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Conserved domains on  [gi|12643776|sp|Q57168|]
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RecName: Full=Type I restriction enzyme HindI methylase subunit; Short=M protein; AltName: Full=Type I methyltransferase M.HindI; Short=M.HindI; AltName: Full=Type I restriction enzyme HindVIIP methylase subunit

Protein Classification

SAM-dependent methyltransferase( domain architecture ID 12034797)

SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
N6_Mtase pfam02384
N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against ...
92-403 2.66e-159

N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The R-M system is a complex containing three polypeptides: M (this family), S (pfam01420), and R. This family consists of N-6 adenine-specific DNA methylase EC:2.1.1.72 from Type I and Type IC restriction systems. These methylases have the same sequence specificity as their corresponding restriction enzymes.


:

Pssm-ID: 426749 [Multi-domain]  Cd Length: 310  Bit Score: 452.16  E-value: 2.66e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643776    92 AKDILGHVYEYFLSRFAQAEGKRSGQYFTPKSIVSLIVEMLEPYSGR-VYDPAMGSGGFFVQTERFITAHQGNINNVSIY 170
Cdd:pfam02384   1 SRDLFGDAYEYLLRKFAPNAGKSGGEFFTPREVSKLIVELLDPKPGEsIYDPACGSGGFLIQAEKFVKEHDGDTNDLSIY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643776   171 GQEFNPTTWKLAAMNMAIRGIDYD-FGKYNADSFTQPQHI-DKKMDFIMANPHFNDKEWWNESLADDPRW--AYGTPPKG 246
Cdd:pfam02384  81 GQEKNPTTYRLARMNMILHGIEYDdFHIRHGDTLTSPKFEdDKKFDVVVANPPFSDKWDANDTLENDPRFrpAYGVAPKS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643776   247 NANFAWLQHMIYHLSPNGKIALLLANGSMSSqTNNEGEIRKAIINADLVECMVALPGQLFTNTKIPACIWFLNRNKK-RK 325
Cdd:pfam02384 161 NADLAFLQHIIYYLAPGGRAAVVLPNGVLFR-GGAEGKIRKALVDKDLVETVIALPPNLFYNTSIPTCILFLTKNKAeRK 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12643776   326 GEVLFIDARQIGYMKDRvLRDFTADDIAKIADTLHAWqtsdgyEDQAAFCKSATLEEIKNNDFVLTPGRYVGTAEQED 403
Cdd:pfam02384 240 GKVLFIDASNEFKKEGK-LNILTDEHIEKIIDTFGEF------KDVDGFSKSATLEEIAANDYNLNVGRYVGTEEEEE 310
 
Name Accession Description Interval E-value
N6_Mtase pfam02384
N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against ...
92-403 2.66e-159

N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The R-M system is a complex containing three polypeptides: M (this family), S (pfam01420), and R. This family consists of N-6 adenine-specific DNA methylase EC:2.1.1.72 from Type I and Type IC restriction systems. These methylases have the same sequence specificity as their corresponding restriction enzymes.


