CLP1_XENLA
ID CLP1_XENLA Reviewed; 439 AA.
AC Q6NS21;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Polyribonucleotide 5'-hydroxyl-kinase Clp1 {ECO:0000255|HAMAP-Rule:MF_03035};
DE EC=2.7.1.78 {ECO:0000255|HAMAP-Rule:MF_03035};
DE AltName: Full=Polyadenylation factor Clp1 {ECO:0000255|HAMAP-Rule:MF_03035};
DE AltName: Full=Polynucleotide kinase Clp1 {ECO:0000255|HAMAP-Rule:MF_03035};
DE AltName: Full=Pre-mRNA cleavage complex II protein Clp1 {ECO:0000255|HAMAP-Rule:MF_03035};
GN Name=clp1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Polynucleotide kinase that can phosphorylate the 5'-hydroxyl
CC groups of double-stranded RNA (dsRNA), single-stranded RNA (ssRNA),
CC double stranded DNA (dsDNA) and double-stranded DNA:RNA hybrids. dsRNA
CC is phosphorylated more efficiently than dsDNA, and the RNA component of
CC a DNA:RNA hybrid is phosphorylated more efficiently than the DNA
CC component. Plays a role in both tRNA splicing and mRNA 3'-end
CC formation. Component of the tRNA splicing endonuclease complex:
CC phosphorylates the 5'-terminus of the tRNA 3'-exon during tRNA
CC splicing; this phosphorylation event is a prerequisite for the
CC subsequent ligation of the two exon halves and the production of a
CC mature tRNA. Its role in tRNA splicing and maturation is required for
CC cerebellar development. Component of the pre-mRNA cleavage complex II
CC (CF-II), which seems to be required for mRNA 3'-end formation. Also
CC phosphorylates the 5'-terminus of exogenously introduced short
CC interfering RNAs (siRNAs), which is a necessary prerequisite for their
CC incorporation into the RNA-induced silencing complex (RISC). However,
CC endogenous siRNAs and microRNAs (miRNAs) that are produced by the
CC cleavage of dsRNA precursors by dicer1 already contain a 5'-phosphate
CC group, so this protein may be dispensible for normal RNA-mediated gene
CC silencing (By similarity). {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 Evidence={ECO:0000255|HAMAP-Rule:MF_03035};
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03035};
CC -!- SUBUNIT: Component of the tRNA splicing endonuclease complex. Component
CC of pre-mRNA cleavage complex II (CF-II). {ECO:0000255|HAMAP-
CC Rule:MF_03035}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03035}.
CC -!- SIMILARITY: Belongs to the Clp1 family. Clp1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03035}.
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DR EMBL; BC070530; AAH70530.1; -; mRNA.
DR RefSeq; NP_001084787.1; NM_001091318.1.
DR RefSeq; XP_018079928.1; XM_018224439.1.
DR AlphaFoldDB; Q6NS21; -.
DR SMR; Q6NS21; -.
DR IntAct; Q6NS21; 1.
DR MaxQB; Q6NS21; -.
DR DNASU; 431824; -.
DR GeneID; 431824; -.
DR KEGG; xla:431824; -.
DR CTD; 431824; -.
DR Xenbase; XB-GENE-1008976; clp1.L.
DR OrthoDB; 814241at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 431824; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005849; C:mRNA cleavage factor complex; IEA:UniProtKB-UniRule.
DR GO; GO:0000214; C:tRNA-intron endonuclease complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046404; F:polydeoxyribonucleotide 5'-hydroxyl-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0051733; F:polydeoxyribonucleotide kinase activity; ISS:UniProtKB.
DR GO; GO:0051736; F:polyribonucleotide 5'-hydroxyl-kinase activity; ISS:UniProtKB.
DR GO; GO:0021695; P:cerebellar cortex development; ISS:UniProtKB.
DR GO; GO:0098795; P:global gene silencing by mRNA cleavage; ISS:UniProtKB.
DR GO; GO:0031124; P:mRNA 3'-end processing; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0070922; P:RISC complex assembly; ISS:UniProtKB.
DR GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; ISS:UniProtKB.
DR Gene3D; 2.40.30.330; -; 1.
DR Gene3D; 2.60.120.1030; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03035; Clp1; 1.
DR InterPro; IPR028606; Clp1.
DR InterPro; IPR045116; Clp1/Grc3.
DR InterPro; IPR010655; Clp1_C.
DR InterPro; IPR038238; Clp1_C_sf.
DR InterPro; IPR032324; Clp1_N.
DR InterPro; IPR038239; Clp1_N_sf.
DR InterPro; IPR032319; CLP1_P.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12755; PTHR12755; 1.
DR Pfam; PF06807; Clp1; 1.
DR Pfam; PF16573; CLP1_N; 1.
DR Pfam; PF16575; CLP1_P; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; mRNA processing; Nucleotide-binding; Nucleus;
KW Reference proteome; Transferase; tRNA processing.
FT CHAIN 1..439
FT /note="Polyribonucleotide 5'-hydroxyl-kinase Clp1"
FT /id="PRO_0000375170"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
FT BINDING 74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
FT BINDING 136..141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
SQ SEQUENCE 439 AA; 48336 MW; F76AC3E057E0072A CRC64;
MSSEDLSAPG PSAPDSSWSS TGPSTKFELE RETELRLEVE GTDPVRVELV SGLAEVFGTE
LTRNKKYTFP PGSRAAIFTW HGCTVQLWGS PDMAYVSRDT PMLLYLNTQV GLEQMRVQAE
REGERGPRVL VAGPSDVGKS TLCRLLLNYA VRRGRRPTLV ELDVGQGSVS VPGTMGALCV
ERPADVEEGF SAQAPLVYHF GSTTPGTNIK LYNKLTSRLA HVFNLRCDSN RRASVSGCLI
NTCGWVKGSG YQALIHAASA FEVDVVLVLD QERLYNDLLR DLPHFVRTLL LPKSGGASER
SKECRRESRD QRVREYFYGP RGSLYPHAFE IKFSEVRVYK VGAPTIPDSC LPLGMSQEDN
QLKLVPVTPG RDMAHHLLSV VPLDGGSAEE GIEERSVAGF IVITGVDTER QTLTLLSPAP
RPLPKCVLLI MDIRFMDLK
