ID   A0A0G0ZWA8_9BACT        Unreviewed;       426 AA.
AC   A0A0G0ZWA8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Peptidase M16 domain protein {ECO:0000313|EMBL:KKS26311.1};
GN   ORFNames=UU84_C0027G0011 {ECO:0000313|EMBL:KKS26311.1};
OS   Candidatus Yanofskybacteria bacterium GW2011_GWC2_41_9.
OC   Bacteria; Candidatus Yanofskybacteria.
OX   NCBI_TaxID=1619029 {ECO:0000313|EMBL:KKS26311.1, ECO:0000313|Proteomes:UP000033859};
RN   [1] {ECO:0000313|EMBL:KKS26311.1, ECO:0000313|Proteomes:UP000033859}
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:KKS26311.1}.
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DR   EMBL; LCCE01000027; KKS26311.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0ZWA8; -.
DR   PATRIC; fig|1619029.3.peg.486; -.
DR   Proteomes; UP000033859; 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          23..158
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          170..344
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   426 AA;  47909 MW;  F8D7B3BE50AFD046 CRC64;
     MNYFNHQFHT FDSGLRLITI PMEGTRTVTV LVLVGTGSKY ETKNINGISH FLEHMMFKGT
     EKRPGALDIS RQLDIIGAEY NAFTSKEYTG YYAKASSDKL DTVMDVIFDI FLNSKLDAKE
     IAMEKGVIAE EINMYRDTPS RYVSDLFEQL LYGDQPAGWD VAGEKEIIQK LERDDFVQYF
     NSHYVAGDTV VAVAGNINPE KIKEKTAEYF KNVRNGTKVS KLPVNEQQSE PATLIHWKET
     DQSHFNLGVR SYHMFDDRKY PLSILSTILG GGMSSRLFQE VREKRGLAYY IGSSSDEYTD
     TGFFMVRAGV DKNRTMDAIK VVIEELAKAR DGGVSAKELQ DAKDHINGGM ALFLEHSDNV
     ASAYASPILF ENKVLTIEDK LAKINAVTLE DIGGVAKDII KNDRLNLALI GPFKDPEPFK
     QILKIQ
//