ID   W4S3T3_9XANT            Unreviewed;       732 AA.
AC   W4S3T3;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Dipeptidyl peptidase IV {ECO:0000313|EMBL:GAE50813.1};
GN   ORFNames=XPU_2345 {ECO:0000313|EMBL:GAE50813.1};
OS   Xanthomonas arboricola pv. pruni str. MAFF 311562.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=1414836 {ECO:0000313|EMBL:GAE50813.1, ECO:0000313|Proteomes:UP000019143};
RN   [1] {ECO:0000313|EMBL:GAE50813.1, ECO:0000313|Proteomes:UP000019143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 311562 {ECO:0000313|Proteomes:UP000019143};
RA   Fujikawa T., Nakazono-Nagaoka E.;
RT   "Genome sequence and analysis of Xanthomonas arboricola pv. pruni.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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:GAE50813.1}.
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DR   EMBL; BAVB01000273; GAE50813.1; -; Genomic_DNA.
DR   Proteomes; UP000019143; Unassembled WGS sequence.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002469; Peptidase_S9B_N.
DR   PANTHER; PTHR11731:SF193; DIPEPTIDYL PEPTIDASE 9; 1.
DR   PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR   Pfam; PF00930; DPPIV_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..732
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004848100"
FT   DOMAIN          126..451
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          547..730
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   732 AA;  80612 MW;  C9542063266A13ED CRC64;
     MRALFAALAL MLSTITTAHA EKLTLDAITG PLPLSGPTLM KPKVAPDGSR VSFLRGRDSD
     RNQLDLWEYD IASGQTRLLV DSKLVLPGTE TLSDVEKARR ERQRIAAFAG IVDYQWAPDA
     HALLFPLGGE LYLYDLRKTG AAAVRKLTHG EGFATDAKLS PRGGFVSFVR ERNLWVIDLA
     SGKQLQLTSD GSDTIGNGVA EFVADEEMDR HTGYWWAPDD SAIAFARIDE SGVPVQKRPE
     VYADHTEVIS QRYPQAGQPN VAVRLGVTAP RANAAPRWIE LGNNPDIYLA RVDWRDAQRL
     TFQRQSRDQK TLELIETTLA SGKQRVLITE TSPTWVPLHN DLRFLKDGRF IWNSERSGYE
     HLYVASEDGR TLTPLTSGAW VVDALLAVDE QAGTVYFSAS KESPTQAHIY AVPLAGGAIE
     KRSTPHGTHA ASFANNASVY VDSWSNTATP PQIELFRANG EKIATLLKND LADPQHPYAR
     YRDAQRPVEF GTLTAADGTT PLQYRLIKPD NFDPSKRYPV MVYVYGGPAA QTVLDAWPSR
     GDALFDQYLA QRGYVVFSLD NRGTPRRGRD FSGALYGRQG TVEVDDQLQG VAWXIGVQGW
     SNGGYMTLML LAKHSEAYAC GVAGAPVTDW GLYDTHYTER YMDLPAGNAD GYRDARIATH
     LDGLRAKLLL IHGMADDNVL FTNSTALMSA LQARGTAFEL MTYPGAKHGL SGSTALHRYK
     TAEAFIQRCL MP
//