KRR1_YEAST
ID KRR1_YEAST Reviewed; 316 AA.
AC P25586; D6VQV7;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=KRR1 small subunit processome component;
DE AltName: Full=KRR-R motif-containing protein 1;
DE AltName: Full=Ribosomal RNA assembly protein KRR1;
GN Name=KRR1; OrderedLocusNames=YCL059C; ORFNames=YCL59C;
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=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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP IDENTIFICATION.
RX PubMed=8675026; DOI=10.1016/0378-1119(96)00024-8;
RA Gromadka R., Kaniak A., Slonimski P.P., Rytka J.;
RT "A novel cross-phylum family of proteins comprises a KRR1 (YCL059c) gene
RT which is essential for viability of Saccharomyces cerevisiae cells.";
RL Gene 171:27-32(1996).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11996121;
RA Gromadka R., Rytka J.;
RT "The KRR1 gene encodes a protein required for 18S rRNA synthesis and 40S
RT ribosomal subunit assembly in Saccharomyces cerevisiae.";
RL Acta Biochim. Pol. 47:993-1005(2000).
RN [6]
RP FUNCTION, INTERACTION WITH KRI1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-20; PHE-45; LYS-66; LEU-95; CYS-162; ARG-207 AND ASP-261.
RX PubMed=11027267; DOI=10.1128/mcb.20.21.7971-7979.2000;
RA Sasaki T., Toh-e A., Kikuchi Y.;
RT "Yeast Krr1p physically and functionally interacts with a novel essential
RT Kri1p, and both proteins are required for 40S ribosome biogenesis in the
RT nucleolus.";
RL Mol. Cell. Biol. 20:7971-7979(2000).
RN [7]
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 [8]
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 [9]
RP FUNCTION, INTERACTION WITH RIBOSOMAL PROTEINS AND KRI1, SUBCELLULAR
RP LOCATION, AND MUTANT KRR1-21.
RX PubMed=15094838;
RA Gromadka R., Karkusiewicz I., Rempola B., Rytka J.;
RT "Functional and physical interactions of Krr1p, a Saccharomyces cerevisiae
RT nucleolar protein.";
RL Acta Biochim. Pol. 51:173-187(2004).
RN [10]
RP FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU
RP PROCESSOME, AND SUBCELLULAR LOCATION.
RX PubMed=15590835; DOI=10.1128/ec.3.6.1619-1626.2004;
RA Bernstein K.A., Gallagher J.E.G., Mitchell B.M., Granneman S.,
RA Baserga S.J.;
RT "The small-subunit processome is a ribosome assembly intermediate.";
RL Eukaryot. Cell 3:1619-1626(2004).
CC -!- FUNCTION: Required for 40S ribosome biogenesis. Involved in nucleolar
CC processing of pre-18S ribosomal RNA and ribosome assembly. Essential
CC for vegetative growth. {ECO:0000269|PubMed:11027267,
CC ECO:0000269|PubMed:11996121, ECO:0000269|PubMed:15094838,
CC ECO:0000269|PubMed:15590835}.
CC -!- SUBUNIT: Component of the ribosomal small subunit (SSU) processome
CC composed of at least 40 protein subunits and snoRNA U3. Interacts with
CC snoRNA U3. Interacts with MPP10, KRI1 and with ribosomal proteins
CC RPS1A, RPS4A, RPS4B, RPS8A, RPS8B, RPS11A, RPS11B, RPS13, RPS24, RPS25,
CC RPL4A, RPL7B, RPL8, RPL23, RPL25 and RPL28.
CC {ECO:0000269|PubMed:11027267, ECO:0000269|PubMed:15094838,
CC ECO:0000269|PubMed:15590835}.
