ID   NOL9_DICDI              Reviewed;         683 AA.
AC   Q54Z27;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Polynucleotide 5'-hydroxyl-kinase nol9;
DE            EC=2.7.1.-;
DE   AltName: Full=Nucleolar protein 9 homolog;
GN   Name=nol9; ORFNames=DDB_G0277945;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Polynucleotide 5'-kinase involved in rRNA processing.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Clp1 family. NOL9/GRC3 subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAFI02000023; EAL68145.1; -; Genomic_DNA.
DR   RefSeq; XP_642025.1; XM_636933.1.
DR   AlphaFoldDB; Q54Z27; -.
DR   SMR; Q54Z27; -.
DR   STRING; 44689.DDB0237577; -.
DR   PaxDb; Q54Z27; -.
DR   EnsemblProtists; EAL68145; EAL68145; DDB_G0277945.
DR   GeneID; 8621236; -.
DR   KEGG; ddi:DDB_G0277945; -.
DR   dictyBase; DDB_G0277945; nol9.
DR   eggNOG; KOG2750; Eukaryota.
DR   HOGENOM; CLU_021128_2_0_1; -.
DR   InParanoid; Q54Z27; -.
DR   OMA; CLYGQVE; -.
DR   PhylomeDB; Q54Z27; -.
DR   Reactome; R-DDI-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   PRO; PR:Q54Z27; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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; 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); IBA:GO_Central.
DR   GO; GO:0000460; P:maturation of 5.8S rRNA; ISS:UniProtKB.
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.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; Kinase; Nucleotide-binding; Nucleus;
KW   Reference proteome; rRNA processing; Transferase.
FT   CHAIN           1..683
FT                   /note="Polynucleotide 5'-hydroxyl-kinase nol9"
FT                   /id="PRO_0000368209"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          414..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          420..454
FT                   /evidence="ECO:0000255"
FT   BINDING         277..284
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   683 AA;  78065 MW;  0D6F496DC86E827A CRC64;
     MEINKNDNNN NINNNNINNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN QNNNQKNNYR
     NYKPIKTGTL IQHQILQQTL SNFQTKNKVF QLGSDKLILI FKENETIYFH GTIQARSIIG
     SVEVYGYTIT PQSTTYYPIY SPFCSPTLSI TSNNSNNKLY TLKEIIENQL IKIPELVKNK
     LKENEKQIEI DEPTLAISSI IVLKILDDHC ENPKMFTKKK IEIIDSFKLL KGFYPLYQPD
     FNTQLLTIPN EWLNLINTQF LYNDHCNNNG LSILTCGERN VGKSTFNRIL INKLLKKYTH
     IIFIETDTGQ TEFTPSGIMS IDIINSPLLG PPFTHCKNNP LKSYFFGDTS PKNNPEYFLN
     LSFQLIDCCN LIKQQYPNIP IILNTNGWLK SLGLHLTQEI IKYFKPTSIV QLINNNNNNN
     NNNNNNNNNN NNNNNNNNNL NDNLNNFINR FDSTVTFSQD CINQLFEDCD DDNDDNKNLK
     TTIITKLYSI NSINNFSQSI YKPIFNLGSS EIRNLMFKSY FKLESKGSLS HQSPYQVSWK
     ELKVKILTNN VPPSQTMYAL NASLVGICID EDPEKNYKYI SYKVGNNLPT IINQSPLISQ
     CIGLGLIRSI DMVNGYYYII TPIDPSLLEI SNTILKGSIE IPQTLTISVS SKGKILVPYL
     QLDVLSSYGT GSDVMNRPSF FDD