ID RRP5_YEAST Reviewed; 1729 AA. AC Q05022; D6W054; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 14-DEC-2022, entry version 185. DE RecName: Full=rRNA biogenesis protein RRP5; DE AltName: Full=Ribosomal RNA-processing protein 5; DE AltName: Full=U3 small nucleolar RNA-associated protein RRP5; DE Short=U3 snoRNA-associated protein RRP5; GN Name=RRP5; Synonyms=FMI1; OrderedLocusNames=YMR229C; ORFNames=YM9959.11C; 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=9169872; RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."; RL Nature 387:90-93(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 FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=8896463; DOI=10.1002/j.1460-2075.1996.tb00954.x; RA Venema J., Tollervey D.; RT "RRP5 is required for formation of both 18S and 5.8S rRNA in yeast."; RL EMBO J. 15:5701-5714(1996). RN [4] RP INTERACTION WITH MPP10 AND SNORNA U3, AND IDENTIFICATION IN SSU PROCESSOME RP BY MASS SPECTROMETRY. RX PubMed=12068309; DOI=10.1038/nature00769; RA Dragon F., Gallagher J.E.G., Compagnone-Post P.A., Mitchell B.M., RA Porwancher K.A., Wehner K.A., Wormsley S., Settlage R.E., Shabanowitz J., RA Osheim Y., Beyer A.L., Hunt D.F., Baserga S.J.; RT "A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA RT biogenesis."; RL Nature 417:967-970(2002). 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=YAL6B; RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200; RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., RA Jensen O.N.; RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling RT pathway."; RL Mol. Cell. Proteomics 4:310-327(2005). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47; SER-187 AND SER-188, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ADR376; RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17287358; DOI=10.1073/pnas.0607084104; RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; RT "Analysis of phosphorylation sites on proteins from Saccharomyces RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187; SER-188 AND SER-1724, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187; SER-188 AND SER-1724, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). CC -!- FUNCTION: Involved in the biogenesis of rRNA. Required for the CC formation of 18S and 5.8S rRNA. {ECO:0000269|PubMed:8896463}. CC -!- SUBUNIT: Interacts with snoRNA U3. Interacts with MPP10. Component of CC the ribosomal small subunit (SSU) processome composed of at least 40 CC protein subunits and snoRNA U3. {ECO:0000269|PubMed:12068309}. CC -!- INTERACTION: CC Q05022; Q08235: BRX1; NbExp=3; IntAct=EBI-16011, EBI-3775; CC Q05022; P53914: KRE33; NbExp=2; IntAct=EBI-16011, EBI-28914; CC Q05022; Q12176: MAK21; NbExp=7; IntAct=EBI-16011, EBI-10944; CC Q05022; P39744: NOC2; NbExp=4; IntAct=EBI-16011, EBI-29259; CC Q05022; Q12499: NOP58; NbExp=4; IntAct=EBI-16011, EBI-12126; CC Q05022; P42945: UTP10; NbExp=4; IntAct=EBI-16011, EBI-1884; CC Q05022; P35194: UTP20; NbExp=2; IntAct=EBI-16011, EBI-1871; CC Q05022; Q06078: UTP21; NbExp=2; IntAct=EBI-16011, EBI-359; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:8896463}. CC -!