ID Q2H705_CHAGB Unreviewed; 1456 AA.
AC Q2H705;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Vacuolar import and degradation protein 21 {ECO:0000256|ARBA:ARBA00029670};
GN ORFNames=CHGG_05560 {ECO:0000313|EMBL:EAQ88941.1};
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ88941.1, ECO:0000313|Proteomes:UP000001056};
RN [1] {ECO:0000313|Proteomes:UP000001056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC {ECO:0000313|Proteomes:UP000001056};
RX PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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; CH408031; EAQ88941.1; -; Genomic_DNA.
DR RefSeq; XP_001221655.1; XM_001221654.1.
DR STRING; 306901.Q2H705; -.
DR GeneID; 4390005; -.
DR VEuPathDB; FungiDB:CHGG_05560; -.
DR eggNOG; ENOG502RGMX; Eukaryota.
DR HOGENOM; CLU_001331_0_0_1; -.
DR InParanoid; Q2H705; -.
DR OrthoDB; 1334563at2759; -.
DR Proteomes; UP000001056; 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; 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:UP000001056}.
FT DOMAIN 645..724
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 906..966
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT REGION 135..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1429..1456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1456 AA; 159183 MW; EADE21278C9BEB86 CRC64;
METSSRRSDI RTRHRGIAST RRAFLRSLFS SSFLTPDIPR RGAKHQPRSI AFSRKRKLRE
LFAVATDDGI PNHDPNDPDA PTTTPAEQKF LNEFDILQGR RFDKLTIPAR RKVFDAHRLR
AIYDSTTIAE ATPFAAPAKI ENQPPEPCYT NGTKLDKPTN QPRGSIQHAS PQATGKALPV
GQGSPSTAQS SVVAPKTHKD SSRDQAKEAP THPASCRQVE GVTGSRPSTD SASTATAQHP
SLQVPATALS RVDVQISRTN QKPVQSEVDE RRDFKDGEPA VSDQQPLTSN PSSHLDILSS
PGSTAQSMLT PAVHDASADT SPDSEATHNL ERVEEKAAVE LQGDLMPEEE AAIAMPPPSG
LENITPIATS PTRKGPLGAR DKIVDEHQVG STAARVGSLQ HGEWLSDTLA GPSMIPGNAS
VEDRNGGDGG ISALMDIDKP EDAATENEGV ANAGLSQESH ATATAVPAPP QPAGVLAAET
TSTVEVAVNP RSSSLSLAPI EPTRPVSADR DGSRSMRDEE IDPEAPPTQL KLYASRTRDR
RRRSTPTVIF GKQPKKPRPS DDGTVAVGQQ QPGHLPSDDY FTPLFIEGFT RQSTWMKPIE
KLINQAHKTI STTDQYISML DHQACKILRR VYHLQQHDKW SLRQPVRCSE PTRPASHWDV
LLQEMKWMRT DFREENKWKR TVARNLAHAC AEWVHSDPAE RLMLQVNAVI PPRPAEVEMK
GANLGDEALP DLVHTDSPIE NEDDLPEILV DCVAPSAIFA LPDDEVVFGL QPSKTADLLL
ENLPLHGSPL TVPKFDVSDT DYDPDAKWKR PAVPLSKYVE GGMVLASNGP PRKRRRYDYL
AEDDPDNNDD EVIFGYEPAN NNRELQAENS MVALFNPEMK GIRDRLHAGH QFRPPNEHAM
PPQSFFESRT ASQWTWAEDE QLKSLVRECS YNWSLISAMS STVSAFASGA ERRTPWECFE
RWVNLVSLDG LPNDMARTPY FKAYQARIDA AQRAIAQHNQ NAQQQVGPNG AVTPIPRRRP
TTSIRVERRR NQKHLALIDA MRKLAKKREA TAQKAQQAAN LAAMRKANEV PRQQIQNKTP
RDYSIMRWER DQALAERMAA YAIRQADANA RRLKQNHPGQ GPGTPGVAQG AQTAAQLAAV
ASANGAARLN VPGQLAAAAA AQNRTPGRVT SSGWPSSNCN TQQQVQQTQQ GQAQQSQSQQ
SQTQPQQQQP QPQPQPQPSP QQQQQQQQQQ QQHPLHLQHQ PQQQQAAQHA QQQVAQQQQS
QTNQTQQLPQ TNGAQGSPTP LRNVVNGVNQ GAFLTNAQAM MASFGAANGA GLVTSPGAGL
SLPAMAGRSP GGILNQHITQ RLAELEAHYR AKNPNLPPET VRQLATEHLG RMIVQSQQQA
AMNAAAGAVA QQSMNSPHQY ASLLRAQQQA QAQQAQAQQA QVQQAAQQAA QQAAQQQQVG
QHQRQSSGSA TPAPGK
//
