RPA1_YEAST
ID RPA1_YEAST Reviewed; 1664 AA.
AC P10964; D6W336; Q99330;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=DNA-directed RNA polymerase I subunit RPA190;
DE EC=2.7.7.6;
DE AltName: Full=DNA-directed RNA polymerase I 190 kDa polypeptide;
DE Short=A190;
DE AltName: Full=DNA-directed RNA polymerase I largest subunit;
GN Name=RPA190; Synonyms=RPA1, RRN1; OrderedLocusNames=YOR341W;
GN ORFNames=O6276;
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=2830265; DOI=10.1016/s0021-9258(18)69144-6;
RA Memet S., Gouy M., Marck C., Sentenac A., Buhler J.-M.;
RT "RPA190, the gene coding for the largest subunit of yeast RNA polymerase
RT A.";
RL J. Biol. Chem. 263:2830-2839(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 90843 / S288c / FY73;
RX PubMed=8948102;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1475::aid-yea32>3.0.co;2-v;
RA Purnelle B., Goffeau A.;
RT "Nucleotide sequence analysis of a 40 kb segment on the right arm of yeast
RT chromosome XV reveals 18 open reading frames including a new pyruvate
RT kinase and three homologues to chromosome I genes.";
RL Yeast 12:1475-1481(1996).
RN [3]
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 [4]
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 [5]
RP IDENTIFICATION IN THE RNA POL I COMPLEX.
RX PubMed=11717393; DOI=10.1073/pnas.231181398;
RA Fath S., Milkereit P., Peyroche G., Riva M., Carles C., Tschochner H.;
RT "Differential roles of phosphorylation in the formation of transcriptional
RT active RNA polymerase I.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:14334-14339(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1636, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-889, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [9]
RP ELECTRON MICROSCOPY OF THE RNA POLYMERASE I COMPLEX.
RX PubMed=12145213; DOI=10.1093/emboj/cdf392;
RA Bischler N., Brino L., Carles C., Riva M., Tschochner H., Mallouh V.,
RA Schultz P.;
RT "Localization of the yeast RNA polymerase I-specific subunits.";
RL EMBO J. 21:4136-4144(2002).
RN [10]
RP IDENTIFICATION IN THE RNA POL I COMPLEX.
RX PubMed=11918799; DOI=10.1046/j.1365-2958.2002.02824.x;
RA Van Mullem V., Landrieux E., Vandenhaute J., Thuriaux P.;
RT "Rpa12p, a conserved RNA polymerase I subunit with two functional
RT domains.";
RL Mol. Microbiol. 43:1105-1113(2002).
RN [11]
RP IDENTIFICATION IN THE RNA POL I COMPLEX.
RX PubMed=12407181; DOI=10.1073/pnas.232580799;
RA Peyroche G., Levillain E., Siaut M., Callebaut I., Schultz P., Sentenac A.,
RA Riva M., Carles C.;
RT "The A14-A43 heterodimer subunit in yeast RNA pol I and their relationship
RT to Rpb4-Rpb7 pol II subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14670-14675(2002).
RN [12]
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 [13]
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 [14]
RP STRUCTURE BY ELECTRON MICROSCOPY (12.00 ANGSTROMS) OF THE POL I COMPLEX,
RP FUNCTION, CATALYTIC ACTIVITY, 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 [15]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION,
RP CATALYTIC ACTIVITY, ZINC-BINDING, AND 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 [16]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION,
RP CATALYTIC ACTIVITY, 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 Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA
CC precursors. Besides, RNA polymerase I has intrinsic RNA cleavage
CC activity. RPA190 and RPA135 both contribute to the polymerase catalytic
CC activity and together form the Pol I active center. In addition,
CC subunit RPA12 contributes a catalytic zinc ribbon that is required for
CC RNA cleavage by Pol I. A single stranded DNA template strand of the
CC promoter is positioned within the central active site cleft of Pol I. A
CC bridging helix emanates from RPA190 and crosses the cleft near the
CC catalytic site and is thought to promote translocation of Pol I by
CC acting as a ratchet that moves the RNA-DNA hybrid through the active
CC site by switching from straight to bent conformations at each step of
CC nucleotide addition. {ECO:0000269|PubMed:18160037,
CC ECO:0000269|PubMed:24153182, ECO:0000269|PubMed:24153184}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6; Evidence={ECO:0000269|PubMed:18160037,
CC ECO:0000269|PubMed:24153182, ECO:0000269|PubMed:24153184};
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8,
CC RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34. The complex is composed of
CC a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5,
CC RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and
CC RPA190 form the DNA-binding cleft. Outside of the core, RPA14 and RPA43
CC form the stalk that mediates interactions with transcription initiation
CC factors and newly synthesized RNA. {ECO:0000269|PubMed:11717393,
CC ECO:0000269|PubMed:11918799, ECO:0000269|PubMed:12407181,
CC ECO:0000269|PubMed:18160037, ECO:0000269|PubMed:24153182,
CC ECO:0000269|PubMed:24153184}.
