ID J4HVY5_9APHY Unreviewed; 1216 AA.
AC J4HVY5;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Histone acetyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=FIBRA_03371 {ECO:0000313|EMBL:CCM01322.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM01322.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCM01322.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM01322.1,
RC ECO:0000313|Proteomes:UP000006352};
RX PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA Diehl S.V.;
RT "Short-read sequencing for genomic analysis of the brown rot fungus
RT Fibroporia radiculosa.";
RL Appl. Environ. Microbiol. 78:2272-2281(2012).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; HE797027; CCM01322.1; -; Genomic_DNA.
DR RefSeq; XP_012180605.1; XM_012325215.1.
DR AlphaFoldDB; J4HVY5; -.
DR STRING; 599839.J4HVY5; -.
DR GeneID; 24096233; -.
DR HOGENOM; CLU_003589_0_0_1; -.
DR InParanoid; J4HVY5; -.
DR OrthoDB; 163389at2759; -.
DR Proteomes; UP000006352; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd04369; Bromodomain; 1.
DR CDD; cd15492; PHD_BRPF_JADE_like; 1.
DR CDD; cd05839; PWWP_BRPF; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13793:SF164; BROMODOMAIN-CONTAINING PROTEIN, 140KD, ISOFORM A; 1.
DR PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF10513; EPL1; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF00855; PWWP; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006352};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 147..197
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 201..259
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 431..501
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1095..1164
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT REGION 269..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1075
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1216 AA; 136222 MW; A9FD79159C7860A7 CRC64;
MARGPASPPP TPLPKVSFMK VQDEFSSYPM GVHDAQAKTY GYNELTDFKR PEHYIRYIGM
VDFMLLLQAV ALRTSEPLES DLATQVEYDM DEQDHEWLNT VNVERKKLQQ DGVSYEVFEI
VMDRLEKEWF DLTKNIPKPD LALPSEDSTC AICDDSEGEN TNAIVFCDGC NLAVHQDCYG
VPYIPEGQWL CRKCTVSPEN PVSCILCPNE GGAFKQTVHG DWVHLLCAIW VPETRVANDV
FMEPITGIDK ISKQRWRLKE QQDTRAAALV AESNDQPEDD STSPKSSKTA RAYAKTYKPG
PPLVPHIIVE RILQYIGKVN IRHKREFVIL VCKYWSLKRE ARRGAAFLKR LHLEPWTASS
TTRQQTDEEK AIKLEFMRRL RRDLESIRMV TEMCRKREAL KLERAESRQF VFDKTLLTHE
PPLRMAFEKI IGADRQEYFK NPVSKLDVPD YYDIVKQPMC WSIIDRKLDR HEYLDLHEFK
DDVNLVINNA IIYNKPGTPY YKTAQKIQSS AEPIMAELDR LVNHRFPVQG SSDQEQPQYS
TGGLEPPLHL LQLLLSEDSV KEDLALILDK SPLEALFSYE LPRIRPPPPP KPKRNRKADL
ERKRQQRLES AAEFRTRTRR GAATFAQFEA EIQETTETPA LTPVPEAGPS NELEVSQVAR
PGKPGRKKRM SGPGFAHANL PPMVETVDNQ QSFKLFERGW VLPPDQRRGN RPRPSFPTAP
PKKKLKIGER GKYHMFSFTS PGDEHETSQA QLPSESNVGP EEDMMELDEV PIASAKDQPA
ENYTATIAEQ SVEHPISHAA GPATDPSIAT AEQVTDHHPS PTTEQSSEQR IGVAARQLIA
HPDALVVQKL IDQPTSRPEI QQSARLPAAV ELPTAILAGH VVAEQTTLLS AASGTTNPFE
PPAVLSTTSF EDVTPLADRL TEHPVAPVVN QSIQEKRELS AGPTAGPSSM QSASSAMEPA
AVAMEVDRPI RKPKPVRIAR IVIEELDTPA IRREKNLRRK AEKARLAALA AAAATASRGS
SSIGPDATME TGKDYEMSSD LSSLSDLSDD GEGTMDGQVS SRTPDASSQH PRIPMTSATA
EPGAVVLEPG RTLEGGTLVW AKAATFPWWP AVVFEPDDHT IPPNMLPVHH RGDTRGPIHL
VRFYDSKRSW QWVTLNKMKM LGEDDDLDAE LLANSSKLQK WKTPKLRKQC RDAFREALAE
MEDAGVDEEH DPISES
//
