ID A0A1L9VLA7_ASPGL Unreviewed; 1476 AA.
AC A0A1L9VLA7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=ABC transporter domain-containing protein {ECO:0000259|PROSITE:PS50893};
GN ORFNames=ASPGLDRAFT_148750 {ECO:0000313|EMBL:OJJ84718.1};
OS Aspergillus glaucus CBS 516.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Aspergillus.
OX NCBI_TaxID=1160497 {ECO:0000313|EMBL:OJJ84718.1, ECO:0000313|Proteomes:UP000184300};
RN [1] {ECO:0000313|Proteomes:UP000184300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 516.65 {ECO:0000313|Proteomes:UP000184300};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) subfamily. {ECO:0000256|ARBA:ARBA00006012}.
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DR EMBL; KV878896; OJJ84718.1; -; Genomic_DNA.
DR STRING; 1160497.A0A1L9VLA7; -.
DR VEuPathDB; FungiDB:ASPGLDRAFT_148750; -.
DR OrthoDB; 5473955at2759; -.
DR Proteomes; UP000184300; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd03233; ABCG_PDR_domain1; 1.
DR CDD; cd03232; ABCG_PDR_domain2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC2_TM.
DR InterPro; IPR029481; ABC_trans_N.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR034001; ABCG_PDR_1.
DR InterPro; IPR034003; ABCG_PDR_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010929; PDR_CDR_ABC.
DR PANTHER; PTHR19241; ATP-BINDING CASSETTE TRANSPORTER; 1.
DR PANTHER; PTHR19241:SF625; ATP-DEPENDENT PERMEASE PDR10-RELATED; 1.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF14510; ABC_trans_N; 1.
DR Pfam; PF06422; PDR_CDR; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000184300};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 508..531
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 543..564
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 617..639
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 651..670
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 756..777
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1172..1193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1205..1227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1248..1273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1293..1315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1327..1351
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1444..1464
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 144..398
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 834..1076
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 1476 AA; 165345 MW; 49260E74397BA2A0 CRC64;
MSVLGGIPAM DSSEYQQRLG AGLEVRDTDT VSSTTQIDKM DGNQLAVDME DEIEEMVRQL
TRHSTHFSSS NAKNPFFEED KETTWHPDSP FFKPKDWVRS LIAAQSQDPE RFLQRSVGVA
FKNLHVHGFG SPTDYQKDVF NALLSVGGLV RNIIGVGKQK VHILNNFNGL VRSGEMLVVL
GRPGSGCSTF LKSIAGEMNG IYVNDDSYMN YQGISAPTMH KQFRGEAIFS AETDVHFPQL
TVGETLTFAA MARAPRTRFP NLTRKEYAEH LRDVVMTMLG LKHTFNTRVG NDFVRGVSGG
ERKRVSIAEA ILSGAPLQCW DNSTRGLDSA NALEFCKNIR LMSDYTGTTA CVAIYQASQN
AYDVFDKVVV LYEGEQIYFG PTGEARKFFT NMGFDCPSRQ TTADFLTSLT SPTERRVKPG
YEAKVPRTPA EFAQRWQRSQ ECARLLREID TFDKEHPIGG QSLTTFSEAR RLMQSKRQRL
KSPYTLSVLE QINLNLVRGF QRLKADMTLT YSALFGNFFI SLILGSVFYN LPGDTSSFFS
RGVLLFYAVL LAAFASALEI LTLYAQRPIV EKQSRYAFYH PFTEAAASML CDIPYKLTNS
VTFNLPLYFL SNLKREPGAF FIFWLFSIMT TLTMSMVFRT FGAASRSLAQ ALVPAALLIL
GLVIYTGFII PTKDMLGWSR WMNYIDPIAY SFESMMVNEF RNRKFPCTSF VPSGEGYENV
DSINTICSTV SSTAGDPNID GDAYLQTAYA YSNGHLWRNL GIVIAFMIFF MCVYLIATEY
ITEAPSKGEV LLFRRGNQPK HLQEDAENTP DAAYRADENA EGTGANIQRQ TAIFQWQDLC
YDIKIKNEPR RILDNVNGWV KPGTATALMG VSGAGKTTLL DVLATRVTMG VVTGDVLVDG
QPRDDSFQRK TGYVQQQDVH LPTSTVREAL QFSAILRQPA HLSRQEKLAY VEEVLELLGM
QSYADAVVGV PGEGLNVEQR KRLTIGVELA ARPQLLLFLD EPTSGLDSQT SWSILDLIEI
LTKHGQAILC TIHQPSAMLF QRFDRLLFLA KGGRTVYFGQ IGENSSILAD YFMRNGGHTL
ADGENPAEWM LDVIGAAPGS HSDIDWPAVW NKSPEKEAVV HHLGELKSTL SQKEKETGTN
ADYREFASPT SVQLWECLSR VFSQYWCTPS YIYSKLILSI LTALYNGFSF FHAKNTQQGL
QNQMFSIFML MTIFGNLVQQ IMPNFIIQRS IFEVRERPSK MYSWRVFMAS NILVELPWNL
LVAVLMFFCW YYPVGLYQNA QPTDAVHERG ALMFLYLLMF LWFTSTFSHM VVAGVENAET
GGNIANLLFS LLLLFCGVVS TPEAMPGFWI FMYRVSPFTY LVSGMLSTAV SGTSVTCSAI
ETLVFNPPDS QTCYDYLNPY AVRTGGYIEN PNATSSCSYC PMASTDTFLA QVNSYWGEAW
RNFGILWAYL AFNIVVALGI YWLARVPKGS KAKGSV
//
