Reviewed, UniProtKB/Swiss-Prot Q4R7R3 (CLP1_MACFA)

Names and origin

Protein names

Recommended name:
    Polyribonucleotide 5'-hydroxyl-kinase Clp1
    EC=2.7.1.78
Alternative name(s):
    Polynucleotide kinase Clp1
    Pre-mRNA cleavage complex II protein Clp1

Gene names

Name:	CLP1
ORF Names:	QtsA-14570

Organism

Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey)

Taxonomic identifier

9541 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Macaca

Protein attributes

Sequence length	425 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Polynucleotide kinase that can phosphorylate the 5'-hydroxyl groups of double-stranded RNA (dsRNA), single-stranded RNA (ssRNA), double stranded DNA (dsDNA) and double-stranded DNA:RNA hybrids. dsRNA is phosphorylated more efficiently than dsDNA, and the RNA component of a DNA:RNA hybrid is phosphorylated more efficiently than the DNA component. Appears to have roles in both tRNA splicing and mRNA 3'-end formation. Component of the tRNA splicing endonuclease complex. Phosphorylates the 5'-terminus of the tRNA 3'-exon during tRNA splicing; this phosphorylation event is a prerequisite for the subsequent ligation of the two exon halves and the production of a mature tRNA. Component of the pre-mRNA cleavage complex II (CF-II), which seems to be required for mRNA 3'-end formation. Also phosphorylates the 5'-terminus of exogenously introduced short interfering RNAs (siRNAs), which is a necessary prerequisite for their incorporation into the RNA-induced silencing complex (RISC). However endogenous siRNAs and microRNAs (miRNAs) that are produced by the cleavage of dsRNA precursors by DICER1 already contain a 5'-phosphate group, so this protein may be dispensible for normal RNA-mediated gene silencing By similarity.
Catalytic activity	ATP + 5'-dephospho-DNA = ADP + 5'-phospho-DNA. ATP + 5'-dephospho-RNA = ADP + 5'-phospho-RNA.
Cofactor	Magnesium, manganese or nickel By similarity.
Subunit structure	Component of the tRNA splicing endonuclease complex, composed of CLP1, TSEN2, TSEN15, TSEN34 and TSEN54. Component of pre-mRNA cleavage complex II (CF-II). Also associates with numerous components of the pre-mRNA cleavage complex I (CF-I/CFIm), including NUDT21, CPSF2, CPSF3, CPSF6 and CPSF7. Interacts with CSTF2 and SYMPK By similarity.
Subcellular location	Nucleus By similarity.
Sequence similarities	Belongs to the Clp1 family.

Ontologies

Keywords
Biological process	mRNA processing tRNA processing
Cellular component	Nucleus
Ligand	ATP-binding Magnesium Manganese Nickel Nucleotide-binding
Molecular function	Kinase Transferase
Gene Ontology (GO)
Biological process	mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW siRNA loading onto RISC involved in RNA interference Inferred from sequence or structural similarity. Source: UniProtKB tRNA splicing, via endonucleolytic cleavage and ligation Inferred from sequence or structural similarity. Source: UniProtKB targeting of mRNA for destruction involved in RNA interference Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	tRNA-intron endonuclease complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase activity Inferred from electronic annotation. Source: EC ATP-dependent polyribonucleotide 5'-hydroxyl-kinase activity Inferred from sequence or structural similarity. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW nickel ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 425	425	Polyribonucleotide 5'-hydroxyl-kinase Clp1		PRO_0000375167
Regions
	Nucleotide binding	121 – 128	8	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	Q4R7R3-1 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: 640AF4768994CFE6	FASTA	425	47,646
	10 20 30 40 50 60 MGEEANDDKK PTTKFELERE TELRFEVEAS QSVQLELLTG MAEIFGTELT RNKKFTFDAG 70 80 90 100 110 120 AKVAVFTWHG CSVQLSGRTE VAYVSKDTPM LLYLNTHTAL EQMRRQAEKE EERGPRVMVV 130 140 150 160 170 180 GPTDVGKSTV CRLLLNYAVR LGRRPTYVEL DVGQGSVSIP GTMGALYIER PADVEEGFSI 190 200 210 220 230 240 QAPLVYHFGS TTPGTNIKLY NKITSRLADV FNQRCEVNRR ASVSGCVINT CGWVKGSGYQ 250 260 270 280 290 300 ALVHAASAFE VDVVVVLDQE RLYNELKRDL PHFVRTVLLP KSGGVVERSK DFRRECRDER 310 320 330 340 350 360 IREYFYGFRG CFYPHAFNVK FSDVKIYKVG APTIPDSCLP LGMSQEDNQL KLVPVTPGRD 370 380 390 400 410 420 MVHHLLSVST AEGTEENLSE TSVAGFIVVT SVDLEHQVFT VLSPAPRPLP KNFLLIMDIR FMDLK

References

[1]	"DNA sequences of macaque genes expressed in brain or testis and its evolutionary implications." International consortium for macaque cDNA sequencing and analysis Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB168751 mRNA. Translation: BAE00859.1.
3D structure databases
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q4R7R3.
Family and domain databases
InterPro	IPR010655. Clp1. [Graphical view]
Pfam	PF06807. Clp1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CLP1_MACFA

Accession

Primary (citable) accession number: Q4R7R3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 26, 2009
Last sequence update:	July 19, 2005
Last modified:	October 13, 2009
This is version 16 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)