ID A0A0A2VID9_BEABA Unreviewed; 678 AA.
AC A0A0A2VID9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 22-FEB-2023, entry version 18.
DE RecName: Full=Prolyl endopeptidase {ECO:0000256|RuleBase:RU368024};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU368024};
GN ORFNames=BBAD15_g8605 {ECO:0000313|EMBL:KGQ06082.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ06082.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ06082.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ06082.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S9A family.
CC {ECO:0000256|ARBA:ARBA00005228, ECO:0000256|RuleBase:RU368024}.
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:KGQ06082.1}.
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DR EMBL; ANFO01000875; KGQ06082.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2VID9; -.
DR HOGENOM; CLU_011290_4_0_1; -.
DR Proteomes; UP000030106; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR023302; Pept_S9A_N.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002470; Peptidase_S9A.
DR PANTHER; PTHR42881; PROLYL ENDOPEPTIDASE; 1.
DR PANTHER; PTHR42881:SF13; PROLYL ENDOPEPTIDASE; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR Pfam; PF02897; Peptidase_S9_N; 1.
DR PRINTS; PR00862; PROLIGOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU368024};
KW Protease {ECO:0000256|RuleBase:RU368024};
KW Reference proteome {ECO:0000313|Proteomes:UP000030106};
KW Serine protease {ECO:0000256|RuleBase:RU368024}.
FT DOMAIN 6..406
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 471..676
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 678 AA; 75758 MW; 10FD073F56DC9C69 CRC64;
MTQPVIQDLL NQLETPEDAA ALRWVENQNK RTTDRFATGE RFQQMRGSIL QSLDDKTNIP
WGSHYRNTVY NFRQDDEHPR GIWRRTSESS YFTADPEWET VLDVDRLNEE EGANWSYHGA
DLLHPDYSRA LIFLSSGGDA CEIREFDLVS KTFISGGFFL PESKSSVSWL DENTLLLALD
AGDDTLTTSG YPRSVYRWAR GTSPQDAPLI YAGEATDMAV SAWHDDTPGF ERDVVHCSKD
FYHGQTWLLT GQNTLTLIDV PTDASCGFFK DWLLVTLTSD WPIAETVWPA GALLAIDLAA
FQRGERNFIP LFTPNSRTTL QGYSSTRDYL LLNLSQDAVE KVEFVKIDHG QRHCIKTLEL
PDFTNVSASG IDDESNRYRL VSHGFLQPNS LSYGDLDSDT LNLIKQDPAC FDAAAFNVTQ
HFALSLDGTR VPYFQVAAKA LALSGDNPTL LYGYGGFEVS LTPHYLGSKG ATWLQKGGVY
IVANIRGGGE YGPAWHQAAL KQHRHRAWED FTAVATDLAA RKVTCATRLA AQGGSNGGLL
IGNMLTDYPG LFGALVCEVP LLDMLNYHRW LAGASWIAEY GDPDIAEERE WLRRYSPFDK
VSADVGYPPT LFTTGTQDDR VSPAHARRMV ARMQQQGHEN VWLYEETEAG HGSAPENSQI
AAHQAMIEEF LWQMLTGK
//