- MISCELLANEOUS: Present with 8860 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. 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; Z49939; CAA90200.1; -; Genomic_DNA. DR EMBL; BK006946; DAA10128.1; -; Genomic_DNA. DR PIR; S57596; S57596. DR RefSeq; NP_013956.1; NM_001182736.1. DR PDB; 5C9S; X-ray; 2.70 A; B=1163-1729. DR PDB; 5NLG; X-ray; 2.35 A; A=1408-1721. DR PDB; 5WLC; EM; 3.80 A; NJ=1-1729. DR PDB; 5WWM; X-ray; 2.81 A; A=1399-1729. DR PDB; 5WYJ; EM; 8.70 A; R2=1-1729. DR PDB; 6LQQ; EM; 4.10 A; RD=1-1729. DR PDB; 6LQR; EM; 8.60 A; RD=1-1729. DR PDB; 6LQS; EM; 3.80 A; RD=1-1729. DR PDB; 6LQT; EM; 4.90 A; RD=1-1729. DR PDB; 6LQU; EM; 3.70 A; RD=1-1729. DR PDB; 6ZQC; EM; 3.80 A; JI=1-1729. DR PDB; 6ZQD; EM; 3.80 A; JI=1-1729. DR PDB; 7AJT; EM; 4.60 A; JI=1-1729. DR PDB; 7AJU; EM; 3.80 A; JI=1-1729. DR PDB; 7D4I; EM; 4.00 A; RD=1-1729. DR PDB; 7D5S; EM; 4.60 A; RD=1-1729. DR PDB; 7D5T; EM; 6.00 A; RD=1-1729. DR PDB; 7D63; EM; 12.30 A; RD=1-1729. DR PDB; 7SUK; EM; 3.99 A; NJ=1457-1721. DR PDBsum; 5C9S; -. DR PDBsum; 5NLG; -. DR PDBsum; 5WLC; -. DR PDBsum; 5WWM; -. DR PDBsum; 5WYJ; -. DR PDBsum; 6LQQ; -. DR PDBsum; 6LQR; -. DR PDBsum; 6LQS; -. DR PDBsum; 6LQT; -. DR PDBsum; 6LQU; -. DR PDBsum; 6ZQC; -. DR PDBsum; 6ZQD; -. DR PDBsum; 7AJT; -. DR PDBsum; 7AJU; -. DR PDBsum; 7D4I; -. DR PDBsum; 7D5S; -. DR PDBsum; 7D5T; -. DR PDBsum; 7D63; -. DR PDBsum; 7SUK; -. DR AlphaFoldDB; Q05022; -. DR SMR; Q05022; -. DR BioGRID; 35407; 389. DR ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1. DR ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2. DR ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3. DR DIP; DIP-6535N; -. DR IntAct; Q05022; 170. DR MINT; Q05022; -. DR STRING; 4932.YMR229C; -. DR iPTMnet; Q05022; -. DR MaxQB; Q05022; -. DR PaxDb; Q05022; -. DR PeptideAtlas; Q05022; -. DR EnsemblFungi; YMR229C_mRNA; YMR229C; YMR229C. DR GeneID; 855269; -. DR KEGG; sce:YMR229C; -. DR AGR; SGD:S000004842; -. DR SGD; S000004842; RRP5. DR VEuPathDB; FungiDB:YMR229C; -. DR eggNOG; KOG1070; Eukaryota. DR GeneTree; ENSGT00390000012228; -. DR HOGENOM; CLU_000845_0_0_1; -. DR InParanoid; Q05022; -. DR OMA; GQYLRAY; -. DR BioCyc; YEAST:G3O-32910-MON; -. DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR PRO; PR:Q05022; -. DR Proteomes; UP000002311; Chromosome XIII. DR RNAct; Q05022; protein. DR GO; GO:0030686; C:90S preribosome; HDA:SGD. DR GO; GO:0005730; C:nucleolus; IDA:SGD. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0032040; C:small-subunit processome; IDA:SGD. DR GO; GO:0034512; F:box C/D RNA binding; IDA:SGD. DR GO; GO:0034513; F:box H/ACA snoRNA binding; IDA:SGD. DR GO; GO:0003729; F:mRNA binding; HDA:SGD. DR GO; GO:0008266; F:poly(U) RNA binding; IDA:SGD. