ABC7_MAGO7
ID ABC7_MAGO7 Reviewed; 1683 AA.
AC G4N2B5;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=ABC transporter 7 {ECO:0000303|PubMed:27902426};
DE AltName: Full=Pyriculol/pyriculariol biosynthesis cluster protein ABC7 {ECO:0000303|PubMed:27902426};
GN Name=ABC7 {ECO:0000303|PubMed:27902426}; ORFNames=MGG_04855;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
RN [2]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=27902426; DOI=10.1099/mic.0.000396;
RA Jacob S., Groetsch T., Foster A.J., Schueffler A., Rieger P.H.,
RA Sandjo L.P., Liermann J.C., Opatz T., Thines E.;
RT "Unravelling the biosynthesis of pyriculol in the rice blast fungus
RT Magnaporthe oryzae.";
RL Microbiology 163:541-553(2017).
CC -!- FUNCTION: ABC transporter; part of the gene cluster that mediates the
CC biosynthesis of pyriculol and pyriculariol, two heptaketides that
CC induce lesion formation upon application on rice leaves but are
CC dispensable for pathogenicity (PubMed:27902426). With the MFS
CC transporter MFS1, is most likely responsible for pyriculol and
CC pyriculariol secretion and thereby may contribute to intrinsic
CC resistance (Probable). {ECO:0000269|PubMed:27902426,
CC ECO:0000305|PubMed:27902426}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; CM001233; EHA52527.1; -; Genomic_DNA.
DR RefSeq; XP_003712334.1; XM_003712286.1.
DR AlphaFoldDB; G4N2B5; -.
DR SMR; G4N2B5; -.
DR STRING; 318829.MGG_04855T0; -.
DR EnsemblFungi; MGG_04855T0; MGG_04855T0; MGG_04855.
DR GeneID; 2675285; -.
DR KEGG; mgr:MGG_04855; -.
DR VEuPathDB; FungiDB:MGG_04855; -.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_6_1; -.
DR InParanoid; G4N2B5; -.
DR OMA; ICMATPV; -.
DR OrthoDB; 138195at2759; -.
DR Proteomes; UP000009058; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1683
FT /note="ABC transporter 7"
FT /id="PRO_0000446274"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 496..516
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 602..622
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 632..648
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1016..1036
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1111..1131
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1182..1202
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1204..1224
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1304..1324
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1327..1347
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 338..664
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 700..949
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1028..1351
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1392..1649
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 53..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..998
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 742..749
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1426..1433
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 956
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1097
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1683 AA; 186100 MW; 490B5CDCAEF7D7F0 CRC64;
MGGVGQCQWP VWQVDDLTPC FQHDYLRILL PAVVIGLSVL NLGFRSARHA ASRSKSPSTH
AYAPVSNGDN SRPGAHRTDI SPDDDAIAQD DEDDDEGLAI GGGRLALVKT ATKGSIVQAD
TPPAQTLSVV VEELAIAGLV AVYVIALLSP KAHGSYTLTG TIIGLTTWVY VLVLATLRLF
LGNTQWRVPH LWNHTAAIYS CQWLFLIGIF RSAMVHPSSK LAQILVIVEF ALTSLLFFMA
ITTRKGNKTV LLEWEDGIPP ARENLASLFS SFTFSWVDQI VWQGYKEPFE MGKVWNLLPK
DKAATVLSHY RRVKKTTKLY WHLLRYFKGD LLSQAGWAVM SGMFTFAPTM LLKAILEYVE
EPESAPRSVV WLYVILLPVT DIIRSLGDNR ALWIGRKICI NVRAILVGEI YAKALRRKAA
TGKDTVLGSE KKEDKPKGGF ISKIKKMLCL GDNDESEDGK DGDKDKEDSS DEQANHGTII
NLMSVDSFNV SEVTSYLHFL FASAPTQLLV SVVLLYQVLG MSAIPGFVVM VLLLPVNIGF
GRAFNSTQKK IMACSDKRIH STNEVLQNIR IIKYFAWEHR FSESVDEKRK AELKALRARY
MVWACAVAVW NTVPLLITFF SFLMYTTVEK RPLHPSIAFT SISLFMLLRH PLDQLGDMLA
HVQEAKVSID RIEEFLSEEE TDKFIQLGED NVNEEGTRII ALKDAAFIWG GKDIIAADGS
QAFRLLDIDT EFMIGKLNVI AGPTGSGKTS LLMALLGEMT LLKGRVYLPG GRSREDVRPD
PETGLAETCA YVAQQAWLVN ANIKDNILFS ARFDEKRYRD VIVACALERD LEILDNGDET
LVGEKGITLS GGQKQRISLA RAVYSNSKHL LLDDCLSAVD SHTAQWIFNN CIRGPLMKDR
TCIMVTHNIP LCVPHSDFVV VMDNGRITHQ GRALEVITSG ALGEEIAQKA KSETPNISRI
PSRVPSSVGE GSGNTLLDTD GDDHLSKPKN AKKAKKAEAM EETKATGAVK WPVMKLYLAS
MGSWWFWVVA GCIFISQQAS DVVSNLWIKQ WASQYTTEVS SVPISTSSHM YGTQSFAPTY
MVPVQTYVKD QLARNGNATA LDIVVNSEVN AQYYLVVLAI IGLAGSLTAF LRDLWIFFGS
LTASAKIHTR LLNTVTRAKF RFFDVTPLGQ MMNRFSKDME AVDQEVAPIA IGILSCALGI
TVTVVLIASI TPGFLIAAVF ITIAYVLLAK FYLASSRDLK RLESVQRSPL FQQFGETLSG
VTTIRAYGDE RRFVRDNLTR INGQLRPMIY LWATNRWLAF RTDLLGDFVS FFAGVFVILS
IGVIDAGWAG ISLSYAIGFA ENILWLVRLY SINEQNMNAV ERIKEYLEVE QEAAPICEKN
RPPQNWPAQG SVEFINYTTS YRKELDPVLR NVTFKISPQE KVGIVGRTGA GKSSLALAIF
RALEADGGKI LIDGIDIGLI GLRDLREAIT IVPQEPTLFT GTIRSNLDPF HLFTDEQIYK
SLQRVQLIGP DETIPTADAS PVLPASPTTP GGASNKNIFL NLSSKVSESG SNLSQGQRQL
LCLARALLKE PRVLVMDEAT ASIDYATDSK IQDTIREMKD TTIITIAHRL QTIADYDKVL
VLDKGEVVEY AHPWELMRKG EGGSFKSMCD MSGDTELLAK AAKKAFDAKK LIDVDDEAAD
AAP
