ID RCL1_YEAST Reviewed; 367 AA. AC Q08096; D6W257; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 182. DE RecName: Full=RNA 3'-terminal phosphate cyclase-like protein; GN Name=RCL1; Synonyms=RTC1; OrderedLocusNames=YOL010W; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169874; RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."; RL Nature 387:98-102(1997). RN [2] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [3] RP CHARACTERIZATION. RX PubMed=10790377; DOI=10.1093/emboj/19.9.2115; RA Billy E., Wegierski T., Nasr F., Filipowicz W.; RT "Rcl1p, the yeast protein similar to the RNA 3'-phosphate cyclase, RT associates with U3 snoRNP and is required for 18S rRNA biogenesis."; RL EMBO J. 19:2115-2126(2000). RN [4] RP INTERACTION WITH BMS1. RX PubMed=11565748; DOI=10.1017/s1355838201012079; RA Wegierski T., Billy E., Nasr F., Filipowicz W.; RT "Bms1p, a G-domain-containing protein, associates with Rcl1p and is RT required for 18S rRNA biogenesis in yeast."; RL RNA 7:1254-1267(2001). RN [5] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). CC -!- FUNCTION: Does not have cyclase activity. Plays a role in 40S- CC ribosomal-subunit biogenesis in the early pre-rRNA processing steps at CC sites A0, A1 and A2 that are required for proper maturation of the 18S CC RNA. Essential for viability. CC -!- SUBUNIT: Associates with U3 snoRNP but is not its structural component. CC Associates with RCL1. CC -!- INTERACTION: CC Q08096; Q08965: BMS1; NbExp=7; IntAct=EBI-14892, EBI-3683; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. CC -!- MISCELLANEOUS: Present with 10000 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the RNA 3'-terminal cyclase family. Type 2 CC subfamily. {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; Z74752; CAA99009.1; -; Genomic_DNA. DR EMBL; BK006948; DAA10773.1; -; Genomic_DNA. DR PIR; S66692; S66692. DR RefSeq; NP_014633.1; NM_001183264.1. DR PDB; 4CLQ; X-ray; 2.02 A; A=1-367. DR PDB; 5JPQ; EM; 7.30 A; Z=1-367. DR PDB; 5TZS; EM; 5.10 A; h=1-367. DR PDB; 5WLC; EM; 3.80 A; SH=1-367. DR PDB; 5WYJ; EM; 8.70 A; R1=1-367. DR PDB; 5WYK; EM; 4.50 A; R1=1-367. DR PDB; 6KE6; EM; 3.40 A; RK=1-367. DR PDB; 6LQP; EM; 3.20 A; RK=1-367. DR PDB; 6LQQ; EM; 4.10 A; RK=1-367. DR PDB; 6LQR; EM; 8.60 A; RK=1-367. DR PDB; 6LQS; EM; 3.80 A; RK=1-367. DR PDB; 6LQT; EM; 4.90 A; RK=1-367. DR PDB; 6LQU; EM; 3.70 A; RK=1-367. DR PDB; 6LQV; EM; 4.80 A; RK=1-367. DR PDB; 6ZQA; EM; 4.40 A; CM=1-367. DR PDB; 6ZQB; EM; 3.90 A; CM=1-367. DR PDB; 6ZQC; EM; 3.80 A; CM=1-367. DR PDB; 6ZQD; EM; 3.80 A; CM=1-367. DR PDB; 6ZQE; EM; 7.10 A; CM=1-367. DR PDB; 6ZQF; EM; 4.90 A; CM=1-367. DR PDB; 6ZQG; EM; 3.50 A; CM=1-367. DR PDB; 7AJT; EM; 4.60 A; CM=1-367. DR PDB; 7AJU; EM; 3.80 A; CM=1-367. DR PDB; 7D4I; EM; 4.00 A; RK=1-367. DR PDB; 7D5S; EM; 4.60 A; RK=1-367. DR PDB; 7D5T; EM; 6.00 A; RK=1-367. DR PDB; 7D63; EM; 12.30 A; RK=1-367. DR PDB; 7SUK; EM; 3.99 A; SH=7-366. DR PDBsum; 4CLQ; -. DR PDBsum; 5JPQ; -. DR PDBsum; 5TZS; -. DR PDBsum; 5WLC; -. DR PDBsum; 5WYJ; -. DR PDBsum; 5WYK; -. DR PDBsum; 6KE6; -. DR PDBsum; 6LQP; -. DR PDBsum; 6LQQ; -. DR