|
Name |
Accession |
Description |
Interval |
E-value |
| mutL |
PRK00095 |
DNA mismatch repair endonuclease MutL; |
3-644 |
0e+00 |
|
DNA mismatch repair endonuclease MutL;
Pssm-ID: 234630 [Multi-domain] Cd Length: 617 Bit Score: 823.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 3 KIKELETSLANKIAAGEVVERPSSVVKELLENAIDAQATEINIEVEQSGVSSIRVVDNGTGIAQEDLGLVFHRHATSKIV 82
Cdd:PRK00095 2 PIQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 83 ADDDLFHIRTLGFRGEALASISSVAKVTLKTCTDNEN-GHEIYAEDGKIIHQKPAKAKKGTDIQVESLFYNTPARLKYIK 161
Cdd:PRK00095 82 SLDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADAAeGWQIVYEGGEIVEVKPAAHPVGTTIEVRDLFFNTPARRKFLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 162 SLYTELGKITDIVNRMAMSHPKIRIALVSDGKTLLSTNGSGRTNEVMAEIYGMKVAKDLVHISGDTSDYHLEGFVAKPEH 241
Cdd:PRK00095 162 SEKTELGHIDDVVNRLALAHPDVAFTLTHNGKLVLQTRGAGQLLQRLAAILGREFAENALPIDAEHGDLRLSGYVGLPTL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 242 SRSNKHYISIFINGRYIKNFVLNKAILEGYHTLLTIGRFPICYINIQMDPILVDVNVHPTKLEVRLSKEDQLYDLIVTKI 321
Cdd:PRK00095 242 SRANRDYQYLFVNGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLVHDLIVQAI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 322 REAFKDKILIPQndlnrTPKKNKVLETFEQQKINFEKKQSQIGETSAPYvhdqkdknhdveshrndldstSSTNNESTEV 401
Cdd:PRK00095 322 QEALAQSGLIPA-----AAGANQVLEPAEPEPLPLQQTPLYASGSSPPA---------------------SSPSSAPPEQ 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 402 SNELHNHIDDSYLQSQKEVLFDMEQDTSNEYKTLNQQSNDIKGTVSQTPHRRVPYMEIVGQVHGTYIIAQNENGMFMIDQ 481
Cdd:PRK00095 376 SEESQEESSAEKNPLQPNASQSEAAAAASAEAAAAAPAAAPEPAEAAEEADSFPLGYALGQLHGTYILAENEDGLYLVDQ 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 482 HAAQERIKYEYFREKIGEVTNEVQNLLIPLTFHFSKDEQMIIDQYKDELDKVGVHLEHFGGHDYIVNSYPVWFPKVEAEE 561
Cdd:PRK00095 456 HAAHERLLYEQLKDKLAEVGLASQPLLIPLVLELSEDEADRLEEHKELLARLGLELEPFGPNSFAVREVPALLGQQELEE 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 562 IIKDMIELVLKHKSVDVKKIREdAAIMMSCKKSIKANHYLKNNEMADLIDQLREAEDPFTCPHGRPIIINFSNYELEKLF 641
Cdd:PRK00095 536 LIRDLLDELAEEGDSDTLKERE-LLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIELSLSDLEKLF 614
|
...
