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Database: UniProt
Entry: A0A059J768_TRIIM
LinkDB: A0A059J768_TRIIM
Original site: A0A059J768_TRIIM 
ID   A0A059J768_TRIIM        Unreviewed;      1408 AA.
AC   A0A059J768;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Vacuolar import and degradation protein 21 {ECO:0000256|ARBA:ARBA00029670};
GN   ORFNames=H109_04424 {ECO:0000313|EMBL:KDB23670.1};
OS   Trichophyton interdigitale (strain MR816).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=1215338 {ECO:0000313|EMBL:KDB23670.1, ECO:0000313|Proteomes:UP000024533};
RN   [1] {ECO:0000313|EMBL:KDB23670.1, ECO:0000313|Proteomes:UP000024533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR816 {ECO:0000313|EMBL:KDB23670.1,
RC   ECO:0000313|Proteomes:UP000024533};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C.A., White T.C., Graser Y., Martinez-Rossi N., Heitman J.,
RA   Young S.K., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., Martinez D., Murphy C., Pearson M.D.,
RA   Persinoti G., Poon T., Priest M., Roberts A.D., Saif S., Shea T.D.,
RA   Sykes S.N., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Trichophyton interdigitale MR816.";
RL   Submitted (FEB-2014) 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:KDB23670.1}.
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DR   EMBL; AOKY01000297; KDB23670.1; -; Genomic_DNA.
DR   STRING; 1215338.A0A059J768; -.
DR   HOGENOM; CLU_001331_1_0_1; -.
DR   OMA; KQQHASH; -.
DR   Proteomes; UP000024533; 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   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:UP000024533}.
FT   DOMAIN          555..630
FT                   /note="HSA"
FT                   /evidence="ECO:0000259|PROSITE:PS51204"
FT   DOMAIN          820..880
FT                   /note="Myb-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50090"
FT   REGION          67..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          615..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1151..1190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1220..1239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1359..1408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          892..919
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        67..83
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..208
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..309
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..335
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..356
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..440
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..486
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1359..1386
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1408 AA;  155190 MW;  3EAEDE6E6994AA8D CRC64;
     MLSDRPLASR HDEIARCLWS RKRKLSELYY ATATFPHPSD TSGHREPLAR QKEAAFLDAN
     DLSKGRLYDE NTLPERPRLE TVLAEYESKY GPPRPDKLDR PQTPVPQPAA GIASHEQPTQ
     GGLAAGNDQP QLTVSSAGVQ TTEPPETVQS VPSVQHQPNG IDTSHPQHAA EAPAKPASSP
     ETAVQATTQA TAHPLSPPET NRTSSFNDRL GVAPIIVPPK STEAASSPMS TGPSSSHTSA
     TERSPASSST ESVASITESP SMGKHSTDES PSNVQSQPIS TAVPSTPDEQ LQLEAAMSIR
     NSTTPKQPII AQDKDGDQHM AEAPSELKEP QLKREPTESV TNSRPSSSSG PQTAPDGKTA
     TKPVEIQRQP AEQQHSRPER MTTRVASGAI RHKSVSEILG ESPKPGATPE TEQHSRDSRR
     SSVFDRQTGT SHTSPASPSK LRLSERPDKE RSRLSTVVFP KTSSQEKEKA MQLASRRDEE
     TRKSPNEEQD YLYTLFQAKA HYPPRTMSLN TLLSTAHKTL STSNHFLEYH EQMDCRTLKR
     IYQLQHSNRW ALRQLQRSPE PPRQATHWDI MLDHVKWMRM DFREERKWKL TAAKRCAEWC
     ADYVASDEDC RRSLRIPAKI PPPPATEAPE TDKLMDGHPD EVLPNNHPTP DLIHSADDDS
     VSDGFNDEHP DFDDGNVPAA IFSSGSDEFT FRMERTIASE KILGELPFYC PVQIAPETNK
     PAFKIQPDDV WKTQLLPVSK YAQGTIQFKE DGPPRKRSRY DYEQDTYYDG EEENGYRSLS
     PEQVDVALFS PDYKALRDRI HPGNAFRPPT EYIMPPLGFY ESRQSSHWTL AEDDELRKLV
     QEYSFNWSLI ASCLAPRSSF VSTSERRTPW ECFERWISLE GLPPDMAKTP YFRTYNARLE
     AAQRTIMNAQ QQAVQQQQQQ QQNGGQVNPS AQALIRRRTA QPLRVERKRS SRHLALLAGM
     RKLSQKRETN LQKQQHATQL ASMRKVNEAT QPRPPISTPQ EFSQLKHERE LKFLEKQEQY
     RQQMIAHQRA AMAQRAAQLN PSGQFNGMPV RPPAAVPNGA GGVQVPIANG LANGIPNGAA
     VSQSRPHPGM AAMPNGLPAT GPIPVPSGMS MKMMPQQGLQ QPINGRPGLP IQTSPDNSRI
     IREANRLQEQ QRLLQSRQQQ HQFHGGQQGF APQQGPHSSP NMNATPATTS SNPALMAAFQ
     AATNGGSPSF AASSLTPGVM PASSPRMNHP STSLNNAPSL PNVNNIQASL QRLHPTMSQE
     QVSKLATERL QQYQQQRLSQ AALNAAAGNL GVGNLPSNYQ AGNSGQQIPQ QGTVNGVSSV
     PMQNQTQGYM NRLGVSQAGG QQNRPGVGIA SPAMTNMLMH QSRSATPQSQ RPSSQGGPQQ
     QQQPQQQQAQ PPPPGKSPKP AQAQTASS
//
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