RRN3_YEAST
ID RRN3_YEAST Reviewed; 627 AA.
AC P36070; D6VX70;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=RNA polymerase I-specific transcription initiation factor RRN3;
GN Name=RRN3; OrderedLocusNames=YKL125W;
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], AND CHARACTERIZATION.
RX PubMed=8670901; DOI=10.1002/j.1460-2075.1996.tb00770.x;
RA Yamamoto R.T., Nogi Y., Dodd J.A., Nomura M.;
RT "RRN3 gene of Saccharomyces cerevisiae encodes an essential RNA polymerase
RT I transcription factor which interacts with the polymerase independently of
RT DNA template.";
RL EMBO J. 15:3964-3973(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 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 [5]
RP INTERACTION WITH NOP53.
RX PubMed=18631361; DOI=10.1111/j.1742-4658.2008.06565.x;
RA Granato D.C., Machado-Santelli G.M., Oliveira C.C.;
RT "Nop53p interacts with 5.8S rRNA co-transcriptionally, and regulates
RT processing of pre-rRNA by the exosome.";
RL FEBS J. 275:4164-4178(2008).
CC -!- FUNCTION: Required for efficient transcription initiation by RNA
CC polymerase I. Interacts with Pol I in the absence of template DNA and
CC stimulates recruitment of Pol I, but does not remain as part of stable
CC preinitiation complex.
CC -!- SUBUNIT: Monomer (Probable). Interacts with NOP53.
CC {ECO:0000269|PubMed:18631361, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 138 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RRN3 family. {ECO:0000305}.
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DR EMBL; Z71927; CAA96470.1; -; Genomic_DNA.
DR EMBL; Z28125; CAA81966.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09036.1; -; Genomic_DNA.
DR PIR; S37954; S37954.
DR RefSeq; NP_012797.1; NM_001179691.1.
DR PDB; 3TJ1; X-ray; 2.85 A; A/B=1-627.
DR PDB; 5G5L; EM; 4.80 A; O=1-627.
DR PDB; 5N5Y; EM; 7.70 A; O=1-627.
DR PDB; 5N5Z; EM; 7.70 A; O=1-627.
DR PDB; 5N60; EM; 7.70 A; O=1-627.
DR PDB; 5N61; EM; 3.40 A; O=1-627.
DR PDB; 5OA1; EM; 4.40 A; O=1-627.
DR PDB; 6RQH; EM; 3.70 A; O=1-627.
DR PDB; 6RQL; EM; 2.90 A; O=1-627.
DR PDB; 6RQT; EM; 4.00 A; O=1-627.
DR PDB; 6RRD; EM; 3.10 A; O=1-627.
DR PDB; 6RUI; EM; 2.70 A; O=1-627.
DR PDB; 6RUO; EM; 3.50 A; O=1-627.
DR PDB; 6RWE; EM; 3.00 A; O=1-627.
DR PDB; 6TPS; EM; 3.54 A; O=1-627.
DR PDBsum; 3TJ1; -.
DR PDBsum; 5G5L; -.
DR PDBsum; 5N5Y; -.
DR PDBsum; 5N5Z; -.
DR PDBsum; 5N60; -.
DR PDBsum; 5N61; -.
DR PDBsum; 5OA1; -.
DR PDBsum; 6RQH; -.
DR PDBsum; 6RQL; -.
DR PDBsum; 6RQT; -.
DR PDBsum; 6RRD; -.
DR PDBsum; 6RUI; -.
DR PDBsum; 6RUO; -.
DR PDBsum; 6RWE; -.
DR PDBsum; 6TPS; -.
DR AlphaFoldDB; P36070; -.
DR SMR; P36070; -.
DR BioGRID; 34011; 157.
DR DIP; DIP-6657N; -.
DR IntAct; P36070; 9.
DR MINT; P36070; -.
DR STRING; 4932.YKL125W; -.
DR MaxQB; P36070; -.
DR PaxDb; P36070; -.
DR PRIDE; P36070; -.
