|
Name |
Accession |
Description |
Interval |
E-value |
| mutL |
PRK00095 |
DNA mismatch repair endonuclease MutL; |
4-647 |
0e+00 |
|
DNA mismatch repair endonuclease MutL;
Pssm-ID: 234630 [Multi-domain] Cd Length: 617 Bit Score: 847.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 4 IIELPEVLANQIAAGEVVERPASVVKELVENAIDAKSSQITVEIEESGLKMIQVTDNGEGMSHEDLPLSLRRHATSKIKS 83
Cdd:PRK00095 3 IQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKIAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 84 QSDLFRIRTLGFRGEALPSVASISKITIKTATKEVTHGSLLIATGGEIETLEAISTPTGTKIKVENLFYNTPARLKYMKS 163
Cdd:PRK00095 83 LDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADAAEGWQIVYEGGEIVEVKPAAHPVGTTIEVRDLFFNTPARRKFLKS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 164 LQAELAHIVDVVNRLSLAHPEVAFTLISDGRQLTQTSGTGDLRQAIAGIYGLNTTKKMLAISNADLDFEVSGYVSLPELT 243
Cdd:PRK00095 163 EKTELGHIDDVVNRLALAHPDVAFTLTHNGKLVLQTRGAGQLLQRLAAILGREFAENALPIDAEHGDLRLSGYVGLPTLS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 244 RANRNYMTILVNGRYIKNFLLNRAILDGYGSKLMVGRFPIVVIDIQIDPYLADVNVHPTKQEVRISKERELMALISTAIS 323
Cdd:PRK00095 243 RANRDYQYLFVNGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLVHDLIVQAIQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 324 ESLKEQDLIPDalenlAKSSTRHFSKPEQTQLPLQSRGLYYDPQKNDFFVKESAVSEKIPETDFYFGTVDNSvkvekael 403
Cdd:PRK00095 323 EALAQSGLIPA-----AAGANQVLEPAEPEPLPLQQTPLYASGSSPPASSPSSAPPEQSEESQEESSAEKNP-------- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 404 lphseevigpssvkhASRPQNTFTETDHPNLDLKNRQKLSQMLTRLENEEQSVFPELDYFGQMHGTYLFAQGKDGLFIID 483
Cdd:PRK00095 390 ---------------LQPNASQSEAAAAASAEAAAAAPAAAPEPAEAAEEADSFPLGYALGQLHGTYILAENEDGLYLVD 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 484 QHAAQERVKYEYYRDKIGEVDSSLQQLLVPYLFEFSGSDFINLQEKMALLNEVGIFLEVYGHNTFILREHPIWMKEEEIA 563
Cdd:PRK00095 455 QHAAHERLLYEQLKDKLAEVGLASQPLLIPLVLELSEDEADRLEEHKELLARLGLELEPFGPNSFAVREVPALLGQQELE 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 564 SGVYEMCDMLLLTNEVSIKTYRaELAIMMSCKRSIKANHSLDDYSARNLLLQLAQCQNPYNCPHGRPVLINFSKADMEKM 643
Cdd:PRK00095 535 ELIRDLLDELAEEGDSDTLKER-ELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIELSLSDLEKL 613
|
....
