RPB7_YEAST
ID RPB7_YEAST Reviewed; 171 AA.
AC P34087; D6VT36;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB7;
DE Short=RNA polymerase II subunit B7;
DE AltName: Full=B16;
GN Name=RPB7; OrderedLocusNames=YDR404C; ORFNames=D9509.22;
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].
RX PubMed=8488730; DOI=10.1002/yea.320090309;
RA McKune K., Richards K.L., Edwards A.M., Young R.A., Woychik N.A.;
RT "RPB7, one of two dissociable subunits of yeast RNA polymerase II, is
RT essential for cell viability.";
RL Yeast 9:295-299(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 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 FUNCTION OF THE RPB4-RPB7 COMPLEX, RNA-BINDING, AND MUTAGENESIS OF
RP 108-VAL--HIS-113 AND 151-ILE--HIS-158.
RX PubMed=11087726; DOI=10.1074/jbc.m003165200;
RA Orlicky S.M., Tran P.T., Sayre M.H., Edwards A.M.;
RT "Dissociable Rpb4-Rpb7 subassembly of RNA polymerase II binds to single-
RT strand nucleic acid and mediates a post-recruitment step in transcription
RT initiation.";
RL J. Biol. Chem. 276:10097-10102(2001).
RN [6]
RP FUNCTION OF THE RPB4-RPB7 COMPLEX.
RX PubMed=15304220; DOI=10.1016/j.molcel.2004.06.035;
RA Kamenski T., Heilmeier S., Meinhart A., Cramer P.;
RT "Structure and mechanism of RNA polymerase II CTD phosphatases.";
RL Mol. Cell 15:399-407(2004).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=17056745; DOI=10.1128/ec.00288-06;
RA Selitrennik M., Duek L., Lotan R., Choder M.;
RT "Nucleocytoplasmic shuttling of the Rpb4p and Rpb7p subunits of
RT Saccharomyces cerevisiae RNA polymerase II by two pathways.";
RL Eukaryot. Cell 5:2092-2103(2006).
RN [8]
RP INTERACTION WITH NRD1.
RX PubMed=12907709; DOI=10.1093/nar/gkg688;
RA Mitsuzawa H., Kanda E., Ishihama A.;
RT "Rpb7 subunit of RNA polymerase II interacts with an RNA-binding protein
RT involved in processing of transcripts.";
RL Nucleic Acids Res. 31:4696-4701(2003).
RN [9]
RP ELECTRON MICROSCOPY OF THE RNA POL II/TFIIF COMPLEX, AND INTERACTION WITH
RP TFG1.
RX PubMed=14580350; DOI=10.1016/s1097-2765(03)00387-3;
RA Chung W.H., Craighead J.L., Chang W.H., Ezeokonkwo C., Bareket-Samish A.,
RA Kornberg R.D., Asturias F.J.;
RT "RNA polymerase II/TFIIF structure and conserved organization of the
RT initiation complex.";
RL Mol. Cell 12:1003-1013(2003).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PAT1.
RX PubMed=17875743; DOI=10.1083/jcb.200701165;
RA Lotan R., Goler-Baron V., Duek L., Haimovich G., Choder M.;
RT "The Rpb7p subunit of yeast RNA polymerase II plays roles in the two major
RT cytoplasmic mRNA decay mechanisms.";
RL J. Cell Biol. 178:1133-1143(2007).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF THE RNA POL II COMPLEX IN COMPLEX
RP WITH DST1.
RX PubMed=12914699; DOI=10.1016/s0092-8674(03)00598-1;
RA Kettenberger H., Armache K.J., Cramer P.;
RT "Architecture of the RNA polymerase II-TFIIS complex and implications for
RT mRNA cleavage.";
RL Cell 114:347-357(2003).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (4.2 ANGSTROMS) OF THE RNA POL II COMPLEX.
RX PubMed=12746495; DOI=10.1073/pnas.1030608100;
RA Armache K.J., Kettenberger H., Cramer P.;
RT "Architecture of initiation-competent 12-subunit RNA polymerase II.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:6964-6968(2003).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (4.5 ANGSTROMS) OF THE RNA POL II COMPLEX.
RX PubMed=15610738; DOI=10.1016/j.molcel.2004.11.040;
RA Kettenberger H., Armache K.J., Cramer P.;
RT "Complete RNA polymerase II elongation complex structure and its
RT interactions with NTP and TFIIS.";
RL Mol. Cell 16:955-965(2004).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF THE RNA POL II COMPLEX.