gi 488387956 642 KRV 644
Cdd:PRK00095 615 KRI 617
|
|
| MutL |
COG0323 |
DNA mismatch repair ATPase MutL [Replication, recombination and repair]; |
1-643 |
0e+00 |
|
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
Pssm-ID: 440092 [Multi-domain] Cd Length: 515 Bit Score: 738.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 1 MGKIKELETSLANKIAAGEVVERPSSVVKELLENAIDAQATEINIEVEQSGVSSIRVVDNGTGIAQEDLGLVFHRHATSK 80
Cdd:COG0323 1 MPKIRLLPDELANQIAAGEVVERPASVVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLPLAFERHATSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 81 IVADDDLFHIRTLGFRGEALASISSVAKVTLKTCT-DNENGHEIYAEDGKIIHQKPAKAKKGTDIQVESLFYNTPARLKY 159
Cdd:COG0323 81 IRSAEDLFRIRTLGFRGEALASIASVSRLTLTTRTaGAELGTRIEVEGGKVVEVEPAAAPKGTTVEVRDLFFNTPARRKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 160 IKSLYTELGKITDIVNRMAMSHPKIRIALVSDGKTLLSTNGSGRTNEVMAEIYGMKVAKDLVHISGDTSDYHLEGFVAKP 239
Cdd:COG0323 161 LKSDATELAHITDVVRRLALAHPDIAFTLIHNGREVFQLPGAGDLLQRIAAIYGREFAENLLPVEAEREGLRLSGYIGKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 240 EHSRSNKHYISIFINGRYIKNFVLNKAILEGYHTLLTIGRFPICYINIQMDPILVDVNVHPTKLEVRLSKEDQLYDLIVT 319
Cdd:COG0323 241 EFSRSNRDYQYFFVNGRPVRDKLLSHAVREAYRDLLPKGRYPVAVLFLELDPELVDVNVHPTKTEVRFRDEREVYDLVRS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 320 KIREAFKDkilipqndlnrtpkknkvletfeqqkinfekkqsqigetsapyvhdqkdknhdveshrndldstsstnnest 399
Cdd:COG0323 321 AVREALAQ------------------------------------------------------------------------ 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 400 evsnelhnhiddsylqsqkevlfdmeqdtsneyktlnqqsndikgtvsqtphrrvpymEIVGQVHGTYIIAQNENGMFMI 479
Cdd:COG0323 329 ----------------------------------------------------------AALGQLHGTYILAENEDGLVLI 350
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 480 DQHAAQERIKYEYFREKIGEVTNEVQNLLIPLTFHFSKDEQMIIDQYKDELDKVGVHLEHFGGHDYIVNSYPVWFPKVEA 559
Cdd:COG0323 351 DQHAAHERILYERLKKALAEGGVASQPLLIPETLELSPAEAALLEEHLEELARLGFEIEPFGPNTVAVRAVPALLGEGDA 430
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 560 EEIIKDMIELVLKH-KSVDVKKIREDAAIMMSCKKSIKANHYLKNNEMADLIDQLREAEDPFTCPHGRPIIINFSNYELE 638
Cdd:COG0323 431 EELLRDLLDELAEEgSSESLEELREELLATMACHGAIKAGRRLSLEEMNALLRDLEATENPYTCPHGRPTWIELSLEELE 510
|
....*
gi 488387956 639 KLFKR 643
Cdd:COG0323 511 KLFKR 515
|
|
| mutl |
TIGR00585 |
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ... |
2-306 |
1.32e-116 |
|
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: 350.79 E-value: 1.32e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 2 GKIKELETSLANKIAAGEVVERPSSVVKELLENAIDAQATEINIEVEQSGVSSIRVVDNGTGIAQEDLGLVFHRHATSKI 81
Cdd:TIGR00585 1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 82 VADDDLFHIRTLGFRGEALASISSVAKVTLKTCTDNENG--HEIYAEDGKIIHQKPAKAKKGTDIQVESLFYNTPARLKY 159
Cdd:TIGR00585 81 QSFEDLERIETLGFRGEALASISSVSRLTITTKTSAADGlaYQALLEGGMIESIKPAPRPVGTTVEVRDLFYNLPVRRKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 160 IKSLYTELGKITDIVNRMAMSHPKIRIALVSDGKTLL--STNGSGRTNEVMA-EIYGMKVAKDLVHI-SGDTSDYHLEGF 235
Cdd:TIGR00585 161 LKSPKKEFRKILDVLQRYALIHPDISFSLTHDGKKVLqlSTKPNQSTKENRIrSVFGTAVLRKLIPLdEWEDLDLQLEGF 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488387956 236 VAKPEHSRS-NKHYISIFINGRYIKNFVLNKAILEGYHTLLTIGRFPICYINIQMDPILVDVNVHPTKLEVR 306
Cdd:TIGR00585 241 ISQPNVTRSrRSGWQFLFINGRPVELKLLLKAIREVYHEYLPKGQYPVFVLNLEIDPELVDVNVHPDKKEVR 312
|
|
| HATPase_MutL-MLH-PMS-like |
cd16926 |
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ... |
11-196 |
3.80e-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: 298.20 E-value: 3.80e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 11 LANKIAAGEVVERPSSVVKELLENAIDAQATEINIEVEQSGVSSIRVVDNGTGIAQEDLGLVFHRHATSKIVADDDLFHI 90
Cdd:cd16926 1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 91 RTLGFRGEALASISSVAKVTLKTCT-DNENGHEIYAEDGKII-HQKPAKAKKGTDIQVESLFYNTPARLKYIKSLYTELG 168
Cdd:cd16926 81 TTLGFRGEALASIASVSRLTITTRTaDDDVGTRLVVDGGGIIeEVKPAAAPVGTTVTVRDLFYNTPARRKFLKSPKTELS 160
|
170 180
....*....|....*....|....*...
