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Database: UniProt
Entry: E5ABD9_LEPMJ
LinkDB: E5ABD9_LEPMJ
Original site: E5ABD9_LEPMJ 
ID   E5ABD9_LEPMJ            Unreviewed;       638 AA.
AC   E5ABD9;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Similar to Vps18 protein {ECO:0000313|EMBL:CBY00980.1};
GN   ORFNames=LEMA_P021100.1 {ECO:0000313|EMBL:CBY00980.1};
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:ARBA00004287};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004287};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the VPS18 family.
CC       {ECO:0000256|ARBA:ARBA00010454}.
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DR   EMBL; FP929138; CBY00980.1; -; Genomic_DNA.
DR   RefSeq; XP_003844459.1; XM_003844411.1.
DR   AlphaFoldDB; E5ABD9; -.
DR   STRING; 985895.E5ABD9; -.
DR   EnsemblFungi; CBY00980; CBY00980; LEMA_P021100.1.
DR   GeneID; 13293111; -.
DR   eggNOG; KOG2034; Eukaryota.
DR   HOGENOM; CLU_003488_2_0_1; -.
DR   InParanoid; E5ABD9; -.
DR   OMA; ECDELIN; -.
DR   OrthoDB; 22879at2759; -.
DR   Proteomes; UP000002668; Genome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   CDD; cd16462; RING-H2_Pep3p-like; 1.
DR   InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR   InterPro; IPR007810; Pep3_Vps18.
DR   PANTHER; PTHR23323; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN; 1.
DR   PANTHER; PTHR23323:SF26; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 18 HOMOLOG; 1.
DR   Pfam; PF00637; Clathrin; 1.
DR   Pfam; PF05131; Pep3_Vps18; 1.
DR   PROSITE; PS50236; CHCR; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          1..106
FT                   /note="Pep3/Vps18/deep orange beta-propeller"
FT                   /evidence="ECO:0000259|Pfam:PF05131"
FT   COILED          486..527
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   638 AA;  72685 MW;  7C1F2302B5A72195 CRC64;
     MILSQWHILQ LVEGRIVAVN RLDDTIVLDQ NVLEPGQSAL GLVADLKKNT YWLFTTQEIF
     EVVVTDENRD IWKIMLKAQQ FEAASQYAKT SAQKDAVATA SGDYLVGKGQ YMEAAAVYGR
     STKPFEQVAL TFIDNGEQDA LRKYLLTKLS TLKKSSIMQR TMVATWLIEL YMAKLNILDD
     TITTRAELSE SMNTAETHDQ LSAIRKEYQD FVTKYKADLD RKTVYDIISS HGREEELLYF
     ATVVNDYNYV LSYWIQRERW AESLNVLKKQ TDPEIFYKYS SVLMGQVPVE LVDIMMRHSN
     FDAQKLIPAF LSYNNHTKVP LSQNQAVRYL LFEINQRNST DAAIHNTLIS VYASHPTTDE
     SALLAYLEGQ SQAHEQNYDA DFALRLCIQH KRVQSCVHIY SSMQQYAQAV DLALKYDEID
     LASTVADRSH TTPALRKKLW LAIAKKVISQ SSGIKTAIEF LRRVDLLRIE DLIPFFPDFV
     VIDDFKEEIC AALEDYSRKI DALKTEMDDS EQTAAHIKQD IKALEQRYAI VEPGEKCFLC
     GLPLLARQFF VFPCQHAFHS DCLAKRVVEL AGVARGKRIQ ELQVEVLKGV RMGKGREKVV
     RELDALVGGS CVLCGEMAVK LIDEPFIRPT DDKAEWAL
//
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