|
Name |
Accession |
Description |
Interval |
E-value |
| mutL |
PRK00095 |
DNA mismatch repair endonuclease MutL; |
1-609 |
0e+00 |
|
DNA mismatch repair endonuclease MutL;
Pssm-ID: 234630 [Multi-domain] Cd Length: 617 Bit Score: 881.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 1 MAIKQLSETLINQIAAGEVIERPSSATKELVENAIDAGATRIEIATAGGGKGLVRITDNGCGMSPADLELAVRRHCTSKI 80
Cdd:PRK00095 1 MPIQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 81 SDtLDD---IRTLGFRGEALPSIGSVAKLTITSRQQGAEQGSVISVTGGKVSDVRPAASNAGTIVEVRDLFFATPARLKF 157
Cdd:PRK00095 81 AS-LDDleaIRTLGFRGEALPSIASVSRLTLTSRTADAAEGWQIVYEGGEIVEVKPAAHPVGTTIEVRDLFFNTPARRKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 158 LKTERAEAAAITEVVKRMAIAFPHIRFVLSGTDRSTLEIPSTGDdHLARMAQILGAEFKDNAIEIDAGREDVTLSGFAGV 237
Cdd:PRK00095 160 LKSEKTELGHIDDVVNRLALAHPDVAFTLTHNGKLVLQTRGAGQ-LLQRLAAILGREFAENALPIDAEHGDLRLSGYVGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 238 PTFNRGNSAHQYVFVNGRPVQDKLLLSAIRGAYAETVPHGRYPVAVLSITLDPAFVDVNVHPAKSDVRFRDPGLIRGLIV 317
Cdd:PRK00095 239 PTLSRANRDYQYLFVNGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLVHDLIV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 318 GAIRQALTRDGDRAATTGANQMMNAFRP---------GYSPSGLRPSPSMAAPAPWSAATSPSRPLAVSGNMQFAEAVQS 388
Cdd:PRK00095 319 QAIQEALAQSGLIPAAAGANQVLEPAEPeplplqqtpLYASGSSPPASSPSSAPPEQSEESQEESSAEKNPLQPNASQSE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 389 RFSdITMPTARAEPREAYEASPDSSPEPVVYPLGAARAQLHENYIIAQTENGLVIVDQHAAHERLVFEQMRNALHSRRPP 468
Cdd:PRK00095 399 AAA-AASAEAAAAAPAAAPEPAEAAEEADSFPLGYALGQLHGTYILAENEDGLYLVDQHAAHERLLYEQLKDKLAEVGLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 469 SQVLLIPEIIDLPEEDCDRLMDHAAGFDALGLVIERFGPGAVAVRETPAMLGEVNVQGLVRQLADEIAEWDAASTLanKL 548
Cdd:PRK00095 478 SQPLLIPLVLELSEDEADRLEEHKELLARLGLELEPFGPNSFAVREVPALLGQQELEELIRDLLDELAEEGDSDTL--KE 555
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046555426 549 EYVAATMACHGSVRSGRRMRPEEMNALLRQMENTPGSGQCNHGRPTYIELKLSDIERLFGR 609
Cdd:PRK00095 556 RELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIELSLSDLEKLFKR 616
|
|
| MutL |
COG0323 |
DNA mismatch repair ATPase MutL [Replication, recombination and repair]; |
1-609 |
0e+00 |
|
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
Pssm-ID: 440092 [Multi-domain] Cd Length: 515 Bit Score: 800.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 1 MAIKQLSETLINQIAAGEVIERPSSATKELVENAIDAGATRIEIATAGGGKGLVRITDNGCGMSPADLELAVRRHCTSKI 80
Cdd:COG0323 2 PKIRLLPDELANQIAAGEVVERPASVVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLPLAFERHATSKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 81 SDT--LDDIRTLGFRGEALPSIGSVAKLTITSRQQGAEQGSVISVTGGKVSDVRPAASNAGTIVEVRDLFFATPARLKFL 158
Cdd:COG0323 82 RSAedLFRIRTLGFRGEALASIASVSRLTLTTRTAGAELGTRIEVEGGKVVEVEPAAAPKGTTVEVRDLFFNTPARRKFL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 159 KTERAEAAAITEVVKRMAIAFPHIRFVLSGTDRSTLEIPSTGDdHLARMAQILGAEFKDNAIEIDAGREDVTLSGFAGVP 238