gi 488387956 169 KITDIVNRMAMSHPKIRIALVSDGKTLL 196
Cdd:cd16926 161 KILDLVQRLALAHPDVSFSLTHDGKLVL 188
|
|
| MutL_C |
pfam08676 |
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ... |
460-601 |
4.58e-58 |
|
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: 192.05 E-value: 4.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 460 VGQVHGTYIIAQNENGMFMIDQHAAQERIKYEYFREKIGEVTNEVQNLLIPLTFHFSKDEQMIIDQYKDELDKVGVHLEH 539
Cdd:pfam08676 4 LGQVHGTYILAENEDGLYLIDQHAAHERILYEKLKRALAEGGLAAQPLLIPLVLELSPEEAALLEEHKEELAQLGFELEE 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488387956 540 FGGHDYIVNSYPVWFPKVEAEEIIKDMIELVLKHKSVDVKKIREDAAIMMSCKKSIKANHYL 601
Cdd:pfam08676 84 FGPNSVIVRSVPALLRQQNLQELIRELLDELAEKGGSSLEESLEELLATMACHSAVRAGRRL 145
|
|
| MutL_C |
smart00853 |
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ... |
459-600 |
9.85e-49 |
|
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: 166.76 E-value: 9.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 459 IVGQVHGTYIIAQNENGMFMIDQHAAQERIKYEYFREKigEVTNEVQNLLIPLTFHFSKDEQMIIDQYKDELDKVGVHLE 538
Cdd:smart00853 1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQ--AGGLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELE 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488387956 539 HFGGHDYIVNSYPVWFPKVEAEEIIKDMIELVLKHKSVDVKKIREDAAIMMSCKKSIKANHY 600
Cdd:smart00853 79 IFGPQSLILRSVPALLRQQNLQKLIPELLDLLSDEEENARPSRLEALLASLACRSAIRAGDA 140
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| mutL |
PRK00095 |
DNA mismatch repair endonuclease MutL; |
3-644 |
0e+00 |
|
DNA mismatch repair endonuclease MutL;
Pssm-ID: 234630 [Multi-domain] Cd Length: 617 Bit Score: 823.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 3 KIKELETSLANKIAAGEVVERPSSVVKELLENAIDAQATEINIEVEQSGVSSIRVVDNGTGIAQEDLGLVFHRHATSKIV 82
Cdd:PRK00095 2 PIQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 83 ADDDLFHIRTLGFRGEALASISSVAKVTLKTCTDNEN-GHEIYAEDGKIIHQKPAKAKKGTDIQVESLFYNTPARLKYIK 161
Cdd:PRK00095 82 SLDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADAAeGWQIVYEGGEIVEVKPAAHPVGTTIEVRDLFFNTPARRKFLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 162 SLYTELGKITDIVNRMAMSHPKIRIALVSDGKTLLSTNGSGRTNEVMAEIYGMKVAKDLVHISGDTSDYHLEGFVAKPEH 241
Cdd:PRK00095 162 SEKTELGHIDDVVNRLALAHPDVAFTLTHNGKLVLQTRGAGQLLQRLAAILGREFAENALPIDAEHGDLRLSGYVGLPTL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 242 SRSNKHYISIFINGRYIKNFVLNKAILEGYHTLLTIGRFPICYINIQMDPILVDVNVHPTKLEVRLSKEDQLYDLIVTKI 321
Cdd:PRK00095 242 SRANRDYQYLFVNGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLVHDLIVQAI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 322 REAFKDKILIPQndlnrTPKKNKVLETFEQQKINFEKKQSQIGETSAPYvhdqkdknhdveshrndldstSSTNNESTEV 401
Cdd:PRK00095 322 QEALAQSGLIPA-----AAGANQVLEPAEPEPLPLQQTPLYASGSSPPA---------------------SSPSSAPPEQ 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 402 SNELHNHIDDSYLQSQKEVLFDMEQDTSNEYKTLNQQSNDIKGTVSQTPHRRVPYMEIVGQVHGTYIIAQNENGMFMIDQ 481
Cdd:PRK00095 376 SEESQEESSAEKNPLQPNASQSEAAAAASAEAAAAAPAAAPEPAEAAEEADSFPLGYALGQLHGTYILAENEDGLYLVDQ 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 482 HAAQERIKYEYFREKIGEVTNEVQNLLIPLTFHFSKDEQMIIDQYKDELDKVGVHLEHFGGHDYIVNSYPVWFPKVEAEE 561
Cdd:PRK00095 456 HAAHERLLYEQLKDKLAEVGLASQPLLIPLVLELSEDEADRLEEHKELLARLGLELEPFGPNSFAVREVPALLGQQELEE 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 562 IIKDMIELVLKHKSVDVKKIREdAAIMMSCKKSIKANHYLKNNEMADLIDQLREAEDPFTCPHGRPIIINFSNYELEKLF 641
Cdd:PRK00095 536 LIRDLLDELAEEGDSDTLKERE-LLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIELSLSDLEKLF 614
|
...
