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Database: UniProt
Entry: A0A166PLR6_9PEZI
LinkDB: A0A166PLR6_9PEZI
Original site: A0A166PLR6_9PEZI 
ID   A0A166PLR6_9PEZI        Unreviewed;      1492 AA.
AC   A0A166PLR6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=BMR1-like protein (ABC-2 type transporter) {ECO:0000313|EMBL:KZL66916.1};
GN   ORFNames=CT0861_01539 {ECO:0000313|EMBL:KZL66916.1};
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:KZL66916.1, ECO:0000313|Proteomes:UP000076552};
RN   [1] {ECO:0000313|EMBL:KZL66916.1, ECO:0000313|Proteomes:UP000076552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0861 {ECO:0000313|EMBL:KZL66916.1,
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:KZL66916.1}.
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DR   EMBL; LFIV01000159; KZL66916.1; -; Genomic_DNA.
DR   STRING; 708197.A0A166PLR6; -.
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; 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:SF685; 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   Coiled coil {ECO:0000256|SAM:Coils};
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        540..563
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        575..596
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        616..642
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        649..670
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        682..703
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        792..813
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1206..1223
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1235..1255
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1276..1301
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1313..1334
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1346..1364
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1466..1487
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          183..430
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          865..1107
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          475..502
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        104..120
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1492 AA;  165916 MW;  42885D68A8F89780 CRC64;
     MADQDFEKTQ EAVAGGSPAV NEKNTAEAHP APRSSTSTAA DDSENQREEA RRNNPDGFTA
     IHAGVSVHQA EAEFAELQRE LSGMSRASRV NSRNSRSKSE DVEKAVANVN SASPSSDTEG
     EQFDLEAVLR GGVEAERQAG IKPKHIGVYW DGLTVKGMGG TTNYVQTFPD AFVNFVDYVT
     PVMNLLGLNK KGVEATLLDS FKGVCKPGEM VLVLGKPGSG CSTFLKTIAN WRGGYTSVTG
     EVLYGPFTAE EFQQYRGEAV YNQEDDIHHS TLTVEQTLGF ALDTKVPAKR PAGLSKNEFK
     KQVISTLLKM FNIEHTRHTV VGDAFVRGVS GGERKRVSIA EMMISNACVL SWDNSTRGLD
     ASTALDFVKS LRVQTNLYQT STFVSLYQAS ENIYNHFDKV MVIDAGKQVY LGPAKEARAY
     FEGLGFAPRP RQTTPDYVTG CTDEFEREYA AGRSPENAPH SPETLAEAFQ TSKFKKQLDS
     EMEEYKARLV QETEKHEDFQ VAVHEAKRGS SKKSVYAVGF HLQVWALMKR QFVLKLQDRL
     SLFLSWVRSI VIAIVLGTLF FRLGSTSASA FSKGGLMFIS LLFNAFQAFS ELAGTMTGRA
     IVNKHKAYAF HRPSALWIAQ IIVDQAFAAT QILVFSIIVY FMSGLVRDAG AFFTFYLMIL
     SGNIAMTLFF RIIGCISPDF DYAIKFAVVL ITFFVVTSGY LIQYQSEHKW IRWIYWVNAL
     GLAFSAMMEN EFSRLSLTCS DESLIPSGPG YGDINHQVCT LAGSQPGTTL VDGSAYIAAG
     FNYFKGDLWR NWGIIFALIV FFLIMNVTLG ELINFGNNGN SAKVYQKPNE ERKRLNEALI
     EKRAGKRRGD KQEGSDLTIK SEAVLTWENL NYDVPVPGGT RRLLNDVFGY VKPGQLTALM
     GASGAGKTTL LDVLAARKNI GVIHGDVLVD GIKPGKQFQR STSYAEQLDL HDPTQTVREA
     LRFSALLRQP YETPIPERFS YVEEIIALLE MEHIADCIIG SPEFGLTVEQ RKRVTIGVEL
     AAKPELLLFL DEPTSGLDSQ SAFNIVRFLK KLAAAGQAIL CTIHQPNAAL FENFDRLLLL
     QRGGRTVYFG DIGQDAVVLR DYLKRHGAIA KPTDNVAEYM LEAIGAGSAP RVGNKDWADI
     WNDSAELANV KDTISQLKEQ RMAAGRTTNH DLEREYASPQ WHQLKVVVKR MNLSFWRSPN
     YLFTRLFNHV VVALITGLTY LNLDQSRSSL QYKVFVMFQV TVLPALIISQ VEVMFHIKRA
     LFFRESSSKM YNPLTFAAAI TIAELPYSIM CAVAFFLPLY YMPGFQSDSS RAGYQFFMVL
     ITELFSVSLG QALASLTPSP FISSQFDPFI MITFALFCGV TIPAPQMPGF WRAWLYQLDP
     FTRLIGGMVV TALHDLKVAC TKAEFNPFTA PQGQTCGEYM QPFFNNGGPG YLANNDTSSC
     EYCAYKVGDE FYQPLGLEFS NRWRDLGIFA AFVGSNVIIL FMASKFLNFN RR
//
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