ID G3JCL1_CORMM Unreviewed; 646 AA.
AC G3JCL1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Alkaline serine protease AorO, putative {ECO:0000313|EMBL:EGX93823.1};
GN ORFNames=CCM_02092 {ECO:0000313|EMBL:EGX93823.1};
OS Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX93823.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX93823.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX93823.1,
RC ECO:0000313|Proteomes:UP000001610};
RX PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT valued traditional Chinese medicine.";
RL Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01032};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PROSITE-
CC ProRule:PRU01032};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000256|ARBA:ARBA00004239}.
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DR EMBL; JH126400; EGX93823.1; -; Genomic_DNA.
DR RefSeq; XP_006667309.1; XM_006667246.1.
DR AlphaFoldDB; G3JCL1; -.
DR GeneID; 18164121; -.
DR KEGG; cmt:CCM_02092; -.
DR VEuPathDB; FungiDB:CCM_02092; -.
DR eggNOG; ENOG502QTN1; Eukaryota.
DR HOGENOM; CLU_013783_4_0_1; -.
DR InParanoid; G3JCL1; -.
DR OMA; KWEAYFL; -.
DR OrthoDB; 1405251at2759; -.
DR Proteomes; UP000001610; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04056; Peptidases_S53; 1.
DR CDD; cd11377; Pro-peptidase_S53; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015366; S53_propep.
DR InterPro; IPR030400; Sedolisin_dom.
DR PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR PANTHER; PTHR14218:SF19; SERINE PROTEASE AORO, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G10250)-RELATED; 1.
DR Pfam; PF09286; Pro-kuma_activ; 1.
DR SMART; SM00944; Pro-kuma_activ; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51695; SEDOLISIN; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU01032}; Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01032};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01032,
KW ECO:0000313|EMBL:EGX93823.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001610};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..646
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003446006"
FT DOMAIN 241..646
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
FT ACT_SITE 317
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 321
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 550
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 594
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 595
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 624
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 626
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ SEQUENCE 646 AA; 68996 MW; 1DB12A8ABCCF0C1B CRC64;
MKTTLLIASL VAGAVALPSD THTVHQRRNL AQDVRFEKRA AVESSAKIPF EIALKQGSLQ
EAEDILYDIS NPVSPNYGKH LSKEDVVKLF AANDKSIDSV KQWLVGQGIA EKDIRVNPTK
TWITVDTTAG VVERALKTRY HIYRSTASGQ DHIGAEEYSL PNNLLDIVDF IRPGPAMTKV
TVRATKPATG DAAIGEPVRK LSQDEIKSVD EAIKSGPSAG GEPHSAANST LPPYLQICSR
AVTPDCIAYL YKIPKATGTN STNRLGIYES LGDVYSQEDL DLFYSKAAPY IPAGTGPQLD
LIDGATAPNS PANAGGESLL DFDMAIPIIY PQGTTLFQVK ADQYYNIFGD FLSAIDSDYC
SQDPLFNNHK MCGSYEPTNV ISISYGGPED PTDPKSAHRQ CNEFMKLGLM GITTVVASGD
AGVTDRNGYC LGPHHDIFVA DDLCSCPYIT AVGSTLIHTI DKPESATESF SSGGGFSNIF
TRPTWQDDVV GHYLLRHNPG YFAYNTSEGD IPGDAGIYNR GGRGFPDVAA VGDNGLVAVG
GSLGLSGGTS MSAPIVAAIL NRINEKRLSV GKGPIGFANP ALYAMSKRKG TFNDVTVGNQ
ELGGVGSDRG YSACGNNGFS AVEGWDPVTG LGTPVYDKWE AYFLQL
//
