ID   A0A1I0VV87_9PSEU        Unreviewed;       541 AA.
AC   A0A1I0VV87;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Alpha/beta hydrolase fold {ECO:0000313|EMBL:SFA79596.1};
GN   ORFNames=SAMN05216266_101481 {ECO:0000313|EMBL:SFA79596.1};
OS   Amycolatopsis marina.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=490629 {ECO:0000313|EMBL:SFA79596.1, ECO:0000313|Proteomes:UP000243799};
RN   [1] {ECO:0000313|Proteomes:UP000243799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3568 {ECO:0000313|Proteomes:UP000243799};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
CC       {ECO:0000256|ARBA:ARBA00010088}.
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DR   EMBL; FOKG01000001; SFA79596.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0VV87; -.
DR   STRING; 490629.SAMN05216266_101481; -.
DR   OrthoDB; 4273853at2; -.
DR   Proteomes; UP000243799; 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; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SFA79596.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243799};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..541
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017397580"
FT   DOMAIN          112..285
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   DOMAIN          433..530
FT                   /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08386"
FT   REGION          145..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   541 AA;  58709 MW;  3281FF0CD8F8D785 CRC64;
     MKKLRLAVVI PAMAGSLLAG VTPAMAVTPD AEDAAALPLN STDIPARYAN QVLDWHGCTA
     DELPSAPPPG AEDIECATFT TPRNWDRIGE NVDLSIAVSR LKATDGEAKA SVVTNPGGPG
     APGRSFPARL RNQDKLRAQQ EIVGFDPRGT GKSTNITCGG AIGTGSSLDP RDRDRRNLNL
     ILDATRYAAR SCQVKSGELG PLINTRQTVR DIDLLRVLLG RDKINWVGYS AGTWMGAHYA
     TAFPERTGRF VLDSATEFTT NWQKSFDWQP LGFERRWRQD FLPWMAKYDS IYHFGTTGEA
     ARQTYEDLRA ALANEPIELD GETVGPNELD STIAGSLYNK RAFIGLAEHM VNLRTLTGDA
     STAQKAEAAE EVRVKVAAEP DVFGPQPLMV PVDYSDAYDA SFWTIPCNEG HWRGNRASVI
     RQSQHLIDQD LPLLGAGWLI QPCIFWKNKP IALPDVDGEG VPPVLIVQSV HDPATPLEGA
     QRAHRAFENS RMLTITDEGD HGIYAGGNAC ADDVVEKYLV DGIVPNDSSC PGMPLPVPSG
     D
//