RCL1_YEAST
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 03-AUG-2022, entry version 174.
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}.
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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 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 AlphaFoldDB; Q08096; -.
DR SMR; Q08096; -.
DR BioGRID; 34394; 81.
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; Q08096; -.
DR PRIDE; Q08096; -.
DR EnsemblFungi; YOL010W_mRNA; YOL010W; YOL010W.
DR GeneID; 854152; -.
DR KEGG; sce:YOL010W; -.
DR SGD; S000005370; RCL1.
DR VEuPathDB; FungiDB:YOL010W; -.
DR eggNOG; KOG3980; Eukaryota.
DR GeneTree; ENSGT00530000063404; -.
DR HOGENOM; CLU_027882_1_0_1; -.
DR OMA; GCLYSAD; -.
DR BioCyc; YEAST:G3O-33427-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
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:0004521; F:endoribonuclease activity; IDA:SGD.
DR GO; GO:0008047; F:enzyme activator 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; IC:ComplexPortal.
DR GO; GO:2000232; P:regulation of rRNA processing; IDA:ComplexPortal.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IC:ComplexPortal.
DR GO; GO:0006364; P:rRNA processing; IDA:MGI.
DR CDD; cd00875; RNA_Cyclase_Class_I; 1.
DR Gene3D; 3.30.360.20; -; 1.
DR Gene3D; 3.65.10.20; -; 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 PANTHER; PTHR11096; PTHR11096; 1.
DR PANTHER; PTHR11096:SF1; PTHR11096:SF1; 1.
DR Pfam; PF01137; RTC; 1.
DR Pfam; PF05189; RTC_insert; 1.
DR SUPFAM; SSF55205; SSF55205; 1.
DR TIGRFAMs; TIGR03400; 18S_RNA_Rcl1p; 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
