ID B3SBG1_TRIAD Unreviewed; 397 AA.
AC B3SBG1;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=TRIADDRAFT_61606 {ECO:0000313|EMBL:EDV19996.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV19996.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV19996.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV19996.1,
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 A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; DS985264; EDV19996.1; -; Genomic_DNA.
DR RefSeq; XP_002117586.1; XM_002117550.1.
DR AlphaFoldDB; B3SBG1; -.
DR STRING; 10228.B3SBG1; -.
DR MEROPS; A01.010; -.
DR EnsemblMetazoa; TriadT61606; TriadP61606; TriadG61606.
DR GeneID; 6758755; -.
DR KEGG; tad:TRIADDRAFT_61606; -.
DR CTD; 6758755; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_0_1; -.
DR InParanoid; B3SBG1; -.
DR OMA; GFEGMIF; -.
DR OrthoDB; 1120702at2759; -.
DR PhylomeDB; B3SBG1; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR Gene3D; 2.60.40.1960; -; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000009022}.
FT DOMAIN 70..380
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DISULFID 101..105
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 263..267
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 305..342
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 397 AA; 44797 MW; 3B0BF98AC56669AD CRC64;
MYKIRTPLAV LVAFLTFATA LQRIKLYNMV SLRQKLLEAG ITQNMLEAKY TRAHGKNGVE
LLKNYKDAYY YGKISVGTPP QEFTVLFSTG SSEMWIPSIL CGAECKAHNK YHHSKSITYI
PDGGKCFLQY GLGSVDGFMS EDVVNIAGIE IKNQSFIEVT EELSFFLTSA SFDGMVGLRH
KPHSNCDANS VLNNMLAQDL IKKKVFSFYF SRDEEGTAGG EIIFGGSDSR YYEGKFHYTN
VIHKGSWIIK VDSGTVNRGV KFCTHGCTAI IETGTSLIFG PSKDIQRIQH AIGAQKIGGQ
NFIDCTRIKS LPKITFTIDK IRYTLDPEHY VHQYTLKGNK HCISGFLELE EEEDTWIFGD
VFLRSYYTEF DVGKDRIGFA KLKKKYSSSR YLNLLQS
//