NOL9_DROME
ID NOL9_DROME Reviewed; 995 AA.
AC A1ZA92; Q8SZP4;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Polynucleotide 5'-hydroxyl-kinase NOL9;
DE EC=2.7.1.-;
DE AltName: Full=Nucleolar protein 9 homolog;
GN ORFNames=CG8414;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
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}.
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DR EMBL; AE013599; AAF58067.2; -; Genomic_DNA.
DR EMBL; AY070613; AAL48084.1; -; mRNA.
DR RefSeq; NP_611084.2; NM_137240.4.
DR AlphaFoldDB; A1ZA92; -.
DR BioGRID; 62499; 23.
DR IntAct; A1ZA92; 9.
DR STRING; 7227.FBpp0086393; -.
DR PaxDb; A1ZA92; -.
DR PRIDE; A1ZA92; -.
DR EnsemblMetazoa; FBtr0087255; FBpp0086393; FBgn0034073.
DR GeneID; 36774; -.
DR KEGG; dme:Dmel_CG8414; -.
DR UCSC; CG8414-RA; d. melanogaster.
DR FlyBase; FBgn0034073; CG8414.
DR VEuPathDB; VectorBase:FBgn0034073; -.
DR eggNOG; KOG2750; Eukaryota.
DR GeneTree; ENSGT00940000153668; -.
DR HOGENOM; CLU_012180_0_0_1; -.
DR InParanoid; A1ZA92; -.
DR OMA; YHRSPAF; -.
DR OrthoDB; 294689at2759; -.
DR PhylomeDB; A1ZA92; -.
DR Reactome; R-DME-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 36774; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36774; -.
DR PRO; PR:A1ZA92; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034073; Expressed in egg chamber and 37 other tissues.
DR ExpressionAtlas; A1ZA92; baseline and differential.
DR Genevisible; A1ZA92; DM.
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: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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW rRNA processing; Transferase.
FT CHAIN 1..995
FT /note="Polynucleotide 5'-hydroxyl-kinase NOL9"
FT /id="PRO_0000403780"
FT REGION 18..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..357
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 639..646
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 551
FT /note="R -> G (in Ref. 3; AAL48084)"
FT /evidence="ECO:0000305"
FT CONFLICT 806
FT /note="N -> D (in Ref. 3; AAL48084)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 995 AA; 111208 MW; 36D1904310B27714 CRC64;
MLDEHILKEM KLSFQLTEQR ELASGRRKPE KPQHPPAVPK KKVISKVASN PAKISETMIQ
KAQMESPKKS KKNKTAGAKR PLSNNVSNPD SSPSQKRLKK DNTLPKKNPV NKSSNVAAKK
SAATSKSAKL PIPKVHSINE LAPKKTKVKT PNKTKEASLS KKHKVNGNKS SMKVVQNGKV
VEIIGTAAET SDIEMNSLDD WSEEDDYLIE SDSENDVVEE IDETFLKDPK IFKVKCKGPE
YKLSDILPPF EHDEYQPLLL DGDGSGTVRK IKVFKSAQEE TDSDEDDIDY EPEDSDDFGS
EEFDSEESDS EDTSSADYDS DGDFYSEYSD MEDVSDSDSE EFGSDIFDTD DLDSTYEPPD
IEGFFDHPPV GMQREPLIIE EIFDDPPVEK KQERIEQSSV MDIVVKNLSS VPPKKESEVA
IETEENDEVS LPEVVTPEKE NYLQPSDVPF YRNPQANPTE LSVFENSLKS NHVLAVIKED
LEVYGTLVLT LLCGQISVNG YRARRQEAIT IYSPKGLNWV SISPTKTKKP VKDEVNWEEL
NKNFTRAQLD RIKTSFQRQT NAIVLLHRNT SAQQLVDTFG KHMAQNVFPL VNSSNRPFGQ
SETLLHCLIQ SSDQSRTLQV PQVWNKLQMH ATSRIIVAGG KGVGKSSLLR YLINRNLGQF
PSMLLIDLDI GQPEIFVPQT ISCTVIDEPL LGPGFLYNRQ PEHAIVVGHT NIVLCAEQYA
RAVIQLVQNI QNDAKYSNIP WLINTMGYNK GFGIELMALL VDRIRPTDLV QIASPIPINN
FDSVLDRNSL SQIKPIIYSA EEFKINEIPK YTLHKLISAV PAREKGTWSL SAKDMRYSNL
LARLSSCLTG NAKSLTDCQP LGVSLESLKI LHPTSKNYSR EELIRGMEAN VVYLCHHGAG
LPQCLGIGVV RAIDYERKEL YLVPAMPLQK MSLVDCLILG GEQSLPQGFL RDQGQGVSSS
VPFVFILDDS KSSKSIQQIY HRAPAFLGVP ANQRN
