ID A2R4X2_ASPNC Unreviewed; 1117 AA.
AC A2R4X2;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE SubName: Full=Contig An15c0100, genomic contig {ECO:0000313|EMBL:CAK42294.1};
GN ORFNames=An15g01910 {ECO:0000313|EMBL:CAK42294.1};
OS Aspergillus niger (strain ATCC MYA-4892 / 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 {ECO:0000313|EMBL:CAK42294.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK42294.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
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., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC EF3 subfamily. {ECO:0000256|ARBA:ARBA00011054}.
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DR EMBL; AM270337; CAK42294.1; -; Genomic_DNA.
DR RefSeq; XP_001396730.1; XM_001396693.2.
DR AlphaFoldDB; A2R4X2; -.
DR EnsemblFungi; CAK42294; CAK42294; An15g01910.
DR GeneID; 4987792; -.
DR KEGG; ang:An15g01910; -.
DR VEuPathDB; FungiDB:An15g01910; -.
DR HOGENOM; CLU_002848_0_1_1; -.
DR OrthoDB; 49929at2759; -.
DR Proteomes; UP000006706; Chromosome 3R.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0043022; F:ribosome binding; IEA:EnsemblFungi.
DR GO; GO:0008079; F:translation termination factor activity; IEA:EnsemblFungi.
DR GO; GO:0006338; P:chromatin remodeling; IEA:UniProt.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IEA:EnsemblFungi.
DR GO; GO:0006449; P:regulation of translational termination; IEA:EnsemblFungi.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:EnsemblFungi.
DR CDD; cd03221; ABCF_EF-3; 1.
DR CDD; cd18626; CD_eEF3; 1.
DR Gene3D; 2.40.50.990; -; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR015688; eEF3_ABC2_chromodomain-like.
DR InterPro; IPR047038; eEF3_chromodomain-like_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19211:SF14; ATP-BINDING CASSETTE SUB-FAMILY F MEMBER 3; 1.
DR PANTHER; PTHR19211; ATP-BINDING TRANSPORT PROTEIN-RELATED; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF00385; Chromo; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 482..706
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 726..1043
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1117 AA; 123051 MW; 21C38B8A8EDEC931 CRC64;
MPHPEDPTPA MTTVVSKTPS GVPPSADEVG SILNTIFQAE TSQQALDASY ALTNLLIQSV
GCSGFRTYNI LPPIKKAATD KKNGALRESA MLILGALFER FPREHPLSEV VFLLQDGGVL
NLALDLLADK GAVVRDAAQY AIDALFACLK PEAMVNALLP AVSAYLNQST AKWQGFVGAY
SLIEKMATKA QMGTGPLEEE REKDLLREAM GKTLKDLIPL VESGMHDLKN EVAKKAIKAM
NALTTLLSND DVAPRIPLLI KTMEQPSEQT LQKAIHALSQ TTFVAIVTSP VLALLTPLLE
RSLNAPTTPQ ETLRQTVVVV ENLTKLVHDP AEARTFLPKL KPGVQRVKDR ASLPEVRELA
TRALDVIEKA MADKDVAAGV VVKITPEEVL AVLEAKIQEH GGLARPEDAT LYALGKNYVA
EMVREDVNCR MHDRIPACIA PYLRGLLHED KHDAVATAVQ EHFIEEDHRK FGKPAPEDPN
EVEIVNANFS LAYGGMLLLS HTNLRLLKGH RYGLCGRNGA GKSTLMRSIA NEKLEGFPPQ
SEVRTCFVEH NQGEDADLSI FEYVSKDPMI AAEGEEHIRS VLLEFGFTDG PEGRQNQRVG
SLSGGWKMKL ALARAMLRKA DVLLLDEPTN HLDVANVKWL QEYLKKHTDI TSLIVSHDSG
FLDEVCTDIY HYEQKKLVCY KGNLADFVKV KPEAKSYYTL SASIVQFKFP PPGILAGIKS
NTRAILRMTN CTYTYPGASK PSLTDASLSL TLSSRVAIIG GNGAGKSTFI KMLTGETIPQ
TGKVEKHPNL RIGYIKQHAL EHVEMHLEKT PSQYLQWRYA NGDDREVYLK QTRILTEEDK
AQLQKPVDLG DGRGPRRIEA LMGRQKWKKS FQYEVKWVGL LPKHNTMISR ETLLNLGFFK
LVQEFDDHEA SREGLGFRVL DPKVISKHFE DIGLDPEIAN HNEISGLSGG QKVKVVLAGA
MWNNPHLLVL DEPTNFLDRD SLGGLAVAIR DFKGGVVMIS HNEEFVGALC PEQLHVADGR
IVSRTNTAIS LDRFEDSAAS SPQPGSTAVN STATSAAASA VNSGAEEPGE LKFKAKKKKK
LTRAQLKERE ARRRLRHLEW LQSPKGTPKP PDTDDEE
//