Cdd:COG0323 162 KSDATELAHITDVVRRLALAHPDIAFTLIHNGREVFQLPGAGD-LLQRIAAIYGREFAENLLPVEAEREGLRLSGYIGKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 239 TFNRGNSAHQYVFVNGRPVQDKLLLSAIRGAYAETVPHGRYPVAVLSITLDPAFVDVNVHPAKSDVRFRDPGLIRGLIVG 318
Cdd:COG0323 241 EFSRSNRDYQYFFVNGRPVRDKLLSHAVREAYRDLLPKGRYPVAVLFLELDPELVDVNVHPTKTEVRFRDEREVYDLVRS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 319 AIRQALTRdgdraattganqmmnafrpgyspsglrpspsmaapapwsaatspsrplavsgnmqfaeavqsrfsditmpta 398
Cdd:COG0323 321 AVREALAQ------------------------------------------------------------------------ 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 399 raepreayeaspdsspepvvyplgAARAQLHENYIIAQTENGLVIVDQHAAHERLVFEQMRNALHSRRPPSQVLLIPEII 478
Cdd:COG0323 329 ------------------------AALGQLHGTYILAENEDGLVLIDQHAAHERILYERLKKALAEGGVASQPLLIPETL 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 479 DLPEEDCDRLMDHAAGFDALGLVIERFGPGAVAVRETPAMLGEVNVQGLVRQLADEIAEWDAASTLANKLEYVAATMACH 558
Cdd:COG0323 385 ELSPAEAALLEEHLEELARLGFEIEPFGPNTVAVRAVPALLGEGDAEELLRDLLDELAEEGSSESLEELREELLATMACH 464
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1046555426 559 GSVRSGRRMRPEEMNALLRQMENTPGSGQCNHGRPTYIELKLSDIERLFGR 609
Cdd:COG0323 465 GAIKAGRRLSLEEMNALLRDLEATENPYTCPHGRPTWIELSLEELEKLFKR 515
|
|
| mutl |
TIGR00585 |
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ... |
1-305 |
5.94e-114 |
|
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: 342.70 E-value: 5.94e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 1 MAIKQLSETLINQIAAGEVIERPSSATKELVENAIDAGATRIEIATAGGGKGLVRITDNGCGMSPADLELAVRRHCTSKI 80
Cdd:TIGR00585 1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 81 SDtLDD---IRTLGFRGEALPSIGSVAKLTITSRQQGAEQ-GSVISVTGGKVSDVRPAASNAGTIVEVRDLFFATPARLK 156
Cdd:TIGR00585 81 QS-FEDlerIETLGFRGEALASISSVSRLTITTKTSAADGlAYQALLEGGMIESIKPAPRPVGTTVEVRDLFYNLPVRRK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 157 FLKTERAEAAAITEVVKRMAIAFPHIRFVLSGTDRSTLEIPSTGDDHL--ARMAQILGAEFKDNAIEIDAGRE-DVTLSG 233
Cdd:TIGR00585 160 FLKSPKKEFRKILDVLQRYALIHPDISFSLTHDGKKVLQLSTKPNQSTkeNRIRSVFGTAVLRKLIPLDEWEDlDLQLEG 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046555426 234 FAGVPTFNRGNSAH-QYVFVNGRPVQDKLLLSAIRGAYAETVPHGRYPVAVLSITLDPAFVDVNVHPAKSDVR 305
Cdd:TIGR00585 240 FISQPNVTRSRRSGwQFLFINGRPVELKLLLKAIREVYHEYLPKGQYPVFVLNLEIDPELVDVNVHPDKKEVR 312
|
|
| HATPase_MutL-MLH-PMS-like |
cd16926 |
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ... |
10-194 |
9.21e-95 |
|
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: 288.57 E-value: 9.21e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 10 LINQIAAGEVIERPSSATKELVENAIDAGATRIEIATAGGGKGLVRITDNGCGMSPADLELAVRRHCTSKISDT--LDDI 87
Cdd:cd16926 1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFedLFSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 88 RTLGFRGEALPSIGSVAKLTITSRQQGAEQGSVISVT-GGKVSDVRPAASNAGTIVEVRDLFFATPARLKFLKTERAEAA 166
Cdd:cd16926 81 TTLGFRGEALASIASVSRLTITTRTADDDVGTRLVVDgGGIIEEVKPAAAPVGTTVTVRDLFYNTPARRKFLKSPKTELS 160
|
170 180
....*....|....*....|....*...
