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Database: UniProt
Entry: A0A0G4G1P3_VITBC
LinkDB: A0A0G4G1P3_VITBC
Original site: A0A0G4G1P3_VITBC 
ID   A0A0G4G1P3_VITBC        Unreviewed;       855 AA.
AC   A0A0G4G1P3;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=subtilisin {ECO:0000256|ARBA:ARBA00023619};
DE            EC=3.4.21.62 {ECO:0000256|ARBA:ARBA00023619};
GN   ORFNames=Vbra_16640 {ECO:0000313|EMBL:CEM21650.1};
OS   Vitrella brassicaformis (strain CCMP3155).
OC   Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX   NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM21650.1, ECO:0000313|Proteomes:UP000041254};
RN   [1] {ECO:0000313|EMBL:CEM21650.1, ECO:0000313|Proteomes:UP000041254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhu J., Qi W., Song R.;
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins with broad specificity for peptide
CC         bonds, and a preference for a large uncharged residue in P1.
CC         Hydrolyzes peptide amides.; EC=3.4.21.62;
CC         Evidence={ECO:0000256|ARBA:ARBA00023529};
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073}.
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DR   EMBL; CDMY01000542; CEM21650.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4G1P3; -.
DR   VEuPathDB; CryptoDB:Vbra_16640; -.
DR   InParanoid; A0A0G4G1P3; -.
DR   PhylomeDB; A0A0G4G1P3; -.
DR   Proteomes; UP000041254; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000041254}.
FT   DOMAIN          435..651
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
SQ   SEQUENCE   855 AA;  93259 MW;  B8E9923E5FB069B8 CRC64;
     MRSHHHVFFR RGAFIAAFVL LAGIFDQHHP ASAQAFPFPN FSLPKLPWDS APSPSSPTPK
     SASHRDDDAL VHHPLCDWLK QQKQAIQDAA DHFIDATSST STTSHEVPIP LYEQKNAGET
     ERYVIEGGAY NNRQQRESAG LFGLGLLPTY EDSSQPKIEW TSLVKSMLVR RASDDELNHL
     SNSKPFQLVG LQVSLPRKID KKVEELLAEM EGELGGEGGA AASEAERETM AEEQVDLVVR
     AVLREELQLS AQDAMQKAYA KGHVTTHKER KQHMTKIHEE RDALIKSIMQ PIREKVEAMG
     GQGREIFSIS PTMRITLPLG RVRELVSMDE VELVYKEEEF EKEVCDGSDL RKIHQFDNFL
     DDGYTGEGPK GSSPDIPIGV FEIATINPHH PGWLDCGDGI EEEGTHGEAC INGKFGRFIK
     TFSCIQESGC NETSTLNRPY DEHAMGVASV LFGDVTGGQD PGIQDKIAQV ARSGGATEAS
     AFFFELGPST LALQRALDAI LLYEKTMSTD GPFIVNYSAG IIEGESDCSG TDGVSRMAND
     FFRAGRVFVK SAGNQGGGGG KRCTVTRPGS AHGILTIGSL GDTPDLMDDE RCEAEHISSF
     SSRGGDGDRS IVDLVAQGCW SSMYDTDAGY TNKACGTSFA APVVAAAAAV FADWYLNSPI
     GSLIEDPGVL MAAMLMMGDR GSSSGSKRLE KGFDPLWGAG ALRLRRFDDA GLDDPWRWAL
     GWTCIDDGEI LELQVNEGKK IDKDVDSFTG VIFWFDENAE QGLAYADLDL ILKTADGDEI
     MVTSASQFDN KERVWSDKVG GKSIKLEVTG YGIPTTRADP ICGDASQKVY YGWYFEDHDR
     DDSNGPTLAQ ASVNV
//
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