ID A0A1L9UZK2_ASPBC Unreviewed; 1357 AA.
AC A0A1L9UZK2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=ABC transporter domain-containing protein {ECO:0000259|PROSITE:PS50893};
GN ORFNames=ASPBRDRAFT_36188 {ECO:0000313|EMBL:OJJ77002.1};
OS Aspergillus brasiliensis (strain CBS 101740 / IMI 381727 / IBT 21946).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=767769 {ECO:0000313|EMBL:OJJ77002.1, ECO:0000313|Proteomes:UP000184499};
RN [1] {ECO:0000313|Proteomes:UP000184499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101740 / IMI 381727 / IBT 21946
RC {ECO:0000313|Proteomes:UP000184499};
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {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; KV878679; OJJ77002.1; -; Genomic_DNA.
DR STRING; 767769.A0A1L9UZK2; -.
DR VEuPathDB; FungiDB:ASPBRDRAFT_36188; -.
DR OMA; DYHVPFH; -.
DR OrthoDB; 5473955at2759; -.
DR Proteomes; UP000184499; Unassembled WGS sequence.
DR GO; GO:0016020; C: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; 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:SF639; ABC MULTIDRUG TRANSPORTER (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR19241; ATP-BINDING CASSETTE TRANSPORTER; 1.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 2.
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 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:UP000184499};
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 412..433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 440..456
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 485..511
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 523..544
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 556..574
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 659..681
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1058..1077
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1089..1108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1128..1161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1199..1221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1233..1253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1327..1346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 46..302
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 728..970
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 1357 AA; 152791 MW; EAF4BC2C9E6D2D16 CRC64;
MDTSSSSATV DIEPGNSSIP KQLTLTWRNV SVNVTAPDAA LGDTLLSVAD PRQFLGWFSK
SQRPKRTILK DISGQLRPGE MLLVLGRPGS GCTSFLRVIS NDREAFDEVV GETRYGSMDH
KQAKKYRQQI MFNNEDDVHF PTLTVNRTMK FALRNKVPRE RPEHLHNRKD YVQEKRDGIL
ESLGIPHTKK TLVGNEFIRG VSGGERKRVS LAEVMAGQSP VQFWDNPTRG LDSKTAVEFA
RMLRREANEN QKTIMATMYQ AGNGIYDEFD KILVLAEGLV TYYGPRALAR GYFEDMGFIC
PKGANIADFL TSVTVITERI VAPGMEEKVP NSPAEFEARY RQSAIYSQMM NDIQPPEKLV
NEDENLALAV AMEKRKQHVP RPQSVYTAGL WDQILSCTLR QFQILAGDKL SMIIKVVSAI
LQALVCGSLF YNLKLDSSSI FLRPGALFFP ILYFLLETMS ETTGSFMGRP ILSRQKRFGF
YRPTAFAIAN AITDIPIVLV QVSCFSLILY FMSAMQMDAG RFFTYWIIII VQTLCYMQMF
RAIGALCKQF GNASKMTGFL STVFFVYGGY LIPFEKMHVW FRWIFYLNPG AYAFEALMAN
EFTGLELDCV EPDYIPYGSG YPSGSSPYRG CTVKGSNAEG VIDGAAYIKE QYNYTYHHVW
RSFGIIVGFW AFFIFLTAVG FELRNSSAGS SVLLYKRGAK SKKPDEESSV SAKSEGAVLA
QSGKQSTFTW SNLDYHVPFH GQKKQLLDQV FGYVKPGNLV ALMGSSGAGK TTLLDVLAQR
KDSGEIIGSI LIDGRPQGIS FQRTTGYCEQ MDVHEGTATV REALVFSALL RQPDTVPREE
KIAYVDHIID LLELGDIRDA LIGVPGAGLS IEQRKRVTLG VELVAKPTLL FLDEPTSGLD
GQSAYNIIRF LRKLVDSGQA VLCTIHQPSA VLFDAFDSLV LLAKGGKMTY FGETGEESHK
VLDYFAKNGA PCPPDMNPAE HIVEVIQGNT EKPIDWVDVW SRSEERERAL AEIEALNKEG
QSNTDYVEDQ SNFATPVWFQ FKMVLHRLMV QLWRSPDYMW NKIILHVFAA LFSGFTFWKM
GDGTFALQLR LFAIFNFIFV APGCINQMQP FFLHNRDIFE TREKKSKTYH WIAFIGAQAV
SEIPYLIICA TLYFACWYFV AGLPVDAYIS GHMYLQMIFY EFLYTSIGQA IAAYAPNEYF
AAIMNPILIG AGMISFCGVV VPYESITPFW RYWMYYLDPF TYLVGGLLGE VLWDVKVQCE
PSEFIKFNAP SGQTCGQYMA EFISEQTGYL LDANATDTCS FCQYSMGSDY AKTFNLKEKY
YSWRDTGITA LFCITSYALV FLMMKLRSKK TKSARSE
//
