ID   A0A161SCX3_9FLAO        Unreviewed;       717 AA.
AC   A0A161SCX3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE            EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN   ORFNames=AV926_12860 {ECO:0000313|EMBL:KZE78335.1};
OS   Myroides marinus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Myroides.
OX   NCBI_TaxID=703342 {ECO:0000313|EMBL:KZE78335.1, ECO:0000313|Proteomes:UP000076630};
RN   [1] {ECO:0000313|EMBL:KZE78335.1, ECO:0000313|Proteomes:UP000076630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L41 {ECO:0000313|EMBL:KZE78335.1,
RC   ECO:0000313|Proteomes:UP000076630};
RA   Hong K.W.;
RT   "Whole genome sequencing of Myroides marinus L41.";
RL   Submitted (JAN-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}.
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:KZE78335.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LQNU01000065; KZE78335.1; -; Genomic_DNA.
DR   RefSeq; WP_038984401.1; NZ_LQNU01000065.1.
DR   AlphaFoldDB; A0A161SCX3; -.
DR   OrthoDB; 9805367at2; -.
DR   Proteomes; UP000076630; 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   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU366067}.
SQ   SEQUENCE   717 AA;  81547 MW;  F0789896E7C29DE6 CRC64;
     MNKKIKNLFK ALVVLVALPI YAQQGGMWIP SLLKGMNETE MKSLGMKMSV NDIYDVNKSS
     MKDAAPHFNG GCSSEVISPQ GLLLTNHHCG YGQIQAHSTV ENDYLANGFW AKSMAQELPN
     ENLEVTFIVR IEDVTKEVMA GIKDKDSELQ KQAKISENIA KTVASFPKEK WQENKIKSFY
     EGNQYIIFVT ETFKDVRLVG APPSSIGKFG SDTDNWVWPR HTGDFSLFRI YADKDNKPAA
     YSKDNVPYRP KHFFPISLSG IEEGDFTMVF GYPGRTQEYL PSYAVEQIVN DLNPVRIGIR
     DKALKITDEF MRADQGIKIQ YASKYASTAN YWKKWIGESQ GLKKTNAVQA KQDFEKGFIE
     RAKKNKNTKA YADILPKFEK LYGEITPYAI SKDFFAEVVQ RNTELLSAAY KVYALESYAS
     NEKSFESRRA NLIKGQEKFY KNFSKEVDEK VFEAIVAMYA KDAPKQFLPK ELKDANISAI
     SKDIYTNSKL TSYEGFKQLL EGDAKQVIKN INNDKGYVFA KALIENYMSN VLPKYEELDR
     EIAALQRTFM KAQLELYPDA RIFPDANSTL RVTYGKVDGY FPKDATYYEP VTHLEGIMEK
     YVPGDYEFDV PAKLVELYNN KDYGQYADNG KLPVNFIATN HTTGGNSGSP ALDAYGNLIG
     LNFDRVWEGT MSDIYYDPSI CRNIMVDARY ILFIIDKFAD AKHLIDEMKL VEPKKNK
//