Y2068_RHIL3
ID Y2068_RHIL3 Reviewed; 275 AA.
AC Q1MHK3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=UPF0758 protein RL2068;
GN OrderedLocusNames=RL2068;
OS Rhizobium leguminosarum bv. viciae (strain 3841).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=216596;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3841;
RX PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT components.";
RL Genome Biol. 7:R34.1-R34.20(2006).
CC -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}.
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DR EMBL; AM236080; CAK07560.1; -; Genomic_DNA.
DR RefSeq; WP_011651676.1; NC_008380.1.
DR AlphaFoldDB; Q1MHK3; -.
DR SMR; Q1MHK3; -.
DR STRING; 216596.RL2068; -.
DR EnsemblBacteria; CAK07560; CAK07560; RL2068.
DR KEGG; rle:RL2068; -.
DR eggNOG; COG2003; Bacteria.
DR HOGENOM; CLU_073529_0_0_5; -.
DR OMA; AMPDYEL; -.
DR OrthoDB; 1833204at2; -.
DR Proteomes; UP000006575; Chromosome.
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..275
FT /note="UPF0758 protein RL2068"
FT /id="PRO_1000116364"
FT DOMAIN 153..275
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 224..237
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 275 AA; 30279 MW; 653CEFAD28A9E47A CRC64;
MAKGPVSTSS DDELPFETQE PIAADERSFF GGQPQKPSAP NARAALPASL AGQEHYHGHR
ERLRDRFREQ GDAALADYEI LELLLFRLIP RRDTKPIAKA LIERFGSLAG VFGAPQALLM
EVKGVGEAVA LDLKLISTVA HRTLKSELRT KQVLSSWSSV IQYCHAAMAH ETREQFRILF
LDKRNVLIAD EVQGRGTVDH TPVYPREVVK RALELSATAM VLVHNHPSGD PTPSRADIDM
TKVIIDAAKA LDITVHDHII IGKDGHVSLK GLKLI
