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Database: UniProt
Entry: Q5ZML9
LinkDB: Q5ZML9
Original site: Q5ZML9 
ID   SETD3_CHICK             Reviewed;         593 AA.
AC   Q5ZML9; E1C6M7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   10-APR-2019, entry version 81.
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=RCJMB04_1k10 {ECO:0000303|PubMed:15642098};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC   Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J.,
RA   Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M.,
RA   Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red jungle fowl;
RX   PubMed=15592404; DOI=10.1038/nature03154;
RA   Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C.,
RA   Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E.,
RA   Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W.,
RA   Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A., Kremitzki C.,
RA   Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E.,
RA   Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J.,
RA   Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M.,
RA   Paton B., Smith J., Morrice D., Daniels L., Tempest H.G.,
RA   Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V.,
RA   Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J.,
RA   van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J.,
RA   Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H.,
RA   Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA   Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA   Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA   Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S.,
RA   Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J.,
RA   Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H.,
RA   Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C.,
RA   Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C.,
RA   Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P.,
RA   King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S.,
RA   Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S.,
RA   Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S.,
RA   Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z.,
RA   Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J.,
RA   Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z.,
RA   Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA   Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA   Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J.,
RA   Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G.,
RA   Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D.,
RA   Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G.,
RA   Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A.,
RA   Mardis E.R., Wilson R.K.;
RT   "Sequence and comparative analysis of the chicken genome provide
RT   unique perspectives on vertebrate evolution.";
RL   Nature 432:695-716(2004).
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; AJ719365; CAG31024.1; -; mRNA.
DR   EMBL; AADN02003714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AADN02003715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001006486.1; NM_001006486.1.
DR   RefSeq; XP_015142949.1; XM_015287463.1.
DR   RefSeq; XP_015142950.1; XM_015287464.1.
DR   RefSeq; XP_015142951.1; XM_015287465.1.
DR   RefSeq; XP_015142952.1; XM_015287466.1.
DR   UniGene; Gga.22516; -.
DR   ProteinModelPortal; Q5ZML9; -.
DR   SMR; Q5ZML9; -.
DR   STRING; 9031.ENSGALP00000042532; -.
DR   PaxDb; Q5ZML9; -.
DR   PRIDE; Q5ZML9; -.
DR   GeneID; 423445; -.
DR   KEGG; gga:423445; -.
DR   CTD; 84193; -.
DR   eggNOG; KOG1337; Eukaryota.
DR   eggNOG; ENOG410Y7DR; LUCA.
DR   HOGENOM; HOG000049107; -.
DR   HOVERGEN; HBG062823; -.
DR   InParanoid; Q5ZML9; -.
DR   KO; K19199; -.
DR   OrthoDB; 489371at2759; -.
DR   PhylomeDB; Q5ZML9; -.
DR   PRO; PR:Q5ZML9; -.
DR   Proteomes; UP000000539; Unplaced.
DR   Bgee; ENSGALG00000011134; Expressed in 11 organ(s), highest expression level in skeletal muscle tissue.
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    593       Actin-histidine N-methyltransferase.
FT                                /FTId=PRO_0000254177.
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    244    244       Y -> YS (in Ref. 2; AADN02003715/
FT                                AADN02003714). {ECO:0000305}.
SQ   SEQUENCE   593 AA;  67196 MW;  E1B185E0717431E1 CRC64;
     MGKKSRVKTQ KSGTGATAAV SPKELLNLTS ELLQKCSSPT PGPGKEWEEY IQIRSLVEKI
     RKKQKGLSVV FDGKRDDYFP ELIKWATENG ASTEGFEIAN FEEEGFGLKA TREIKAEELF
     LWVPRKLLMT VESAKNSVLG SLYSQDRILQ AMGNITLAFH LLCERANPNS FWLPYIQTLP
     SEYDTPLYFE EDEVQYLRST QAIHDVFSQY KNTARQYAYF YKVIQTHPNA SKLPLKDSFT
     YDDYRWAVSS VMTRQNQIPT EDGSRVTLAL IPLWDMCNHT NGLITTGYNL EDDRCECVAL
     QDFKAGEQIY IFYGTRSNAE FVIHSGFFFD NNSHDRVKIK LGVSKSDRLY AMKAEVLARA
     GIPTSSVFAL HSIEPPISAQ LLAFLRVFCM NEEELKEHLI GEHAIDKIFT LGNSEFPISW
     DNEVKLWTFL EARASLLLKT YKTTVEDDKS FLETHDLTSH ATMAIKLRLG EKEILEKAVK
     SAAASREYYT KQMADGAPLP KYEESNIALL ENTVADSRLP IVLRNLDDVE EQGDLKIDEA
     MDAEVTENGF VNGENSLFNG TKSESENLIK EESNRETEDA KESSSESTDE VKE
//
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