gi 488387956 642 KRV 644
Cdd:PRK00095 615 KRI 617
|
|
| MutL |
COG0323 |
DNA mismatch repair ATPase MutL [Replication, recombination and repair]; |
1-643 |
0e+00 |
|
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
Pssm-ID: 440092 [Multi-domain] Cd Length: 515 Bit Score: 738.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 1 MGKIKELETSLANKIAAGEVVERPSSVVKELLENAIDAQATEINIEVEQSGVSSIRVVDNGTGIAQEDLGLVFHRHATSK 80
Cdd:COG0323 1 MPKIRLLPDELANQIAAGEVVERPASVVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLPLAFERHATSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 81 IVADDDLFHIRTLGFRGEALASISSVAKVTLKTCT-DNENGHEIYAEDGKIIHQKPAKAKKGTDIQVESLFYNTPARLKY 159
Cdd:COG0323 81 IRSAEDLFRIRTLGFRGEALASIASVSRLTLTTRTaGAELGTRIEVEGGKVVEVEPAAAPKGTTVEVRDLFFNTPARRKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 160 IKSLYTELGKITDIVNRMAMSHPKIRIALVSDGKTLLSTNGSGRTNEVMAEIYGMKVAKDLVHISGDTSDYHLEGFVAKP 239
Cdd:COG0323 161 LKSDATELAHITDVVRRLALAHPDIAFTLIHNGREVFQLPGAGDLLQRIAAIYGREFAENLLPVEAEREGLRLSGYIGKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 240 EHSRSNKHYISIFINGRYIKNFVLNKAILEGYHTLLTIGRFPICYINIQMDPILVDVNVHPTKLEVRLSKEDQLYDLIVT 319
Cdd:COG0323 241 EFSRSNRDYQYFFVNGRPVRDKLLSHAVREAYRDLLPKGRYPVAVLFLELDPELVDVNVHPTKTEVRFRDEREVYDLVRS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 320 KIREAFKDkilipqndlnrtpkknkvletfeqqkinfekkqsqigetsapyvhdqkdknhdveshrndldstsstnnest 399
Cdd:COG0323 321 AVREALAQ------------------------------------------------------------------------ 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 400 evsnelhnhiddsylqsqkevlfdmeqdtsneyktlnqqsndikgtvsqtphrrvpymEIVGQVHGTYIIAQNENGMFMI 479
Cdd:COG0323 329 ----------------------------------------------------------AALGQLHGTYILAENEDGLVLI 350
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 480 DQHAAQERIKYEYFREKIGEVTNEVQNLLIPLTFHFSKDEQMIIDQYKDELDKVGVHLEHFGGHDYIVNSYPVWFPKVEA 559
Cdd:COG0323 351 DQHAAHERILYERLKKALAEGGVASQPLLIPETLELSPAEAALLEEHLEELARLGFEIEPFGPNTVAVRAVPALLGEGDA 430
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 560 EEIIKDMIELVLKH-KSVDVKKIREDAAIMMSCKKSIKANHYLKNNEMADLIDQLREAEDPFTCPHGRPIIINFSNYELE 638
Cdd:COG0323 431 EELLRDLLDELAEEgSSESLEELREELLATMACHGAIKAGRRLSLEEMNALLRDLEATENPYTCPHGRPTWIELSLEELE 510
|
....*
gi 488387956 639 KLFKR 643
Cdd:COG0323 511 KLFKR 515
|
|
| mutl |
TIGR00585 |
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ... |
2-306 |
1.32e-116 |
|
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: 350.79 E-value: 1.32e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 2 GKIKELETSLANKIAAGEVVERPSSVVKELLENAIDAQATEINIEVEQSGVSSIRVVDNGTGIAQEDLGLVFHRHATSKI 81
Cdd:TIGR00585 1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 82 VADDDLFHIRTLGFRGEALASISSVAKVTLKTCTDNENG--HEIYAEDGKIIHQKPAKAKKGTDIQVESLFYNTPARLKY 159
Cdd:TIGR00585 81 QSFEDLERIETLGFRGEALASISSVSRLTITTKTSAADGlaYQALLEGGMIESIKPAPRPVGTTVEVRDLFYNLPVRRKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 160 IKSLYTELGKITDIVNRMAMSHPKIRIALVSDGKTLL--STNGSGRTNEVMA-EIYGMKVAKDLVHI-SGDTSDYHLEGF 235
Cdd:TIGR00585 161 LKSPKKEFRKILDVLQRYALIHPDISFSLTHDGKKVLqlSTKPNQSTKENRIrSVFGTAVLRKLIPLdEWEDLDLQLEGF 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488387956 236 VAKPEHSRS-NKHYISIFINGRYIKNFVLNKAILEGYHTLLTIGRFPICYINIQMDPILVDVNVHPTKLEVR 306
