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Database: UniProt
Entry: B7ZUF3
LinkDB: B7ZUF3
Original site: B7ZUF3 
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   13-FEB-2019, entry version 53.
DE   RecName: Full=Actin-histidine N-methyltransferase {ECO:0000250|UniProtKB:Q86TU7};
DE            EC=2.1.1.85 {ECO:0000250|UniProtKB:Q86TU7};
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;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   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 methylation of actin at 'His-73'. Does not have protein-
CC       lysine N-methyltransferase activity and probably only catalyzes
CC       histidine methylation of actin. {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
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. SETD3 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00898}.
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   UniGene; Str.4852; -.
DR   SMR; B7ZUF3; -.
DR   STRING; 8364.ENSXETP00000062313; -.
DR   PaxDb; 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   eggNOG; ENOG410Y7DR; LUCA.
DR   GeneTree; ENSGT00940000153577; -.
DR   HOGENOM; HOG000049107; -.
DR   HOVERGEN; HBG062823; -.
DR   InParanoid; B7ZUF3; -.
DR   KO; K19199; -.
DR   OMA; CERADPN; -.
DR   OrthoDB; 489371at2759; -.
DR   TreeFam; TF354226; -.
DR   Proteomes; UP000008143; Unassembled WGS sequence.
DR   Bgee; ENSXETG00000011436; Expressed in 11 organ(s), highest expression level in skeletal muscle tissue.
DR   ExpressionAtlas; B7ZUF3; baseline.
DR   GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central.
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:0016279; F:protein-lysine N-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR   GO; GO:0010452; P:histone H3-K36 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   Gene3D; 3.90.1420.10; -; 1.
DR   InterPro; IPR025785; Hist-Lys_N-MeTrfase_SETD3.
DR   InterPro; IPR015353; Rubisco_LSMT_subst-bd.
DR   InterPro; IPR036464; Rubisco_LSMT_subst-bd_sf.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF09273; Rubis-subs-bind; 1.
DR   Pfam; PF00856; SET; 1.
DR   SUPFAM; SSF81822; SSF81822; 1.
DR   PROSITE; PS51565; SAM_MT43_SETD3; 1.
DR   PROSITE; PS50280; SET; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; Complete proteome; Cytoplasm; Methyltransferase;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    582       Actin-histidine N-methyltransferase.
FT                                /FTId=PRO_0000408344.
FT   DOMAIN       94    314       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   REGION      104    106       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:Q86TU7}.
FT   REGION      275    279       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:Q86TU7}.
FT   REGION      325    327       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:Q86TU7}.
FT   BINDING      75     75       S-adenosyl-L-methionine.
FT                                {ECO:0000250|UniProtKB:Q86TU7}.
FT   BINDING     254    254       S-adenosyl-L-methionine.
FT                                {ECO:0000250|UniProtKB:Q86TU7}.
FT   CONFLICT     16     16       Missing (in Ref. 1; CAJ81720).
FT                                {ECO:0000305}.
FT   CONFLICT    282    282       G -> S (in Ref. 2; AAI35195).
FT                                {ECO:0000305}.
FT   CONFLICT    564    564       S -> C (in Ref. 1; CAJ81720).
FT                                {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
//
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