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Database: UniProt
Entry: A0A161YF86_9PEZI
LinkDB: A0A161YF86_9PEZI
Original site: A0A161YF86_9PEZI 
ID   A0A161YF86_9PEZI        Unreviewed;      1465 AA.
AC   A0A161YF86;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Multidrug resistance protein cdr1 {ECO:0000313|EMBL:KZL71217.1};
GN   ORFNames=CT0861_11666 {ECO:0000313|EMBL:KZL71217.1};
OS   Colletotrichum tofieldiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL71217.1, ECO:0000313|Proteomes:UP000076552};
RN   [1] {ECO:0000313|EMBL:KZL71217.1, ECO:0000313|Proteomes:UP000076552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0861 {ECO:0000313|EMBL:KZL71217.1,
RC   ECO:0000313|Proteomes:UP000076552};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KZL71217.1}.
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DR   EMBL; LFIV01000076; KZL71217.1; -; Genomic_DNA.
DR   STRING; 708197.A0A161YF86; -.
DR   OrthoDB; 5473955at2759; -.
DR   Proteomes; UP000076552; 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; ATP-BINDING CASSETTE TRANSPORTER; 1.
DR   PANTHER; PTHR19241:SF625; ATP-DEPENDENT PERMEASE PDR10-RELATED; 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; 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:UP000076552};
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        496..520
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        532..554
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        608..628
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        640..659
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        742..763
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1166..1185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1197..1216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1236..1266
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1286..1306
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1318..1343
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          137..387
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          829..1072
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   1465 AA;  165077 MW;  73BCAD21FC0762E2 CRC64;
     MVHLTEKISP KESDDTLRAK AIRRHDHQQD DMDIEANDPR VNDLVRPSTL ELVRSASRLD
     PDINPFLSSH PSLNPSCRDE FNAKKWARAL LQHSRHHPQH YPRLEAGVAY RNLSVHGYGT
     DTDYQKDVLN VLWQAPMMIK QFFSKRQQKM DILREFDGIV KSGELLLVLG RPGSGVSTLL
     KTIAGETQGL HLGSHSHFSY QGIPMETMHK RFRGEVIYQA ETDVHFPHLT VGQTLLFAAL
     ARTPKNRLPG VSRHRYAEHL RDVDMAVFGI SHTVNTKVGN DFVRGVSGGE RKRVSIAEVT
     LSQSPIQCWD NSTRGLDSAT ALEFARTLRL STDIARTTAI VAMYQASQPA YDVFDKVAVL
     YEGRQIYFGS TLLARQYFID MGYHCPERQT TADFLTSLTN PAERVVQPGF ENRVPRTPDE
     FAAAWKSSSP RGRLMDEIHA FEGDYPLNGA EVEKFVETRQ KHKASLLSHQ SPYTISMPMQ
     IWLCMTRGYQ RLLGDWLFFV VTVFGNLVIS LVLGSIFFDL PLDASTMNSR CVLLFFAILF
     NGLSSALEIL TLYAQRPIVE KHARYALYHP FSEAISSTIC DLPSKILSTL AFNVPIYFMA
     KLRQEADAFF IFLLFGFTTT LSMSMILRTI GQTSRTIHQA LTPAALFILS LIIYTGFILP
     TRDMKGWLRW INYINPIAYA FESLVANEFS GRQFPCLQYV PAYPDAAPNE RTCSVAGAAP
     GADFVDGDFY MNATYGYYKS HIWRNFGILI AYIVFFMGVY LLAAEYITTD RSKGEVLVFQ
     RGHLAPTKAK SLDEEAGLTD RVYQSSKNAG HEAQPDAKPK ASYEGRSVFH WKDVCYDITI
     KGKESRILNH VGGWVKPGTL TALMGSTGAG KTTLLDVLAN RVTMGVVSGD ILVNGIPRDQ
     SFQRKTGYVQ QQDIHLETST VREALQFSAM LRQPKSVSKQ EKYDNVEEVI KLLEMEAYAD
     AIVGVPGEGL NVEQRKRLTI GVELAAKPDL LLFLDEPTSG LDSQTAWSIL SLIKKLSENG
     QAILCTIHQP SALLFQQFDR LLLLAHGGNT VYFGDIGENS RTLTSYFEQY GAAPCEQDEN
     PAEWMLKVIG AAPGAKTDRN WSQTWTDSYE CAEARRELER LEQTSKNTGS VETQDELSTY
     AAPFHVQLEL CTRRVFQQYW RTPSYIYSKL FLSGGTSLFI GVSFYNSPLS LQGLQSQMFS
     IFMLLVVFAF LVYQTMPNFI LQREQYEARE RASRAYSWYV FVLVNIIVEL PWNTLAALVI
     FFPFYYLVGM YKNAIPTDAV TERGGLMFLL IWAFMLFEST FADMVVAGVP TAEIGATLSL
     LLFTLCLIFC GVIVPSNALP GFWKFMYRVS PLTYLVDGLL STGLAHNQVR CSDLELLQFN
     PTNGTTCGDY MAPYMQMAGG SVYNSNNTDT CQFCPLVTTD IFLGTVSSSY DQRWRSYGLM
     WVYIVFNILR PCRCTGWLEC QRILH
//
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