ID   A0A2Y9JXM0_ENHLU        Unreviewed;       287 AA.
AC   A0A2Y9JXM0;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   02-DEC-2020, entry version 10.
DE   SubName: Full=phenylethanolamine N-methyltransferase {ECO:0000313|RefSeq:XP_022365753.1};
GN   Name=LOC111151828 {ECO:0000313|RefSeq:XP_022365753.1};
OS   Enhydra lutris kenyoni.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Lutrinae;
OC   Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022365753.1};
RN   [1] {ECO:0000313|RefSeq:XP_022365753.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022365753.1};
RG   RefSeq;
RL   Submitted (JUN-2018) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. NNMT/PNMT/TEMT family. {ECO:0000256|ARBA:ARBA00007996}.
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DR   RefSeq; XP_022365753.1; XM_022510045.1.
DR   KEGG; elk:111151828; -.
DR   Proteomes; UP000248482; Genome assembly.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   InterPro; IPR025820; NNMT/PNMT/TEMT_CS.
DR   InterPro; IPR000940; NNMT_TEMT_trans.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   PANTHER; PTHR10867; PTHR10867; 1.
DR   Pfam; PF01234; NNMT_PNMT_TEMT; 1.
DR   PIRSF; PIRSF000384; PNMTase; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS01100; NNMT_PNMT_TEMT; 1.
DR   PROSITE; PS51681; SAM_MT_NNMT_PNMT_TEMT; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|RefSeq:XP_022365753.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRSR:PIRSR000384-1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679,
KW   ECO:0000313|RefSeq:XP_022365753.1}.
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          83..84
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000384-1"
FT   REGION          162..163
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000384-1"
FT   BINDING         39
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000384-1"
FT   BINDING         44
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000384-1"
FT   BINDING         89
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000384-1"
FT   BINDING         105
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000384-1"
FT   BINDING         110
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000384-1"
SQ   SEQUENCE   287 AA;  31259 MW;  F8276070A04A3BB2 CRC64;
     MSKADLNPAA GTAPDSAPDS DPGPAAVASA YQRFEPRAYL RNNYAPPRGD LSHPDGVGPW
     KLRCLAQTFA TGEVSGHSLI DIGSGPTIYQ LLSACAHFED ITLTDFLEVN RQELGLWLRE
     EPGAFDWSTY SRHVCLIEGK GESWQEKELQ LRARVKRILH IDVHQPQPLG AGSPAPLPAD
     ALVSTFCLEA VSPDLASFQR ALDHITTLLR PGGHLLLIGA LEESWYLAGE ARLAVVPMGK
     EEVMEALVRS GYEVRDLSTY VMPACLQTGV DDVKGIFFAW AQKKVAV
//