Cdd:TIGR00585 241 ISQPNVTRSrRSGWQFLFINGRPVELKLLLKAIREVYHEYLPKGQYPVFVLNLEIDPELVDVNVHPDKKEVR 312
|
|
| HATPase_MutL-MLH-PMS-like |
cd16926 |
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ... |
11-196 |
3.80e-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: 298.20 E-value: 3.80e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 11 LANKIAAGEVVERPSSVVKELLENAIDAQATEINIEVEQSGVSSIRVVDNGTGIAQEDLGLVFHRHATSKIVADDDLFHI 90
Cdd:cd16926 1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 91 RTLGFRGEALASISSVAKVTLKTCT-DNENGHEIYAEDGKII-HQKPAKAKKGTDIQVESLFYNTPARLKYIKSLYTELG 168
Cdd:cd16926 81 TTLGFRGEALASIASVSRLTITTRTaDDDVGTRLVVDGGGIIeEVKPAAAPVGTTVTVRDLFYNTPARRKFLKSPKTELS 160
|
170 180
....*....|....*....|....*...
gi 488387956 169 KITDIVNRMAMSHPKIRIALVSDGKTLL 196
Cdd:cd16926 161 KILDLVQRLALAHPDVSFSLTHDGKLVL 188
|
|
| MutL_C |
pfam08676 |
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ... |
460-601 |
4.58e-58 |
|
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: 192.05 E-value: 4.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 460 VGQVHGTYIIAQNENGMFMIDQHAAQERIKYEYFREKIGEVTNEVQNLLIPLTFHFSKDEQMIIDQYKDELDKVGVHLEH 539
Cdd:pfam08676 4 LGQVHGTYILAENEDGLYLIDQHAAHERILYEKLKRALAEGGLAAQPLLIPLVLELSPEEAALLEEHKEELAQLGFELEE 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488387956 540 FGGHDYIVNSYPVWFPKVEAEEIIKDMIELVLKHKSVDVKKIREDAAIMMSCKKSIKANHYL 601
Cdd:pfam08676 84 FGPNSVIVRSVPALLRQQNLQELIRELLDELAEKGGSSLEESLEELLATMACHSAVRAGRRL 145
|
|
| MutL_C |
smart00853 |
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ... |
459-600 |
9.85e-49 |
|
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: 166.76 E-value: 9.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 459 IVGQVHGTYIIAQNENGMFMIDQHAAQERIKYEYFREKigEVTNEVQNLLIPLTFHFSKDEQMIIDQYKDELDKVGVHLE 538
Cdd:smart00853 1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQ--AGGLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELE 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488387956 539 HFGGHDYIVNSYPVWFPKVEAEEIIKDMIELVLKHKSVDVKKIREDAAIMMSCKKSIKANHY 600
Cdd:smart00853 79 IFGPQSLILRSVPALLRQQNLQKLIPELLDLLSDEEENARPSRLEALLASLACRSAIRAGDA 140
|
|
| MutL_Trans |
cd00782 |
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ... |
206-325 |
9.57e-47 |
|
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: 160.78 E-value: 9.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 206 EVMAEIYGMKVAKDLVHISGDTSDYHLEGFVAKPEHSRSNKHYISIFINGRYIKNFVLNKAILEGYHTLLTIGRFPICYI 285
Cdd:cd00782 3 DRIAQVYGKEVAKNLIEVELESGDFRISGYISKPDFGRSSKDRQFLFVNGRPVRDKLLSKAINEAYRSYLPKGRYPVFVL 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 488387956 286 NIQMDPILVDVNVHPTKLEVRLSKEDQLYDLIVTKIREAF 325
Cdd:cd00782 83 NLELPPELVDVNVHPTKREVRFSDEEEVLELIREALRSAL 122
|
|
| DNA_mis_repair |
pfam01119 |
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ... |
209-324 |
2.39e-46 |
|
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: 159.59 E-value: 2.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 209 AEIYGMKVAKDLVHISGDTSDYHLEGFVAKPEHSRSNKHYISIFINGRYIKNFVLNKAILEGYHTLLTIGRFPICYINIQ 288
Cdd:pfam01119 1 AAIYGKEFAENLLPIEKEDDGLRLSGYISKPTLSRSNRDYQYLFVNGRPVRDKLLSHAIREAYRDLLPKGRYPVAVLFLE 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 488387956 289 MDPILVDVNVHPTKLEVRLSKEDQLYDLIVTKIREA 324
