ID   ACRB_ASPTN              Reviewed;        1013 AA.
AC   Q0CT23;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Probable ubiquitination network signaling protein acrB;
DE   AltName: Full=Acriflavine resistance protein B;
GN   Name=acrB; Synonyms=acr2; ORFNames=ATEG_03161;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476597; EAU36435.1; -; Genomic_DNA.
DR   RefSeq; XP_001212339.1; XM_001212339.1.
DR   AlphaFoldDB; Q0CT23; -.
DR   SMR; Q0CT23; -.
DR   STRING; 341663.Q0CT23; -.
DR   PRIDE; Q0CT23; -.
DR   EnsemblFungi; EAU36435; EAU36435; ATEG_03161.
DR   GeneID; 4317907; -.
DR   VEuPathDB; FungiDB:ATEG_03161; -.
DR   eggNOG; ENOG502QSPS; Eukaryota.
DR   HOGENOM; CLU_005822_0_0_1; -.
DR   OMA; SDEVCFN; -.
DR   OrthoDB; 225448at2759; -.
DR   Proteomes; UP000007963; 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..1013
FT                   /note="Probable ubiquitination network signaling protein
FT                   acrB"
FT                   /id="PRO_0000395731"
FT   TRANSMEM        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        255..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          342..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          574..599
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          878..906
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          954..1013
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          597..806
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        25..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        986..1007
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1013 AA;  109145 MW;  941A54FC7B72C6BD CRC64;
     MPRSSATARK SHSNRHDNGV VGSGKKVSKQ KSNGHLNGNH ANSSTPTSGP SSQVDWPSSR
     SNSDTAIPTT AAAAARLNGA TENSKDIRGH LNGYAKGTSD MSYGQANGAV PQNGCLPGDA
     ARRTEKPATA SKRSGSSASV NPLHLASTIL KSCPMYDTIA ILIFLLQLPP MVLTLVQFLF
     ASLTFMPPSG ASAGSLTSNF DIFQGPAGTP SLGTMIAMDG FCLLFWGLFM WTWAQNFALD
     LAHVQVAITL GGGGSGKNGG VNALCVGIVL VLHLIRSKGI QDFVMGHLLS AKIISPDLLS
     QYSHLIPAEF RRTEPQSSPS WIRSLLAVHI LAQAGTAMAR RSMAKNRAPA PPRTGKRIDT
     EASAGSQTQF DSAFESGASM SSYIGPDGQF ITPATHKDGR DRLISAKKRR RQANQVRSRQ
     PFWAALASTK VTVMREYEHS RALSKTARGL TMTEDDLQGV SLDDGLVWIT DVDSSTIRFA
     AGDFSSPDDA SGSGVCETGR LSDDMEPFYV CVNGAQWATA TISKVPDARK GTSAVHWRGE
     ISGLAPNCAY TCSFMRSDTD EEICAMSVKT PATSDAEQVS SISAPPQPTY RPSSPTTTLK
     NSIINAEAKL NEKRSRMKKA KNDHKLVVSK IRKELENYNH RLHSGTDENR QKQRSLQLER
     NIKQTEEATA ALGEQLDNLE NIPEEELEEW TMQKAKYERE LELLNSVKEE LIAARSAVAR
     EVSSLESELN STVQRRERLQ GRRTRVNEQY ERIISANAQG LNERERRAAE QFAREQDQAK
     LEANFNEQLA SITQSIQEYQ LRTNQLWQQS AAIEQAIQQQ QQQMLMDSAP LTPEGNLPGT
     NPLGDTPSLA LAGLTTSAPS SRSLLGLNFP PLKSSPLQHA SSLVGATSSH PASPTQTPSY
     LQHFPTSPLA NASSPFDPDF VYRDRSFSNR SGRSSLYGFD LIDSSRRAPF QFDLSEAASE
     KRRSSGSESN GPNLGLRPIS SPFPRAGSRA SGSGSGGSGS GSGSPSSAAG KGI