CC -!- INTERACTION:
CC P10964; P53131: PRP43; NbExp=2; IntAct=EBI-15730, EBI-505;
CC P10964; P22138: RPA135; NbExp=4; IntAct=EBI-15730, EBI-15736;
CC P10964; P07703: RPC40; NbExp=4; IntAct=EBI-15730, EBI-15831;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2840 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {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; J03530; AAA34890.1; -; Genomic_DNA.
DR EMBL; X95720; CAA65029.1; -; Genomic_DNA.
DR EMBL; Z75249; CAA99665.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11102.1; -; Genomic_DNA.
DR PIR; S67250; S67250.
DR RefSeq; NP_014986.3; NM_001183761.3.
DR PDB; 4C2M; X-ray; 2.80 A; A/P=1-1664.
DR PDB; 4C3H; X-ray; 3.27 A; A=1-1664.
DR PDB; 4C3I; X-ray; 3.00 A; A=1-1664.
DR PDB; 4C3J; X-ray; 3.35 A; A=1-1664.
DR PDB; 4YM7; X-ray; 5.50 A; AA/BA/CA/DA/EA/FA=1-1664.
DR PDB; 5G5L; EM; 4.80 A; A=1-1664.
DR PDB; 5LMX; EM; 4.90 A; A=1-1664.
DR PDB; 5M3F; EM; 3.80 A; A=1-1664.
DR PDB; 5M3M; EM; 4.00 A; A=1-1664.
DR PDB; 5M5W; EM; 3.80 A; A=1-1664.
DR PDB; 5M5X; EM; 4.00 A; A=1-1664.
DR PDB; 5M5Y; EM; 4.00 A; A=1-1664.
DR PDB; 5M64; EM; 4.60 A; A=1-1664.
DR PDB; 5N5Y; EM; 7.70 A; A=1-1664.
DR PDB; 5N5Z; EM; 7.70 A; A=1-1664.
DR PDB; 5N60; EM; 7.70 A; A=1-1664.
DR PDB; 5N61; EM; 3.40 A; A=1-1664.
DR PDB; 5OA1; EM; 4.40 A; A=1-1664.
DR PDB; 5W5Y; EM; 3.80 A; A=1-1664.
DR PDB; 5W64; EM; 4.20 A; A=1-1664.
DR PDB; 5W65; EM; 4.30 A; A=1-1664.
DR PDB; 5W66; EM; 3.90 A; A=1-1664.
DR PDB; 6H67; EM; 3.60 A; A=1-1664.
DR PDB; 6H68; EM; 4.60 A; A=1-1664.
DR PDB; 6HKO; EM; 3.42 A; A=1-1664.
DR PDB; 6HLQ; EM; 3.18 A; A=1-1664.
DR PDB; 6HLR; EM; 3.18 A; A=1-1664.
DR PDB; 6HLS; EM; 3.21 A; A=1-1664.
DR PDB; 6RQH; EM; 3.70 A; A=1-1664.
DR PDB; 6RQL; EM; 2.90 A; A=1-1664.
DR PDB; 6RQT; EM; 4.00 A; A=1-1664.
DR PDB; 6RRD; EM; 3.10 A; A=1-1664.
DR PDB; 6RUI; EM; 2.70 A; A=1-1664.
DR PDB; 6RUO; EM; 3.50 A; A=1-1664.
DR PDB; 6RWE; EM; 3.00 A; A=1-1664.
DR PDB; 6TPS; EM; 3.54 A; A=1-1664.
DR PDBsum; 4C2M; -.
DR PDBsum; 4C3H; -.
DR PDBsum; 4C3I; -.
DR PDBsum; 4C3J; -.
DR PDBsum; 4YM7; -.
DR PDBsum; 5G5L; -.
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; 5W5Y; -.
DR PDBsum; 5W64; -.
DR PDBsum; 5W65; -.
DR PDBsum; 5W66; -.
DR PDBsum; 6H67; -.
DR PDBsum; 6H68; -.
DR PDBsum; 6HKO; -.
DR PDBsum; 6HLQ; -.
DR PDBsum; 6HLR; -.
DR PDBsum; 6HLS; -.
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; P10964; -.
DR SMR; P10964; -.
