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Database: UniProt
Entry: T0L604_COLGC
LinkDB: T0L604_COLGC
Original site: T0L604_COLGC 
ID   T0L604_COLGC            Unreviewed;      1482 AA.
AC   T0L604;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=ABC transporter domain-containing protein {ECO:0000259|PROSITE:PS50893};
GN   ORFNames=CGLO_17605 {ECO:0000313|EMBL:EQB43715.1};
OS   Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS   (Glomerella cingulata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum gloeosporioides species complex.
OX   NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB43715.1, ECO:0000313|Proteomes:UP000015530};
RN   [1] {ECO:0000313|Proteomes:UP000015530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX   PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA   Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA   Thon M., Fluhr R., Prusky D.;
RT   "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT   gloeosporioides as revealed by transcriptome analysis.";
RL   Mol. Plant Microbe Interact. 26:1345-1358(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:EQB43715.1}.
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DR   EMBL; AMYD01004189; EQB43715.1; -; Genomic_DNA.
DR   STRING; 1237896.T0L604; -.
DR   eggNOG; KOG0065; Eukaryota.
DR   HOGENOM; CLU_000604_35_0_1; -.
DR   OMA; IFCGVMA; -.
DR   OrthoDB; 5473955at2759; -.
DR   Proteomes; UP000015530; 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:UP000015530};
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        502..525
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        537..559
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        613..633
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        645..664
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        747..768
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1173..1192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1204..1223
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1243..1273
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1293..1313
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1325..1350
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1444..1465
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          142..392
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          836..1079
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          65..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1482 AA;  166591 MW;  489417A52CB0BFC1 CRC64;
     MDQHLASPRM DVRSASSNDT LREKTIQEQH HQSDETDLEV SDDGVNELVR GYSLELVRTS
     TRPNSSFVNP FLSKDPSLDP NSREHFNAKK WTRSLLQHSD RDPEQFPRLE AGVAWRNLSV
     HGFGTDTDYQ KDVLNVLLQG PMMIKQFFSN RRQKINILRE FDGIVKSGEM LLVLGRPGSG
     VSTLLKTIAG ETNGLHLESH SHLSYQGIPM ETMHKAFRGE VIYQAETDIH FPHMTVGQTL
     LFAALARTPK NRLPGVSRQR YAEHLRDVVM AVFGISHTIN TKVGNDFVRG VSGGERKRVS
     IAEVTLSQSP IQCWDNSTRG LDSATALEFA KTLRLSTNVA KTSAVVAMYQ ASQPAYDVFD
     KVSVLYQGRQ IYFGPTEHAK HYFVEMGYAC PDRQTTADFL TSLTNPAERV VRPGFENRVP
     RSPDEFVTVW KGSQLRARLM EEIHSFEEQY PMDGSGVNKF SEVRKAHKQS LTSSRSPYTI
     SVPMQIWLCM TRGYQRLSGD KLFFFVTVLG NLVISLVLGS IFFDLPADAS SMNSRCILIF
     FAILFNGLSS ALEILTLYVQ RPIVEKHARY ALYHPFSEAI SSTICDLPSK ILSTLAFNIP
     LYFMAKLRQE ADAFFIFLLF GFTTTLSMSM ILRTIGQTSR TIHQALTPAA IFILALVIYT
     GFILPTSSMK GWLRWINYIN PIAYAFESLV ANEFTGRQFP CADYVPAYPN ATPSQRACAV
     AGAMPGADFV DGDFYMNAHF SYYKSHMWRN FGILIGYIIF FLTVYLVAAE FITTNRSKGE
     VLLFRKGHKS TSPSKAVSDE ETGRSDRVYR NEKEVVSSPR HPATRQPTRQ QNQAVFHWKD
     VCYDITIKGE DRRILSHVAG WVKPGTLTAL MGSTGAGKTT LLDVLANRVT MGVVSGDMLV
     NGIPRDQSFQ RKTGYVQQQD IHLETSTVRE ALQFSAMLRQ PASISKQEKY AYVEEVIELL
     EMEAYADAIV GVPGEGLNVE QRKRLTIGVE LAAKPDLLLF LDEPTSGLDS QTAWSIASLI
     RKLSENGQAI LCTIHQPSAL LFQQFDRLLL LAHGGRTVYF GDIGENSRTL TGYFEQYGAA
     PCGPDENPAE WMLKVIGAAP GAKAERDWHQ TWKDSDESIQ VQRELARLEK ESPASGSLGT
     SEEMSTYATP FSTQLAMCTT RVFQQYWRTP SYIYSKLILS GGTSLFIGVS FYKAELTMQG
     LQSQMFSIFM LLVVFAFLVY QTMPNFILQR EQYEARERAS RAYSWYVFML VNIIVELPWN
     TLAAIVIFFP FYYLVGMYRN TIPTDAVTER GGLMFLLVWA FMLFESTFAD MVVAGVPTAE
     IGATLSLLLF AMCLIFCGVI VPMGSLPTFW KFMYRVSPLT YLVDGLLSTG LAHNAVQCSP
     LELLQFSPPA NVTCGAYMET YMQVAGGRVY NPESTDSCQF CSLADTDMFL AMTSASYDER
     WRNYGLMFVY IVFNLFAALG LYWLARVPKK FSLSQLWKKK TA
//
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