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Database: UniProt
Entry: F4RUY1_MELLP
LinkDB: F4RUY1_MELLP
Original site: F4RUY1_MELLP 
ID   F4RUY1_MELLP            Unreviewed;       392 AA.
AC   F4RUY1;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   22-FEB-2023, entry version 41.
DE   SubName: Full=Aspartic peptidase A1 {ECO:0000313|EMBL:EGG03844.1};
GN   ORFNames=MELLADRAFT_89871 {ECO:0000313|EMBL:EGG03844.1};
OS   Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar leaf
OS   rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Melampsoraceae; Melampsora.
OX   NCBI_TaxID=747676 {ECO:0000313|Proteomes:UP000001072};
RN   [1] {ECO:0000313|Proteomes:UP000001072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=98AG31 / pathotype 3-4-7 {ECO:0000313|Proteomes:UP000001072};
RX   PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA   Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA   Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA   Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA   Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA   Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA   Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA   Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA   Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA   Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA   Grigoriev I.V., Szabo L.J., Martin F.;
RT   "Obligate biotrophy features unraveled by the genomic analysis of rust
RT   fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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DR   EMBL; GL883122; EGG03844.1; -; Genomic_DNA.
DR   RefSeq; XP_007412958.1; XM_007412896.1.
DR   AlphaFoldDB; F4RUY1; -.
DR   EnsemblFungi; EGG03844; EGG03844; MELLADRAFT_89871.
DR   GeneID; 18935357; -.
DR   KEGG; mlr:MELLADRAFT_89871; -.
DR   VEuPathDB; FungiDB:MELLADRAFT_89871; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_038846_0_0_1; -.
DR   InParanoid; F4RUY1; -.
DR   OrthoDB; 656651at2759; -.
DR   Proteomes; UP000001072; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF74; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001072};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..392
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003321800"
FT   DOMAIN          43..383
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   392 AA;  43227 MW;  CFA72EF62B87E4DA CRC64;
     MFSYFVHFRI SSTLLFLSVV FVRSEQTEKV KLSIPIVNSL NLYTLNVGIG TPPTPHALGI
     ATGSANTFAG AFNPGTFQPT PSTTNLQKPF FIPYGYGNVT GTLLTETLTF TANENSLTLP
     NVTIGNVSKL VSHHSSSIQQ QGFDGFDGLL GLGLSSESYP RDAENIGELL TPTGIMYDRE
     VLEEVMFGIS FMPTRSAPDP NGLITFGGVN PNRFIGDLVW YPCSSYHTWD WKASISYGDA
     TLSETELRGS FDTSYTNSPA IPRYLFDKYV VSIPGAVWDD SWLELNPAGQ VNEYMLRIPR
     ASVAEMEDLC FSSGDRKWCL VPEAQLVPDG IVPNADPAYR YGYVSPVQTA DASQQNSTFV
     FGMKAMERFY VAFDLANYRI GLAETEWTNC TF
//
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