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Conserved domains on  [gi|157816899|ref|NP_001102492|]
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indolethylamine N-methyltransferase [Rattus norvegicus]

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

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
NNMT_PNMT_TEMT pfam01234
NNMT/PNMT/TEMT family;
1-260 6.16e-148

NNMT/PNMT/TEMT family;


:

Pssm-ID: 395988  Cd Length: 261  Bit Score: 414.13  E-value: 6.16e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157816899    1 MAGKVYMGGEDYEKEFTPKDYLTTFYSFDSGTVAEQEIVKFSLQNLYQTFSTGGVGGDVLIDIGSGPTIYQLLSACEVFR 80
Cdd:pfam01234   1 MDGEGFLAGEEYKKKFNPRAYLNTYYKFASGDAAEMQIVLFFLPNLLQTFGPGGVKGDTLIDIGSGPTIYQLLSACEVFK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157816899   81 EIIATDYTPQNLQELQKWLKKEPGAYDWSSIVQHVCELEGDRSRWQEKEAKLRRTVTRVLRCDVTKTPPLGS-AQVPLAD 159
Cdd:pfam01234  81 EIHLSDYLPQNRDELIKWLKKEPGAFDWSPVLKHICELEGDRECWQEKEEKLRALVKRVLKCDVHQSPPLGAgVQLPPAD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157816899  160 CVLTFLAMECACPDVDTYRAALRRLAGLLKPGGHLVTLVTLRFQHYMVGPKKFSGVYLEKETVEKAIQDAGFQVLRCNCV 239
Cdd:pfam01234 161 CVVTIFCLEYACPDLEEYCRALRNLASLLKPGGHLVLGGVLEESWYMFGEKKFSCLYLSKEVVEDALVDAGLDVEALQIM 240
                         250       260
                  ....*....|....*....|.
gi 157816899  240 SLSYSEAYCVNDGLYFVVARK 260
Cdd:pfam01234 241 PQSYSYKVADHDGVFFLVARK 261
 
Name Accession Description Interval E-value
NNMT_PNMT_TEMT pfam01234
NNMT/PNMT/TEMT family;
1-260 6.16e-148

NNMT/PNMT/TEMT family;


Pssm-ID: 395988  Cd Length: 261  Bit Score: 414.13  E-value: 6.16e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157816899    1 MAGKVYMGGEDYEKEFTPKDYLTTFYSFDSGTVAEQEIVKFSLQNLYQTFSTGGVGGDVLIDIGSGPTIYQLLSACEVFR 80
Cdd:pfam01234   1 MDGEGFLAGEEYKKKFNPRAYLNTYYKFASGDAAEMQIVLFFLPNLLQTFGPGGVKGDTLIDIGSGPTIYQLLSACEVFK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157816899   81 EIIATDYTPQNLQELQKWLKKEPGAYDWSSIVQHVCELEGDRSRWQEKEAKLRRTVTRVLRCDVTKTPPLGS-AQVPLAD 159
Cdd:pfam01234  81 EIHLSDYLPQNRDELIKWLKKEPGAFDWSPVLKHICELEGDRECWQEKEEKLRALVKRVLKCDVHQSPPLGAgVQLPPAD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157816899  160 CVLTFLAMECACPDVDTYRAALRRLAGLLKPGGHLVTLVTLRFQHYMVGPKKFSGVYLEKETVEKAIQDAGFQVLRCNCV 239
Cdd:pfam01234 161 CVVTIFCLEYACPDLEEYCRALRNLASLLKPGGHLVLGGVLEESWYMFGEKKFSCLYLSKEVVEDALVDAGLDVEALQIM 240
                         250       260
                  ....*....|....*....|.
gi 157816899  240 SLSYSEAYCVNDGLYFVVARK 260
Cdd:pfam01234 241 PQSYSYKVADHDGVFFLVARK 261
GntF_guanitoxin NF041360
guanitoxin biosynthesis pre-guanitoxin forming N-methyltransferase GntF;
14-232 2.49e-20

guanitoxin biosynthesis pre-guanitoxin forming N-methyltransferase GntF;