RX PubMed=15591044; DOI=10.1074/jbc.m413038200;
RA Armache K.J., Mitterweger S., Meinhart A., Cramer P.;
RT "Structures of complete RNA polymerase II and its subcomplex, Rpb4/7.";
RL J. Biol. Chem. 280:7131-7134(2005).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF THE RNA POL II COMPLEX IN COMPLEX
RP WITH INHIBITING NON-CODING RNA.
RX PubMed=16341226; DOI=10.1038/nsmb1032;
RA Kettenberger H., Eisenfuhr A., Brueckner F., Theis M., Famulok M.,
RA Cramer P.;
RT "Structure of an RNA polymerase II-RNA inhibitor complex elucidates
RT transcription regulation by noncoding RNAs.";
RL Nat. Struct. Mol. Biol. 13:44-48(2006).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (4.15 ANGSTROMS) OF THE RNA POL II COMPLEX.
RX PubMed=16765890; DOI=10.1016/j.str.2006.04.003;
RA Meyer P.A., Ye P., Zhang M., Suh M.H., Fu J.;
RT "Phasing RNA polymerase II using intrinsically bound Zn atoms: an updated
RT structural model.";
RL Structure 14:973-982(2006).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Component of RNA polymerase II which synthesizes mRNA precursors and
CC many functional non-coding RNAs. Pol II is the central component of the
CC basal RNA polymerase II transcription machinery. It is composed of
CC mobile elements that move relative to each other. RPB7 is part of a
CC subcomplex with RPB4 that binds to a pocket formed by RPB1, RPB2 and
CC RPB6 at the base of the clamp element. The RBP4-RPB7 subcomplex seems
CC to lock the clamp via RPB7 in the closed conformation thus preventing
CC double-stranded DNA to enter the active site cleft. The RPB4-RPB7
CC subcomplex binds single-stranded DNA and RNA. The RPB4-RPB7 subcomplex
CC recruits FCP1 to Pol II. {ECO:0000269|PubMed:11087726,
CC ECO:0000269|PubMed:15304220, ECO:0000269|PubMed:17875743}.
CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting
CC of 12 subunits. RPB4 and RPB7 form a subcomplex that protrudes from the
CC 10-subunit Pol II core complex. The RPB4-RPB7 subcomplex probably
CC associates with TFG1. Interacts with NRD1 and PAT1.
CC {ECO:0000269|PubMed:12907709, ECO:0000269|PubMed:12914699,
CC ECO:0000269|PubMed:14580350, ECO:0000269|PubMed:16341226,
CC ECO:0000269|PubMed:17875743}.
CC -!- INTERACTION:
CC P34087; P20433: RPB4; NbExp=8; IntAct=EBI-15790, EBI-15777;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, P-body. Note=Seems
CC to shuttle between nucleus and cytoplasm in a complex with RPB4.
CC -!- MISCELLANEOUS: Present with 6420 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPB7/RPC8 RNA polymerase subunit
CC family. {ECO:0000305}.
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DR EMBL; S59775; AAC60558.1; -; Genomic_DNA.
DR EMBL; U32274; AAB64844.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12246.1; -; Genomic_DNA.
DR PIR; S30140; S30140.
DR RefSeq; NP_010692.3; NM_001180712.3.
DR PDB; 1NT9; X-ray; 4.20 A; G=1-171.
DR PDB; 1PQV; X-ray; 3.80 A; G=1-171.
DR PDB; 1WCM; X-ray; 3.80 A; G=1-171.
DR PDB; 1Y14; X-ray; 2.30 A; B/D=1-171.
DR PDB; 1Y1V; X-ray; 3.80 A; G=1-171.
DR PDB; 1Y1W; X-ray; 4.00 A; G=1-171.
DR PDB; 1Y1Y; X-ray; 4.00 A; G=1-171.
DR PDB; 1Y77; X-ray; 4.50 A; G=1-171.
DR PDB; 2B63; X-ray; 3.80 A; G=1-171.
DR PDB; 2B8K; X-ray; 4.15 A; G=1-171.
DR PDB; 2JA5; X-ray; 3.80 A; G=1-171.
DR PDB; 2JA6; X-ray; 4.00 A; G=1-171.
DR PDB; 2JA7; X-ray; 3.80 A; G/S=1-171.
DR PDB; 2JA8; X-ray; 3.80 A; G=1-171.
