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Database: UniProt
Entry: A0A3B3CJE1_ORYME
LinkDB: A0A3B3CJE1_ORYME
Original site: A0A3B3CJE1_ORYME 
ID   A0A3B3CJE1_ORYME        Unreviewed;       546 AA.
AC   A0A3B3CJE1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=protein-histidine N-methyltransferase {ECO:0000256|PROSITE-ProRule:PRU00898};
DE            EC=2.1.1.85 {ECO:0000256|PROSITE-ProRule:PRU00898};
OS   Oryzias melastigma (Marine medaka).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000017460.1, ECO:0000313|Proteomes:UP000261560};
RN   [1] {ECO:0000313|Ensembl:ENSOMEP00000017460.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-histidyl-[protein] + S-adenosyl-L-methionine = H(+) +
CC         N(tele)-methyl-L-histidyl-[protein] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:19369, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:11600,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16367, ChEBI:CHEBI:29979,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.85;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU00898};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC       superfamily. SETD3 actin-histidine methyltransferase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU00898}.
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DR   AlphaFoldDB; A0A3B3CJE1; -.
DR   Ensembl; ENSOMET00000026208.1; ENSOMEP00000017460.1; ENSOMEG00000019180.1.
DR   GeneTree; ENSGT00940000153577; -.
DR   Proteomes; UP000261560; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0018064; F:protein-L-histidine N-tele-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd19176; SET_SETD3; 1.
DR   Gene3D; 3.90.1420.10; Rubisco LSMT, substrate-binding domain; 1.
DR   Gene3D; 3.90.1410.10; set domain protein methyltransferase, domain 1; 2.
DR   InterPro; IPR015353; Rubisco_LSMT_subst-bd.
DR   InterPro; IPR036464; Rubisco_LSMT_subst-bd_sf.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR025785; SETD3.
DR   InterPro; IPR044428; SETD3_SET.
DR   PANTHER; PTHR13271:SF47; ACTIN-HISTIDINE N-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR13271; UNCHARACTERIZED PUTATIVE METHYLTRANSFERASE; 1.
DR   Pfam; PF09273; Rubis-subs-bind; 1.
DR   Pfam; PF00856; SET; 1.
DR   SUPFAM; SSF81822; RuBisCo LSMT C-terminal, substrate-binding domain; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS51565; SAM_MT85_SETD3; 1.
DR   PROSITE; PS50280; SET; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU00898};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU00898};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00898}.
FT   DOMAIN          94..256
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..546
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   546 AA;  61553 MW;  4015081877B3BE5B CRC64;
     MGKKSRVKTQ KSGSAATTVA SPKEMMNLIS ELLQKCSSPA PSSGKEWEEY IQIRGLVEKI
     RKKQKGLTTV FEGSREDSFP DLMSWAQENG ASCDGFTVTN FGTEGYGLRA TRDIKAEELF
     LWVPRKMLMT VESAQNSILG PIYSQDRILQ AMGNVTLALH LLCERADPAS FWLPYIRSLP
     QEYDTPLYYQ QEDVQLLLCT QAVQDVLNQY KNTARQYAYF YKLVQITTGY NLEDDRCECV
     ALQDYKENEQ VYIFYGTRSN AEFVIHNGFF FQDNAHDRVK IKLGVSKSER LYAMKAEVLA
     RAGIPASCVF ALHCNDPPIS AQLLAFLRVF CMTEEELKDY LLGERAINKI FTLGNSEFPV
     SWENEIKLWT FLETRAALLL KTYKTTSEED RSILEKPDLS LHTRLAVQLR LAEKQILENA
     SASGRAKRLQ FQEKLNEGAP LPQFEESDIA LLENNDPDAK LPVILHKLEE VEEGQGMEEE
     EPLLNGGKGD YGMGTEPNGE AVLEKTQKTL GDSVLIQNGS LDQKGPQEPE NPSANRTEEQ
     PIDTSA
//
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