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0042134; F:rRNA primary transcript binding; IDA:SGD. DR GO; GO:0030515; F:snoRNA binding; IDA:SGD. DR GO; GO:0034511; F:U3 snoRNA binding; IDA:SGD. DR GO; GO:0034463; P:90S preribosome assembly; IMP: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); IMP:SGD. DR GO; GO:0000464; P:endonucleolytic cleavage in ITS1 upstream of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD. 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; IDA:SGD. DR GO; GO:0006364; P:rRNA processing; TAS:UniProtKB. DR DisProt; DP02513; -. DR Gene3D; 1.25.40.10; -; 1. DR Gene3D; 2.40.50.140; -; 10. DR InterPro; IPR003107; HAT. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR045209; Rrp5. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR PANTHER; PTHR23270; PROGRAMMED CELL DEATH PROTEIN 11 PRE-RRNA PROCESSING PROTEIN RRP5; 3. DR Pfam; PF00575; S1; 3. DR SMART; SM00386; HAT; 6. DR SMART; SM00316; S1; 12. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 10. DR SUPFAM; SSF48452; TPR-like; 1. DR PROSITE; PS50126; S1; 11. PE 1: Evidence at protein level; KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Ribonucleoprotein; Ribosome biogenesis; rRNA processing. FT CHAIN 1..1729 FT /note="rRNA biogenesis protein RRP5" FT /id="PRO_0000205763" FT DOMAIN 119..200 FT /note="S1 motif 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180" FT DOMAIN 338..410 FT /note="S1 motif 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180" FT DOMAIN 510..580 FT /note="S1 motif 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180" FT DOMAIN 607..676 FT /note="S1 motif 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180" FT DOMAIN 690..769 FT /note="S1 motif 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180" FT DOMAIN 794..863 FT /note="S1 motif 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180" FT DOMAIN 895..971 FT /note="S1 motif 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180" FT DOMAIN 1003..1083 FT /note="S1 motif 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180" FT DOMAIN 1088..1159 FT /note="S1 motif 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180" FT DOMAIN 1177..1245 FT /note="S1 motif 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180" FT DOMAIN 1265..1336 FT /note="S1 motif 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180" FT REPEAT 1455..1487 FT /note="HAT 1" FT REPEAT 1561..1594 FT /note="HAT 2" FT REPEAT 1632..1664 FT /note="HAT 3" FT REPEAT 1666..1701 FT /note="HAT 4" FT REGION 1..45 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 64..101 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 166..196 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1344..1403 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1417..1444 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..18 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 19..34 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 47 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:15665377, FT ECO:0007744|PubMed:17330950" FT MOD_RES 187 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" FT MOD_RES 188 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" FT MOD_RES 1724 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT