ID Q6VGA5_9ALVE Unreviewed; 287 AA.
AC Q6VGA5;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=subtilisin {ECO:0000256|ARBA:ARBA00023619};
DE EC=3.4.21.62 {ECO:0000256|ARBA:ARBA00023619};
DE Flags: Fragment;
OS Perkinsus marinus.
OC Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC Perkinsus.
OX NCBI_TaxID=31276 {ECO:0000313|EMBL:AAQ54746.1};
RN [1] {ECO:0000313|EMBL:AAQ54746.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=14735929;
RA Brown G.D., Reece K.S.;
RT "Isolation and characterization of serine protease gene(s) from Perkinsus
RT marinus.";
RL Dis. Aquat. Organ. 57:117-126(2003).
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}.
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DR EMBL; AY340228; AAQ54746.1; -; mRNA.
DR AlphaFoldDB; Q6VGA5; -.
DR MEROPS; S08.041; -.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07473; Peptidases_S8_Subtilisin_like; 1.
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; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034204; PfSUB1-like_cat_dom.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 2: Evidence at transcript level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 1..220
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 261..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 42
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 206
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAQ54746.1"
FT NON_TER 287
FT /evidence="ECO:0000313|EMBL:AAQ54746.1"
SQ SEQUENCE 287 AA; 29318 MW; 7E9BDAD2E61D3C76 CRC64;
VDSGVDVSHP DLINQFWKNP DDGSIGFNFL DDNTNVTDEN GHGTHCAGIA GAQTNNSLGI
AGVADVKLMI LKFVGSDRTG PLSGALKALD YAVGMGAAVS SHSYGGNVPS RIFENAIRNA
ANAGHIVVAA SGNEGMNLDE TPTYPCSYSR SIPSMLCVGA SSSTPTSPVS LASFSNIGSV
VNIVAPGVNI LSTYLSGSYA FLSGTSMATP QVAGVAAVLA TLGLAGQSIT DSITRSRTAS
LENPLSLQNL GELDALNAVN EGLDQPTSPP RQPSSTRLSS SVCLWSV
//
