ID A0A0M9WI82_9EURO Unreviewed; 1406 AA.
AC A0A0M9WI82;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Vacuolar import and degradation protein 21 {ECO:0000256|ARBA:ARBA00029670};
GN ORFNames=ACN38_g3189 {ECO:0000313|EMBL:KOS45862.1};
OS Penicillium nordicum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=229535 {ECO:0000313|EMBL:KOS45862.1, ECO:0000313|Proteomes:UP000037696};
RN [1] {ECO:0000313|EMBL:KOS45862.1, ECO:0000313|Proteomes:UP000037696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOMC 185683 {ECO:0000313|EMBL:KOS45862.1,
RC ECO:0000313|Proteomes:UP000037696};
RA Nguyen H.D., Seifert K.A.;
RT "Genome sequencing of Penicillium nordicum.";
RL Submitted (AUG-2015) 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:KOS45862.1}.
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DR EMBL; LHQQ01000037; KOS45862.1; -; Genomic_DNA.
DR STRING; 229535.A0A0M9WI82; -.
DR OrthoDB; 1334563at2759; -.
DR Proteomes; UP000037696; 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:UP000037696}.
FT DOMAIN 570..654
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 837..897
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT REGION 67..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1320..1406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1093
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1406 AA; 155004 MW; 77FFD868911435FD CRC64;
MLRDELLRSK NDEIANCLSR RKRKLSALYL ATVGFGATED AHYHQKEQAF LDANDLSKGR
YFNEATLPPP THARAFSPSR DTIPQTTASS ISAKPAAGIT PPLTVDGGAP HATEPQHRDT
SILDQHRTAP HNLPPTPVDT TGTRRPSVPA ISPKLPTDLN VPPIAVQSLD SSRPDQKDSV
PVVETRLTAH DHDGNQGNIS PHVSKPAATG VSSLEIPSDP LRKKHEARPS LTLGPSQHEQ
PPSPASSIDP YNNNTPVPIA ASPDTSPAEE VTEDAETIDR PKPKHERSAH ARPSLVPLTP
DEQLRLEEAQ SKPEKPFNDV IADLPTSKEV ILESVDTGAD TDRMDIDQET APAPSEPKLP
QEPETTAQDS LSPTAQAEVA ADLAIETPTV KKLSIPPTQP GSAQPERMTT RVSSGAIRHK
SVSEILGETP KSVAHDRSHP ATPSDQGSPD SVARMRFKDR KEREKERSRL STVVFPKQPA
QQEKADMDLT HRDMDAVAKL NEEQDYLFTL FLNRAYAPPR GTNLNTLLSS AHKTLSTSNH
LLEYQEQMDC RTLRRIYALQ NANRWPLRQL KRSVEPPRQG THWDVVLDHM KWMRTDFREE
RKWKIAAAKS CADWCAEYVN SDVEHRTLLR VQVKIPTSTL AEKDPSKVGL SPPSDDVGDE
VFGACHPTPE LIPSAEEESV SDGFNDEPRH DIHDTVAPAA IFSLGSDEFN FSLDMTPAAE
KLLDELPIYG PLQFASGANA PAFKVSPDTV WKTELLPVSK FASAKITFHD DDHPRKRSRY
DYSQYGSDSD NRITELTPEQ TNVALFRPEN KPIRDRIHPG HQFRPPTEHP MPSIGFFESR
SSSQWTYAED DELRRLVKEY SYNWSLISSC LTPSSLFTSG AERRTPWECF ERWVGLEGLP
ADMSKTQYFR AYHQRLETAQ RTVLAQQQAA QQQQQQQQQQ QGANAQPQPP VRRRTTQPLR
VDRRRSSKHL ALLDAMRKLA KKRETMLQKQ QHASHLASLR KANEANQPKP PISSPAEFSR
LKYDREMKLQ ERQEQYRQQM IAQQRASLAA QRSGQVPNQQ QMMNAPGRNN TMPPTSNPSL
PGGTPNGMTN GMPSGAGVNP ARPLPMQNMP NGAQPNGQMP NGMAMKMMPQ AQMQQTPGAR
PGLPMQASPD NTRVIREANR LQEQQRLLQS RQQQPHPPQQ GQQFHNPQFA SQGSPNLNMA
NVNGTPNNPA MMAALQNQGG MQSPSFHGST PQGVSTPSPR MGQPNPLSSG VVPQISTLQS
QIQRTNPNMS PEQVTKLATD RLNQYQQQQQ QRLSQQAAMN AAAGSINANA VQANYQVPHE
AGFQTPNGGS AMQVPQNQGF SPMMRVPQAG QQNRVGANSS PAMNGAAPLP SRSATPQNQR
SGSAQAGAVQ GSSKSPHAPA AQTATS
//
