RRN6_YEAST
ID RRN6_YEAST Reviewed; 894 AA.
AC P32786; D6VPY6;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=RNA polymerase I-specific transcription initiation factor RRN6;
GN Name=RRN6; OrderedLocusNames=YBL014C; ORFNames=YBL0311, YBL0312;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1332308; DOI=10.1002/yea.320080911;
RA Skala J., van Dyck L., Purnelle B., Goffeau A.;
RT "The sequence of an 8 kb segment on the left arm of chromosome II from
RT Saccharomyces cerevisiae identifies five new open reading frames of unknown
RT functions, two tRNA genes and two transposable elements.";
RL Yeast 8:777-785(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 39.
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 [5]
RP INTERACTION WITH RRN6.
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 RRN7 AND RRN11.
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).
CC -!- FUNCTION: Acts as component of the core factor (CF) complex which is
CC essential for the initiation of rDNA transcription by RNA polymerase I.
CC After binding of UAF (upstream activation factor) to an upstream
CC element of the promoter, CF is recruited in a SPT15/TBP-dependent
CC manner to form a preinitiation complex. {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. RRN6 interacts with RRN7, RRN11 and RRN9.
CC {ECO:0000269|PubMed:7958901, ECO:0000269|PubMed:8702872,
CC ECO:0000269|PubMed:8895657}.
CC -!- INTERACTION:
CC P32786; Q04712: RRN11; NbExp=2; IntAct=EBI-15986, EBI-27790;
CC P32786; P40992: RRN7; NbExp=4; IntAct=EBI-15986, EBI-15990;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 237 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; L33863; AAA53130.1; -; Genomic_DNA.
DR EMBL; Z35775; CAA84833.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07106.2; -; Genomic_DNA.
DR PIR; S25332; S25332.
DR RefSeq; NP_009539.2; NM_001178254.2.
DR PDB; 5N5Y; EM; 7.70 A; P=1-894.
DR PDB; 5N5Z; EM; 7.70 A; P=1-894.
DR PDB; 5N60; EM; 7.70 A; P=1-894.
DR PDB; 5N61; EM; 3.40 A; P=1-894.
DR PDB; 5O7X; X-ray; 3.20 A; A/D/G/J/M/P=1-894.
DR PDB; 5OA1; EM; 4.40 A; V=1-894.
DR PDB; 5W5Y; EM; 3.80 A; O=1-894.
DR PDB; 5W64; EM; 4.20 A; O=1-894.
DR PDB; 5W65; EM; 4.30 A; O=1-894.
DR PDB; 5W66; EM; 3.90 A; O=1-894.
DR PDB; 6RQH; EM; 3.70 A; S=1-894.
DR PDB; 6RQL; EM; 2.90 A; S=1-894.
DR PDB; 6RRD; EM; 3.10 A; S=1-894.
DR PDB; 6RUI; EM; 2.70 A; S=1-894.
DR PDB; 6RUO; EM; 3.50 A; S=1-894.
DR PDB; 6RWE; EM; 3.00 A; S=1-894.
DR PDB; 6TPS; EM; 3.54 A; P=169-779.
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; P32786; -.
DR SMR; P32786; -.
DR BioGRID; 32686; 24.
DR ComplexPortal; CPX-1836; RNA polymerase I core factor complex.
DR DIP; DIP-1595N; -.
DR IntAct; P32786; 4.
DR MINT; P32786; -.
DR STRING; 4932.YBL014C; -.
DR MaxQB; P32786; -.
DR PaxDb; P32786; -.
DR PRIDE; P32786; -.
DR EnsemblFungi; YBL014C_mRNA; YBL014C; YBL014C.
DR GeneID; 852269; -.
DR KEGG; sce:YBL014C; -.
DR SGD; S000000110; RRN6.
DR VEuPathDB; FungiDB:YBL014C; -.
DR eggNOG; ENOG502QRAW; Eukaryota.
DR HOGENOM; CLU_014997_0_0_1; -.
DR InParanoid; P32786; -.
DR OMA; QIPTIKS; -.
DR BioCyc; YEAST:G3O-28919-MON; -.
DR PRO; PR:P32786; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P32786; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0070860; C:RNA polymerase I core factor complex; IDA:SGD.
DR GO; GO:0001164; F:RNA polymerase I core promoter sequence-specific DNA binding; IC:SGD.
DR GO; GO:0001179; F:RNA polymerase I general transcription initiation factor binding; IDA:SGD.
DR GO; GO:0001163; F:RNA polymerase I transcription regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IDA:SGD.
DR InterPro; IPR019350; RNA_pol_I-sp_TIF_RRN6-like.
