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Database: UniProt
Entry: A0A179F477_METCM
LinkDB: A0A179F477_METCM
Original site: A0A179F477_METCM 
ID   A0A179F477_METCM        Unreviewed;      1514 AA.
AC   A0A179F477;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=ABC transporter {ECO:0000313|EMBL:OAQ60227.1};
GN   ORFNames=VFPPC_10655 {ECO:0000313|EMBL:OAQ60227.1};
OS   Pochonia chlamydosporia 170.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX   NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ60227.1, ECO:0000313|Proteomes:UP000078397};
RN   [1] {ECO:0000313|EMBL:OAQ60227.1, ECO:0000313|Proteomes:UP000078397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=170 {ECO:0000313|EMBL:OAQ60227.1};
RX   PubMed=27416025;
RA   Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT   "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT   Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT   genome mining.";
RL   PLoS Pathog. 12:E1005685-E1005685(2016).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAQ60227.1}.
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DR   EMBL; LSBJ02000009; OAQ60227.1; -; Genomic_DNA.
DR   RefSeq; XP_018138137.1; XM_018288984.1.
DR   STRING; 1380566.A0A179F477; -.
DR   GeneID; 28852978; -.
DR   KEGG; pchm:VFPPC_10655; -.
DR   OrthoDB; 5473955at2759; -.
DR   Proteomes; UP000078397; 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:UP000078397};
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        545..567
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        573..592
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        624..643
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        655..674
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        686..706
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        793..815
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1209..1230
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1242..1261
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1281..1311
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1323..1344
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1356..1374
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1477..1498
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          190..432
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          881..1119
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          1..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..117
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1514 AA;  168774 MW;  9FF09F29807AC36B CRC64;
     MPDNGHELAE SKLPTTHDNS TANVNNETDV QLSDDTSNED GYWGDTYADG PVSQRAAREG
     FKELQHELSR RSTNASAAQK KKSSGGIVGR IFSNQSRQVD PEKQASPDAD EADSERTAHA
     DGFELEQFIR EGHLEKRNPQ NGESTKKVGV LFKNLTVKGV GVSATSVRTL PQAIAGTFGP
     DLYNFVSSWI PALNFRSPGK PRDLIRDFTG VVRPGEMMLV LGRPGAGCST FLKVVANNRG
     SYQAVEGDVV YGGITSSKMG KRFRGEAVYN AEDDQHMPSL TVGQTLKFSL LTKTKKNERS
     NIDVIVDSFL KMFAMSHTKD TLVGDAFTRG VSGGERKRVS IAETLATKST VTCWDNSTRG
     LDASTAYNYA KSLRIMTDVS DRTTLTTLYQ AGEGIYDLMD KVLVIDEGRM LYQGPASEAK
     QYFVDLGFYC PPRQTTADFL TSVCDVNARQ FREGFEDRCP KTAEELEKAF RESHAYQVVL
     DDVASFEKHI TDTGHSDAQT FVDSVRGAKS KTVLKQSVYT VSLWKQVLAC TRREFWLIWG
     DKTSLYTKFF VIISNGLIVG SLFYNTPTNT SGAFLRGGVA FFSILFLGWL QLSELMKAVS
     GRAIISRHSE YAFYRPSAVS LARVLADLPM LIVEVIIFGL IMYFMTGLDL SAGKFFIYLL
     FVYVTTICLT ALYRMFAAVS PTMDDAVRFS GIALNLLIVY TGYTLAKPIL LNQKIWFGWL
     YYVNPISYAF EAVLTNEFAG RTMECAPSQL VPQGPGILPE NQGCAIAGSH PGSPQVPGSE
     YLSSQFEYSR SHLWRNFGIL LAFTVGYIGL TVLATEKFSF AGSGMGALVF KSAKKPKQVA
     KAQNKTDEEH TQPDELTAAA IARQRTPDEV LEAFNRSEQI FTWENISYTV PTPQGPKKLL
     NDINGYAKPG VLVALMGASG AGKTTLLNTL SQRQTVGVVE GNMLVDGSAL ASDFQRRTGF
     VEQMDLHEGS ATVREALEFS ALLRQSRDVP REEKLEYVDK VIDLLELNEI QDAVVASLGV
     EPRKRLTIGV ELAAKPSLLL FLDEPTSGLD SQAAYSIVRF LRKLCASGQA IVCTIHQPSS
     ELIEQFDKIL ALNPGGNIFY FGPVGHNGQA VVDYFDARGA HCPEGKNIAE FLIETGARAD
     AREHWNEQWR QSDENKALIA DIQKIKQQRL QEASSSTEEV LSHEFAAPVS EQIKLLSKRM
     FINQWRQPSY IYGKFFTAVI VGIFNGFTFW KLGDTVNDMQ SRMFTSFLIL LIPPTVLNAI
     LPKFYMDRAL WEAREYPSRI YGWVAFCTSS ILSEIPGSLL AGVIYWALWY WPTGLPTDSL
     TSGYVFLMTV LFFLFQSSWG QWICAWAPSF TVISNVLPFF LVMFSLFNGV VVPYEQLNVF
     WRYWLYYLNP STYWISGVLA TTLAHQPVKC ASNEAAYFNP PSGKTCSEFA MDFVKRAGQD
     YLVNPNDTEN CSYCPYASGA EYLAGLNIEP SQKWRDLGIF IAFCISNWML VYFFIYTVRV
     RRWNFGMGYI FKFL
//
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