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Database: UniProt
Entry: A0A0Q4YM37_9BURK
LinkDB: A0A0Q4YM37_9BURK
Original site: A0A0Q4YM37_9BURK 
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
//
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