DR PDB; 2R7Z; X-ray; 3.80 A; G=1-171.
DR PDB; 2R92; X-ray; 3.80 A; G=1-171.
DR PDB; 2R93; X-ray; 4.00 A; G=1-171.
DR PDB; 2VUM; X-ray; 3.40 A; G=1-171.
DR PDB; 3FKI; X-ray; 3.88 A; G=1-171.
DR PDB; 3H3V; X-ray; 4.00 A; H=1-171.
DR PDB; 3HOU; X-ray; 3.20 A; G/S=1-171.
DR PDB; 3HOV; X-ray; 3.50 A; G=1-171.
DR PDB; 3HOW; X-ray; 3.60 A; G=1-171.
DR PDB; 3HOX; X-ray; 3.65 A; G=1-171.
DR PDB; 3HOY; X-ray; 3.40 A; G=1-171.
DR PDB; 3HOZ; X-ray; 3.65 A; G=1-171.
DR PDB; 3I4M; X-ray; 3.70 A; G=1-171.
DR PDB; 3I4N; X-ray; 3.90 A; G=1-171.
DR PDB; 3J0K; EM; 36.00 A; G=1-171.
DR PDB; 3J1N; EM; 16.00 A; G=1-171.
DR PDB; 3K1F; X-ray; 4.30 A; G=1-171.
DR PDB; 3PO2; X-ray; 3.30 A; G=1-171.
DR PDB; 3PO3; X-ray; 3.30 A; G=1-171.
DR PDB; 3QT1; X-ray; 4.30 A; G=1-171.
DR PDB; 4A3B; X-ray; 3.50 A; G=1-171.
DR PDB; 4A3C; X-ray; 3.50 A; G=1-171.
DR PDB; 4A3D; X-ray; 3.40 A; G=1-171.
DR PDB; 4A3E; X-ray; 3.40 A; G=1-171.
DR PDB; 4A3F; X-ray; 3.50 A; G=1-171.
DR PDB; 4A3G; X-ray; 3.50 A; G=1-171.
DR PDB; 4A3I; X-ray; 3.80 A; G=1-171.
DR PDB; 4A3J; X-ray; 3.70 A; G=1-171.
DR PDB; 4A3K; X-ray; 3.50 A; G=1-171.
DR PDB; 4A3L; X-ray; 3.50 A; G=1-171.
DR PDB; 4A3M; X-ray; 3.90 A; G=1-171.
DR PDB; 4A93; X-ray; 3.40 A; G=1-171.
DR PDB; 4BBR; X-ray; 3.40 A; G=1-171.
DR PDB; 4BBS; X-ray; 3.60 A; G=1-171.
DR PDB; 4BXX; X-ray; 3.28 A; G=1-171.
DR PDB; 4BXZ; X-ray; 4.80 A; G=1-171.
DR PDB; 4BY1; X-ray; 3.60 A; G=1-171.
DR PDB; 4BY7; X-ray; 3.15 A; G=1-171.
DR PDB; 4V1N; EM; 7.80 A; G=1-171.
DR PDB; 4V1O; EM; 9.70 A; G=1-171.
DR PDB; 5C3E; X-ray; 3.70 A; G=1-171.
DR PDB; 5C44; X-ray; 3.95 A; G=1-171.
DR PDB; 5C4A; X-ray; 4.20 A; G=1-171.
DR PDB; 5C4X; X-ray; 4.00 A; G=1-171.
DR PDB; 5FMF; EM; 6.00 A; G=1-171.
DR PDB; 5FYW; EM; 4.35 A; G=1-171.
DR PDB; 5FZ5; EM; 8.80 A; G=1-171.
DR PDB; 5IP7; X-ray; 3.52 A; G=1-171.
DR PDB; 5IP9; X-ray; 3.90 A; G=1-171.
DR PDB; 5OQJ; EM; 4.70 A; G=1-171.
DR PDB; 5OQM; EM; 5.80 A; G=1-171.
DR PDB; 5OT2; X-ray; 3.20 A; G=1-171.
DR PDB; 5SVA; EM; 15.30 A; G=1-171.
DR PDB; 5U5Q; X-ray; 3.80 A; G=1-171.
DR PDB; 5VVR; EM; 5.80 A; G=1-171.
DR PDB; 5VVS; EM; 6.40 A; G=1-171.
DR PDB; 6GYK; EM; 5.10 A; G=1-171.
