ID A0A0S7DT38_9EURO Unreviewed; 1463 AA.
AC A0A0S7DT38;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Vacuolar import and degradation protein 21 {ECO:0000256|ARBA:ARBA00029670};
GN ORFNames=ALT_008200 {ECO:0000313|EMBL:GIM39717.1};
OS Aspergillus lentulus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM39717.1};
RN [1] {ECO:0000313|EMBL:GIM39717.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM39717.1};
RA Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT lentulus IFM 54703T.";
RL Genome Announc. 4:e01568-15(2016).
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:GIM39717.1}.
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DR EMBL; BCLY01000009; GIM39717.1; -; Genomic_DNA.
DR STRING; 293939.A0A0S7DT38; -.
DR VEuPathDB; FungiDB:TMP_alenIFM54703_5347; -.
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}.
SQ SEQUENCE 1463 AA; 160925 MW; 96E1D53714AC5BFF CRC64;
MLRDELLRSK NDEIARCLLS RKRKLSELYF ATVGFAGATE IAPTNALYHQ REQTFLDAND
LSKGRYFNEA TLPPFPDFAA LIPRPEEQQT SPEVIEPVVQ TQDVSVNAPK AEGAVRGIAP
SFQQREGQTA QVIERRLVED SLKKDDARIH QQPALAATSE IPQVAKSPAT SAQPDQLPQK
ASFAVPETPP TSTSHESADV SVSPALKEQP PGEVVPPRAA SNQLPSAQRK PESRPSLALA
QSLEDQPLSP ASSAGPYSNN TPAPVAVSPD TSPAEEVTEA ADEVALSPKH VGPVQLQPGL
VPSTPDEQLQ LEAAQSLQQN TLAGKSISDV TTASSLSNEV IKEDVGSPPS AAADPLKETQ
DQTSASVVPP EPKRPDGVVV TPEESQPLAQ RIQEGTQPQV GAELKAVAPM TPAGKKPTAA
AMVPAQPERM TTRVSSGAIR HKSVSEILGE TPKPSVVQPE KAHPIEKPAD MVRARPSASP
ESAAKMRLKD RKAREKERSK LSTVVFPKQQ QQQQQQQEKD DSLDIVRQYA GELARLNEEQ
DYLFTLFQNK AYAPPRGTNL STLLASAHKT LTTSNHLLEY QEQMDCRTLR RIYALQNANR
WPLRQLKRSV EPPRQGTHWD VLLDHMKWMR TDFREERKWK LAAAKSCADW CAEYVNSDPE
HRALLRVPCR IPSSNLEKKE VHASSMISPP EETTEEMLVV SQPTPDLIPS AEDESVSDGF
NDEIRHDIRD TVAPAAIFSL GSDEFTFSLD MTPAAQKLLD ELPIYTPVKV APGTNLPMFE
QPPDSAWKTE LLPVSKYASG RIKFHETEPP RKRSRYDYSQ YDSNPEHGML DLPPEQTNVA
LFRPENKPIR DRIHPGHSFR PPTEYPMPSV GFFESRQSSQ WTYAEDDELR RLVKEYSYNW
SLISSCLTPS SQFTSGAERR TPWECFERWV GLEGLPADMS KTQYFRAYHQ RIETAQRTVL
AQQQAAQQQQ QQQQQGGNNS GQAQPPIRRR TTQPVRVDRR RSSKHLALLD AMRKLAKKRE
TMLQKQQHAS HLASLRKVNE ANQPKPPISS PAEFSRLKYD RELKLQERQE QYRQQMIAQQ
RANLAAQRAG QIPNQQPMMN APPGRTPNGI PHNPGTPGIP GATPNGMPNG MPNALPNGIP
SGMGVSQGRP HMQGMPTGGP PMNGPIPPNP MAMKMMPQAG MPQGPGGRPG MPMQTSPDNT
RVMREANRLQ EQQRIVQSRQ QQPQPPQHQQ PQAQQAQQQF HNQQQFGPQG SHSPNMNLPH
VNGAPNNPAM MAALQAGSGM QSPSLHNAMP QGMSTPSPRM GQPNLLSGGV VPTISSIQTQ
IQRSNPNMPP EQVNKLATDR LHQYQQQRMS QVAMNAAAGN MASVQANYQV PHDANFQSPQ
PGMNGGPGMQ VPQSQGFSPM MRVPQPAQQN RMGVGNSPAM NGTLAQQSRS ATPQTQRSGS
AQAGPVPGSS KSPHPPQAQI PSG
//