gi 1046555426 167 AITEVVKRMAIAFPHIRFVLSGTDRSTL 194
Cdd:cd16926 161 KILDLVQRLALAHPDVSFSLTHDGKLVL 188
|
|
| MutL_C |
pfam08676 |
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ... |
420-566 |
5.61e-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: 191.28 E-value: 5.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 420 PLGaaRAQLHENYIIAQTENGLVIVDQHAAHERLVFEQMRNALHSRRPPSQVLLIPEIIDLPEEDCDRLMDHAAGFDALG 499
Cdd:pfam08676 1 PLG--LGQVHGTYILAENEDGLYLIDQHAAHERILYEKLKRALAEGGLAAQPLLIPLVLELSPEEAALLEEHKEELAQLG 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046555426 500 LVIERFGPGAVAVRETPAMLGEVNVQGLVRQLADEIAEWDaASTLANKLEYVAATMACHGSVRSGRR 566
Cdd:pfam08676 79 FELEEFGPNSVIVRSVPALLRQQNLQELIRELLDELAEKG-GSSLEESLEELLATMACHSAVRAGRR 144
|
|
| MutL_C |
smart00853 |
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ... |
424-566 |
7.80e-50 |
|
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: 169.46 E-value: 7.80e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 424 ARAQLHENYIIAQTENGLVIVDQHAAHERLVFEQMRNalHSRRPPSQVLLIPEIIDLPEEDCDRLMDHAAGFDALGLVIE 503
Cdd:smart00853 1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLK--QAGGLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELE 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046555426 504 RFGPGAVAVRETPAMLGEVNVQGLVRQLADEIAEwDAASTLANKLEYVAATMACHGSVRSGRR 566
Cdd:smart00853 79 IFGPQSLILRSVPALLRQQNLQKLIPELLDLLSD-EEENARPSRLEALLASLACRSAIRAGDA 140
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| mutL |
PRK00095 |
DNA mismatch repair endonuclease MutL; |
1-609 |
0e+00 |
|
DNA mismatch repair endonuclease MutL;
Pssm-ID: 234630 [Multi-domain] Cd Length: 617 Bit Score: 881.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 1 MAIKQLSETLINQIAAGEVIERPSSATKELVENAIDAGATRIEIATAGGGKGLVRITDNGCGMSPADLELAVRRHCTSKI 80
Cdd:PRK00095 1 MPIQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 81 SDtLDD---IRTLGFRGEALPSIGSVAKLTITSRQQGAEQGSVISVTGGKVSDVRPAASNAGTIVEVRDLFFATPARLKF 157
Cdd:PRK00095 81 AS-LDDleaIRTLGFRGEALPSIASVSRLTLTSRTADAAEGWQIVYEGGEIVEVKPAAHPVGTTIEVRDLFFNTPARRKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 158 LKTERAEAAAITEVVKRMAIAFPHIRFVLSGTDRSTLEIPSTGDdHLARMAQILGAEFKDNAIEIDAGREDVTLSGFAGV 237
Cdd:PRK00095 160 LKSEKTELGHIDDVVNRLALAHPDVAFTLTHNGKLVLQTRGAGQ-LLQRLAAILGREFAENALPIDAEHGDLRLSGYVGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 238 PTFNRGNSAHQYVFVNGRPVQDKLLLSAIRGAYAETVPHGRYPVAVLSITLDPAFVDVNVHPAKSDVRFRDPGLIRGLIV 317
