ID   A0A0B7HYK0_9FLAO        Unreviewed;       726 AA.
AC   A0A0B7HYK0;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE            EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN   ORFNames=CCAND38_180068 {ECO:0000313|EMBL:CEN44505.1};
OS   Capnocytophaga canis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=1848903 {ECO:0000313|EMBL:CEN44505.1, ECO:0000313|Proteomes:UP000045051};
RN   [1] {ECO:0000313|EMBL:CEN44505.1, ECO:0000313|Proteomes:UP000045051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CcD38 {ECO:0000313|EMBL:CEN44505.1,
RC   ECO:0000313|Proteomes:UP000045051};
RA   Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL   Submitted (JAN-2015) 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; CDOI01000090; CEN44505.1; -; Genomic_DNA.
DR   RefSeq; WP_042343696.1; NZ_CDOI01000090.1.
DR   AlphaFoldDB; A0A0B7HYK0; -.
DR   Proteomes; UP000045051; 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   InterPro; IPR019500; Pep_S46.
DR   InterPro; IPR009003; Peptidase_S1_PA.
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   Reference proteome {ECO:0000313|Proteomes:UP000045051};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU366067}; Signal {ECO:0000256|RuleBase:RU366067}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT   CHAIN           18..726
FT                   /note="Dipeptidyl-peptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT                   /id="PRO_5023075793"
SQ   SEQUENCE   726 AA;  83368 MW;  1AB9BBC1CACBC177 CRC64;
     MKYVKLLLLF CSVSLYAQQG GMWIPSLLEG MNEKEMKSLG MRMSVSDIYS VNKSSLKDAV
     PHFNNGCTSE MISAQGLLLT NHHCGYGQIQ SHSTLKNDYL ADGFWAMSKS EELPNLGTVA
     TFIIRIEDVT EKILKGIENV SSETEKSNVI EKNTAELVKT SPKEAWQENR VRAFYNGNQY
     ILFVVENFKD VRLVGAPPSS IGKFGSDTDN WLYPRHTGDF ALFRIYADKN NRPAEYSKDN
     VPYRPKHFFP ISLDGISEDD FTMVFGYPGR TQEYLPSVAV EQIINVVNPA RIGIRDVVLK
     VQDGYMRKDQ AIKIKYASKY ARVANYWKKW IGESQGLKKS NAVAIKQQQE AIFVKNIEKD
     KKTEEYGAIL PEFSKKYKAF EPYSLSNELF NELMLRNIDF LTNGYRMYQL QLILEKRGQQ
     SFNDRKKNLL ETFKNVFKDY EKVVDRDVFE KAIVFYAENM PKQFLVENLR SFDSKKLADE
     LYGNSFLASY EEIEKVLSLS PQDFAQKLKD DKGMQFVTLM AENYVNNVLP TYQKLDAEIQ
     ALQRTYMKAI LEFSKPEDRI FPDANSTLRV TYGKVKGYAP ADAVYYSPVT YLEGVMEKYV
     PNDYEFDVPQ KLRDLYEKKD FGAYADKNGK MPVCFIATNH TTGGNSGSPA IDAHGNLIGL
     NFDRVWEGTM SDIHYDPEIC RNIMVDIRYV LFIIDKYAGA KHLIDEMRLV HPKKNTSSKK
     SKKKRK
//