(data stored in SCRATCH 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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