ID E9FC24_METRA Unreviewed; 348 AA.
AC E9FC24;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 2.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Peptidase S1/S6, chymotrypsin/Hap {ECO:0000313|EMBL:EFY94699.2};
GN ORFNames=MAA_09823 {ECO:0000313|EMBL:EFY94699.2};
OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS anisopliae (strain ARSEF 23)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655844 {ECO:0000313|EMBL:EFY94699.2, ECO:0000313|Proteomes:UP000002498};
RN [1] {ECO:0000313|EMBL:EFY94699.2, ECO:0000313|Proteomes:UP000002498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
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).
RN [2] {ECO:0000313|EMBL:EFY94699.2, ECO:0000313|Proteomes:UP000002498}
RP GENOME REANNOTATION.
RC STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFY94699.2}.
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DR EMBL; ADNJ02000011; EFY94699.2; -; Genomic_DNA.
DR RefSeq; XP_007826012.2; XM_007827821.2.
DR AlphaFoldDB; E9FC24; -.
DR MEROPS; S01.103; -.
DR GeneID; 19264109; -.
DR KEGG; maj:MAA_09823; -.
DR HOGENOM; CLU_006842_7_5_1; -.
DR OrthoDB; 2486832at2759; -.
DR Proteomes; UP000002498; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1.
DR PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..348
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003236421"
FT DOMAIN 26..249
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 252..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 348 AA; 36872 MW; 2DB2781477BAC939 CRC64;
MVPNIAIALA AFSVVSSAAT TIDKRVIGGE NAKDGEFPFI VSLSRKEGQC SGSLLDSTTV
LTVAHCLEGQ FTSVRAGTLN RRMGGVTANI ASAIEHPSYI KGHGVHDIAI LKLSTPIERN
ETIGIDYAVL PENGSDPAPN STAITAGWGV QGNGDPDRNG AVDKLAKVVI PVHPRQDCRL
RFHPPEAHPD TICAGVNGKD ACLGDSGGPL IDQETGQLIG LVSRGQCTKP PTVYTRVGSY
IPWIKDHLGG VGSGPDPISP TSSLLPEGTP TPGQKRPWIE PINYSVITGC GFTENREEKC
GTETYCGLFD WSPATDGAFK NSKECFDAHV PKPKAARASF PRTTRHQQ
//
