ID   A0A5N8YU90_9CHLR        Unreviewed;       420 AA.
AC   A0A5N8YU90;
DT   22-APR-2020, integrated into UniProtKB/TrEMBL.
DT   22-APR-2020, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Insulinase family protein {ECO:0000313|EMBL:MQF69083.1};
GN   ORFNames=FIM12_01920 {ECO:0000313|EMBL:MQF69083.1};
OS   SAR202 cluster bacterium AD-804-J14_MRT_500m.
OC   Bacteria; Chloroflexota; SAR202 cluster.
OX   NCBI_TaxID=2587836 {ECO:0000313|EMBL:MQF69083.1, ECO:0000313|Proteomes:UP000327227};
RN   [1] {ECO:0000313|EMBL:MQF69083.1, ECO:0000313|Proteomes:UP000327227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD-804-J14_MRT_500m {ECO:0000313|EMBL:MQF69083.1};
RA   Saw J.H., Nunoura T., Hirai M., Takaki Y., Parsons R., Michelsen M.,
RA   Longnecker K., Kujawinski E.B., Stepanauskas R., Landry Z., Carlson C.A.,
RA   Giovannoni S.J.;
RT   "Pangenomics reveal diversification of enzyme families and niche
RT   specialization in globally abundant SAR202 bacteria.";
RL   Submitted (JUN-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:MQF69083.1}.
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DR   EMBL; VEXF01000005; MQF69083.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5N8YU90; -.
DR   Proteomes; UP000327227; 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:UP000327227}.
FT   DOMAIN          12..157
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          167..339
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   420 AA;  46849 MW;  89C2E829E9B054A5 CRC64;
     MHQSAVLGNG LRIVTSKMPQ TFSVTVAVLV GSGSRYETDE IAGATHFLEH LLFKGTESMP
     TAKQISAAIE GVGGVMNAST DRELTVYWCK VARSHFKTAL SVLIDMVKNP LLDPEEMEKE
     RHIIFEELRM SADYPSNRVD LLIDEMLWPD QPMGRDIGGS KESVGRIKRE DLLDLMEKQY
     TPSNVVISVA GDVDHDEVID LLDISTVGWE SKEAGTWNPV ILNQNEPAIR VEYKKSEQVH
     LCVGLPGLQL NHPDTYAANL VNVMLGEGMS SRLFQEIREN QALAYDVHSY LGQFRDCGSL
     IVYCGTEPSR SALALDAIMG QLKTLAEGFS EDELEMAREY AKGSLMLRME DSRTVAMWQG
     GQEMLVGQVN TVEHVLSSLD LVTLQDVNRV ACDFIKPDQL NVAIVGPFRS HRRFQRSLRF
//