gi 489082266 644 FRRI 647
Cdd:PRK00095 614 FKRI 617
|
|
| MutL |
COG0323 |
DNA mismatch repair ATPase MutL [Replication, recombination and repair]; |
1-646 |
0e+00 |
|
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
Pssm-ID: 440092 [Multi-domain] Cd Length: 515 Bit Score: 727.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 1 MTNIIELPEVLANQIAAGEVVERPASVVKELVENAIDAKSSQITVEIEESGLKMIQVTDNGEGMSHEDLPLSLRRHATSK 80
Cdd:COG0323 1 MPKIRLLPDELANQIAAGEVVERPASVVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLPLAFERHATSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 81 IKSQSDLFRIRTLGFRGEALPSVASISKITIKTATKEVTHGSLLIATGGEIETLEAISTPTGTKIKVENLFYNTPARLKY 160
Cdd:COG0323 81 IRSAEDLFRIRTLGFRGEALASIASVSRLTLTTRTAGAELGTRIEVEGGKVVEVEPAAAPKGTTVEVRDLFFNTPARRKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 161 MKSLQAELAHIVDVVNRLSLAHPEVAFTLISDGRQLTQTSGTGDLRQAIAGIYGLNTTKKMLAISNADLDFEVSGYVSLP 240
Cdd:COG0323 161 LKSDATELAHITDVVRRLALAHPDIAFTLIHNGREVFQLPGAGDLLQRIAAIYGREFAENLLPVEAEREGLRLSGYIGKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 241 ELTRANRNYMTILVNGRYIKNFLLNRAILDGYGSKLMVGRFPIVVIDIQIDPYLADVNVHPTKQEVRISKERELMALIST 320
Cdd:COG0323 241 EFSRSNRDYQYFFVNGRPVRDKLLSHAVREAYRDLLPKGRYPVAVLFLELDPELVDVNVHPTKTEVRFRDEREVYDLVRS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 321 AISESLKEQdlipdalenlaksstrhfskpeqtqlplqsrglyydpqkndffvkesavsekipetdfyfgtvdnsvkvek 400
Cdd:COG0323 321 AVREALAQA----------------------------------------------------------------------- 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 401 aellphseevigpssvkhasrpqntftetdhpnldlknrqklsqmltrleneeqsvfpeldYFGQMHGTYLFAQGKDGLF 480
Cdd:COG0323 330 -------------------------------------------------------------ALGQLHGTYILAENEDGLV 348
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 481 IIDQHAAQERVKYEYYRDKIGEVDSSLQQLLVPYLFEFSGSDFINLQEKMALLNEVGIFLEVYGHNTFILREHPIWMKEE 560
Cdd:COG0323 349 LIDQHAAHERILYERLKKALAEGGVASQPLLIPETLELSPAEAALLEEHLEELARLGFEIEPFGPNTVAVRAVPALLGEG 428
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 561 EIASGVYEMCDMLLLTNE-VSIKTYRAELAIMMSCKRSIKANHSLDDYSARNLLLQLAQCQNPYNCPHGRPVLINFSKAD 639
Cdd:COG0323 429 DAEELLRDLLDELAEEGSsESLEELREELLATMACHGAIKAGRRLSLEEMNALLRDLEATENPYTCPHGRPTWIELSLEE 508
|
....*..
gi 489082266 640 MEKMFRR 646
Cdd:COG0323 509 LEKLFKR 515
|
|
| mutl |
TIGR00585 |
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ... |
4-307 |
6.83e-123 |
|
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: 367.35 E-value: 6.83e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 4 IIELPEVLANQIAAGEVVERPASVVKELVENAIDAKSSQITVEIEESGLKMIQVTDNGEGMSHEDLPLSLRRHATSKIKS 83
Cdd:TIGR00585 3 IKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKIQS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 84 QSDLFRIRTLGFRGEALPSVASISKITIKTAT-KEVTHGSLLIATGGEIETLEAISTPTGTKIKVENLFYNTPARLKYMK 162
Cdd:TIGR00585 83 FEDLERIETLGFRGEALASISSVSRLTITTKTsAADGLAYQALLEGGMIESIKPAPRPVGTTVEVRDLFYNLPVRRKFLK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 163 SLQAELAHIVDVVNRLSLAHPEVAFTLISDGRQLTQTSG--TGDLRQA-IAGIYGL-NTTKKMLAISNADLDFEVSGYVS 238
Cdd:TIGR00585 163 SPKKEFRKILDVLQRYALIHPDISFSLTHDGKKVLQLSTkpNQSTKENrIRSVFGTaVLRKLIPLDEWEDLDLQLEGFIS 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 239 LPELTRANRNYMTIL-VNGRYIKNFLLNRAILDGYGSKLMVGRFPIVVIDIQIDPYLADVNVHPTKQEVR 307
Cdd:TIGR00585 243 QPNVTRSRRSGWQFLfINGRPVELKLLLKAIREVYHEYLPKGQYPVFVLNLEIDPELVDVNVHPDKKEVR 312
|
|
| HATPase_MutL-MLH-PMS-like |
cd16926 |
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ... |
11-197 |
5.34e-105 |
|
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: 316.30 E-value: 5.34e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 11 LANQIAAGEVVERPASVVKELVENAIDAKSSQITVEIEESGLKMIQVTDNGEGMSHEDLPLSLRRHATSKIKSQSDLFRI 90
Cdd:cd16926 1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 91 RTLGFRGEALPSVASISKITIKTATKEVTHG-SLLIATGGEIETLEAISTPTGTKIKVENLFYNTPARLKYMKSLQAELA 169
Cdd:cd16926 81 TTLGFRGEALASIASVSRLTITTRTADDDVGtRLVVDGGGIIEEVKPAAAPVGTTVTVRDLFYNTPARRKFLKSPKTELS 160
|
170 180
....*....|....*....|....*...
