ID   V2X7L6_MONRO            Unreviewed;       546 AA.
AC   V2X7L6;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Pepsinogen c {ECO:0000313|EMBL:ESK88781.1};
GN   ORFNames=Moror_17115 {ECO:0000313|EMBL:ESK88781.1};
OS   Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS   (Crinipellis roreri).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK88781.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK88781.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK88781.1,
RC   ECO:0000313|Proteomes:UP000017559};
RX   PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA   Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA   Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA   Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA   Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT   "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT   Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT   mechanisms of the biotrophic and necrotrophic phases.";
RL   BMC Genomics 15:164-164(2014).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ESK88781.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AWSO01000619; ESK88781.1; -; Genomic_DNA.
DR   RefSeq; XP_007851901.1; XM_007853710.1.
DR   AlphaFoldDB; V2X7L6; -.
DR   KEGG; mrr:Moror_17115; -.
DR   HOGENOM; CLU_037038_0_0_1; -.
DR   OrthoDB; 1696312at2759; -.
DR   Proteomes; UP000017559; Unassembled WGS sequence.
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   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; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF89; SACCHAROPEPSIN; 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   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..546
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004711279"
FT   DOMAIN          54..396
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        70
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        281
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        83..88
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        317..351
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   546 AA;  58252 MW;  45C7FF66F0ADBEF9 CRC64;
     MRFPYLVALF VLVAGVLGGS RSQRAPSLLS RDLAVDGVNA TIVSLALASD HQSYYVVLKT
     GEISFRVALD TASSDIWILS SLCTTNTCFN APRYPLTYQS PTFSSVNANS TKYQVKYADG
     TAASGFVAKE DIHVGNMTLP QQAFGMITET NVVFTDQESG ILGLGFPRLS KIDRNVAGSA
     PFLTTLSEQG LLNYPLFGLS LTRDTSGTLS LGAIDGTVVT NITRIEWNEV VQFPPLGVEN
     NVSTYWHWAL PLQGISVHSR AVSLSPSYPT ITDGLPIAMF DVGVSGIYGP WADVAKIFEA
     IEESRLVDAS GQWAVPCDTR VLMTFTFGTQ NFTLQPTDYL IGPTSGNPTL CLSWPRAVTP
     SPDGIDWQLG SPFLRTVYSI FSYGIDMKEP PMIGLYALNN SVLAPSPAEV SAFFSSISVQ
     IPTTLPNYLL PTPTISTPPY SLNSSITAPT GGIVSSGLAN STYSPIFAQE VTNLSALPII
     TAEPTVATFT LTDPAGGVST TTSHLSMASV ALGVPPGWNS APSTTRLPSA SNFMLPILIA
     WTLYCI
//