(data stored in SCRATCH zone)

SWISSPROT: RNZ_LACP7

ID   RNZ_LACP7               Reviewed;         304 AA.
AC   A9KSU3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   11-DEC-2019, entry version 74.
DE   RecName: Full=Ribonuclease Z {ECO:0000255|HAMAP-Rule:MF_01818};
DE            Short=RNase Z {ECO:0000255|HAMAP-Rule:MF_01818};
DE            EC=3.1.26.11 {ECO:0000255|HAMAP-Rule:MF_01818};
DE   AltName: Full=tRNA 3 endonuclease {ECO:0000255|HAMAP-Rule:MF_01818};
DE   AltName: Full=tRNase Z {ECO:0000255|HAMAP-Rule:MF_01818};
GN   Name=rnz {ECO:0000255|HAMAP-Rule:MF_01818}; OrderedLocusNames=Cphy_0350;
OS   Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
OS   (Clostridium phytofermentans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae.
OX   NCBI_TaxID=357809;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700394 / DSM 18823 / ISDg;
RA   Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L.,
RA   LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA   Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E.A., Richardson P.;
RT   "Complete genome sequence of Clostridium phytofermentans ISDg.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Zinc phosphodiesterase, which displays some tRNA 3'-
CC       processing endonuclease activity. Probably involved in tRNA maturation,
CC       by removing a 3'-trailer from precursor tRNA. {ECO:0000255|HAMAP-
CC       Rule:MF_01818}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of RNA, removing extra 3' nucleotides
CC         from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy
CC         group is left at the tRNA terminus and a 5'-phosphoryl group is left
CC         at the trailer molecule.; EC=3.1.26.11; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01818};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01818};
CC       Note=Binds 2 Zn(2+) ions. {ECO:0000255|HAMAP-Rule:MF_01818};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01818}.
CC   -!- SIMILARITY: Belongs to the RNase Z family. {ECO:0000255|HAMAP-
CC       Rule:MF_01818}.
DR   EMBL; CP000885; ABX40737.1; -; Genomic_DNA.
DR   RefSeq; WP_012198380.1; NC_010001.1.
DR   SMR; A9KSU3; -.
DR   STRING; 357809.Cphy_0350; -.
DR   PRIDE; A9KSU3; -.
DR   EnsemblBacteria; ABX40737; ABX40737; Cphy_0350.
DR   KEGG; cpy:Cphy_0350; -.
DR   eggNOG; ENOG4105IES; Bacteria.
DR   eggNOG; COG1234; LUCA.
DR   HOGENOM; HOG000272419; -.
DR   KO; K00784; -.
DR   OMA; HNGYLLR; -.
DR   OrthoDB; 1712770at2; -.
DR   BioCyc; CPHY357809:G1GAJ-373-MONOMER; -.
DR   Proteomes; UP000000370; 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; A9KSU3.
DR   SWISS-2DPAGE; A9KSU3.
KW   Endonuclease; Hydrolase; Metal-binding; Nuclease; Reference proteome;
KW   tRNA processing; Zinc.
FT   CHAIN           1..304
FT                   /note="Ribonuclease Z"
FT                   /id="PRO_1000088334"
FT   ACT_SITE        65
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   METAL           61
FT                   /note="Zinc 1; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   METAL           63
FT                   /note="Zinc 1; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   METAL           65
FT                   /note="Zinc 2; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   METAL           66
FT                   /note="Zinc 2; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   METAL           138
FT                   /note="Zinc 1; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   METAL           206
FT                   /note="Zinc 1; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   METAL           206
FT                   /note="Zinc 2; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   METAL           265
FT                   /note="Zinc 2; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
SQ   SEQUENCE   304 AA;  34300 MW;  F87FB436B656D5BC CRC64;
     MLDVCLLGTS GMMPLPGRWL TALMTRLNGS SLLIDCGEGT QIAIREKGWS FHSIDIICFT
     HYHGDHISGL PGLLLSMGNA DRTQPVTVIG PKGLERVVSA LRVIAPELPF ELNFIEVTNP
     QETICVNDYV INAFRVNHNV ICYGYTIEVK RTGRFIPEMA MQNEVPIELW SRLQKGQTIE
     KDSRVFTPDM ILGPQRKGIK LTYCTDSRPV PQIIEQAQGS DLFICEGMYG EKEKQSNAIE
     NKHMTFYEAA ELAKQAGVKE LWLTHYSPSL TRPEEYMKET KEIFPNAKAG KDRKSITLEF
     DKNE
//

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