ID S3CIV2_GLAL2 Unreviewed; 608 AA.
AC S3CIV2;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:EPE26427.1};
GN ORFNames=GLAREA_02340 {ECO:0000313|EMBL:EPE26427.1};
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:EPE26427.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE26427.1, 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).
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DR EMBL; KE145370; EPE26427.1; -; Genomic_DNA.
DR RefSeq; XP_008085617.1; XM_008087426.1.
DR AlphaFoldDB; S3CIV2; -.
DR STRING; 1116229.S3CIV2; -.
DR GeneID; 19461397; -.
DR KEGG; glz:GLAREA_02340; -.
DR eggNOG; ENOG502RV5I; Eukaryota.
DR HOGENOM; CLU_009988_3_0_1; -.
DR OrthoDB; 1831139at2759; -.
DR Proteomes; UP000016922; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR Pfam; PF00026; Asp; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:EPE26427.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:EPE26427.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016922};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..608
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004518656"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 58..413
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 428..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 608 AA; 66491 MW; 1EF6E97D61194CA0 CRC64;
MNFVRCSFAV SYLVSLAIAP IPPSVQSIDP RAASPNTTLT PIVVPVSQYF DGDDGEWSTI
IIRVGNPEQS VRVFVSTNSP ITGVVEPGGC EIEAIPRGVP DDCANSRGRT FNSNSSLSWF
WQGQSTLNGG NGVGFEANLG YDFYLDYGQD TIALGFQDGP DSVRLTNQTV AAYTRPRPLY
VGFFGIGTER VIYGNFGNYS GPSFFKQLAI DRKIPSLSWS YTAGARYQLA GGQYMQLIFG
GYDTSRFIPN NVRFTLGADV TRDIVVGVQS ILFTGTNTTP LLRSPIYAFV ESTDPNIWLP
MEACLLFEKA FGLTWDNSTS KYLLSDNQYN VLSKSDPKVT FRLAVSTVGG TTADITLPFR
AFALRAKYPY VQNATYYFPL QRANDSSQYT LGRAFLQEAY LTVDYDRRNF TLSQCIFNQG
ATPDILPIYS PTTNNGSGNG TEDVSNASTR NSQGRHTTTI VASVVVSVLV IIGGVGLWLW
KKRKDKKKRD SDQTPARATG PAAPVEQGPV ENIDLKGYYK PELDNRGELY EVPGTIVDAS
DDIGPAELHG HGAAHELVGS PVERTRDSEA MYRRVSSPLP RALERKAVSA PVSPLSPPIP
QSSFRQGR
//