SETD3_XENTR
ID SETD3_XENTR Reviewed; 582 AA.
AC B7ZUF3; A4IGP7; Q28I16;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Actin-histidine N-methyltransferase {ECO:0000250|UniProtKB:Q86TU7};
DE EC=2.1.1.85 {ECO:0000250|UniProtKB:Q86TU7};
DE AltName: Full=Protein-L-histidine N-tele-methyltransferase {ECO:0000305};
DE AltName: Full=SET domain-containing protein 3 {ECO:0000305};
GN Name=setd3 {ECO:0000250|UniProtKB:Q86TU7};
GN ORFNames=TEgg034h09.1 {ECO:0000303|Ref.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neurula;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protein-histidine N-methyltransferase that specifically
CC mediates 3-methylhistidine (tele-methylhistidine) methylation of actin
CC at 'His-73'. Does not have protein-lysine N-methyltransferase activity
CC and probably only catalyzes histidine methylation of actin.
CC {ECO:0000250|UniProtKB:Q86TU7}.
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:0000250|UniProtKB:Q86TU7};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86TU7}.
CC -!- DOMAIN: The SET domain specifically recognizes and binds actin,
CC suggesting that it does not accommodate substrates diverging from
CC actin. {ECO:0000250|UniProtKB:Q86TU7}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. SETD3 actin-histidine methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00898}.
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DR EMBL; CR760640; CAJ81720.1; -; mRNA.
DR EMBL; BC135194; AAI35195.1; -; mRNA.
DR EMBL; BC171209; AAI71209.1; -; mRNA.
DR RefSeq; NP_001016577.1; NM_001016577.2.
DR RefSeq; XP_012823880.1; XM_012968426.2.
DR AlphaFoldDB; B7ZUF3; -.
DR SMR; B7ZUF3; -.
DR STRING; 8364.ENSXETP00000062313; -.
DR PaxDb; B7ZUF3; -.
DR PRIDE; B7ZUF3; -.
DR Ensembl; ENSXETT00000065894; ENSXETP00000062313; ENSXETG00000011436.
DR GeneID; 549331; -.
DR KEGG; xtr:549331; -.
DR CTD; 84193; -.
DR Xenbase; XB-GENE-1016707; setd3.
DR eggNOG; KOG1337; Eukaryota.
DR HOGENOM; CLU_028272_0_0_1; -.
DR InParanoid; B7ZUF3; -.
DR OMA; DFWMKIP; -.
DR OrthoDB; 489371at2759; -.
DR PhylomeDB; B7ZUF3; -.
DR TreeFam; TF354226; -.
DR Reactome; R-XTR-3214841; PKMTs methylate histone lysines.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000011436; Expressed in skeletal muscle tissue and 15 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); ISS:UniProtKB.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IBA:GO_Central.
DR GO; GO:0018064; F:protein-L-histidine N-tele-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0030047; P:actin modification; ISS:UniProtKB.
DR GO; GO:0010452; P:histone H3-K36 methylation; ISS:UniProtKB.
DR GO; GO:0018021; P:peptidyl-histidine methylation; ISS:UniProtKB.
DR GO; GO:0018027; P:peptidyl-lysine dimethylation; ISS:UniProtKB.
DR GO; GO:0018026; P:peptidyl-lysine monomethylation; ISS:UniProtKB.
DR GO; GO:0018023; P:peptidyl-lysine trimethylation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR CDD; cd19176; SET_SETD3; 1.
DR Gene3D; 3.90.1420.10; -; 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 Pfam; PF09273; Rubis-subs-bind; 1.
DR Pfam; PF00856; SET; 1.
DR SUPFAM; SSF81822; SSF81822; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51565; SAM_MT85_SETD3; 1.
DR PROSITE; PS50280; SET; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Cytoplasm; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..582
FT /note="Actin-histidine N-methyltransferase"
FT /id="PRO_0000408344"
FT DOMAIN 94..314
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 550..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 75
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86TU7"
FT BINDING 104..106
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86TU7"
FT BINDING 254
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86TU7"
FT BINDING 275..279
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86TU7"
FT BINDING 325..327
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86TU7"
FT CONFLICT 16
FT /note="Missing (in Ref. 1; CAJ81720)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="G -> S (in Ref. 2; AAI35195)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="S -> C (in Ref. 1; CAJ81720)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 582 AA; 66117 MW; 492BAA37924ED14E CRC64;
MGKKSRVKTQ KSGSGAAAAV SPKEMLNLIS ELLQKCSNPN STPGREWEEY VQIRGLVEKI
RKKQRGLSVV FDGKREDYFP ELMEWCKENG ASTDGFELVE FPEEGFGLKA TREIKAEELF
LWVPRKLLMT VESAKGSVLG PLYSQDRILQ AMGNITLAFH LLCERADPNS FWLPYIKTLP
NEYDTPLYFN EDEVQYLQST QAILDVFSQY KNTARQYAYF YKVIQTHPNA NKLPLKDSFT
FDDYRWAVSS VMTRQNQIPT EDGSRVTLAL IPLWDMCNHT NGLITTGYNL EDDRCECVAL
QDFKSGEQIY IFYGTRSNAE FVIHNGFFFE NNLHDRVKIK LGVSKSDRLY AMKAEVLARA
GIPTSSVFAL HVTEPPISAQ LLAFLRVFCM NEDELKGHLI GDHAIDKIFT LGNSEFPVSW
ENEIKLWTFL EARASLLLKT YKTTVEDDNK VLEQPDMTFH SAMAIKLRRV EKEILEKALK
SASDNRKLYS KNSEEGTPLP KYEASNIAFV ENSVADSKLP VVLKSLDDEE VKLQEAITIS
EITENGFLND KDLLPNGTKS ENDSFLAEDN QQETGNAKDF CS
