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Database: UniProt
Entry: A0A0A2GC14_9PORP
LinkDB: A0A0A2GC14_9PORP
Original site: A0A0A2GC14_9PORP 
ID   A0A0A2GC14_9PORP        Unreviewed;       715 AA.
AC   A0A0A2GC14;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE            EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN   ORFNames=HQ47_09020 {ECO:0000313|EMBL:KGN72991.1};
OS   Porphyromonas macacae.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=28115 {ECO:0000313|EMBL:KGN72991.1, ECO:0000313|Proteomes:UP000030103};
RN   [1] {ECO:0000313|EMBL:KGN72991.1, ECO:0000313|Proteomes:UP000030103}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COT-192 OH2859 {ECO:0000313|Proteomes:UP000030103};
RA   Wallis C., Deusch O., O'Flynn C., Davis I., Horsfall A., Kirkwood N.,
RA   Harris S., Eisen J.A., Coil D.A., Darling A.E., Jospin G., Alexiev A.;
RT   "Draft Genome Sequence of Porphyromonas macacae COT-192_OH2859.";
RL   Submitted (SEP-2014) 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:KGN72991.1}.
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DR   EMBL; JRFA01000025; KGN72991.1; -; Genomic_DNA.
DR   RefSeq; WP_036852173.1; NZ_JRFB01000011.1.
DR   AlphaFoldDB; A0A0A2GC14; -.
DR   STRING; 28115.HQ47_09020; -.
DR   eggNOG; COG3591; Bacteria.
DR   OrthoDB; 9805367at2; -.
DR   Proteomes; UP000030103; 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   Reference proteome {ECO:0000313|Proteomes:UP000030103};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU366067}.
SQ   SEQUENCE   715 AA;  81370 MW;  5DB759498877ECD1 CRC64;
     MRKTLKLFLI SSLLLIVFGF RAFADKGMWI MSELNKQNIE RMRELGFKLP IDSLYSLDKP
     SITNAVVIFG NGCTGITVSN EGLIFTNHHC GYEAIQSQST VDHDYLRDGF VSQNFAQELP
     IAGLEVRYLR SVRDVTKEIT DSLTSCKTEM ERLQKAKILC SKIAIAEQNK LGDNVEVIVE
     PFYANNAYYM IAYDVFKDVR MVFAPPSSIG KFGGDTDNWM WPRHTGDFSV FRVYAGKDNK
     PAGYNKENKP FRPKYYAAVS LAGVSKDDYA MTVGFPGSTS RYIPSWGIRS RIDNTNTPRI
     EVRGIKQEIW KEAMSADQAT RIKYASKYAQ SANYWKNSIG MNRGLEKLRV LDRKRMEEDA
     FQKWTGTNKK GEQYKETLSL LKNGYENSGS FKRNQTYIQE ALLTGAEVGL IALYANMAAM
     TPSSKAELLK HLNENVYKDY LPSLDRKVLP AMLKVVKERV PAEYLPDIYI TIDKDYGGDY
     KAYADHLFDT SIIPYADKLN EVMKLPADQL QAKLANDPAV VFCNSVRNIL QDINNKTMEA
     TMDISKGNRL YFAGRRVMDP NRQMPSDANF SMRMSYGSVK GYEPSDATWF SYYTTEKGIM
     EKYDPKSYEF NVQDEILNLI KKKDFGRYAA KDGHLHIAFL STNDITGGNS GSPVFDKNGR
     LIGLAFDGNW EAMSGDIEFE PDLQRTISVD IRYVLWTIDK WGKCPRLIKE LKLMK
//
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