ID S3D027_GLAL2 Unreviewed; 854 AA.
AC S3D027;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:EPE30514.1};
GN ORFNames=GLAREA_03481 {ECO:0000313|EMBL:EPE30514.1};
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:EPE30514.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE30514.1, 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; KE145363; EPE30514.1; -; Genomic_DNA.
DR RefSeq; XP_008081925.1; XM_008083734.1.
DR AlphaFoldDB; S3D027; -.
DR GeneID; 19462536; -.
DR KEGG; glz:GLAREA_03481; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_9_4_1; -.
DR OMA; FGCKEAT; -.
DR OrthoDB; 615305at2759; -.
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 Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
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:SF81; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 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 Hydrolase {ECO:0000313|EMBL:EPE30514.1};
KW Protease {ECO:0000313|EMBL:EPE30514.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016922};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..854
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004519344"
FT DOMAIN 72..386
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 416..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 854 AA; 86092 MW; 8586F9DC4DC0DBC5 CRC64;
MISLPSTLCG RLALLSLAAL SNALPSSSAG QNNGILRLPV TAQAVNVTDL ATFGRRDIVE
VPLQNALTGT LYLIQVPLGS VPQSVPLAID TSSGETFVNP ICSTSGNAAF CSSLPRFTSS
ATLVDYGVTG SVDFGTSSAS FSYVGDSLRF GTFTISQQIF GVIFSSTNLV AGVLGLGGDV
DNPYPFVIDS LKSQGVTPSR AFSLDLRSVD SPDGAVIFGG IDTKKYIGAL EKRPMIPLAQ
TPTPNIAARY WIYINSVGIT KPGSTPKLYP ATGTAQGQPA FINSRATISR LPTTLVNTIV
ADFPGATQDA SGLYVVDCAV GSQAGTVDFG FGSTIIHISF KDFLWQNGGI CYLGVTADDI
APQLGDSFLR AAFVVFDLDN QNVHLANAAN CGTNLAAITT GLNAVPSIVG GCAAPTSTTS
SASSTSTSSS STSSSTSTLT TTTTTSSTTS TTSSTTSTTT STTPSTTSST TSSTTSSTTS
SDTPSTTSTT TSTTSSTTSS TISSDTPSTT SSTTSSTTPS TISSTISTTA SSSTSSSSSS
SISGSSSGTS TAAPVGSTIS TVTTSISSSN LPTSIPTSTS GVSSSTSSTA VNSTFSTSSV
VSTLIVDPTS TRIPSGPGSN STTATTVTSS SSTSSLPQST TIYTISTVYT TSIYTITSCT
ARITNCPAII GQVTTEVISL YTTVCPVTIA ASTIKPVPTS TPTPSAIEYT ISTVYATKTY
TITSCAPNVT NCPASIGKVT IALYTTYCPV TKGEVSGSIT NIAIGSQIPA TTPTKTNSAV
GVTNSAVGVA TIVSVSIAPV NVLPSQGATG NSTVKVAASS TPTNILITNS APTAFGPESL
KFGSIMLIAF MVYL
//