gi 489082266 170 HIVDVVNRLSLAHPEVAFTLISDGRQLT 197
Cdd:cd16926 161 KILDLVQRLALAHPDVSFSLTHDGKLVL 188
|
|
| MutL_C |
pfam08676 |
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ... |
464-604 |
1.36e-46 |
|
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: 161.23 E-value: 1.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 464 GQMHGTYLFAQGKDGLFIIDQHAAQERVKYEYYRDKIGEVDSSLQQLLVPYLFEFSGSDFINLQEKMALLNEVGIFLEVY 543
Cdd:pfam08676 5 GQVHGTYILAENEDGLYLIDQHAAHERILYEKLKRALAEGGLAAQPLLIPLVLELSPEEAALLEEHKEELAQLGFELEEF 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489082266 544 GHNTFILREHPIWMKEEEIASGVYEMCDMLLLTNEVSIKTYRAELAIMMSCKRSIKANHSL 604
Cdd:pfam08676 85 GPNSVIVRSVPALLRQQNLQELIRELLDELAEKGGSSLEESLEELLATMACHSAVRAGRRL 145
|
|
| MutL_C |
smart00853 |
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ... |
462-602 |
3.54e-41 |
|
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: 146.35 E-value: 3.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 462 YFGQMHGTYLFAQGKDGLFIIDQHAAQERVKYEYYRDKIGEVDSslQQLLVPYLFEFSGSDFINLQEKMALLNEVGIFLE 541
Cdd:smart00853 1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQAGGLES--QPLLIPVRLELSPQEAALLEEHLELLRQLGFELE 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489082266 542 VYGHNTFILREHPIWMKEEEIASGVYEMCDMLLLTNEVSIKTYRAELAIMMSCKRSIKANH 602
Cdd:smart00853 79 IFGPQSLILRSVPALLRQQNLQKLIPELLDLLSDEEENARPSRLEALLASLACRSAIRAGD 139
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| mutL |
PRK00095 |
DNA mismatch repair endonuclease MutL; |
4-647 |
0e+00 |
|
DNA mismatch repair endonuclease MutL;
Pssm-ID: 234630 [Multi-domain] Cd Length: 617 Bit Score: 847.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 4 IIELPEVLANQIAAGEVVERPASVVKELVENAIDAKSSQITVEIEESGLKMIQVTDNGEGMSHEDLPLSLRRHATSKIKS 83
Cdd:PRK00095 3 IQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKIAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 84 QSDLFRIRTLGFRGEALPSVASISKITIKTATKEVTHGSLLIATGGEIETLEAISTPTGTKIKVENLFYNTPARLKYMKS 163
Cdd:PRK00095 83 LDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADAAEGWQIVYEGGEIVEVKPAAHPVGTTIEVRDLFFNTPARRKFLKS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 164 LQAELAHIVDVVNRLSLAHPEVAFTLISDGRQLTQTSGTGDLRQAIAGIYGLNTTKKMLAISNADLDFEVSGYVSLPELT 243
Cdd:PRK00095 163 EKTELGHIDDVVNRLALAHPDVAFTLTHNGKLVLQTRGAGQLLQRLAAILGREFAENALPIDAEHGDLRLSGYVGLPTLS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 244 RANRNYMTILVNGRYIKNFLLNRAILDGYGSKLMVGRFPIVVIDIQIDPYLADVNVHPTKQEVRISKERELMALISTAIS 323
Cdd:PRK00095 243 RANRDYQYLFVNGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLVHDLIVQAIQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 324 ESLKEQDLIPDalenlAKSSTRHFSKPEQTQLPLQSRGLYYDPQKNDFFVKESAVSEKIPETDFYFGTVDNSvkvekael 403
Cdd:PRK00095 323 EALAQSGLIPA-----AAGANQVLEPAEPEPLPLQQTPLYASGSSPPASSPSSAPPEQSEESQEESSAEKNP-------- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 404 lphseevigpssvkhASRPQNTFTETDHPNLDLKNRQKLSQMLTRLENEEQSVFPELDYFGQMHGTYLFAQGKDGLFIID 483
Cdd:PRK00095 390 ---------------LQPNASQSEAAAAASAEAAAAAPAAAPEPAEAAEEADSFPLGYALGQLHGTYILAENEDGLYLVD 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 484 QHAAQERVKYEYYRDKIGEVDSSLQQLLVPYLFEFSGSDFINLQEKMALLNEVGIFLEVYGHNTFILREHPIWMKEEEIA 563
Cdd:PRK00095 455 QHAAHERLLYEQLKDKLAEVGLASQPLLIPLVLELSEDEADRLEEHKELLARLGLELEPFGPNSFAVREVPALLGQQELE 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 564 SGVYEMCDMLLLTNEVSIKTYRaELAIMMSCKRSIKANHSLDDYSARNLLLQLAQCQNPYNCPHGRPVLINFSKADMEKM 643
Cdd:PRK00095 535 ELIRDLLDELAEEGDSDTLKER-ELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIELSLSDLEKL 613
|
....
