ID A0A3B3S7Q8_9TELE Unreviewed; 573 AA.
AC A0A3B3S7Q8;
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 Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000026021.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000026021.1}
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; A0A3B3S7Q8; -.
DR STRING; 1676925.ENSPKIP00000026021; -.
DR Ensembl; ENSPKIT00000006770.1; ENSPKIP00000026021.1; ENSPKIG00000008654.1.
DR GeneTree; ENSGT00940000153577; -.
DR OrthoDB; 51002at2759; -.
DR Proteomes; UP000261540; 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; 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 550..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 573 AA; 64077 MW; DD2A9DCBC54D2F35 CRC64;
MGKKSRVKTQ KWGTGPTAVA NPKEMLNLVS ELLQKCSGAA PPPGQEWAEY VQIRSLVEKI
RKKQKGLSVV FDGMREEHFP ELMAWAAENG ASCEGFEICN FAEQGYGLKA TRDIKAEELF
LWIPRKMLLT VESAKNSVLG SLYSQDRILQ AMGNVTLALH LLCERSNPSS FWLPYIKSLP
SEYDTPLYYE EEEVRCLQAT QAIQDVFSQY KNTARQYAYF FKVIQTHPAA SKLPFKESFT
FDDYRWAVSS VMTRQNQIPT EDGSRVTLAL IPLWDMCNHT NGLITTGYNL EDDRCECVAL
MDYKKDEQIY IFYGTRSNAE FVIHNGFFYE TNAHDRVKIK LGVSKSERLY AMKAEVLARA
GIPASSMFAL HGADPPMSAQ LLAFLRVFCM TEEELKDYLV GEQAMNNILS LGNVELPVSW
ENEIKLWTFL ETRASLLLKT YSSTTESDQA LLEQPGLSFH TRVAIQLRLA EKQILEGAVG
SGRAQREHFR KLLEEEAPLP RRQEAGDPDG QLPLVLRELE EANDATLGPG DAGDAADALL
LNGGVAMEIG NGVPHKGGPG VERTGDGVEE NSQ
//
