ID A0A068SCU4_9FUNG Unreviewed; 418 AA.
AC A0A068SCU4;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Pepsinogen 2 {ECO:0000313|EMBL:CDH60084.1};
GN ORFNames=LCOR_10877.1 {ECO:0000313|EMBL:CDH60084.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH60084.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH60084.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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:CDH60084.1}.
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DR EMBL; CBTN010000083; CDH60084.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068SCU4; -.
DR STRING; 1263082.A0A068SCU4; -.
DR VEuPathDB; FungiDB:LCOR_10877.1; -.
DR OrthoDB; 1351244at2759; -.
DR Proteomes; UP000027586; Unassembled WGS sequence.
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:SF51; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000027586};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..418
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001655754"
FT DOMAIN 51..397
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 397..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 418 AA; 45762 MW; 4A8495DFD11DF173 CRC64;
MMHKGVFILL ASCLITLPGQ AQALQRIPLH RRNNDGGGLK TEPMTFDDGS LVGTVKIGSP
AQEFSVLFDT GSSLSWVPST KCHSTECRSL GHTPYDAEDS STAFDLNQKE SIRYSDDSCI
DVELYTETIS VAGLTVENQL FGAAYSVKNI GDDKYIGYLG LGGFSEDGST NFNGSTSKDI
QKRAFVNSNG FAQNAFQTGY GGNSQQFGMV TYNNNGFYGK KRWNKPDGEF IFGGVDHDLY
DGKIAYMPLP TCDYGDSPYW KTRMNCVKLG HLADIKLAHK SLASFGTNNN YISGPSSQVE
LLHKAMGAKQ SGGSYQIKCC EADKLPDLTF TFDNYQVSLP ASAWTSPVDG ADRDDEEAMC
KTSIRGNNNE KEWVLGGAFL NNFYHIYDQG NKRVGLATPK DSNSKAKIIK TGSRKNRD
//
