RPAB5_YEAST
ID RPAB5_YEAST Reviewed; 70 AA.
AC P22139; D6W2R6;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=DNA-directed RNA polymerases I, II, and III subunit RPABC5;
DE Short=RNA polymerases I, II, and III subunit ABC5;
DE AltName: Full=ABC10-beta;
DE AltName: Full=ABC8;
DE AltName: Full=DNA-directed RNA polymerases I, II, and III 8.3 kDa polypeptide;
GN Name=RPB10; OrderedLocusNames=YOR210W;
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 PROTEIN SEQUENCE OF 1-27.
RX PubMed=2211663; DOI=10.1016/s0021-9258(18)38236-x;
RA Woychik N.A., Young R.A.;
RT "RNA polymerase II subunit RPB10 is essential for yeast cell viability.";
RL J. Biol. Chem. 265:17816-17819(1990).
RN [2]
RP ERRATUM OF PUBMED:2211663, AND SEQUENCE REVISION.
RX PubMed=8505344; DOI=10.1016/s0021-9258(19)50331-3;
RA Woychik N.A., Young R.A.;
RL J. Biol. Chem. 268:12230-12230(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX PubMed=8516295; DOI=10.1073/pnas.90.12.5524;
RA Lalo D., Carles C., Sentenac A., Thuriaux P.;
RT "Interactions between three common subunits of yeast RNA polymerases I and
RT III.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5524-5528(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [5]
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 [6]
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 [7]
RP REVIEW ON THE RNA POL III COMPLEX.
RX PubMed=10384303; DOI=10.1101/sqb.1998.63.381;
RA Chedin S., Ferri M.L., Peyroche G., Andrau J.-C., Jourdain S., Lefebvre O.,
RA Werner M., Carles C., Sentenac A.;
RT "The yeast RNA polymerase III transcription machinery: a paradigm for
RT eukaryotic gene activation.";
RL Cold Spring Harb. Symp. Quant. Biol. 63:381-389(1998).
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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-59, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [11]
RP ELECTRON MICROSCOPY OF THE RNA POL II/TFIIF COMPLEX.
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 [12]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE RNA POL II CORE COMPLEX.
RX PubMed=11313498; DOI=10.1126/science.1059493;
RA Cramer P., Bushnell D.A., Kornberg R.D.;
RT "Structural basis of transcription: RNA polymerase II at 2.8 A
RT resolution.";
RL Science 292:1863-1876(2001).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF THE RNA POL II CORE COMPLEX.
RX PubMed=11313499; DOI=10.1126/science.1059495;
RA Gnatt A.L., Cramer P., Fu J., Bushnell D.A., Kornberg R.D.;
RT "Structural basis of transcription: an RNA polymerase II elongation complex
RT at 3.3 A resolution.";
RL Science 292:1876-1882(2001).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE RNA POL II CORE COMPLEX IN
RP COMPLEX WITH ALPHA-AMANITIN.
RX PubMed=11805306; DOI=10.1073/pnas.251664698;
RA Bushnell D.A., Cramer P., Kornberg R.D.;
RT "Structural basis of transcription: alpha-amanitin-RNA polymerase II
RT cocrystal at 2.8 A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:1218-1222(2002).
RN [15]
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 [16]
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 [17]
RP X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS) OF THE RNA POL II CORE COMPLEX.
RX PubMed=12746498; DOI=10.1073/pnas.1130601100;
RA Bushnell D.A., Kornberg R.D.;
RT "Complete, 12-subunit RNA polymerase II at 4.1-A resolution: implications
RT for the initiation of transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:6969-6973(2003).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF THE RNA POL II CORE COMPLEX IN
RP COMPLEX WITH ZINC.
RX PubMed=15537538; DOI=10.1016/j.cell.2004.10.016;
RA Westover K.D., Bushnell D.A., Kornberg R.D.;
RT "Structural basis of transcription: nucleotide selection by rotation in the
RT RNA polymerase II active center.";
RL Cell 119:481-489(2004).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (4.5 ANGSTROMS).
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 [20]
RP X-RAY CRYSTALLOGRAPHY (4.5 ANGSTROMS) OF THE RNA POL II CORE COMPLEX.
RX PubMed=14963322; DOI=10.1126/science.1090838;
RA Bushnell D.A., Westover K.D., Davis R.E., Kornberg R.D.;
RT "Structural basis of transcription: an RNA polymerase II-TFIIB cocrystal at
RT 4.5 Angstroms.";
RL Science 303:983-988(2004).
