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Database: UniProt
Entry: Q7SXS7
LinkDB: Q7SXS7
Original site: Q7SXS7 
ID   SETD3_DANRE             Reviewed;         596 AA.
AC   Q7SXS7; A9JTB8;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   13-FEB-2019, entry version 86.
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=zgc:63842 {ECO:0000303|Ref.1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB; TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   CAUTION.
RX   PubMed=21307598; DOI=10.1271/bbb.100648;
RA   Kim D.W., Kim K.B., Kim J.Y., Seo S.B.;
RT   "Characterization of a novel histone H3K36 methyltransferase setd3 in
RT   zebrafish.";
RL   Biosci. Biotechnol. Biochem. 75:289-294(2011).
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}.
CC   -!- CAUTION: Was initially reported to have histone methyltransferase
CC       activity and methylate 'Lys-36' of histone H3 (H3K36me)
CC       (PubMed:21307598). However, this conclusion was based on mass
CC       spectrometry data wherin mass shifts were inconsistent with a bona
CC       fide methylation event and the histone methyltransferase activity
CC       could not be confirmed (By similarity).
CC       {ECO:0000250|UniProtKB:Q86TU7, ECO:0000269|PubMed:21307598}.
DR   EMBL; BC055261; AAH55261.1; -; mRNA.
DR   EMBL; BC155278; AAI55279.1; -; mRNA.
DR   RefSeq; NP_956348.1; NM_200054.1.
DR   UniGene; Dr.11469; -.
DR   ProteinModelPortal; Q7SXS7; -.
DR   SMR; Q7SXS7; -.
DR   BioGrid; 87213; 1.
DR   STRING; 7955.ENSDARP00000110046; -.
DR   PaxDb; Q7SXS7; -.
DR   PRIDE; Q7SXS7; -.
DR   GeneID; 337193; -.
DR   KEGG; dre:337193; -.
DR   CTD; 84193; -.
DR   ZFIN; ZDB-GENE-030131-9137; setd3.
DR   eggNOG; KOG1337; Eukaryota.
DR   eggNOG; ENOG410Y7DR; LUCA.
DR   HOGENOM; HOG000049107; -.
DR   HOVERGEN; HBG062823; -.
DR   InParanoid; Q7SXS7; -.
DR   KO; K19199; -.
DR   OrthoDB; 489371at2759; -.
DR   PhylomeDB; Q7SXS7; -.
DR   BRENDA; 2.1.1.43; 928.
DR   PRO; PR:Q7SXS7; -.
DR   Proteomes; UP000000437; Unplaced.
DR   GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central.
DR   GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IDA: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; IDA:UniProtKB.
DR   GO; GO:0008283; P:cell population proliferation; TAS:UniProtKB.
DR   GO; GO:0010452; P:histone H3-K36 methylation; IDA:UniProtKB.
DR   GO; GO:0018027; P:peptidyl-lysine dimethylation; IDA:UniProtKB.
DR   GO; GO:0018026; P:peptidyl-lysine monomethylation; IDA:UniProtKB.
DR   GO; GO:0018023; P:peptidyl-lysine trimethylation; IDA: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; IDA:UniProtKB.
DR   GO; GO:0001558; P:regulation of cell growth; TAS: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    596       Actin-histidine N-methyltransferase.
FT                                /FTId=PRO_0000408343.
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    346    346       G -> S (in Ref. 1; AAI55279).
FT                                {ECO:0000305}.
FT   CONFLICT    464    464       A -> T (in Ref. 1; AAI55279).
FT                                {ECO:0000305}.
FT   CONFLICT    595    595       G -> D (in Ref. 1; AAI55279).
FT                                {ECO:0000305}.
SQ   SEQUENCE   596 AA;  67251 MW;  9842DCF0FE31E109 CRC64;
     MGKKSRVKTQ KSGTGATAAV SPKEMMNLIS ELLQKCSSAA PSPGKEWEEY VQIRALVEKI
     RKKQKGMSVS FEGIREDFFS ELMAWAAECR ASCDGFEISN FADEGYGLKA TKDIKAEELF
     LWIPRKMLMT VESAKNSVLG PLYSQDRILQ AMGNVTLALH LLCERANPSS PWLPYIKTLP
     SEYDTPLYFE EEEVRHLLAT QAIQDVLSQY KNTARQYAYF YKVIHTHPNA SKLPLKDAFT
     FDDYRWAVSS VMTRQNQIPT ADGSRVTLAL IPLWDMCNHT NGLITTGYNL EDDRCECVAL
     KDYKEGEQIY IFYGTRSNAE FVIHNGFFFE DNAHDRVKIK LGVSKGERLY AMKAEVLARA
     GIPASSIFAL HCSEPPISAQ LLAFLRVFCM TEEELRDYLV GDHAINKIFT LGNTEFPVSW
     ENEIKLWTFL ETRAALLLKT YKTASEEDRS MLEKPDLSLH SRIAIKLRLA EKEILEHAVS
     CGRAKRLHFQ KQLDEGAPLP LYEESDIALL ENADAKLPII LRKLEEEEEE HVEEMNQLTP
     DAVCMNSSKI PVLNGQCKDL NGTQEDPPGG GAVVKEIEKH DPSAKRTEGE PKDAGK
//
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