gi 489082266 644 FRRI 647
Cdd:PRK00095 614 FKRI 617
|
|
| MutL |
COG0323 |
DNA mismatch repair ATPase MutL [Replication, recombination and repair]; |
1-646 |
0e+00 |
|
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
Pssm-ID: 440092 [Multi-domain] Cd Length: 515 Bit Score: 727.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 1 MTNIIELPEVLANQIAAGEVVERPASVVKELVENAIDAKSSQITVEIEESGLKMIQVTDNGEGMSHEDLPLSLRRHATSK 80
Cdd:COG0323 1 MPKIRLLPDELANQIAAGEVVERPASVVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLPLAFERHATSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 81 IKSQSDLFRIRTLGFRGEALPSVASISKITIKTATKEVTHGSLLIATGGEIETLEAISTPTGTKIKVENLFYNTPARLKY 160
Cdd:COG0323 81 IRSAEDLFRIRTLGFRGEALASIASVSRLTLTTRTAGAELGTRIEVEGGKVVEVEPAAAPKGTTVEVRDLFFNTPARRKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 161 MKSLQAELAHIVDVVNRLSLAHPEVAFTLISDGRQLTQTSGTGDLRQAIAGIYGLNTTKKMLAISNADLDFEVSGYVSLP 240
Cdd:COG0323 161 LKSDATELAHITDVVRRLALAHPDIAFTLIHNGREVFQLPGAGDLLQRIAAIYGREFAENLLPVEAEREGLRLSGYIGKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 241 ELTRANRNYMTILVNGRYIKNFLLNRAILDGYGSKLMVGRFPIVVIDIQIDPYLADVNVHPTKQEVRISKERELMALIST 320
Cdd:COG0323 241 EFSRSNRDYQYFFVNGRPVRDKLLSHAVREAYRDLLPKGRYPVAVLFLELDPELVDVNVHPTKTEVRFRDEREVYDLVRS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 321 AISESLKEQdlipdalenlaksstrhfskpeqtqlplqsrglyydpqkndffvkesavsekipetdfyfgtvdnsvkvek 400
Cdd:COG0323 321 AVREALAQA----------------------------------------------------------------------- 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 401 aellphseevigpssvkhasrpqntftetdhpnldlknrqklsqmltrleneeqsvfpeldYFGQMHGTYLFAQGKDGLF 480
Cdd:COG0323 330 -------------------------------------------------------------ALGQLHGTYILAENEDGLV 348
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 481 IIDQHAAQERVKYEYYRDKIGEVDSSLQQLLVPYLFEFSGSDFINLQEKMALLNEVGIFLEVYGHNTFILREHPIWMKEE 560
Cdd:COG0323 349 LIDQHAAHERILYERLKKALAEGGVASQPLLIPETLELSPAEAALLEEHLEELARLGFEIEPFGPNTVAVRAVPALLGEG 428
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 561 EIASGVYEMCDMLLLTNE-VSIKTYRAELAIMMSCKRSIKANHSLDDYSARNLLLQLAQCQNPYNCPHGRPVLINFSKAD 639
Cdd:COG0323 429 DAEELLRDLLDELAEEGSsESLEELREELLATMACHGAIKAGRRLSLEEMNALLRDLEATENPYTCPHGRPTWIELSLEE 508
|
....*..
