ID A0A0V1D2V5_TRIBR Unreviewed; 473 AA.
AC A0A0V1D2V5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
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|EMBL:KRY55845.1};
GN ORFNames=T03_6474 {ECO:0000313|EMBL:KRY55845.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY55845.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY55845.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY55845.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY55845.1}.
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DR EMBL; JYDI01000050; KRY55845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1D2V5; -.
DR STRING; 45882.A0A0V1D2V5; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
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:InterPro.
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}; Reference proteome {ECO:0000313|Proteomes:UP000054653};
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 78..312
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
SQ SEQUENCE 473 AA; 54205 MW; 411E59C9A39CC19C CRC64;
MVIGKDEILS RCGLITKDMV MNLTTDVSLN SRNAQWNRLI YVKSGADALI DTQKPFQRKF
IRNRMDFKEE FEQWCKKNGV KTFSVKPEAV DNCGIGMVAT EDIPQGKLLV LVPRKVMLTT
ESCLQSCPAM RDLLMGDPIL SSMNNVSLTM AVLYELFLGK KSCWYEYLRF LPTEYSVPLY
FDEEAFSVLK FSAFFDQVVS VYTSIVRQYS YFYQLLINRN SPFRGTPFKE TNFTFENFRW
AASTVMTRIN FIPFSEMSVA SAMNEAALIP MWDLFNHEIQ TLCSDYDTDT DYGRVFSVKS
WSAGDQVFIH YGNRGNYELL IGGGFVVDNN PFDYFPLKLS LGQASENYSL RLEVLQQRDL
AETKVHRICW AEDEMFQPSI LQFAIVHSAD VAALEEIKNM PTGTAPISDQ LRFKAKSFLK
NRLSLLLNTY AKLPEENDEN PHQKLCLVCL DSEKQLLQHA IDALESCTFP TEI
//