RN [21]
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 [22]
RP 3D-STRUCTURE MODELING OF THE POL III CORE COMPLEX.
RX PubMed=16818233; DOI=10.1016/j.molcel.2006.05.013;
RA Jasiak A.J., Armache K.J., Martens B., Jansen R.P., Cramer P.;
RT "Structural biology of RNA polymerase III: subcomplex C17/25 X-ray
RT structure and 11 subunit enzyme model.";
RL Mol. Cell 23:71-81(2006).
RN [23]
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 [24]
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).
RN [25]
RP STRUCTURE BY ELECTRON MICROSCOPY (12.00 ANGSTROMS) OF THE POL I COMPLEX,
RP FUNCTION, AND SUBUNIT.
RX PubMed=18160037; DOI=10.1016/j.cell.2007.10.051;
RA Kuhn C.D., Geiger S.R., Baumli S., Gartmann M., Gerber J., Jennebach S.,
RA Mielke T., Tschochner H., Beckmann R., Cramer P.;
RT "Functional architecture of RNA polymerase I.";
RL Cell 131:1260-1272(2007).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION, AND
RP SUBUNIT.
RX PubMed=24153184; DOI=10.1038/nature12636;
RA Fernandez-Tornero C., Moreno-Morcillo M., Rashid U.J., Taylor N.M.,
RA Ruiz F.M., Gruene T., Legrand P., Steuerwald U., Muller C.W.;
RT "Crystal structure of the 14-subunit RNA polymerase I.";
RL Nature 502:644-649(2013).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION,
RP ZINC-BINDING, AND SUBUNIT.
RX PubMed=24153182; DOI=10.1038/nature12712;
RA Engel C., Sainsbury S., Cheung A.C., Kostrewa D., Cramer P.;
RT "RNA polymerase I structure and transcription regulation.";
RL Nature 502:650-655(2013).
CC -!- FUNCTION: DNA-dependent RNA polymerases catalyze the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Common component of RNA polymerases I, II and III which synthesize
CC ribosomal RNA precursors, mRNA precursors and many functional non-
CC coding RNAs, and a small RNAs, such as 5S rRNA and tRNAs, respectively.
CC Pol II is the central component of the basal RNA polymerase II
CC transcription machinery. Pols are composed of mobile elements that move
CC relative to each other. In Pol II, RBP10 is part of the core element
CC with the central large cleft. {ECO:0000269|PubMed:18160037,
CC ECO:0000269|PubMed:24153182, ECO:0000269|PubMed:24153184}.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I), RNA polymerase II
CC (Pol II) and RNA polymerase III (Pol III) complexes. Component of the
CC RNA polymerase I (Pol I) complex consisting of 14 subunits: RPA135,
CC RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8, RPA12, RPB10, RPC19,
CC RPC10, RPA49 and RPA34. The complex is composed of a horseshoe-shaped
CC core containing ten subunits (RPA135, RPA190, RPB5, RPO26, RPB8, RPB10,
CC RPC10, RPA12, RPC19 and RPC40) where RPA135 and RPA190 form the DNA-
CC binding cleft. Outside of the core, RPA14 and RPA43 form the stalk that
CC mediates interactions with transcription initiation factors and newly
CC synthesized RNA. Component of the RNA polymerase II (Pol II) complex
CC consisting of 12 subunits: RPO21, RPB2, RPB3, RPB4, RPB5, RPO26, RPB7,
CC RPB8, RPB9, RPB10 and RPC10. Component of the RNA polymerase III (Pol
CC III) complex consisting of 17 subunits. {ECO:0000269|PubMed:11805306,
CC ECO:0000269|PubMed:12914699, ECO:0000269|PubMed:16341226,
CC ECO:0000269|PubMed:18160037, ECO:0000269|PubMed:24153182,
CC ECO:0000269|PubMed:24153184}.
CC -!- INTERACTION:
CC P22139; P08518: RPB2; NbExp=2; IntAct=EBI-15802, EBI-15767;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 5300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo10/eukaryotic RPB10 RNA
CC polymerase subunit family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M60479; AAA34995.1; ALT_SEQ; Genomic_DNA.
DR EMBL; S62098; AAB27020.1; -; Genomic_DNA.
DR EMBL; L11274; AAB59318.1; -; Genomic_DNA.
DR EMBL; Z75118; CAA99425.1; -; Genomic_DNA.
DR EMBL; AY558433; AAS56759.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10982.1; -; Genomic_DNA.
DR PIR; S48885; S48885.
DR RefSeq; NP_014853.3; NM_001183629.3.