DR PDB; 6GYL; EM; 4.80 A; G=1-171.
DR PDB; 6GYM; EM; 6.70 A; G=1-171.
DR PDB; 6I84; EM; 4.40 A; G=1-171.
DR PDB; 7NKX; EM; 2.90 A; G=1-171.
DR PDB; 7NKY; EM; 3.20 A; G=1-171.
DR PDB; 7O4I; EM; 3.20 A; G=1-171.
DR PDB; 7O4J; EM; 2.90 A; G=1-171.
DR PDB; 7O4K; EM; 3.60 A; G=1-171.
DR PDB; 7O4L; EM; 3.40 A; G=1-171.
DR PDB; 7O72; EM; 3.40 A; G=1-171.
DR PDB; 7O73; EM; 3.40 A; G=1-171.
DR PDB; 7O75; EM; 3.20 A; G=1-171.
DR PDBsum; 1NT9; -.
DR PDBsum; 1PQV; -.
DR PDBsum; 1WCM; -.
DR PDBsum; 1Y14; -.
DR PDBsum; 1Y1V; -.
DR PDBsum; 1Y1W; -.
DR PDBsum; 1Y1Y; -.
DR PDBsum; 1Y77; -.
DR PDBsum; 2B63; -.
DR PDBsum; 2B8K; -.
DR PDBsum; 2JA5; -.
DR PDBsum; 2JA6; -.
DR PDBsum; 2JA7; -.
DR PDBsum; 2JA8; -.
DR PDBsum; 2R7Z; -.
DR PDBsum; 2R92; -.
DR PDBsum; 2R93; -.
DR PDBsum; 2VUM; -.
DR PDBsum; 3FKI; -.
DR PDBsum; 3H3V; -.
DR PDBsum; 3HOU; -.
DR PDBsum; 3HOV; -.
DR PDBsum; 3HOW; -.
DR PDBsum; 3HOX; -.
DR PDBsum; 3HOY; -.
DR PDBsum; 3HOZ; -.
DR PDBsum; 3I4M; -.
DR PDBsum; 3I4N; -.
DR PDBsum; 3J0K; -.
DR PDBsum; 3J1N; -.
DR PDBsum; 3K1F; -.
DR PDBsum; 3PO2; -.
DR PDBsum; 3PO3; -.
DR PDBsum; 3QT1; -.
DR PDBsum; 4A3B; -.
DR PDBsum; 4A3C; -.
DR PDBsum; 4A3D; -.
DR PDBsum; 4A3E; -.
DR PDBsum; 4A3F; -.
DR PDBsum; 4A3G; -.
DR PDBsum; 4A3I; -.
DR PDBsum; 4A3J; -.
DR PDBsum; 4A3K; -.
DR PDBsum; 4A3L; -.
DR PDBsum; 4A3M; -.
DR PDBsum; 4A93; -.
DR PDBsum; 4BBR; -.
DR PDBsum; 4BBS; -.
DR PDBsum; 4BXX; -.
DR PDBsum; 4BXZ; -.
DR PDBsum; 4BY1; -.
DR PDBsum; 4BY7; -.
DR PDBsum; 4V1N; -.
DR PDBsum; 4V1O; -.
DR PDBsum; 5C3E; -.
DR PDBsum; 5C44; -.
DR PDBsum; 5C4A; -.
DR PDBsum; 5C4X; -.
DR PDBsum; 5FMF; -.
DR PDBsum; 5FYW; -.
DR PDBsum; 5FZ5; -.
DR PDBsum; 5IP7; -.
DR PDBsum; 5IP9; -.
DR PDBsum; 5OQJ; -.
DR PDBsum; 5OQM; -.
DR PDBsum; 5OT2; -.
DR PDBsum; 5SVA; -.
DR PDBsum; 5U5Q; -.
DR PDBsum; 5VVR; -.
DR PDBsum; 5VVS; -.
DR PDBsum; 6GYK; -.
DR PDBsum; 6GYL; -.
DR PDBsum; 6GYM; -.
DR PDBsum; 6I84; -.
DR PDBsum; 7NKX; -.
DR PDBsum; 7NKY; -.
DR PDBsum; 7O4I; -.
DR PDBsum; 7O4J; -.
DR PDBsum; 7O4K; -.
DR PDBsum; 7O4L; -.
DR PDBsum; 7O72; -.
DR PDBsum; 7O73; -.
DR PDBsum; 7O75; -.
