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Conserved domains on  [gi|1717508352|ref|NP_001358974|]
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nicotinamide N-methyltransferase [Homo sapiens]

Protein Classification

NNMT/PNMT/TEMT family class I SAM-dependent methyltransferase( domain architecture ID 10472236)

NNMT/PNMT/TEMT family class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; similar to nicotinamide N-methyltransferase (NNMT) and phenylethanolamine N-methyltransferase (PNMT)

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008170|GO:1904047
PubMed:  12504684|12826405
SCOP:  3000118|4003307

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NNMT_PNMT_TEMT pfam01234
NNMT/PNMT/TEMT family;
2-259 4.56e-153

NNMT/PNMT/TEMT family;


:

Pssm-ID: 395988  Cd Length: 261  Bit Score: 426.84  E-value: 4.56e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717508352   2 ESGFTSKDTYLSHFNPRDYLEKYYKFGSRHSAESQILKHLLKNLFKIFCLDGVKGDLLIDIGSGPTIYQLLSACESFKEI 81
Cdd:pfam01234   3 GEGFLAGEEYKKKFNPRAYLNTYYKFASGDAAEMQIVLFFLPNLLQTFGPGGVKGDTLIDIGSGPTIYQLLSACEVFKEI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717508352  82 VVTDYSDQNLQELEKWLKKEPEAFDWSPVVTYVCDLEGNRVKGPEKEEKLRQAVKQVLKCDVTQSQPLGA-VPLPPADCV 160
Cdd:pfam01234  83 HLSDYLPQNRDELIKWLKKEPGAFDWSPVLKHICELEGDRECWQEKEEKLRALVKRVLKCDVHQSPPLGAgVQLPPADCV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717508352 161 LSTLCLDAACPDLPTYCRALRNLGSLLKPGGFLVIMDALKSSYYMIGEQKFSSLPLGREAVEAAVKEAGYTIEWFEVISQ 240
Cdd:pfam01234 163 VTIFCLEYACPDLEEYCRALRNLASLLKPGGHLVLGGVLEESWYMFGEKKFSCLYLSKEVVEDALVDAGLDVEALQIMPQ 242
                         250
                  ....*....|....*....
gi 1717508352 241 SYSSTMANNEGLFSLVARK 259
Cdd:pfam01234 243 SYSYKVADHDGVFFLVARK 261
 
Name Accession Description Interval E-value
NNMT_PNMT_TEMT pfam01234
NNMT/PNMT/TEMT family;
2-259 4.56e-153

NNMT/PNMT/TEMT family;


Pssm-ID: 395988  Cd Length: 261  Bit Score: 426.84  E-value: 4.56e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717508352   2 ESGFTSKDTYLSHFNPRDYLEKYYKFGSRHSAESQILKHLLKNLFKIFCLDGVKGDLLIDIGSGPTIYQLLSACESFKEI 81
Cdd:pfam01234   3 GEGFLAGEEYKKKFNPRAYLNTYYKFASGDAAEMQIVLFFLPNLLQTFGPGGVKGDTLIDIGSGPTIYQLLSACEVFKEI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717508352  82 VVTDYSDQNLQELEKWLKKEPEAFDWSPVVTYVCDLEGNRVKGPEKEEKLRQAVKQVLKCDVTQSQPLGA-VPLPPADCV 160
Cdd:pfam01234  83 HLSDYLPQNRDELIKWLKKEPGAFDWSPVLKHICELEGDRECWQEKEEKLRALVKRVLKCDVHQSPPLGAgVQLPPADCV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717508352 161 LSTLCLDAACPDLPTYCRALRNLGSLLKPGGFLVIMDALKSSYYMIGEQKFSSLPLGREAVEAAVKEAGYTIEWFEVISQ 240
Cdd:pfam01234 163 VTIFCLEYACPDLEEYCRALRNLASLLKPGGHLVLGGVLEESWYMFGEKKFSCLYLSKEVVEDALVDAGLDVEALQIMPQ 242
                         250
                  ....*....|....*....
gi 1717508352 241 SYSSTMANNEGLFSLVARK 259
Cdd:pfam01234 243 SYSYKVADHDGVFFLVARK 261
GntF_guanitoxin NF041360
guanitoxin biosynthesis pre-guanitoxin forming N-methyltransferase GntF;
1-208 6.69e-26

guanitoxin biosynthesis pre-guanitoxin forming N-methyltransferase GntF;


