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Database: UniProt
Entry: A0A074WEK8_9PEZI
LinkDB: A0A074WEK8_9PEZI
Original site: A0A074WEK8_9PEZI 
ID   A0A074WEK8_9PEZI        Unreviewed;      1535 AA.
AC   A0A074WEK8;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=ABC drug exporter AtrF {ECO:0000313|EMBL:KEQ71520.1};
GN   ORFNames=M436DRAFT_83793 {ECO:0000313|EMBL:KEQ71520.1};
OS   Aureobasidium namibiae CBS 147.97.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ71520.1, ECO:0000313|Proteomes:UP000027730};
RN   [1] {ECO:0000313|EMBL:KEQ71520.1, ECO:0000313|Proteomes:UP000027730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ71520.1,
RC   ECO:0000313|Proteomes:UP000027730};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA   Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA   Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
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; KL584714; KEQ71520.1; -; Genomic_DNA.
DR   RefSeq; XP_013425723.1; XM_013570269.1.
DR   STRING; 1043004.A0A074WEK8; -.
DR   GeneID; 25417236; -.
DR   HOGENOM; CLU_000604_35_0_1; -.
DR   OrthoDB; 5473955at2759; -.
DR   Proteomes; UP000027730; 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; 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:SF298; ABC MULTIDRUG TRANSPORTER (EUROFUNG); 1.
DR   PANTHER; PTHR19241; ATP-BINDING CASSETTE TRANSPORTER; 1.
DR   Pfam; PF01061; ABC2_membrane; 2.
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   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027730};
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        544..566
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        572..591
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        623..643
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        655..673
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        685..704
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        796..829
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1216..1237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1249..1266
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1286..1314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1326..1345
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1357..1376
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1481..1500
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1506..1525
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          187..431
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          875..1119
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          78..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          841..870
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..55
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1535 AA;  170763 MW;  65CE3D1FB6A2B1D7 CRC64;
     MWGSGVADDP RVARMDSQGG QNAWHNPAEQ RAGRLHNDPE SQSTSSEEAD RNGTWGEHDA
     GIPNEVMAME DYRALRRELT NRSRTSRPQS LGRSSRRHST ATNAVDEESV VGGNTEVQGK
     DEDDFELSDF MRQGHLGQRK GDKSAKKVGV VYKNLTVKGV GAGATFVRTL PDAVLGTFGP
     DLYHILSRFI PFLRSKNGEL KTLINDFSGV VRDGEMMLVL GRPGAGCTTF LKAIANNREG
     YAQVDGDVSY GGISAEKQRK MYRGEVNYNM EDDVHFATLN VWQTFMFALL TKTKKKATGD
     IPLIAEALMK MFGISHTKMT LVGDEYTRGV SGGERKRVSI AETLASKSTV VCWDNSTRGL
     DASTALDYAK SLRIMTDVSN RTTLVTLYQA GQGIYDLMDK VLVIDQGRCI FTGPAAAAKQ
     YFEDLGFQCP ERQTTADFLT AITDPVERKF RPGCEASTPK TPVELERAFR ESSFFTRNNQ
     DIETYEQHLE QTNHEDAKEF EETVQAGKSK TVTKKSPYTV SFIRQVLACT KREFWLLWGD
     TTTLYTKVFI IIANGLIVGS LFYGQSLNTD GAFSRGGSLF FSILFLGWLQ LTELMKAVSG
     RAVVARQKEY AFYRPSAVSV ARVVADFPVI LVQVCLFTVI MYFMTGLDVD AGKFWIYFLF
     VYVNTICITA LYRMFASLSP TIDDAVRFSG IALNLLIIYT GYVIPKTQLL NNYIWFGWIY
     YINPISYSFE AVLANEFSGR TMQCSPDNLV PQGPGIDPAF QGCTLTGAAV NAQSVSGADY
     LQTQYTYTRA HLWRNFGVVI AFTVLYLLVT IAATELFSFV GGGGGALVFK KSKKAKQQVK
     AASSVDEEKA GSDSDTAVGG STGEKEEQEA LDSIVKSESI FTWRDVEYTV PYNGGERKLL
     NKVNGYAKPG LMIALMGASG AGKTTLLNTL SQRQKMGVVQ GEMFVDGRPL GKEFQRNTGF
     CEQMDLHDGT STIREALEFS AILRQDRKIP RAEKIAYVDN VIDLLELNDM QDAIISSLGV
     EQRKRLTIGV ELAAKPSLLL FLDEPTSGLD SQSAYSIIRF LKKLTAAGQA IVCTIHQPSS
     VLIQEFDMVL ALNPGGNTFY FGPIGENGKD VIEYFGARGV KCPPEKNVAE FLLETAIKPR
     KRADGTKIDW NDEWANSKEA QAVIEEIDGL KRMRSKSVSE KQNDDDATEF AAPVWLQTTM
     LTKRVFTQYW RDPSYLYGKL FVAVIVGIFN GFTFWQLGNS IQDMQNRMFT AFLILTIPPT
     VVNAVVPKFY QNMALWMARE LPSRIYGWFA FSTAMVVAEI PIAVVSAVVY WLLWYFPSGL
     PTDSSTAGYV FFMVLLFFFF QASWGQWICA FAPSFTVISN VLPFFFVMFS LFNGVVRPYA
     SIPVFWRYWM YYVNPSTYWI SGVLAKTLDG IRVECTPSET ARFNVPGGQT CQSYAGAFAT
     SAGGYLLNPD ATADCQYCPY EYANGYLASL NIKASQAWRD LGIFCIFVVS NWALVYFFIY
     TVRIKGWSFG FGPLFGALGS MVGAIKKPFK SKKKE
//
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