ACRB_ASPNC
ID ACRB_ASPNC Reviewed; 1017 AA.
AC A2Q9L8;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Probable ubiquitination network signaling protein acrB;
DE AltName: Full=Acriflavine resistance protein B;
GN Name=acrB; Synonyms=acr2; ORFNames=An01g08310;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAK43924.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AM269976; CAK43924.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001389257.2; XM_001389220.2.
DR AlphaFoldDB; A2Q9L8; -.
DR SMR; A2Q9L8; -.
DR PaxDb; A2Q9L8; -.
DR EnsemblFungi; CAK43924; CAK43924; An01g08310.
DR GeneID; 4977242; -.
DR KEGG; ang:ANI_1_1106014; -.
DR Proteomes; UP000006706; Chromosome 2R.
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..1017
FT /note="Probable ubiquitination network signaling protein
FT acrB"
FT /id="PRO_0000395729"
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..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 604..783
FT /evidence="ECO:0000255"
FT COMPBIAS 28..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1017 AA; 109559 MW; 2212E78FC77496E5 CRC64;
MPRSSATARK SHSNRHENGL VGPGKKVNKQ KSNGNLNGNT NGASAPNSGP STQVDWPASR
SSSDSALTSS ATTASKVNGS ADTSKADGNG RGLLNGYAKG NADMSYGQTN GAVPQNGGLA
GQASRRTEKP ATGSKKSGSI NPLQLASTIL KSCPMYDTIA ILIFLLQLPP MVLTLVQFLF
ASLTFMPPSG ASSGSLTSNF DIFQGPAGTP SLGTMIAMDG FCLLFWGLFM WTWAQNFALD
LAHVQVAITL GGGGSGKNGG VNALCVGIVL VLHLIRSKGI QDFVIGHLLS AKIVSPDFLS
QYSHLMPPEF RRTEPQSSPS WMRSLLAVHI LAQAGTAMAR RSMAKNRSPA PPRNGKRVDT
EASAGSQTQI DSAFESGASV SSYIGADGQL VTPATHKDGR DRLMSAKKRR RQANQVRSRQ
PFWAALASTK VTVMREYEHS RALNKTGRGL MMTEEDLQGI SLDDGLVWIT EVDSSTIKFA
AGDFSSVDDP ALAGVCETAR LGNDETEPFY VCVNGALWAT ATITKVQDAP KGSNTVHWRG
EVSGLAPNCA YTCSFVRSDT DEEICVMSVK TPAATDAEQV SSIPTPPQPS YRPSSPTTTL
KNSIVNAEVK LNEKRARLRK AKNDHKLVIS KIRKELDNYN HRLQSGTDEN RQKQRSLQLE
RNIKQTEEIT AALESQLDNL ENIPEEELEE WSTQKSKYEQ ELEQLNLAKE ELVSARAAVA
REVSSLESEL NSAIQRKERL QGRRTRVNEQ YERIVSANAQ GLNERERRAA EQFAREQDQA
KLEANFHEQF ASISQSVQEY QVRTNQLWQQ AAAIEQAIQQ QQQQMLLDSA PLTPEGNLPG
TNPLTEAPGM SLGALTTTAP NTRSLLGLSF PSLKSSPLQH ASSPVGAASS HPTSPTQPPS
YLQHFPTSPL GNTGNYFDMD FTYRDRSFSN RSAHSSLYGA DFLDSNRRGP FQLDLSDTVI
EKRMDSGSEG VTPNPIMRPI STPFQRADSR GSGSGSGSSG ASGSGSGSPS STGGKGN
