ID   B3S5K1_TRIAD            Unreviewed;       262 AA.
AC   B3S5K1;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|PROSITE:PS50240};
GN   ORFNames=TRIADDRAFT_63128 {ECO:0000313|EMBL:EDV21967.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV21967.1, ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV21967.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV21967.1,
RC   ECO:0000313|Proteomes:UP000009022};
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000256|ARBA:ARBA00007664}.
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DR   EMBL; DS985251; EDV21967.1; -; Genomic_DNA.
DR   RefSeq; XP_002115604.1; XM_002115568.1.
DR   AlphaFoldDB; B3S5K1; -.
DR   STRING; 10228.B3S5K1; -.
DR   MEROPS; S01.110; -.
DR   EnsemblMetazoa; TriadT63128; TriadP63128; TriadG63128.
DR   GeneID; 6756710; -.
DR   KEGG; tad:TRIADDRAFT_63128; -.
DR   CTD; 6756710; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   HOGENOM; CLU_006842_7_5_1; -.
DR   InParanoid; B3S5K1; -.
DR   OrthoDB; 2910936at2759; -.
DR   PhylomeDB; B3S5K1; -.
DR   Proteomes; UP000009022; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1.
DR   PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..262
FT                   /note="Peptidase S1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012655180"
FT   DOMAIN          39..262
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
SQ   SEQUENCE   262 AA;  28161 MW;  A2E547A2DDDA2739 CRC64;
     MKILVVIALF ACATAFRLPP AYKQVPQEPR FENDEDDKIV GGYEAKKHEF PFIISLQRYG
     SHFCGGSIVS STKVLTAAHC TRAVSYWQIT ANAGRHNVRT SESTGQSKSA SSMSEHWGYN
     SNTYRYDVAV VRLSSAFKFN SYVKTVTLSS SNPSSGTRVT VAGWGTLSSG GSSPSKLQKV
     DVYVDSYSSC NSDYSGIIDD YTMLCASSGG KDSCQGDSGG PLVRAGTSTQ VGVVSWGYGC
     ADSRYPGVYA KVAATRSWIN SQ
//