ID   A0A1H1ANC5_9FLAO        Unreviewed;       736 AA.
AC   A0A1H1ANC5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE            EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN   ORFNames=SAMN05421664_1486 {ECO:0000313|EMBL:SDQ40686.1};
OS   Chryseobacterium soldanellicola.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=311333 {ECO:0000313|EMBL:SDQ40686.1, ECO:0000313|Proteomes:UP000199627};
RN   [1] {ECO:0000313|EMBL:SDQ40686.1, ECO:0000313|Proteomes:UP000199627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17072 {ECO:0000313|EMBL:SDQ40686.1,
RC   ECO:0000313|Proteomes:UP000199627};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNKL01000002; SDQ40686.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1ANC5; -.
DR   STRING; 311333.SAMN05421664_1486; -.
DR   OrthoDB; 9805367at2; -.
DR   Proteomes; UP000199627; 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; PERIPLASMIC PEPTIDASE SUBFAMILY S1B; 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}.
FT   REGION          714..736
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   736 AA;  82793 MW;  1F6151183CEF6CA4 CRC64;
     MKRLFLLFTF LLGFAQMRAD EGMWLLMLIK RLNGVDMQKE GLHLTPEEIY SVNNSSLKDA
     IVSFGGFCTG EIVSDKGLIF TNHHCGYGAV AAASTPEKDY LKNGFWAMKQ KDEFNAKDLY
     VRFLVRMDDA TQRINSKLNN KMTAAERKAV IDAETKAIQS ENSENGKYTV VVRDFFNGNE
     FYYFVYQDYK DIRLVGAPPS SLGKFGGDTD NWEWPRHTAD FTVFRVYADA AGNPAEFSPS
     NVPLKPKHFL PVSLKGVKPG DFSMILGYPG RTNRYLTSYG IQQMVGKDYP AWVEASKLAM
     DVMKKYMDKD KGTQLNYASQ YASVANYWKN RQGTIDAVIK NGTITDKQKI EETFRAWAVQ
     PANIAEYESV LDDIAIYYKQ TSDRNVERNY MSQLSRNAKY FAIALQVGSV LKAYAKQDMA
     GRLAMKPKVE AALKTAYESI NTNLEGEMMN SMVNLYQTKV KADVASATIM GLDAKNLSNV
     AYSSIFANKT SATNFMLNPD PLKLDADPLW KIANSLIEDQ KISAEKFVKI DDNFAKNNRL
     FLAGLMKSMP EKKFYPDANS TMRLTYGTVD KLPIRDDRNY FGVTDNYYTD MTGLVGKYKK
     GDEEFDLPQR VIDLYNLKDF GQYADAKGYM PVNFLSNNDI TGGNSGSPVI DGDGNLIGIA
     FDGNSEALSG DIVFEQEWQK TINVDVRFVL WTIDKYAGAR RLIDELNLVR DENTPADTKT
     KAAKPDHVKA AGKKKK
//