ID   FER6_ZYMTI              Reviewed;        1353 AA.
AC   F9X9V4;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=ABC-type transporter MYCGRDRAFT_41235 {ECO:0000303|PubMed:28818040};
DE   AltName: Full=ATP-binding cassette sub-family C member MYCGRDRAFT_41235 {ECO:0000305};
DE   AltName: Full=Ferrichrome A-like siderophore biosynthesis protein MYCGRDRAFT_41235 {ECO:0000303|PubMed:28818040};
GN   ORFNames=MYCGRDRAFT_41235;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115943 / IPO323;
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).
RN   [2]
RP   FUNCTION.
RX   PubMed=28818040; DOI=10.1186/s12864-017-3969-y;
RA   Cairns T., Meyer V.;
RT   "In silico prediction and characterization of secondary metabolite
RT   biosynthetic gene clusters in the wheat pathogen Zymoseptoria tritici.";
RL   BMC Genomics 18:631-631(2017).
CC   -!- FUNCTION: Multidrug resistance protein; part of the gene cluster 14
CC       that mediates the biosynthesis of a ferrichrome A-like siderophors
CC       which may contribute to organismal virulence.
CC       {ECO:0000305|PubMed:28818040}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC       Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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DR   EMBL; CM001199; EGP87768.1; -; Genomic_DNA.
DR   RefSeq; XP_003852792.1; XM_003852744.1.
DR   AlphaFoldDB; F9X9V4; -.
DR   SMR; F9X9V4; -.
DR   STRING; 1047171.Mycgr3P41235; -.
DR   EnsemblFungi; Mycgr3T41235; Mycgr3P41235; Mycgr3G41235.
DR   GeneID; 13397113; -.
DR   KEGG; ztr:MYCGRDRAFT_41235; -.
DR   eggNOG; KOG0054; Eukaryota.
DR   HOGENOM; CLU_000604_27_1_1; -.
DR   InParanoid; F9X9V4; -.
DR   Proteomes; UP000008062; Chromosome 4.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma 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   Gene3D; 1.20.1560.10; -; 2.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00664; ABC_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF90123; SSF90123; 2.
DR   PROSITE; PS50929; ABC_TM1F; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1353
FT                   /note="ABC-type transporter MYCGRDRAFT_41235"
FT                   /id="PRO_0000451095"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        364..384
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        397..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        748..768
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        796..816
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        864..882
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        888..907
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        973..993
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        1002..1022
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   DOMAIN          129..420
FT                   /note="ABC transmembrane type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          460..684
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          756..1030
FT                   /note="ABC transmembrane type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          1070..1334
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          687..720
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1191..1223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         496..503
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         1104..1111
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        481
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   1353 AA;  148040 MW;  85C24B16FF8B8753 CRC64;
     MSKSLAYPPR KWYRRVPFLS DKSSLTLLDS NGNRKITPEA SASLWNWFFF SWLNPLIAIG
     YSRPHIQSEL YLLPPSSDVS VYAGKLDGHI EGLRERVPEG GGKRRRFNFH SPSWRLARAL
     NASVLVWFWV GGAMKLFADV ATITSPLLVR AIIRFLQTSE QNRKAGLPEP SIGQGFGMAI
     GLALLLASGV MANVHGFYRS YTSGILLRSA LIDSLFRRTS AFSPLERAKH NLETSRIISM
     ISTDVSRIDF ACGYFHATWT SVIQILICLG LTIASLGPAA LTGFGLMAIL VPSQNYIVKY
     LFLLRKRSMP FTDARLSAIS EALASIRLVK VYAWESALLS KISFLRRSEL KLLRSRLLLR
     AVNVALSFSV PTLAAVVSFV TYAALGNELD AAEVFSALTL FMLLRTPLLL LPVAFGAAAD
     GANAIQRLAG AFDAPMPDHG LPIDGDIEAA VEVKDATVSY RVQDHSDEKS EKQTSSFQLT
     NLTVHINRGE LFMIVGPVGA GKSTFLGSLV GETRLETGHA VLGSRAAYAP QQAWLKSGSI
     RENIVFGRPW NPDRYNSVLS ACCLTQDLST FPSGDETMIG ENGISLSGGQ RQRVALARTI
     YEPSPLLLLD DVFSALDAHV QSEVVQKVVL ERDPGTTLVL VTHSLHLLRH ADRICCLNEG
     RVEEMGSFAE LMGKEGGQMR RVVEEFASKS SAEEEEVEDG DLKDGVPSTD GGDASQTTSN
     KAMMQTEERF IGSVTARTYA SYIRAGKPAF TLTFFILSML IFQGGSILSP LWLQWWQEGR
     FPTLSSGTYM GVYAALGVSQ AIGLLAMSSI FGFFIFYSAC QIHADAIRSV LYAPISFFDT
     TPLGRITHRF SKDIDAIDNV IGEAFRMLLS TVAQVVGAVV LISIILPWFL LAVFVIVILY
     ILTGMYYRPT ARELRRLDAL TRSPIYEHVS ESLNGIMVIR SLGALQTTLD RNRENLNTEN
     SPYWLSVACQ RWLSVRLDLL GTCLVLLVGL IVVGSRSSIS AAQGGVALSY IVTVQAVFGF
     MIRQSAEIEN NMNAIERLLY YSHDVPQEPP HKREGDVGLV EKKWPGQGAI EMRDVVFTHR
     EGLEPSLRGV NLVIPAGCRL ALVGRTGSGK STMLAALVGM GEITAGTIMV DGVDVSTIGL
     NLLRKRIAFM PQEAAVLSGT LRYNLDPFGE HDDADLWRVM HQVGLSSISA QSSAETLTSS
     DQEKSSPDDA AISPSSHSHS QHLTLDTPIH AERSDLSSGQ RSLISLARAL IKDASIFVLD
     EATASMDMEL DHRLQRVLRE NLRGKTTIVI AHRLDSVVGS SDLICVMDEG RVAQCGSPMD
     LFGEEGGHFR SLCSDAGLGE LDLVEARRRF VSS