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Conserved domains on  [gi|767995052|ref|XP_011523211|]
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phenylethanolamine N-methyltransferase isoform X1 [Homo sapiens]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 106779)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
1-181 3.86e-96

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.).


The actual alignment was detected with superfamily member pfam01234:

Pssm-ID: 473071  Cd Length: 261  Bit Score: 279.31  E-value: 3.86e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995052    1 MTDFLEVNRQELGRWLQEEPGAFNWSMYSQHACLIEGKGECWQDKERQLRARVKRVLPIDVHQPQPLGAGSPAPlPADAL 80
Cdd:pfam01234  84 LSDYLPQNRDELIKWLKKEPGAFDWSPVLKHICELEGDRECWQEKEEKLRALVKRVLKCDVHQSPPLGAGVQLP-PADCV 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995052   81 VSAFCLEAVSPDLASFQRALDHITTLLRPGGHLLLIGALEESWYLAGEARLTVVPVSEEEVREALVRSGYKVRDLRtyIM 160
Cdd:pfam01234 163 VTIFCLEYACPDLEEYCRALRNLASLLKPGGHLVLGGVLEESWYMFGEKKFSCLYLSKEVVEDALVDAGLDVEALQ--IM 240
                         170       180
                  ....*....|....*....|.
gi 767995052  161 PAHLQTGVDDVKGVFFAWAQK 181
Cdd:pfam01234 241 PQSYSYKVADHDGVFFLVARK 261
 
Name Accession Description Interval E-value
NNMT_PNMT_TEMT pfam01234
NNMT/PNMT/TEMT family;
1-181 3.86e-96

NNMT/PNMT/TEMT family;


Pssm-ID: 395988  Cd Length: 261  Bit Score: 279.31  E-value: 3.86e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995052    1 MTDFLEVNRQELGRWLQEEPGAFNWSMYSQHACLIEGKGECWQDKERQLRARVKRVLPIDVHQPQPLGAGSPAPlPADAL 80
Cdd:pfam01234  84 LSDYLPQNRDELIKWLKKEPGAFDWSPVLKHICELEGDRECWQEKEEKLRALVKRVLKCDVHQSPPLGAGVQLP-PADCV 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995052   81 VSAFCLEAVSPDLASFQRALDHITTLLRPGGHLLLIGALEESWYLAGEARLTVVPVSEEEVREALVRSGYKVRDLRtyIM 160
Cdd:pfam01234 163 VTIFCLEYACPDLEEYCRALRNLASLLKPGGHLVLGGVLEESWYMFGEKKFSCLYLSKEVVEDALVDAGLDVEALQ--IM 240
                         170       180
                  ....*....|....*....|.
gi 767995052  161 PAHLQTGVDDVKGVFFAWAQK 181
Cdd:pfam01234 241 PQSYSYKVADHDGVFFLVARK 261
GntF_guanitoxin NF041360
guanitoxin biosynthesis pre-guanitoxin forming N-methyltransferase GntF;
1-157 4.71e-20

guanitoxin biosynthesis pre-guanitoxin forming N-methyltransferase GntF;


Pssm-ID: 469252  Cd Length: 273  Bit Score: 84.68  E-value: 4.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995052   1 MTDFLEVNRQELGRWLQEEPGAFNWSMYSQHACLIEG--------------KGECWQDKERQLRARVKRVLPIDVHQPQP 66
Cdd:NF041360  83 MSDYLQQNLEQVKLWQQGKPEAFDWNPYLRRALQIETalnqnqpidsfldvTDEEIEERARLLQEKITSIRKGNARATNP 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995052  67 LGAGSPAPLpaDALVSAFCLEAVSPDLASFQRALDHITTLLRPGGHLLLIGALEESWYLAGEARLTVVPVSEEEVREALV 146
Cdd:NF041360 163 VGEEGKALY--EAVISCFCLEGVAEDLAEWKNLIANLSSIIKPGGLLIFATQIEADSYRIGDDYGRVLNLTEQDIVQTLL 240
                        170
                 ....*....|.
gi 767995052 147 RSGYKVRDLRT 157
Cdd:NF041360 241 NCNFELGSIKT 251
 
