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   03-AUG-2022, entry version 119.
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; 4896.SPCC830.03.1; -.
DR   iPTMnet; Q9UU96; -.
DR   MaxQB; Q9UU96; -.
DR   PaxDb; Q9UU96; -.
DR   PRIDE; Q9UU96; -.
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; PLYQRIW; -.
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:0006396; P:RNA processing; IBA:GO_Central.
DR   GO; GO:0006364; P:rRNA processing; ISS:UniProtKB.
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.
DR   SUPFAM; SSF52540; SSF52540; 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