gi 489082266 640 MEKMFRR 646
Cdd:COG0323 509 LEKLFKR 515
|
|
| mutl |
TIGR00585 |
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ... |
4-307 |
6.83e-123 |
|
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: 367.35 E-value: 6.83e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 4 IIELPEVLANQIAAGEVVERPASVVKELVENAIDAKSSQITVEIEESGLKMIQVTDNGEGMSHEDLPLSLRRHATSKIKS 83
Cdd:TIGR00585 3 IKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKIQS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 84 QSDLFRIRTLGFRGEALPSVASISKITIKTAT-KEVTHGSLLIATGGEIETLEAISTPTGTKIKVENLFYNTPARLKYMK 162
Cdd:TIGR00585 83 FEDLERIETLGFRGEALASISSVSRLTITTKTsAADGLAYQALLEGGMIESIKPAPRPVGTTVEVRDLFYNLPVRRKFLK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 163 SLQAELAHIVDVVNRLSLAHPEVAFTLISDGRQLTQTSG--TGDLRQA-IAGIYGL-NTTKKMLAISNADLDFEVSGYVS 238
Cdd:TIGR00585 163 SPKKEFRKILDVLQRYALIHPDISFSLTHDGKKVLQLSTkpNQSTKENrIRSVFGTaVLRKLIPLDEWEDLDLQLEGFIS 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 239 LPELTRANRNYMTIL-VNGRYIKNFLLNRAILDGYGSKLMVGRFPIVVIDIQIDPYLADVNVHPTKQEVR 307
Cdd:TIGR00585 243 QPNVTRSRRSGWQFLfINGRPVELKLLLKAIREVYHEYLPKGQYPVFVLNLEIDPELVDVNVHPDKKEVR 312
|
|
| HATPase_MutL-MLH-PMS-like |
cd16926 |
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ... |
11-197 |
5.34e-105 |
|
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: 316.30 E-value: 5.34e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 11 LANQIAAGEVVERPASVVKELVENAIDAKSSQITVEIEESGLKMIQVTDNGEGMSHEDLPLSLRRHATSKIKSQSDLFRI 90
Cdd:cd16926 1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 91 RTLGFRGEALPSVASISKITIKTATKEVTHG-SLLIATGGEIETLEAISTPTGTKIKVENLFYNTPARLKYMKSLQAELA 169
Cdd:cd16926 81 TTLGFRGEALASIASVSRLTITTRTADDDVGtRLVVDGGGIIEEVKPAAAPVGTTVTVRDLFYNTPARRKFLKSPKTELS 160
|
170 180
....*....|....*....|....*...
gi 489082266 170 HIVDVVNRLSLAHPEVAFTLISDGRQLT 197
Cdd:cd16926 161 KILDLVQRLALAHPDVSFSLTHDGKLVL 188
|
|
| MutL_C |
pfam08676 |
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ... |
464-604 |
1.36e-46 |
|
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: 161.23 E-value: 1.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 464 GQMHGTYLFAQGKDGLFIIDQHAAQERVKYEYYRDKIGEVDSSLQQLLVPYLFEFSGSDFINLQEKMALLNEVGIFLEVY 543
Cdd:pfam08676 5 GQVHGTYILAENEDGLYLIDQHAAHERILYEKLKRALAEGGLAAQPLLIPLVLELSPEEAALLEEHKEELAQLGFELEEF 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489082266 544 GHNTFILREHPIWMKEEEIASGVYEMCDMLLLTNEVSIKTYRAELAIMMSCKRSIKANHSL 604
Cdd:pfam08676 85 GPNSVIVRSVPALLRQQNLQELIRELLDELAEKGGSSLEESLEELLATMACHSAVRAGRRL 145
|
|
| DNA_mis_repair |
pfam01119 |
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ... |
210-326 |
4.03e-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: 159.20 E-value: 4.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 210 AGIYGLNTTKKMLAISNADLDFEVSGYVSLPELTRANRNYMTILVNGRYIKNFLLNRAILDGYGSKLMVGRFPIVVIDIQ 289
Cdd:pfam01119 1 AAIYGKEFAENLLPIEKEDDGLRLSGYISKPTLSRSNRDYQYLFVNGRPVRDKLLSHAIREAYRDLLPKGRYPVAVLFLE 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 489082266 290 IDPYLADVNVHPTKQEVRISKERELMALISTAISESL 326
