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Database: UniProt
Entry: A0A179UBM5_BLAGS
LinkDB: A0A179UBM5_BLAGS
Original site: A0A179UBM5_BLAGS 
ID   A0A179UBM5_BLAGS        Unreviewed;      1543 AA.
AC   A0A179UBM5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Vacuolar import and degradation protein 21 {ECO:0000256|ARBA:ARBA00029670};
GN   ORFNames=BDBG_01822 {ECO:0000313|EMBL:OAT05425.1};
OS   Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=559298 {ECO:0000313|EMBL:OAT05425.1, ECO:0000313|Proteomes:UP000002038};
RN   [1] {ECO:0000313|Proteomes:UP000002038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SLH14081 {ECO:0000313|Proteomes:UP000002038};
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(2015).
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; GG657450; OAT05425.1; -; Genomic_DNA.
DR   RefSeq; XP_002627151.1; XM_002627105.1.
DR   STRING; 559298.A0A179UBM5; -.
DR   GeneID; 8506962; -.
DR   KEGG; bgh:BDBG_01822; -.
DR   VEuPathDB; FungiDB:BDBG_01822; -.
DR   OrthoDB; 1334563at2759; -.
DR   Proteomes; UP000002038; 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:UP000002038}.
FT   DOMAIN          647..722
FT                   /note="HSA"
FT                   /evidence="ECO:0000259|PROSITE:PS51204"
FT   DOMAIN          915..975
FT                   /note="Myb-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50090"
FT   REGION          69..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          710..758
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1013..1048
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1138..1204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1480..1543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..167
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..249
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..326
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..394
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..491
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..544
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..573
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        727..741
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1013..1027
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1138..1184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1480..1495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1543 AA;  169260 MW;  1F77F195D2A36A05 CRC64;
     MLRDELLQSK HDEIARCVSS RKRKLSELYF ATVGFPGATD GSPQHLQYQQ REQEFLDAND
     ITKGRLFNEG TLPRRPDVAP LQVSPRDDKL NQGSLSASAA DRITDSHRRK PIFSPVRIAV
     SSPKLPSTGT YTETGSQDIF RPQDHTPTGT TESVAVQASS GELDIPQITP SASHDAIREK
     EVSSPASTQQ TIAATVTPVT DVDMDEAPDG QDNTGTTEVP APESDLPIGS RKTVAEIQDN
     ATGASLPTSD APERQHGKRS GNDLPCLATD ASPKSTDQPL SPASSRGQLS STTSVSDRTP
     ATSPAKEQPQ REPQNESTTP PNSGRSIPVP MVTADISTIR RAPATPDEQL KFEAEQSSIQ
     QAASKPTKNA PYTGSAFSSF QLTPENSFSS PKKPPDSHNE PDLSKSSKTS VAPENRPLVN
     GALRLDTEGV KPEPVSKSHE PQSAPVTLEL PEGAGGSPLP SATRKTSTSS APTQPHFQPE
     RMTTRVSSGA IRHRSVSEIL GETPKSAMDK TFDKAVSESP TATSENSQVR SRPKNKRENQ
     KERSKLSTVV FPKQQSAAEK NESADLVRTP SGHTRSLNEE KDYLFTLFQA KAHYPPRSMH
     LSSLLSTAHK TLTTANHFVE YQEQMDCRSL KRIYQLQHAN RWPLRQLQRS AEPERSGTHW
     DVLLDHMKWM RTDFREERKW KIAAAKRCAD WCAEYVSSSD GRRAELRIPA RVPPATSKIE
     ESGNHKTTPS YSDDRVDDSL PHSQPTPDLI SSMEDDSVSE GFNDEVHPDL SDGVVPAAIF
     SLGSDEFTFG MERTPAFEKI LEELPLYIPI NISSETNLPQ FKRPPDSSWR KELLAVSKYA
     TGKLEFTSKQ PPRKRSRYDY SDNDDDVDVD AIEIPPEQTN VALFQPQNKH IRDRIHPGQV
     FRPPTEFLMP SLGFYESRQP SQWTCAEEDE LKRIVKEYSF NWSLISACLT PPSLYTSGAD
     RRTPWECFEK WVQLEGLPTE MLKTPYFRAY TSRVESAQRA VLAAQQQQQQ QAQAQVQAQA
     QANPQRQGSN PPPTPTAILR RRPTTPMRVE RKRSVRHLTL LDCMRKLSKK RETLLQKQQH
     ATHLAASRKL NEVNQPRPPI STPAEFSRLK HERELKIQEN QEQYKQAMIA QRMAMAHRVA
     QQQQAQHQQQ QQQLQQQQQH RQMPNQQALL NGIPPRNTAS APPNGVMQGI PAPSGLPNGL
     PVSAALAQSR PHPGMQLPTG AQVNGMPNPG MGLKMIPQPG IPQAMNGRPG IQTQASSDNA
     RIIREASRVQ EEQQRMVQSR QQQLQNQQQS FIPQGPHSSP NMSMGNMNVN PNNPAMLTFQ
     AVSGVNSPSF HASSLAQGVS TASPRLNHAN VLANAAAGLP TLVSIQNTIR RTNPNMSQEQ
     ITKLATERLQ HIQQQRMSQA AMNAAAGNTM GSMQTSYQMH HDGNMHQLSH ANVPNGGVPA
     SMQTLQQTQG YSPLMRVTQT VQQPNRMGVN GSPAMNAAMA VQQGRSATAQ AHRSTGGQGG
     HGPGPVPGPG PSPGGVSGSG QGSGVGPGPG KSPRPPQAQM ASS
//
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