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Database: UniProt
Entry: A0A1J4VQZ8_9BACT
LinkDB: A0A1J4VQZ8_9BACT
Original site: A0A1J4VQZ8_9BACT 
ID   A0A1J4VQZ8_9BACT        Unreviewed;       290 AA.
AC   A0A1J4VQZ8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Peptidase M16 N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=AUJ75_04095 {ECO:0000313|EMBL:OIO37537.1};
OS   Candidatus Omnitrophica bacterium CG1_02_49_10.
OC   Bacteria; Candidatus Omnitrophota.
OX   NCBI_TaxID=1805289 {ECO:0000313|EMBL:OIO37537.1, ECO:0000313|Proteomes:UP000182804};
RN   [1] {ECO:0000313|EMBL:OIO37537.1, ECO:0000313|Proteomes:UP000182804}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG1_02_49_10 {ECO:0000313|EMBL:OIO37537.1};
RX   PubMed=27112493;
RA   Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA   Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT   "Genomic resolution of a cold subsurface aquifer community provides
RT   metabolic insights for novel microbes adapted to high CO concentrations.";
RL   Environ. Microbiol. 0:0-0(2016).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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:OIO37537.1}.
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DR   EMBL; MNVT01000117; OIO37537.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J4VQZ8; -.
DR   Proteomes; UP000182804; Unassembled WGS sequence.
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; METALLOPROTEASE; 1.
DR   PANTHER; PTHR11851:SF49; MITOCHONDRIAL-PROCESSING PEPTIDASE SUBUNIT ALPHA; 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          14..160
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          169..290
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   NON_TER         290
FT                   /evidence="ECO:0000313|EMBL:OIO37537.1"
SQ   SEQUENCE   290 AA;  32624 MW;  E9BD91259BF65E1C CRC64;
     MIYKKTALDN GLNVVSIPMP HMKSVSLGIW VAVGGRYEDE ENAGISHFIE HLLFKGTLTR
     TSRDIKTEIE SKGGSLNAFT GEECTCFLAR MPREHWKAAF DVLSDMVVSP RLDDKDMEKE
     RLIILEEIKM YLDLPNQHVH EILNGLMWPG QPLGMNLSGT ARSVKSMALS DIRSYKERHY
     MASKIIVIAA GALEHRDLED KASSAFSSMD SRRASGFEKA NAGQNAPRFK VENKKTKQTH
     IVLGFHALPK GDPDIYILSL LNIIMGGNMS SRLYHEIRER SALAYEIHSY
//
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