ID A0A074ME94_ERYLO Unreviewed; 356 AA.
AC A0A074ME94;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=2-alkenal reductase {ECO:0000313|EMBL:KEO91090.1};
GN ORFNames=EH31_00040 {ECO:0000313|EMBL:KEO91090.1};
OS Erythrobacter longus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1044 {ECO:0000313|EMBL:KEO91090.1, ECO:0000313|Proteomes:UP000027647};
RN [1] {ECO:0000313|EMBL:KEO91090.1, ECO:0000313|Proteomes:UP000027647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6997 {ECO:0000313|EMBL:KEO91090.1,
RC ECO:0000313|Proteomes:UP000027647};
RA Zheng Q.;
RT "A comprehensive comparison of genomes of Erythrobacter spp. strains.";
RL Submitted (APR-2014) 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:KEO91090.1}.
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DR EMBL; JMIW01000001; KEO91090.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074ME94; -.
DR STRING; 1044.EH31_00040; -.
DR eggNOG; COG0265; Bacteria.
DR Proteomes; UP000027647; 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; 2.40.10.10; 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:UP000027647};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..356
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001697111"
FT DOMAIN 244..343
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 356 AA; 37760 MW; D9B683223D1ECDD6 CRC64;
MNIALLSAVG SLLLLQSAPA AETPIVTPRG DLGADERATI DLFQNARGSV VFISTRERVT
NFWTRNVYTV PRGSGSGLVW DNAGHIVTNY HVIEGASEAQ IQLVDGREFN ARLVGVSPQH
DLAVLKIGGA GFAAPRRIPI GTSSDLQVGQ NVFAIGNPFG LDWTLTKGIV SALDRSLPNE
GGPDIRHLIQ TDAAINPGNS GGPLLDSAGR LIGINTAIYS PSGASAGIGF AVPVDTVMRV
VPQLIENGRY IRPTLGIESD DDINDRLKRA ADIEGVFVLR VAPGSVADRA GLIPARRTRR
GVVPGDIVVA LNGRPVDRVG DLLARLDDFS VGERVELTLL RSGDRRRVNL QLEAGN
//
