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Database: UniProt
Entry: A0A317SH22_9PEZI
LinkDB: A0A317SH22_9PEZI
Original site: A0A317SH22_9PEZI 
ID   A0A317SH22_9PEZI        Unreviewed;      1699 AA.
AC   A0A317SH22;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Vacuolar import and degradation protein 21 {ECO:0000256|ARBA:ARBA00029670};
GN   ORFNames=C7212DRAFT_365973 {ECO:0000313|EMBL:PWW73713.1};
OS   Tuber magnatum (white Piedmont truffle).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Tuber.
OX   NCBI_TaxID=42249 {ECO:0000313|EMBL:PWW73713.1, ECO:0000313|Proteomes:UP000246991};
RN   [1] {ECO:0000313|EMBL:PWW73713.1, ECO:0000313|Proteomes:UP000246991}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=091103-1 {ECO:0000313|EMBL:PWW73713.1};
RA   Murat C., Payen T., Noel B., Kuo A., Martin F.M.;
RT   "Genomes of Pezizomycetes fungi and the evolution of truffles.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:PWW73713.1}.
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DR   EMBL; PYWC01000075; PWW73713.1; -; Genomic_DNA.
DR   STRING; 42249.A0A317SH22; -.
DR   Proteomes; UP000246991; 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; 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; 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:UP000246991}.
FT   DOMAIN          919..1001
FT                   /note="HSA"
FT                   /evidence="ECO:0000259|PROSITE:PS51204"
FT   DOMAIN          1214..1266
FT                   /note="Myb-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50090"
FT   REGION          133..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          275..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          486..605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          686..707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          719..776
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1115..1154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1617..1699
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..171
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..290
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..412
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..548
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        573..590
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1617..1637
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1666..1682
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1683..1699
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1699 AA;  185901 MW;  6A6891C38CB474DB CRC64;
     MVEKISIQNL RNNALSTRLE ERKNIVISRK RKLQEVYAVC RHIDRTKPFP NADIVETWGT
     IERYGGANME DGEKRFLDEN DIERGRLFQE STLPPHSSYL PEPGGFQKTF AAQLTPHHGV
     KAISRHATPL SASVPEKPVQ ALEHPAVSRE PELLTEKEAR HAFDVRNRME DQSPTKSGVT
     NGKRSSEAPT EDGSVDSEAT EEDLGSLSHI TEPNERVKLG NAAPVVGIGG VPVVQEAATR
     VPDDHERSLG VRPPPIPSEL VDAARGKATQ IAAVRDGKTR ERDTRVEKAK STEPVTVTSF
     GDSVREVPDS FESSQVSSLS EPPSPATSKG TILELGEEPR LPVASPEIQH IPPQPPLVII
     TNKENRPAPI PPSKSPSRHA SHSDVCSPTS SVDGDNRSTP GNILSSATSP DANHMLGPDP
     RSEERNGQIK EVVAESGPYG VRTMPAKEAE EEELAGTFVE GKVVPCGVQS ERSLPSVIVA
     AEFVMDEEGT QSQLPTTPPP ELTNGGEPDL AAVEAGVAIT LPKADEAQSA RTNKSTSPDP
     SAQLRLENSL AQDDIEPDSL ANEGPHSSQK LTGVGETHDE DLEDRVQLVG SGEPEPRAAG
     PAREVAEVVR EVKHASENME IDIPDKVGDM EAAGHDTAMS GVDQSAVHGA TSGMHVGDIS
     IGTISLPEQQ SLEVSTLQEI DDSKMEVDHT ANEQHDETGL PGKAPTPDVN TLVDATVEPP
     GSPANSMFEP DNEEEVPSSG GMVVGGAESE GSLIPSTSPV KQPLRRRETR KKQAKLSKVV
     ISSTHHALAA LEEEAKRLHE DQIAQGPIVV ARRRDQQAAS AAARRSAVFQ PGSKIDAITR
     YGITEPPSEE KSKVKNADMF DIAYTAKASG TLISDLLQRS SKTLTTGDHQ VHYFEAQAVR
     IENRILELQD QGLWSLRQIP RVVEPRRRKC HWDYLLEEAK WLRDDFKGER KWKITMARYY
     AKEAARWHHA GEGRWQLQID RKQLGVVPKG IREERRRVAH IEMQDSDMNQ PTPDLVEGCG
     SPESDDDFPM DDRHHDTNQG NFAHIYEPPA TLFTLSPEET VFAMPASKAS DDILNQLPLY
     GPPEPPTGRH DEVEEEWMKL PVVAISKYAS GKLVIQEEQG PPSKKSRYEY EENQDTYADD
     SDEDERLGGG RLIGRSKRDK LRKPSFLPPE QTNVALFKPE YKPLLQRVHN THVPRLPSDF
     PPPSFFENRH PSLWLASEDE MLKTLVREYH YNWGLVSQCL TLPGDWHSGS ERRSPWECFE
     RWIALEPIPP EFAKSPHFKP IQQRLDVAAR VNGLYGNVPG SAGGSSSGGV KPRRGTAPIR
     VEKRRNTRNF MLIESMRKLA KKRETSVNKQ QTNKNQVVAA MKRASESQAS TANPLRTPQY
     FSAMKFEREQ KHLEQKNIYS QMQMQQARNG IPPPQARIPH PGQHHALANG VPIPVQQRVG
     APAPQGPNGV LQVPRAAPMQ NGTNGLPMRS LPAPLSQGQQ TQRCAPEYFA HLRRITQQHV
     IAAPQGYPSS GALGTQGSQP SAQGMQTILQ QAQQAALGQN QQVSVNQQAP QQKCIVPPPI
     DSQASVSSPP IPPTPTQLKL ARVLIQEMAA LVQYQNPNRE ATQQTLASYH AQLSQNIQAQ
     ARSPVRPSPT RTAADNTGPM IGVNGPVNPA AGPPAVGAIS AGSPRLGNGQ IPTQLPQSQQ
     PQANQPLPQP QPAPQQQPI
//
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