ID J4G6W4_9APHY Unreviewed; 1250 AA.
AC J4G6W4;
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=Vacuolar import and degradation protein 21 {ECO:0000256|ARBA:ARBA00029670};
GN ORFNames=FIBRA_04139 {ECO:0000313|EMBL:CCM02063.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM02063.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCM02063.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM02063.1,
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 -!- 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; HE797062; CCM02063.1; -; Genomic_DNA.
DR RefSeq; XP_012181346.1; XM_012325956.1.
DR AlphaFoldDB; J4G6W4; -.
DR STRING; 599839.J4G6W4; -.
DR GeneID; 24096974; -.
DR HOGENOM; CLU_006074_0_0_1; -.
DR InParanoid; J4G6W4; -.
DR OrthoDB; 1334563at2759; -.
DR Proteomes; UP000006352; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Reference proteome {ECO:0000313|Proteomes:UP000006352}.
FT DOMAIN 330..415
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 769..824
FT /note="HTH myb-type"
FT /evidence="ECO:0000259|PROSITE:PS51294"
FT DOMAIN 769..816
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT REGION 221..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1047..1086
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 243..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..946
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1178
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1250 AA; 139914 MW; D9E4F7A8C55C0422 CRC64;
MSDSMDDYVQ DRLAQLSEIA RRRNQLLQEM YHMIQRRNHV GTILAYEGDD AEELQEFLER
FDLEKHPDTG HIDSLTDTEL LVPTSPLESH DTDNTNVSTP IDTILLSPGP VGSHQQIPLF
PDVQVLDSAA MDIDQSNMPF HTESGGYCPP QWQQAFDLSE SDLPTTGVEV RPRTYIIPAP
HHSPAQACFH FDDVIESLDD SSAAEVAKRI TEQIQYDPKY TLPPSKILPV EFNRKGKSSR
HQRKRDKEKD KSDKPGDRSD TRKEDWVSMG FHKWCATIRA NPVYKKLPKA NKCITTREWN
IGMTELRLIR TFERMELLKE SQRWSFRQPK KQRGVGISAK SHWDYLMDEM KWMRIDFREE
RIWKMALAYS LAHAVMDWHI AGTLKERVSR GICVLWKRPR PQTPEEKSGD RRFNDEVELP
DMDDDREVDS RETNTPANDY VSEDDSDDEQ EKDRPDGLDL LASGEVVEDA ITTHEELRID
RDSGKQSPSD VDHFQPKLED VEDLSALHSS NPQDDLNAMD VDAEIQGTSA AGEREEAVTK
VEESTAPLRG LKSDSKDPIL GSSIIDDRQS APLPHKSKPK SNSYAPIRSQ IMNLDDHEVF
LDLDAFDLVK GMSELSTHDY SSPAHPTPDL LSIFPNLTPL SLFDPIAPGV MSAGGSDGRR
KSDKKADKDD PHRRVDETTV NRLVPMSGFM HIRPTLLGPL QPSRHWKGDH WNDIDEMPVE
TDPDMLPPRP VDETSCSLFE NKLNSPAAHS SSLPGSSKGN KGRGNDHYWT PHEDVLLKQL
YEKYHNNWRL IADAFNSSRV TISTDRRTAQ DCLDRWLARW SSGSHPQDDV HPKISTAPSQ
MTTRGHKRSM STTALVNANN NPVPLTESKK RRRHNLLHDF IRKSIKKKEA TLKNNAAVQR
KPQPAIHDTH GQYNKMPRLT PQELSRMKAE RESRESQESI IRRRNESELA RQQQLLREAQ
RLQGAPNAQI AQQQQQQQQQ QQQQQQQQQP QPQQQQVQNG AARAINNGVS QTQMPQIRSQ
VGISQQQRLS NPMALANARL SPTQVMQAQA QAQAQAQARA LAQAQAQQAQ AQAQAQAQAQ
AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAAAS NALNAAASIN
GGHLSPPYAA RATSSSPAVP QQSPPLPVGT PIHPANSPRP PSAQAQVHQG VPGQAGGAAR
QGTNMGYYHI PGLHNAQFTQ EQMEQAMQLQ NLLRRNAANL PPNAQNGAYS
//
