ID A0A2D0RR15_ICTPU Unreviewed; 569 AA.
AC A0A2D0RR15;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=protein-histidine N-methyltransferase {ECO:0000256|PROSITE-ProRule:PRU00898};
DE EC=2.1.1.85 {ECO:0000256|PROSITE-ProRule:PRU00898};
GN Name=setd3 {ECO:0000313|RefSeq:XP_017332382.1,
GN ECO:0000313|RefSeq:XP_017332384.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017332382.1};
RN [1] {ECO:0000313|RefSeq:XP_017332382.1, ECO:0000313|RefSeq:XP_017332384.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017332382.1,
RC ECO:0000313|RefSeq:XP_017332384.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_017332382.1; XM_017476893.3.
DR RefSeq; XP_017332384.1; XM_017476895.3.
DR RefSeq; XP_017332385.1; XM_017476896.1.
DR STRING; 7998.ENSIPUP00000014621; -.
DR Ensembl; ENSIPUT00000015222; ENSIPUP00000014610; ENSIPUG00000009958.
DR GeneID; 108270323; -.
DR KEGG; ipu:108270323; -.
DR CTD; 84193; -.
DR OMA; DFWMKIP; -.
DR OrthoDB; 51002at2759; -.
DR Proteomes; UP000221080; Chromosome 9.
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; 1.
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..314
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 525..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 569 AA; 64400 MW; 51FA6569F87DEB8F CRC64;
MGKKSRVKTQ KSGTGGTAMV SPKEMMNLIS ELLQKCSGAA PSPGKEWDEY VQIRTLVEKI
RKKQKGVSVG FEGSREDYFP ELMAWAAECG ASCEGFEIAS FGDEGYGLRA TRDIKAEELF
LWIPRKMLMT VESAKNSVLG PLYGQDRILQ AMGNVTLALH LLCERANPES PWLPYIKTLP
AHYDTPLYFE EEEVRHLLAT QAIQDVLSQY KNTARQYAYF YKVIHTHPNA SKLPLKDAFT
FDDYRWAVSS VMTRQNQIPT EDGSRVTLAL IPLWDMCNHT NGLITTGYNL EDDRCECVAL
HDYKESEQIY IFYGTRSNAE FVIHSGFFFE DNAHDRVKIK LGVSKSERLY AMKAEVLARA
GIPASSVFAL HCSEPPISAQ LLAFLRVFCM TEEELRDYLV GDHAINKIFT LGNAEFPVSW
ENEIKLWTFL ETRAALLLKT YKSTSEEDGA MLQKPDLSPH SRMAVKLRRA EKEILERAEA
SGRGKRLHFQ KQLDDGAPLP VYEESDIALL ENADAKLPIV LHQLEEEEED EDLKMPLLNG
ERKEKQGETG GERAEPSAQR TEDTCKDPE
//
