ID C5KIE9_PERM5 Unreviewed; 238 AA.
AC C5KIE9;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=subtilisin {ECO:0000256|ARBA:ARBA00023619};
DE EC=3.4.21.62 {ECO:0000256|ARBA:ARBA00023619};
GN ORFNames=Pmar_PMAR004415 {ECO:0000313|EMBL:EER15744.1};
OS Perkinsus marinus (strain ATCC 50983 / TXsc).
OC Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC Perkinsus.
OX NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN [1] {ECO:0000313|EMBL:EER15744.1, ECO:0000313|Proteomes:UP000007800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL Submitted (JUL-2008) 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. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; GG673160; EER15744.1; -; Genomic_DNA.
DR RefSeq; XP_002783948.1; XM_002783902.1.
DR AlphaFoldDB; C5KIE9; -.
DR EnsemblProtists; EER15744; EER15744; Pmar_PMAR004415.
DR GeneID; 9060425; -.
DR InParanoid; C5KIE9; -.
DR OrthoDB; 1330511at2759; -.
DR Proteomes; UP000007800; 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; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007800}.
FT DOMAIN 3..159
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
SQ SEQUENCE 238 AA; 24971 MW; 101B6FBE666DF422 CRC64;
MPLRVFGPDG VGDVRLALKA LNYAVENGAD LSSHSYGSSD FSATFRVAIS RAAEKGHLVV
AAAGNEGRDM SVDKVYPCAF TEQIDMLCVA SSGKRSNDRL APHSNYAAFV DIAAPGEEIP
STYPNNEYVY MTGTSMATPH VTGVAALLYA LGLSREDVSN SILASTDVLT TGLGSKNPYF
GRLNAAKAVE VALSKPTILA RESRSVGGDD CIPKTSAAGP VGNSLTAVFL FSVFYALF
//