Pssm-ID: 426749 [Multi-domain]  Cd Length: 310  Bit Score: 452.16  E-value: 2.66e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643776    92 AKDILGHVYEYFLSRFAQAEGKRSGQYFTPKSIVSLIVEMLEPYSGR-VYDPAMGSGGFFVQTERFITAHQGNINNVSIY 170
Cdd:pfam02384   1 SRDLFGDAYEYLLRKFAPNAGKSGGEFFTPREVSKLIVELLDPKPGEsIYDPACGSGGFLIQAEKFVKEHDGDTNDLSIY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643776   171 GQEFNPTTWKLAAMNMAIRGIDYD-FGKYNADSFTQPQHI-DKKMDFIMANPHFNDKEWWNESLADDPRW--AYGTPPKG 246
Cdd:pfam02384  81 GQEKNPTTYRLARMNMILHGIEYDdFHIRHGDTLTSPKFEdDKKFDVVVANPPFSDKWDANDTLENDPRFrpAYGVAPKS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643776   247 NANFAWLQHMIYHLSPNGKIALLLANGSMSSqTNNEGEIRKAIINADLVECMVALPGQLFTNTKIPACIWFLNRNKK-RK 325
Cdd:pfam02384 161 NADLAFLQHIIYYLAPGGRAAVVLPNGVLFR-GGAEGKIRKALVDKDLVETVIALPPNLFYNTSIPTCILFLTKNKAeRK 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12643776   326 GEVLFIDARQIGYMKDRvLRDFTADDIAKIADTLHAWqtsdgyEDQAAFCKSATLEEIKNNDFVLTPGRYVGTAEQED 403
Cdd:pfam02384 240 GKVLFIDASNEFKKEGK-LNILTDEHIEKIIDTFGEF------KDVDGFSKSATLEEIAANDYNLNVGRYVGTEEEEE 310
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
94-335 9.26e-111

Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 325.99  E-value: 9.26e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643776  94 DILGHVYEYFLSRFAQAEGKRSGQYFTPKSIVSLIVEMLEPYSG-RVYDPAMGSGGFFVQTERFITAHQGN-INNVSIYG 171
Cdd:COG0286   1 DVLGDAYEYLLRKFAEESGKKAGEFYTPREVVRLMVELLDPKPGeTVYDPACGSGGFLVEAAEYLKEHGGDeRKKLSLYG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643776 172 QEFNPTTWKLAAMNMAIRGIDyDFGKYNADSFTQPQHIDKKMDFIMANPHFNDKeWWNESLADD--PRWAYGTPPKGNAN 249
Cdd:COG0286  81 QEINPTTYRLAKMNLLLHGIG-DPNIELGDTLSNDGDELEKFDVVLANPPFGGK-WKKEELKDDllGRFGYGLPPKSNAD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643776 250 FAWLQHMIYHLSPNGKIALLLANGSMSSqtNNEGEIRKAIINADLVECMVALPGQLFTNTKIPACIWFLNRNKK-RKGEV 328
Cdd:COG0286 159 LLFLQHILSLLKPGGRAAVVLPDGVLFR--GAEKEIRKKLLENDLLEAIIGLPSNLFYNTGIPTCILFLTKGKPeRTGKV 236

                ....*..
gi 12643776 329 LFIDARQ 335
Cdd:COG0286 237 LFIDASK 243
hsdM TIGR00497
type I restriction system adenine methylase (hsdM); Function: methylation of specific adenine ...
94-404 8.09e-49

type I restriction system adenine methylase (hsdM); Function: methylation of specific adenine residues; required for both restriction and modification activities. The ECOR124/3 I enzyme recognizes 5'GAA(N7)RTCG. for E.coli see (J. Mol. Biol. 257: 960-969 (1996)). [DNA metabolism, Restriction/modification]


Pssm-ID: 211578 [Multi-domain]  Cd Length: 501  Bit Score: 173.99  E-value: 8.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643776    94 DILGHVYEYFLSRFAQAEGKRSGQYFTPKSIVSLIVEML---EPYSGRVYDPAMGSGGFFVQterFITAHQGNINNVSIY 170
Cdd:TIGR00497 173 DAFGDAYEFLISMYAQNAGKSGGEFFTPQDISELLARIAigkKDTVDDVYDMACGSGSLLLQ---VIKVLGEKTSLVSYY 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643776   171 GQEFNPTTWKLAAMNMAIRGIDY-DFGKYNADSFTQPQHIDKK-MDFIMANPHFNDKewW----NESLADDPRWA-YGT- 242
Cdd:TIGR00497 250 GQEINHTTYNLCRMNMILHNIDYaNFNIINADTLTTKEWENENgFEVVVSNPPYSIS--WagdkKSNLVSDVRFKdAGTl 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643776   243 PPKGNANFAWLQHMIYHLSPNGKIALLLANGSMSSQtNNEGEIRKAIINADLVECMVALPGQLFTNTKIPACIWFLNRNK 322
Cdd:TIGR00497 328 APNSKADLAFVLHALYVLGQEGTAAIVCFPGILYRE-GKEQTIRKYLVDQNFVDAVIQLPSNLFSTTSIATSILVLKKNR 406
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643776   323 KrKGEVLFIDARQiGYMKDRVLRDFTADDIAKIADTLHAwqtsdgYEDQAAFCKSATLEEIKNNDFVLTPGRYVgtaEQE 402
Cdd:TIGR00497 407 K-KDPIFFIDGSN-EFVREKKNNRLSPKNIEKIVDCFNS------KKEEANFAKSVERDKIRESNYDLTVGKYV---NSE 475