Cdd:PRK00095 239 PTLSRANRDYQYLFVNGRYVRDKLLNHAIRQAYHDLLPRGRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLVHDLIV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 318 GAIRQALTRDGDRAATTGANQMMNAFRP---------GYSPSGLRPSPSMAAPAPWSAATSPSRPLAVSGNMQFAEAVQS 388
Cdd:PRK00095 319 QAIQEALAQSGLIPAAAGANQVLEPAEPeplplqqtpLYASGSSPPASSPSSAPPEQSEESQEESSAEKNPLQPNASQSE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 389 RFSdITMPTARAEPREAYEASPDSSPEPVVYPLGAARAQLHENYIIAQTENGLVIVDQHAAHERLVFEQMRNALHSRRPP 468
Cdd:PRK00095 399 AAA-AASAEAAAAAPAAAPEPAEAAEEADSFPLGYALGQLHGTYILAENEDGLYLVDQHAAHERLLYEQLKDKLAEVGLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 469 SQVLLIPEIIDLPEEDCDRLMDHAAGFDALGLVIERFGPGAVAVRETPAMLGEVNVQGLVRQLADEIAEWDAASTLanKL 548
Cdd:PRK00095 478 SQPLLIPLVLELSEDEADRLEEHKELLARLGLELEPFGPNSFAVREVPALLGQQELEELIRDLLDELAEEGDSDTL--KE 555
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046555426 549 EYVAATMACHGSVRSGRRMRPEEMNALLRQMENTPGSGQCNHGRPTYIELKLSDIERLFGR 609
Cdd:PRK00095 556 RELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTYIELSLSDLEKLFKR 616
|
|
| MutL |
COG0323 |
DNA mismatch repair ATPase MutL [Replication, recombination and repair]; |
1-609 |
0e+00 |
|
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
Pssm-ID: 440092 [Multi-domain] Cd Length: 515 Bit Score: 800.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 1 MAIKQLSETLINQIAAGEVIERPSSATKELVENAIDAGATRIEIATAGGGKGLVRITDNGCGMSPADLELAVRRHCTSKI 80
Cdd:COG0323 2 PKIRLLPDELANQIAAGEVVERPASVVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLPLAFERHATSKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 81 SDT--LDDIRTLGFRGEALPSIGSVAKLTITSRQQGAEQGSVISVTGGKVSDVRPAASNAGTIVEVRDLFFATPARLKFL 158
Cdd:COG0323 82 RSAedLFRIRTLGFRGEALASIASVSRLTLTTRTAGAELGTRIEVEGGKVVEVEPAAAPKGTTVEVRDLFFNTPARRKFL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 159 KTERAEAAAITEVVKRMAIAFPHIRFVLSGTDRSTLEIPSTGDdHLARMAQILGAEFKDNAIEIDAGREDVTLSGFAGVP 238
Cdd:COG0323 162 KSDATELAHITDVVRRLALAHPDIAFTLIHNGREVFQLPGAGD-LLQRIAAIYGREFAENLLPVEAEREGLRLSGYIGKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 239 TFNRGNSAHQYVFVNGRPVQDKLLLSAIRGAYAETVPHGRYPVAVLSITLDPAFVDVNVHPAKSDVRFRDPGLIRGLIVG 318
Cdd:COG0323 241 EFSRSNRDYQYFFVNGRPVRDKLLSHAVREAYRDLLPKGRYPVAVLFLELDPELVDVNVHPTKTEVRFRDEREVYDLVRS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 319 AIRQALTRdgdraattganqmmnafrpgyspsglrpspsmaapapwsaatspsrplavsgnmqfaeavqsrfsditmpta 398
