ID TSR1_DROME Reviewed; 814 AA. AC Q9VP47; B5RIG8; Q86PD4; Q95TR7; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 08-NOV-2023, entry version 133. DE RecName: Full=Pre-rRNA-processing protein TSR1 homolog; DE AltName: Full=Tsr1 ribosome assembly factor {ECO:0000312|FlyBase:FBgn0037073}; GN Name=Tsr1 {ECO:0000312|FlyBase:FBgn0037073}; GN ORFNames=CG7338 {ECO:0000312|FlyBase:FBgn0037073}; 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; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Booth B., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 189-814. 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). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-444, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RC TISSUE=Embryo; RX PubMed=18327897; DOI=10.1021/pr700696a; RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.; RT "Phosphoproteome analysis of Drosophila melanogaster embryos."; RL J. Proteome Res. 7:1675-1682(2008). CC -!- FUNCTION: Required during maturation of the 40S ribosomal subunit in CC the nucleolus. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Bms1-like GTPase family. TSR1 subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAL13820.1; Type=Erroneous initiation; Evidence={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; AE014296; AAF51709.1; -; Genomic_DNA. DR EMBL; BT003192; AAO24947.1; -; mRNA. DR EMBL; BT044092; ACH92157.1; -; mRNA. DR EMBL; AY058591; AAL13820.1; ALT_INIT; mRNA. DR RefSeq; NP_649304.1; NM_141047.4. DR AlphaFoldDB; Q9VP47; -. DR SMR; Q9VP47; -. DR BioGRID; 65608; 4. DR IntAct; Q9VP47; 2. DR STRING; 7227.FBpp0077998; -. DR iPTMnet; Q9VP47; -. DR PaxDb; 7227-FBpp0077998; -. DR DNASU; 40360; -. DR EnsemblMetazoa; FBtr0078342; FBpp0077998; FBgn0037073. DR GeneID; 40360; -. DR KEGG; dme:Dmel_CG7338; -. DR UCSC; CG7338-RA; d. melanogaster. DR AGR; FB:FBgn0037073; -. DR CTD; 55720; -. DR FlyBase; FBgn0037073; Tsr1. DR VEuPathDB; VectorBase:FBgn0037073; -. DR eggNOG; KOG1980; Eukaryota. DR GeneTree; ENSGT00940000153195; -. DR HOGENOM; CLU_009858_1_0_1; -. DR InParanoid; Q9VP47; -. DR OMA; CGYRRFV; -. DR OrthoDB; 118510at2759; -. DR PhylomeDB; Q9VP47; -. DR BioGRID-ORCS; 40360; 1 hit in 1 CRISPR screen. DR GenomeRNAi; 40360; -. DR PRO; PR:Q9VP47; -. DR Proteomes; UP000000803; Chromosome 3L. DR Bgee; FBgn0037073; Expressed in egg chamber and 25 other tissues. DR Genevisible; Q9VP47; DM. DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB. DR GO; GO:0030688; C:preribosome, small subunit precursor; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IBA:GO_Central. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0034511; F:U3 snoRNA binding; IBA:GO_Central. DR GO; GO:0000479; P:endonucleolytic cleavage of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central. DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central. DR InterPro; IPR012948; AARP2CN. DR InterPro; IPR039761; Bms1/Tsr1. DR InterPro; IPR007034; BMS1_TSR1_C. DR InterPro; IPR030387; G_Bms1/Tsr1_dom. DR PANTHER; PTHR12858:SF1; PRE-RRNA-PROCESSING PROTEIN TSR1 HOMOLOG; 1. DR PANTHER; PTHR12858; RIBOSOME BIOGENESIS PROTEIN; 1. DR Pfam; PF08142; AARP2CN; 1. DR Pfam; PF04950; RIBIOP_C; 1. DR SMART; SM00785; AARP2CN; 1. DR SMART; SM01362; DUF663; 1. DR PROSITE; PS51714; G_BMS1; 1. PE 1: Evidence at protein level; KW Nucleus; Phosphoprotein; Reference proteome; Ribosome biogenesis. FT CHAIN 1..814 FT /note="Pre-rRNA-processing protein TSR1 homolog" FT /id="PRO_0000311280" FT DOMAIN 84..249 FT /note="Bms1-type G" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01051" FT REGION 1..67 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 316..357 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 392..448 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 317..341 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 394..423 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 424..447 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 444 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:18327897" FT CONFLICT 570 FT /note="E -> V (in Ref. 3; AAO24947)" FT /evidence="ECO:0000305" SQ SEQUENCE 814 AA; 93717 MW; 3C9299F0F65556A3 CRC64; MADHAFHRPG PLKQANKAHK TGRHRSKGAI DNAQKGKIGL RPISHKHKQQ QRKEQRRNQM NQLRKNKREE VLEQKRKLGG QNTAPFLVCL LPMHEQIDPM SALEILKSCD SELVVENSPS GIVYINLPRF KQRFAFVTPP VGRGNELIAL DYLKVCDTTL LLTTAAFGDD EIFDRWGQRI FNMMSAQGIP TPVVALMDLE SINPKRRPAA KQAAQKVISK LLPEEKIMQL DTASEALNVM RRIGGQKKRI LHNVANRPHL FGDVVEFKPG SDPSDDLGTL EVTGFLRGQS LNVNGLVHIP GLGDFQLSQV VAPPDPYKLD KSRDGENSEV RLLDRSDPSK RTSLQSENIP DPMDAEQTWP TEDEIAASQA ETKKMKLVKR VPKGYSEYQA AWIPDVEEVE DPDGKDDDDM SEDDDDDKED DNEDFMSCDN KSFEDEYEKR DSDTEEFQDT VSVASEAAIN DEKYDQQMDF QEERETLKKL QQARTDQLWP DEIDTPLDVP ARERFQKYRG LESFRTSPWD AKENLPADYA RIYQFQNFDR TKRRILNEAK EFEGVLPGLY VTLYVINVPE SRWNAFKSAQ LMDNIIVYGM LPHEHQMCVM NVVLQRMPDS EVPLKSKEQL IIQCGYRRFV VNPIYSQHTN GDKHKFERYF RPYETVCATF YAPIQFPPAP VLAFKVNPDS TLALVARGRL LSCNPDRIVL KRVVLSGHPM RINRKSASIR YMFFYKEDVE YFKPVKLRTK CGRLGHIKES LGTHGHMKCY FDGQLRSYDT AFMYLYKRVF PKWTYEECLV RTAEHERQHA SANRRSSQQV AMEE //