ID   A0A2A2JZW3_9BILA        Unreviewed;       397 AA.
AC   A0A2A2JZW3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=WR25_15197 {ECO:0000313|EMBL:PAV67316.1};
OS   Diploscapter pachys.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX   NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV67316.1, ECO:0000313|Proteomes:UP000218231};
RN   [1] {ECO:0000313|EMBL:PAV67316.1, ECO:0000313|Proteomes:UP000218231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF1309 {ECO:0000313|EMBL:PAV67316.1};
RA   Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA   Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT   "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL   Curr. Biol. 0:0-0(2017).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PAV67316.1}.
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DR   EMBL; LIAE01009955; PAV67316.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2JZW3; -.
DR   STRING; 2018661.A0A2A2JZW3; -.
DR   Proteomes; UP000218231; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   InterPro; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966:SF45; ASPARTIC PROTEASE 6; 1.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   Pfam; PF00026; Asp; 2.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000218231}.
FT   DOMAIN          67..397
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   397 AA;  44223 MW;  7888A19CE87F1585 CRC64;
     MGSSIHDKVD SMVGPTAAFI IAEQLKATKV GDRFYYENAP EQTVRGLTDG ELAETRKATL
     GGMICRAFPS NIFKVPQNIF QTRVRMMESG EWSTYLKYEN EMRSNAKYGS IYGSLSQPVH
     DWGDFEYLGN ITIGTPDQQF LVVLDTDPQA MRNINLRFDK TKSSTYQENG KRLDALFRRA
     FFSKGLTHIP DATDGILGLA FQALAVDNVV PPLQNAINQG LLDQPLFTVW LEHRGNMNDA
     AGGVFTYGAV DTTNCGPLIA YQPLSSATYW QFKIAGISLG TYKNTQSYNV ISDTGTSFIG
     GPNAVISGLA KAAGATYHPQ DEAYYIDCNA NPGTVDIVIG TNTYSIQPVN YIVPDISRLA
     LLQVFRELQV FSQLKVLRQL KMFRQLKMFR QLKMFRQ
//