Cdd:COG0323 321 AVREALAQ------------------------------------------------------------------------ 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 399 raepreayeaspdsspepvvyplgAARAQLHENYIIAQTENGLVIVDQHAAHERLVFEQMRNALHSRRPPSQVLLIPEII 478
Cdd:COG0323 329 ------------------------AALGQLHGTYILAENEDGLVLIDQHAAHERILYERLKKALAEGGVASQPLLIPETL 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 479 DLPEEDCDRLMDHAAGFDALGLVIERFGPGAVAVRETPAMLGEVNVQGLVRQLADEIAEWDAASTLANKLEYVAATMACH 558
Cdd:COG0323 385 ELSPAEAALLEEHLEELARLGFEIEPFGPNTVAVRAVPALLGEGDAEELLRDLLDELAEEGSSESLEELREELLATMACH 464
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1046555426 559 GSVRSGRRMRPEEMNALLRQMENTPGSGQCNHGRPTYIELKLSDIERLFGR 609
Cdd:COG0323 465 GAIKAGRRLSLEEMNALLRDLEATENPYTCPHGRPTWIELSLEELEKLFKR 515
|
|
| mutl |
TIGR00585 |
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ... |
1-305 |
5.94e-114 |
|
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: 342.70 E-value: 5.94e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 1 MAIKQLSETLINQIAAGEVIERPSSATKELVENAIDAGATRIEIATAGGGKGLVRITDNGCGMSPADLELAVRRHCTSKI 80
Cdd:TIGR00585 1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 81 SDtLDD---IRTLGFRGEALPSIGSVAKLTITSRQQGAEQ-GSVISVTGGKVSDVRPAASNAGTIVEVRDLFFATPARLK 156
Cdd:TIGR00585 81 QS-FEDlerIETLGFRGEALASISSVSRLTITTKTSAADGlAYQALLEGGMIESIKPAPRPVGTTVEVRDLFYNLPVRRK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 157 FLKTERAEAAAITEVVKRMAIAFPHIRFVLSGTDRSTLEIPSTGDDHL--ARMAQILGAEFKDNAIEIDAGRE-DVTLSG 233
Cdd:TIGR00585 160 FLKSPKKEFRKILDVLQRYALIHPDISFSLTHDGKKVLQLSTKPNQSTkeNRIRSVFGTAVLRKLIPLDEWEDlDLQLEG 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046555426 234 FAGVPTFNRGNSAH-QYVFVNGRPVQDKLLLSAIRGAYAETVPHGRYPVAVLSITLDPAFVDVNVHPAKSDVR 305
Cdd:TIGR00585 240 FISQPNVTRSRRSGwQFLFINGRPVELKLLLKAIREVYHEYLPKGQYPVFVLNLEIDPELVDVNVHPDKKEVR 312
|
|
| HATPase_MutL-MLH-PMS-like |
cd16926 |
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ... |
10-194 |
9.21e-95 |
|
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: 288.57 E-value: 9.21e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 10 LINQIAAGEVIERPSSATKELVENAIDAGATRIEIATAGGGKGLVRITDNGCGMSPADLELAVRRHCTSKISDT--LDDI 87
Cdd:cd16926 1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFedLFSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 88 RTLGFRGEALPSIGSVAKLTITSRQQGAEQGSVISVT-GGKVSDVRPAASNAGTIVEVRDLFFATPARLKFLKTERAEAA 166
Cdd:cd16926 81 TTLGFRGEALASIASVSRLTITTRTADDDVGTRLVVDgGGIIEEVKPAAAPVGTTVTVRDLFYNTPARRKFLKSPKTELS 160
|
170 180
....*....|....*....|....*...
