ID   A0A229TEL8_9PSEU        Unreviewed;       536 AA.
AC   A0A229TEL8;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Peptidase {ECO:0000313|EMBL:OXM69440.1};
GN   ORFNames=CF165_07905 {ECO:0000313|EMBL:OXM69440.1};
OS   Amycolatopsis vastitatis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=1905142 {ECO:0000313|EMBL:OXM69440.1, ECO:0000313|Proteomes:UP000215199};
RN   [1] {ECO:0000313|Proteomes:UP000215199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H5 {ECO:0000313|Proteomes:UP000215199};
RA   Adamek M., Alanjary M., Sales-Ortells H., Goodfellow M., Bull A.T.,
RA   Kalinowski J., Ziemert N.;
RT   "Comparative genome mining reveals phylogenetic distribution patterns of
RT   secondary metabolites in Amycolatopsis.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
CC       {ECO:0000256|ARBA:ARBA00010088}.
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:OXM69440.1}.
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DR   EMBL; NMUL01000007; OXM69440.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A229TEL8; -.
DR   OrthoDB; 4006962at2; -.
DR   Proteomes; UP000215199; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR013595; Pept_S33_TAP-like_C.
DR   PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR   PANTHER; PTHR43248:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   Pfam; PF08386; Abhydrolase_4; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..536
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012579084"
FT   DOMAIN          101..263
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   DOMAIN          421..521
FT                   /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08386"
SQ   SEQUENCE   536 AA;  57480 MW;  843F8F63E96B3780 CRC64;
     MRSFALVGAL VAGVGLAGTA GTAAAAEDSV VKPAVVGATA AVTWGTCSAD TLAGVPADQV
     KFYSCARYRV PIDHDNAALG TIDIALLKRA ARTPDKRVGS LFLNPGGPGG SGLRMPISGQ
     YYFQPQVLDR FDLVGFDPRG VGQSNPLRCF TTQEDADEVF SAQIPVPLTR AQISGTLASY
     RDYGRFCKNN AGSLLNHMST KDVVRDLDTL RAAVGDQKLT YVGFSYGTLI GSTYTSMFPK
     QSRAIVIDGN VDPALRTSDG VEYDRERAQG FEISLDGFLK RCDQVGAKCA FSDGNPRAKF
     DELREYLRKQ PITLPSGTVD INQFTGAVSS VLYSPGAFPG LAEDLQALYT AIHPAGAQAQ
     ALQGRPLKVI TKGKRGLADQ NPDSPYTSDD SYFAVNCSDK PFKISQEQVP SIAAKWERES
     PTFGRYQAFA DTAGCPVWPA KRPDVYRGPW RAKTDVPVVV VSNYYDPATQ YKFGQRMAAE
     LGNSRLLSVD AFGHCILGDA LGVDKAVADY LTDLKVPAAG QVFQPNVQPF ETAAQG
//