ID A0A1Y2WVX2_9PEZI Unreviewed; 1572 AA.
AC A0A1Y2WVX2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=ABC transporter domain-containing protein {ECO:0000259|PROSITE:PS50893};
GN ORFNames=K445DRAFT_65464 {ECO:0000313|EMBL:OTB12958.1};
OS Daldinia sp. EC12.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Daldinia.
OX NCBI_TaxID=1001832 {ECO:0000313|EMBL:OTB12958.1, ECO:0000313|Proteomes:UP000243732};
RN [1] {ECO:0000313|EMBL:OTB12958.1, ECO:0000313|Proteomes:UP000243732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC12 {ECO:0000313|EMBL:OTB12958.1,
RC ECO:0000313|Proteomes:UP000243732};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(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; KZ112951; OTB12958.1; -; Genomic_DNA.
DR STRING; 1001832.A0A1Y2WVX2; -.
DR OrthoDB; 5473955at2759; -.
DR Proteomes; UP000243732; 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; 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:SF682; ABC MULTIDRUG TRANSPORTER (EUROFUNG); 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; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000243732};
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 586..606
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 618..637
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 658..683
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 695..713
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 725..745
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 835..853
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1271..1289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1334..1356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1376..1396
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1408..1429
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1534..1554
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 224..481
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 930..1173
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 525..552
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 24..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..900
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1572 AA; 175695 MW; ECB952D2B86CDF49 CRC64;
MDGDRPTPAD TDIPGGFPET PSSIPAKRLS TISREFSLAA NRDSSISVGK SFNTNTDAFT
STHSDGVNNV NVDGATGGNA RPSDASPFSS HQAVTAPQAQ TAPGETSSDE SEKTEVEPRF
APIKSTVEQP KLQRNESEIK TEDDLFRALS RRRSITSNAE SQGENDEIER LMSRMFGQAR
QQNSEEEKTR HAGVIFRNLT VKGVGLGASL QPTVGDIFLG LPRFLLNLVT KGPKAATGKP
PVRELISNFN GCVRPGEMLL VLGRPGSGCT TFLKTFCNQR AGFKDVVGDV TYGGTDAKRM
AKDFRGEIIY NPEDDLHYAT LSVKNTLTFA LRTRTPGKES RMEGESREDY VREFLRVAAK
LLWIEHTMDT KVGNEYIRGV SGGERKRVSI AEALITRASV QGWDNSSKGL DASTAVEYVQ
SLRALTNMAQ VSTAVSLYQA GESLYNLVDK VLLIDNGQCL YYGPSDRAKQ YFLDLGFDCP
ERWTTADFLT SVTDSHERSV RPGWEDRIPR SAQEFAEIYR KSEAYQRNLD DISDYEAHLE
EQRRERAENT SEKNKRKNYT ISFHQQVIAL TKRQALVMLG DRASLIGKWG GIVFQSLIVG
SLFYNLPPTA AGAFTRGGVL FFILMFNALM ALAEQTAAYE SKPILLKHKN FSFYRPSAYA
LAQTVVDIPL VFIQVFLFDI IIYWMAGLSA TPSQFFISLL ILWLITMTTY AFFRSISALF
KTLDDATKIT GVAIQIIIVY TGYLIPPSSM HPWFSWLRWI NWLQYGFECL MSNEFYNLEL
ACQPPFLVPN GVEGASPEYQ SCTLAGSRPG EVVVNGGNYI QVAFNYSRSH LWRNFGFLWA
FFGFFLVVSM IGMERMKPNA GGAAVTVFKR GQVPKSLQKS IETGGRKGTK GDEEAGSSSE
KVTIPEEASA AQEKRDEETM QTVAKNETIF TFQNVNYTIP YQGGERKLLQ NVQGFVRPGK
LTALMGASGA GKTTLLNTLA QRINFGVVTG DFLVDGRPLP KSFQRATGFA EQLDIHEPTA
TVREALQFSA LLRQPKEVPV KEKYAYCETI IELLEMQDIA GATIGVVGEG LNAEQRKRLT
IGVELASKPE LLMFLDEPTS GLDSGAAFNI VRFLRKLADA GQAILCTIHQ PSAVLFEIFD
ELILLKSGGR VVYAGELGKD SQRMINYFES NGGQKCPPDA NPAEWMLEVI GAGNPDYAGQ
DWGDTWLESK NFEEQSKEIA QMAEKRRNIQ HSKNVQDDRE YAMPLSTQII AVVKRSFVAY
WRSPNYIMGK MILHIFTGLF NTFTFWRLGD ASIDMQSRLF SIFMNLTISP PLIQQLQPVF
LNSRNIFESR ENNAKIYSWV AWTTAAVLAE IPYAIVGGAI YFNCWWWGLM GYKMTGFPSG
FTFLCMMVFE LYYVSFGQAI AAFSPNQLLA SLFVPLFFLF VVAFCGVAVP PESLPYFWKS
WMYPLTPFHY LMEAFVGVAI HDQPVNCKPS ELARFPPPPG MDCESYTANY TMQASGKLQS
VTDGLCEFCQ YKDGDEFGRQ FSIYYSNIWR DFGIAWAYIV FNYGVVYFAT YLRFRGKNPI
SGFLAKRKQR KA
//
