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rRNA biogenesis protein RRP5 (Ribosomal RNA-processing protein 5) (U3 small nucleolar RNA-associated protein RRP5) (U3 snoRNA-associated protein RRP5)

 RRP5_YEAST              Reviewed;        1729 AA.
Q05022; D6W054;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
22-NOV-2017, entry version 155.
RecName: Full=rRNA biogenesis protein RRP5;
AltName: Full=Ribosomal RNA-processing protein 5;
AltName: Full=U3 small nucleolar RNA-associated protein RRP5;
Short=U3 snoRNA-associated protein RRP5;
Name=RRP5; Synonyms=FMI1; OrderedLocusNames=YMR229C;
ORFNames=YM9959.11C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169872;
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S.,
Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome
XIII.";
Nature 387:90-93(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=8896463;
Venema J., Tollervey D.;
"RRP5 is required for formation of both 18S and 5.8S rRNA in yeast.";
EMBO J. 15:5701-5714(1996).
[4]
INTERACTION WITH MPP10 AND SNORNA U3, AND IDENTIFICATION IN SSU
PROCESSOME BY MASS SPECTROMETRY.
PubMed=12068309; DOI=10.1038/nature00769;
Dragon F., Gallagher J.E.G., Compagnone-Post P.A., Mitchell B.M.,
Porwancher K.A., Wehner K.A., Wormsley S., Settlage R.E.,
Shabanowitz J., Osheim Y., Beyer A.L., Hunt D.F., Baserga S.J.;
"A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA
biogenesis.";
Nature 417:967-970(2002).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone
signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47; SER-187 AND SER-188,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187; SER-188 AND
SER-1724, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187; SER-188 AND
SER-1724, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Involved in the biogenesis of rRNA. Required for the
formation of 18S and 5.8S rRNA. {ECO:0000269|PubMed:8896463}.
-!- SUBUNIT: Interacts with snoRNA U3. Interacts with MPP10. Component
of the ribosomal small subunit (SSU) processome composed of at
least 40 protein subunits and snoRNA U3.
{ECO:0000269|PubMed:12068309}.
-!- INTERACTION:
Q08235:BRX1; NbExp=3; IntAct=EBI-16011, EBI-3775;
P53914:KRE33; NbExp=2; IntAct=EBI-16011, EBI-28914;
Q12176:MAK21; NbExp=7; IntAct=EBI-16011, EBI-10944;
P39744:NOC2; NbExp=4; IntAct=EBI-16011, EBI-29259;
Q12499:NOP58; NbExp=4; IntAct=EBI-16011, EBI-12126;
P42945:UTP10; NbExp=4; IntAct=EBI-16011, EBI-1884;
P35194:UTP20; NbExp=2; IntAct=EBI-16011, EBI-1871;
Q06078:UTP21; NbExp=2; IntAct=EBI-16011, EBI-359;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:8896463}.
-!- MISCELLANEOUS: Present with 8860 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-----------------------------------------------------------------------
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EMBL; Z49939; CAA90200.1; -; Genomic_DNA.
EMBL; BK006946; DAA10128.1; -; Genomic_DNA.
PIR; S57596; S57596.
RefSeq; NP_013956.1; NM_001182736.1.
PDB; 5C9S; X-ray; 2.70 A; B=1163-1729.
PDB; 5WLC; EM; 3.80 A; NJ=1-1729.
PDB; 5WWM; X-ray; 2.81 A; A=1399-1729.
PDB; 5WYJ; EM; 8.70 A; R2=1-1729.
PDBsum; 5C9S; -.
PDBsum; 5WLC; -.
PDBsum; 5WWM; -.
PDBsum; 5WYJ; -.
ProteinModelPortal; Q05022; -.
SMR; Q05022; -.
BioGrid; 35407; 354.
DIP; DIP-6535N; -.
IntAct; Q05022; 167.
MINT; MINT-8285401; -.
STRING; 4932.YMR229C; -.
iPTMnet; Q05022; -.
MaxQB; Q05022; -.
PRIDE; Q05022; -.
EnsemblFungi; YMR229C; YMR229C; YMR229C.
GeneID; 855269; -.
KEGG; sce:YMR229C; -.
EuPathDB; FungiDB:YMR229C; -.
SGD; S000004842; RRP5.
GeneTree; ENSGT00390000012228; -.
HOGENOM; HOG000167551; -.
InParanoid; Q05022; -.
KO; K14792; -.
OMA; RMKFFFK; -.
OrthoDB; EOG092C03ZV; -.
BioCyc; YEAST:G3O-32910-MONOMER; -.
Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
PRO; PR:Q05022; -.
Proteomes; UP000002311; Chromosome XIII.
GO; GO:0005730; C:nucleolus; IDA:SGD.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0032040; C:small-subunit processome; IDA:SGD.