PDBsum; 6LQR; -. DR PDBsum; 6LQS; -. DR PDBsum; 6LQT; -. DR PDBsum; 6LQU; -. DR PDBsum; 6LQV; -. DR PDBsum; 6ZQA; -. DR PDBsum; 6ZQB; -. DR PDBsum; 6ZQC; -. DR PDBsum; 6ZQD; -. DR PDBsum; 6ZQE; -. DR PDBsum; 6ZQF; -. DR PDBsum; 6ZQG; -. DR PDBsum; 7AJT; -. DR PDBsum; 7AJU; -. DR PDBsum; 7D4I; -. DR PDBsum; 7D5S; -. DR PDBsum; 7D5T; -. DR PDBsum; 7D63; -. DR PDBsum; 7SUK; -. DR AlphaFoldDB; Q08096; -. DR EMDB; EMD-0949; -. DR EMDB; EMD-0950; -. DR EMDB; EMD-0951; -. DR EMDB; EMD-0952; -. DR EMDB; EMD-0953; -. DR EMDB; EMD-0954; -. DR EMDB; EMD-0955; -. DR EMDB; EMD-11357; -. DR EMDB; EMD-11358; -. DR EMDB; EMD-11359; -. DR EMDB; EMD-11360; -. DR EMDB; EMD-11361; -. DR EMDB; EMD-11362; -. DR EMDB; EMD-11363; -. DR EMDB; EMD-11807; -. DR EMDB; EMD-11808; -. DR EMDB; EMD-25441; -. DR EMDB; EMD-30574; -. DR EMDB; EMD-30584; -. DR EMDB; EMD-30585; -. DR EMDB; EMD-30588; -. DR EMDB; EMD-6695; -. DR EMDB; EMD-6696; -. DR EMDB; EMD-8473; -. DR EMDB; EMD-9964; -. DR SMR; Q08096; -. DR BioGRID; 34394; 133. DR ComplexPortal; CPX-1606; RCL1-BMS1 40S ribosomal subunit maturation complex. DR DIP; DIP-4539N; -. DR IntAct; Q08096; 21. DR MINT; Q08096; -. DR STRING; 4932.YOL010W; -. DR iPTMnet; Q08096; -. DR MaxQB; Q08096; -. DR PaxDb; 4932-YOL010W; -. DR PeptideAtlas; Q08096; -. DR EnsemblFungi; YOL010W_mRNA; YOL010W; YOL010W. DR GeneID; 854152; -. DR KEGG; sce:YOL010W; -. DR AGR; SGD:S000005370; -. DR SGD; S000005370; RCL1. DR VEuPathDB; FungiDB:YOL010W; -. DR eggNOG; KOG3980; Eukaryota. DR GeneTree; ENSGT00530000063404; -. DR HOGENOM; CLU_027882_1_0_1; -. DR InParanoid; Q08096; -. DR OMA; YTDQNKG; -. DR OrthoDB; 231692at2759; -. DR BioCyc; YEAST:G3O-33427-MONOMER; -. DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR BioGRID-ORCS; 854152; 0 hits in 10 CRISPR screens. DR PRO; PR:Q08096; -. DR Proteomes; UP000002311; Chromosome XV. DR RNAct; Q08096; Protein. DR GO; GO:0030686; C:90S preribosome; IDA:GO_Central. DR GO; GO:0005730; C:nucleolus; IDA:SGD. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0032040; C:small-subunit processome; IPI:ComplexPortal. DR GO; GO:0008047; F:enzyme activator activity; IDA:SGD. DR GO; GO:0004521; F:RNA endonuclease activity; IDA:SGD. DR GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD. DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IDA: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:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD. DR GO; GO:0030490; P:maturation of SSU-rRNA; NAS:ComplexPortal. DR GO; GO:2000232; P:regulation of rRNA processing; IDA:ComplexPortal. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; NAS:ComplexPortal. DR GO; GO:0006364; P:rRNA processing; IDA:MGI. DR CDD; cd00875; RNA_Cyclase_Class_I; 1. DR Gene3D; 3.65.10.20; RNA 3'-terminal phosphate cyclase domain; 1. DR Gene3D; 3.30.360.20; RNA 3'-terminal phosphate cyclase, insert domain; 1. DR InterPro; IPR013791; RNA3'-term_phos_cycl_insert. DR InterPro; IPR023797; RNA3'_phos_cyclase_dom. DR InterPro; IPR037136; RNA3'_phos_cyclase_dom_sf. DR InterPro; IPR000228; RNA3'_term_phos_cyc. DR InterPro; IPR016443; RNA3'_term_phos_cyc_type_2. DR