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}.
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; 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
//