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Database: UniProt
Entry: A0A0A2V6R7_BEABA
LinkDB: A0A0A2V6R7_BEABA
Original site: A0A0A2V6R7_BEABA 
ID   A0A0A2V6R7_BEABA        Unreviewed;       442 AA.
AC   A0A0A2V6R7;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Pro-apoptotic serine protease NMA111 {ECO:0000256|ARBA:ARBA00020338};
DE   AltName: Full=Pro-apoptotic serine protease nma111 {ECO:0000256|ARBA:ARBA00021524};
GN   ORFNames=BBAD15_g11219 {ECO:0000313|EMBL:KGQ03546.1};
OS   Beauveria bassiana D1-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ03546.1, ECO:0000313|Proteomes:UP000030106};
RN   [1] {ECO:0000313|EMBL:KGQ03546.1, ECO:0000313|Proteomes:UP000030106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1-5 {ECO:0000313|EMBL:KGQ03546.1,
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   -!- FUNCTION: Nuclear serine protease which mediates apoptosis.
CC       {ECO:0000256|ARBA:ARBA00002558}.
CC   -!- SIMILARITY: Belongs to the peptidase S1C family.
CC       {ECO:0000256|ARBA:ARBA00010541}.
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:KGQ03546.1}.
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DR   EMBL; ANFO01001201; KGQ03546.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2V6R7; -.
DR   STRING; 1245745.A0A0A2V6R7; -.
DR   eggNOG; KOG1421; Eukaryota.
DR   HOGENOM; CLU_619608_0_0_1; -.
DR   Proteomes; UP000030106; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   PANTHER; PTHR46366; PRO-APOPTOTIC SERINE PROTEASE NMA111; 1.
DR   PANTHER; PTHR46366:SF8; PRO-APOPTOTIC SERINE PROTEASE NMA111; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW   Protease {ECO:0000313|EMBL:KGQ03546.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030106};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825}.
SQ   SEQUENCE   442 AA;  47092 MW;  B5C91B2FDF3E2446 CRC64;
     MELLLKLKAG GARARFLEVV GPAAELLPEL GPPRTTVKSP EFVGSTAGLL VKPGLPRTAV
     NWPEFGGFAA CPHSVSYKNA DVPTGQRVVA AICSTAGNML CEAVRQAFRG RAAKSSGCPA
     HQSRKDLSRI IRNIVVIRFS HTLPFDGDGA QTSEATGFVV DAKRGYILTN RHVAGPGPFW
     GLCIFGQEAV SCRPLYIDPI HDFAFLKYDP ESVQNMKIDG LSLSSGGASV GQPVLVVGND
     AGEATSIIDG AISRTDRNAP EYDGPYSDFN ISYYMANMNL SGGSSGSPAL GEDGLVLGMV
     SGRRTDGAIC FLLPTGPILR ILCRLRQGQD VPRGDIQCKF VMKPIHECKG LGLDSGWEER
     LRRQITASGG LLVASKVLVG GPSCGRILPG DILLEANGAV ALQFDELEDA FNENFSVSST
     SSIFTTSCQN VLYRWEAFSA MM
//
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