gi 1046555426 167 AITEVVKRMAIAFPHIRFVLSGTDRSTL 194
Cdd:cd16926 161 KILDLVQRLALAHPDVSFSLTHDGKLVL 188
|
|
| MutL_C |
pfam08676 |
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ... |
420-566 |
5.61e-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: 191.28 E-value: 5.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 420 PLGaaRAQLHENYIIAQTENGLVIVDQHAAHERLVFEQMRNALHSRRPPSQVLLIPEIIDLPEEDCDRLMDHAAGFDALG 499
Cdd:pfam08676 1 PLG--LGQVHGTYILAENEDGLYLIDQHAAHERILYEKLKRALAEGGLAAQPLLIPLVLELSPEEAALLEEHKEELAQLG 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046555426 500 LVIERFGPGAVAVRETPAMLGEVNVQGLVRQLADEIAEWDaASTLANKLEYVAATMACHGSVRSGRR 566
Cdd:pfam08676 79 FELEEFGPNSVIVRSVPALLRQQNLQELIRELLDELAEKG-GSSLEESLEELLATMACHSAVRAGRR 144
|
|
| DNA_mis_repair |
pfam01119 |
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ... |
208-324 |
2.60e-51 |
|
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: 172.30 E-value: 2.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 208 AQILGAEFKDNAIEIDAGREDVTLSGFAGVPTFNRGNSAHQYVFVNGRPVQDKLLLSAIRGAYAETVPHGRYPVAVLSIT 287
Cdd:pfam01119 1 AAIYGKEFAENLLPIEKEDDGLRLSGYISKPTLSRSNRDYQYLFVNGRPVRDKLLSHAIREAYRDLLPKGRYPVAVLFLE 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1046555426 288 LDPAFVDVNVHPAKSDVRFRDPGLIRGLIVGAIRQAL 324
Cdd:pfam01119 81 IDPELVDVNVHPTKREVRFRDEREVYDFIKEALREAL 117
|
|
| MutL_C |
smart00853 |
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ... |
424-566 |
7.80e-50 |
|
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: 169.46 E-value: 7.80e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 424 ARAQLHENYIIAQTENGLVIVDQHAAHERLVFEQMRNalHSRRPPSQVLLIPEIIDLPEEDCDRLMDHAAGFDALGLVIE 503
Cdd:smart00853 1 ALGQVAGTYILAEREDGLYLLDQHAAHERILYEQLLK--QAGGLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELE 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046555426 504 RFGPGAVAVRETPAMLGEVNVQGLVRQLADEIAEwDAASTLANKLEYVAATMACHGSVRSGRR 566
Cdd:smart00853 79 IFGPQSLILRSVPALLRQQNLQKLIPELLDLLSD-EEENARPSRLEALLASLACRSAIRAGDA 140
|
|
| MutL_Trans |
cd00782 |
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ... |
203-324 |
4.57e-48 |
|
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: 163.87 E-value: 4.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 203 HLARMAQILGAEFKDNAIEIDAGREDVTLSGFAGVPTFNRGNSAHQYVFVNGRPVQDKLLLSAIRGAYAETVPHGRYPVA 282
Cdd:cd00782 1 LKDRIAQVYGKEVAKNLIEVELESGDFRISGYISKPDFGRSSKDRQFLFVNGRPVRDKLLSKAINEAYRSYLPKGRYPVF 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1046555426 283 VLSITLDPAFVDVNVHPAKSDVRFRDPGLIRGLIVGAIRQAL 324
Cdd:cd00782 81 VLNLELPPELVDVNVHPTKREVRFSDEEEVLELIREALRSAL 122
|
|
| MutL_Trans_MutL |
cd03482 |
MutL_Trans_MutL: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
203-325 |
5.15e-45 |
|
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: 155.82 E-value: 5.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 203 HLARMAQILGAEFKDNAIEIDAGREDVTLSGFAGVPTFNRGNSAHQYVFVNGRPVQDKLLLSAIRGAYAETVPHGRYPVA 282
Cdd:cd03482 1 KLQRLADILGEDFAEQALAIDEEAGGLRLSGWIALPTFARSQADIQYFYVNGRMVRDKLISHAVRQAYSDVLHGGRHPAY 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1046555426 283 VLSITLDPAFVDVNVHPAKSDVRFRDPGLIRGLIVGAIRQALT 325
Cdd:cd03482 81 VLYLELDPAQVDVNVHPAKHEVRFRDSRLVHDFIYHAVKKALA 123
|
|
| TopoII_MutL_Trans |
cd00329 |
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ... |
203-305 |
1.26e-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: 110.04 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 203 HLARMAQILGAEFKDNAIEIDAGREDVTLSGFAGVPTFNRGNSAHQYVFVNGRPV-QDKLLLSAIRGAYAETV---PHGR 278
Cdd:cd00329 1 LKDRLAEILGDKVADKLIYVEGESDGFRVEGAISYPDSGRSSKDRQFSFVNGRPVrEGGTHVKAVREAYTRALngdDVRR 80
|
90 100
....*....|....*....|....*..