CC -!- INTERACTION:
CC P25586; P38333: ENP1; NbExp=5; IntAct=EBI-21773, EBI-6482;
CC P25586; P42846: KRI1; NbExp=2; IntAct=EBI-21773, EBI-28360;
CC P25586; P15646: NOP1; NbExp=4; IntAct=EBI-21773, EBI-6838;
CC P25586; Q12481: RRP36; NbExp=3; IntAct=EBI-21773, EBI-31770;
CC P25586; Q12136: SAS10; NbExp=3; IntAct=EBI-21773, EBI-36084;
CC P25586; P53866: SQS1; NbExp=2; IntAct=EBI-21773, EBI-29168;
CC P25586; P40362: UTP18; NbExp=2; IntAct=EBI-21773, EBI-4534;
CC P25586; P53254: UTP22; NbExp=3; IntAct=EBI-21773, EBI-1878;
CC P25586; Q02354: UTP6; NbExp=3; IntAct=EBI-21773, EBI-22119;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11027267,
CC ECO:0000269|PubMed:11996121, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15094838, ECO:0000269|PubMed:15590835}.
CC -!- MISCELLANEOUS: Present with 4340 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Cold-sensitive mutant KRR1-21 is a deletion of amino
CC acids 234-239.
CC -!- SIMILARITY: Belongs to the KRR1 family. {ECO:0000305}.
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DR EMBL; X59720; CAA42386.1; -; Genomic_DNA.
DR EMBL; AY692923; AAT92942.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07426.1; -; Genomic_DNA.
DR PIR; S19389; S19389.
DR RefSeq; NP_009872.1; NM_001178703.1.
DR PDB; 4QMF; X-ray; 2.80 A; B/D=32-222.
DR PDB; 5WLC; EM; 3.80 A; NK=1-316.
DR PDB; 5WYJ; EM; 8.70 A; K1=1-316.
DR PDB; 5WYK; EM; 4.50 A; K1=1-316.
DR PDB; 6KE6; EM; 3.40 A; RC=1-316.
DR PDB; 6LQP; EM; 3.20 A; RC=1-316.
DR PDB; 6LQQ; EM; 4.10 A; RC=1-316.
DR PDB; 6LQU; EM; 3.70 A; RC=1-316.
DR PDB; 6ZQA; EM; 4.40 A; JO=1-316.
DR PDB; 6ZQB; EM; 3.90 A; JO=1-316.
DR PDB; 6ZQC; EM; 3.80 A; JO=1-316.
DR PDB; 7AJT; EM; 4.60 A; JO=1-316.
DR PDB; 7D5S; EM; 4.60 A; RC=1-316.
DR PDBsum; 4QMF; -.
DR PDBsum; 5WLC; -.
DR PDBsum; 5WYJ; -.
DR PDBsum; 5WYK; -.
DR PDBsum; 6KE6; -.
DR PDBsum; 6LQP; -.
DR PDBsum; 6LQQ; -.
DR PDBsum; 6LQU; -.
DR PDBsum; 6ZQA; -.
DR PDBsum; 6ZQB; -.
DR PDBsum; 6ZQC; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7D5S; -.
DR AlphaFoldDB; P25586; -.
DR SMR; P25586; -.
DR BioGRID; 30927; 742.
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-1408N; -.
DR IntAct; P25586; 77.
DR MINT; P25586; -.
DR STRING; 4932.YCL059C; -.
DR MaxQB; P25586; -.
DR PaxDb; P25586; -.
DR PRIDE; P25586; -.
DR EnsemblFungi; YCL059C_mRNA; YCL059C; YCL059C.
DR GeneID; 850298; -.
DR KEGG; sce:YCL059C; -.
DR SGD; S000000564; KRR1.
DR VEuPathDB; FungiDB:YCL059C; -.
DR eggNOG; KOG2874; Eukaryota.
DR GeneTree; ENSGT00390000018775; -.
DR HOGENOM; CLU_040185_0_2_1; -.
DR InParanoid; P25586; -.
DR OMA; HKKEKFV; -.
DR BioCyc; YEAST:G3O-29310-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P25586; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25586; 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:0030688; C:preribosome, small subunit precursor; IDA:GO_Central.
DR GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:SGD.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR Gene3D; 3.30.1370.10; -; 2.
DR InterPro; IPR041174; KH_8.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR024166; rRNA_assembly_KRR1.
DR PANTHER; PTHR12581; PTHR12581; 1.