DR PDB; 1I3Q; X-ray; 3.10 A; J=1-70.
DR PDB; 1I50; X-ray; 2.80 A; J=1-70.
DR PDB; 1I6H; X-ray; 3.30 A; J=1-70.
DR PDB; 1K83; X-ray; 2.80 A; J=1-70.
DR PDB; 1NIK; X-ray; 4.10 A; J=1-70.
DR PDB; 1NT9; X-ray; 4.20 A; J=1-70.
DR PDB; 1PQV; X-ray; 3.80 A; J=1-70.
DR PDB; 1R5U; X-ray; 4.50 A; J=1-70.
DR PDB; 1R9S; X-ray; 4.25 A; J=1-70.
DR PDB; 1R9T; X-ray; 3.50 A; J=1-70.
DR PDB; 1SFO; X-ray; 3.61 A; J=1-70.
DR PDB; 1TWA; X-ray; 3.20 A; J=1-70.
DR PDB; 1TWC; X-ray; 3.00 A; J=1-70.
DR PDB; 1TWF; X-ray; 2.30 A; J=1-70.
DR PDB; 1TWG; X-ray; 3.30 A; J=1-70.
DR PDB; 1TWH; X-ray; 3.40 A; J=1-70.
DR PDB; 1WCM; X-ray; 3.80 A; J=1-70.
DR PDB; 1Y1V; X-ray; 3.80 A; J=1-70.
DR PDB; 1Y1W; X-ray; 4.00 A; J=1-70.
DR PDB; 1Y1Y; X-ray; 4.00 A; J=1-70.
DR PDB; 1Y77; X-ray; 4.50 A; J=1-70.
DR PDB; 2B63; X-ray; 3.80 A; J=1-70.
DR PDB; 2B8K; X-ray; 4.15 A; J=1-70.
DR PDB; 2E2H; X-ray; 3.95 A; J=1-70.
DR PDB; 2E2I; X-ray; 3.41 A; J=1-70.
DR PDB; 2E2J; X-ray; 3.50 A; J=1-70.
DR PDB; 2JA5; X-ray; 3.80 A; J=1-70.
DR PDB; 2JA6; X-ray; 4.00 A; J=1-70.
DR PDB; 2JA7; X-ray; 3.80 A; J/V=1-70.
DR PDB; 2JA8; X-ray; 3.80 A; J=1-70.
DR PDB; 2NVQ; X-ray; 2.90 A; J=1-70.
DR PDB; 2NVT; X-ray; 3.36 A; J=1-70.
DR PDB; 2NVX; X-ray; 3.60 A; J=1-70.
DR PDB; 2NVY; X-ray; 3.40 A; J=1-70.
DR PDB; 2NVZ; X-ray; 4.30 A; J=1-70.
DR PDB; 2R7Z; X-ray; 3.80 A; J=1-70.
DR PDB; 2R92; X-ray; 3.80 A; J=1-70.
DR PDB; 2R93; X-ray; 4.00 A; J=1-70.
DR PDB; 2VUM; X-ray; 3.40 A; J=1-70.
DR PDB; 2YU9; X-ray; 3.40 A; J=1-70.
DR PDB; 3CQZ; X-ray; 2.80 A; J=1-70.
DR PDB; 3FKI; X-ray; 3.88 A; J=1-70.
DR PDB; 3GTG; X-ray; 3.78 A; J=1-70.
DR PDB; 3GTJ; X-ray; 3.42 A; J=1-70.
DR PDB; 3GTK; X-ray; 3.80 A; J=1-70.
DR PDB; 3GTL; X-ray; 3.38 A; J=1-70.
DR PDB; 3GTM; X-ray; 3.80 A; J=1-70.
DR PDB; 3GTO; X-ray; 4.00 A; J=1-70.
DR PDB; 3GTP; X-ray; 3.90 A; J=1-70.
DR PDB; 3GTQ; X-ray; 3.80 A; J=1-70.
DR PDB; 3H3V; X-ray; 4.00 A; K=1-70.
DR PDB; 3HOU; X-ray; 3.20 A; J/V=1-70.
DR PDB; 3HOV; X-ray; 3.50 A; J=1-70.
DR PDB; 3HOW; X-ray; 3.60 A; J=1-70.
DR PDB; 3HOX; X-ray; 3.65 A; J=1-70.
DR PDB; 3HOY; X-ray; 3.40 A; J=1-70.
DR PDB; 3HOZ; X-ray; 3.65 A; J=1-70.
