RRN7_YEAST
ID RRN7_YEAST Reviewed; 514 AA.
AC P40992; D6VWF7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=RNA polymerase I-specific transcription initiation factor RRN7;
GN Name=RRN7; OrderedLocusNames=YJL025W; ORFNames=J1273;
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 IDENTIFICATION IN THE CF COMPLEX.
RX PubMed=7958901; DOI=10.1101/gad.8.19.2349;
RA Keys D.A., Vu L., Steffan J.S., Dodd J.A., Yamamoto R.T., Nogi Y.,
RA Nomura M.;
RT "RRN6 and RRN7 encode subunits of a multiprotein complex essential for the
RT initiation of rDNA transcription by RNA polymerase I in Saccharomyces
RT cerevisiae.";
RL Genes Dev. 8:2349-2362(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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].
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 [5]
RP INTERACTION WITH RRN9.
RX PubMed=8895657; DOI=10.1101/gad.10.20.2551;
RA Steffan J.S., Keys D.A., Dodd J.A., Nomura M.;
RT "The role of TBP in rDNA transcription by RNA polymerase I in Saccharomyces
RT cerevisiae: TBP is required for upstream activation factor-dependent
RT recruitment of core factor.";
RL Genes Dev. 10:2551-2563(1996).
RN [6]
RP INTERACTION WITH RRN6; RRN11 AND SPT15.
RX PubMed=8702872; DOI=10.1074/jbc.271.35.21062;
RA Lalo D., Steffan J.S., Dodd J.A., Nomura M.;
RT "RRN11 encodes the third subunit of the complex containing Rrn6p and Rrn7p
RT that is essential for the initiation of rDNA transcription by yeast RNA
RT polymerase I.";
RL J. Biol. Chem. 271:21062-21067(1996).
RN [7]
RP FUNCTION OF THE CF COMPLEX.
RX PubMed=8887672; DOI=10.1128/mcb.16.11.6436;
RA Lin C.W., Moorefield B., Payne J., Aprikian P., Mitomo K., Reeder R.H.;
RT "A novel 66-kilodalton protein complexes with Rrn6, Rrn7, and TATA-binding
RT protein to promote polymerase I transcription initiation in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 16:6436-6443(1996).
RN [8]
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 [9]
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 [10]
RP FUNCTION.
RX PubMed=21940764; DOI=10.1101/gad.17363311;
RA Blattner C., Jennebach S., Herzog F., Mayer A., Cheung A.C., Witte G.,
RA Lorenzen K., Hopfner K.P., Heck A.J., Aebersold R., Cramer P.;
RT "Molecular basis of Rrn3-regulated RNA polymerase I initiation and cell
RT growth.";
RL Genes Dev. 25:2093-2105(2011).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF CYS-29 AND HIS-33.
RX PubMed=21921198; DOI=10.1126/science.1207699;
RA Knutson B.A., Hahn S.;
RT "Yeast Rrn7 and human TAF1B are TFIIB-related RNA polymerase I general
RT transcription factors.";
RL Science 333:1637-1640(2011).
CC -!- FUNCTION: Component of RNA polymerase I core factor complex (CF) that
CC acts as a SUA7/TFIIB-like factor and plays a key role in multiple steps
CC during transcription initiation such as pre-initiation complex (PIC)
CC assembly and postpolymerase recruitment events in polymerase I (Pol I)
CC transcription. Binds rDNA promoters and plays a role in Pol I
CC recruitment. After binding of UAF (upstream activation factor) to an
CC upstream element of the promoter, CF is recruited in a SPT15/TBP-
CC dependent manner to form a pre-initiation complex.
CC {ECO:0000269|PubMed:21921198, ECO:0000269|PubMed:21940764,
CC ECO:0000269|PubMed:8887672}.
CC -!- SUBUNIT: Component of the core factor (CF) complex, which consists of
CC RRN6, RRN7 and RRN11. The CF heterotrimer may further dimerize to form
CC a hexamer. RRN7 interacts with RRN6, RRN11, SPT15 and RRN9.
