ID A0A371DVQ9_9APHY Unreviewed; 1362 AA.
AC A0A371DVQ9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Vacuolar import and degradation protein 21 {ECO:0000256|ARBA:ARBA00029670};
GN ORFNames=OH76DRAFT_1369355 {ECO:0000313|EMBL:RDX56558.1};
OS Polyporus brumalis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Polyporus.
OX NCBI_TaxID=139420 {ECO:0000313|EMBL:RDX56558.1, ECO:0000313|Proteomes:UP000256964};
RN [1] {ECO:0000313|EMBL:RDX56558.1, ECO:0000313|Proteomes:UP000256964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM 1820 {ECO:0000313|EMBL:RDX56558.1,
RC ECO:0000313|Proteomes:UP000256964};
RX PubMed=30061923; DOI=10.1186/s13068-018-1198-5;
RA Miyauchi S., Rancon A., Drula E., Hage H., Chaduli D., Favel A., Grisel S.,
RA Henrissat B., Herpoel-Gimbert I., Ruiz-Duenas F.J., Chevret D., Hainaut M.,
RA Lin J., Wang M., Pangilinan J., Lipzen A., Lesage-Meessen L., Navarro D.,
RA Riley R., Grigoriev I.V., Zhou S., Raouche S., Rosso M.N.;
RT "Integrative visual omics of the white-rot fungus Polyporus brumalis
RT exposes the biotechnological potential of its oxidative enzymes for
RT delignifying raw plant biomass.";
RL Biotechnol. Biofuels 11:201-201(2018).
CC -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex which
CC is involved in transcriptional activation of selected genes principally
CC by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is
CC also involved in DNA repair. {ECO:0000256|ARBA:ARBA00025178}.
CC -!- SIMILARITY: Belongs to the EAF1 family.
CC {ECO:0000256|ARBA:ARBA00008913}.
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DR EMBL; KZ857380; RDX56558.1; -; Genomic_DNA.
DR STRING; 139420.A0A371DVQ9; -.
DR Proteomes; UP000256964; Unassembled WGS sequence.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:UniProt.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd00167; SANT; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR PANTHER; PTHR46459:SF1; E1A-BINDING PROTEIN P400; 1.
DR PANTHER; PTHR46459; E1A-BINDING PROTEIN P400-RELATED; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF13921; Myb_DNA-bind_6; 1.
DR SMART; SM00573; HSA; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Reference proteome {ECO:0000313|Proteomes:UP000256964}.
FT DOMAIN 481..560
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 918..974
FT /note="HTH myb-type"
FT /evidence="ECO:0000259|PROSITE:PS51294"
FT DOMAIN 919..970
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT REGION 116..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1331..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1033
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1362 AA; 149373 MW; 2ED16340CAFEA766 CRC64;
MSLPPETSAA SLVEARVMQL HQISKRRNEL LREMYHLIQK RDNLGSVMST DDDVEDGLQS
FLERFDLQKY PETGHIANLL EDEVALHDTP PEYSPVGGPA LELAPEVVSE AAPNVVLDSP
MSEPPASPPA QGREDDGRPR DADAPQSDVP MEVEETVPPP PAEQPEVPPV ELNSDTSSRE
SSQGPQTAPQ SPMVNDEELR PTEPSRPEKT SHTPERLPTP PYVAAVQETP ITHSPQPATR
EPSTSRLSPS REVRSPSSAS RVAQNDTSAI KAEPLDDEVI EDSGTQTQEA LSFPAQESAS
WTPAVSAPTQ VSKERSEDQI MDILGPSQPR SSPAPADVED HPAIDYSIPL PALEPSVSYA
FALGPDELMS FEESSEPPPP FGPDPPYPLP PMNLLPIEFS RRKMSKRKKD KGEVKEWQPM
PLNKWAAVLK ANPVHTKLAK ASKALSTRDW SVGMTELRLL RVFDRIERLK ESEAWSFRQP
RKQRGLGGLT KTHWDYVLDE MKWMRTDFRE ERRWKLALAF TLAHAVVEWH EAGSSEERVR
RGIVVLWKRP PPEDTEMADA SEGDQAEGLF TQDTDENGLQ SSRETGTPLD GYASDDESED
EQDKDAVDSL DPSAALQDAL KQLEEQDDGS NTQPDGVSLK PKVEEIEDLT ALKGRGGVVD
QDETAMDVDG KKPSQPEAAK SANPATSTHG APESHPGLKS SSKNPVFGTS GRDGEGAHGK
TKHKINQFAA VREHIVYSDV DKLFVDLDDL DLVKSMSELS TDDALAASAA TPSHAPHDLT
AIFPDLQLYG MLDVAPTTEI RKKSERKTDK DDPNKRAEDA TYTKIVPVSK FMFVKPALIG
TVKPAVHFKD GHWTPIEPTP VFADVEVPPA RPLDENLCSL FEGTGNKPNI PPGHPMLVPA
PPRDVRKRNA DHHNEAVAWT PAEDALLKQA VEKYAYNWNL IADMFNSSRV TISTDKRTAW
ECLERWKEKF SAQARAEATE ENGPAAASSS SHMTTRKRTA SQMLTASGSG SANSAMPHEP
RKRRRHAVMH DTLRKAAKRR EAVQKSNAAP RQKASVVHDT HGQFTKLPRY TPAELSRMKA
DKEARDAHEL FLRNKKNDEL SRQHAIREQQ QRVGSNTQPQ PPQMLPQGAT PNGVPRTANG
VPQAQIAQQM RAQPQVGISQ SQQRMAAHLA STRMSPPHIS ATQAANLRAL QAQMQAQNQA
QSGQGQGQVP QAQVTPVSNA SAALTAAAPA LSAVHLSPSF AARATSSSPG LPQQSPPLPA
ASPANANALQ RPPSVPGQPV QSVPVNPLLH MPNMANVAAA QYYMQMQNLQ HNLQGRVTPE
QIQALLAQMR QQQQQQQQQQ QQQQQQYAAA HGQAQNPNFP HQ
//
