PNO1_YEAST
ID PNO1_YEAST Reviewed; 274 AA.
AC Q99216; D6W2K3; Q02462; Q7LHP7;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Pre-rRNA-processing protein PNO1;
DE AltName: Full=Partner of NOB1;
DE AltName: Full=Ribosomal RNA-processing protein 20;
GN Name=PNO1; Synonyms=DIM2, RRP20; OrderedLocusNames=YOR145C;
GN ORFNames=O3513, YOR3513C;
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].
RC STRAIN=S288c / FY1678;
RX PubMed=9046089;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<73::aid-yea52>3.0.co;2-m;
RA Bordonne R., Camasses A., Madania A., Poch O., Tarassov I.A., Winsor B.,
RA Martin R.P.;
RT "Analysis of a 35.6 kb region on the right arm of Saccharomyces cerevisiae
RT chromosome XV.";
RL Yeast 13:73-83(1997).
RN [2]
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 [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 57-274.
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=10923024;
RX DOI=10.1002/1097-0061(200008)16:11<1025::aid-yea602>3.0.co;2-1;
RA Grava S., Dumoulin P., Madania A., Tarassov I., Winsor B.;
RT "Functional analysis of six genes from chromosomes XIV and XV of
RT Saccharomyces cerevisiae reveals YOR145c as an essential gene and
RT YNL059c/ARP5 as a strain-dependent essential gene encoding nuclear
RT proteins.";
RL Yeast 16:1025-1033(2000).
RN [6]
RP FUNCTION, INTERACTION WITH NOB1, AND MUTAGENESIS OF GLY-203.
RX PubMed=12502737; DOI=10.1101/gad.1025602;
RA Tone Y., Toh-e A.;
RT "Nob1p is required for biogenesis of the 26S proteasome and degraded upon
RT its maturation in Saccharomyces cerevisiae.";
RL Genes Dev. 16:3142-3157(2002).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=12628929; DOI=10.1093/emboj/cdg121;
RA Schaefer T., Strauss D., Petfalski E., Tollervey D., Hurt E.;
RT "The path from nucleolar 90S to cytoplasmic 40S pre-ribosomes.";
RL EMBO J. 22:1370-1380(2003).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF GLY-235.
RX PubMed=12736301; DOI=10.1093/nar/gkg366;
RA Senapin S., Clark-Walker G.D., Chen X.J., Seraphin B., Daugeron M.-C.;
RT "RRP20, a component of the 90S preribosome, is required for pre-18S rRNA
RT processing in Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 31:2524-2533(2003).
RN [9]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=15037774; DOI=10.1261/rna.5162204;
RA Vanrobays E., Gelugne J.-P., Caizergues-Ferrer M., Lafontaine D.L.J.;
RT "Dim2p, a KH-domain protein required for small ribosomal subunit
RT synthesis.";
RL RNA 10:645-656(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND THR-51, AND
RP 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).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [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: Required for small ribosomal subunit (SSU) synthesis. Has a
CC role in the processing of early nucleolar and late cytoplasmic pre-RNA
CC species. Recruits DIM1 to nucleolar pre-RNAs. Indirectly required for
CC cleavage at the A2 site of the 20S pre-rRNA, forming 18S rRNA, and at
CC A1 and A2 sites of other pre-rRNAs. {ECO:0000269|PubMed:12502737,
CC ECO:0000269|PubMed:12736301, ECO:0000269|PubMed:15037774}.
CC -!- SUBUNIT: Component of the small ribosomal subunit, ribosomal RNA
CC processing complex (SSU RRP complex). Interacts with NOB1.
CC {ECO:0000269|PubMed:12502737, ECO:0000269|PubMed:15037774}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12628929,
CC ECO:0000269|PubMed:15037774}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:10923024, ECO:0000269|PubMed:15037774}.
CC -!- SIMILARITY: Belongs to the PNO1 family. {ECO:0000305}.
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DR EMBL; U55020; AAC49632.1; -; Genomic_DNA.
DR EMBL; Z75053; CAA99349.1; -; Genomic_DNA.
DR EMBL; X94335; CAA64063.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10919.1; -; Genomic_DNA.
DR PIR; S67033; S67033.
DR RefSeq; NP_014788.1; NM_001183564.1.
DR PDB; 5WLC; EM; 3.80 A; SO=1-274.