CC {ECO:0000269|PubMed:7958901, ECO:0000269|PubMed:8702872,
CC ECO:0000269|PubMed:8895657}.
CC -!- INTERACTION:
CC P40992; Q04712: RRN11; NbExp=2; IntAct=EBI-15990, EBI-27790;
CC P40992; P32786: RRN6; NbExp=4; IntAct=EBI-15990, EBI-15986;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: Although it shares weak sequence similarity with SUA7/TFIIB,
CC displays a similar subdomain organization as SUA7/TFIIB, with a N-
CC terminal zinc finger, a connecting region (composed of B-reader and B-
CC linker regions), followed by 2 cyclin folds.
CC {ECO:0000269|PubMed:21921198}.
CC -!- MISCELLANEOUS: Present with 398 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RRN7/TAF1B family. {ECO:0000305}.
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DR EMBL; L33864; AAA53131.1; -; Genomic_DNA.
DR EMBL; Z49300; CAA89316.1; -; Genomic_DNA.
DR EMBL; AY692999; AAT93018.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08773.1; -; Genomic_DNA.
DR PIR; S50785; S50785.
DR RefSeq; NP_012509.1; NM_001181459.1.
DR PDB; 5N5Y; EM; 7.70 A; Q=1-514.
DR PDB; 5N5Z; EM; 7.70 A; Q=1-514.
DR PDB; 5N60; EM; 7.70 A; Q=1-514.
DR PDB; 5N61; EM; 3.40 A; Q=1-514.
DR PDB; 5O7X; X-ray; 3.20 A; B/E/H/K/N/Q=1-514.
DR PDB; 5OA1; EM; 4.40 A; U=1-514.
DR PDB; 5W5Y; EM; 3.80 A; P=1-514.
DR PDB; 5W64; EM; 4.20 A; P=1-514.
DR PDB; 5W65; EM; 4.30 A; P=1-514.
DR PDB; 5W66; EM; 3.90 A; P=1-514.
DR PDB; 6RQH; EM; 3.70 A; Q=1-514.
DR PDB; 6RQL; EM; 2.90 A; Q=1-514.
DR PDB; 6RRD; EM; 3.10 A; Q=1-514.
DR PDB; 6RUI; EM; 2.70 A; Q=1-514.
DR PDB; 6RUO; EM; 3.50 A; Q=1-514.
DR PDB; 6RWE; EM; 3.00 A; Q=1-514.
DR PDB; 6TPS; EM; 3.54 A; Q=1-514.
DR PDBsum; 5N5Y; -.
DR PDBsum; 5N5Z; -.
DR PDBsum; 5N60; -.
DR PDBsum; 5N61; -.
DR PDBsum; 5O7X; -.
DR PDBsum; 5OA1; -.
DR PDBsum; 5W5Y; -.
DR PDBsum; 5W64; -.
DR PDBsum; 5W65; -.
DR PDBsum; 5W66; -.
DR PDBsum; 6RQH; -.
DR PDBsum; 6RQL; -.
DR PDBsum; 6RRD; -.
DR PDBsum; 6RUI; -.
DR PDBsum; 6RUO; -.
DR PDBsum; 6RWE; -.
DR PDBsum; 6TPS; -.
DR AlphaFoldDB; P40992; -.
DR SMR; P40992; -.
DR BioGRID; 33734; 161.
DR ComplexPortal; CPX-1836; RNA polymerase I core factor complex.
DR DIP; DIP-1594N; -.
DR IntAct; P40992; 13.
DR MINT; P40992; -.
DR STRING; 4932.YJL025W; -.
DR MaxQB; P40992; -.
DR PaxDb; P40992; -.
DR PRIDE; P40992; -.
DR TopDownProteomics; P40992; -.
DR EnsemblFungi; YJL025W_mRNA; YJL025W; YJL025W.
