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Database: UniProt
Entry: A0A0S8C041_9PROT
LinkDB: A0A0S8C041_9PROT
Original site: A0A0S8C041_9PROT 
ID   A0A0S8C041_9PROT        Unreviewed;       383 AA.
AC   A0A0S8C041;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=2-alkenal reductase {ECO:0000313|EMBL:KPK16833.1};
GN   ORFNames=AMJ67_14180 {ECO:0000313|EMBL:KPK16833.1};
OS   Betaproteobacteria bacterium SG8_41.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1703391 {ECO:0000313|EMBL:KPK16833.1, ECO:0000313|Proteomes:UP000051544};
RN   [1] {ECO:0000313|EMBL:KPK16833.1, ECO:0000313|Proteomes:UP000051544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_41 {ECO:0000313|EMBL:KPK16833.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPK16833.1}.
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DR   EMBL; LJTT01000064; KPK16833.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8C041; -.
DR   STRING; 1703391.AMJ67_14180; -.
DR   PATRIC; fig|1703391.3.peg.2530; -.
DR   Proteomes; UP000051544; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00987; PDZ_serine_protease; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.40.10.120; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR   PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR   Pfam; PF13180; PDZ_2; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   4: Predicted;
FT   DOMAIN          272..338
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   383 AA;  40569 MW;  CB6A7775E6CEEA9B CRC64;
     MRKLWLVFAQ TATVCLAVLF VVSTLRPDLL SWRARSSVVT IKEPSVSTPA RETASFSEAA
     RKAMPAVVNI FTSQDLKRPR HPLQDDPVFR YFFGDPSDPS VQRREGLGSG VIVSETGYVL
     TNHHVIEAVD QIEVALADSR KVSARVVGAD PETDLAVLKI EVQDAPSITF ARSDRLKVGD
     VVLAIGNPFG VGQTVTLGIV SGLGRSHLGI ATFENFIQTD AAINPGNSGG ALVDAQGNLV
     GINTAILSQT GTAAGISYAI PVSIARQVME QIIQKGSVTR GWVGVGVQDI TKDLAESFKL
     STTSGVLISQ VERGGPADQA GVKPGDILVA VNNTLVNDSV GMLNLIAALA PGARARLKLL
     REQDATEVTV TVGRRPKLQP QKP
//
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