位置:首页 > 蛋白库 > RNP4_PYRAB
RNP4_PYRAB
ID   RNP4_PYRAB              Reviewed;         117 AA.
AC   Q9V166; G8ZJ25;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Ribonuclease P protein component 4 {ECO:0000255|HAMAP-Rule:MF_00757};
DE            Short=RNase P component 4 {ECO:0000255|HAMAP-Rule:MF_00757};
DE            EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00757};
DE   AltName: Full=Rpp21 {ECO:0000255|HAMAP-Rule:MF_00757};
GN   Name=rnp4 {ECO:0000255|HAMAP-Rule:MF_00757}; OrderedLocusNames=PYRAB05620;
GN   ORFNames=PAB0385;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
CC   -!- FUNCTION: Part of ribonuclease P, a protein complex that generates
CC       mature tRNA molecules by cleaving their 5'-ends. {ECO:0000255|HAMAP-
CC       Rule:MF_00757}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides
CC         from tRNA precursor.; EC=3.1.26.5; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00757};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00757};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00757};
CC   -!- SUBUNIT: Consists of a catalytic RNA component and at least 4-5 protein
CC       subunits. {ECO:0000255|HAMAP-Rule:MF_00757}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00757}.
CC   -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC       component 4 family. {ECO:0000255|HAMAP-Rule:MF_00757}.
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; AJ248284; CAB49484.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE69952.1; -; Genomic_DNA.
DR   PIR; E75175; E75175.
DR   RefSeq; WP_010867686.1; NC_000868.1.
DR   AlphaFoldDB; Q9V166; -.
DR   SMR; Q9V166; -.
DR   STRING; 272844.PAB0385; -.
DR   EnsemblBacteria; CAB49484; CAB49484; PAB0385.
DR   GeneID; 1495465; -.
DR   KEGG; pab:PAB0385; -.
DR   PATRIC; fig|272844.11.peg.598; -.
DR   eggNOG; arCOG04345; Archaea.
DR   HOGENOM; CLU_079140_3_1_2; -.
DR   OMA; HVVITCL; -.
DR   OrthoDB; 128960at2157; -.
DR   PhylomeDB; Q9V166; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030677; C:ribonuclease P complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00757; RNase_P_4; 1.
DR   InterPro; IPR016432; RNP4.
DR   InterPro; IPR007175; Rpr2/Snm1/Rpp21.
DR   Pfam; PF04032; Rpr2; 1.
DR   PIRSF; PIRSF004878; RNase_P_4; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW   tRNA processing; Zinc.
FT   CHAIN           1..117
FT                   /note="Ribonuclease P protein component 4"
FT                   /id="PRO_0000153858"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
SQ   SEQUENCE   117 AA;  14272 MW;  673E27AADA398A8B CRC64;
     MKKVSWEKRE KKKVAIERID TLFTLAEKVV KYSPDLARRY VELALEIQKK SKVKLPRKWK
     RRYCKRCHAF LVPGFNARVR LRTDRMPHVV ITCLECGHIM RYPYLREVKE KRKRKKD
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024