HELIX 1409..1417 FT /evidence="ECO:0007829|PDB:5NLG" FT HELIX 1461..1470 FT /evidence="ECO:0007829|PDB:5NLG" FT HELIX 1475..1487 FT /evidence="ECO:0007829|PDB:5NLG" FT HELIX 1491..1504 FT /evidence="ECO:0007829|PDB:5NLG" FT HELIX 1510..1527 FT /evidence="ECO:0007829|PDB:5NLG" FT HELIX 1530..1543 FT /evidence="ECO:0007829|PDB:5NLG" FT HELIX 1546..1559 FT /evidence="ECO:0007829|PDB:5NLG" FT HELIX 1563..1577 FT /evidence="ECO:0007829|PDB:5NLG" FT TURN 1578..1580 FT /evidence="ECO:0007829|PDB:5NLG" FT HELIX 1582..1594 FT /evidence="ECO:0007829|PDB:5NLG" FT HELIX 1598..1611 FT /evidence="ECO:0007829|PDB:5NLG" FT HELIX 1614..1616 FT /evidence="ECO:0007829|PDB:5NLG" FT HELIX 1617..1631 FT /evidence="ECO:0007829|PDB:5NLG" FT HELIX 1634..1647 FT /evidence="ECO:0007829|PDB:5NLG" FT HELIX 1652..1665 FT /evidence="ECO:0007829|PDB:5NLG" FT HELIX 1668..1678 FT /evidence="ECO:0007829|PDB:5NLG" FT HELIX 1685..1700 FT /evidence="ECO:0007829|PDB:5NLG" FT TURN 1701..1703 FT /evidence="ECO:0007829|PDB:5NLG" FT HELIX 1705..1720 FT /evidence="ECO:0007829|PDB:5NLG" SQ SEQUENCE 1729 AA; 193134 MW; 39BF46E5587B3B0A CRC64; MVASTKRKRD EDFPLSREDS TKQPSTSSLV RNTEEVSFPR GGASALTPLE LKQVANEAAS DVLFGNESVK ASEPASRPLK KKKTTKKSTS KDSEASSANS DEARAGLIEH VNFKTLKNGS SLLGQISAIT KQDLCITFTD GISGYVNLTH ISEEFTSILE DLDEDMDSDT DAADEKKSKV EDAEYESSDD EDEKLDKSNE LPNLRRYFHI GQWLRCSVIK NTSLEPSTKK SKKKRIELTI EPSSVNIYAD EDLVKSTSIQ CAVKSIEDHG ATLDVGLPGF TGFIAKKDFG NFEKLLPGAV FLGNITKKSD RSIVVNTDFS DKKNKITQIS SIDAIIPGQI VDLLCESITK NGIAGKVFGL VSGVVNVSHL RTFSEEDLKH KFVIGSSIRC RIIACLENKS GDKVLILSNL PHILKLEDAL RSTEGLDAFP IGYTFESCSI KGRDSEYLYL ALDDDRLGKV HSSRVGEIEN SENLSSRVLG YSPVDDIYQL STDPKYLKLK YLRTNDIPIG ELLPSCEITS VSSSGIELKI FNGQFKASVP PLHISDTRLV YPERKFKIGS KVKGRVISVN SRGNVHVTLK KSLVNIEDNE LPLVSTYENA KNIKEKNEKT LATIQVFKPN GCIISFFGGL SGFLPNSEIS EVFVKRPEEH LRLGQTVIVK LLDVDADRRR IIATCKVSNE QAAQQKDTIE NIVPGRTIIT VHVIEKTKDS VIVEIPDVGL RGVIYVGHLS DSRIEQNRAQ LKKLRIGTEL TGLVIDKDTR TRVFNMSLKS SLIKDAKKET LPLTYDDVKD LNKDVPMHAY IKSISDKGLF VAFNGKFIGL VLPSYAVDSR DIDISKAFYI NQSVTVYLLR TDDKNQKFLL SLKAPKVKEE KKKVESNIED PVDSSIKSWD DLSIGSIVKA KIKSVKKNQL NVILAANLHG RVDIAEVFDT YEEITDKKQP LSNYKKDDVI KVKIIGNHDV KSHKFLPITH KISKASVLEL SMKPSELKSK EVHTKSLEEI NIGQELTGFV NNSSGNHLWL TISPVLKARI SLLDLADNDS NFSENIESVF PLGSALQVKV ASIDREHGFV NAIGKSHVDI NMSTIKVGDE LPGRVLKIAE KYVLLDLGNK VTGISFITDA LNDFSLTLKE AFEDKINNVI PTTVLSVDEQ NKKIELSLRP ATAKTRSIKS HEDLKQGEIV DGIVKNVNDK GIFVYLSRKV EAFVPVSKLS DSYLKEWKKF YKPMQYVLGK VVTCDEDSRI SLTLRESEIN GDLKVLKTYS DIKAGDVFEG TIKSVTDFGV FVKLDNTVNV TGLAHITEIA DKKPEDLSAL FGVGDRVKAI VLKTNPEKKQ ISLSLKASHF SKEAELASTT TTTTTVDQLE KEDEDEVMAD AGFNDSDSES DIGDQNTEVA DRKPETSSDG LSLSAGFDWT ASILDQAQEE EESDQDQEDF TENKKHKHKR RKENVVQDKT IDINTRAPES VADFERLLIG NPNSSVVWMN YMAFQLQLSE IEKARELAER ALKTINFREE AEKLNIWIAM LNLENTFGTE ETLEEVFSRA CQYMDSYTIH TKLLGIYEIS EKFDKAAELF KATAKKFGGE KVSIWVSWGD FLISHNEEQE ARTILGNALK ALPKRNHIEV VRKFAQLEFA KGDPERGRSL FEGLVADAPK RIDLWNVYVD QEVKAKDKKK VEDLFERIIT KKITRKQAKF FFNKWLQFEE SEGDEKTIEY VKAKATEYVA SHESQKADE //