ID F9XII5_ZYMTI Unreviewed; 1481 AA.
AC F9XII5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=ABC transporter {ECO:0000313|EMBL:EGP85077.1};
GN Name=Atr6 {ECO:0000313|EMBL:EGP85077.1};
GN ORFNames=MYCGRDRAFT_74970 {ECO:0000313|EMBL:EGP85077.1};
OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS fungus) (Septoria tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP85077.1, ECO:0000313|Proteomes:UP000008062};
RN [1] {ECO:0000313|EMBL:EGP85077.1, ECO:0000313|Proteomes:UP000008062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT reveals dispensome structure, chromosome plasticity, and stealth
RT pathogenesis.";
RL PLoS Genet. 7:E1002070-E1002070(2011).
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; CM001203; EGP85077.1; -; Genomic_DNA.
DR RefSeq; XP_003850101.1; XM_003850053.1.
DR EnsemblFungi; Mycgr3T74970; Mycgr3P74970; Mycgr3G74970.
DR GeneID; 13394735; -.
DR KEGG; ztr:MYCGRDRAFT_74970; -.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_0_1; -.
DR InParanoid; F9XII5; -.
DR OMA; YQVGFHL; -.
DR OrthoDB; 5473955at2759; -.
DR Proteomes; UP000008062; Chromosome 8.
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:SF685; ABC MULTIDRUG TRANSPORTER (EUROFUNG); 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:UP000008062};
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 528..551
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 563..582
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 603..629
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 641..658
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 670..691
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 697..716
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 780..801
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1195..1212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1219..1240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1274..1291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1303..1323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1329..1351
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1455..1476
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 170..418
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 854..1097
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1481 AA; 164957 MW; 27240A2E4C07B372 CRC64;
MTQPSNGIAR EQPDGFAKEA VEDTHTGYST ANASSRQSLD TPPGHGVNVG RAEREFHELQ
RTLSGLSQAD RRLSRVQSQR SQKSEKQNAT QDIEKAGSAS PASSEDEPFD LEETLRHNKR
MEDESGIKQK QIGVVWDKLS VSGMGGAKIF QPTFPDAFTG FFGFPIRAAM GLLGLGKKGE
EVKILNNFRG VVKPGEMVLV LGRPGSGCTS FLKVIANQRY GYTSVDGEVS YGPFTSEEFD
KRYRGESVYL QEDDVHHPTL TVGQTLGFAL ETKVPGKRPG GVTAAEFKEK VVDMLLRMFN
IEHTKNTIVG NPFVRGISGG ERKRVSIAEL MITGGSVYSH DNSTRGLDAS TALDYAKSLR
VLSNIYRTST FVSLYQASES IYAQFDKVLL IHEGHQIYFG PAKEARAYFE SLGYLPKPRQ
TSPDYLTGIT DDFEREYQEG RDSSNTPSTP QELVEAFEKS KYATQLNSEM DTWRQRVTEE
KQVYNDFQTA VREGKRRAPA KSVYSIPLYM QIWALMKRQF ILKWNDKFSL VTSYITSIVI
AILLGTVWLQ LPQTSSGAFT RGGLLFISLL FNAFQAFGEL ASTMIGRPIV NKHRAYAFHR
PGALWIAQIG VDIAFASVQI MVFSIMVYFM CGLVLDAGAF FTFYLVIVSG YLAITLFFRT
IGTVSQDFDY AIKFAATIIT LYVLTSGYLI QYMSQQVWLR WIFYINPVGL GFAALMENEF
SRLDIQCEGA SLIPYGPGYG DIQHQVCTLP GSQAGNPTVS GSAYIDTAFQ YADGLLWRNW
GIIIVLITAF LISNVTLGEW IKWGAGGKTV TFYAKEDNER KQLNDALREK KSKRTKKDGD
QGGSELSVES KAILTWEDLC YDVPVPSGQL RLLKNIYGYV KPGQLTALMG ASGAGKTTLL
DVLASRKNIG VISGDKLVDG APPGTAFQRG TSYAEQLDVH EGSATVREAL RFSAVLRQPF
EVPQEEKYAY VEEIIALLEM EDIADAIIGS PEAGLAVEQR KRVTIGVELA AKPELLLFLD
EPTSGLDSQS AFNIVRFLRK LAAAGQAILC TIHQPNSALF ENFDRLLLLQ RGGETVYFGD
IGKDANVLLS YFKKYGAHCP PTANPAEWML DAIGAGQAAR IGDKDWGEIW RDSEELSAIK
SDIVRMKEER IKEVGSQPQV AQKEFATPLW HQIKTVQART HKAFWRSPNY GFTRLFNHVI
IALLTGLMFL RLGDSRTSLQ YRVFIIFQVT VLPALILAQV EPKYDLSRLI YYREAASKTY
KQLPFALSMV VAEIPYSILC AVAFFLPLYY IPGFQSPSSR AGYNFLMVLV TEFFSVTLGQ
TISALTPSTF IAVLLNPFII IVFALLCGVT IPKPQIPGFW RAWLYELNPL TRLISGLVSN
ELHDRVVNCQ PFEFNTFTAP EGQTCGEYMS DFFAMGGPGY IADNSTSNCQ YCAYRIGDQF
YEPLGISFST RWRDFGILTA FIGSNLILLF IGSRYLNFNR R
//