InterPro; IPR020719; RNA3'_term_phos_cycl-like_CS. DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b. DR InterPro; IPR036553; RPTC_insert. DR NCBIfam; TIGR03400; 18S_RNA_Rcl1p; 1. DR PANTHER; PTHR11096; RNA 3' TERMINAL PHOSPHATE CYCLASE; 1. DR PANTHER; PTHR11096:SF1; RNA 3'-TERMINAL PHOSPHATE CYCLASE-LIKE PROTEIN; 1. DR Pfam; PF01137; RTC; 1. DR Pfam; PF05189; RTC_insert; 1. DR SUPFAM; SSF55205; EPT/RTPC-like; 1. DR PROSITE; PS01287; RTC; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Nucleus; Reference proteome; KW Ribosome biogenesis. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..367 FT /note="RNA 3'-terminal phosphate cyclase-like protein" FT /id="PRO_0000156444" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:22814378" FT STRAND 9..14 FT /evidence="ECO:0007829|PDB:4CLQ" FT HELIX 17..27 FT /evidence="ECO:0007829|PDB:4CLQ" FT STRAND 31..34 FT /evidence="ECO:0007829|PDB:4CLQ" FT TURN 36..39 FT /evidence="ECO:0007829|PDB:4CLQ" FT STRAND 40..42 FT /evidence="ECO:0007829|PDB:4CLQ" FT HELIX 47..59 FT /evidence="ECO:0007829|PDB:4CLQ" FT STRAND 60..62 FT /evidence="ECO:0007829|PDB:4CLQ" FT STRAND 64..67 FT /evidence="ECO:0007829|PDB:4CLQ" FT STRAND 74..77 FT /evidence="ECO:0007829|PDB:4CLQ" FT STRAND 84..89 FT /evidence="ECO:0007829|PDB:4CLQ" FT HELIX 96..104 FT /evidence="ECO:0007829|PDB:4CLQ" FT HELIX 107..109 FT /evidence="ECO:0007829|PDB:4CLQ" FT STRAND 114..120 FT /evidence="ECO:0007829|PDB:4CLQ" FT STRAND 125..127 FT /evidence="ECO:0007829|PDB:4CLQ" FT HELIX 130..135 FT /evidence="ECO:0007829|PDB:4CLQ" FT HELIX 137..143 FT /evidence="ECO:0007829|PDB:4CLQ" FT STRAND 150..155 FT /evidence="ECO:0007829|PDB:4CLQ" FT TURN 159..161 FT /evidence="ECO:0007829|PDB:4CLQ" FT STRAND 164..170 FT /evidence="ECO:0007829|PDB:4CLQ" FT STRAND 190..200 FT /evidence="ECO:0007829|PDB:4CLQ" FT HELIX 203..216 FT /evidence="ECO:0007829|PDB:4CLQ" FT STRAND 219..230 FT /evidence="ECO:0007829|PDB:4CLQ" FT HELIX 233..235 FT /evidence="ECO:0007829|PDB:4CLQ" FT STRAND 240..249 FT /evidence="ECO:0007829|PDB:4CLQ" FT TURN 250..253 FT /evidence="ECO:0007829|PDB:4CLQ" FT STRAND 254..261 FT /evidence="ECO:0007829|PDB:4CLQ" FT HELIX 268..284 FT /evidence="ECO:0007829|PDB:4CLQ" FT STRAND 287..289 FT /evidence="ECO:0007829|PDB:4CLQ" FT TURN 291..293 FT /evidence="ECO:0007829|PDB:4CLQ" FT HELIX 294..302 FT /evidence="ECO:0007829|PDB:4CLQ" FT STRAND 306..313 FT /evidence="ECO:0007829|PDB:4CLQ" FT HELIX 315..317 FT /evidence="ECO:0007829|PDB:4CLQ" FT HELIX 320..333 FT /evidence="ECO:0007829|PDB:4CLQ" FT STRAND 338..341 FT /evidence="ECO:0007829|PDB:4CLQ" FT STRAND 350..355 FT /evidence="ECO:0007829|PDB:4CLQ" SQ SEQUENCE 367 AA; 40171 MW; C5DDA7F9B0C1E296 CRC64; MSSSAPKYTT FQGSQNFRLR IVLATLSGKP IKIEKIRSGD LNPGLKDYEV SFLRLIESVT NGSVIEISYT GTTVIYRPGI IVGGASTHIC PSSKPVGYFV EPMLYLAPFS KKKFSILFKG ITASHNDAGI EAIKWGLMPV MEKFGVRECA LHTLKRGSPP LGGGEVHLVV DSLIAQPITM HEIDRPIISS ITGVAYSTRV SPSLVNRMID GAKKVLKNLQ CEVNITADVW RGENSGKSPG WGITLVAQSK QKGWSYFAED IGDAGSIPEE LGEKVACQLL EEISKSAAVG RNQLPLAIVY MVIGKEDIGR LRINKEQIDE RFIILLRDIK KIFNTEVFLK PVDEADNEDM IATIKGIGFT NTSKKIA //