DR PDB; 3I4M; X-ray; 3.70 A; J=1-70.
DR PDB; 3I4N; X-ray; 3.90 A; J=1-70.
DR PDB; 3J0K; EM; 36.00 A; J=1-70.
DR PDB; 3J1N; EM; 16.00 A; J=1-70.
DR PDB; 3K1F; X-ray; 4.30 A; J=1-70.
DR PDB; 3K7A; X-ray; 3.80 A; J=1-70.
DR PDB; 3M3Y; X-ray; 3.18 A; J=1-70.
DR PDB; 3M4O; X-ray; 3.57 A; J=1-70.
DR PDB; 3PO2; X-ray; 3.30 A; J=1-70.
DR PDB; 3PO3; X-ray; 3.30 A; J=1-70.
DR PDB; 3QT1; X-ray; 4.30 A; J=1-70.
DR PDB; 3RZD; X-ray; 3.30 A; J=1-70.
DR PDB; 3RZO; X-ray; 3.00 A; J=1-70.
DR PDB; 3S14; X-ray; 2.85 A; J=1-70.
DR PDB; 3S15; X-ray; 3.30 A; J=1-70.
DR PDB; 3S16; X-ray; 3.24 A; J=1-70.
DR PDB; 3S17; X-ray; 3.20 A; J=1-70.
DR PDB; 3S1M; X-ray; 3.13 A; J=1-70.
DR PDB; 3S1N; X-ray; 3.10 A; J=1-70.
DR PDB; 3S1Q; X-ray; 3.30 A; J=1-70.
DR PDB; 3S1R; X-ray; 3.20 A; J=1-70.
DR PDB; 3S2D; X-ray; 3.20 A; J=1-70.
DR PDB; 3S2H; X-ray; 3.30 A; J=1-70.
DR PDB; 4A3B; X-ray; 3.50 A; J=1-70.
DR PDB; 4A3C; X-ray; 3.50 A; J=1-70.
DR PDB; 4A3D; X-ray; 3.40 A; J=1-70.
DR PDB; 4A3E; X-ray; 3.40 A; J=1-70.
DR PDB; 4A3F; X-ray; 3.50 A; J=1-70.
DR PDB; 4A3G; X-ray; 3.50 A; J=1-70.
DR PDB; 4A3I; X-ray; 3.80 A; J=1-70.
DR PDB; 4A3J; X-ray; 3.70 A; J=1-70.
DR PDB; 4A3K; X-ray; 3.50 A; J=1-70.
DR PDB; 4A3L; X-ray; 3.50 A; J=1-70.
DR PDB; 4A3M; X-ray; 3.90 A; J=1-70.
DR PDB; 4A93; X-ray; 3.40 A; J=1-70.
DR PDB; 4BBR; X-ray; 3.40 A; J=1-70.
DR PDB; 4BBS; X-ray; 3.60 A; J=1-70.
DR PDB; 4BXX; X-ray; 3.28 A; J=1-70.
DR PDB; 4BXZ; X-ray; 4.80 A; J=1-70.
DR PDB; 4BY1; X-ray; 3.60 A; J=1-70.
DR PDB; 4BY7; X-ray; 3.15 A; J=1-70.
DR PDB; 4C2M; X-ray; 2.80 A; J/Y=1-70.
DR PDB; 4C3H; X-ray; 3.27 A; J=1-70.
DR PDB; 4C3I; X-ray; 3.00 A; J=1-70.
DR PDB; 4C3J; X-ray; 3.35 A; J=1-70.
DR PDB; 4V1M; EM; 6.60 A; J=1-70.
DR PDB; 4V1N; EM; 7.80 A; J=1-70.
DR PDB; 4V1O; EM; 9.70 A; J=1-70.
DR PDB; 4X67; X-ray; 4.10 A; J=1-70.
DR PDB; 4X6A; X-ray; 3.96 A; J=1-70.
DR PDB; 4Y52; X-ray; 3.50 A; J=1-70.
DR PDB; 4Y7N; X-ray; 3.30 A; J=1-70.
DR PDB; 4YM7; X-ray; 5.50 A; AJ/BJ/CJ/DJ/EJ/FJ=1-70.
DR PDB; 5C3E; X-ray; 3.70 A; J=1-70.
DR PDB; 5C44; X-ray; 3.95 A; J=1-70.
DR PDB; 5C4A; X-ray; 4.20 A; J=1-70.
DR PDB; 5C4J; X-ray; 4.00 A; J=1-70.
DR PDB; 5C4X; X-ray; 4.00 A; J=1-70.