Cdd:pfam01119 81 IDPELVDVNVHPTKREVRFRDEREVYDFIKEALREA 116
|
|
| TopoII_MutL_Trans |
cd00329 |
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ... |
206-306 |
7.63e-28 |
|
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: 107.73 E-value: 7.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 206 EVMAEIYGMKVAKDLVHISGDTSDYHLEGFVAKPEHSRSNKHYISIFINGRYI-KNFVLNKAILEGYHTLLT---IGRFP 281
Cdd:cd00329 3 DRLAEILGDKVADKLIYVEGESDGFRVEGAISYPDSGRSSKDRQFSFVNGRPVrEGGTHVKAVREAYTRALNgddVRRYP 82
|
90 100
....*....|....*....|....*
gi 488387956 282 ICYINIQMDPILVDVNVHPTKLEVR 306
Cdd:cd00329 83 VAVLSLKIPPSLVDVNVHPTKEEVR 107
|
|
| MutL_Trans_MutL |
cd03482 |
MutL_Trans_MutL: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
208-326 |
5.58e-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: 91.49 E-value: 5.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 208 MAEIYGMKVAKDLVHISGDTSDYHLEGFVAKPEHSRSNKHYISIFINGRYIKNFVLNKAILEGYHTLLTIGRFPICYINI 287
Cdd:cd03482 5 LADILGEDFAEQALAIDEEAGGLRLSGWIALPTFARSQADIQYFYVNGRMVRDKLISHAVRQAYSDVLHGGRHPAYVLYL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 488387956 288 QMDPILVDVNVHPTKLEVRLSKEDQLYDLIVTKIREAFK 326
Cdd:cd03482 85 ELDPAQVDVNVHPAKHEVRFRDSRLVHDFIYHAVKKALA 123
|
|
| MutL_Trans_MLH1 |
cd03483 |
MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
211-330 |
1.19e-15 |
|
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: 73.81 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 211 IYGMKVAKDLVHISGDTSDYHL----EGFVAKPEHSRSNKHYIsIFINGRYIKNFVLNKAILEGYHTLLTIGRFPICYIN 286
Cdd:cd03483 9 VYGAAVANELIEVEISDDDDDLgfkvKGLISNANYSKKKIIFI-LFINNRLVECSALRRAIENVYANYLPKGAHPFVYLS 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 488387956 287 IQMDPILVDVNVHPTKLEVRLSKEDQlydlIVTKIREAFKDKIL 330
Cdd:cd03483 88 LEIPPENVDVNVHPTKREVHFLNEEE----IIERIQKLVEDKLS 127
|
|
| MutL_Trans_hPMS_2_like |
cd03484 |
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
206-325 |
8.32e-10 |
|
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: 57.28 E-value: 8.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 206 EVMAEIYGMKVAKDL--VHISGD---------------TSDYHLEGFVAKPEH--SRSNKHYISIFINGRYIKNFVLNKA 266
Cdd:cd03484 4 DNIINVFGGKVIKGLipINLELDvnptkeeldsdedlaDSEVKITGYISKPSHgcGRSSSDRQFFYINGRPVDLKKVAKL 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 488387956 267 ILEGYHTLLTIgRFPICYINIQMDPILVDVNVHPTKLEVRLSKEDQLYDLIVTKIREAF 325
Cdd:cd03484 84 INEVYKSFNSR-QYPFFILNISLPTSLYDVNVTPDKRTVLLHDEDRLIDTLKTSLSELF 141
|
|
| HATPase_c |
pfam02518 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
27-82 |
1.73e-08 |
|
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: 52.76 E-value: 1.73e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 488387956 27 VVKELLENAID--AQATEINIEVEQSGVSSIRVVDNGTGIAQEDLGLVFHRHATSKIV 82
Cdd:pfam02518 9 VLSNLLDNALKhaAKAGEITVTLSEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKR 66
|
|
| HATPase_c_3 |
pfam13589 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ... |
26-118 |
2.93e-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: 52.72 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 26 SVVKELLENAIDAQATEINIEVEQ--SGVSSIRVVDNGTGIAQEDLGLVFHRHATSKivadDDLFHIRTLGFRG--EALA 101
Cdd:pfam13589 3 GALAELIDNSIDADATNIKIEVNKnrGGGTEIVIEDDGHGMSPEELINALRLATSAK----EAKRGSTDLGRYGigLKLA 78
|
90
....*....|....*..