gi 1046555426 279 YPVAVLSITLDPAFVDVNVHPAKSDVR 305
Cdd:cd00329 81 YPVAVLSLKIPPSLVDVNVHPTKEEVR 107
|
|
| MutL_Trans_hPMS_2_like |
cd03484 |
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
216-324 |
3.38e-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: 64.21 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 216 KDNAIEIDAGREDVTLSGFAGVPTFN--RGNSAHQYVFVNGRPVQDKLLLSAIRGAYaETVPHGRYPVAVLSITLDPAFV 293
Cdd:cd03484 32 EELDSDEDLADSEVKITGYISKPSHGcgRSSSDRQFFYINGRPVDLKKVAKLINEVY-KSFNSRQYPFFILNISLPTSLY 110
|
90 100 110
....*....|....*....|....*....|.
gi 1046555426 294 DVNVHPAKSDVRFRDpgliRGLIVGAIRQAL 324
Cdd:cd03484 111 DVNVTPDKRTVLLHD----EDRLIDTLKTSL 137
|
|
| MutL_Trans_MLH1 |
cd03483 |
MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
251-306 |
5.43e-12 |
|
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: 63.02 E-value: 5.43e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1046555426 251 FVNGRPVQDKLLLSAIRGAYAETVPHGRYPVAVLSITLDPAFVDVNVHPAKSDVRF 306
Cdd:cd03483 53 FINNRLVECSALRRAIENVYANYLPKGAHPFVYLSLEIPPENVDVNVHPTKREVHF 108
|
|
| HATPase_c_3 |
pfam13589 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ... |
25-132 |
1.78e-11 |
|
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: 61.96 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 25 SATKELVENAIDAGATRIEIA--TAGGGKGLVRITDNGCGMSPADLELAVRRHCTSKisDTLDDIRTLGFRG--EALPSI 100
Cdd:pfam13589 3 GALAELIDNSIDADATNIKIEvnKNRGGGTEIVIEDDGHGMSPEELINALRLATSAK--EAKRGSTDLGRYGigLKLASL 80
|
90 100 110
....*....|....*....|....*....|..
gi 1046555426 101 GSVAKLTITSRQQGAEqgSVISVTGGKVSDVR 132
Cdd:pfam13589 81 SLGAKLTVTSKKEGKS--STLTLDRDKISNEN 110
|
|
| MutL_Trans_hPMS_1_like |
cd03485 |
MutL_Trans_hPMS1_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
202-308 |
3.13e-10 |
|
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: 58.44 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 202 DHLARMAQILGAEFKDNAIEIDAGRED--VTLSGFAGVPTFNRGN--SAHQYVFVNGRPV---QD--KLLLSAIRGAYAE 272
Cdd:cd03485 1 DHKEALARVLGTAVAANMVPVQSTDEDpqISLEGFLPKPGSDVSKtkSDGKFISVNSRPVslgKDigKLLRQYYSSAYRK 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 1046555426 273 TVPHgRYPVAVLSITLDPAFVDVNVHPAKSDVRFRD 308
Cdd:cd03485 81 SSLR-RYPVFFLNILCPPGLVDVNIEPDKDDVLLQN 115
|
|
| MutL_Trans_MLH3 |
cd03486 |
MutL_Trans_MLH3: transducer domain, having a ribosomal S5 domain 2-like fold, found in ... |
204-325 |
7.17e-08 |
|
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: 51.93 E-value: 7.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046555426 204 LARMAQILGAEFKDNAIEIDAGREDVTLSGFAGVPTFnrGNSAHQYVFVNGRPVQDKLLLSAI-------------RGAY 270
Cdd:cd03486 3 LSVFKQIYGLVLAQKLKEVSAKFQEYEVSGYISSEGH--YSKSFQFIYVNGRLYLKTRFHKLInklfrktsavaknKSSP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046555426 271 AETVPHG------RYPVAVLSITLDPAFVDVNVHPAKSDVRFRDPGLIRGLIVGAIRQALT 325
Cdd:cd03486 81 QSKSSRRgkrsqeSYPVFVLNITCPASEYDLSQEPSKTIIEFKDWKTLLPLILEVVKSFLK 141
