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Database: UniProt
Entry: A0A257K0A3_9FLAO
LinkDB: A0A257K0A3_9FLAO
Original site: A0A257K0A3_9FLAO 
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
//
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