RRP7_YEAST
ID RRP7_YEAST Reviewed; 297 AA.
AC P25368; D6VQY4;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Ribosomal RNA-processing protein 7;
GN Name=RRP7; OrderedLocusNames=YCL031C; ORFNames=YCL184, YCL31C;
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 [GENOMIC DNA].
RX PubMed=1897318; DOI=10.1002/yea.320070513;
RA Rad M.R., Luetzenkirchen K., Xu G., Kleinhans U., Hollenberg C.P.;
RT "The complete sequence of a 11,953 bp fragment from C1G on chromosome III
RT encompasses four new open reading frames.";
RL Yeast 7:533-538(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-218.
RX PubMed=7049842; DOI=10.1016/0378-1119(82)90055-5;
RA Donahue T.F., Farabaugh P.J., Fink G.R.;
RT "The nucleotide sequence of the HIS4 region of yeast.";
RL Gene 18:47-59(1982).
RN [5]
RP CHARACTERIZATION.
RX PubMed=9271380; DOI=10.1128/mcb.17.9.5023;
RA Baudin-Baillieu A., Tollervey D., Cullin C., Lacroute F.;
RT "Functional analysis of Rrp7p, an essential yeast protein involved in pre-
RT rRNA processing and ribosome assembly.";
RL Mol. Cell. Biol. 17:5023-5032(1997).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
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 [8]
RP IDENTIFICATION IN THE 90S PRE-RIBOSOMAL PARTICLE.
RX PubMed=17515605; DOI=10.1128/mcb.00380-07;
RA Perez-Fernandez J., Roman A., De Las Rivas J., Bustelo X.R., Dosil M.;
RT "The 90S preribosome is a multimodular structure that is assembled through
RT a hierarchical mechanism.";
RL Mol. Cell. Biol. 27:5414-5429(2007).
CC -!- FUNCTION: Plays an important role in the synthesis of 18S rRNA but is
CC not required for the 5.8S and 25S pathway. Is necessary for the
CC cleavage at site A2. Is required for efficient association of RPS27
CC with the pre-ribosomal particle.
CC -!- SUBUNIT: Component of the 90S pre-ribosomal particle.
CC {ECO:0000269|PubMed:17515605}.
CC -!- INTERACTION:
CC P25368; P32790: SLA1; NbExp=3; IntAct=EBI-16019, EBI-17313;
CC P25368; P53254: UTP22; NbExp=7; IntAct=EBI-16019, EBI-1878;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2610 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RRP7 family. {ECO:0000305}.
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DR EMBL; X59720; CAA42385.1; -; Genomic_DNA.
DR EMBL; V01310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006937; DAA07453.1; -; Genomic_DNA.
DR PIR; S17474; S17474.
DR RefSeq; NP_009899.1; NM_001178676.1.
DR PDB; 2MBY; NMR; -; A=256-297.
DR PDB; 4M5D; X-ray; 1.97 A; B=1-297.
DR PDB; 5WLC; EM; 3.80 A; NI=1-297.
DR PDB; 5WYJ; EM; 8.70 A; CA=1-297.
DR PDB; 5WYK; EM; 4.50 A; CA=1-297.
DR PDB; 6KE6; EM; 3.40 A; RF=1-297.
DR PDB; 6LQP; EM; 3.20 A; RF=1-297.
DR PDB; 6LQQ; EM; 4.10 A; RF=1-297.
DR PDB; 6LQR; EM; 8.60 A; RF=1-297.
DR PDB; 6LQS; EM; 3.80 A; RF=1-297.
DR PDB; 6LQT; EM; 4.90 A; RF=1-297.
DR PDB; 6LQU; EM; 3.70 A; RF=1-297.
DR PDB; 6ZQA; EM; 4.40 A; CN=1-297.
DR PDB; 6ZQB; EM; 3.90 A; CN=1-297.
DR PDB; 6ZQC; EM; 3.80 A; CN=1-297.
DR PDB; 6ZQD; EM; 3.80 A; CN=1-297.
DR PDB; 6ZQE; EM; 7.10 A; CN=1-297.
DR PDB; 6ZQF; EM; 4.90 A; CN=1-297.
DR PDB; 7AJT; EM; 4.60 A; CN=1-297.
DR PDB; 7AJU; EM; 3.80 A; CN=1-297.
