ID A0A452ER43_CAPHI Unreviewed; 578 AA.
AC A0A452ER43;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=LOC108633232 {ECO:0000313|Ensembl:ENSCHIP00000014565.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000014565.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000014565.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000014565.1}
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 -!- SUBUNIT: Interacts with MYOD1. {ECO:0000256|ARBA:ARBA00011368}.
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 EMBL; LWLT01000007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A452ER43; -.
DR STRING; 9925.ENSCHIP00000014565; -.
DR Ensembl; ENSCHIT00000022363.1; ENSCHIP00000014565.1; ENSCHIG00000015564.1.
DR GeneTree; ENSGT00940000153577; -.
DR OMA; STIWSRF; -.
DR Proteomes; UP000291000; Chromosome 8.
DR Bgee; ENSCHIG00000015564; Expressed in longissimus thoracis muscle and 17 other cell types or tissues.
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; 2.
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}; Reference proteome {ECO:0000313|Proteomes:UP000291000};
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 101..321
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 578 AA; 65022 MW; 4E470E335BAACCF3 CRC64;
MAPVSQKMGK KSRVKTQKSG TGAAASVSPK ETLNLTSELL QKCSSPAPGP GKEWEEYVQI
RSLVEKIRKK QKGLSVTFDG KREDYFPDLM KWASENGASV EGFEIVNFKE EGFGLRATRD
IKAEELFLWV PRKLLMTVES AKTSVLGPLY SQDRILQAMG NITLAFHLLC ERADPNSFWQ
PYIQTLPSEY DTPLYFEEDE VRYLQSTQAI HDVFSQYKNT ARQYAYFYKV IQTHPHAHKL
PLKDSFTYED YRRAVSSVMT RQNQIPTEDG SRVTLALIPL WDMCNHTSGL ITTGYNLEDD
RCECVAQQDF RAGEQIYIFY GTRSNAEFVI HSGFFFDNNS HDRVKIKLGV SRGDRLYAMK
AEVLARAGIP TSSVFALHFT EPPISAQLLA FLRVFCMTEE ELKEHLLGDS AIDRIFTLGN
SEYPVSWDNE EDKSFLKNHD LSARATMAIK LRLGEKEILE RAVKSAAANR EFYRRQMEER
APLPKYEEGG AGLLEGVADS RLPLVLRSLE GEAGAQEALT LSEAVRRAQA AEHGLVNGES
AIPNGTRSEK ETLTQEESKR ATGDAKEPSS DSAEDVAQ
//
