ID A0A0Q5UVZ2_9FLAO Unreviewed; 235 AA.
AC A0A0Q5UVZ2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=(Alpha)-aspartyl dipeptidase {ECO:0000313|EMBL:KQS50285.1};
GN ORFNames=ASG38_04760 {ECO:0000313|EMBL:KQS50285.1};
OS Flavobacterium sp. Leaf359.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1736351 {ECO:0000313|EMBL:KQS50285.1, ECO:0000313|Proteomes:UP000051024};
RN [1] {ECO:0000313|Proteomes:UP000051024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf359 {ECO:0000313|Proteomes:UP000051024};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf359 {ECO:0000313|Proteomes:UP000051024};
RA Vorholt J.;
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 S51 family.
CC {ECO:0000256|ARBA:ARBA00006534}.
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:KQS50285.1}.
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DR EMBL; LMPW01000010; KQS50285.1; -; Genomic_DNA.
DR RefSeq; WP_056068257.1; NZ_LMPW01000010.1.
DR AlphaFoldDB; A0A0Q5UVZ2; -.
DR STRING; 1736351.ASG38_04760; -.
DR OrthoDB; 3373764at2; -.
DR Proteomes; UP000051024; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03146; GAT1_Peptidase_E; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR005320; Peptidase_S51.
DR PANTHER; PTHR20842:SF0; ALPHA-ASPARTYL DIPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR20842; PROTEASE S51 ALPHA-ASPARTYL DIPEPTIDASE; 1.
DR Pfam; PF03575; Peptidase_S51; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000051024};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
SQ SEQUENCE 235 AA; 26491 MW; D790D8B2C7E2D8E5 CRC64;
MKNLIIASTS TLHNGGYLEY LLPELSVHFK NVSELVFIPY ARPSGISHDE YTEKVRQAFS
KINIKVKGLH EFEDPKEALK QAEGIFTGGG NTFLLVTQLY RHDLMTLLSE TLKKGTPYLG
TSAGSNITGL TMQTTNDMPI IYPPSFQTLG MIPFNLNPHY LDPDSNSTHM GETRETRIKE
FHQFNTLPVL GLREGSWLEV RNETITLKGS LKARLFRQNQ QPEELESGSD LSFLN
//
