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
//