ID A0A257K0A3_9FLAO Unreviewed; 714 AA.
AC A0A257K0A3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN ORFNames=CFE23_07375 {ECO:0000313|EMBL:OYU80783.1};
OS Flavobacterium sp. BFFFF1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2015557 {ECO:0000313|EMBL:OYU80783.1, ECO:0000313|Proteomes:UP000216055};
RN [1] {ECO:0000313|EMBL:OYU80783.1, ECO:0000313|Proteomes:UP000216055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFFFF1 {ECO:0000313|EMBL:OYU80783.1};
RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT formosa and its bacterial cohort.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the removal of dipeptides from the N-terminus of
CC oligopeptides. {ECO:0000256|RuleBase:RU366067}.
CC -!- SIMILARITY: Belongs to the peptidase S46 family.
CC {ECO:0000256|ARBA:ARBA00010491, ECO:0000256|RuleBase:RU366067}.
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:OYU80783.1}.
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DR EMBL; NKJE01000009; OYU80783.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257K0A3; -.
DR Proteomes; UP000216055; Unassembled WGS sequence.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070009; F:serine-type aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043171; P:peptide catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR019500; Pep_S46.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR PANTHER; PTHR38469; -; 1.
DR PANTHER; PTHR38469:SF1; DIPEPTIDYL-PEPTIDASE; 1.
DR Pfam; PF10459; Peptidase_S46; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU366067}; Hydrolase {ECO:0000256|RuleBase:RU366067};
KW Protease {ECO:0000256|RuleBase:RU366067};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU366067}.
SQ SEQUENCE 714 AA; 80417 MW; 253B986BBDE5CE15 CRC64;
MKKIILFLLL GLSAFPMRAD EGMWFLMFIE RLNHRDMEKM GLQLTADEIY SINHHSLKDA
IVQFNGGCTA EIVSKDGLVL TNHHCGYDAI AELSTAEQNY LKNGFWAKSR KQEMKPSSLF
VRFFVRMDDV SKRILAKLND KMTEAERDKA IAAETALIEK ENNEGGKYTV SVRSFFQGNE
FYYFVYQDYK DVRLVGTPPE SVGKFGGDTD NWEWPRHTGD FSMFRVYADK DGNPADYSEN
NVPLQPKHYL PVSLKGVKEN DFAMILGYPG RTNRWMPAGG IEQNVKFAYP AWVEGAKTGM
DQMKKYMDQD AGIRLMYASK YASTANYWKN RQGMIDALSK FGTAKTKAAQ EAKFDKWANK
SENKAKYGNA IANINKFYGM TNEKSRHDNY LQQLLRTSSY GTISRSLGKA LLDYASAAQE
ERDLQKPDLA MAIDEFFKEV YIPAERDILA AQLHLYATKA TGYKLAPMVD KLGKANNNDF
STYVTSAFEL SMFSSKERMK AFLEVPSAGM VTGDPLYALS TDLLAHLTSK SDEIAKAQND
YGAAFRNLVD GLRVSKMAPI KYPDANSTLR LTYGKVRSLP ADKRNDAKIN NYTTMEGMIK
KYKAGDEEFD LPARLMELNK NKDFGQYADK AGYMPVNFLT DNDITGGNSG SPVLNGKGEL
IGIAFDGNIE AMAGDVIFDP KLQRTINVDI RYVLWIIDKY AGAKNIVDEM TIVK
//