DR PDB; 5FJ8; EM; 3.90 A; J=1-70.
DR PDB; 5FJ9; EM; 4.60 A; J=1-70.
DR PDB; 5FJA; EM; 4.65 A; J=1-70.
DR PDB; 5FMF; EM; 6.00 A; J=1-65.
DR PDB; 5FYW; EM; 4.35 A; J=1-70.
DR PDB; 5FZ5; EM; 8.80 A; J=1-70.
DR PDB; 5G5L; EM; 4.80 A; J=1-70.
DR PDB; 5IP7; X-ray; 3.52 A; J=1-65.
DR PDB; 5IP9; X-ray; 3.90 A; J=1-65.
DR PDB; 5LMX; EM; 4.90 A; J=1-70.
DR PDB; 5M3F; EM; 3.80 A; J=1-70.
DR PDB; 5M3M; EM; 4.00 A; J=1-70.
DR PDB; 5M5W; EM; 3.80 A; J=1-70.
DR PDB; 5M5X; EM; 4.00 A; J=1-70.
DR PDB; 5M5Y; EM; 4.00 A; J=1-70.
DR PDB; 5M64; EM; 4.60 A; J=1-70.
DR PDB; 5N5Y; EM; 7.70 A; J=1-70.
DR PDB; 5N5Z; EM; 7.70 A; J=1-70.
DR PDB; 5N60; EM; 7.70 A; J=1-70.
DR PDB; 5N61; EM; 3.40 A; J=1-70.
DR PDB; 5OA1; EM; 4.40 A; J=1-70.
DR PDB; 5OQJ; EM; 4.70 A; J=1-70.
DR PDB; 5OQM; EM; 5.80 A; J=1-70.
DR PDB; 5OT2; X-ray; 3.20 A; J=1-70.
DR PDB; 5SVA; EM; 15.30 A; J=1-70.
DR PDB; 5U5Q; X-ray; 3.80 A; J=1-70.
DR PDB; 5VVR; EM; 5.80 A; J=1-70.
DR PDB; 5VVS; EM; 6.40 A; J=1-70.
DR PDB; 5W4U; X-ray; 3.60 A; J=1-70.
DR PDB; 5W51; X-ray; 3.40 A; J=1-70.
DR PDB; 5W5Y; EM; 3.80 A; J=1-70.
DR PDB; 5W64; EM; 4.20 A; J=1-70.
DR PDB; 5W65; EM; 4.30 A; J=1-70.
DR PDB; 5W66; EM; 3.90 A; J=1-70.
DR PDB; 6BLO; X-ray; 3.40 A; J=1-70.
DR PDB; 6BLP; X-ray; 3.20 A; J=1-70.
DR PDB; 6BM2; X-ray; 3.40 A; J=1-70.
DR PDB; 6BM4; X-ray; 2.95 A; J=1-70.
DR PDB; 6BQF; X-ray; 3.35 A; J=1-70.
DR PDB; 6CNB; EM; 4.10 A; J=1-70.
DR PDB; 6CNC; EM; 4.10 A; J=1-70.
DR PDB; 6CND; EM; 4.80 A; J=1-70.
DR PDB; 6CNF; EM; 4.50 A; J=1-70.
DR PDB; 6EU0; EM; 4.00 A; J=1-70.
DR PDB; 6EU1; EM; 3.40 A; J=1-70.
DR PDB; 6EU2; EM; 3.40 A; J=1-70.
DR PDB; 6EU3; EM; 3.30 A; J=1-70.
DR PDB; 6F40; EM; 3.70 A; J=1-70.
DR PDB; 6F41; EM; 4.30 A; J=1-70.
DR PDB; 6F42; EM; 5.50 A; J=1-70.
DR PDB; 6F44; EM; 4.20 A; J=1-70.
DR PDB; 6GYK; EM; 5.10 A; J=1-70.
DR PDB; 6GYL; EM; 4.80 A; J=1-70.
DR PDB; 6GYM; EM; 6.70 A; J=1-70.
DR PDB; 6H67; EM; 3.60 A; J=1-70.
DR PDB; 6H68; EM; 4.60 A; J=1-70.
DR PDB; 6HKO; EM; 3.42 A; J=1-70.
DR PDB; 6HLQ; EM; 3.18 A; J=1-70.
DR PDB; 6HLR; EM; 3.18 A; J=1-70.
DR PDB; 6HLS; EM; 3.21 A; J=1-70.
DR PDB; 6I84; EM; 4.40 A; J=1-70.
