ID   A0A0T6AP89_9BACT        Unreviewed;       116 AA.
AC   A0A0T6AP89;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Aspartyl protease {ECO:0008006|Google:ProtNLM};
GN   ORFNames=XU14_C0027G0005 {ECO:0000313|EMBL:KRT76864.1};
OS   Armatimonadetes bacterium CSP1-3.
OC   Bacteria; Armatimonadota.
OX   NCBI_TaxID=1640515 {ECO:0000313|EMBL:KRT76864.1, ECO:0000313|Proteomes:UP000051026};
RN   [1] {ECO:0000313|EMBL:KRT76864.1, ECO:0000313|Proteomes:UP000051026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSP1-3 {ECO:0000313|EMBL:KRT76864.1};
RA   Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA   Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT   "Critical biogeochemical functions in the subsurface are associated with
RT   bacteria from new phyla and little studied lineages.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KRT76864.1}.
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DR   EMBL; LDXQ01000027; KRT76864.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0T6AP89; -.
DR   Proteomes; UP000051026; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   Pfam; PF13650; Asp_protease_2; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
PE   4: Predicted;
SQ   SEQUENCE   116 AA;  12411 MW;  529B8A19DC03C2C8 CRC64;
     MGIVYVDGIA RGPSGEATVR FLADSGATYS VLPSDVWQGI GLTPRRTVTF SLADGTTIDR
     RISECYFILP QGEGTSPVVL GEPGDYALLG VLTLEALGLV LNPFTRELQP MRLLLV
//