ID E9E8D0_METAQ Unreviewed; 916 AA.
AC E9E8D0;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Subtilisin-like protease {ECO:0000313|EMBL:EFY87880.1};
GN ORFNames=MAC_06128 {ECO:0000313|EMBL:EFY87880.1};
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:EFY87880.1, ECO:0000313|Proteomes:UP000002499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY87880.1,
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 -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; GL698520; EFY87880.1; -; Genomic_DNA.
DR RefSeq; XP_007812468.1; XM_007814277.1.
DR AlphaFoldDB; E9E8D0; -.
DR GeneID; 19250439; -.
DR KEGG; maw:MAC_06128; -.
DR eggNOG; KOG4266; Eukaryota.
DR HOGENOM; CLU_003559_3_1_1; -.
DR InParanoid; E9E8D0; -.
DR OMA; FNHPALG; -.
DR OrthoDB; 662485at2759; -.
DR Proteomes; UP000002499; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07489; Peptidases_S8_5; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR Gene3D; 2.60.40.1710; Subtilisin-like superfamily; 1.
DR InterPro; IPR010435; Fn3_5.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034187; Peptidases_S8_5.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF06280; fn3_5; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000002499};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..916
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003235539"
FT DOMAIN 166..583
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 627..742
FT /note="Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF06280"
FT ACT_SITE 175
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 214
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 550
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 916 AA; 97661 MW; 2A097A97D987D7E7 CRC64;
MHAMVTFLLA VAALAATPSA ANKTPSRVIP GTYFIELHED ADVAGFAHRV KREANARVRR
QIDYVPDKAK ATAPYKALSI EINDAGKINV VASMEGVVKI HPVEMHSLGG IAPPSDRAKG
EKQRSFVGKL SKRQATRRAL PETNTTAYPP HVMMQVDKLR SKGITGKGIK IAMIDTGVDY
EHPALGGCFG PGCLFSFGAD LVNNEPTPKD CNGHGTNAAG IIGARPNPMG FTGAAPGAQL
GMYRITCSGE FPSDVMVDAI YRALEEGVDI ISSSAGLPGG WPGSLLSSAA TRVVESGVVF
VQGAGNDGEL GLFSQLDPAV GSGVISVGSV HSRVSPELVV EAKYTIGNGS EVPFLFYPTA
PSDNFTGTPM EVYALPVNGS GAGNDTHACG PIRDDIPDLS DKLVLLHFRL SPGDCNLWTR
VKLVHEKGAT RILAYMASED WTPGLYYLDD FPEGVVGLGM LEFNSAKSML KALEAGRKVL
ATAFPYDDAP LVYVETPNEK VAGSVSSFSS WGPSWNLGLK PSLTAVGERI ITTSPRDQYI
SGYEITQGTS FSGPLIAAIV ALIGEARGSL DAATIESLLV SHSHPQLYHN RHGFLSYLAP
VAQQGGGLAR AYDAAYATTL VQPASLSFND TEHMHTAAPF SFTIKNMGAG VVTYRLSHVP
AVTVYTFTQN GTISSYPNKL DTLEVPATIT LSDTTVTVAP GNSVNIRVSA SAPKSLDPSR
MPLWSGWIAI NGSDSSSLSV PYQGFSGSIR KHQVLPPDGA TLVYRNVSVS EGTTVVLPTP
GSITTSQLML NINATLGTPL VRAEVVPLNS TANATNIATK PIGQLQGFPV QWRPSNLQQS
PDLLQFTQFK WNGQLDTGSN VPEGYYKLVV RALRIFGNPS NDEDWDISES PRFQITYCQK
RNSSTTVRRR AEKGYN
//