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Database: UniProt
Entry: A0A0D0C079_9AGAR
LinkDB: A0A0D0C079_9AGAR
Original site: A0A0D0C079_9AGAR 
ID   A0A0D0C079_9AGAR        Unreviewed;      1468 AA.
AC   A0A0D0C079;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=ABC transporter domain-containing protein {ECO:0000259|PROSITE:PS50893};
GN   ORFNames=GYMLUDRAFT_248509 {ECO:0000313|EMBL:KIK55699.1};
OS   Collybiopsis luxurians FD-317 M1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis;
OC   Collybiopsis luxurians.
OX   NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK55699.1, ECO:0000313|Proteomes:UP000053593};
RN   [1] {ECO:0000313|EMBL:KIK55699.1, ECO:0000313|Proteomes:UP000053593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK55699.1,
RC   ECO:0000313|Proteomes:UP000053593};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (APR-2014) 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}.
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DR   EMBL; KN834804; KIK55699.1; -; Genomic_DNA.
DR   HOGENOM; CLU_000604_35_0_1; -.
DR   OrthoDB; 5473955at2759; -.
DR   Proteomes; UP000053593; 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:SF498; ABC TRANSPORTER PROTEIN; 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; 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:UP000053593};
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        492..515
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        527..548
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        569..592
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        604..625
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        637..657
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        745..765
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1166..1187
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1199..1216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1236..1267
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1287..1309
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1321..1345
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1440..1458
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          128..382
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          824..1067
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1468 AA;  164238 MW;  CDB98A35D1AFE9C3 CRC64;
     MTDGKWPLGH SDASSNSQAD AVTLEGSQVE HVTQLARTVT KMSIGSGKAQ ETGTIDGQNP
     FIGTEHDSLN PLSGRFDYTK WIRSVLAITS RDPERYPTRT AGIVFTNLNV YGYGSAADHQ
     KTVGNILLDI PSMIAGLFGK KGRRVGILRD FEGLVKQGEM LVVLGPPGSG CTTLLKTLSG
     ETHGLYIGDD VKINYQGIPW ETMHKDFRGE VVYNAETEVH FPNLTVGQTL SFAARARTPR
     TRLPGVTREQ WAEHMKDVVM AIFGLSHTVN TKVGNDFIRG VSGGERKRVS LAEVVLAGSP
     LQCWDNSTRG LDSATALEFI KNVNISAKYM GSTAIIAVYQ ASQSIYDMFD KVTVLYEGRQ
     IYFGPTEDAK KFFVDMGFHC PDRQSTADFL TSLTNPAERR ARPGYESRVP RTSDEFARVW
     KESSDRKRLL QEIEQFNQEF PIGGTQLDKF RTSRKSVQAK GLGSKSPYTI SVPMQIKLCL
     SRGFQRLQGD MSLFFTTVLG NFFFSLIISS IFYNLPSNTG SFYSRGALLF WATLMNALSS
     VLEILTLYEQ RPIVEKHSRM AFYHPFSEAV SAMICDLPAK IITAITFNVT LYFMTNLRRT
     PAHFFIFLLF SFSCTLTMSM IFRTIGASSR TIAQAMAPAA IIMLALMIYT GFTIPIADMH
     PWFRWINYIN PIAYAFESLM VNEFNAREFP CVSFIPRGPG YTNVTGTEHI CATTGAQAGS
     SIVEGTAYLA VTFHYFKSHL WRNLGIIWGS TVFFLSTCLI ATEYITAAKS KGEVLVFRRG
     HVPEGTNLNK TNDEESARPV KDRIEEKPKG VEDVAGLQKQ TSIFHWEDVC YDIKIKGAPR
     RLLDNVDGWV EPGTLTALMG ASGAGKTTLL DVLASRVTMG VVTGSMFVDG HQRDESFQRK
     TGYVQQQDLH LQTSTVREAL IFSARLRQPR DVPDEEKVVY CSEIIRLLGM EKYADAVVGV
     PGEGLNVEQR KRLTIGVELA AKPKLLLFLD EPTSGLDSQT AWSICTLLRD LANNGQAILC
     TIHQPSSLLF QGFDRLLFLA SGGRTVYFGD IGENSKTLTS YFERQGASPC PPDANPAEWM
     LQVIGAAPGA VAERDYAEAW RQSDEYIAMK KELVRKRELA QIRPQPTAEE KRRSSDYSEF
     AAPFSHQFRL CLYRVFQQLY RTPSYIWSKT FLSITTALFI GFTFYRADNT LQGLQNQRFS
     VFMLMTIFGN LVYQIMPHFV TQRSLYEVRE RPSKVYSWLA FMLANICAEL PWNTLMSVLI
     FFCWYYPIGL YRNAVPTDAV TERGGLLFLL LWSFLMFTST FTHMVIAAVE VAENGGTIAQ
     LLFCLCLLFC GVLVSPSNLP GFWIFMYRVS PFTYLVDAML SVSLANAPAF CSSVEVSLFD
     PPTGQTCGEY LQAYISFAGG LISNPNATSQ CEFCSITNTN AFLAGVDSFY SNRWRNFGLM
     WAYILFNVFA ALGFYWLGRV PKNMKKEN
//
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