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Database: UniProt
Entry: G3JS91_CORMM
LinkDB: G3JS91_CORMM
Original site: G3JS91_CORMM 
ID   G3JS91_CORMM            Unreviewed;      1522 AA.
AC   G3JS91;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=ABC drug exporter AtrF {ECO:0000313|EMBL:EGX88790.1};
GN   ORFNames=CCM_08836 {ECO:0000313|EMBL:EGX88790.1};
OS   Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX   NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX88790.1, ECO:0000313|Proteomes:UP000001610};
RN   [1] {ECO:0000313|EMBL:EGX88790.1, ECO:0000313|Proteomes:UP000001610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM01 {ECO:0000313|EMBL:EGX88790.1,
RC   ECO:0000313|Proteomes:UP000001610};
RX   PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA   Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA   Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT   "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT   valued traditional Chinese medicine.";
RL   Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
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; JH126405; EGX88790.1; -; Genomic_DNA.
DR   RefSeq; XP_006674035.1; XM_006673972.1.
DR   GeneID; 18170841; -.
DR   KEGG; cmt:CCM_08836; -.
DR   VEuPathDB; FungiDB:CCM_08836; -.
DR   eggNOG; KOG0065; Eukaryota.
DR   HOGENOM; CLU_000604_35_0_1; -.
DR   InParanoid; G3JS91; -.
DR   OMA; FCISNWA; -.
DR   OrthoDB; 5473955at2759; -.
DR   Proteomes; UP000001610; 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:UP000001610};
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        548..569
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        581..603
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        624..646
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        658..677
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        689..708
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        800..833
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1217..1238
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1250..1269
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1289..1317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1329..1348
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1360..1382
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1485..1506
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          191..435
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          885..1123
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          1..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          844..866
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..125
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        844..862
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1522 AA;  168910 MW;  13E22A362C72C560 CRC64;
     MAAEEQQTVP TTATAGATDA VTTANPITTT TSADTSSSNA SFEGYWGDAD AGGPVRRESA
     RQGYNDLQRE LSRHASNTSG VSKAKSHTAA GRSGGLLSAL RKRPSRAPDV EADSQATKHH
     DDDFQLDEFM RQGHLEKRHP ESGESTKKVG VVFKNLTVQG AAMSAMTVRT LPQAILGTFG
     PDLYGHLTKL IPALNFGKGS GPEIRDLIHD FTGVVRPGEM MLVLGRPGAG CTTFLKAIAN
     NRQGYVAVTG DVRYGGIDAA EMDRRYRGEV VYNPENDRHL PSLTVGQTLE FSLRTKTKKA
     DSGRIGLIVD AFLQMFAIAH TKNTNVGDEY TRGVSGGERK RVSIAETLAT KSTVTCWDNS
     TRGLDASTAL NYARSLRVMT DVSDRTTLTT LYQAGEGIYE LMDKVLVLDQ GRMLYQGPAT
     EARQYFVDLG FFAPPRQTTA DFLTSVCDVN ARRFRDGWAD RCPKTPVELE AAFRASAAYK
     SVLADVADYE RHLAATSHVD AETFQQSVQE AKSRTVLQRS NYTVSYWRQV LACTRREFWL
     LWGDKQTLYT KFGIIISMGL IVGSLFYDIP SDTSGLFLRG GAAFFSILFL GWLQLSELIR
     AIAGRDVIER HKEYAFYRPS AVNFARILAD FPLLFVEVVV FGVILYFMCN FDLDAGKFFI
     YLLYIYTTTI CITALYRMFA ALSPSIDDAV RFSGITFNLL LIFTGYAISK PTLISKKIWF
     GWFYYINPVS YAFEGVISNE LSSRNMQCAP SQLVPQGPNI LPENQGCAVP GSAAGAATVN
     GADYLSANYD YHRSNLWRNW AVLIAFSVLY ILVTVLATET ISFATSGMGI LVFKKSKAGA
     AAAKKTKEGD EESGKKEAQG SDNLRRQITT PDEILQEFQR SEKIFTWENV NYTVPSADGP
     KKLLNNVQGY AKPGVMVALM GASGAGKTTL LNTLSQRQTV GVVEGSMLVD GTALPTDFQR
     GTGFVEQMDL HEESTTVREA LEFSALLRQS KETPRADKIA YVDKIIDLLE MQPLEDAIVF
     SLGVEQKKRL TIGVELAAKP SLLLFLDEPT SGLDSQSAFS IIRFLRKLCA AGQAIICTIH
     QPSSELIEQF DQILALNPGG NVFYFGPVGE NGSAVVDYFA ARGSQCPDGK NVAEFLIEQG
     AKPAGRAFWN EQWLQSDQNK TLTEEIARIK RDRSAAAAQL QHASGGAARQ DEFAASVYEQ
     TTLLTKRMFI KQWRQPSYVY GKFFVAVLIG IFNGFTFWQL GNTVEDMQSR MFTSFLVLLF
     LPATMNAVLP KFFMDRALWE AREYPSRIYG WVAFCSASIL SEIPSAVISA VLYWILWYYP
     TGLPTDSSTA GYVFLMTLLF FLFQTSWAQW ICAFAPSFTV ISNVLPFFLV MFSVFNGVFV
     PYEQLAVFWR YWMYYVNPST YFVGGVLSST LAHQQVRCAD SEAAHFTPPS GKTCAEFAGD
     FVVKAGRGYL IDPNATDMCG YCPYADGTQY LASLHIEPSQ KWRDFGIFLA FCISNWALVY
     FFIYTVRVRR WSFGFNYLFK WF
//
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