DR PDB; 6O6C; EM; 3.10 A; H=1-70.
DR PDB; 6RQH; EM; 3.70 A; J=1-70.
DR PDB; 6RQL; EM; 2.90 A; J=1-70.
DR PDB; 6RQT; EM; 4.00 A; J=1-70.
DR PDB; 6RRD; EM; 3.10 A; J=1-70.
DR PDB; 6RUI; EM; 2.70 A; J=1-70.
DR PDB; 6RUO; EM; 3.50 A; J=1-70.
DR PDB; 6RWE; EM; 3.00 A; J=1-70.
DR PDB; 6TPS; EM; 3.54 A; J=1-70.
DR PDB; 6TUT; EM; 3.25 A; J=1-70.
DR PDB; 6UPX; X-ray; 3.40 A; J=1-70.
DR PDB; 6UPY; X-ray; 3.40 A; J=1-70.
DR PDB; 6UPZ; X-ray; 3.10 A; J=1-70.
DR PDB; 6UQ0; X-ray; 3.56 A; J=1-70.
DR PDB; 6UQ1; X-ray; 3.60 A; J=1-70.
DR PDB; 6UQ2; X-ray; 3.20 A; J=1-70.
DR PDB; 6UQ3; X-ray; 3.47 A; J=1-70.
DR PDB; 7KED; X-ray; 3.60 A; J=1-70.
DR PDB; 7KEE; X-ray; 3.45 A; J=1-70.
DR PDB; 7KEF; X-ray; 3.89 A; J=1-70.
DR PDB; 7NKX; EM; 2.90 A; J=1-70.
DR PDB; 7NKY; EM; 3.20 A; J=1-70.
DR PDB; 7O4I; EM; 3.20 A; J=1-70.
DR PDB; 7O4J; EM; 2.90 A; J=1-70.
DR PDB; 7O72; EM; 3.40 A; J=1-70.
DR PDB; 7O73; EM; 3.40 A; J=1-70.
DR PDB; 7O75; EM; 3.20 A; J=1-70.
DR PDB; 7RIM; X-ray; 2.90 A; J=1-70.
DR PDB; 7RIP; X-ray; 3.30 A; J=1-70.
DR PDB; 7RIQ; X-ray; 3.00 A; J=1-70.
DR PDB; 7RIW; X-ray; 3.20 A; J=1-70.
DR PDB; 7RIX; X-ray; 3.40 A; J=1-70.
DR PDB; 7RIY; X-ray; 3.70 A; J=1-70.
DR PDBsum; 1I3Q; -.
DR PDBsum; 1I50; -.
DR PDBsum; 1I6H; -.
DR PDBsum; 1K83; -.
DR PDBsum; 1NIK; -.
DR PDBsum; 1NT9; -.
DR PDBsum; 1PQV; -.
DR PDBsum; 1R5U; -.
DR PDBsum; 1R9S; -.
DR PDBsum; 1R9T; -.
DR PDBsum; 1SFO; -.
DR PDBsum; 1TWA; -.
DR PDBsum; 1TWC; -.
DR PDBsum; 1TWF; -.
DR PDBsum; 1TWG; -.
DR PDBsum; 1TWH; -.
DR PDBsum; 1WCM; -.
DR PDBsum; 1Y1V; -.
DR PDBsum; 1Y1W; -.
DR PDBsum; 1Y1Y; -.
DR PDBsum; 1Y77; -.
DR PDBsum; 2B63; -.
DR PDBsum; 2B8K; -.
DR PDBsum; 2E2H; -.
DR PDBsum; 2E2I; -.
DR PDBsum; 2E2J; -.
DR PDBsum; 2JA5; -.
DR PDBsum; 2JA6; -.
DR PDBsum; 2JA7; -.
DR PDBsum; 2JA8; -.
DR PDBsum; 2NVQ; -.
DR PDBsum; 2NVT; -.
DR PDBsum; 2NVX; -.
DR PDBsum; 2NVY; -.
DR PDBsum; 2NVZ; -.
DR PDBsum; 2R7Z; -.
DR PDBsum; 2R92; -.
DR PDBsum; 2R93; -.
DR PDBsum; 2VUM; -.
DR PDBsum; 2YU9; -.
DR PDBsum; 3CQZ; -.
DR PDBsum; 3FKI; -.
DR PDBsum; 3GTG; -.
DR PDBsum; 3GTJ; -.
DR PDBsum; 3GTK; -.
DR PDBsum; 3GTL; -.
DR PDBsum; 3GTM; -.
DR PDBsum; 3GTO; -.