Cdd:pfam01119 81 IDPELVDVNVHPTKREVRFRDEREVYDFIKEALREAL 117
|
|
| MutL_Trans |
cd00782 |
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ... |
205-326 |
1.44e-45 |
|
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: 157.70 E-value: 1.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 205 LRQAIAGIYGLNTTKKMLAISNADLDFEVSGYVSLPELTRANRNYMTILVNGRYIKNFLLNRAILDGYGSKLMVGRFPIV 284
Cdd:cd00782 1 LKDRIAQVYGKEVAKNLIEVELESGDFRISGYISKPDFGRSSKDRQFLFVNGRPVRDKLLSKAINEAYRSYLPKGRYPVF 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 489082266 285 VIDIQIDPYLADVNVHPTKQEVRISKERELMALISTAISESL 326
Cdd:cd00782 81 VLNLELPPELVDVNVHPTKREVRFSDEEEVLELIREALRSAL 122
|
|
| MutL_C |
smart00853 |
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ... |
462-602 |
3.54e-41 |
|
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: 146.35 E-value: 3.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 462 YFGQMHGTYLFAQGKDGLFIIDQHAAQERVKYEYYRDKIGEVDSslQQLLVPYLFEFSGSDFINLQEKMALLNEVGIFLE 541
Cdd:smart00853 1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLKQAGGLES--QPLLIPVRLELSPQEAALLEEHLELLRQLGFELE 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489082266 542 VYGHNTFILREHPIWMKEEEIASGVYEMCDMLLLTNEVSIKTYRAELAIMMSCKRSIKANH 602
Cdd:smart00853 79 IFGPQSLILRSVPALLRQQNLQKLIPELLDLLSDEEENARPSRLEALLASLACRSAIRAGD 139
|
|
| TopoII_MutL_Trans |
cd00329 |
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ... |
205-307 |
5.00e-25 |
|
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: 99.64 E-value: 5.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 205 LRQAIAGIYGLNTTKKMLAISNADLDFEVSGYVSLPELTRANRNYMTILVNGRYIK-NFLLNRAILDGYGSKL---MVGR 280
Cdd:cd00329 1 LKDRLAEILGDKVADKLIYVEGESDGFRVEGAISYPDSGRSSKDRQFSFVNGRPVReGGTHVKAVREAYTRALngdDVRR 80
|
90 100
....*....|....*....|....*..
gi 489082266 281 FPIVVIDIQIDPYLADVNVHPTKQEVR 307
Cdd:cd00329 81 YPVAVLSLKIPPSLVDVNVHPTKEEVR 107
|
|
| MutL_Trans_MutL |
cd03482 |
MutL_Trans_MutL: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
194-327 |
1.66e-20 |
|
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: 87.64 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 194 RQLTQTSGTGDLRQAIAgiyglnttkkmLAISNADLdfEVSGYVSLPELTRANRNYMTILVNGRYIKNFLLNRAILDGYG 273
Cdd:cd03482 3 QRLADILGEDFAEQALA-----------IDEEAGGL--RLSGWIALPTFARSQADIQYFYVNGRMVRDKLISHAVRQAYS 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 489082266 274 SKLMVGRFPIVVIDIQIDPYLADVNVHPTKQEVRISKERELMALISTAISESLK 327
Cdd:cd03482 70 DVLHGGRHPAYVLYLELDPAQVDVNVHPAKHEVRFRDSRLVHDFIYHAVKKALA 123
|
|
| MutL_Trans_MLH1 |
cd03483 |
MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
209-327 |
3.06e-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: 66.87 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 209 IAGIYGLNTTKKMLAIS----NADLDFEVSGYVSlpeltraNRNY------MTILVNGRYIKNFLLNRAILDGYGSKLMV 278
Cdd:cd03483 6 IRSVYGAAVANELIEVEisddDDDLGFKVKGLIS-------NANYskkkiiFILFINNRLVECSALRRAIENVYANYLPK 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 489082266 279 GRFPIVVIDIQIDPYLADVNVHPTKQEVRISKERELMALISTAISESLK 327
Cdd:cd03483 79 GAHPFVYLSLEIPPENVDVNVHPTKREVHFLNEEEIIERIQKLVEDKLS 127
