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Database: UniProt
Entry: S3CNL2_GLAL2
LinkDB: S3CNL2_GLAL2
Original site: S3CNL2_GLAL2 
ID   S3CNL2_GLAL2            Unreviewed;       428 AA.
AC   S3CNL2;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   08-NOV-2023, entry version 39.
DE   SubName: Full=Acid protease {ECO:0000313|EMBL:EPE26759.1};
GN   ORFNames=GLAREA_02673 {ECO:0000313|EMBL:EPE26759.1};
OS   Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE26759.1, ECO:0000313|Proteomes:UP000016922};
RN   [1] {ECO:0000313|EMBL:EPE26759.1, ECO:0000313|Proteomes:UP000016922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX   PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA   Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA   Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT   "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT   the fungus Glarea lozoyensis.";
RL   BMC Genomics 14:339-339(2013).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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DR   EMBL; KE145370; EPE26759.1; -; Genomic_DNA.
DR   RefSeq; XP_008085949.1; XM_008087758.1.
DR   AlphaFoldDB; S3CNL2; -.
DR   GeneID; 19461729; -.
DR   KEGG; glz:GLAREA_02673; -.
DR   eggNOG; ENOG502SMFH; Eukaryota.
DR   HOGENOM; CLU_039077_0_0_1; -.
DR   OrthoDB; 2342359at2759; -.
DR   Proteomes; UP000016922; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
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; 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; NAPSIN-A; 1.
DR   Pfam; PF00026; Asp; 1.
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   Hydrolase {ECO:0000313|EMBL:EPE26759.1};
KW   Protease {ECO:0000313|EMBL:EPE26759.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016922};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..428
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004518789"
FT   DOMAIN          44..426
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   DISULFID        352..387
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   428 AA;  46252 MW;  3CFEE03F9B143F96 CRC64;
     MSFSASIFLT LSLGLVANAH PATPKTPCNQ PYDIPLLRDP GYGWMANISV GTPPQPITMF
     VDWTWTSQYV VSTTCNGRDD NTAACLHPAQ QLYNQSLSST YKSEKALYPS ESWYPNEFFP
     APFNVDYASD VQTIGPVTSR IVLQTSNIQP GIFTSAPLPF GGIYGMMPDP KGENGQLLLP
     SLDILDACSP SDLAPFNQQY RAKAWPQPYS AFAMCPNPSC PKGADAIQTL GGYSPALARK
     GLSWYDIVEV PEVNEIDFVF APGVYSYWSI GLSGLYIGNQ AQKLNTTAAL TKEGVPAAIF
     DHASKGRGVP LSVDAYANLV KIAGGKPIAP NSPLLTPYAP NNGPQPFFSI DCKKTKTLPV
     ISYAFTGSRK QWSVQPSEYV VNVAGTCILD VRAIGEGSFL LGNFGDNFLK GKYVVFDYAS
     QRVGLAEL
//
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