DR PDBsum; 3GTP; -.
DR PDBsum; 3GTQ; -.
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; 3K7A; -.
DR PDBsum; 3M3Y; -.
DR PDBsum; 3M4O; -.
DR PDBsum; 3PO2; -.
DR PDBsum; 3PO3; -.
DR PDBsum; 3QT1; -.
DR PDBsum; 3RZD; -.
DR PDBsum; 3RZO; -.
DR PDBsum; 3S14; -.
DR PDBsum; 3S15; -.
DR PDBsum; 3S16; -.
DR PDBsum; 3S17; -.
DR PDBsum; 3S1M; -.
DR PDBsum; 3S1N; -.
DR PDBsum; 3S1Q; -.
DR PDBsum; 3S1R; -.
DR PDBsum; 3S2D; -.
DR PDBsum; 3S2H; -.
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; 4C2M; -.
DR PDBsum; 4C3H; -.
DR PDBsum; 4C3I; -.
DR PDBsum; 4C3J; -.
DR PDBsum; 4V1M; -.
DR PDBsum; 4V1N; -.
DR PDBsum; 4V1O; -.
DR PDBsum; 4X67; -.
DR PDBsum; 4X6A; -.
DR PDBsum; 4Y52; -.
DR PDBsum; 4Y7N; -.
DR PDBsum; 4YM7; -.
DR PDBsum; 5C3E; -.
DR PDBsum; 5C44; -.
DR PDBsum; 5C4A; -.
DR PDBsum; 5C4J; -.
DR PDBsum; 5C4X; -.
DR PDBsum; 5FJ8; -.
DR PDBsum; 5FJ9; -.
DR PDBsum; 5FJA; -.
DR PDBsum; 5FMF; -.
DR PDBsum; 5FYW; -.
DR PDBsum; 5FZ5; -.
DR PDBsum; 5G5L; -.
DR PDBsum; 5IP7; -.
DR PDBsum; 5IP9; -.
DR PDBsum; 5LMX; -.
DR PDBsum; 5M3F; -.
DR PDBsum; 5M3M; -.
DR PDBsum; 5M5W; -.
DR PDBsum; 5M5X; -.
DR PDBsum; 5M5Y; -.
DR PDBsum; 5M64; -.
DR PDBsum; 5N5Y; -.
DR PDBsum; 5N5Z; -.
DR PDBsum; 5N60; -.
DR PDBsum; 5N61; -.
DR PDBsum; 5OA1; -.
DR PDBsum; 5OQJ; -.
DR PDBsum; 5OQM; -.
DR PDBsum; 5OT2; -.
DR PDBsum; 5SVA; -.
DR PDBsum; 5U5Q; -.
DR PDBsum; 5VVR; -.
DR PDBsum; 5VVS; -.
DR PDBsum; 5W4U; -.
DR PDBsum; 5W51; -.
DR PDBsum; 5W5Y; -.
DR PDBsum; 5W64; -.
DR PDBsum; 5W65; -.
DR PDBsum; 5W66; -.
DR PDBsum; 6BLO; -.
DR PDBsum; 6BLP; -.
DR PDBsum; 6BM2; -.
DR PDBsum; 6BM4; -.
DR PDBsum; 6BQF; -.
DR PDBsum; 6CNB; -.
DR PDBsum; 6CNC; -.
DR PDBsum; 6CND; -.
DR PDBsum; 6CNF; -.
DR PDBsum; 6EU0; -.
DR PDBsum; 6EU1; -.
DR PDBsum; 6EU2; -.
DR PDBsum; 6EU3; -.
DR PDBsum; 6F40; -.
DR PDBsum; 6F41; -.
DR PDBsum; 6F42; -.
DR PDBsum; 6F44; -.
DR PDBsum; 6GYK; -.
DR PDBsum; 6GYL; -.
DR PDBsum; 6GYM; -.
DR PDBsum; 6H67; -.
DR PDBsum; 6H68; -.
DR PDBsum; 6HKO; -.
DR PDBsum; 6HLQ; -.
DR PDBsum; 6HLR; -.
DR PDBsum; 6HLS; -.
DR PDBsum; 6I84; -.
DR PDBsum; 6O6C; -.
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 PDBsum; 6TUT; -.
DR PDBsum; 6UPX; -.
DR PDBsum; 6UPY; -.
DR PDBsum; 6UPZ; -.
DR PDBsum; 6UQ0; -.
DR PDBsum; 6UQ1; -.
DR PDBsum; 6UQ2; -.
DR PDBsum; 6UQ3; -.
