ID   A0A0G1L366_9BACT        Unreviewed;       501 AA.
AC   A0A0G1L366;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Peptidase M16 domain protein {ECO:0000313|EMBL:KKT90396.1};
GN   ORFNames=UW90_C0002G0045 {ECO:0000313|EMBL:KKT90396.1};
OS   Candidatus Yanofskybacteria bacterium GW2011_GWB1_45_11.
OC   Bacteria; Candidatus Yanofskybacteria.
OX   NCBI_TaxID=1619026 {ECO:0000313|EMBL:KKT90396.1, ECO:0000313|Proteomes:UP000034368};
RN   [1] {ECO:0000313|EMBL:KKT90396.1, ECO:0000313|Proteomes:UP000034368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKT90396.1}.
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DR   EMBL; LCKD01000002; KKT90396.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1L366; -.
DR   Proteomes; UP000034368; 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;
FT   DOMAIN          120..252
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          260..431
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   501 AA;  57020 MW;  01A9A3F56E2384FB CRC64;
     MCDEQSDLVP LSGQSSKGCT EHLSMPGKPE AEPQPSLRQY CSWRIRWPMM MWTSRLPRNR
     AICLAATKMV STLAEAGEGV AARRGYSHFF IMHTYSESIL PNKLRVITST HVDSWINFME
     LWVNAGSRHE NAGGLGYAHI LEHMLLKGTK KWPTPYLLGL EKDRIGVYSN AQTNLEKISL
     TINGLSKYKD RMMHVLAEQA LNSIIDEIAL ENEKKVILEE YKKSADDPVR HIARISQMNF
     FENHPLGKNI LGNPESIKAV TQDSLLAYHH SFFVPSQTAL IISGDIKHGE AYDMASKYFG
     GWKDVKSKNN FQNFRLNNHS FFEKRDISQF HIAISYNTTG VELSKRQLAL SILANYLNFG
     YTSPLMQELR IKNGLVYQIN IMNGRYVDAG RFSIQTSTTE PQKVIDIILE TINSIPDKLT
     PSLFEEIKNQ YIDGLLVNMS DFEKEISFLG TNFILRGKMS SPADTLKEIE SIDRDFLMDT
     VKGFFVEERR HIAVLGPCQI F
//