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Database: UniProt
Entry: A0A409YYK7_9AGAR
LinkDB: A0A409YYK7_9AGAR
Original site: A0A409YYK7_9AGAR 
ID   A0A409YYK7_9AGAR        Unreviewed;      1291 AA.
AC   A0A409YYK7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Vacuolar import and degradation protein 21 {ECO:0000256|ARBA:ARBA00029670};
GN   ORFNames=CVT24_010573 {ECO:0000313|EMBL:PPR08112.1};
OS   Panaeolus cyanescens.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Galeropsidaceae; Panaeolus.
OX   NCBI_TaxID=181874 {ECO:0000313|EMBL:PPR08112.1, ECO:0000313|Proteomes:UP000284842};
RN   [1] {ECO:0000313|EMBL:PPR08112.1, ECO:0000313|Proteomes:UP000284842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2629 {ECO:0000313|EMBL:PPR08112.1,
RC   ECO:0000313|Proteomes:UP000284842};
RX   PubMed=30283667; DOI=10.1002/evl3.42;
RA   Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA   Matheny P.B., Slot J.C.;
RT   "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT   diversity.";
RL   Evol. Lett. 2:88-101(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}.
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:PPR08112.1}.
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DR   EMBL; NHTK01000155; PPR08112.1; -; Genomic_DNA.
DR   STRING; 181874.A0A409YYK7; -.
DR   InParanoid; A0A409YYK7; -.
DR   OrthoDB; 1334563at2759; -.
DR   Proteomes; UP000284842; 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:UP000284842}.
FT   DOMAIN          489..561
FT                   /note="HSA"
FT                   /evidence="ECO:0000259|PROSITE:PS51204"
FT   DOMAIN          897..948
FT                   /note="Myb-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50090"
FT   REGION          58..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          558..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          635..714
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          768..798
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          947..1059
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1087..1152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1256..1291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..91
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..132
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..154
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..179
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..230
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..253
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..333
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        596..611
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        649..713
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        779..798
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        967..1003
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1007..1035
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1036..1055
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1121..1150
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1291 AA;  141781 MW;  679473AC0D28F9AE CRC64;
     MKISLCFSLW KNMTCKKSMS TIFILESDIK LGQSPLNASI SNLEEQEFLS ALHKTSLYQP
     EPKPLSSASS DHADTKPPST SRATRSRSRA VELAQVSPPP MDSTEGPSTV EKLVQDVSVG
     SVPTSPSPKM KSKSPEPRTD TSSKDEDDLD DLDLVHPSSP MSQNGGQPSV KGSSRTPPLR
     RSPSAPPAIS EQEISPEVPA VTETNNVGLE ETPVKKGEEE EEEEEAKEDM DVDLIAQSDM
     SDHAEKPVED DSAMEVDNDS AETAPSVEPA ADTGNNGIIV VSSDTDKALD AVEEQAQTHI
     ATINPSVLSV SEPTPPPPPP PPPPPPPPTQ VPYVPVKITY PPSIHKAIQI PHTTPVEQPH
     FTFESVVESK PVPSTQDGTS TKSISFDYPL PPLSLLPPEF TRKAKYAKRR RNPDKDVKRE
     KDRDELPLGI HRWNASILAN PLWKRVARST KCLSTKEWSI AMTELKLMRT LERVERLKDE
     GRWSFRQPKK QRGVGGLTKT HWDYLMDEMK WMRIDFREER RWKLVVAYNL AHAAVDWHSL
     ETLEERLEAG ICVKWRPIVP REPSPPEAEE VPSQVQRPVP PQPLQQQTSF LGVDYGSDAD
     DDEDMETDEQ QVIDSLEPNN PVADALEETE GLKLKSEDVD DPSSLDLHNL PNAPDSPMNT
     LPTSDGDVLG SSTSIDGLKT SSSNPMLGDA STKSSSQSAN EDGESQSAFP KISKQQLAPV
     REKIVYGGVS QVFLTMDDIA DVVNEELEST DLTNLNVLFP ELTPLTLLDV APPAPPPVDG
     RKKGERRSDR DDPNRRIEDT TYTKLYPIGR FMYEKPTLLG PLQPAKRWKD DHWLPAPEIL
     WTQDNDVWTR TGTEEVGVSN DLFEGRPSNT TSFGFPIQTS SFKDKDNRKR GACDIVWSAN
     DDALLKSLVD RYSNNWALVA ECYNASRLTT PSDKRSPTEC AERWKERWGQ ERKIPLPDAA
     APSQTLADDT GAGSAMTSGS QMTTRGVKRM ASSSVSSSAP PVIASGSEPK KRRRHLVLQE
     GIRRLARRRQ ESAAKLATQR KSTGIHETHN QYNKLPKLSP AELGRMKAER DNQANQELAL
     ARRRNEEFQR LRDQASRGQA SQPPQPPAKP STQPAPQAAQ VQPAQPAPPT PSIPQTTPPV
     PTPHQATPPQ VAPVPHAQLA QLQQLQNRAN AAAGAAALGN RPTRLAATPN NRNIPQQMLL
     QQARLQLGPQ GLGQIGLLQQ AQGAAGGVNG SFYGLPSNLT QEQILMIALT AQQQQVAQQQ
     QQQQQQQQQQ SQGSSGNAGN NGSTNGFIPQ T
//
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