DR InterPro; IPR016531; Rrn6.
DR PANTHER; PTHR28221; PTHR28221; 2.
DR Pfam; PF10214; Rrn6; 1.
DR PIRSF; PIRSF007939; RNA_pol_I_RRN6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..894
FT /note="RNA polymerase I-specific transcription initiation
FT factor RRN6"
FT /id="PRO_0000097448"
FT REGION 803..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 39
FT /note="K -> N (in Ref. 2; no nucleotide entry and 3;
FT CAA84833)"
FT /evidence="ECO:0000305"
FT CONFLICT 663
FT /note="L -> V (in Ref. 1; AAA53130)"
FT /evidence="ECO:0000305"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:5O7X"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:6RQL"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:5O7X"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:6RWE"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:5N61"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:5N61"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:5N61"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:5O7X"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:5N61"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 260..274
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:6RQL"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:6RQL"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:6RWE"
FT STRAND 321..327
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 344..350
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 367..370
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 371..375
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 377..384
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 385..388
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 389..395
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:5O7X"
FT STRAND 402..406
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 409..412
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 415..420
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 422..425
FT /evidence="ECO:0007829|PDB:5O7X"
FT STRAND 429..433
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:6RWE"
FT STRAND 449..457
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 462..474
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 476..483
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 485..487
FT /evidence="ECO:0007829|PDB:5O7X"
FT STRAND 490..495
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 501..505
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 534..538
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 547..553
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 572..575
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 576..579
FT /evidence="ECO:0007829|PDB:6RWE"
FT HELIX 583..585
FT /evidence="ECO:0007829|PDB:5O7X"
FT HELIX 586..611
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 613..615
FT /evidence="ECO:0007829|PDB:5N61"
FT HELIX 617..638
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 639..644
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 645..647
FT /evidence="ECO:0007829|PDB:5O7X"
FT STRAND 657..659
FT /evidence="ECO:0007829|PDB:5O7X"
FT STRAND 664..668
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 672..684
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 688..690
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 697..699
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 700..702
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 703..705
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 712..719
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 723..725
FT /evidence="ECO:0007829|PDB:6RQL"
FT STRAND 726..728
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 731..743
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 753..765
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 768..772
FT /evidence="ECO:0007829|PDB:6RQL"
SQ SEQUENCE 894 AA; 102049 MW; BF42EFD2AED77F15 CRC64;
MSEGQIPSSD VLGSQLGVGV QGASLYCPQE NYTTKKQEKP QWLRPVDDTL AEDALDLHIV
VKSLLCDTAI RYISDDKVLQ ESDADDDLIT SDIDEDTDNQ GDTSIVVNPV IPVVPKDVHF
FKKVDVGNDS MFGVNCDTPV SFQDYIPSDL LRNLDDTLQE STNSSRPMQD AFFWDPTVAN
RLDSQYIQTA SDLRNYRDGT EIIAYASGKT GSVLNIAVLT RQNTLHLNRH NNVTSIELHS
PIKSIKIPGA SESIGRRSNL VGIITENSFQ IFRIESVHSR SCDVMVSSSE PLYFVEIDDL
QVVDFAFNPW DLQQFAIIDI KGNWSIGRIP KNFNNNNKRK LQLIDNLHGT IFDPEELSSW
KRIEWFSHFQ KILVFDRSKM IEIDFMNNWQ TEVVQAKAWS NIRDYKRIDD KNGILLTSRE
IIIVGASESN DPVRRISWKH DLDPDDTTLR ITVQKVKKPD HILLVAFVYS MRHKRIYMHV
FSHRKANLFQ SLGCSTVLEI PGGTPTGIET ILTLDHIDDE SRREEDADEN FELVVDFLVK
LRNSSEVYYY ALSNTQNSEP NKQETPIIVD HPEWASLFNN ADEREKESIG ALVSQIKLKE
RERISRVQNL IEHENSHDED KYLQDLGYRL SIATNELLES WQKTKDESIL SGSLSHSKLK
NLLENSDSFA SIPEFSSLLD QFFQYYQDQD VTFIGFEKLL HLFLHEDVPG LDIFYNKLLQ
CWVLVSPQAE LLTKEIVKDI IWSLARLEKP SLFEPIQNEI SRSLSGPYQD IISSWDMDDI
NEEDESNEFN FDSQFSAPFN GRPPFNLNSQ SQIPTIKSSQ SSGLARRKRI LKTQSQKATP
LSQSTQNLSV LPDSMTPAFT LMQPPSSQIS FVNDSQPRNS QKAKKKKKRI RGFG