|
|
| MutL_Trans_hPMS_2_like |
cd03484 |
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
204-324 |
3.44e-11 |
|
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: 61.51 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 204 DLRQAIAGIYGLNTTKKMLAI-----------------SNADLDFEVSGYVSLPE--LTRANRNYMTILVNGRYIKNFLL 264
Cdd:cd03484 1 DIKDNIINVFGGKVIKGLIPInleldvnptkeeldsdeDLADSEVKITGYISKPShgCGRSSSDRQFFYINGRPVDLKKV 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 265 NRAILDGYGSKLMVgRFPIVVIDIQIDPYLADVNVHPTKQEVRISKERELMALISTAISE 324
Cdd:cd03484 81 AKLINEVYKSFNSR-QYPFFILNISLPTSLYDVNVTPDKRTVLLHDEDRLIDTLKTSLSE 139
|
|
| HATPase_c |
pfam02518 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
19-85 |
1.66e-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: 55.84 E-value: 1.66e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489082266 19 EVVERPASVVKELVENAID--AKSSQITVEIEESGLKMIQVTDNGEGMSHEDLPLSLRRHATSKIKSQS 85
Cdd:pfam02518 1 GDELRLRQVLSNLLDNALKhaAKAGEITVTLSEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGGG 69
|
|
| HATPase_c_3 |
pfam13589 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ... |
24-119 |
3.84e-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: 49.64 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 24 PASVVKELVENAIDAKSSQITVEI--EESGLKMIQVTDNGEGMSHEDLPLSLRRHATSKiksqSDLFRIRTLGFRG--EA 99
Cdd:pfam13589 1 LEGALAELIDNSIDADATNIKIEVnkNRGGGTEIVIEDDGHGMSPEELINALRLATSAK----EAKRGSTDLGRYGigLK 76
|
90 100
....*....|....*....|
gi 489082266 100 LPSVASISKITIKTATKEVT 119
Cdd:pfam13589 77 LASLSLGAKLTVTSKKEGKS 96
|
|
| HATPase_c |
smart00387 |
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
27-85 |
6.94e-06 |
|
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 45.33 E-value: 6.94e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489082266 27 VVKELVENAIDA--KSSQITVEIEESGLK-MIQVTDNGEGMSHEDLPLSLRRHATSKIKSQS 85
Cdd:smart00387 9 VLSNLLDNAIKYtpEGGRITVTLERDGDHvEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRK 70
|
|
| HATPase_TopVIB-like |
cd16933 |
Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family ... |
27-148 |
1.91e-05 |
|
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: 46.19 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 27 VVKELVENAIDAKSS-----QITVEIEESGLKMIQVT--DNGEGMSHEDLPlslrrHATSKIKSQSDLFRIRTLGFRGEA 99
Cdd:cd16933 23 TVRELVENSLDATEEagilpDIKVEIEEIGKDHYKVIveDNGPGIPEEQIP-----KVFGKVLYGSKYHNKQSRGQQGLG 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489082266 100 LPSVASISKIT------IKTATKE---VTHGSLLIATG---GEI---ETLEAISTPTGTKIKVE 148
Cdd:cd16933 98 ISAAVLYSQMTtgkpveIISSTKDsnyAYVVKLMIDTDknePEIlekEEVENRYKWHGTRVELE 161
|
|
| HATPase_MORC-like |
cd16931 |
Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger ... |
24-102 |
6.58e-05 |
|
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: 42.78 E-value: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 24 PASVVKELVENAIDAKSSQITVEIEESGLK----MIQVTDNGEGMSHEDLplslrRHATSKIKSQSDLFRIRTLGFRGEA 99
Cdd:cd16931 12 PFGAVAELVDNARDADATRLDIFIDDINLLrggfMLSFLDDGNGMTPEEA-----HHMISFGFSDKRSDDHDHIGRYGNG 86
|
...
