ID   A0A1G8MAR9_9GAMM        Unreviewed;       729 AA.
AC   A0A1G8MAR9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Dipeptidyl-peptidase IV Serine peptidase. MEROPS family S09B {ECO:0000313|EMBL:SDI64965.1};
GN   ORFNames=SAMN04488540_102320 {ECO:0000313|EMBL:SDI64965.1};
OS   Ferrimonas sediminum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Ferrimonadaceae; Ferrimonas.
OX   NCBI_TaxID=718193 {ECO:0000313|EMBL:SDI64965.1, ECO:0000313|Proteomes:UP000199527};
RN   [1] {ECO:0000313|EMBL:SDI64965.1, ECO:0000313|Proteomes:UP000199527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23317 {ECO:0000313|EMBL:SDI64965.1,
RC   ECO:0000313|Proteomes:UP000199527};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNEM01000002; SDI64965.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8MAR9; -.
DR   OrthoDB; 1094230at2; -.
DR   Proteomes; UP000199527; 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..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..729
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011724389"
FT   DOMAIN          122..444
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          534..728
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   729 AA;  82958 MW;  975D945D75BABB9F CRC64;
     MRRILFTGLL CCSAWLSAEP LTLSRIVSEP SLAGSQPSKP ALSPDGQRVT WLAPREDDLD
     RYDLWQYQLG SGQRTRLVDS TLFEEGELSE EEKARRERQR IYGKGLLEYQ WDTQGKALLF
     PIGGDIWLYR LESGKPQQLT RTEAFETDAR FSPKGNYVSF IRQQNLVVID LRTGQEQSLT
     VDGKGPLKNG MSEFVAQEEM DRMSGYWWSP DESAIAFLQV DESPVEQVIR NEIFADGIKL
     TEQRYPYAGR DNASVRVGVV SLDGGAIQWL PGARDNGGYL PRVNWNADGS AVTWQWQSRD
     QQTLQLWQWR KASQRRSLLL TETSRSWVNL SDDLHFLSTQ PGFIWSSERS GFRHLYLMDE
     QGNLVRQLTE GNWAVDAVEA IDEAGGWVYF SGRRDTPLER HLYRVPLSGG EVQRLSQRAG
     FHQPVFSDDG SVYLDHFSST RQPPQLSLHQ ADGKAIGWIA ENAIEGDHPL VRYWSDWTQP
     QYGTLKADNG MTLHYRLFKP KTRPGQRYPV VVRVYGGPHA QTVRDSWSRH DYFTQYLVQQ
     GFAVFQLDNR GSAARGLAFE SEIYQRLGKV EVADQVAGAE YLTSLPWVDP DRIGIYGHSY
     GGYMTLMSLF TAPESFAAGV SGAPVTDWSL YDTHYTERYL AHPASNAEGY RLSSVFPYVD
     KLKGQLFVYH GMADDNVLYQ NSTKLYKSLQ DAGKLYESKD YPGSKHSMRG KTVQLHLMAT
     IEDFLKRRL
//