DR PDB; 5WYJ; EM; 8.70 A; P1=1-274.
DR PDB; 5WYK; EM; 4.50 A; P1=1-274.
DR PDB; 6EML; EM; 3.60 A; p=1-274.
DR PDB; 6FAI; EM; 3.40 A; h=1-274.
DR PDB; 6RBD; EM; 3.47 A; h=1-274.
DR PDB; 6Y7C; EM; 3.80 A; h=1-274.
DR PDB; 6ZQA; EM; 4.40 A; JJ=1-274.
DR PDB; 6ZQB; EM; 3.90 A; JJ=1-274.
DR PDB; 6ZQC; EM; 3.80 A; JJ=1-274.
DR PDB; 6ZQD; EM; 3.80 A; JJ=1-274.
DR PDB; 6ZQE; EM; 7.10 A; JJ=1-274.
DR PDB; 6ZQF; EM; 4.90 A; JJ=1-274.
DR PDB; 6ZQG; EM; 3.50 A; JJ=1-274.
DR PDB; 7AJT; EM; 4.60 A; JJ=1-274.
DR PDB; 7AJU; EM; 3.80 A; JJ=1-274.
DR PDBsum; 5WLC; -.
DR PDBsum; 5WYJ; -.
DR PDBsum; 5WYK; -.
DR PDBsum; 6EML; -.
DR PDBsum; 6FAI; -.
DR PDBsum; 6RBD; -.
DR PDBsum; 6Y7C; -.
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 AlphaFoldDB; Q99216; -.
DR SMR; Q99216; -.
DR BioGRID; 34542; 110.
DR DIP; DIP-4687N; -.
DR IntAct; Q99216; 24.
DR MINT; Q99216; -.
DR STRING; 4932.YOR145C; -.
DR iPTMnet; Q99216; -.
DR MaxQB; Q99216; -.
DR PaxDb; Q99216; -.
DR PRIDE; Q99216; -.
DR EnsemblFungi; YOR145C_mRNA; YOR145C; YOR145C.
DR GeneID; 854317; -.
DR KEGG; sce:YOR145C; -.
DR SGD; S000005671; PNO1.
DR VEuPathDB; FungiDB:YOR145C; -.
DR eggNOG; KOG3273; Eukaryota.
DR GeneTree; ENSGT00390000018052; -.
DR HOGENOM; CLU_064992_0_2_1; -.
DR InParanoid; Q99216; -.
DR OMA; IHIMGSF; -.
DR BioCyc; YEAST:G3O-33664-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q99216; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q99216; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IDA: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: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:0043248; P:proteasome assembly; IMP:SGD.
DR Gene3D; 3.30.1370.10; -; 1.
DR InterPro; IPR041174; KH_8.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR039912; PNO1-like.
DR PANTHER; PTHR12826:SF13; PTHR12826:SF13; 1.
DR Pfam; PF17903; KH_8; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; RNA-binding.
FT CHAIN 1..274
FT /note="Pre-rRNA-processing protein PNO1"
FT /id="PRO_0000270553"
FT DOMAIN 195..247
FT /note="KH"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 51
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 203
FT /note="G->D: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:12502737"
FT MUTAGEN 235
FT /note="G->D: Accumulation of aberrant 22S and 23S rRNA
FT intermediates."
FT /evidence="ECO:0000269|PubMed:12736301"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 106..123
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:6FAI"
FT TURN 132..135
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:6RBD"
FT HELIX 149..163
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 168..176
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 178..186
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 196..206
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 211..218
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 228..236
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 237..251
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 256..272
FT /evidence="ECO:0007829|PDB:6FAI"
SQ SEQUENCE 274 AA; 30332 MW; F61E17CAB85BF60C CRC64;
MVAPTALKKA TVTPVSGQDG GSSRIIGINN TESIDEDDDD DVLLDDSDNN TAKEEVEGEE
GSRKTHESKT VVVDDQGKPR FTSASKTQGN KIKFESRKIM VPPHRMTPLR NSWTKIYPPL
VEHLKLQVRM NLKTKSVELR TNPKFTTDPG ALQKGADFIK AFTLGFDLDD SIALLRLDDL
YIETFEVKDV KTLTGDHLSR AIGRIAGKDG KTKFAIENAT RTRIVLADSK IHILGGFTHI
RMARESVVSL ILGSPPGKVY GNLRTVASRL KERY