Pssm-ID: 469252  Cd Length: 273  Bit Score: 102.40  E-value: 6.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717508352   1 MESGFTSKDtyLSHFNPRDYLEKYY------KFGSRHSAESQILKHLLKNLFKifclDGVKGDLLIDIGSGPTIYQLLSA 74
Cdd:NF041360    1 MELKFKEND--FQSFEAIPYLNEYFnnypsdKYGGIGFENEKFLQFFAEVAHE----HHLNNSLLLDFGCGPTIYSIISL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717508352  75 CESFKEIVVTDYSDQNLQELEKWLKKEPEAFDWSPVVTYVCDLEGN-----------RVKGPEKEEK---LRQAVKQVLK 140
Cdd:NF041360   75 GQNCREIHMSDYLQQNLEQVKLWQQGKPEAFDWNPYLRRALQIETAlnqnqpidsflDVTDEEIEERarlLQEKITSIRK 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717508352 141 CDVTQSQPLGAVPLPPADCVLSTLCLDAACPDLPTYCRALRNLGSLLKPGGFLVIMDALKSSYYMIGE 208
Cdd:NF041360  155 GNARATNPVGEEGKALYEAVISCFCLEGVAEDLAEWKNLIANLSSIIKPGGLLIFATQIEADSYRIGD 222
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
59-199 3.45e-05

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 42.03  E-value: 3.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717508352  59 LIDIGSGPTIYQLLSACESFKEIVVTDYSDQNLQELEKWLKKepeafdwspvvtyvcdLEGNRVKgpekeeklrqavkqV 138
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAA----------------LLADNVE--------------V 51
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717508352 139 LKCDVTQSQPLgavPLPPADCVLSTLCLDAACPDLPtycRALRNLGSLLKPGGFLVIMDAL 199
Cdd:cd02440    52 LKGDAEELPPE---ADESFDVIISDPPLHHLVEDLA---RFLEEARRLLKPGGVLVLTLVL 106
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
126-249 9.78e-05

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 42.21  E-value: 9.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717508352 126 EKEEKLRQAVKQVLKCDVTQSQPLgavPLPPADCVLSTLCLDAACPDLPTycRALRNLGSLLKPGGFLVIMDALKSSYYM 205
Cdd:COG0500    67 ARAAKAGLGNVEFLVADLAELDPL---PAESFDLVVAFGVLHHLPPEERE--ALLRELARALKPGGVLLLSASDAAAALS 141
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1717508352 206 IGE-------QKFSSLPLGREAVEAAVKEAGYTIEWFEVISQSYSSTMANN 249
Cdd:COG0500   142 LARllllataSLLELLLLLRLLALELYLRALLAAAATEDLRSDALLESANA 192
 
Name Accession Description Interval E-value
NNMT_PNMT_TEMT pfam01234
NNMT/PNMT/TEMT family;
2-259 4.56e-153

NNMT/PNMT/TEMT family;


Pssm-ID: 395988  Cd Length: 261  Bit Score: 426.84  E-value: 4.56e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717508352   2 ESGFTSKDTYLSHFNPRDYLEKYYKFGSRHSAESQILKHLLKNLFKIFCLDGVKGDLLIDIGSGPTIYQLLSACESFKEI 81
Cdd:pfam01234   3 GEGFLAGEEYKKKFNPRAYLNTYYKFASGDAAEMQIVLFFLPNLLQTFGPGGVKGDTLIDIGSGPTIYQLLSACEVFKEI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717508352  82 VVTDYSDQNLQELEKWLKKEPEAFDWSPVVTYVCDLEGNRVKGPEKEEKLRQAVKQVLKCDVTQSQPLGA-VPLPPADCV 160
Cdd:pfam01234  83 HLSDYLPQNRDELIKWLKKEPGAFDWSPVLKHICELEGDRECWQEKEEKLRALVKRVLKCDVHQSPPLGAgVQLPPADCV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717508352 161 LSTLCLDAACPDLPTYCRALRNLGSLLKPGGFLVIMDALKSSYYMIGEQKFSSLPLGREAVEAAVKEAGYTIEWFEVISQ 240
Cdd:pfam01234 163 VTIFCLEYACPDLEEYCRALRNLASLLKPGGHLVLGGVLEESWYMFGEKKFSCLYLSKEVVEDALVDAGLDVEALQIMPQ 242
                         250
                  ....*....|....*....
gi 1717508352 241 SYSSTMANNEGLFSLVARK 259
Cdd:pfam01234 243 SYSYKVADHDGVFFLVARK 261
GntF_guanitoxin NF041360
guanitoxin biosynthesis pre-guanitoxin forming N-methyltransferase GntF;
1-208 6.69e-26

guanitoxin biosynthesis pre-guanitoxin forming N-methyltransferase GntF;