Pssm-ID: 469252  Cd Length: 273  Bit Score: 87.38  E-value: 2.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157816899  14 KEFTPKDYLTTF---YSFD--SGTVAEQEivKFsLQNLYQTFSTGGVGGDVLIDIGSGPTIYQLLSACEVFREIIATDYT 88
Cdd:NF041360  11 QSFEAIPYLNEYfnnYPSDkyGGIGFENE--KF-LQFFAEVAHEHHLNNSLLLDFGCGPTIYSIISLGQNCREIHMSDYL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157816899  89 PQNLQELQKWLKKEPGAYDWSSIVQHVCELEG--------------DRSRWQEKEAKLRRTVTRVLRCDVTKTPPLGSAQ 154
Cdd:NF041360  88 QQNLEQVKLWQQGKPEAFDWNPYLRRALQIETalnqnqpidsfldvTDEEIEERARLLQEKITSIRKGNARATNPVGEEG 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157816899 155 VPLADCVLTFLAMECACPDVDTYRAALRRLAGLLKPGGHLVTLVTLRFQHYMVGPKKFSGVYLEKETVEKAIQDAGFQ 232
Cdd:NF041360 168 KALYEAVISCFCLEGVAEDLAEWKNLIANLSSIIKPGGLLIFATQIEADSYRIGDDYGRVLNLTEQDIVQTLLNCNFE 245
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
60-200 2.43e-04

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: 39.72  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157816899  60 LIDIGSGPTIYQLLSACEVFREIIATDYTPQNLQELQKwlkkepgaydwssivqhvcelegdrsrwqeKEAKLRRTVTRV 139
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARK------------------------------AAAALLADNVEV 51
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157816899 140 LRCDVTKTPPLGSAQVplaDCVLTFLAMECACPDvdtYRAALRRLAGLLKPGGHLVTLVTL 200
Cdd:cd02440   52 LKGDAEELPPEADESF---DVIISDPPLHHLVED---LARFLEEARRLLKPGGVLVLTLVL 106
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
57-232 6.25e-04

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: 39.21  E-value: 6.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157816899  57 GDVLIDIGSGpTIYQLLSACEVFREIIATDYTPQNLQELqkwlkkepgaydwssivqhvcelegdRSRWQEKEAKLRrtv 136
Cdd:COG2226   23 GARVLDLGCG-TGRLALALAERGARVTGVDISPEMLELA--------------------------RERAAEAGLNVE--- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157816899 137 trVLRCDVTKTPpLGSAQVplaDCVLTFLAMeCACPDVDtyrAALRRLAGLLKPGGHLVTLVTLRfqhymvgPkkfsgvy 216
Cdd:COG2226   73 --FVVGDAEDLP-FPDGSF---DLVISSFVL-HHLPDPE---RALAEIARVLKPGGRLVVVDFSP-------P------- 128
                        170
                 ....*....|....*.
gi 157816899 217 lEKETVEKAIQDAGFQ 232
Cdd:COG2226  129 -DLAELEELLAEAGFE 143
 
Name Accession Description Interval E-value
NNMT_PNMT_TEMT pfam01234
NNMT/PNMT/TEMT family;
1-260 6.16e-148

NNMT/PNMT/TEMT family;


Pssm-ID: 395988  Cd Length: 261  Bit Score: 414.13  E-value: 6.16e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157816899    1 MAGKVYMGGEDYEKEFTPKDYLTTFYSFDSGTVAEQEIVKFSLQNLYQTFSTGGVGGDVLIDIGSGPTIYQLLSACEVFR 80
Cdd:pfam01234   1 MDGEGFLAGEEYKKKFNPRAYLNTYYKFASGDAAEMQIVLFFLPNLLQTFGPGGVKGDTLIDIGSGPTIYQLLSACEVFK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157816899   81 EIIATDYTPQNLQELQKWLKKEPGAYDWSSIVQHVCELEGDRSRWQEKEAKLRRTVTRVLRCDVTKTPPLGS-AQVPLAD 159
Cdd:pfam01234  81 EIHLSDYLPQNRDELIKWLKKEPGAFDWSPVLKHICELEGDRECWQEKEEKLRALVKRVLKCDVHQSPPLGAgVQLPPAD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157816899  160 CVLTFLAMECACPDVDTYRAALRRLAGLLKPGGHLVTLVTLRFQHYMVGPKKFSGVYLEKETVEKAIQDAGFQVLRCNCV 239
Cdd:pfam01234 161 CVVTIFCLEYACPDLEEYCRALRNLASLLKPGGHLVLGGVLEESWYMFGEKKFSCLYLSKEVVEDALVDAGLDVEALQIM 240
                         250       260
                  ....*....|....*....|.
gi 157816899  240 SLSYSEAYCVNDGLYFVVARK 260
Cdd:pfam01234 241 PQSYSYKVADHDGVFFLVARK 261
GntF_guanitoxin NF041360
guanitoxin biosynthesis pre-guanitoxin forming N-methyltransferase GntF;
14-232 2.49e-20

guanitoxin biosynthesis pre-guanitoxin forming N-methyltransferase GntF;