DR PDBsum; 7KED; -.
DR PDBsum; 7KEE; -.
DR PDBsum; 7KEF; -.
DR PDBsum; 7NKX; -.
DR PDBsum; 7NKY; -.
DR PDBsum; 7O4I; -.
DR PDBsum; 7O4J; -.
DR PDBsum; 7O72; -.
DR PDBsum; 7O73; -.
DR PDBsum; 7O75; -.
DR PDBsum; 7RIM; -.
DR PDBsum; 7RIP; -.
DR PDBsum; 7RIQ; -.
DR PDBsum; 7RIW; -.
DR PDBsum; 7RIX; -.
DR PDBsum; 7RIY; -.
DR AlphaFoldDB; P22139; -.
DR SMR; P22139; -.
DR BioGRID; 34605; 449.
DR ComplexPortal; CPX-1664; DNA-directed RNA Polymerase I complex.
DR ComplexPortal; CPX-2660; DNA-directed RNA polymerase III complex.
DR ComplexPortal; CPX-2662; DNA-directed RNA polymerase II complex.
DR DIP; DIP-825N; -.
DR IntAct; P22139; 27.
DR MINT; P22139; -.
DR STRING; 4932.YOR210W; -.
DR iPTMnet; P22139; -.
DR MaxQB; P22139; -.
DR PaxDb; P22139; -.
DR PRIDE; P22139; -.
DR EnsemblFungi; YOR210W_mRNA; YOR210W; YOR210W.
DR GeneID; 854385; -.
DR KEGG; sce:YOR210W; -.
DR SGD; S000005736; RPB10.
DR VEuPathDB; FungiDB:YOR210W; -.
DR eggNOG; KOG3497; Eukaryota.
DR GeneTree; ENSGT00390000007087; -.
DR HOGENOM; CLU_143122_2_1_1; -.
DR InParanoid; P22139; -.
DR OMA; YCCRRMF; -.
DR BioCyc; YEAST:G3O-33712-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-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-SCE-73772; RNA Polymerase I Promoter Escape.
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-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-SCE-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
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; P22139; -.
DR PRO; PR:P22139; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P22139; protein.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0005736; C:RNA polymerase I complex; IDA:UniProtKB.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IDA:SGD.
DR GO; GO:0005666; C:RNA polymerase III complex; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0001054; F:RNA polymerase I activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:SGD.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IDA:ComplexPortal.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; IDA:ComplexPortal.
DR GO; GO:0006386; P:termination of RNA polymerase III transcription; IDA:ComplexPortal.
DR GO; GO:0006360; P:transcription by RNA polymerase I; IDA:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IDA:ComplexPortal.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; IDA:ComplexPortal.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; IDA:ComplexPortal.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0006384; P:transcription initiation from RNA polymerase III promoter; IDA:ComplexPortal.
DR GO; GO:0001172; P:transcription, RNA-templated; IEA:GOC.
DR GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IDA:SGD.
DR HAMAP; MF_00250; RNApol_arch_Rpo10; 1.
DR InterPro; IPR023580; RNA_pol_su_RPB10.
DR InterPro; IPR020789; RNA_pol_suN_Zn-BS.
DR InterPro; IPR000268; RPABC5/Rpb10.
DR PANTHER; PTHR23431; PTHR23431; 1.
DR Pfam; PF01194; RNA_pol_N; 1.
DR PIRSF; PIRSF005653; RNA_pol_N/8_sub; 1.
DR SUPFAM; SSF46924; SSF46924; 1.
DR PROSITE; PS01112; RNA_POL_N_8KD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-directed RNA polymerase;
KW Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Ribosome biogenesis; Transcription; Ubl conjugation; Zinc.
FT CHAIN 1..70
FT /note="DNA-directed RNA polymerases I, II, and III subunit
FT RPABC5"
FT /id="PRO_0000121342"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15537538,
FT ECO:0007744|PDB:1TWF"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15537538,
FT ECO:0007744|PDB:1TWF"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15537538,
FT ECO:0007744|PDB:1TWF"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15537538,
FT ECO:0007744|PDB:1TWF"
FT CROSSLNK 59
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:1TWF"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:1I6H"
FT HELIX 32..38
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 44..51
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:6RUO"
SQ SEQUENCE 70 AA; 8278 MW; E1F5733E8F466BE0 CRC64;
MIVPVRCFSC GKVVGDKWES YLNLLQEDEL DEGTALSRLG LKRYCCRRMI LTHVDLIEKF
LRYNPLEKRD