gi 489082266 100 LPS 102
Cdd:cd16931 87 FKS 89
|
|
| MutL_Trans_hPMS_1_like |
cd03485 |
MutL_Trans_hPMS1_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
204-311 |
1.04e-04 |
|
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: 42.64 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 204 DLRQAIAGIYGLNTTKKM--LAISNADLDFEVSGYVSLPE--LTRANRNYMTILVNGRYIKNFL----LNRAILDGYGSK 275
Cdd:cd03485 1 DHKEALARVLGTAVAANMvpVQSTDEDPQISLEGFLPKPGsdVSKTKSDGKFISVNSRPVSLGKdigkLLRQYYSSAYRK 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 489082266 276 LMVGRFPIVVIDIQIDPYLADVNVHPTKQEVRISKE 311
Cdd:cd03485 81 SSLRRYPVFFLNILCPPGLVDVNIEPDKDDVLLQNK 116
|
|
| PRK14868 |
PRK14868 |
DNA topoisomerase VI subunit B; Provisional |
28-244 |
1.07e-04 |
|
DNA topoisomerase VI subunit B; Provisional
Pssm-ID: 237842 [Multi-domain] Cd Length: 795 Bit Score: 45.56 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 28 VKELVENAIDAKSS-----QITVEIEESG--LKMIqVTDNGEGMSHEDLP-------LSLRRHATSKIKSQsdlfriRTL 93
Cdd:PRK14868 51 VKEAVDNALDATEEagilpDIYVEIEEVGdyYRLV-VEDNGPGITKEQIPkvfgkllYGSRFHAREQSRGQ------QGI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 94 GFRGEALPS---VASISKITIKT-ATKEVTHGSLLIATGG---EIETLEAIS--TPTGTKIKVEnLFYNTPARlkymKSL 164
Cdd:PRK14868 124 GISAAVLYSqltSGKPAKITSRTqGSEEAQYFELIIDTDTnepEISVEETTTwdRPHGTRIELE-MEANMRAR----QQL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 165 QAELAHIVdVVN---RLSLAHPEVAFTLISDGRQLTQTsgTGDLRQAIAGIYgLNTTKKMLAISNAdldFEVSGYVSlPE 241
Cdd:PRK14868 199 HDYIKHTA-VVNphaRIELREPDESLKFERATDQLPAE--TEEIRPHPHGVE-LGTLLKMLEATDS---YSVSGFLQ-EE 270
|
...
gi 489082266 242 LTR 244
Cdd:PRK14868 271 FTR 273
|
|
| KdpD |
COG2205 |
K+-sensing histidine kinase KdpD [Signal transduction mechanisms]; |
4-70 |
9.65e-04 |
|
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
Pssm-ID: 441807 [Multi-domain] Cd Length: 239 Bit Score: 41.43 E-value: 9.65e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 4 IIELPEVLANQIAAGEVVERpasVVKELVENAIDA--KSSQITVEIEESGLKM-IQVTDNGEGMSHEDLP 70
Cdd:COG2205 116 ELDLPPELPLVYADPELLEQ---VLANLLDNAIKYspPGGTITISARREGDGVrISVSDNGPGIPEEELE 182
|
|
| BaeS |
COG0642 |
Signal transduction histidine kinase [Signal transduction mechanisms]; |
27-70 |
3.50e-03 |
|
Signal transduction histidine kinase [Signal transduction mechanisms];
Pssm-ID: 440407 [Multi-domain] Cd Length: 328 Bit Score: 39.89 E-value: 3.50e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 489082266 27 VVKELVENAIDA--KSSQITVEIEESGLKM-IQVTDNGEGMSHEDLP 70
Cdd:COG0642 227 VLLNLLSNAIKYtpEGGTVTVSVRREGDRVrISVEDTGPGIPPEDLE 273
|
|
| MutL_Trans_MLH3 |
cd03486 |
MutL_Trans_MLH3: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
204-327 |
4.52e-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: 38.07 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082266 204 DLRQAIAGIYGLNTTKKMLAISNADLDFEVSGYVSLPELtrANRNYMTILVNGR-YIK-------NFLL----------- 264
Cdd:cd03486 1 SILSVFKQIYGLVLAQKLKEVSAKFQEYEVSGYISSEGH--YSKSFQFIYVNGRlYLKtrfhkliNKLFrktsavaknks 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489082266 265 -NRAILDGYGSKLMVgRFPIVVIDIQIDPYLADVNVHPTKQEVRISKERELMALISTAISESLK 327
Cdd:cd03486 79 sPQSKSSRRGKRSQE-SYPVFVLNITCPASEYDLSQEPSKTIIEFKDWKTLLPLILEVVKSFLK 141
|
|
| |
