ID A0A0Q4YM37_9BURK Unreviewed; 358 AA.
AC A0A0Q4YM37;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=2-alkenal reductase {ECO:0000313|EMBL:KQP23589.1};
GN ORFNames=ASF43_02080 {ECO:0000313|EMBL:KQP23589.1};
OS Pseudorhodoferax sp. Leaf267.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1736316 {ECO:0000313|EMBL:KQP23589.1, ECO:0000313|Proteomes:UP000051560};
RN [1] {ECO:0000313|EMBL:KQP23589.1, ECO:0000313|Proteomes:UP000051560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf267 {ECO:0000313|EMBL:KQP23589.1,
RC ECO:0000313|Proteomes:UP000051560};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP23589.1, ECO:0000313|Proteomes:UP000051560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf267 {ECO:0000313|EMBL:KQP23589.1,
RC ECO:0000313|Proteomes:UP000051560};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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:KQP23589.1}.
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DR EMBL; LMMV01000001; KQP23589.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q4YM37; -.
DR STRING; 1736316.ASF43_02080; -.
DR Proteomes; UP000051560; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
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 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000051560};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..358
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006241071"
FT DOMAIN 247..329
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 358 AA; 37333 MW; AC765F5D562E337F CRC64;
MLHRLLCLAC TAALLAPPVF ARTDAAPRAI APRGPLGAEE LNNIAVFKAA SPSVVNITSL
ALEREMFSLN VQQVPQGTGT GFVWDTQGHI VTNFHVIQNA RGARVTLADQ SSHAAQLVGV
FPDRDLAVLK IDVPAAQLRA LPIGRSADLQ VGQAVYAIGN PFGLDQTLTT GIVSALNREI
ESVTRRTIRG AIQTDAAINP GNSGGPLLDS AGRLIGVNTA IYSPSGASAG IGFSIPVDEV
NRIVPRLIRD GRFVRPALGV AYAPAQLNRA LGLPRGVAIV RVQPGSPAAQ AGLRAFTRSE
RGVNAGDVIT AIGGEPVASA DDVLNALERL QPGDRAELTL WRGGSTRTGR VTLAASEE
//