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Y979_BURP6
ID   Y979_BURP6              Reviewed;         278 AA.
AC   A3N6Q9;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=UPF0758 protein BURPS668_0979;
GN   OrderedLocusNames=BURPS668_0979;
OS   Burkholderia pseudomallei (strain 668).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=668;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
CC   -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}.
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DR   EMBL; CP000570; ABN84392.1; -; Genomic_DNA.
DR   RefSeq; WP_011851209.1; NC_009074.1.
DR   AlphaFoldDB; A3N6Q9; -.
DR   SMR; A3N6Q9; -.
DR   EnsemblBacteria; ABN84392; ABN84392; BURPS668_0979.
DR   KEGG; bpd:BURPS668_0979; -.
DR   HOGENOM; CLU_073529_0_1_4; -.
DR   OMA; AMPDYEL; -.
DR   Proteomes; UP000002153; Chromosome I.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd08071; MPN_DUF2466; 1.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR025657; RadC_JAB.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR001405; UPF0758.
DR   InterPro; IPR020891; UPF0758_CS.
DR   PANTHER; PTHR30471; PTHR30471; 1.
DR   Pfam; PF04002; RadC; 1.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   TIGRFAMs; TIGR00608; radc; 1.
DR   PROSITE; PS50249; MPN; 1.
DR   PROSITE; PS01302; UPF0758; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Zinc.
FT   CHAIN           1..278
FT                   /note="UPF0758 protein BURPS668_0979"
FT                   /id="PRO_0000322677"
FT   DOMAIN          156..278
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           227..240
FT                   /note="JAMM motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   COMPBIAS        32..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         227
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         229
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         240
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ   SEQUENCE   278 AA;  29422 MW;  AA27E847D3AF849E CRC64;
     MQYEIVSAGE DVDDERARGR RAAAPAAPSS AVPSSAALSS AALSSAARPT GAPPATAAAR
     RGRDLPRERL LARGPAALSD AELVALLLGS GLPGHDVFAL AHTLLARFGS LRALLDAAPD
     DFKGLRGIGP ARTAILVAVV ELARRALAEK ARERPLVDSP GAVDDYLRLL IGTRPREVFV
     CLFLDARHRL VQTEETAHGS LTRMAVYPRE IVRRALALNA AALIVAHNHP SGAVRPSAAD
     RRLTRVLRDA LALVDIKLID HFVVGASDTF SFAQAGWI
 
 
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