ID   A0A0B7IB01_9FLAO        Unreviewed;       723 AA.
AC   A0A0B7IB01;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=170 kDa melanoma membrane-bound gelatinase {ECO:0000313|EMBL:CEN47068.1};
DE            EC=3.4.14.5 {ECO:0000313|EMBL:CEN47068.1};
GN   ORFNames=CCAND38_420011 {ECO:0000313|EMBL:CEN47068.1};
OS   Capnocytophaga canis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=1848903 {ECO:0000313|EMBL:CEN47068.1, ECO:0000313|Proteomes:UP000045051};
RN   [1] {ECO:0000313|EMBL:CEN47068.1, ECO:0000313|Proteomes:UP000045051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CcD38 {ECO:0000313|EMBL:CEN47068.1,
RC   ECO:0000313|Proteomes:UP000045051};
RA   Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CDOI01000154; CEN47068.1; -; Genomic_DNA.
DR   RefSeq; WP_052458173.1; NZ_CDOI01000154.1.
DR   AlphaFoldDB; A0A0B7IB01; -.
DR   Proteomes; UP000045051; 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:CEN47068.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000045051};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..723
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002132954"
FT   DOMAIN          102..438
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          529..723
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   723 AA;  83938 MW;  453A73DF17409154 CRC64;
     MKLKTLLTSF ILGISFAGLF AQTSITLEDI WAKGVLYPQR MAHLSAMKNT NQYTVLNYDR
     QSNSQQIDLY DFATLKKVKT IFDTKNFQLE IKSISDYSFD KNESKILIAT NTQSIYRHSF
     IADFYVYDIK NQTLQRVSDK KIQEPVFSPD GKSVFFVAEN NIYHFDLQSK SETAITLDGA
     KNKIINGITD WVYEEEFSFV RAFDVSKNGD YLAYIRFDER EVPEFSMDVY GNELYPQQQV
     FKYPKAGENN SKVSLHIYHV KTKNTVEIPL DAYYIPRIQW TQENDILSVQ TMNRHQNHLK
     LQFINASNQL IKTILEEKDK AYIDITDNLT FLYDNSFVWT SEKDGFNHIY HYDKNGNLKK
     QITKGNWEVT EYYGYDPRSR RIFYQSTENG SINRGVYSID LGGKNKKALS AQRGMNKATF
     SPDFSLYINQ FSSATEPPIY TLNDSQKGKQ VKEILNNKSL KNNIKQFGFS DKEFTEITNE
     KGDKLNAWII KPADFDPNKK YPLLMYQYSG PGSQQVNNVW HSSNDYWHYL LAQKGYIIVC
     VDGRGTGYKG ADFKKCTYKE LGKYEVEDQI FVARFFAEQP YIDKTRIGIW GWSFGGFMSS
     NCLFQGADVF KTAIAVAPVT SWRFYDTIYT ERFMQTPQEN PSGYDQNSPI THAQKLKGNY
     LLIHGTADDN VHVQNAMVLI NQLVHLNKDF DWLIYPDKDH GIYGGYTRLQ LYKKMTDYIL
     EKL
//