ID GRC3_SCHPO Reviewed; 736 AA.
AC Q9UU96; Q9UTY4;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 24-JAN-2024, entry version 124.
DE RecName: Full=Polynucleotide 5'-hydroxyl-kinase grc3;
DE EC=2.7.1.-;
GN Name=grc3; ORFNames=SPCC830.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 335-525, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP INTERACTION WITH CRB3; RIX1 AND LAS1, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=21385875; DOI=10.1074/jbc.m110.201343;
RA Kitano E., Hayashi A., Kanai D., Shinmyozu K., Nakayama J.;
RT "Roles of fission yeast Grc3 protein in ribosomal RNA processing and
RT heterochromatic gene silencing.";
RL J. Biol. Chem. 286:15391-15402(2011).
CC -!- FUNCTION: Polynucleotide 5'-kinase required for both rRNA processing
CC and heterochromatic gene silencing. {ECO:0000269|PubMed:21385875}.
CC -!- SUBUNIT: Interacts with crb3, rix1 and Las1.
CC {ECO:0000269|PubMed:21385875}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:21385875}.
CC Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:21385875}.
CC Chromosome {ECO:0000269|PubMed:10759889}. Note=Nuclear dots.
CC {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:21385875}.
CC -!- SIMILARITY: Belongs to the Clp1 family. NOL9/GRC3 subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329672; CAB52876.1; -; Genomic_DNA.
DR EMBL; AB027930; BAA87234.1; -; Genomic_DNA.
DR PIR; T41629; T41629.
DR RefSeq; NP_588473.1; NM_001023464.2.
DR AlphaFoldDB; Q9UU96; -.
DR SMR; Q9UU96; -.
DR BioGRID; 275895; 7.
DR STRING; 284812.Q9UU96; -.
DR iPTMnet; Q9UU96; -.
DR MaxQB; Q9UU96; -.
DR PaxDb; 4896-SPCC830-03-1; -.
DR EnsemblFungi; SPCC830.03.1; SPCC830.03.1:pep; SPCC830.03.
DR GeneID; 2539329; -.
DR KEGG; spo:SPCC830.03; -.
DR PomBase; SPCC830.03; grc3.
DR VEuPathDB; FungiDB:SPCC830.03; -.
DR eggNOG; KOG2750; Eukaryota.
DR HOGENOM; CLU_012180_0_0_1; -.
DR InParanoid; Q9UU96; -.
DR OMA; EHVWKVR; -.
DR PhylomeDB; Q9UU96; -.
DR Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q9UU96; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0099115; C:chromosome, subtelomeric region; IDA:PomBase.
DR GO; GO:0090730; C:Las1 complex; ISO:PomBase.
DR GO; GO:0031934; C:mating-type region heterochromatin; IDA:PomBase.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR GO; GO:0097356; C:perinucleolar compartment; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; NAS:PomBase.
DR GO; GO:0051731; F:polynucleotide 5'-hydroxyl-kinase activity; ISS:UniProtKB.
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); IMP:PomBase.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR045116; Clp1/Grc3.
DR InterPro; IPR032319; CLP1_P.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12755; CLEAVAGE/POLYADENYLATION FACTOR IA SUBUNIT CLP1P; 1.
DR PANTHER; PTHR12755:SF3; POLYNUCLEOTIDE 5'-HYDROXYL-KINASE NOL9; 1.
DR Pfam; PF16575; CLP1_P; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chromosome; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; rRNA processing; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..736
FT /note="Polynucleotide 5'-hydroxyl-kinase grc3"
FT /id="PRO_0000087595"
FT REGION 26..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 338..345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 736 AA; 83251 MW; 13364A669BEB8939 CRC64;
MVKRQRIESS NVPLSAFAVR QLTLSKAARK KDNSSGKKRS VSEEESQDKY EDEMKTEGEF
PSYKHTLVQV VVPGVDHRTK LHSESSKNDS EITPDINRSK VNPQEYSEFS VASPQTISPS
LPLNLDDETV SENVPHSPQS SNDAIPVIKI TEENSFRVKD TLYVGLHKDQ KLAMVGTFIF
RSVRGKFQLF GATYSSACMS WFPLNAPLAF ATPVFSAIDN ALPAMQISEY EEDSLNLRSF
AVPSYSPKEH EYELEPKDIL PNFETVIAFR ENENGLSKIA RVLPFAKRLF SFKNLLQDAS
SISNNFEITP ESWCSFSNQL LFSTSKSDYV VPRLMVCGPK GSGKSSFSRY ITNRLLQQYR
HIAYLDLDPG QPEVVPSGHI SLYYINSPLQ GPVFARMLFP TYMLRLHLGD ISPQKDPDHY
IACVTRLFAE YKDYIFNQEI SQKEIIPLII NCPGWIRGGG AELLSSIVDI CQPTEVVYMS
REDMKSSHRE KKSIYQHKEY MPDFLSSRDE FQLTLLESTW QYLPDPNVNK VTSADNRMLG
LLSYLYFNCN LQRWDFTTSL TACQPIATAF KGSSKGIDAV NIIGEPLNVN DVAKTINGTL
MALYACDTAS LDNSNTQRIV SSPEGIPLII NDGLPLDPNT SHCLGLIVLR TIDLKRNEFH
FVGPLNLELI KDAYAKSLKI VLERGRLELP VYAMLDHRLA QYSELPYLDR NHDRVAVGAH
RRRVRRNIIR RSTFVG
//
