ID A0A066Y2L3_COLSU Unreviewed; 1739 AA.
AC A0A066Y2L3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Vacuolar import and degradation protein 21 {ECO:0000256|ARBA:ARBA00029670};
GN ORFNames=CSUB01_06218 {ECO:0000313|EMBL:KDN72291.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN72291.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
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:KDN72291.1}.
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DR EMBL; JMSE01000008; KDN72291.1; -; Genomic_DNA.
DR STRING; 1173701.A0A066Y2L3; -.
DR eggNOG; ENOG502QSEY; Eukaryota.
DR HOGENOM; CLU_001331_0_0_1; -.
DR OMA; KQQHASH; -.
DR OrthoDB; 1334563at2759; -.
DR Proteomes; UP000027238; 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:UP000027238}.
FT DOMAIN 662..741
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 937..991
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT REGION 97..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1268..1333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1357..1381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1468..1739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..199
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1739 AA; 190799 MW; AB2C16B061EC9478 CRC64;
MTEVGPADRS RLLRSKRDEF SSIVTSRKRK LRQLFAVATE SDALPTNDFA NPDAPPTSAA
ELQFLQTCDI SQGRKLNEAN VPARPQLRYD VLRDSLDNSG LFAPEPVPAP PAKQDASTEL
QTKNTTAPSH QQPVAATSDT NGVAPSPRTV AGSTLPSSLP PKPPTTAAVV ATPAISARPE
VVKPSAVPVP VPSPSPAAAP TNDPLHASRE EASEATDNNV TDKPDSSPVR TPSSSISKQA
GSLPADAPPV APPQLAPQPT AVQLPSRPDA KKTDDTNPPT VKLPSDATKV ADGLSSPGST
TQTAATPAVH DVSTDTSPDN EGPQYVERVE GRSEVDAADR AEEAKDSDTM RFSDADPFNG
RIPDGPEAQL LQESMAVDSK QTLPVEPVAK QPSPPTIPAV SVVPLKDAPE LTASPTQPIS
QDAPLTTVEP KTSAATKEIA DSQESQPADR MDVDPPISTQ TEEKPSVQVQ DTDSVEPCSA
EAQTPSQARP ETPQDPERAV TRTASGAIRQ KSVAEILGET KTRTDLDVKA PPSQLTPMTS
TPQSPSRPKI FAHKKKEKEK AKNKPSAVVF GKQTKRSVDK SLVSSQQKQS FLPTDDYFTP
LFVQGFTQTS KWMKPIEVIL NQSHKTVSTP DAYVAIQDNQ ACRVLRRVYH LQQHDKWSLR
QPKRCPEPVR PESHLDVLLQ EMKWMRTDFR EEKKWKLAAA RNLAHACAEW VASTEEERKD
IQVPAYIPPK PQPLDTEADT SMVDAMLDVA DAQATPELVP SRDHDSPEHV DELREEVLET
VAPSAIFALE EDDVVFELRS SPTADQLLQE LPMYGAPLKI PAFDFTGPEF DPDAHWRRPA
LPLSKYVEGE MKLSSYGPPR KRSRYQYEEE EDDDDEKIVF GSQPTKKMKL PPQNIDVALF
NPEMKSIRDR LHAGHQFRPP AEHQMPMQSF YECRSSSQWT LPEDDELRSL VREYSYNWSL
ISSLLTPRSV FTSGAERRTP WECFERWINL EGLPTDMQKT QYFKAYQNRI DAANRVIMQQ
NQIAQQQAAG STTPATPVAR RRPSTPLRVE RRRNQKHLTL IDAMRKLAKK RETAAQKQQH
ATQMAAMRKA NEAAQPRGPT KTPRDYSLMR WERDQQLAEK VAQFHQRQET QRRIAMQARQ
GQVAAQVATT PGTGQVQPNA AAQVNGNIPR PNMPNQLAVP GQAGRGRMPM QAPTANMGGV
PAQMGGLVPP AMQMNGVPQA QMQAAMQAQH RMPMPNPQPD VNLMLQARRI SEQQRQAVQL
QQAQQQAQQV HQQPQQPQQA QQHQQSQQQQ QQQQQAQQMH QGTPTSHASQ SHSPPNMRPP
SVNGVNGANG VNGVNGVNQQ SIYANAQAMM ASINSANSAG VSTPPAGGLH MPNGTSGSPR
PLTQVPASIQ VQLNNLEAQY RAKNPNLTPE QVRQAATEYL TRLMIAQRTT MSQNAMNAAA
GGGGAASPGI ANGLAATTSP HQYAALLRQQ QQQQAAAAAA QNGQPQTGQH QQAHHQQHHS
PQQAQQQQQQ QQHHVQQQQN GHQQHVQPQH TQHQQHQVRA QPTPQHQHTS QPPQTQQLQK
QSQHQAQQVQ RPPSAQPTQA AQHLQQAQAQ QAQKVQQQQQ PQQVQQTQKP PTPHMPHTSA
QQAQKPPTPQ MAQQAQKPPT PHTPAQQAQK PPTPQMQQAQ TTPHMLKAPT PQMQKAPTPQ
LQKAQTPATP QQTQQAQQGQ QAQKQAQQHA QQQVQQVAQQ AQQQRQASGS ATPSATPTA
//