DR GeneID; 853428; -.
DR KEGG; sce:YJL025W; -.
DR SGD; S000003562; RRN7.
DR VEuPathDB; FungiDB:YJL025W; -.
DR eggNOG; ENOG502RYCI; Eukaryota.
DR HOGENOM; CLU_016553_3_1_1; -.
DR InParanoid; P40992; -.
DR OMA; GLTICQF; -.
DR BioCyc; YEAST:G3O-31495-MON; -.
DR Reactome; R-SCE-73772; RNA Polymerase I Promoter Escape.
DR PRO; PR:P40992; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P40992; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0070860; C:RNA polymerase I core factor complex; IDA:UniProtKB.
DR GO; GO:0005668; C:RNA polymerase transcription factor SL1 complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001164; F:RNA polymerase I core promoter sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0017025; F:TBP-class protein binding; IDA:SGD.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IDA:SGD.
DR InterPro; IPR033599; TAF1B/Rrn7.
DR InterPro; IPR021752; TF_Rrn7_Zf.
DR PANTHER; PTHR31576; PTHR31576; 2.
DR Pfam; PF11781; zf-RRN7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..514
FT /note="RNA polymerase I-specific transcription initiation
FT factor RRN7"
FT /id="PRO_0000097450"
FT ZN_FING 3..36
FT /note="RRN7-type"
FT REGION 37..66
FT /note="B-reader"
FT REGION 67..101
FT /note="B-linker"
FT REGION 102..210
FT /note="N-terminal cyclin fold"
FT REGION 211..320
FT /note="C-terminal cyclin fold"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT MUTAGEN 29
FT /note="C->A: Impaired binding to Pol I."
FT /evidence="ECO:0000269|PubMed:21921198"
FT MUTAGEN 33
FT /note="H->S: Impaired binding to Pol I."
FT /evidence="ECO:0000269|PubMed:21921198"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:6RQL"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:5N61"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 99..121
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 128..145
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 160..171
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 178..183
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 184..188
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:5N61"
FT TURN 194..198
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 203..206
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 209..213
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:5O7X"
FT HELIX 225..236
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 249..260
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 265..276
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:5O7X"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:5N61"
FT HELIX 302..319
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 328..338
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 347..356
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 365..368
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 371..385
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 407..416
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 422..424
FT /evidence="ECO:0007829|PDB:6RQL"
FT STRAND 426..429
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 438..448
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 470..476
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 477..489
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 490..492
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 495..513
FT /evidence="ECO:0007829|PDB:6RUI"
SQ SEQUENCE 514 AA; 60357 MW; 30459F9BC27197D6 CRC64;
MSTFIRGPIC GTDNCPSRLW RIIDGRRTCQ YGHVMEGDVE FNDDEDDLNG LGAGVITRRL
NLTTNATGSF QSSQLTNSQL LQQQQRQSHK KFKKLIGHEA KLLFLKSFQF ILKRQIRWLI
TEMRFPKEFE HVAKIIWLKI LKTINDQPQE ELKLQLHMTS TISILYLAST HLSLPVYTCD
YIKWICTAKM PYFQASEILP KSWRIQLPNY YVSILEGSIS PFNGQLYNKI ALTCGMIHFK
EFFNSEISCQ GLLLKLVMQC ALPPEFYFYT KQVIEFEETD IRNLTLWERT DERHTGRVSN
HAELRVLSYF MLTINWMLSF DRDRQYPLKW ILSLTESLTQ RTTTSESIGR NIVKVVYPDK
PTSSDYFQWS EEETLEFLKW MEKQFLPTQT KSLHNENGSM EMTIDQKIAR RKLYKIFPLD
REANHDGEFN DSTHQLTFIE DLQERYAKQT PFFESNKIRD SLNYQEANPP ARKEAIGRLL
THIASQLLVD FAISKEQLKD CISRIKNACL HRMN
