ID M5D965_STEMA Unreviewed; 741 AA.
AC M5D965;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Dipeptidyl-peptidase 4 {ECO:0000313|EMBL:CCP18872.1};
DE EC=3.4.14.5 {ECO:0000313|EMBL:CCP18872.1};
GN ORFNames=SMRA8_4388 {ECO:0000313|EMBL:CCP18872.1};
OS Stenotrophomonas maltophilia RA8.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=1118157 {ECO:0000313|EMBL:CCP18872.1, ECO:0000313|Proteomes:UP000012177};
RN [1] {ECO:0000313|EMBL:CCP18872.1, ECO:0000313|Proteomes:UP000012177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA8 {ECO:0000313|EMBL:CCP18872.1,
RC ECO:0000313|Proteomes:UP000012177};
RA Linke B., Adamek M., Schwartz T.;
RT "Stenotrophomonas maltophilia SKK35 and RA8 Genome sequencing: Analysis and
RT Comparison of Viurlence genes.";
RL Submitted (JUL-2012) 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:CCP18872.1}.
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DR EMBL; CALM01001275; CCP18872.1; -; Genomic_DNA.
DR RefSeq; WP_006400853.1; NZ_CALM01001275.1.
DR AlphaFoldDB; M5D965; -.
DR MEROPS; S09.009; -.
DR Proteomes; UP000012177; Unassembled WGS sequence.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
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 Hydrolase {ECO:0000313|EMBL:CCP18872.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..741
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004065202"
FT DOMAIN 126..450
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 546..740
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 741 AA; 82218 MW; 5DB819417207033F CRC64;
MRHLFASLAL MLATSTAAHA EKLTLEAITG PLPLSGPTLM KPKVAPDGSQ VSFLRGKDSD
RNQLDLWTYD IGSGQTRLLV DSKVVLPGTE TLSDEEKARR ERQRIAAMTG IVDYQWSPDA
QRLLFPLGGE LYLYDLKQQG QAAVRQLTHG EGFATDAKLS PKGGFVSFIR GRNLWVIDLA
SGKQLQLTRD GSTTIGNGVA EFVADEEMDR HTGYWWAPDD SAIAFARIDE APVPVQKRYE
VYADRTDVIE QRYPAAGDAN VRVQLGVIAP AADAQPRWVD LGKEQDIYLA RVDWRDAQHL
SFQRQSRDQR QLDLVEVALD SNRQRVLAHE TSPTWVPLHN SLRFLDDGSV LWSSERTGFQ
HLYRIDSKGK ATALTHGNWP VDELLAVDEK AGKAYFRAGI ETSRESQIYA VSLQGGEPQR
LSKAPGMHSA SFARNASVYV DSWSNSTTPP QIELFRANGE KIATLLENDL ADPKHPYARY
RDAQRPIEFG TLTAADGKTP LNYSLIKPAG FDPNKRYPVA VYVYGGPASQ TVTDSWPGRG
DHLFNQYLAQ QGYVVFSLDN RGTPRRGRDF GGALYGKQGT VEVTDQLRGV TWLKQQSWVD
PARIGVQGWS NGGYMTLMLL AKASNQYACG VAGAPVTDWG LYDSHYTERY MDLPARNEAG
YREARVLTHI EGLRSPLLLI HGMADDNVLF TNSTSLMSAL QKRAQPFELM TYPGAKHGLS
GADALHRYRV AEAFLGRCLK P
//
