ID A0A1Q5T5X9_9EURO Unreviewed; 1414 AA.
AC A0A1Q5T5X9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Vacuolar import and degradation protein 21 {ECO:0000256|ARBA:ARBA00029670};
GN ORFNames=PENSUB_11142 {ECO:0000313|EMBL:OKO95630.1};
OS Penicillium subrubescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKO95630.1, ECO:0000313|Proteomes:UP000186955};
RN [1] {ECO:0000313|EMBL:OKO95630.1, ECO:0000313|Proteomes:UP000186955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 132785 {ECO:0000313|EMBL:OKO95630.1,
RC ECO:0000313|Proteomes:UP000186955};
RA De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA Grigoriev I., Riley R., Granchi Z.;
RT "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL Submitted (OCT-2016) 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:OKO95630.1}.
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DR EMBL; MNBE01000702; OKO95630.1; -; Genomic_DNA.
DR STRING; 1316194.A0A1Q5T5X9; -.
DR OrthoDB; 1334563at2759; -.
DR Proteomes; UP000186955; 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 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:UP000186955}.
FT DOMAIN 567..642
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 835..895
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT REGION 93..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1228..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1322..1414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1414 AA; 155083 MW; 10777502BB06BF7B CRC64;
MLRDELLRSK NDEIANCLLS RKRKLTELYY ATVGFEGATA DSLYQQKEQA FLDANDLTKG
RYFDEATLPL PTHVRARSPT RKPVTPAITA EVKSQQAAGI TPPPTIDGRA ALPPPGTSPQ
GGSNLAATPG VASIPQVAPE SNQPAAPVLP IAEGLEVSTA TAPSTQPVAD QKANISVPAT
RLGPQDHNAA ELTVSSGAAQ LAAATGTAPS SLEIPPTNLP RKKSDARPSL TLGPSHPEQP
LSPASSIDPY STNTPIPVAA SPDTSPGEEV AEVRKLGRQS PKDSRSMQPR PGLIPSTPDE
QLRMEEAQSL RRASTNGLPL TDKAVQETAK APADQDQMDV DQEPLVAIQE PKLSTRTVAT
GTERLSPTEQ LTTDGGQPVG ETPTETKKPV SLPPTQPEIP QLRMTTRVSS GAIRHKSVSE
ILGETPRHVA HDKSHATVEP QTPESLARMR FKDRKDREKE RTRVSTVVFP KQPSSLQDKA
ESMDLVSWDS GDAVAKLNEE QDYLFTLFLN RAYAPPRGTN LNTLLASAHK TLSTSNHLLE
YQEQMDCRTL RRIYALQNAN RWPLRQMKRS AEPPRSFSHL DVMLDHMKWM RTDFREERKW
KLAAAKSCAD WCAEYVNSDD EHRSLLRLNA KIPSPRSVGC DASKLGVASP SEETGDETFA
ASHPTPDLVP SAEEESVSDG FNEEPRHDLH DTVAPAAIFS LGSDEFNFSI DMTPSAEKLL
DELPFYEPVR FVRETQKPSF RDLPDSAWKQ DLLPVSKFAS TKITFHQDDE RPRKHTRYDY
SQYGSASEHR IADLPPEQTN VALFRPENKP IRDRIHPGHS FRPPTEHPMP SVGFFESRQS
SQWTVSEDDE LRRLVKEYSY NWSLISSCLT SPSIFTSGAE RRTPWECFER WVGLEGLPAD
MSKTQYFRAY HQRLETAQRT VLAQQQAAQQ QQQQAANNGQ PQQPIRRRTT QPLRVDRRRS
SRHLALLDAM RKLAKKRETI LQKQQHASHL ASLRKANEVN QPKPPISSPA EFSRLKHERE
MKLQERQEQY RQQMIAQQRA SMVAQRGGQL PNQQQPPQQM MNAPGRPNNL PPNAPNAAMV
NGAPNGIPAG MAPNVAVNQA RAQAMQGMPA GAAPVNGQIP ANPMAMKMMP QGQMPNVGAR
PGMPMQASPD NARVIREANR LQEQQRLLQS RQQQVPQPTG QPQQAQQQFH NQQFVPQGSH
SPNLNVPSVN GAPSNPAMIA ALQAQGGIQS PSFHNGTPQG VSTPSPRMAQ PNPLSGGVVP
TISTFQSQIQ RANPNLPADQ VNKLATERLN QYQQQRMSQQ AAMNAAAGGM NNVQANYQVP
HDGNFQAPQQ PGMPNGGSAM QVPQNQGFSP MMRVPQNNPQ NRVNVTSSPA VNGAVPQASR
SATPQTQRSG SAQAGAVQGS SKSPHPPPAQ TASS
//