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Database: UniProt
Entry: B0D3R4_LACBS
LinkDB: B0D3R4_LACBS
Original site: B0D3R4_LACBS 
ID   B0D3R4_LACBS            Unreviewed;      1313 AA.
AC   B0D3R4;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=Vacuolar import and degradation protein 21 {ECO:0000256|ARBA:ARBA00029670};
GN   ORFNames=LACBIDRAFT_316023 {ECO:0000313|EMBL:EDR10974.1};
OS   Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS   (Laccaria laccata var. bicolor).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX   NCBI_TaxID=486041 {ECO:0000313|Proteomes:UP000001194};
RN   [1] {ECO:0000313|EMBL:EDR10974.1, ECO:0000313|Proteomes:UP000001194}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 / ATCC MYA-4686 {ECO:0000313|Proteomes:UP000001194};
RX   PubMed=18322534; DOI=10.1038/nature06556;
RA   Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA   Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA   Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA   Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA   DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA   Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA   Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA   Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA   Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA   Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA   Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA   Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA   Tuskan G., Grigoriev I.V.;
RT   "The genome of Laccaria bicolor provides insights into mycorrhizal
RT   symbiosis.";
RL   Nature 452:88-92(2008).
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; DS547096; EDR10974.1; -; Genomic_DNA.
DR   RefSeq; XP_001878275.1; XM_001878240.1.
DR   STRING; 486041.B0D3R4; -.
DR   GeneID; 6073658; -.
DR   KEGG; lbc:LACBIDRAFT_316023; -.
DR   HOGENOM; CLU_006074_0_0_1; -.
DR   InParanoid; B0D3R4; -.
DR   OrthoDB; 1334563at2759; -.
DR   Proteomes; UP000001194; 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; IPR017930; Myb_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; PS51294; HTH_MYB; 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:UP000001194}.
FT   DOMAIN          495..593
FT                   /note="HSA"
FT                   /evidence="ECO:0000259|PROSITE:PS51204"
FT   DOMAIN          893..948
FT                   /note="HTH myb-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51294"
FT   DOMAIN          893..944
FT                   /note="Myb-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50090"
FT   REGION          135..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          408..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          576..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          656..712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          980..1002
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1028..1050
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1084..1121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1148..1172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1207..1261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1290..1313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..156
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..171
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        656..709
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        980..995
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1100..1121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1207..1222
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1235..1261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1313 AA;  145399 MW;  E0048D9C857D6C7A CRC64;
     MTESSRAVLI KERVAQLHAI SARRNELLRQ MYHLIQQRNN VGALLPTEAQ EEDEPGLHKF
     LQRFDLTRNG NASIANLTED EWSPIPLVVD QDSKAAIFIL PDLTSLTPQC ETTYDQFQTF
     SPNLASYSVP PLGASPESKL PLSLESTLQV SSSKPQLAEE SEEDHDKSSI PILDESLGAP
     TSVSPSSTSP AEIDAHKEKL PPVSPVTFKS TKEEAADIQD VTMEEDGVPV QLPSATSITQ
     LSTTIQEPVE SMDVDEDHRD FHAAMNPEGN REDIREDEIT VVSGVRHSQA LELDATSEEV
     LINSLSDSNY SEGNEDPELL STAVTHSLST LRPISLAPVL TRPPQRPIII ATPSAPPIND
     QLFQLDMATL PELSMGQTSP PHPHYQSSTR YTLPPINVLP PEFVRKAKTL KQRKRDKERE
     KTEGKKEKED LLPLGLNRWA ATLSANPVWK KVSRASKCLN SRDWAVAMTE LRLIRTLDRV
     EFLKDGGRWS FRQPKKQRGV GGLAKTHWDY LMDEMKWMRI DFREERKWKM ALAYALSTAV
     LEWHAMDSWE ERILCGVCVK WKSSYSSTEA FEDDGEAMDI DDTQPQKKSL VSVNYGSDDD
     DDDEQDKDAQ SVVDPLEPAA MIEDALDTAS HLIDGVGENT VQPKMEDFDD LSALQNESET
     TNESIQGMPT PSQSNVSTDV ATGLKSTSHN PVLGSKSSSQ SSSGDSDPVG SSVKAIKPIK
     YGLLRENIAY ADDEKLFLNS NDVTQSSNEM PNYESAHSLD LDALFPDLQP LCLLDVTPAT
     VGIEGKKKLG KNSDRDDPNK RIEETTYTKL YPTDKFMFAK PTLIGPLLPS KRWKDSTWLP
     MEEMPVVPDS DGPMKIPDDS GNDLFDVRSS NGPAILAFQV AKDKGKRGVD HIWSASDDTL
     LRSLSDKYPN NWALIAECFN GSRLTTPTDR RSASDCLERW KEKWGPEMRQ RPLEIVQAPL
     EETVVPSTPS QMTTRGVKRL ASSSVSSQNA PIINSGSEPK KRRRHLLLQD SMRKAAKKRV
     ELAQKMVAGQ RKTPAIHETH GQYSKMPKLT PAELSRMKAE KDARDVQDLA LARRRQEELA
     RQNLLREQSQ RIGVPPVPAT QAPLSQQQPQ PQPQQQQQQQ QQLSQIQQSQ IQHLQQLQLM
     HQATQAQRVN SAGSLSNARP GVGGSSRIST PSLATNNRLG LTAQQVMQLQ AIGGGSAILS
     GHLPTNHQFT KRDATNSPSQ ASPPHGPVVP PSGVNSPRPE QTNHVQGPQV PGSGIARPTS
     SLGNQYYPAT AAYIPDQVTV ALRLQMLQQQ QLLQQQQQAQ QQHQQAQGFP NSS
//
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