DR Pfam; PF17903; KH_8; 1.
DR PIRSF; PIRSF006515; KRR1; 1.
DR SMART; SM00322; KH; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome; Ribonucleoprotein;
KW Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..316
FT /note="KRR1 small subunit processome component"
FT /id="PRO_0000202553"
FT DOMAIN 122..192
FT /note="KH"
FT REGION 279..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 20
FT /note="K->E: In temperature-sensitive mutant KRR1-17; grows
FT normally at 25 degrees Celsius but fails to grow at 35
FT degrees Celsius; when associated with N-66; R-162 and A-
FT 261."
FT /evidence="ECO:0000269|PubMed:11027267"
FT MUTAGEN 45
FT /note="F->L: In temperature-sensitive mutant KRR1-18; grows
FT normally at 25 degrees Celsius but fails to grow at 35
FT degrees Celsius; when associated with S-95 and G-207."
FT /evidence="ECO:0000269|PubMed:11027267"
FT MUTAGEN 66
FT /note="K->N: In temperature-sensitive mutant KRR1-17; grows
FT normally at 25 degrees Celsius but fails to grow at 35
FT degrees Celsius; when associated with E-20; R-162 and A-
FT 261."
FT /evidence="ECO:0000269|PubMed:11027267"
FT MUTAGEN 95
FT /note="L->S: In temperature-sensitive mutant KRR1-18; grows
FT normally at 25 degrees Celsius but fails to grow at 35
FT degrees Celsius; when associated with L-45 and G-207."
FT /evidence="ECO:0000269|PubMed:11027267"
FT MUTAGEN 162
FT /note="C->R: In temperature-sensitive mutant KRR1-17; grows
FT normally at 25 degrees Celsius but fails to grow at 35
FT degrees Celsius; when associated with E-20; N-66 and A-
FT 261."
FT /evidence="ECO:0000269|PubMed:11027267"
FT MUTAGEN 207
FT /note="R->G: In temperature-sensitive mutant KRR1-18; grows
FT normally at 25 degrees Celsius but fails to grow at 35
FT degrees Celsius; when associated with L-45 and S-95."
FT /evidence="ECO:0000269|PubMed:11027267"
FT MUTAGEN 261
FT /note="D->A: In temperature-sensitive mutant KRR1-17; grows
FT normally at 25 degrees Celsius but fails to grow at 35
FT degrees Celsius; when associated with E-20; N-66 and R-
FT 162."
FT /evidence="ECO:0000269|PubMed:11027267"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:4QMF"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:4QMF"
FT HELIX 50..65
FT /evidence="ECO:0007829|PDB:4QMF"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:4QMF"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:4QMF"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:4QMF"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:4QMF"
FT HELIX 93..105
FT /evidence="ECO:0007829|PDB:4QMF"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:4QMF"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:4QMF"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:4QMF"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:4QMF"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:4QMF"
FT HELIX 136..146
FT /evidence="ECO:0007829|PDB:4QMF"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:4QMF"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:4QMF"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:4QMF"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:4QMF"
FT HELIX 177..191
FT /evidence="ECO:0007829|PDB:4QMF"
FT HELIX 197..209
FT /evidence="ECO:0007829|PDB:4QMF"
SQ SEQUENCE 316 AA; 37159 MW; 7A7F964E2C7FD056 CRC64;
MVSTHNRDKP WDTDDIDKWK IEEFKEEDNA SGQPFAEESS FMTLFPKYRE SYLKTIWNDV
TRALDKHNIA CVLDLVEGSM TVKTTRKTYD PAIILKARDL IKLLARSVPF PQAVKILQDD
MACDVIKIGN FVTNKERFVK RRQRLVGPNG NTLKALELLT KCYILVQGNT VSAMGPFKGL
KEVRRVVEDC MKNIHPIYHI KELMIKRELA KRPELANEDW SRFLPMFKKR NVARKKPKKI
RNVEKKVYTP FPPAQLPRKV DLEIESGEYF LSKREKQMKK LNEQKEKQME REIERQEERA
KDFIAPEEEA YKPNQN