GO; GO:0034512; F:box C/D snoRNA binding; IDA:SGD.
GO; GO:0034513; F:box H/ACA snoRNA binding; IDA:SGD.
GO; GO:0008266; F:poly(U) RNA binding; IDA:SGD.
GO; GO:0042134; F:rRNA primary transcript binding; IDA:SGD.
GO; GO:0030515; F:snoRNA binding; IDA:SGD.
GO; GO:0034511; F:U3 snoRNA binding; IDA:SGD.
GO; GO:0034463; P:90S preribosome assembly; IMP:SGD.
GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
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.
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.
GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
GO; GO:0030490; P:maturation of SSU-rRNA; IDA:SGD.
GO; GO:0031167; P:rRNA methylation; TAS:Reactome.
GO; GO:0006364; P:rRNA processing; TAS:UniProtKB.
Gene3D; 1.25.40.10; -; 3.
InterPro; IPR003107; HAT.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR022967; S1_dom.
InterPro; IPR003029; S1_domain.
InterPro; IPR011990; TPR-like_helical_dom_sf.
Pfam; PF00575; S1; 3.
SMART; SM00386; HAT; 6.
SMART; SM00316; S1; 12.
SUPFAM; SSF48452; SSF48452; 1.
SUPFAM; SSF50249; SSF50249; 11.
PROSITE; PS50126; S1; 11.
1: Evidence at protein level;
3D-structure; Complete proteome; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Ribonucleoprotein; Ribosome biogenesis;
rRNA processing.
CHAIN 1 1729 rRNA biogenesis protein RRP5.
/FTId=PRO_0000205763.
DOMAIN 119 200 S1 motif 1. {ECO:0000255|PROSITE-
ProRule:PRU00180}.
DOMAIN 338 410 S1 motif 2. {ECO:0000255|PROSITE-
ProRule:PRU00180}.
DOMAIN 510 580 S1 motif 3. {ECO:0000255|PROSITE-
ProRule:PRU00180}.
DOMAIN 607 676 S1 motif 4. {ECO:0000255|PROSITE-
ProRule:PRU00180}.
DOMAIN 690 769 S1 motif 5. {ECO:0000255|PROSITE-
ProRule:PRU00180}.
DOMAIN 794 863 S1 motif 6. {ECO:0000255|PROSITE-
ProRule:PRU00180}.
DOMAIN 895 971 S1 motif 7. {ECO:0000255|PROSITE-
ProRule:PRU00180}.
DOMAIN 1003 1083 S1 motif 8. {ECO:0000255|PROSITE-
ProRule:PRU00180}.
DOMAIN 1088 1159 S1 motif 9. {ECO:0000255|PROSITE-
ProRule:PRU00180}.
DOMAIN 1177 1245 S1 motif 10. {ECO:0000255|PROSITE-
ProRule:PRU00180}.
DOMAIN 1265 1336 S1 motif 11. {ECO:0000255|PROSITE-
ProRule:PRU00180}.
REPEAT 1455 1487 HAT 1.
REPEAT 1561 1594 HAT 2.
REPEAT 1632 1664 HAT 3.
REPEAT 1666 1701 HAT 4.
MOD_RES 47 47 Phosphothreonine.
{ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:17330950}.
MOD_RES 187 187 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 188 188 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 1724 1724 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
HELIX 1409 1416 {ECO:0000244|PDB:5C9S}.
HELIX 1461 1470 {ECO:0000244|PDB:5C9S}.
HELIX 1475 1487 {ECO:0000244|PDB:5C9S}.
HELIX 1491 1504 {ECO:0000244|PDB:5C9S}.
HELIX 1510 1527 {ECO:0000244|PDB:5C9S}.
HELIX 1530 1543 {ECO:0000244|PDB:5C9S}.
HELIX 1546 1560 {ECO:0000244|PDB:5C9S}.
HELIX 1563 1577 {ECO:0000244|PDB:5C9S}.
TURN 1578 1580 {ECO:0000244|PDB:5C9S}.
HELIX 1583 1594 {ECO:0000244|PDB:5C9S}.
HELIX 1598 1611 {ECO:0000244|PDB:5C9S}.
HELIX 1614 1616 {ECO:0000244|PDB:5C9S}.
HELIX 1617 1630 {ECO:0000244|PDB:5C9S}.
HELIX 1634 1647 {ECO:0000244|PDB:5C9S}.
HELIX 1652 1665 {ECO:0000244|PDB:5C9S}.
HELIX 1668 1679 {ECO:0000244|PDB:5C9S}.
HELIX 1685 1702 {ECO:0000244|PDB:5C9S}.
HELIX 1705 1719 {ECO:0000244|PDB:5C9S}.
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


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