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
//
