位置:首页 > 蛋白库 > PRNK_PYRAB
PRNK_PYRAB
ID   PRNK_PYRAB              Reviewed;         354 AA.
AC   Q9V290; G8ZG19;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 2.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Polyribonucleotide 5'-hydroxyl-kinase PYRAB01840;
DE            EC=2.7.1.78;
DE   AltName: Full=Polynucleotide kinase PYRAB01840;
GN   OrderedLocusNames=PYRAB01840; ORFNames=PAB0124;
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: Polynucleotide kinase that can phosphorylate the 5'-hydroxyl
CC       groups of both single-stranded RNA (ssRNA) and single-stranded DNA
CC       (ssDNA). Exhibits a strong preference for ssRNA (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end dephospho-2'-deoxyribonucleoside-DNA + ATP = a 5'-end
CC         5'-monophospho-2'-deoxyribonucleoside-DNA + ADP + H(+);
CC         Xref=Rhea:RHEA:15669, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:13184,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:136412,
CC         ChEBI:CHEBI:136416, ChEBI:CHEBI:456216; EC=2.7.1.78;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end dephospho-ribonucleoside-RNA + ATP = a 5'-end 5'-
CC         monophospho-ribonucleoside-RNA + ADP + H(+); Xref=Rhea:RHEA:54580,
CC         Rhea:RHEA-COMP:13935, Rhea:RHEA-COMP:13936, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:138282, ChEBI:CHEBI:138284,
CC         ChEBI:CHEBI:456216; EC=2.7.1.78;
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB49108.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; AJ248283; CAB49108.1; ALT_INIT; Genomic_DNA.
DR   EMBL; HE613800; CCE69560.1; -; Genomic_DNA.
DR   PIR; E75207; E75207.
DR   RefSeq; WP_048146503.1; NC_000868.1.
DR   AlphaFoldDB; Q9V290; -.
DR   SMR; Q9V290; -.
DR   STRING; 272844.PAB0124; -.
DR   EnsemblBacteria; CAB49108; CAB49108; PAB0124.
DR   GeneID; 1495071; -.
DR   KEGG; pab:PAB0124; -.
DR   PATRIC; fig|272844.11.peg.198; -.
DR   eggNOG; arCOG04127; Archaea.
DR   HOGENOM; CLU_051301_0_1_2; -.
DR   OrthoDB; 90701at2157; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046404; F:polydeoxyribonucleotide 5'-hydroxyl-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR045116; Clp1/Grc3.
DR   InterPro; IPR032319; CLP1_P.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12755; PTHR12755; 1.
DR   Pfam; PF16575; CLP1_P; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..354
FT                   /note="Polyribonucleotide 5'-hydroxyl-kinase PYRAB01840"
FT                   /id="PRO_0000376015"
FT   BINDING         36..43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   354 AA;  39991 MW;  148E73955314911C CRC64;
     MASNKAMFTN DVPQDRLLAV EKIESLRKPA KVMIIGDVDT GKTTLTIYLA NELLSRGFRV
     AIIDSDIGQK GILPPATISL AFVDSHFTSL DDLKAFSHYF IGTITPNQYF GEMVVGVMKL
     SELAMKFSDV VLIDTTGMIY GSGVELKRMK IEAVKPNLIL ALERNNELAP ILKGYEDITI
     RLEVSEKAKD FSRSERRELR REKWRKYFEN SKIVNFNLDD VLVTGTSLFQ GEEIGDTEKS
     LLERLFKWLI IHGRKIGNKY FVVKVDASEG PRIVDKNVVK YFDFSKLSNI LLGLIDKQGF
     CIGLGILKSI NFKEKKIEVL TPVEDLSSVA EIRFGRVRVR EDGEELGLLD REAL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024