ID A0A445GM02_GLYSO Unreviewed; 1673 AA.
AC A0A445GM02;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=D0Y65_039527 {ECO:0000313|EMBL:RZB62232.1};
OS Glycine soja (Wild soybean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3848 {ECO:0000313|EMBL:RZB62232.1, ECO:0000313|Proteomes:UP000289340};
RN [1] {ECO:0000313|EMBL:RZB62232.1, ECO:0000313|Proteomes:UP000289340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. W05 {ECO:0000313|Proteomes:UP000289340};
RC TISSUE=Hypocotyl of etiolated seedlings {ECO:0000313|EMBL:RZB62232.1};
RA Xie M., Chung C.Y.L., Li M.-W., Wong F.-L., Chan T.-F., Lam H.-M.;
RT "A high-quality reference genome of wild soybean provides a powerful tool
RT to mine soybean genomes.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acetyltransferase enzyme. Acetylates histones, giving a
CC specific tag for transcriptional activation.
CC {ECO:0000256|ARBA:ARBA00002581}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000256|ARBA:ARBA00000780};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RZB62232.1}.
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DR EMBL; QZWG01000015; RZB62231.1; -; Genomic_DNA.
DR EMBL; QZWG01000015; RZB62232.1; -; Genomic_DNA.
DR EMBL; QZWG01000015; RZB62233.1; -; Genomic_DNA.
DR SMR; A0A445GM02; -.
DR OrthoDB; 5490807at2759; -.
DR Proteomes; UP000289340; Chromosome 15.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd15614; PHD_HAC_like; 1.
DR Gene3D; 3.30.60.90; -; 2.
DR Gene3D; 1.20.1020.10; TAZ domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031162; CBP_P300_HAT.
DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR InterPro; IPR035898; TAZ_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000197; Znf_TAZ.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR13808; CBP/P300-RELATED; 1.
DR PANTHER; PTHR13808:SF1; HISTONE ACETYLTRANSFERASE; 1.
DR Pfam; PF08214; HAT_KAT11; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF02135; zf-TAZ; 2.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM01250; KAT11; 1.
DR SMART; SM00551; ZnF_TAZ; 2.
DR SMART; SM00291; ZnF_ZZ; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF57933; TAZ domain; 2.
DR PROSITE; PS51727; CBP_P300_HAT; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50134; ZF_TAZ; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 2.
PE 4: Predicted;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000289340};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RZB62232.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 606..687
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 1057..1493
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1375..1438
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1495..1548
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1555..1638
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT REGION 156..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..863
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1673 AA; 189640 MW; 963EA5D095E9CBD0 CRC64;
MPNIGVCTTM DPEFLRARSL TLEKIYNILL QRYQHPVTEA HRRKVKDLAK RLEEGMFKTA
ISKEDYMNLD TLESRLSNFL RRSSMTNHNQ QHPQLVSSSP IGTMIPTPGM SHVTNSTMII
ASSVDASMIA AGGCNSIASS SVNSVSMLPA GNMLGSSLNR SDGGNMSSVG VPRATSQMIP
TPGFSVSNNR SYTNLDPSTN SSSFSAVDST KLSQSQSQPQ RHQKLQDSGH NNHALHNLGS
QMDGGMRSDL LQNSFAYPND SINNGLGLIG NSIQLANEPG TDDYSSAYTN SPKHLQQHFD
QNQQLVVQGD RYGLLNADTF TSVSFYASAT SSGSMMNTQN MNAVKLPSIP ITSSLISGHS
NLNSMHQTSH QKSQAINSLK NLKYQSSLTS RDGHVHTQQQ YEQRPQQCHQ SERYAPQQFQ
LKLQGQQPQH LVNNDAFSQS QLSSNLDNIV KSESGVEPHK EVLDSQLSEQ FRVSKMQNQF
QQISSNDCSK VAQHFSLGQN DSSSSPPQIS QQMLHPHRLL SESQNNFSCL SAGSQSTSIL
INQWPRSLDG HHIPQGMPHE QHLPMDFHRR ISGQDVAQCN TLSSDGSIIG QAVAPRSSTE
QIDPSSNIKK SHRNQQRWLL FLFHARHCSA PEGHCLERHC STAQKLCNHI DGCTIPYCPY
PRCHHTRRLL LHFIKCNNPH CPVCVLVRKY RHAFQLKPKI WSDPESCLAN ALNGSCESYN
VVGPSPRLIS KSPLVVETSE DLPSLKRMKT EQCTQSINPE YDNSSSSVLN CDSRDSKDTQ
CQVYLSGEMS ISTKSEPTEV KEEVLVHSIH ENLSETKMDE DSAHDKMPTG KPVTHTEPAN
IARPENIKTE KQSGQDKQEN VDQPSDHGAG TKSGKPKIKG VSLTELFTPE QVREHITGLR
RWVGQSKSKA EKNQAMEHSM SENSCQLCAV EKLTFEPSPI YCTTCGVRIK RNNMYYTMGT
GDTRHYFCIP CYNEPRGDTI VVDGTPFPKS RLEKKKNDEE TEEWWVQCDK CEAWQHQICA
LFNGRRNDGG QADYTCPNCY IQEVERSERK PLPQSAVLGA KDLPRTILSD HIEQQLFRRL
KHERQERARL QGKSYDEVPG AEALVIRVVS SVDKKLEVKQ RFLEIFQEEN YPTEFPYKSK
VILLFQKIEG VEVCLFGMYV QEFGSECQFP NQRRVYLSYL DSVKYFRPEV KAVTGEALRT
FVYHEILIGY LEYCKKRGFT SCYIWACPPL KGEDYILYCH PEIQKTPKSD KLREWYLSML
RKASKENIVV DLTNLYDHFF VSSGECRAKV TAARLPYFDG DYWPGAAEDL IYQLRQEEDG
RKQNKKGTTK KTITKRALKA SGQSDLSGNA SKDLLLMHKL GETICPMKED FIMVHLQHAC
THCCILMVSG NRWVCRQCKN FQICDKCYEA ELKREEREQH PINQREKHTL YPVEITDVPA
DTKDKDEILE SEFFDTRQAF LSLCQGNHYQ YDTLRRAKHS SMMILYHLHN PTAPAFVTTC
NICRLDIETG QGWRCEVCPE YDVCNACYQK DRGADHPHKL TNHPSMADRD AQNKEARQLR
VLQLRKMLDL LVHASQCRSA HCQYPNCRKV KGLFRHGMHC KIRASGGCVL CKKMWYLLQL
HARACKESEC HVPRCRDLKE HLRRLQQQSD SRRRAAVMEM MRQRAAEVAN SSG
//
