ID   A0A4Y8KUX7_9BACT        Unreviewed;       407 AA.
AC   A0A4Y8KUX7;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Insulinase family protein {ECO:0000313|EMBL:TFD93202.1};
GN   ORFNames=E2605_17115 {ECO:0000313|EMBL:TFD93202.1};
OS   Dysgonomonas capnocytophagoides.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC   Dysgonomonas.
OX   NCBI_TaxID=45254 {ECO:0000313|EMBL:TFD93202.1, ECO:0000313|Proteomes:UP000297861};
RN   [1] {ECO:0000313|EMBL:TFD93202.1, ECO:0000313|Proteomes:UP000297861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSN571793 {ECO:0000313|EMBL:TFD93202.1,
RC   ECO:0000313|Proteomes:UP000297861};
RA   Blyth D.M., Mccarthy S.L., Schall S.E., Stam J.A., Ong A.C., Mcgann P.T.;
RT   "San Antonio Military Medical Center submission to MRSN (WRAIR), pending
RT   publication.";
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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:TFD93202.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; SOML01000013; TFD93202.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Y8KUX7; -.
DR   STRING; 1121485.GCA_000426485_02734; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000297861; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851:SF149; GH01077P; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000297861}.
FT   DOMAIN          22..159
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          172..342
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   407 AA;  46377 MW;  69EA920F50D5A884 CRC64;
     MNIYQSHTLK NGLRIVHLPL ASHVSYCGFI VNTGTRDEQA EEFGMAHFVE HMLFKGTEKR
     RSHHIINRME AVGGEINAYT NKEETVIYSI FLEEYFERAF ELLTDLTFHS TFPKQEIEKE
     IDVILDEINS YEDSPSELIY DEFENLIYKG SQLGHNILGE PDLLSKFDCK MARQFTGKHY
     HPDNMVFFST GKTDFRKIVK LSEKYLSDIP VSSEKTERLT PQSTVKGEIS LQKDTTQSHV
     LIGGQCYDMH NPKKTTLHML NNILGGPGMN SRLNISLREK RGYVYNVESS TTLYTDTGLF
     AIYFGCDKRN TEKCIKLIQK ELNLLKNTSL TSIQLSAAKK QLTGQIAVSS DNHENLALAL
     GKSYLNHNHF NSIEETIQKI DKITSSDILN AANEIFAEQN LSTLSYL
//