位置:首页 > 蛋白库 > RNZ_PROM9
RNZ_PROM9
ID   RNZ_PROM9               Reviewed;         312 AA.
AC   Q319D8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=PMT9312_1447;
OS   Prochlorococcus marinus (strain MIT 9312).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9312;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
RL   Submitted (JUL-2005) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000111; ABB50507.1; -; Genomic_DNA.
DR   RefSeq; WP_011376991.1; NC_007577.1.
DR   AlphaFoldDB; Q319D8; -.
DR   SMR; Q319D8; -.
DR   STRING; 74546.PMT9312_1447; -.
DR   EnsemblBacteria; ABB50507; ABB50507; PMT9312_1447.
DR   KEGG; pmi:PMT9312_1447; -.
DR   eggNOG; COG1234; Bacteria.
DR   HOGENOM; CLU_031317_2_0_3; -.
DR   OMA; GTQRQMM; -.
DR   OrthoDB; 1712770at2; -.
DR   Proteomes; UP000002715; 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; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
DR   TIGRFAMs; TIGR02651; RNase_Z; 1.
PE   3: Inferred from homology;
KW   Endonuclease; Hydrolase; Metal-binding; Nuclease; tRNA processing; Zinc.
FT   CHAIN           1..312
FT                   /note="Ribonuclease Z"
FT                   /id="PRO_1000070318"
FT   ACT_SITE        66
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         144
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         215
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         215
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         273
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
SQ   SEQUENCE   312 AA;  34299 MW;  926B66BF1EDFD210 CRC64;
     MNITFLGTSS GVPSLTRNVS SLALKLSQSS EVWLFDCGEG TQHQIMKSNI KSSQIKKIFI
     THMHGDHIYG LPGLLATLGL SGNSNGIEIY GPLGLRSFIS SALSSSFCKL SFPLHFVEVE
     NFASENKILF ENNKLKVNCA CLKHKIPAYG YRVSEKDKPG IFDIKKAESM KIAPGPIYSK
     LQQGKEVLLP DGRTVNGKEF CGPPRKGESF VYCTDTVFSE SAVSLSKNAD LLVHESTFSQ
     EDESMAYEKL HSTTIMAAKT ALLSNTKKLI ITHLSPRYTS KNSITPSDLL KEAQKVFPNT
     HLAKDFLVAD IK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024