ID V2XJ58_MONRO Unreviewed; 477 AA.
AC V2XJ58;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Pepsinogen a2 {ECO:0000313|EMBL:ESK92886.1};
GN ORFNames=Moror_9089 {ECO:0000313|EMBL:ESK92886.1};
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:ESK92886.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK92886.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK92886.1,
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, ECO:0000256|RuleBase:RU000454}.
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:ESK92886.1}.
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DR EMBL; AWSO01000241; ESK92886.1; -; Genomic_DNA.
DR RefSeq; XP_007847824.1; XM_007849633.1.
DR AlphaFoldDB; V2XJ58; -.
DR KEGG; mrr:Moror_9089; -.
DR HOGENOM; CLU_013253_8_3_1; -.
DR OrthoDB; 1611889at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
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; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..477
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004712294"
FT TRANSMEM 437..459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 57..393
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 73
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 275
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 86..91
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 477 AA; 51893 MW; D4D08DFA04C4E05E CRC64;
MHVMVHILFL LFLHVCHVTA TSSLKKGFKI PLHRVPRVER RGITDSVPIS NVNEFSYLVD
VGVGKQFFPL ILDTGSSDLW IVSDECDVSD CATVRRYSPA SSKDLSISRK PFHLDYLKGS
VSGLVAFETV SMGLFEINPQ VLGLVNVIQS MNLASTGNSG ILGLSFPTEA TIFIKSGSTV
LENIFAYLDE PFFAFKLGKN SGPNSPTSSL TFGQLDTTYS SDMSSFLITP VSQAGANDYS
FWKLPLQSII VNNYTLPLSQ SSVQGVHEEQ IAVLDTGTTL ILGPTSDVDS FWAMIGPDAR
YNIASCMWEI KCNKAVGVQF VLGDKDAHRA FTMDYADVNW AEGGSDGEWC MGGIQANDNV
DSGDWLLGDV FLRNVYSIHH GGNSTHPPFI GLLGTMNQSA ALTDFRTSRG PDLESGSSSM
PHIHGTLERR ASLAAPMLYS LVTASGFVIG AASTTLFRAR RRMWGFRRYS KSAAASL
//
