SETD3_CHICK
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 03-AUG-2022, entry version 91.
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=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; Phasianidae;
OC 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., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA 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., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., 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., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., 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., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
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; 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 AlphaFoldDB; Q5ZML9; -.
DR SMR; Q5ZML9; -.
DR STRING; 9031.ENSGALP00000042532; -.
DR PaxDb; Q5ZML9; -.
DR GeneID; 423445; -.
DR KEGG; gga:423445; -.
DR CTD; 84193; -.
DR VEuPathDB; HostDB:geneid_423445; -.
DR eggNOG; KOG1337; Eukaryota.
DR HOGENOM; CLU_028272_0_0_1; -.
DR InParanoid; Q5ZML9; -.
DR OrthoDB; 489371at2759; -.
DR PhylomeDB; Q5ZML9; -.
DR PRO; PR:Q5ZML9; -.
DR Proteomes; UP000000539; Unplaced.
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..593
FT /note="Actin-histidine N-methyltransferase"
FT /id="PRO_0000254177"
FT DOMAIN 94..314
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..593
FT /note="Basic and acidic 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 244
FT /note="Y -> YS (in Ref. 2; AADN02003715/AADN02003714)"
FT /evidence="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
