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Database: UniProt
Entry: E4ZUJ7_LEPMJ
LinkDB: E4ZUJ7_LEPMJ
Original site: E4ZUJ7_LEPMJ 
ID   E4ZUJ7_LEPMJ            Unreviewed;      1099 AA.
AC   E4ZUJ7;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Similar to ATP-binding cassette sub-family G member 2 {ECO:0000313|EMBL:CBX95076.1};
GN   ORFNames=LEMA_P114910.1 {ECO:0000313|EMBL:CBX95076.1};
OS   Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS   (Blackleg fungus) (Phoma lingam).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC   Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX   NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN   [1] {ECO:0000313|Proteomes:UP000002668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC   {ECO:0000313|Proteomes:UP000002668};
RX   PubMed=21326234; DOI=10.1038/ncomms1189;
RA   Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA   Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA   Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA   Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA   Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA   Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA   Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA   Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT   "Effector diversification within compartments of the Leptosphaeria maculans
RT   genome affected by Repeat-Induced Point mutations.";
RL   Nat. Commun. 2:202-202(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       Eye pigment precursor importer (TC 3.A.1.204) subfamily.
CC       {ECO:0000256|ARBA:ARBA00005814}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; FP929126; CBX95076.1; -; Genomic_DNA.
DR   RefSeq; XP_003838555.1; XM_003838507.1.
DR   AlphaFoldDB; E4ZUJ7; -.
DR   STRING; 985895.E4ZUJ7; -.
DR   EnsemblFungi; CBX95076; CBX95076; LEMA_P114910.1.
DR   GeneID; 13288173; -.
DR   eggNOG; KOG0061; Eukaryota.
DR   HOGENOM; CLU_000604_57_1_1; -.
DR   InParanoid; E4ZUJ7; -.
DR   OMA; NCQLDAF; -.
DR   OrthoDB; 359054at2759; -.
DR   Proteomes; UP000002668; Genome.
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; cd03213; ABCG_EPDR; 1.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013525; ABC2_TM.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR043926; ABCG_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR48041; ABC TRANSPORTER G FAMILY MEMBER 28; 1.
DR   PANTHER; PTHR48041:SF139; PROTEIN SCARLET; 1.
DR   Pfam; PF01061; ABC2_membrane; 1.
DR   Pfam; PF19055; ABC2_membrane_7; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:CBX95076.1};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW   Signal {ECO:0000256|SAM:SignalP};
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   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1099
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003194543"
FT   TRANSMEM        318..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        844..866
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        878..900
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        921..945
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        957..980
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        987..1007
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1074..1096
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          82..121
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          374..615
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          667..724
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        667..686
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        691..705
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        111..120
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1099 AA;  120969 MW;  C0B95A1B019498BF CRC64;
     MRQTAWAASL LALISLTGSS AAHKTLANYS LPDSQASLFS LYDDRPDGCP PCFNCNLDDF
     KCHQFADCSK ANGRCNCPPG FGGVDCSEPL CGSLADGKDR APRGGEAECQ CKEGWTGINC
     NVCETNQACN ALMPEGEGGV CYKDGQLVKE NYQICDITNR KILDQLKEKK PQATFSCNAE
     SEECNFQFWV AQRESFYCSL DTCTSQFTAE SDRNITKYRC ENIKCECVPD RMLCGEDGSV
     DIGDFLKESI KGPAEFRSIA STNSKESGSV FSEPAMNDLI QSIFGDESIF LQCDTGECLY
     HTEVPGYERP VKKINTPLIA GVIAGCALFI VAAILGIWYL THRNEYQRYG AIHLSDDEED
     ENAKLLADHK PAALLFENVA YNLNGKQILT GISGAVHPGE LLAIMGASGA GKTTFLDILA
     RKNKIGATSG DFYLNGEKIR DDEFRGVIGF VDQEDTLLPT LTVHETILDS ALLRLPKEMS
     RMSKEQKVED VERQLGIYHI RNQKIGSEES GRGISGGEKR RVGIACELVT SPSILFLDEP
     TSGLDAFNAF NVVECLVNLV KNYNRTVVFT IHQPRSNIVA LFDQLILLAK GRAVYSGPFE
     NCQAYFDDIG YTCPPGFNIA DYIVDLTMHA SAARHTIDED SSLFNREGLH TSASSAIAVK
     SIPSINTSEF DRDVPGSPSN SSIRPKGKRR TSIKQQQERE LFTRKKTASL QNGTMSPKTD
     DEVPYDRRGA IKAQWLKLTR QQGGVPPQIL EDPDEYPPPA NGSTGTNLDI LINAYNASDI
     AASLREDIAS AVASANQANG TNGVSDLNGF VAAGKLKGFR KVGFFGQFSI LSRRTWRNLY
     RNPMLMLTHY AIAIVLAVFL GFLFYGLTDD IKGFQNRLGL FLFVLSLFGF SSLTILTVFA
     PERLLFTRER AKGYYSPPSY FLAKVLFDII PLRLLPPLIL GIIVYPMTGL IPAWANFLKF
     ELFLTLFNLA AAAIFLFIGI VFRNSGVANL IGVLVMLFSL LFSGFFLNKE SIPAIAKWLQ
     SLSIFHYAFE GLIVNEVKYL SLIDHKYGLD IEVPGSAILS SFGFNTAALW TDCIGLAVFG
     SAFVVLAYLA MHLLLVERR
//
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