GRC3_YEAST
ID GRC3_YEAST Reviewed; 632 AA.
AC Q07845; D6VXX0; Q9P4W6;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Polynucleotide 5'-hydroxyl-kinase GRC3;
DE EC=2.7.1.-;
DE AltName: Full=Protein GRC3;
GN Name=GRC3; OrderedLocusNames=YLL035W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 401-598.
RA Dallinger G.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INDUCTION.
RX PubMed=10649456;
RX DOI=10.1002/(sici)1097-0061(200002)16:3<277::aid-yea524>3.0.co;2-g;
RA El-Moghazy A.-N., Zhang N., Ismail T., Wu J., Butt A., Ahmed Khan S.,
RA Merlotti C., Cara Woodwark K., Gardner D.C.J., Gaskell S.J., Oliver S.G.;
RT "Functional analysis of six novel ORFs on the left arm of chromosome XII in
RT Saccharomyces cerevisiae reveals two essential genes, one of which is under
RT cell-cycle control.";
RL Yeast 16:277-288(2000).
RN [5]
RP FUNCTION.
RX PubMed=12837249; DOI=10.1016/s0092-8674(03)00466-5;
RA Peng W.-T., Robinson M.D., Mnaimneh S., Krogan N.J., Cagney G.,
RA Morris Q.D., Davierwala A.P., Grigull J., Yang X., Zhang W., Mitsakakis N.,
RA Ryan O.W., Datta N., Jojic V., Pal C., Canadien V., Richards D.P.,
RA Beattie B., Wu L.F., Altschuler S.J., Roweis S., Frey B.J., Emili A.,
RA Greenblatt J.F., Hughes T.R.;
RT "A panoramic view of yeast noncoding RNA processing.";
RL Cell 113:919-933(2003).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-252 AND SER-253.
RX PubMed=20814424; DOI=10.1038/embor.2010.130;
RA Braglia P., Heindl K., Schleiffer A., Martinez J., Proudfoot N.J.;
RT "Role of the RNA/DNA kinase Grc3 in transcription termination by RNA
RT polymerase I.";
RL EMBO Rep. 11:758-764(2010).
CC -!- FUNCTION: Polynucleotide 5'-kinase involved in rRNA processing.
CC Required for the efficient termination by RNA polymerase I and the
CC processing of the IST2 pre-rRNA internal transcribed spacer localized
CC between the 5.8S and 25S rRNAs. May act by maintaining the
CC phosphorylated status of the downstream RNT1 cleavage product, which in
CC turn allows the torpedo activity of RAT1 to efficiently terminate Pol I
CC transcription. In vitro, displays polynucleotide kinase activity on
CC both single- and double-stranded RNA and on single-stranded DNA alone,
CC but not double-stranded DNA alone. {ECO:0000269|PubMed:12837249,
CC ECO:0000269|PubMed:20814424}.
CC -!- INTERACTION:
CC Q07845; P36146: LAS1; NbExp=5; IntAct=EBI-3741923, EBI-10053;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:20814424}.
CC Note=Associates with rDNA.
CC -!- INDUCTION: Cell cycle-regulated with a peak of transcription at the
CC G1/S boundary. {ECO:0000269|PubMed:10649456}.
CC -!- SIMILARITY: Belongs to the Clp1 family. NOL9/GRC3 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA57511.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z73140; CAA97484.1; -; Genomic_DNA.
DR EMBL; X81985; CAA57511.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006945; DAA09286.1; -; Genomic_DNA.
DR PIR; S64786; S64786.
DR RefSeq; NP_013065.1; NM_001181855.1.
DR AlphaFoldDB; Q07845; -.
DR SMR; Q07845; -.
DR BioGRID; 31218; 209.
DR ComplexPortal; CPX-3384; LAS1 RNA processome complex.
DR IntAct; Q07845; 2.
DR STRING; 4932.YLL035W; -.
DR iPTMnet; Q07845; -.
DR MaxQB; Q07845; -.
DR PaxDb; Q07845; -.
DR PRIDE; Q07845; -.
DR EnsemblFungi; YLL035W_mRNA; YLL035W; YLL035W.
DR GeneID; 850624; -.
DR KEGG; sce:YLL035W; -.
DR SGD; S000003958; GRC3.
DR VEuPathDB; FungiDB:YLL035W; -.
DR eggNOG; KOG2750; Eukaryota.
DR GeneTree; ENSGT00940000153668; -.
DR HOGENOM; CLU_010345_1_1_1; -.
DR OMA; EHVWKVR; -.
DR BioCyc; YEAST:G3O-32138-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q07845; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q07845; protein.
DR GO; GO:0090730; C:Las1 complex; IPI:ComplexPortal.
DR GO; GO:0030874; C:nucleolar chromatin; IPI:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051731; F:polynucleotide 5'-hydroxyl-kinase activity; IDA:SGD.
DR GO; GO:0000448; P:cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IDA:SGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; IMP:SGD.
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.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW rRNA processing; Transferase.
FT CHAIN 1..632
FT /note="Polynucleotide 5'-hydroxyl-kinase GRC3"
FT /id="PRO_0000087597"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 246..253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MUTAGEN 252
FT /note="K->A: Abolishes kinase activity and termination by
FT RNA polymerase I."
FT /evidence="ECO:0000269|PubMed:20814424"
FT MUTAGEN 253
FT /note="S->A: Abolishes kinase activity and termination by
FT RNA polymerase I."
FT /evidence="ECO:0000269|PubMed:20814424"
SQ SEQUENCE 632 AA; 72258 MW; 1F45D9E16E7EA1E8 CRC64;
MVIDSKQDLP QYTKDSGSES DSDSSNNFIV ESPSIPSSKS ATVVLNSEEY EDDEGDDLNG
LDAELIDNIT YEGDEDETMF VGLKEKQKLH LSGVFRLQVV KGGIVYNNVH YNASREILTF
WHPLSQSIPT IDFSHFAGWQ DTFFMPRNNR FKIRDEEFKS FPCVLRVFNS NHTGLLEAGH
LYRDVNYLWK PKEPYFPLNE RTTYHLLHES DRIQSLSVPG YWSTPLEKLY LSHKNAAYDT
RIMVIGGKNS GKSTFLRLLL EKFTQDIRDS TTSQEELVYL DLDPGQPEYS LPDSISLNKI
LSSPISLGQH LCQGSNFQTL LQFYAGSSSP QDEPTSYLNC ADKLIDHLEE QAFFGTSLLN
LPGWIKGFGM QILNHIIRKY KPTHLLFLET ANSKRHLDEL TIPQSFSTSL RDAYAPEVVR
VPAHSLNHTL SSRFHASQLR TFKILALFHK ITQFDYDFAP LLKSAPLQIS YGKGKSGIKG
IQFPMEFQDL NPQDIKSALE GTVIGIYTYS GEDSLEVKSL NTFPILQSCT SSSKNFITLG
LIHSIDTSQQ IMNIYVPPCH TQILDKQPED AQWIIVRNKT ETPFCDFLPS PRTITWDDNI
QIPFATFERR KKLEHVWKVR KNVMRRGQFM KR