Name Accession Description Interval E-value
NNMT_PNMT_TEMT pfam01234
NNMT/PNMT/TEMT family;
1-181 3.86e-96

NNMT/PNMT/TEMT family;


Pssm-ID: 395988  Cd Length: 261  Bit Score: 279.31  E-value: 3.86e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995052    1 MTDFLEVNRQELGRWLQEEPGAFNWSMYSQHACLIEGKGECWQDKERQLRARVKRVLPIDVHQPQPLGAGSPAPlPADAL 80
Cdd:pfam01234  84 LSDYLPQNRDELIKWLKKEPGAFDWSPVLKHICELEGDRECWQEKEEKLRALVKRVLKCDVHQSPPLGAGVQLP-PADCV 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995052   81 VSAFCLEAVSPDLASFQRALDHITTLLRPGGHLLLIGALEESWYLAGEARLTVVPVSEEEVREALVRSGYKVRDLRtyIM 160
Cdd:pfam01234 163 VTIFCLEYACPDLEEYCRALRNLASLLKPGGHLVLGGVLEESWYMFGEKKFSCLYLSKEVVEDALVDAGLDVEALQ--IM 240
                         170       180
                  ....*....|....*....|.
gi 767995052  161 PAHLQTGVDDVKGVFFAWAQK 181
Cdd:pfam01234 241 PQSYSYKVADHDGVFFLVARK 261
GntF_guanitoxin NF041360
guanitoxin biosynthesis pre-guanitoxin forming N-methyltransferase GntF;
1-157 4.71e-20

guanitoxin biosynthesis pre-guanitoxin forming N-methyltransferase GntF;


Pssm-ID: 469252  Cd Length: 273  Bit Score: 84.68  E-value: 4.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995052   1 MTDFLEVNRQELGRWLQEEPGAFNWSMYSQHACLIEG--------------KGECWQDKERQLRARVKRVLPIDVHQPQP 66
Cdd:NF041360  83 MSDYLQQNLEQVKLWQQGKPEAFDWNPYLRRALQIETalnqnqpidsfldvTDEEIEERARLLQEKITSIRKGNARATNP 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995052  67 LGAGSPAPLpaDALVSAFCLEAVSPDLASFQRALDHITTLLRPGGHLLLIGALEESWYLAGEARLTVVPVSEEEVREALV 146
Cdd:NF041360 163 VGEEGKALY--EAVISCFCLEGVAEDLAEWKNLIANLSSIIKPGGLLIFATQIEADSYRIGDDYGRVLNLTEQDIVQTLL 240
                        170
                 ....*....|.
gi 767995052 147 RSGYKVRDLRT 157
Cdd:NF041360 241 NCNFELGSIKT 251
AAA_8 pfam12780
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ...
92-176 5.79e-05

P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This particular family is the D4 ATP-binding region of the motor.


Pssm-ID: 463701 [Multi-domain]  Cd Length: 259  Bit Score: 42.21  E-value: 5.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995052   92 DLASFQRALDHITTLLR----PGGHLLLIGaleeswyLAGEARLTVVPVS----EEEVREALVRSGYKVRDLRTYIMPAH 163
Cdd:pfam12780   2 DLVLFRDALEHLCRICRilrqPRGHALLVG-------VGGSGRQSLTKLAafiaGYELFQIEVTRNYDMNEFREDLKKVL 74
                          90
                  ....*....|...
gi 767995052  164 LQTGVDDVKGVFF 176
Cdd:pfam12780  75 KKAGIKGKPTVFL 87
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
45-113 2.35e-03

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 35.81  E-value: 2.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767995052   45 KERQLRARVKRVLPIDVHQPQplgAGSPAPLPADALVSAFCLEAVsPDLasfQRALDHITTLLRPGGHL 113
Cdd:pfam08242  37 RERLAALGLLNAVRVELFQLD---LGELDPGSFDVVVASNVLHHL-ADP---RAVLRNIRRLLKPGGVL 98
 
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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