Pssm-ID: 469252  Cd Length: 273  Bit Score: 102.40  E-value: 6.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717508352   1 MESGFTSKDtyLSHFNPRDYLEKYY------KFGSRHSAESQILKHLLKNLFKifclDGVKGDLLIDIGSGPTIYQLLSA 74
Cdd:NF041360    1 MELKFKEND--FQSFEAIPYLNEYFnnypsdKYGGIGFENEKFLQFFAEVAHE----HHLNNSLLLDFGCGPTIYSIISL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717508352  75 CESFKEIVVTDYSDQNLQELEKWLKKEPEAFDWSPVVTYVCDLEGN-----------RVKGPEKEEK---LRQAVKQVLK 140
Cdd:NF041360   75 GQNCREIHMSDYLQQNLEQVKLWQQGKPEAFDWNPYLRRALQIETAlnqnqpidsflDVTDEEIEERarlLQEKITSIRK 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717508352 141 CDVTQSQPLGAVPLPPADCVLSTLCLDAACPDLPTYCRALRNLGSLLKPGGFLVIMDALKSSYYMIGE 208
Cdd:NF041360  155 GNARATNPVGEEGKALYEAVISCFCLEGVAEDLAEWKNLIANLSSIIKPGGLLIFATQIEADSYRIGD 222
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
59-199 3.45e-05

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 42.03  E-value: 3.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717508352  59 LIDIGSGPTIYQLLSACESFKEIVVTDYSDQNLQELEKWLKKepeafdwspvvtyvcdLEGNRVKgpekeeklrqavkqV 138
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAA----------------LLADNVE--------------V 51
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717508352 139 LKCDVTQSQPLgavPLPPADCVLSTLCLDAACPDLPtycRALRNLGSLLKPGGFLVIMDAL 199
Cdd:cd02440    52 LKGDAEELPPE---ADESFDVIISDPPLHHLVEDLA---RFLEEARRLLKPGGVLVLTLVL 106
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
126-249 9.78e-05

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 42.21  E-value: 9.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717508352 126 EKEEKLRQAVKQVLKCDVTQSQPLgavPLPPADCVLSTLCLDAACPDLPTycRALRNLGSLLKPGGFLVIMDALKSSYYM 205
Cdd:COG0500    67 ARAAKAGLGNVEFLVADLAELDPL---PAESFDLVVAFGVLHHLPPEERE--ALLRELARALKPGGVLLLSASDAAAALS 141
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1717508352 206 IGE-------QKFSSLPLGREAVEAAVKEAGYTIEWFEVISQSYSSTMANN 249
Cdd:COG0500   142 LARllllataSLLELLLLLRLLALELYLRALLAAAATEDLRSDALLESANA 192
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
147-233 1.00e-04

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 41.64  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717508352 147 QPLGAVPLPPADCVLSTLCLDAacpdLPTYCRALRNLGSLLKPGGFLVIMDALKSSYY-MIGEQKFSSLPLG-------R 218
Cdd:pfam13489  71 EQEAAVPAGKFDVIVAREVLEH----VPDPPALLRQIAALLKPGGLLLLSTPLASDEAdRLLLEWPYLRPRNghislfsA 146
                          90
                  ....*....|....*
gi 1717508352 219 EAVEAAVKEAGYTIE 233
Cdd:pfam13489 147 RSLKRLLEEAGFEVV 161
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
51-231 1.25e-03

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 38.05  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717508352  51 LDGVKGDLLIDIGSGpTIYQLLSACESFKEIVVTDYSDQNLQELEKwlkkepeafdwspvvtyvcdlegnrvKGPEKEEK 130
Cdd:COG2226    18 LGLRPGARVLDLGCG-TGRLALALAERGARVTGVDISPEMLELARE--------------------------RAAEAGLN 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717508352 131 LRqavkqVLKCDVTqsqplgAVPLPPA--DCVLSTLCLDAaCPDLPtycRALRNLGSLLKPGGFLVIMDALKSSyymige 208
Cdd:COG2226    71 VE-----FVVGDAE------DLPFPDGsfDLVISSFVLHH-LPDPE---RALAEIARVLKPGGRLVVVDFSPPD------ 129
                         170       180
                  ....*....|....*....|...
gi 1717508352 209 qkfsslplgREAVEAAVKEAGYT 231
Cdd:COG2226   130 ---------LAELEELLAEAGFE 143
 
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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