CLP5_ARATH
ID CLP5_ARATH Reviewed; 424 AA.
AC Q9FLE2;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Protein CLP1 homolog 5 {ECO:0000255|HAMAP-Rule:MF_03035};
DE AltName: Full=CLP-like protein 5;
DE AltName: Full=Protein CLP-SIMILAR PROTEIN 5;
GN Name=CLPS5 {ECO:0000303|PubMed:18479511};
GN OrderedLocusNames=At5g39930 {ECO:0000312|Araport:AT5G39930};
GN ORFNames=MYH19.12 {ECO:0000312|EMBL:BAB10217.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Underwood B.A., Xiao Y., Moskal W., Monaghan E., Wang W., Redman J.,
RA Wu H.C., Utterback T., Town C.D.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH PCFS1; FIPS3 AND CPSF30, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18479511; DOI=10.1186/1471-2164-9-220;
RA Hunt A.G., Xu R., Addepalli B., Rao S., Forbes K.P., Meeks L.R., Xing D.,
RA Mo M., Zhao H., Bandyopadhyay A., Dampanaboina L., Marion A.,
RA Von Lanken C., Li Q.Q.;
RT "Arabidopsis mRNA polyadenylation machinery: comprehensive analysis of
RT protein-protein interactions and gene expression profiling.";
RL BMC Genomics 9:220-220(2008).
CC -!- FUNCTION: Required for endonucleolytic cleavage during polyadenylation-
CC dependent pre-mRNA 3'-end formation. {ECO:0000255|HAMAP-Rule:MF_03035}.
CC -!- SUBUNIT: Forms a complex with cleavage and polyadenylation specificity
CC factor (CPSF) subunits PCFS1, FIPS3 and CPSF30.
CC {ECO:0000269|PubMed:18479511}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9SR06,
CC 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; AB010077; BAB10217.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94492.1; -; Genomic_DNA.
DR EMBL; AY954872; AAX55198.1; -; mRNA.
DR RefSeq; NP_198809.2; NM_123356.3.
DR AlphaFoldDB; Q9FLE2; -.
DR SMR; Q9FLE2; -.
DR BioGRID; 19241; 1.
DR IntAct; Q9FLE2; 1.
DR STRING; 3702.AT5G39930.1; -.
DR PaxDb; Q9FLE2; -.
DR PRIDE; Q9FLE2; -.
DR ProteomicsDB; 246653; -.
DR EnsemblPlants; AT5G39930.1; AT5G39930.1; AT5G39930.
DR GeneID; 833990; -.
DR Gramene; AT5G39930.1; AT5G39930.1; AT5G39930.
DR KEGG; ath:AT5G39930; -.
DR Araport; AT5G39930; -.
DR TAIR; locus:2178072; AT5G39930.
DR eggNOG; KOG2749; Eukaryota.
DR HOGENOM; CLU_018195_1_0_1; -.
DR InParanoid; Q9FLE2; -.
DR OMA; DITGWWP; -.
DR OrthoDB; 814241at2759; -.
DR PhylomeDB; Q9FLE2; -.
DR PRO; PR:Q9FLE2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLE2; baseline and differential.
DR Genevisible; Q9FLE2; AT.
DR GO; GO:0005849; C:mRNA cleavage factor complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051731; F:polynucleotide 5'-hydroxyl-kinase activity; IBA:GO_Central.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IBA:GO_Central.
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; 1.
PE 1: Evidence at protein level;
KW ATP-binding; mRNA processing; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..424
FT /note="Protein CLP1 homolog 5"
FT /id="PRO_0000431352"
FT BINDING 16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
FT BINDING 56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
FT BINDING 124..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
SQ SEQUENCE 424 AA; 47489 MW; 50CC9AE9B42B32C9 CRC64;
MFGPQIRRVK LEKQSELRIE LQPTSPLRLR LLDGKAEIFG YELPHEVWIT FPPLMTFAVF
TWYGATIEID GITGNEYISC ETPMVNYLGL HNSLQVQRHR VTSSTRDSAS SQEGPRVIIV
GDIDSGKSTL AKMLLNWAVK DGWKPTFVDL NVGQSSITIP GTIAAAPIKM LVDPVEGFPL
DKALIHYFGL TNPSVNLRLY RTLVEELARE LKEEFSANAE SRASGMVIDT MGFIVREGYA
LLLHAIRTFN ASLVIVVGQE EKLVYDLKKN LKFKKNLQVL NLEKSEGVFS RSSDFRKTLR
NSNIQNYFYG VTNDLTVYTK TVKFSDVQVY RIGDFRVSGS TSAHQRGNDP LKITLVTIDE
HLVNKVLAIS YAIKPDQIIS SIVAGFVCIK NVDISEERIT YVSPSAAELP SKILILGTLT
WHVT
