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Database: UniProt
Entry: A0A239DMT3_9FLAO
LinkDB: A0A239DMT3_9FLAO
Original site: A0A239DMT3_9FLAO 
ID   A0A239DMT3_9FLAO        Unreviewed;       733 AA.
AC   A0A239DMT3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Dipeptidyl-peptidase-4 {ECO:0000313|EMBL:SNS33459.1};
GN   ORFNames=SAMN06265376_11190 {ECO:0000313|EMBL:SNS33459.1};
OS   Dokdonia pacifica.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Dokdonia.
OX   NCBI_TaxID=1627892 {ECO:0000313|EMBL:SNS33459.1, ECO:0000313|Proteomes:UP000198379};
RN   [1] {ECO:0000313|EMBL:SNS33459.1, ECO:0000313|Proteomes:UP000198379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25597 {ECO:0000313|EMBL:SNS33459.1,
RC   ECO:0000313|Proteomes:UP000198379};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FZNY01000011; SNS33459.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239DMT3; -.
DR   OrthoDB; 9812921at2; -.
DR   Proteomes; UP000198379; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase 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; IPR002471; Pept_S9_AS.
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.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198379};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..733
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012692403"
FT   DOMAIN          101..449
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          538..733
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   733 AA;  83959 MW;  AFE79F39A1A9A735 CRC64;
     MRITTFMIAF FLLATPIITA QNKSITIADI WKPNVNTFRT ERLQALHSMA NGKEYAVQNF
     DNNTRVASVD IYNYESGEKV RTAVSTAEIE GLDYFIAYEF SADEQKVLLS TQIKSIFRRS
     TLGEYYVYDL LSRKLTKVSD DLIQEPTFSP DGTKIAYGKN NNLYVFDIDR NETNQFTFDG
     KKNSIINGIT DWVYEEEFGF VRAFDWSADG KRIAYIRFDE TNVPEFSMDV YGDKLYQTQT
     VFKYPKAGEE NAKVSLHVYS LGEALTGTNV VQTKQISFGN IDPYYIPRIA WSKDPNILSI
     QTLNRNQNDL VLVFYNASTN KVSQPLRDRD QAYVDVTDNL TFLEDNSFIW TSEKDGWNHI
     YHYNKDGSLK KQVTSGKWEV TEYYGYDAAS NRIFYQSTEN GSINRGIYAI DISGKNKTPL
     AVDAGSNNAD FSADFTYFIN TFSDTTTPWR YTLHNAKDGK LIKTLKDNET LKTLYNSYKV
     SPKEFFTLPI NGEDLNGYMI KPLDFDPTKK YPLFMYQYSG PGSQSVKNSW NSSNDMWFQM
     LAQEGYIVVC IDPRGTGLKG RDFKKITQKE LGKYEVIDQI AAAEKLGKRE YIDADRIGIF
     GWSYGGFMAS NCLFQGADTF KMAIAVAPVT SWRFYDTIYT ERYMLTPQVN PGGYDRNSPL
     SHVEKLKGDL LLVHGSADDN VHVQNSTRLV EALVQANKQF TYFNYPDKNH GIYGGNTRYH
     LYTMMTNYIK EKL
//
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