                  ..
gi 12643776   403 DD 404
Cdd:TIGR00497 476 AE 477
 
Name Accession Description Interval E-value
N6_Mtase pfam02384
N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against ...
92-403 2.66e-159

N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The R-M system is a complex containing three polypeptides: M (this family), S (pfam01420), and R. This family consists of N-6 adenine-specific DNA methylase EC:2.1.1.72 from Type I and Type IC restriction systems. These methylases have the same sequence specificity as their corresponding restriction enzymes.


Pssm-ID: 426749 [Multi-domain]  Cd Length: 310  Bit Score: 452.16  E-value: 2.66e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643776    92 AKDILGHVYEYFLSRFAQAEGKRSGQYFTPKSIVSLIVEMLEPYSGR-VYDPAMGSGGFFVQTERFITAHQGNINNVSIY 170
Cdd:pfam02384   1 SRDLFGDAYEYLLRKFAPNAGKSGGEFFTPREVSKLIVELLDPKPGEsIYDPACGSGGFLIQAEKFVKEHDGDTNDLSIY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643776   171 GQEFNPTTWKLAAMNMAIRGIDYD-FGKYNADSFTQPQHI-DKKMDFIMANPHFNDKEWWNESLADDPRW--AYGTPPKG 246
Cdd:pfam02384  81 GQEKNPTTYRLARMNMILHGIEYDdFHIRHGDTLTSPKFEdDKKFDVVVANPPFSDKWDANDTLENDPRFrpAYGVAPKS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643776   247 NANFAWLQHMIYHLSPNGKIALLLANGSMSSqTNNEGEIRKAIINADLVECMVALPGQLFTNTKIPACIWFLNRNKK-RK 325
Cdd:pfam02384 161 NADLAFLQHIIYYLAPGGRAAVVLPNGVLFR-GGAEGKIRKALVDKDLVETVIALPPNLFYNTSIPTCILFLTKNKAeRK 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12643776   326 GEVLFIDARQIGYMKDRvLRDFTADDIAKIADTLHAWqtsdgyEDQAAFCKSATLEEIKNNDFVLTPGRYVGTAEQED 403
Cdd:pfam02384 240 GKVLFIDASNEFKKEGK-LNILTDEHIEKIIDTFGEF------KDVDGFSKSATLEEIAANDYNLNVGRYVGTEEEEE 310
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
94-335 9.26e-111

Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 325.99  E-value: 9.26e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643776  94 DILGHVYEYFLSRFAQAEGKRSGQYFTPKSIVSLIVEMLEPYSG-RVYDPAMGSGGFFVQTERFITAHQGN-INNVSIYG 171
Cdd:COG0286   1 DVLGDAYEYLLRKFAEESGKKAGEFYTPREVVRLMVELLDPKPGeTVYDPACGSGGFLVEAAEYLKEHGGDeRKKLSLYG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643776 172 QEFNPTTWKLAAMNMAIRGIDyDFGKYNADSFTQPQHIDKKMDFIMANPHFNDKeWWNESLADD--PRWAYGTPPKGNAN 249
Cdd:COG0286  81 QEINPTTYRLAKMNLLLHGIG-DPNIELGDTLSNDGDELEKFDVVLANPPFGGK-WKKEELKDDllGRFGYGLPPKSNAD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643776 250 FAWLQHMIYHLSPNGKIALLLANGSMSSqtNNEGEIRKAIINADLVECMVALPGQLFTNTKIPACIWFLNRNKK-RKGEV 328
Cdd:COG0286 159 LLFLQHILSLLKPGGRAAVVLPDGVLFR--GAEKEIRKKLLENDLLEAIIGLPSNLFYNTGIPTCILFLTKGKPeRTGKV 236

