ID E4ZZE5_LEPMJ Unreviewed; 715 AA.
AC E4ZZE5;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=LEMA_P110050.1 {ECO:0000313|EMBL:CBX96740.1};
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 -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; FP929129; CBX96740.1; -; Genomic_DNA.
DR RefSeq; XP_003840219.1; XM_003840171.1.
DR AlphaFoldDB; E4ZZE5; -.
DR STRING; 985895.E4ZZE5; -.
DR MEROPS; A01.057; -.
DR EnsemblFungi; CBX96740; CBX96740; LEMA_P110050.1.
DR GeneID; 13283289; -.
DR eggNOG; ENOG502RV5I; Eukaryota.
DR HOGENOM; CLU_009988_2_0_1; -.
DR InParanoid; E4ZZE5; -.
DR OMA; PGRTEWC; -.
DR OrthoDB; 1945974at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd05471; pepsin_like; 1.
DR CDD; cd12087; TM_EGFR-like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47965; ASPARTYL PROTEASE-RELATED; 1.
DR PANTHER; PTHR47965:SF12; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00026; Asp; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 441..468
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 38..406
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 502..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 715 AA; 76682 MW; C286EAA4EA935F8C CRC64;
MAFEKRASAV TVLPTPLDVP VSGDFDGDDG KWSSFHINIG NDGTGTGQNF KVLISTSSSV
TLVPQQASWC DTECALQRGV QLFRGSSSRG LEITSSKTWN ELGSYEIPLP DWFTANLTLD
PSGLLPGATF GEDYVATGQS VASTRKSPKQ FVGAYPDKDF YMGWLGLAVG ENGLTNGSLL
NFLDNLVATD DPVIPSRSFG YSVGAHYRNN QRGVPGSLVL GGFDSSRFTG DGVSINMPSA
QDNSLVVGVQ SILYKTDPAV STITRSFTSN EERPEGGFMA VIDSTIPYLI LPNDICGFFA
KEFQLTYDEV SRYYLVNDSA HTSNIQRNPT VSFKIGVGDQ DSAQDYTNIA LPYAAFDSQL
SSPKVNQTTR YFPIRHSDGG KSVLGRTFLQ EAYLIVDYEH VNFTIARAAL DDVPTSKLVP
IFPQDYVPPS LNNGSGGSQG LAAGGIAGIV VGIVLAFIIA GIAGLVFFKK RRRANKKDSY
HESSEVDATY AGNEVKYRRV SELTGSELQS PKGSAAGYYS SDPKAIPPIS EMSPESTPAE
LYSPPADGRD TFDYLVAGRV RRRGATRDRD SSGNNTPRTP IAELSGEGAL SLAFNEKDRG
PSDISLQTNI DEVIANERSS DTKASAEVAS SSVKPGEPAT ATGIAQAKVD ASTDANSTED
EQGQQSTTER RPSHTRDLSD ITIQSDSTAV SQPTPGELEH WARSGNQGPR RPMSP
//
