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Database: UniProt
Entry: S0GNQ0_9BACT
LinkDB: S0GNQ0_9BACT
Original site: S0GNQ0_9BACT 
ID   S0GNQ0_9BACT            Unreviewed;       719 AA.
AC   S0GNQ0;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE            EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN   ORFNames=C803_02871 {ECO:0000313|EMBL:EOS17237.1};
OS   Parabacteroides goldsteinii dnLKV18.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=1235789 {ECO:0000313|EMBL:EOS17237.1, ECO:0000313|Proteomes:UP000014140};
RN   [1] {ECO:0000313|EMBL:EOS17237.1, ECO:0000313|Proteomes:UP000014140}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=dnLKV18 {ECO:0000313|Proteomes:UP000014140};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Xavier R., Kuhn K., Stappenbeck T., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Parabacteroides goldsteinii dnLKV18.";
RL   Submitted (APR-2013) 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:EOS17237.1}.
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DR   EMBL; ASSQ01000014; EOS17237.1; -; Genomic_DNA.
DR   RefSeq; WP_010802002.1; NZ_KE159519.1.
DR   AlphaFoldDB; S0GNQ0; -.
DR   PATRIC; fig|1235789.3.peg.2869; -.
DR   HOGENOM; CLU_013776_0_0_10; -.
DR   Proteomes; UP000014140; 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}; Signal {ECO:0000256|RuleBase:RU366067}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT   CHAIN           20..719
FT                   /note="Dipeptidyl-peptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT                   /id="PRO_5023152896"
SQ   SEQUENCE   719 AA;  81920 MW;  B2D307967EF36930 CRC64;
     MKKILLSVLA AALSLPAVAD EGMWLLPLLQ QQKFPEMQAL GLKLQDYDIY SPDSASLKDA
     VVIFGGGCTG EIVSPDGLLL TNHHCGYGQI QQHSTLEHDY LTDGFWATTR EQELPNPGLT
     VTFIDKIEDV TDYVKKELEK DTDPQSMNFL SPKYLNGLAK AKVGEKFLQD NPGTEVEIKA
     FYGGNVYYMF TKKIYSDIRL VGAPPSSVGK FGADTDNWMW PRHTGDFSVF RVYADANGNP
     AEYSESNVPL RPKRWFKISV KGVEEDDYAM MMGFPGRTNK YYTSWEVAER RDIDNTVRIN
     IRNLRQEVML DEMLKDPSVR IQYASKYAGS TNAYKNAIGS NWAIKKRNFE QVKKEEQDRL
     IAWAQKNNES SYPEALLTLE QIVSDRKDLR FRSWMLDEAI LRGIEFTKVP TEVQSVSDAL
     KGKDRNEQQK QIRLLDMAYH RFADKDYAPE VDKKIAKVML KEYRRLVPAK SQPAYFSLID
     KKFKGDVDRF VDYLFDKSIY GSEENFDKFK TRPSVKALEQ DPMILFAKSV QEEKANLNAA
     LADFDSGYAL AHKEYVKGLL AMYQDKANFP DANFSLRLTY GQVKGYRPKD AVYYNCQTTL
     DGVMEKEDST NWEFVVPSRL KALYEAKDFG RYQMPDGRMP VAFSATTHTT GGNSGSPVLN
     ANGELIGINF DRNWEGVGGD IQYLPDYQRS IIVDIRYVLF LIDKYAGAGY LLEEMDLVE
//
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