(data stored in ACNUC7421 zone)

SWISSPROT: D6XXC3_BACIE

ID   D6XXC3_BACIE            Unreviewed;       309 AA.
AC   D6XXC3;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   RecName: Full=Ribonuclease Z {ECO:0000256|HAMAP-Rule:MF_01818};
DE            Short=RNase Z {ECO:0000256|HAMAP-Rule:MF_01818};
DE            EC=3.1.26.11 {ECO:0000256|HAMAP-Rule:MF_01818};
DE   AltName: Full=tRNA 3 endonuclease {ECO:0000256|HAMAP-Rule:MF_01818};
DE   AltName: Full=tRNase Z {ECO:0000256|HAMAP-Rule:MF_01818};
GN   Name=rnz {ECO:0000256|HAMAP-Rule:MF_01818};
GN   OrderedLocusNames=Bsel_0442 {ECO:0000313|EMBL:ADH97980.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97980.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97980.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Zinc phosphodiesterase, which displays some tRNA 3'-
CC       processing endonuclease activity. Probably involved in tRNA
CC       maturation, by removing a 3'-trailer from precursor tRNA.
CC       {ECO:0000256|HAMAP-Rule:MF_01818}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of RNA, removing extra 3'
CC         nucleotides from tRNA precursor, generating 3' termini of tRNAs.
CC         A 3'-hydroxy group is left at the tRNA terminus and a 5'-
CC         phosphoryl group is left at the trailer molecule.; EC=3.1.26.11;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01818};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01818};
CC       Note=Binds 2 Zn(2+) ions. {ECO:0000256|HAMAP-Rule:MF_01818};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01818}.
CC   -!- SIMILARITY: Belongs to the RNase Z family. {ECO:0000256|HAMAP-
CC       Rule:MF_01818}.
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DR   EMBL; CP001791; ADH97980.1; -; Genomic_DNA.
DR   RefSeq; WP_013171409.1; NC_014219.1.
DR   STRING; 439292.Bsel_0442; -.
DR   EnsemblBacteria; ADH97980; ADH97980; Bsel_0442.
DR   KEGG; bse:Bsel_0442; -.
DR   eggNOG; ENOG4105IES; Bacteria.
DR   eggNOG; COG1234; LUCA.
DR   HOGENOM; HOG000272419; -.
DR   KO; K00784; -.
DR   OMA; GTQRQMM; -.
DR   OrthoDB; 1712770at2; -.
DR   BioCyc; BSEL439292:G1GLR-473-MONOMER; -.
DR   Proteomes; UP000000271; Chromosome.
DR   GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   CDD; cd07717; RNaseZ_ZiPD-like_MBL-fold; 1.
DR   Gene3D; 3.60.15.10; -; 1.
DR   HAMAP; MF_01818; RNase_Z_BN; 1.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR013471; RNase_Z/BN.
DR   Pfam; PF12706; Lactamase_B_2; 2.
DR   SUPFAM; SSF56281; SSF56281; 1.
DR   TIGRFAMs; TIGR02651; RNase_Z; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6XXC3.
DR   SWISS-2DPAGE; D6XXC3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_01818};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01818,
KW   ECO:0000313|EMBL:ADH97980.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01818};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01818};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01818};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01818}.
FT   DOMAIN       36    151       Lactamase_B. {ECO:0000259|Pfam:PF12706}.
FT   DOMAIN      202    270       Lactamase_B. {ECO:0000259|Pfam:PF12706}.
FT   ACT_SITE     67     67       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01818}.
FT   METAL        63     63       Zinc 1; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01818}.
FT   METAL        65     65       Zinc 1; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01818}.
FT   METAL        67     67       Zinc 2; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01818}.
FT   METAL        68     68       Zinc 2; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01818}.
FT   METAL       140    140       Zinc 1; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01818}.
FT   METAL       211    211       Zinc 1; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01818}.
FT   METAL       211    211       Zinc 2; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01818}.
FT   METAL       269    269       Zinc 2; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01818}.
SQ   SEQUENCE   309 AA;  34115 MW;  BB761114B7FEE61C CRC64;
     MELHMLGTGA GVPTKERNVT AMVMKGVDGK KACWMIDCGE GTQHQILHAP IKAGAITKVF
     ITHLHGDHLY GLPGFLGSRS FQGADQPLTV YGPSGLRPYI EQSLAVSGTH LTYPLTVHEV
     EEGEIVDDGN WRISCLALDH RMPSFGYRFD EKEQPGRLDR ERLLKDDIPS GPWLGDLKEQ
     KTVTLPDGRV VDGRDYVTEP VKGRRIVILG DTRPMPAVAD FAKEADLLVH EATFMAGERE
     TADRFAHSTT LDAAEIARQA DVSRLLLTHI SARYKAADMA GYTEEARSRF PNTKTAADFG
     VYSLERGDR
//

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