|
|
| HATPase_MORC-like |
cd16931 |
Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger ... |
23-87 |
1.34e-06 |
|
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: 47.40 E-value: 1.34e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046555426 23 PSSATKELVENAIDAGATRIEI----ATAGGGKGLVRITDNGCGMSPADLELAVRRHCTSKISDTLDDI 87
Cdd:cd16931 12 PFGAVAELVDNARDADATRLDIfiddINLLRGGFMLSFLDDGNGMTPEEAHHMISFGFSDKRSDDHDHI 80
|
|
| HATPase_c |
pfam02518 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
29-83 |
1.98e-06 |
|
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.
Pssm-ID: 460579 [Multi-domain] Cd Length: 109 Bit Score: 46.59 E-value: 1.98e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1046555426 29 ELVENAID--AGATRIEIATAGGGKGLVRITDNGCGMSPADLELAVRRHCTSKISDT 83
Cdd:pfam02518 12 NLLDNALKhaAKAGEITVTLSEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGG 68
|
|
| HATPase_c |
smart00387 |
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
29-69 |
3.10e-05 |
|
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 43.41 E-value: 3.10e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1046555426 29 ELVENAIDAGATRIEI---ATAGGGKGLVRITDNGCGMSPADLE 69
Cdd:smart00387 12 NLLDNAIKYTPEGGRItvtLERDGDHVEITVEDNGPGIPPEDLE 55
|
|
| COG4191 |
COG4191 |
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ... |
30-69 |
6.84e-04 |
|
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];
Pssm-ID: 443345 [Multi-domain] Cd Length: 361 Bit Score: 42.09 E-value: 6.84e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1046555426 30 LVENAIDA----GATRIEIAT-AGGGKGLVRITDNGCGMSPADLE 69
Cdd:COG4191 264 LLINAIDAmeegEGGRITISTrREGDYVVISVRDNGPGIPPEVLE 308
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
30-69 |
1.15e-03 |
|
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: 41.87 E-value: 1.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1046555426 30 LVENAIDAGATRIEI---ATAGGGKGLVRITDNGCGMSPADLE 69
Cdd:COG5000 325 LLKNAIEAIEEGGEIevsTRREDGRVRIEVSDNGPGIPEEVLE 367
|
|
| BaeS |
COG0642 |
Signal transduction histidine kinase [Signal transduction mechanisms]; |
30-69 |
2.10e-03 |
|
Signal transduction histidine kinase [Signal transduction mechanisms];
Pssm-ID: 440407 [Multi-domain] Cd Length: 328 Bit Score: 40.66 E-value: 2.10e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1046555426 30 LVENAIDAGA--TRIEI-ATAGGGKGLVRITDNGCGMSPADLE 69
Cdd:COG0642 231 LLSNAIKYTPegGTVTVsVRREGDRVRISVEDTGPGIPPEDLE 273
|
|
| KdpD |
COG2205 |
K+-sensing histidine kinase KdpD [Signal transduction mechanisms]; |
29-69 |
9.13e-03 |
|
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
Pssm-ID: 441807 [Multi-domain] Cd Length: 239 Bit Score: 38.35 E-value: 9.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1046555426 29 ELVENAIDAG--ATRIEI-ATAGGGKGLVRITDNGCGMSPADLE 69
Cdd:COG2205 139 NLLDNAIKYSppGGTITIsARREGDGVRISVSDNGPGIPEEELE 182
|
|
| |
