ID   OBLD_COCH5              Reviewed;        1508 AA.
AC   M2UCE5;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=ABC-type transporter oblD {ECO:0000303|PubMed:27116000};
DE   AltName: Full=Ophiobolin biosynthesis cluster protein D {ECO:0000303|PubMed:27116000};
GN   Name=oblD {ECO:0000303|PubMed:27116000}; ORFNames=COCHEDRAFT_98522;
OS   Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) (Southern
OS   corn leaf blight fungus) (Bipolaris maydis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=701091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC 48332 / race O;
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC 48332 / race O;
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
RN   [3]
RP   FUNCTION.
RX   PubMed=27116000; DOI=10.1021/acs.orglett.6b00552;
RA   Narita K., Chiba R., Minami A., Kodama M., Fujii I., Gomi K., Oikawa H.;
RT   "Multiple oxidative modifications in the ophiobolin biosynthesis: P450
RT   oxidations found in genome mining.";
RL   Org. Lett. 18:1980-1983(2016).
CC   -!- FUNCTION: ABC-type transporter; part of the gene cluster that mediates
CC       the biosynthesis of the sesterterpenes ophiobolins, fungal phytotoxins
CC       with potential anti-cancer activities (PubMed:27116000). Acts as a
CC       specific transporter involved in ophiobolins secretion
CC       (PubMed:27116000). {ECO:0000269|PubMed:27116000}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:27116000};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC       PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
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DR   EMBL; KB445570; EMD96239.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2UCE5; -.
DR   SMR; M2UCE5; -.
DR   STRING; 5016.M2UCE5; -.
DR   EnsemblFungi; EMD96239; EMD96239; COCHEDRAFT_98522.
DR   eggNOG; KOG0065; Eukaryota.
DR   HOGENOM; CLU_000604_35_0_1; -.
DR   OMA; TFAHFMI; -.
DR   Proteomes; UP000016936; Unassembled WGS sequence.
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   CDD; cd03233; ABCG_PDR_domain1; 1.
DR   CDD; cd03232; ABCG_PDR_domain2; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013525; ABC_2_trans.
DR   InterPro; IPR029481; ABC_trans_N.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
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   Pfam; PF01061; ABC2_membrane; 2.
DR   Pfam; PF19055; ABC2_membrane_7; 2.
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; SSF52540; 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..1508
FT                   /note="ABC-type transporter oblD"
FT                   /id="PRO_0000451174"
FT   TRANSMEM        501..521
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        536..556
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        610..630
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        643..663
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        752..772
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1172..1192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1206..1226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1296..1316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1322..1342
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1443..1463
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          136..390
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          828..1070
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          54..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         864..871
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CARBOHYD        24
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        35
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        231
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        314
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1390
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   1508 AA;  168877 MW;  35A90402BF688ACC CRC64;
     MSLGPGGFEA TPNSVMPSDA SLHNQSHHTD SLTNNDSIAS TEQREKEVHQ LARKYTQNSV
     YSTTSQNPFA AEPGSKLDPN GGNFSARAWA KAMLQTHTDD NQAHPLRTLG VSFSNLNVYG
     FGFDTDYQKS VGNIWLEAVG LVRKLMGQRE RKIEILRDLE GLVEAGEMLV VLGPPGAGCS
     TFLKTLTGQT HGFYVDDKSN LNYQGVTPKQ LIKNFRGEAI YTAEVDVHFP NITVGDTLFF
     AARARAPRHI PGGATIDQYA EHMRDVIMAS FGISHTKNTI VGNDFIRGVS GGERKRVSIS
     EACLSQAPLQ CWDNSTRGLD SANAIEFCKT LRMQTEINGA TACVAIYQAP QAAYDYFDKV
     LVLYKGRQIY FGPTAQAKQY FLNMGFVCPD RQTDADFLTS MTSHLERVVQ PGYENQVPRT
     PDEFAARWKA SRERAELLNQ IEMYNSKYAT GGEHLERFKE SRRAQQAKAQ RVSSPYTLSY
     TQQIKLCLWR SWVRLKGDPS ITISSAMGNA IIALIISSMF FNLKDDTSSF FQRGSLLFFA
     IVINAFSSGL EMLTLYAQRP IVEKHSRFAL YHPSAEAIAS MLMDLPYKTL NAISSNLILY
     FMTNLRREPG NFFFFVFTSF VLTLTMSMFF RSIASLTRSL VEALPFAAIL ITGLTMYTGF
     TIPTSYMPGW SRWMAYIDPI AYGFESIMVN EFSGREFLCV NYVPAGPSYN VGGNNRVCST
     VGSVPGQPFV LGDDYIRSTY GYEASRKWRN VGIIFAFMVI LCAIYLVASD FITEKKSKGE
     ILVFRRGHKN LDRSTGQDDV EGGSERTTTA ANTKSDDIAI IEQQTAIFQW KDICYDIQIQ
     KERRRILDHV DGWVKPGTLT ALMGVSGAGK TTLLDVLASR TTMGVISGEM LVDGKERDDS
     FQRKTGYAQQ QDLHLSTATV REALTFSALL RQPAHIPREE KIAYVTEVIK LLEMTEFADA
     VVGIPGEGLN VEQRKRLTIG VELAARPALL LFLDEPTSGL DSQTSWAILD LLDKLKKNGQ
     AILCTIHQPS AMLFQRFDRL LFLKSGGQTV YYGDVGENSK ILIDYFTRNG GPPCPPAANP
     AEWMLEVIGA APGSHTDIDW HDTWRKSPEY AYVQAHLAEL KEERSRMTDL SRTASRQAHD
     AASFREFAAP FWAQFYEVQL RVFQQLWRTP TYIYSKAFLC VSTSLYVGFS LYNTPNTLQG
     LQNQMFAIFT LFFLFGQFIQ QIMPHFVAQR ALYEARERPS KTYSWKAFIM SNIIVELPWN
     TLMSVLLFLC WYYPIGLSHN AEATDSTALR GAQMWLFVWV FLMFASTFAH FMIAALDTAE
     NAGNMGNLLF TLCVIFCGIL TTPEQMPRFW IFMYRVSPFT YLVGGMMAVG VADSSVTCAA
     NEYLHFDPVN GTCGEYMAQY QAMAGGYVQN PSATSNCAFC PMGDTNVFLK TVHAEYSNVW
     RNFGLMWVFV VFNAFAACGL YYWARVPKRP TIEKEAAPIR AEGSLDSETV VGRTSAVEQQ
     DAEKRAAF