ID   ACRB_EMENI              Reviewed;        1015 AA.
AC   Q876Q0; C8V482; Q5B783;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Ubiquitination network signaling protein acrB;
DE   AltName: Full=Acriflavine resistance protein B;
GN   Name=acrB; Synonyms=acr2; ORFNames=AN3597;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=12750323; DOI=10.1093/genetics/164.1.95;
RA   Boase N.A., Lockington R.A., Adams J.R., Rodbourn L., Kelly J.M.;
RT   "Molecular characterization and analysis of the acrB gene of Aspergillus
RT   nidulans: a gene identified by genetic interaction as a component of the
RT   regulatory network that includes the CreB deubiquitination enzyme.";
RL   Genetics 164:95-104(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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. {ECO:0000269|PubMed:12750323}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the acrB family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CBF75809.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAA59805.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF485329; AAO26698.1; -; Genomic_DNA.
DR   EMBL; AACD01000061; EAA59805.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001302; CBF75809.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_661201.1; XM_656109.1.
DR   AlphaFoldDB; Q876Q0; -.
DR   SMR; Q876Q0; -.
DR   STRING; 162425.CADANIAP00005147; -.
DR   EnsemblFungi; EAA59805; EAA59805; AN3597.2.
DR   GeneID; 2873016; -.
DR   KEGG; ani:AN3597.2; -.
DR   eggNOG; ENOG502QSPS; Eukaryota.
DR   HOGENOM; CLU_005822_0_0_1; -.
DR   InParanoid; Q876Q0; -.
DR   OrthoDB; 225448at2759; -.
DR   Proteomes; UP000000560; Chromosome II.
DR   Proteomes; UP000005890; 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..1015
FT                   /note="Ubiquitination network signaling protein acrB"
FT                   /id="PRO_0000395732"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          102..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          337..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          573..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          722..742
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          952..1015
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          596..753
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        26..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        961..977
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        983..1015
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1015 AA;  108927 MW;  776CA7359F5515C3 CRC64;
     MPRSSATARK SHSNRQDHGG GGSGKKPSKQ KSSGHLNATY NGTAGSETGP SSQVDWPSHR
     SGDQSIAAAA AKSNGPVDSL KADTNGRGYP GGYAKGNADM SYGQTNGGVS PNGGLAGPAS
     RRTDKSVTGT KRTTSNASVN PFQLASTILR SCPMYDTIAI LIFLLQLPPM VLTLVQFLFA
     SLTFMPPSGT ASGSFTSNFD IFQGPAGTPS LGTMIAMDGF CLLVWGLFMW TWAQNFALDL
     AHVQVAITLG GGGAGKNGGV NALCVGIVLI LHLIRSKGIQ DFVVGHLVSA KIISPDLLSH
     YSYLMPAEFK RTESQSSPSW IRSLLAVHIL AQAGTAMARR SMTKNRTPAP SRSGKRVDTE
     ASAGSQTQID SAFESAASVS SYLGPDGQII TAAHKDGRDR LISAKKRRRQ ANQVRSRQPF
     WAALASTKVT VMREYEHSRA LSKTARGLAT TEDDLQGVSL DDGLVWITYV DSSTIKFAAG
     DFASSDDHSA SGVCEAGRVS SEDAEPFYVC VNGAPWATVV ITKEHDPSKA SNTIYWRGEI
     SGLAPNCAYT CSFVKCDTDE EICAMSVKTP AANDAEQANS VPAPPQPSYR PSSPTTTLKN
     SIINAEAKLN EKRARLRKAK NDHKLAISKI KKELDNYTNR LQSGTDENRQ KQRSLQLERN
     IRQTEEATAA LDNQIDNLGN VPDDEYQEWV EQKAKYEREL ELLKSAKAEI AATRTANARE
     LSSLESELNS TTQRRERLQG RRTRVNEQYE RIISANAQGL NERERRAAEQ FAREQDQSKL
     EQSFNEQFAS ISQSVQDYQL RTSQLWQQCT AVEQALQQQL LMEPAPLTPE GELPGTSTFA
     DAPSVPLGTL ASNMPSHRSL LGQSFPPLKS SPLQHYASPI GTAPSHPTSP IAAPSYQPFS
     SSPFGNAASF LDPDFVYRDR SFSNRSARSS LYGSEFPDAI TARRVPFGVD PFELGNEKRR
     GSGSDSTPLN GPSGLRPISS PFQRAASRAS GTGSGGSGGS GSGSGSPSSA RGKGN