ID B3RTN0_TRIAD Unreviewed; 408 AA.
AC B3RTN0;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=CUB domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=TRIADDRAFT_55983 {ECO:0000313|EMBL:EDV25661.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV25661.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV25661.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV25661.1,
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR EMBL; DS985244; EDV25661.1; -; Genomic_DNA.
DR RefSeq; XP_002111694.1; XM_002111658.1.
DR AlphaFoldDB; B3RTN0; -.
DR STRING; 10228.B3RTN0; -.
DR MEROPS; S01.035; -.
DR EnsemblMetazoa; TriadT55983; TriadP55983; TriadG55983.
DR GeneID; 6753404; -.
DR KEGG; tad:TRIADDRAFT_55983; -.
DR CTD; 6753404; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_674984_0_0_1; -.
DR InParanoid; B3RTN0; -.
DR OMA; ESATNCK; -.
DR OrthoDB; 2952710at2759; -.
DR PhylomeDB; B3RTN0; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24252:SF8; ACROSIN; 1.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
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}.
FT DOMAIN 28..137
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 173..405
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 408 AA; 43665 MW; F33C1CA5CB2D8BEE CRC64;
MTLKKSVNYE DCHRFIVYFR LGYRQATCGS TSYAKSGTIE SPSYPSNYPR RTDCTSTVVA
SSDEVVTVTF SEFDVESATN CKYDYVSLYD GNTLRHTYCG KGSVPTFTTS PGSNFVLTFH
TDGSVQKKGF ALSFTVTKVA APTGSTTGTV STGTYNPGTC GKTAYKLSLT DRIVGGAECS
PKHALPWQVS LQTNTGFHFC GGSIISDRYV VTAAHCVDGQ TPTSWRIVLG AHNIGSNEPS
QFVATVKRAK MHPSYDTSTL SNDIAIIELN EKITFTNEIS PVCVSKTRIA DNADVIVSGW
GTLTAGGASP DTLQRVIVPT ISRSECSSTV YGTGYIDSTM LCAGLMSGGK DSCQGDSGGP
LVHDRSGTYY LEGVVSWGYG CADPNRPGVY ARVSSLYSFL ETETGLTF
//
