ID   ACRB_ASPCL              Reviewed;        1018 AA.
AC   A1CIK0;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Probable ubiquitination network signaling protein acrB;
DE   AltName: Full=Acriflavine resistance protein B;
GN   Name=acrB; Synonyms=acr2; ORFNames=ACLA_051770;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: Component of the regulatory network controlling carbon source
CC       utilization through ubiquitination and deubiquitination involving creA,
CC       creB, creC, creD and acrB. Involved in resistance to acriflavine, and
CC       required for normal growth on a range of sole carbon sources, including
CC       fructose, cellobiose, raffinose, and starch, and reduced utilization of
CC       amino acids, including GABA and beta-alanine, as sole carbon and
CC       nitrogen sources (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the acrB family. {ECO:0000305}.
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DR   EMBL; DS027054; EAW10705.1; -; Genomic_DNA.
DR   RefSeq; XP_001272131.1; XM_001272130.1.
DR   AlphaFoldDB; A1CIK0; -.
DR   SMR; A1CIK0; -.
DR   STRING; 5057.CADACLAP00004694; -.
DR   EnsemblFungi; EAW10705; EAW10705; ACLA_051770.
DR   GeneID; 4703619; -.
DR   KEGG; act:ACLA_051770; -.
DR   VEuPathDB; FungiDB:ACLA_051770; -.
DR   eggNOG; ENOG502QSPS; Eukaryota.
DR   HOGENOM; CLU_005822_0_0_1; -.
DR   OMA; SDEVCFN; -.
DR   OrthoDB; 225448at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   PROSITE; PS00589; PTS_HPR_SER; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Ubl conjugation pathway.
FT   CHAIN           1..1018
FT                   /note="Probable ubiquitination network signaling protein
FT                   acrB"
FT                   /id="PRO_0000395726"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        217..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        258..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          342..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          581..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          962..1018
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          601..788
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        965..979
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        986..1018
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1018 AA;  109618 MW;  213017EEBF382787 CRC64;
     MPRSSATARK NQSNRNENGA SSGKKVAKQK SNGHLNGSLN GGSTPGSVSS SQVDLPSSRS
     TSDSAIAPAA AASSNLNGIS DSSKEDCNGR EKLNGYTKGN ADMSYVQTNG AGSQNGGDHA
     GQASHRTDKS ATGAKRSTSN ASINPLQLAS TILKSCPMYD TIAILIFLLQ LPPMVLTLVQ
     FLFASLTFMP PSGASAGSLS SNFDIFQGPA GTPSLSTMIA MDGFCLLIWA LLMWTWAQNF
     ALDLAHVQVA ITLGGGGSGK NGGVNTLCVG IVLILHLIRS KGIQDFVIGH LLSSNIISPD
     LLAQYSHLLP TEFRRTESQT SPSWIRSLLA VHILAQAGTA MARRSMAKNR SPNPPRPGKR
     VDTEASAGSQ TQIDSAFESG ASVSSYLGPD GQLITPTAHK DGRDRLLSAK KRRRQANQVR
     SRQPFWAALA STKVTVMREY EHSRALSKTA RGLPMTENDL QGVSFDDGLV WITDVDASTI
     KFAAGDFASA DDSGLSGACE DGRLGNEEIE PFYVCVNGAL WATATISRVP DAQKGSGMVH
     WRGEVSGLAP NCAYTCSFMR SDTDEEICAI SVKTPVTNDT EQFSLVSPPP QPSYRPSSPT
     TTLKNSIVNA EAKLNEKRSR LRKAKNDHKL IISKIRKELD NYNHRLHSGT DENRQKQRSL
     QLERNIRQTE EATALLEGQL DSLENIPEEE LREWSDQKAK YDQELQLLNS AKEELVSARS
     AVAREVSSLE SDLGSTVQRR ERLQSRRTRV NEQYERIVSA NAQGLNERER RAAEQFAREQ
     DQAKLEANFN EQFGSIGQSV QEYQLRAQQI WQQCDAIEQA IQQQQQRMLL DSAPLTPEGN
     LPGTNPFSET SALPLGALTS TAPNSRSLLG LSFPAIKSSP LQTISSALDA SSSHPTSPVQ
     PPSFLNFPAS PLVNATSHLD SDFTYRDRSF SNRSARSSLY GSEFLDSSRR QPFQIDLPEL
     LGEKRNSGSD STALKSGLRP VSSPFQRAGS RGSGSGSNGS GGSGSGSGSP SSAYGKPN