gi 488387956 102 SISSVAKVTLKTCTDNE 118
Cdd:pfam13589 79 SLSLGAKLTVTSKKEGK 95
|
|
| HATPase_c |
smart00387 |
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
27-75 |
5.11e-07 |
|
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 48.41 E-value: 5.11e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 488387956 27 VVKELLENAIDA--QATEINIEVEQSGVS-SIRVVDNGTGIAQEDLGLVFHR 75
Cdd:smart00387 9 VLSNLLDNAIKYtpEGGRITVTLERDGDHvEITVEDNGPGIPPEDLEKIFEP 60
|
|
| MutL_Trans_hPMS_1_like |
cd03485 |
MutL_Trans_hPMS1_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
209-323 |
2.04e-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: 47.26 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 209 AEIYGMKVAKDLVHISGDTSD--YHLEGFVAKPE--HSRSNKHYISIFINGRYIKnfvLNKAI-------LEGYHTLLTI 277
Cdd:cd03485 7 ARVLGTAVAANMVPVQSTDEDpqISLEGFLPKPGsdVSKTKSDGKFISVNSRPVS---LGKDIgkllrqyYSSAYRKSSL 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 488387956 278 GRFPICYINIQMDPILVDVNVHPTKLEVRLSKEDQLYDLIVTKIRE 323
Cdd:cd03485 84 RRYPVFFLNILCPPGLVDVNIEPDKDDVLLQNKEAVLQAVENLLES 129
|
|
| BaeS |
COG0642 |
Signal transduction histidine kinase [Signal transduction mechanisms]; |
27-80 |
2.06e-05 |
|
Signal transduction histidine kinase [Signal transduction mechanisms];
Pssm-ID: 440407 [Multi-domain] Cd Length: 328 Bit Score: 47.21 E-value: 2.06e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 488387956 27 VVKELLENAIDA--QATEINIEVEQSGVS-SIRVVDNGTGIAQEDLGLVFHRHATSK 80
Cdd:COG0642 227 VLLNLLSNAIKYtpEGGTVTVSVRREGDRvRISVEDTGPGIPPEDLERIFEPFFRTD 283
|
|
| KdpD |
COG2205 |
K+-sensing histidine kinase KdpD [Signal transduction mechanisms]; |
27-80 |
8.64e-05 |
|
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
Pssm-ID: 441807 [Multi-domain] Cd Length: 239 Bit Score: 44.51 E-value: 8.64e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 488387956 27 VVKELLENAIDA--QATEINIEVEQSGVS-SIRVVDNGTGIAQEDLGLVFHRHATSK 80
Cdd:COG2205 136 VLANLLDNAIKYspPGGTITISARREGDGvRISVSDNGPGIPEEELERIFERFYRGD 192
|
|
| HATPase_BasS-like |
cd16940 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
25-75 |
2.73e-04 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BasS HK of the BasS-BasR two-component regulatory system (TCS). Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some contain a HAMP sensory domain, while some an N-terminal two-component sensor kinase domain.
