd16933 |
Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family ... |
30-183 |
6.78e-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: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 30 VAKELLENSLDAGSRR-----IDVEVEQGG--IKLLRVRDDGRGIPADDLPLALAR-HATSKIRELEdlERVM-SLGFRG 100
Cdd:cd16933 23 TVRELVENSLDATEEAgilpdIKVEIEEIGkdHYKVIVEDNGPGIPEEQIPKVFGKvLYGSKYHNKQ--SRGQqGLGISA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600139 101 EALASISSVAR-LTMTSRTADAGEAWQVE-------TEGRDMQPRVQPAAH-PVGTSVEVrDLFFNTPARRKFlraekte 171
Cdd:cd16933 101 AVLYSQMTTGKpVEIISSTKDSNYAYVVKlmidtdkNEPEILEKEEVENRYkWHGTRVEL-ELEGNWVAARSQ------- 172
|
170
....*....|..
gi 15600139 172 fdhLQEVIKRLA 183
Cdd:cd16933 173 ---ILEYYKRTA 181
|
|
| CitA |
COG3290 |
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ... |
34-83 |
1.69e-03 |
|
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];
Pssm-ID: 442519 [Multi-domain] Cd Length: 389 Bit Score: 40.99 E-value: 1.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600139 34 LLENSLDA------GSRRIDVEVEQ-GGIKLLRVRDDGRGIPADDLPLALARHATSK 83
Cdd:COG3290 289 LLDNAIEAveklpeEERRVELSIRDdGDELVIEVEDSGPGIPEELLEKIFERGFSTK 345
|
|
| HATPase_GyrB-like |
cd16928 |
Histidine kinase-like ATPase domain of the B subunit of DNA gyrase; This family includes ... |
32-70 |
3.85e-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: 38.67 E-value: 3.85e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 15600139 32 KELLENSLD---AGS-RRIDVEVEQGGikLLRVRDDGRGIPAD 70
Cdd:cd16928 6 WEIVDNSIDealAGYaTEIEVTLHEDN--SITVEDNGRGIPVD 46
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| PRK04184 |
PRK04184 |
DNA topoisomerase VI subunit B; Validated |
32-78 |
4.46e-03 |
|
DNA topoisomerase VI subunit B; Validated
Pssm-ID: 235246 [Multi-domain] Cd Length: 535 Bit Score: 39.88 E-value: 4.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600139 32 KELLENSLDA----GSR-----RIDVEVEQGGIKLLRVRDDGRGIPADDLPLALAR 78
Cdd:PRK04184 42 KELVDNSLDAceeaGILpdikiEIKRVDEGKDHYRVTVEDNGPGIPPEEIPKVFGK 97
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| KdpD |
COG2205 |
K+-sensing histidine kinase KdpD [Signal transduction mechanisms]; |
33-73 |
6.85e-03 |
|
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
Pssm-ID: 441807 [Multi-domain] Cd Length: 239 Bit Score: 38.73 E-value: 6.85e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 15600139 33 ELLENSL---DAGSR-RIDVEVEQGGIkLLRVRDDGRGIPADDLP 73
Cdd:COG2205 139 NLLDNAIkysPPGGTiTISARREGDGV-RISVSDNGPGIPEEELE 182
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| HATPase_HupT_MifS-like |
cd16976 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
30-73 |
7.69e-03 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhodobacter capsulatus HupT and Pseudomonas aeruginosa MifS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Rhodobacter capsulatus HupT of the HupT-HupR two-component regulatory system (TCS), which regulates the synthesis of HupSL, a membrane bound [NiFe]hydrogenase. It also contains the HATPase domain of Pseudomonas aeruginosa MifS, the HK of the MifS-MifR TCS, which may be involved in sensing alpha-ketoglutarate and regulating its transport and subsequent metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also have a C-terminal PAS sensor domain.
Pssm-ID: 340435 [Multi-domain] Cd Length: 102 Bit Score: 36.28 E-value: 7.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 15600139 30 VAKELLENSLDA-GSR---RIDVEVE-QGGIKLLRVRDDGRGIPADDLP 73
Cdd:cd16976 4 VLMNLLQNALDAmGKVenpRIRIAARrLGGRLVLVVRDNGPGIAEEHLS 52
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