DR EnsemblFungi; YKL125W_mRNA; YKL125W; YKL125W.
DR GeneID; 853734; -.
DR KEGG; sce:YKL125W; -.
DR SGD; S000001608; RRN3.
DR VEuPathDB; FungiDB:YKL125W; -.
DR eggNOG; KOG2434; Eukaryota.
DR GeneTree; ENSGT00390000001488; -.
DR HOGENOM; CLU_010579_2_0_1; -.
DR InParanoid; P36070; -.
DR OMA; FKHFYAA; -.
DR BioCyc; YEAST:G3O-31907-MON; -.
DR Reactome; R-SCE-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-SCE-73772; RNA Polymerase I Promoter Escape.
DR PRO; PR:P36070; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36070; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000182; F:rDNA binding; IDA:SGD.
DR GO; GO:0001042; F:RNA polymerase I core binding; IDA:SGD.
DR GO; GO:0001181; F:RNA polymerase I general transcription initiation factor activity; IDA:SGD.
DR GO; GO:0001179; F:RNA polymerase I general transcription initiation factor binding; IDA:SGD.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; IMP:SGD.
DR InterPro; IPR007991; RNA_pol_I_trans_ini_fac_RRN3.
DR PANTHER; PTHR12790; PTHR12790; 1.
DR Pfam; PF05327; RRN3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..627
FT /note="RNA polymerase I-specific transcription initiation
FT factor RRN3"
FT /id="PRO_0000211430"
FT REGION 263..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..284
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 61..66
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 90..100
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 104..108
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 123..126
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 130..146
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:3TJ1"
FT HELIX 151..159
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 170..182
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:3TJ1"
FT HELIX 187..194
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:5N61"
FT HELIX 205..220
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 227..245
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:6RRD"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:3TJ1"
FT HELIX 327..346
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 349..353
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 357..368
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 369..374
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:6RQL"
FT HELIX 383..388
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 393..396
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 397..401
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 402..407
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 414..430
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:6RUO"
FT HELIX 436..457
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 459..461
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 462..465
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 467..470
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 471..486
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 488..490
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:6RQL"
FT HELIX 499..501
FT /evidence="ECO:0007829|PDB:3TJ1"
FT HELIX 502..509
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 516..518
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 522..534
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 541..550
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 583..586
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 587..590
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 602..606
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 607..609
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 613..616
FT /evidence="ECO:0007829|PDB:3TJ1"
SQ SEQUENCE 627 AA; 72388 MW; A31E7386A9873FDB CRC64;
MMAFENTSKR PPQDFVAPID QKKRKVQFSD STGLVTLQPE EIKDEVFSAA MYSRFVKSAL
DDLDKNDSTQ IGIIANQVAL PSKNPERIND KNLNILLDIL SSNINRIESS RGTFLIQSII
NFEKWWELPP HTLSKYIYFI KILCSSIPKW WQDVSMILVS CFILPIKQTV CHHDMLKYFL
RMIPSSMGFI DTYLAKFFPN KNDTRRKLVN YTSNLLKLRG YCSELGFQIW SLLIEKIISI
DVELQNELDE LDDDVDDDDL EEVDLEDDDD LDDDSGDDDD ENCGNSNEEL RSGAADGSQS
DSEDMDIIEG MDGTEEYNVE LTQGIKELST KLDSILTLVS THVEEQVTPE SLESGEGVGV
FNTLTTLFKT HVLPTYYTRS IQYIMFHVSQ QQLELMDSFL VTLIDISFAV NEAAEKKIKS
LQYLGSYIAR AKKLSRTQII FVASYLTSWL NRYVIEREEE VDQRGGMERF KHFYAAFQAL
CYIFCFRHNI FRDTDGNWEC ELDKFFQRMV ISKFNPLKFC NENVMLMFAR IAQQESVAYC
FSIIENNNNE RLRGIIGKAD SDKKENSAQA NTTSSSWSLA TRQQFIDLQS YFPYDPLFLK
NYKILMKEYY IEWSEASGEY ESDGSDD
