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Database: UniProt
Entry: A0A2G5HJ15_CERBT
LinkDB: A0A2G5HJ15_CERBT
Original site: A0A2G5HJ15_CERBT 
ID   A0A2G5HJ15_CERBT        Unreviewed;      1429 AA.
AC   A0A2G5HJ15;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   13-SEP-2023, entry version 21.
DE   SubName: Full=ABC transporter G family member 19 {ECO:0000313|EMBL:PIA92556.1};
GN   ORFNames=CB0940_04099 {ECO:0000313|EMBL:PIA92556.1};
OS   Cercospora beticola (Sugarbeet leaf spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX   NCBI_TaxID=122368 {ECO:0000313|EMBL:PIA92556.1, ECO:0000313|Proteomes:UP000230605};
RN   [1] {ECO:0000313|EMBL:PIA92556.1, ECO:0000313|Proteomes:UP000230605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=09-40 {ECO:0000313|EMBL:PIA92556.1,
RC   ECO:0000313|Proteomes:UP000230605};
RA   De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA   Thomma B.P., Van De Peer Y., Bolton M.D.;
RT   "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT   several fungal lineages and shown to be expanded in Cercospora beticola
RT   based on microsynteny with recipient genomes.";
RL   Submitted (OCT-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:PIA92556.1}.
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DR   EMBL; LKMD01000105; PIA92556.1; -; Genomic_DNA.
DR   OrthoDB; 5473955at2759; -.
DR   Proteomes; UP000230605; Chromosome 4.
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:SF639; ABC MULTIDRUG TRANSPORTER (EUROFUNG)-RELATED; 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   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        537..568
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        580..601
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        613..630
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        715..736
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1136..1154
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1160..1181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1202..1233
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1245..1268
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1280..1298
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1400..1418
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          107..359
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          799..1042
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          765..787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1429 AA;  159375 MW;  5E3C71264C15C5E4 CRC64;
     MPSLQRSGSW TTPGPGSGSG EEVYRTLSNA ISRTFSGKKS EYEDPMESDE SISKAKDWKL
     MEEVKAVAQQ TQADGGKARK LGVTWKDLTV KGIGADAAFN ENAISQFNIP RLIKESRQKP
     PLKTIIDDSH GCVKPGEMLL VLGRPGAGCT SLLKMLANKR LGYAEVTGDV KFGSMDAKEA
     EQYRGQIVMN TEEELFFPTL TVGQTMDFAT RMKIPNHLPS NVKTTEEFQQ ITRDFFLRSM
     GIEHTHETKV GNEYVRGVSG GERKRVSIIE TMASRGSVFC WDNSTRGLDA STALEYTRCI
     RAMTDVMGLS SIVTLYQAGN GIYELFDKVL VLDEGKQIFY GPMAQAKPFM EDLGFQYTEG
     ANVADYLTGV TVPTERKIRP GFEDRFPRTA DEIRAEYERT SIKFLMEKEY DYPTTSDAIS
     NTADFKEGVQ HDKAPSLPKK SPLTVDLYTQ TKAAVIRQYQ LIWGDKATFV IKQGSTIVQA
     LIAGSLFYDS PNTSGGLFSK GGAIFFSLLY MSLIAMSEVT DSFAARPVLA KHRSFAFYHP
     AAFCFAQIAA DIPIIFFQVT VFALPLYFMV GLKETAGAFF SYWVILFASA ICMTAFFRWL
     GAAFETFDDA SKVSGFAVSA LIMYAGYLIA KPDMHPWFVW IYWINPLAYG FEALFGVEFK
     DTIIPCTGPN LVPLGPNYTD SSFQACTGVR GAEVGAAFVT GEQYLEGLSY SSSRIWRNFG
     IIWAWWVLFV ACTVYCTSRW SMASGNSGFL VIPREKQKAA MHLVSDEENL PEKTRARDAE
     KSSQDGNVED QLIRNTSVFT WKNLTYTVQT PSGPRVLLDD VQGWVKPGML GALMGSSGAG
     KTTLLDVLAQ RKTEGTIKGS ILVDGRELPI SFQRSAGYCE QLDIHEPLAT VREALEFSAL
     LRQSRETPRE EKLKYVDTII DLLEMHDIEN TIIGTSRAGL SVEQRKRLTI GVELVSKPSI
     LIFLDEPTSG LDGQAAFNIV RFLRKLADVG QAVLVTIHQP SAALFAQFDT LLLLAKGGKT
     VYFGDIGDNG ATIKEYFGRY DAPCPPNANP AEHMIDVVSG TLSKGKDWNQ VWLNSPEYKN
     MTTELDHIIQ DAASKPPGTV DDGHEFAMPI WDQMKLVTQR MNTALFRNNE YTNNKFALHI
     GSALFNGFTF WQIGDSVTDL QLALFTIFNF VFVAPGVMAQ LQPLFLERRD IYEAREKKSK
     MYHWSAFVTG LIVSEIPYLI ICAILYYVCW YYTVGFPGDS NKAGAVFFVM LMYEFIYTGI
     GQFVAAYAPN AVFAALTNPL IIGVLVSFCG VLLPYSQIQP FWRYWMYYLN PFNYLMGSML
     VFTLFDAEVQ CNEDQFAVFD TPNGETCASY LSEYLQGPGS RTNLVNPDDT SGCRVCQYGR
     GSDYLHTLNL NDYYYGWRDA GIVALFAFSS YALVYVLMKL RTKQSKKAE
//
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