DR PDB; 7D4I; EM; 4.00 A; RF=1-297.
DR PDB; 7D5S; EM; 4.60 A; RF=1-297.
DR PDB; 7D5T; EM; 6.00 A; RF=1-297.
DR PDB; 7D63; EM; 12.30 A; RF=1-297.
DR PDBsum; 2MBY; -.
DR PDBsum; 4M5D; -.
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; 6ZQA; -.
DR PDBsum; 6ZQB; -.
DR PDBsum; 6ZQC; -.
DR PDBsum; 6ZQD; -.
DR PDBsum; 6ZQE; -.
DR PDBsum; 6ZQF; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7D4I; -.
DR PDBsum; 7D5S; -.
DR PDBsum; 7D5T; -.
DR PDBsum; 7D63; -.
DR AlphaFoldDB; P25368; -.
DR BMRB; P25368; -.
DR SMR; P25368; -.
DR BioGRID; 30952; 130.
DR ComplexPortal; CPX-771; UTP-C complex variant 2.
DR ComplexPortal; CPX-772; UTP-C complex variant 1.
DR ComplexPortal; CPX-773; UTP-C complex variant 3.
DR ComplexPortal; CPX-774; CURI complex variant 1.
DR ComplexPortal; CPX-775; CURI complex variant 2.
DR ComplexPortal; CPX-776; CURI complex variant 3.
DR DIP; DIP-4974N; -.
DR IntAct; P25368; 27.
DR MINT; P25368; -.
DR STRING; 4932.YCL031C; -.
DR MaxQB; P25368; -.
DR PaxDb; P25368; -.
DR PRIDE; P25368; -.
DR EnsemblFungi; YCL031C_mRNA; YCL031C; YCL031C.
DR GeneID; 850326; -.
DR KEGG; sce:YCL031C; -.
DR SGD; S000000536; RRP7.
DR VEuPathDB; FungiDB:YCL031C; -.
DR eggNOG; KOG4008; Eukaryota.
DR GeneTree; ENSGT00390000018482; -.
DR HOGENOM; CLU_053375_0_0_1; -.
DR InParanoid; P25368; -.
DR OMA; FIRLMDP; -.
DR BioCyc; YEAST:G3O-29291-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P25368; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25368; protein.
DR GO; GO:0032545; C:CURI complex; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0032040; C:small-subunit processome; IPI:ComplexPortal.
DR GO; GO:0034456; C:UTP-C complex; IDA:SGD.
DR GO; GO:0019843; F:rRNA binding; IDA:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IDA:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:0060962; P:regulation of ribosomal protein gene transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IMP:SGD.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR InterPro; IPR040447; RRM_Rrp7.
DR InterPro; IPR040446; RRP7.
DR InterPro; IPR024326; RRP7_C.
DR PANTHER; PTHR13191; PTHR13191; 1.
DR Pfam; PF17799; RRM_Rrp7; 1.
DR Pfam; PF12923; RRP7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome; Ribosome biogenesis;
KW rRNA processing.
FT CHAIN 1..297
FT /note="Ribosomal RNA-processing protein 7"
FT /id="PRO_0000097457"
FT CONFLICT 66
FT /note="H -> R (in Ref. 4; V01310)"
FT /evidence="ECO:0000305"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 64..77
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 100..104
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 131..144
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 177..188
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 256..265
FT /evidence="ECO:0007829|PDB:2MBY"
FT HELIX 269..288
FT /evidence="ECO:0007829|PDB:2MBY"
SQ SEQUENCE 297 AA; 34470 MW; 768F43B0057788F2 CRC64;
MGIEDISAMK NGFIVVPFKL PDHKALPKSQ EASLHFMFAK RHQSSNSNES DCLFLVNLPL
LSNIEHMKKF VGQLCGKYDT VSHVEELLYN DEFGLHEVDL SALTSDLMSS TDVNEKRYTP
RNTALLKFVD AASINNCWNA LKKYSNLHAK HPNELFEWTY TTPSFTTFVN FYKPLDIDYL
KEDIHTHMAI FEQREAQAQE DVQSSIVDED GFTLVVGKNT KSLNSIRKKI LNKNPLSKHE
NKAKPISNID KKAKKDFYRF QVRERKKQEI NQLLSKFKED QERIKVMKAK RKFNPYT