Pssm-ID: 340417 [Multi-domain] Cd Length: 113 Bit Score: 40.85 E-value: 2.73e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 488387956 25 SSVVKELLENAI--DAQATEINIEVEQSGVSSIRVVDNGTGIAQEDLGLVFHR 75
Cdd:cd16940 15 FLLLRNLVDNAVrySPQGSRVEIKLSADDGAVIRVEDNGPGIDEEELEALFER 67
|
|
| HATPase_HupT_MifS-like |
cd16976 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
27-82 |
6.90e-04 |
|
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: 39.36 E-value: 6.90e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488387956 27 VVKELLENAIDA----QATEINIEVE-QSGVSSIRVVDNGTGIAQEDLGLVFHRHATSKIV 82
Cdd:cd16976 4 VLMNLLQNALDAmgkvENPRIRIAARrLGGRLVLVVRDNGPGIAEEHLSRVFDPFFTTKPV 64
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
31-80 |
7.08e-04 |
|
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];
Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 42.64 E-value: 7.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 488387956 31 LLENAIDAQATEINIEVE---QSGVSSIRVVDNGTGIAQEDLGLVFHRHATSK 80
Cdd:COG5000 325 LLKNAIEAIEEGGEIEVStrrEDGRVRIEVSDNGPGIPEEVLERIFEPFFTTK 377
|
|
| HATPase_TopVIB-like |
cd16933 |
Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family ... |
27-75 |
7.74e-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: 7.74e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 488387956 27 VVKELLENAIDAQAT-----EINIEVEQSGVS--SIRVVDNGTGIAQEDLGLVFHR 75
Cdd:cd16933 23 TVRELVENSLDATEEagilpDIKVEIEEIGKDhyKVIVEDNGPGIPEEQIPKVFGK 78
|
|
| PRK04184 |
PRK04184 |
DNA topoisomerase VI subunit B; Validated |
27-195 |
1.34e-03 |
|
DNA topoisomerase VI subunit B; Validated
Pssm-ID: 235246 [Multi-domain] Cd Length: 535 Bit Score: 41.80 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 27 VVKELLENAIDAqaTE-------INIEV----EQSGVSSIRVVDNGTGIAQEDLGLVFHRH-ATSKivadddlFHIRT-- 92
Cdd:PRK04184 40 TVKELVDNSLDA--CEeagilpdIKIEIkrvdEGKDHYRVTVEDNGPGIPPEEIPKVFGKLlYGSK-------FHNLRqs 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 93 -----LGFRGEALASISSVAK-VTLKTCTDNENgHEIYAE--------DGKII--HQKPAKAKKGTDIQVEslFYNTPAR 156
Cdd:PRK04184 111 rgqqgIGISAAVLYAQMTTGKpVRVISSTGGSK-KAYYFElkidtkknEPIILerEEVDWDRWHGTRVELE--IEGDWYR 187
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488387956 157 LKyiKSLYTELgKITDIVNrmamshPKIRIALVS-DGKTL 195
Cdd:PRK04184 188 AK--QRIYEYL-KRTAIVN------PHARITFKDpDGEIL 218
|
|
| CitA |
COG3290 |
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ... |
26-80 |
1.70e-03 |
|
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];
Pssm-ID: 442519 [Multi-domain] Cd Length: 389 Bit Score: 41.37 E-value: 1.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488387956 26 SVVKELLENAIDAQAT------EINIEVEQSG-VSSIRVVDNGTGIAQEDLGLVFHRHATSK 80
Cdd:COG3290 284 TILGNLLDNAIEAVEKlpeeerRVELSIRDDGdELVIEVEDSGPGIPEELLEKIFERGFSTK 345
|
|
| COG4191 |
COG4191 |
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ... |
31-73 |
2.59e-03 |
|
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];
Pssm-ID: 443345 [Multi-domain] Cd Length: 361 Bit Score: 40.55 E-value: 2.59e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 488387956 31 LLENAIDA----QATEINIEVEQSG--VSsIRVVDNGTGIAQEDLGLVF 73
Cdd:COG4191 264 LLINAIDAmeegEGGRITISTRREGdyVV-ISVRDNGPGIPPEVLERIF 311
|
|
| MutL_Trans_MLH3 |
cd03486 |
MutL_Trans_MLH3: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
211-326 |
6.82e-03 |
|
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: 37.30 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488387956 211 IYGMKVAKDLVHISGDTSDYHLEGFVAKPEHsrSNKHYISIFINGRYIKNFVLNKAILEGYHTLLTIG------------ 278
Cdd:cd03486 9 IYGLVLAQKLKEVSAKFQEYEVSGYISSEGH--YSKSFQFIYVNGRLYLKTRFHKLINKLFRKTSAVAknksspqskssr 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 488387956 279 -------RFPICYINIQMDPILVDVNVHPTKLEVRLSKedqlYDLIVTKIREAFK 326
Cdd:cd03486 87 rgkrsqeSYPVFVLNITCPASEYDLSQEPSKTIIEFKD----WKTLLPLILEVVK 137
|
|
| ComP |
COG4585 |
Signal transduction histidine kinase ComP [Signal transduction mechanisms]; |
27-72 |
9.49e-03 |
|
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
Pssm-ID: 443642 [Multi-domain] Cd Length: 252 Bit Score: 38.45 E-value: 9.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 488387956 27 VVKELLENAID-AQATEINIEVEQSGVS-SIRVVDNGTGIAQED-----LGLV 72
Cdd:COG4585 166 IVQEALTNALKhAGATRVTVTLEVDDGElTLTVRDDGVGFDPEAapgggLGLR 218
|
|
| |