DR AlphaFoldDB; P34087; -.
DR SMR; P34087; -.
DR BioGRID; 32464; 363.
DR ComplexPortal; CPX-1891; RPB4-RPB7 subcomplex.
DR DIP; DIP-725N; -.
DR IntAct; P34087; 31.
DR MINT; P34087; -.
DR STRING; 4932.YDR404C; -.
DR iPTMnet; P34087; -.
DR MaxQB; P34087; -.
DR PaxDb; P34087; -.
DR PRIDE; P34087; -.
DR EnsemblFungi; YDR404C_mRNA; YDR404C; YDR404C.
DR GeneID; 852013; -.
DR KEGG; sce:YDR404C; -.
DR SGD; S000002812; RPB7.
DR VEuPathDB; FungiDB:YDR404C; -.
DR eggNOG; KOG3298; Eukaryota.
DR GeneTree; ENSGT00390000008975; -.
DR HOGENOM; CLU_085878_2_0_1; -.
DR InParanoid; P34087; -.
DR OMA; MRQPGLG; -.
DR BioCyc; YEAST:G3O-29948-MON; -.
DR Reactome; R-SCE-113418; Formation of the Early Elongation Complex.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-SCE-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SCE-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-SCE-72086; mRNA Capping.
DR Reactome; R-SCE-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-SCE-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-SCE-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-SCE-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-SCE-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR Reactome; R-SCE-9018519; Estrogen-dependent gene expression.
DR EvolutionaryTrace; P34087; -.
DR PRO; PR:P34087; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P34087; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000932; C:P-body; IDA:SGD.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IDA:SGD.
DR GO; GO:1990328; C:RPB4-RPB7 complex; IPI:ComplexPortal.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:SGD.
DR GO; GO:0031369; F:translation initiation factor binding; IPI:SGD.
DR GO; GO:0000291; P:nuclear-transcribed mRNA catabolic process, exonucleolytic; IGI:SGD.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IMP:SGD.
DR GO; GO:0045948; P:positive regulation of translational initiation; IMP:SGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IGI:SGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:SGD.
DR GO; GO:0001172; P:transcription, RNA-templated; IEA:GOC.
DR DisProt; DP01187; -.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.1490.120; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR036898; RNA_pol_Rpb7-like_N_sf.
DR InterPro; IPR045113; Rpb7-like.
DR InterPro; IPR005576; Rpb7-like_N.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR12709; PTHR12709; 1.
DR Pfam; PF00575; S1; 1.
DR Pfam; PF03876; SHS2_Rpb7-N; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF88798; SSF88798; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-directed RNA polymerase; Nucleus;
KW Reference proteome; Transcription.
FT CHAIN 1..171
FT /note="DNA-directed RNA polymerase II subunit RPB7"
FT /id="PRO_0000073993"
FT MUTAGEN 108..113
FT /note="Missing: Lowers nucleic-acid binding of RPB4-RPB7 by
FT 10-fold; no effect on association with Pol II core complex;
FT abolishes transcriptional activity of Pol II."
FT /evidence="ECO:0000269|PubMed:11087726"
FT MUTAGEN 151..158
FT /note="Missing: No effect on nucleic-acid binding of RPB4-
FT RPB7 and on association with Pol II core complex; abolishes
FT transcriptional activity of Pol II."
FT /evidence="ECO:0000269|PubMed:11087726"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:1Y14"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:3HOU"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:1Y14"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1Y14"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:1Y14"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:1Y14"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:1Y14"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:4BY7"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 71..79
FT /evidence="ECO:0007829|PDB:1Y14"
FT STRAND 86..95
FT /evidence="ECO:0007829|PDB:1Y14"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:1Y14"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:1Y14"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1Y14"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:1Y14"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:3HOU"
FT STRAND 142..153
FT /evidence="ECO:0007829|PDB:1Y14"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:1Y14"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:2VUM"
SQ SEQUENCE 171 AA; 19058 MW; 44C85603A93CDE67 CRC64;
MFFIKDLSLN ITLHPSFFGP RMKQYLKTKL LEEVEGSCTG KFGYILCVLD YDNIDIQRGR
ILPTDGSAEF NVKYRAVVFK PFKGEVVDGT VVSCSQHGFE VQVGPMKVFV TKHLMPQDLT
FNAGSNPPSY QSSEDVITIK SRIRVKIEGC ISQVSSIHAI GSIKEDYLGA I