Pssm-ID: 469252  Cd Length: 273  Bit Score: 87.38  E-value: 2.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157816899  14 KEFTPKDYLTTF---YSFD--SGTVAEQEivKFsLQNLYQTFSTGGVGGDVLIDIGSGPTIYQLLSACEVFREIIATDYT 88
Cdd:NF041360  11 QSFEAIPYLNEYfnnYPSDkyGGIGFENE--KF-LQFFAEVAHEHHLNNSLLLDFGCGPTIYSIISLGQNCREIHMSDYL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157816899  89 PQNLQELQKWLKKEPGAYDWSSIVQHVCELEG--------------DRSRWQEKEAKLRRTVTRVLRCDVTKTPPLGSAQ 154
Cdd:NF041360  88 QQNLEQVKLWQQGKPEAFDWNPYLRRALQIETalnqnqpidsfldvTDEEIEERARLLQEKITSIRKGNARATNPVGEEG 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157816899 155 VPLADCVLTFLAMECACPDVDTYRAALRRLAGLLKPGGHLVTLVTLRFQHYMVGPKKFSGVYLEKETVEKAIQDAGFQ 232
Cdd:NF041360 168 KALYEAVISCFCLEGVAEDLAEWKNLIANLSSIIKPGGLLIFATQIEADSYRIGDDYGRVLNLTEQDIVQTLLNCNFE 245
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
60-200 2.43e-04

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: 39.72  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157816899  60 LIDIGSGPTIYQLLSACEVFREIIATDYTPQNLQELQKwlkkepgaydwssivqhvcelegdrsrwqeKEAKLRRTVTRV 139
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARK------------------------------AAAALLADNVEV 51
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157816899 140 LRCDVTKTPPLGSAQVplaDCVLTFLAMECACPDvdtYRAALRRLAGLLKPGGHLVTLVTL 200
Cdd:cd02440   52 LKGDAEELPPEADESF---DVIISDPPLHHLVED---LARFLEEARRLLKPGGVLVLTLVL 106
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
57-232 6.25e-04

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: 39.21  E-value: 6.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157816899  57 GDVLIDIGSGpTIYQLLSACEVFREIIATDYTPQNLQELqkwlkkepgaydwssivqhvcelegdRSRWQEKEAKLRrtv 136
Cdd:COG2226   23 GARVLDLGCG-TGRLALALAERGARVTGVDISPEMLELA--------------------------RERAAEAGLNVE--- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157816899 137 trVLRCDVTKTPpLGSAQVplaDCVLTFLAMeCACPDVDtyrAALRRLAGLLKPGGHLVTLVTLRfqhymvgPkkfsgvy 216
Cdd:COG2226   73 --FVVGDAEDLP-FPDGSF---DLVISSFVL-HHLPDPE---RALAEIARVLKPGGRLVVVDFSP-------P------- 128
                        170
                 ....*....|....*.
gi 157816899 217 lEKETVEKAIQDAGFQ 232
Cdd:COG2226  129 -DLAELEELLAEAGFE 143
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
61-195 6.98e-03

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 34.95  E-value: 6.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157816899   61 IDIGSGPTIYqLLSACEVFREIIATDYTPQNLQELQKWLKKEPGAYdwssivqhvcelegdrsrwqekeaklrrtvtrvL 140
Cdd:pfam08241   1 LDVGCGTGLL-TELLARLGARVTGVDISPEMLELAREKAPREGLTF---------------------------------V 46
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 157816899  141 RCDVTKTPpLGSAQVplaDCVLTFLAMECaCPDVDtyrAALRRLAGLLKPGGHLV 195
Cdd:pfam08241  47 VGDAEDLP-FPDNSF---DLVLSSEVLHH-VEDPE---RALREIARVLKPGGILI 93
 
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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