ID A0A178BD01_9PLEO Unreviewed; 1444 AA.
AC A0A178BD01;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Vacuolar import and degradation protein 21 {ECO:0000256|ARBA:ARBA00029670};
GN ORFNames=IQ06DRAFT_262958 {ECO:0000313|EMBL:OAL06678.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL06678.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAL06678.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL06678.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-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}.
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DR EMBL; KV441705; OAL06678.1; -; Genomic_DNA.
DR STRING; 765868.A0A178BD01; -.
DR InParanoid; A0A178BD01; -.
DR OrthoDB; 1334563at2759; -.
DR Proteomes; UP000077206; 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:UP000077206}.
FT DOMAIN 638..713
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 906..966
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT REGION 76..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 996..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1184..1204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1063
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1098
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1444 AA; 159102 MW; D1940BD720A7C25C CRC64;
MSLNGLRDEL FREKTNESTA CEGRRVQHLR ALLRYTQLVA AGRGLQVEDC HYNDPPDQDE
ISFLDKNDLA KGRHFNDATL PWPTLDQPLP SSLPFESSLR PSSKSASSAV GTPSLEEQLR
TASASPSVTT QVLPSESLNP KDAGSLSQKA PSKPRVDASL SSAIDPVDHA PQALQDATSP
ATAPAVQQTG DVKDPSIDGP SVNPSVVVSS DPDQPTDPAE SNEPKAPQVV HLPPKEVQEA
RLRETERKLE KAAEKERGEE EKVAIPPTSG PMDLISSPSS TVGPYSQATP HAPHHSPDTS
PDTESFNGLS HTIPPSTDAL DPAAEQVKED HERALQKEMR EARERAREIA SPTPEVEKQI
EDEQAIRLAR DGKSRLSESS SEPRAGLVLH ASEIAREAAS AEKQAVETRA PLDQAVDSLP
TPTTTAPEPS TMDADIAEPD THKHEEPDSH PTPPADLDIE MADAPATKLQ TSPARPTRID
RSGTRLSSGT MQQKSISEII TDNAAPKAVL TPRSSNLSTS VSPPRPKTRD SKSREVTSVV
FAKKSQGGAS KALQSYNEEY AALLGASEDS SRDYLEGLFK WNAHVPPRSI PLADLVSSSR
KTISTSGTLA MIREGQDYKL LRRVYHLQNA NRWSLRQIKK SAEPERQFTH LDQLLLEMKA
MQTDFKEERK WKQALAATFA GWCAEYVHSN TDERAALRVN ARIPEVSSSA HGGDDEDMND
APTPDLVQSH AHETESESFA DEDELRTPLN ANPPTGIFSL GFNDVVMKIH RTSASDTMFR
ELPFYEPMLE GMSDGTPFSD PHMLPVSRYV TGKIVSQIRG PPKKRSRYDY DSEDELSTPP
SRSGTSAEHS MPSTPGRRLF CRNDLPPEMT DVALFNAENK HVRDRLQAAH QFRPPTEFNM
PSVAFFEHRT PSQWLWEEDQ KLRSLVKEFT FNWSLVSQQL SLPSLFVSGS GRRTPWECFE
RWVQLEGLPA EMSKTQYFRT YQGRLEQANK TVFAQYQAQQ QQQQQQQGQA PAQPRRRPTT
TPIRVERRRE NRHLAIIDGM RKLARKRESA AHKQAESQKA AALRKAHEPA APKSSVHTPQ
EFSRLKWERE EKMKLRQQQQ EMAVRQQMAA QRQAQMQAQG GMPNGANQMP RNGASMGNPN
GSTQMANSTS QQGHNSAAMA ARAHQGQQGA QANFANGNMA GMPMGTPGVP QAQMQGNMQN
GQRMGPPNQM HMAMQRGQFP NNSQQHQFQL QQQQINMASG MTQGMGMNNM PNANMMASMS
NQNMNGNMNG GMNNGMNGMP NNVGSPRPNQ VNGNMQNSAR PLSSGHMPGI LQLQNSLKVQ
HPEWSHEQVQ KAASDQLQRY MAKQQRTQAM NAAAGSSGMS SSPQIGNNHY LPPNNGMANS
PSAPNAVQNY QQQLVQQQRL MSQARQQAGS PGINTARPPS RSATPQNPQM QQSPGLQQAQ
VNRS
//
