ID E9DWM7_METAQ Unreviewed; 669 AA.
AC E9DWM7;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Alkaline serine protease AorO {ECO:0000313|EMBL:EFY92077.1};
GN ORFNames=MAC_02025 {ECO:0000313|EMBL:EFY92077.1};
OS Metarhizium acridum (strain CQMa 102).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN [1] {ECO:0000313|EMBL:EFY92077.1, ECO:0000313|Proteomes:UP000002499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY92077.1,
RC ECO:0000313|Proteomes:UP000002499};
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(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; GL698478; EFY92077.1; -; Genomic_DNA.
DR RefSeq; XP_007808365.1; XM_007810174.1.
DR AlphaFoldDB; E9DWM7; -.
DR MEROPS; S53.007; -.
DR GeneID; 19246336; -.
DR KEGG; maw:MAC_02025; -.
DR eggNOG; ENOG502QTN1; Eukaryota.
DR HOGENOM; CLU_013783_4_0_1; -.
DR InParanoid; E9DWM7; -.
DR OMA; FELANCD; -.
DR OrthoDB; 1405251at2759; -.
DR Proteomes; UP000002499; 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:EFY92077.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002499};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..669
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003234833"
FT DOMAIN 212..636
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
FT ACT_SITE 288
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 292
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 549
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 592
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 593
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 614
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 616
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ SEQUENCE 669 AA; 72124 MW; 466DF9E2AC1C63E4 CRC64;
MKFGLILLGG LMPAIVATPV DQYKVHEQRG PLHQQWIRGQ QASGSTFVPV RIALKQSNLE
KAKDYLLQVS DPASPKYGQH FTTQQVVDLF APSEQIINQV KTWLVSSGIS AGSIALSNSK
GWINFNTTAS ELESLLKTKF YLYTNNVTDG VYFGTEAYSL PHDVSSLVDL VMPGISFTQM
QKKTARIAHP SSSSKLHGAS IDPNGTDHCD TYVTPRCISA LYNIPPTRLA SPSNTMGIFE
TGGDVYSQED LNQFYAAAAP SIPKGTGPII NLINGATAPS PPSSAGPESD LDFEIAIPII
HPQKTSLYQI QYPPNAGYKN FNYIFNDFLD AFSGPYCHDD GDEASGKECN NLTAPNVLSV
SWGDSEDPSL VNFHKVRRHA GSQQKQTMQT NHGFAQRQCT EWMKYGLQGT SVFVASGDYG
VAENTCLGPK QNIFVPDGLC GCPYITAVGS TYLPKGAKVG DPEVATERFS SGGGFSNIFA
TPEWQSSAVS GYLTKHKPSY ESYNTTDGKL PTLGGIYNRG GRGYPDISAI GDNGVVVVGG
EQGTSGGTSM SAPLVAAIFN RINEERLNIG KSPVGFINPA LYKAYSKNAF NDITKGDQPG
GGGCGTTGFS AASGWDPVTG LGTPKYTQLL EYFLSLTRPR GWLPRRLLGL TVEQWSEKKQ
QYLPLAKDP
//
