GenomeNet

Database: UniProt
Entry: A0A0G1WZQ0_9BACT
LinkDB: A0A0G1WZQ0_9BACT
Original site: A0A0G1WZQ0_9BACT 
ID   A0A0G1WZQ0_9BACT        Unreviewed;       434 AA.
AC   A0A0G1WZQ0;
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=Processing peptidase {ECO:0000313|EMBL:KKU87665.1};
GN   ORFNames=UY16_C0021G0015 {ECO:0000313|EMBL:KKU87665.1};
OS   Candidatus Gottesmanbacteria bacterium GW2011_GWA2_47_9.
OC   Bacteria; Candidatus Gottesmanbacteria.
OX   NCBI_TaxID=1618445 {ECO:0000313|EMBL:KKU87665.1, ECO:0000313|Proteomes:UP000034739};
RN   [1] {ECO:0000313|EMBL:KKU87665.1, ECO:0000313|Proteomes:UP000034739}
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:KKU87665.1}.
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; LCOY01000021; KKU87665.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1WZQ0; -.
DR   PATRIC; fig|1618445.3.peg.698; -.
DR   Proteomes; UP000034739; 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          34..170
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          181..355
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   434 AA;  49876 MW;  AF149852289B7AF2 CRC64;
     MMSKGATRTK VRYYEKHVLP NGVRLMLVPM EGVNSVATAV MVGVGSRYET PEINGISHFL
     EHMVFKGTKK YPTTDDVNTI EKIGGLQNAY TDIDITNYHN KVLSTDWQQA LDINRELALA
     PLLLQKHVDK ERDVILEEMK RYEDEPAAKV GETFHSMLYP STSLGMRIIG EEKSLRAVAS
     TELKQYHDRW YSPERMVVIL AGSIRGSVLG IKEKTEDWFG RLEQRKDGFE QVKESQNKPQ
     LTVVTKPDAS QAHLILGLRT FNRGSDDRFA WNVFNLIMGV SFTSRLFKEV REKRGLCYHV
     RSSSDNWADV GYWSIYAGVA TAKVEEATRA ILHEVAKAAD RGVTEEEIRI AKKRLKTMIA
     FKSEDPEFMT EYYGRQEMYH QPILTLEDYI RKIEKVTKED INRLTKKYLV QKTLNMALVW
     NKPREEKLAA LLTL
//
DBGET integrated database retrieval system