ID M1W2J6_CLAP2 Unreviewed; 1542 AA.
AC M1W2J6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Probable ATP-binding multidrug cassette transport protein {ECO:0000313|EMBL:CCE31921.1};
GN ORFNames=CPUR_05777 {ECO:0000313|EMBL:CCE31921.1};
OS Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE31921.1, ECO:0000313|Proteomes:UP000016801};
RN [1] {ECO:0000313|EMBL:CCE31921.1, ECO:0000313|Proteomes:UP000016801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20.1 {ECO:0000313|EMBL:CCE31921.1,
RC ECO:0000313|Proteomes:UP000016801};
RX PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA Yoshida R., Zeng Z.;
RT "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT Clavicipitaceae reveals dynamics of alkaloid loci.";
RL PLoS Genet. 9:E1003323-E1003323(2013).
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:CCE31921.1}.
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DR EMBL; CAGA01000035; CCE31921.1; -; Genomic_DNA.
DR STRING; 1111077.M1W2J6; -.
DR VEuPathDB; FungiDB:CPUR_05777; -.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_0_1; -.
DR OrthoDB; 5473955at2759; -.
DR PhylomeDB; M1W2J6; -.
DR Proteomes; UP000016801; 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, ECO:0000313|EMBL:CCE31921.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000016801};
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 547..568
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 580..607
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 619..648
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 654..675
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 687..707
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 792..812
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1239..1258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1308..1341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1353..1375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1381..1401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1504..1524
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 192..443
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 902..1144
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1542 AA; 172105 MW; 03065DCEB6E2FFF6 CRC64;
MAAQDKIASA DDYRGSSSTA YSSIIPERDD TDSPSHSPPN NNSNGLQNTT GPDQRPDSSS
ASSSSSGSQV KQTQTREPIR RRRTIQTEDD LVQALSRRRT SRDDRTPEDE EESQEIKRLM
SKMFGQKRQE QSEEEQTRHS GVVFRNLTVK GVGLGAGLQP TVGDIFTSLP RSIANLFRSV
FRASSGTGDG KAAVKAAVSA KPPVRDLISD FNGCVRPGEL LLVLGRPGSG CSTFLKAFCN
QRSGFVAVDG QVTYGGTSAE DMAKNFRGDI IYNPEDDLHY ATLSVKRTLS FALQMRTPGK
ESRLDGESRE DYVREFLRVV TKLFWIEHTL GTKVGNEFVR GVSGGERKRV SIAEAMIARA
SVQGWDNSSK GLDASTALEY VRSIRTMTNM ADVSTAVSLY QAGESLYDLV DKVLLIDEGQ
CLYFGPAEQA KQYFQDLGFE CRERWTTPDF LTSVVDHHER NIREGCEDRI PRSARDFAAR
YRESDVCRAA LADMEDFEAS LKERIDERRA NQSKKTATKN YTLPFHKQVL ACTHRQFLVM
LGDKASLFGK WGGLLFQGLI VGSLFFNLPK TAAGAFPRGG TLFFLLLFNA LLALAEQTAA
FVAKPILLKH KSFSFYRPAA YAIAQTVCDV PMVFVQVFLF NVVIYFMANL SRTASQFFIC
TLILWMVTMV TYAFFRTISA WCKTLDLATR FTGISVQILV VYTGYLIPPS SMHPWFSWLR
WINWIQYGFE CLVANEFAGL DLECVPPYLV PQGPQASPQY QSCALKGSVS GQTSVDGSQY
IQESFTYSRS HLWRNFGFLW AFFFFFVALT ALGMELMKPN AGGGAITVFK RGQVPKKLEK
TIESGGHENA AGDEESGPAS HVTPGMAEES QDNEKGHTGG DGDGTKQGGD TMDQVAKNET
VFTFRDINYI IPYEQSERTL LKDVQGYVRP GKLTALMGAS GAGKTTLLNA LAQRLTFGTL
KGEFLVDGRP LPKSFQRATG FAEQMDVHEP TATVREALQF SALLRQPRET PRQEKLDYCE
TIIDLLEMRD IAGAVIGEIG QGLDSEQRKR LTIGVELASK PELLMFLDEP TSGLDSGAAF
NIVRFLRKLA DAGQAVLCTI HQPSAVLFEH FDELLLLKSG GRVVYHGPLG EDSRELIDYL
EGNGASKCPA DANPAEYMLN AIGAGDPNYN GPDWGDVWAG SKEHDKRSQE INEMIEKRKH
MEPSKSLKDD REYAASLSFQ TMTVVKRSFI SYWRTPEYIV GKFTLHILTG LFNCFTFWRL
GYSQTDFQNR LFSIFMTLTI SPPLIQQLQP VFLNSRNIFQ SRENNSKIYS WFAWTTAAVV
VEMPYAIVAG AIYFCCWWWG IFGTRVSSFT SGFALLLVLL FELYYVSFGQ AIASFAPNDL
LASLLVPIFF LFVVSFCGVV VPPQQLPTFW REWMYWLSPF HYLLEGFLGV AIHDQPVECA
PDELARFRAP PGLSCQEYTQ ATIDQAGGYV QQGADGMCEF CQYATGDEFG RGFSVYYDHI
WRDFGIFIGF IVFNYAVVYV STWLRFKGKN PLKSLLAKKR GG
//
