ID A0A1L9NCQ3_ASPTC Unreviewed; 1436 AA.
AC A0A1L9NCQ3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=ABC transporter domain-containing protein {ECO:0000259|PROSITE:PS50893};
GN ORFNames=ASPTUDRAFT_54099 {ECO:0000313|EMBL:OJI87058.1};
OS Aspergillus tubingensis (strain CBS 134.48).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=767770 {ECO:0000313|EMBL:OJI87058.1, ECO:0000313|Proteomes:UP000184304};
RN [1] {ECO:0000313|Proteomes:UP000184304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 134.48 {ECO:0000313|Proteomes:UP000184304};
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; KV878187; OJI87058.1; -; Genomic_DNA.
DR STRING; 767770.A0A1L9NCQ3; -.
DR VEuPathDB; FungiDB:ASPTUDRAFT_54099; -.
DR OMA; MIKHHRG; -.
DR Proteomes; UP000184304; 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:SF620; ABC TRANSPORTER ATP-BINDING PROTEIN_PERMEASE PDR18-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; 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:UP000184304};
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 480..504
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 516..534
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 593..611
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 623..643
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 728..745
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1142..1160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1172..1191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1211..1242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1254..1278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1284..1302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1407..1427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 104..371
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 804..1047
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1436 AA; 161702 MW; 8F730B1F4032EEBB CRC64;
MDEKDASAHD PYPSDKEQTP SSDEEEQELH NLTRIASTRT GRRISQAATI IEKDDPRLDP
ANPAFDQRLW AKLVLTALNQ SGIVPQTQGV VFSNLCVSGS GSALQIQNTI ATQLAAPFRA
AAHALSRRAS PPSRQILHSF DGFLQSGELL LVLGRPGSGC TTFLKTLCGH LGGLTLEPQS
TIHYQGIEYE DMIKHHRGEV AYNKEVDQHF PHLTVGQTLS FAAHARTPQK RIEGLTRSEY
VETLTQVVLA VFGLSHTYHT KVGDNFVRGV SGGERKRVSI AEMFVSRCRI GAWDNSTRGL
DASSALKFVR ALRLSADMGR SCHAIAAYQA SQSMYDLVDK VVVLYEGRQI YFGRRDRAVR
YFEEMGWELP DRQVSGDFLT SVTNPGERKA RPDMVDKVPR TAKEFEEYWK RSPEYQELCG
QIEEYQRAHP PDSDEAKAFK ANHEEQQARH TRPRSPYLLS VPMQVRLCLR RAFQRLRNDL
PTVIVTVVTQ PILALVIGSI FFNSAPTTAT FFQKGAVLYF AVLFNALIAL NEIIQLYSQR
PIAVKQAGYA FVHPFAEALA SWIMDLPIKF TRGTLFCVIL YLMSNLRREP SQFFICYMFL
LTSVLTMSGI FRSLAAATRT SAQAMAMAGV CILCIVVYTG FVLPQPYMHP WLSWIRWVNP
IYYVYEALLA NEFHGRNFEC ASVIPSYAVG SSFICSTVGA VAGERFVSGD AYVEQNYQYY
YSHVWRNYGI LVAYLVLFTG LYLFLSEYNS GETSKAETLV FRSGHVPQYL LSSDGIEDGE
APPDKPEVQN QVDAINLPQQ TDILSWKGLN YDIPVKDGTR RLLDNVNGWV KPGTLTALMG
VSGAGKTTLL DVLAQRVSIG VVTGDVLVNG RALQANFPRE TGYVQQQDLH METTTVREAL
RFSAMLRQPA SVSEKEKYEY VEEIIKVLHM QDFAEAVVGS LGEGLNVEQR KLLSIGVELA
AKPTLLIFLD EPTSGLDSQS SWTICSLLRR LADHGQAVLA TIHQPSALLF QTFDRLLFLA
KGGKTVYFGD IGDQSRILLE YFERCGARPC GDMENPAEYI LETVAGEASE GIDWVQRWND
SPERKEVLAE LERLQDPQQQ PEPRARDGDS NNMEFAMPFT SQLYHVMKRA FQQYYRQPEY
VFAKYSLGIA CGLFIGFSFY KANNTEQGFQ CALFSVFLLA TVFTTLVNQI TPRFVAQRAL
YEVRERPSRV YSWKVFILSN IFVEIPYHFV LGVCVWASFY WAVMGTGQDA ERHVLALLYI
VQFYLYVASM AHFVIAAIPQ APVAGIFAIL MFAFAFIFNG MLQPPGDLPG FWIFMYRVSP
FTYYTAGVGS SILHGRPVEC STSELSVFDP PSNYTCGQYM QKYVDAAGGQ VYNPNATSAC
EYCSMTIADE YLALRWVYWK DRWRDYGIFW CYFVFNIAGA VMLYYVFRVK KWGKGK
//