                ....*..
gi 12643776 329 LFIDARQ 335
Cdd:COG0286 237 LFIDASK 243
hsdM TIGR00497
type I restriction system adenine methylase (hsdM); Function: methylation of specific adenine ...
94-404 8.09e-49

type I restriction system adenine methylase (hsdM); Function: methylation of specific adenine residues; required for both restriction and modification activities. The ECOR124/3 I enzyme recognizes 5'GAA(N7)RTCG. for E.coli see (J. Mol. Biol. 257: 960-969 (1996)). [DNA metabolism, Restriction/modification]


Pssm-ID: 211578 [Multi-domain]  Cd Length: 501  Bit Score: 173.99  E-value: 8.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643776    94 DILGHVYEYFLSRFAQAEGKRSGQYFTPKSIVSLIVEML---EPYSGRVYDPAMGSGGFFVQterFITAHQGNINNVSIY 170
Cdd:TIGR00497 173 DAFGDAYEFLISMYAQNAGKSGGEFFTPQDISELLARIAigkKDTVDDVYDMACGSGSLLLQ---VIKVLGEKTSLVSYY 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643776   171 GQEFNPTTWKLAAMNMAIRGIDY-DFGKYNADSFTQPQHIDKK-MDFIMANPHFNDKewW----NESLADDPRWA-YGT- 242
Cdd:TIGR00497 250 GQEINHTTYNLCRMNMILHNIDYaNFNIINADTLTTKEWENENgFEVVVSNPPYSIS--WagdkKSNLVSDVRFKdAGTl 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643776   243 PPKGNANFAWLQHMIYHLSPNGKIALLLANGSMSSQtNNEGEIRKAIINADLVECMVALPGQLFTNTKIPACIWFLNRNK 322
Cdd:TIGR00497 328 APNSKADLAFVLHALYVLGQEGTAAIVCFPGILYRE-GKEQTIRKYLVDQNFVDAVIQLPSNLFSTTSIATSILVLKKNR 406
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643776   323 KrKGEVLFIDARQiGYMKDRVLRDFTADDIAKIADTLHAwqtsdgYEDQAAFCKSATLEEIKNNDFVLTPGRYVgtaEQE 402
Cdd:TIGR00497 407 K-KDPIFFIDGSN-EFVREKKNNRLSPKNIEKIVDCFNS------KKEEANFAKSVERDKIRESNYDLTVGKYV---NSE 475

                  ..
gi 12643776   403 DD 404
Cdd:TIGR00497 476 AE 477
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
119-220 1.16e-04

Adenine-specific DNA N6-methylase [Replication, recombination and repair];


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 43.78  E-value: 1.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643776 119 FTPKSIVSLIVEMLEPY----SGRVYDPAMGSGGFFVqterfiTAHQGNINNVSIYGQEFNPTTWKLAAMNMAIRGIDYD 194
Cdd:COG0827  95 MTPDAIGLLIGYLVEKFtkkeGLRILDPAVGTGNLLT------TVLNQLKKKVNAYGVEVDDLLIRLAAVLANLQGHPVE 168
                        90       100
                ....*....|....*....|....*.
gi 12643776 195 FgkYNADSFtQPQHIDkKMDFIMANP 220
Cdd:COG0827 169 L--FHQDAL-QPLLID-PVDVVISDL 190
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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