Reviewed, UniProtKB/Swiss-Prot O57936 (PRNK_PYRHO)

Names and origin

Protein names

Recommended name:
    Polyribonucleotide 5'-hydroxyl-kinase PH0197
    EC=2.7.1.78
Alternative name(s):
    Polynucleotide kinase PH0197

Gene names

Ordered Locus Names:

PH0197

Organism

Pyrococcus horikoshii [Complete proteome] [HAMAP]

Taxonomic identifier

53953 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	361 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Polynucleotide kinase that can phosphorylate the 5'-hydroxyl groups of both single-stranded RNA (ssRNA) and single-stranded DNA (ssDNA). Exhibits a strong preference for ssRNA. Ref.2
Catalytic activity	ATP + 5'-dephospho-DNA = ADP + 5'-phospho-DNA. Ref.2 ATP + 5'-dephospho-RNA = ADP + 5'-phospho-RNA. Ref.2
Cofactor	Divalent cation. Ref.2
Enzyme regulation	DNA kinase activity is inhibited by 250mM sodium chloride whereas RNA kinase activity is unaffected. Ref.2
Biophysicochemical properties	Kinetic parameters: KM=16 µM for ATP using 24-mer 5'-OH DNA as substrate pH dependence: Optimum pH is 4.5 to 9.5 using 24-mer 5'-OH DNA as substrate and 4.5 to 6.5 using 24-mer 5'-OH RNA as substrate. Temperature dependence: Optimum temperature is 55 to 75 degrees Celsius using 24-mer 5'-OH DNA as substrate and from 55 to 85 degrees Celsius using 24-mer 5'-OH RNA as substrate.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase activity Inferred from electronic annotation. Source: EC nucleoside-triphosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 361	361	Polyribonucleotide 5'-hydroxyl-kinase PH0197		PRO_0000376017
Regions
	Nucleotide binding	43 – 50	8	ATP Probable
Experimental info
	Mutagenesis	49	1	K → A: 100-fold decrease in kinase activity against both DNA and RNA. Ref.2
	Mutagenesis	73	1	D → A: Abrogates kinase activity against both DNA and RNA. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O57936-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: A1FECEF13DA4116D	FASTA	361	40,941
	10 20 30 40 50 60 MLTEVCKMGT NKAFFTNEVP EDRYIAAEKI SSLKKPATVM IIGDVDTGKT TLTIYLANEL 70 80 90 100 110 120 ISRGFRVSII DSDVGQKSIL PPATISLAFV DTHFSSLEDL TPFAHYFVGT ITPSQFFGEM 130 140 150 160 170 180 VIGVMKLAEL AKKFSDVVLI DTTGMIYGPG VELKRMKIEA IKPDLILALE RENELTPIIK 190 200 210 220 230 240 GFEDITLKLR VSDKVKEFSR SERKELRREK WKRYFENSRI VTFNVNDILV TGTSMFQGKP 250 260 270 280 290 300 IEEGEKNLLE RLFKWLILHG RKLGERYFVV KVDTSEGPRV VDKNVVRYFD FSKLSNLLLG 310 320 330 340 350 360 LLDKEGFCQG VGILKAINFS EGRLEVLTPV KDISIITEIR FGRIRVREDG EELGLLDREV L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3." Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H. DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: OT3.
[2]	"Characterization of a thermostable archaeal polynucleotide kinase homologous to human Clp1." Jain R., Shuman S. RNA 15:923-931(2009) [PubMed: 19299550] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-49 AND ASP-73.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000001 Genomic DNA. Translation: BAA29266.1.
PIR	C71242.
RefSeq	NP_142196.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1444088.
GenomeReviews	Gene locus PH0197 in contig BA000001_GR.
KEGG	pho:PH0197.
NMPDR	fig|70601.1.peg.188.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	O57936.
OMA	NDLGPPT.
Family and domain databases
InterPro	IPR003593. ATPase_AAA+_core. [Graphical view]
SMART	SM00382. AAA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PRNK_PYRHO

Accession

Primary (citable) accession number: O57936

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 26, 2009
Last sequence update:	August 1, 1998
Last modified:	November 3, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)