DR BioGRID; 34724; 487.
DR ComplexPortal; CPX-1664; DNA-directed RNA Polymerase I complex.
DR DIP; DIP-999N; -.
DR IntAct; P10964; 45.
DR MINT; P10964; -.
DR STRING; 4932.YOR341W; -.
DR iPTMnet; P10964; -.
DR MaxQB; P10964; -.
DR PaxDb; P10964; -.
DR PRIDE; P10964; -.
DR TopDownProteomics; P10964; -.
DR EnsemblFungi; YOR341W_mRNA; YOR341W; YOR341W.
DR GeneID; 854519; -.
DR KEGG; sce:YOR341W; -.
DR SGD; S000005868; RPA190.
DR VEuPathDB; FungiDB:YOR341W; -.
DR eggNOG; KOG0262; Eukaryota.
DR GeneTree; ENSGT00920000149138; -.
DR HOGENOM; CLU_000487_2_4_1; -.
DR InParanoid; P10964; -.
DR OMA; RFFNRED; -.
DR BioCyc; YEAST:G3O-33816-MON; -.
DR Reactome; R-SCE-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-SCE-73772; RNA Polymerase I Promoter Escape.
DR PRO; PR:P10964; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P10964; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0005736; C:RNA polymerase I complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:SGD.
DR GO; GO:0001054; F:RNA polymerase I activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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:0006360; P:transcription by RNA polymerase I; IDA:UniProtKB.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; IDA:ComplexPortal.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; IDA:ComplexPortal.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
DR InterPro; IPR015699; DNA-dir_RNA_pol1_lsu.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR PANTHER; PTHR19376:SF11; PTHR19376:SF11; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR SMART; SM00663; RPOLA_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; Transcription; Transferase; Zinc.
FT CHAIN 1..1664
FT /note="DNA-directed RNA polymerase I subunit RPA190"
FT /id="PRO_0000073930"
FT REGION 280..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1004
FT /note="Bridging helix"
FT /evidence="ECO:0000250"
FT REGION 1343..1423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1361..1385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1408..1423
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24153182,
FT ECO:0007744|PDB:4C2M"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24153182,
FT ECO:0007744|PDB:4C2M"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24153182,
FT ECO:0007744|PDB:4C2M"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24153182,
FT ECO:0007744|PDB:4C2M"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24153182,
FT ECO:0007744|PDB:4C2M"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24153182,
FT ECO:0007744|PDB:4C2M"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24153182,
FT ECO:0007744|PDB:4C2M"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24153182,
FT ECO:0007744|PDB:4C2M"
FT BINDING 627
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 629
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 631
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT MOD_RES 889
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1636
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 158
FT /note="N -> T (in Ref. 1; AAA34890)"
FT /evidence="ECO:0000305"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:6RWE"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:6HLQ"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:4C2M"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 77..86
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:6HLQ"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 114..124
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 125..128
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:4C2M"
FT HELIX 175..198
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:4C3I"
FT HELIX 210..223
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 224..228
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 258..261
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 266..269
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:6RQL"
FT HELIX 319..330
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 332..338
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 355..362
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:4C2M"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:4C2M"
FT HELIX 381..405
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:4C2M"
FT HELIX 418..438
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:6RRD"
FT HELIX 455..458
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 461..464
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 467..470
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 473..486
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 488..490
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 494..497
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 499..502
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 506..510
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 516..525
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 526..528
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 533..537
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 551..558
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 559..562
FT /evidence="ECO:0007829|PDB:4C2M"
FT HELIX 568..570
FT /evidence="ECO:0007829|PDB:4C2M"
FT STRAND 576..580
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 586..593
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 597..599
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 600..607
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 613..616
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 618..620
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 621..625
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 628..630
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 632..636
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 641..649
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 653..656
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 660..662
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 674..680
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 682..684
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 686..688
FT /evidence="ECO:0007829|PDB:4C2M"
FT HELIX 689..699
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 702..705
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 708..711
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 721..723
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 725..728
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 729..739
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 742..744
FT /evidence="ECO:0007829|PDB:6RQL"
FT STRAND 748..752
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 757..760
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 761..763
FT /evidence="ECO:0007829|PDB:6RUO"
FT STRAND 768..772
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 775..778
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 783..786
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 793..800
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 803..823
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 831..833
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 839..847
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 848..850
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 853..861
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 873..883
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 886..911
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 912..915
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 916..918
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 920..922
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 924..931
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 932..934
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 937..944
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 953..955
FT /evidence="ECO:0007829|PDB:6RQL"
FT STRAND 961..963
FT /evidence="ECO:0007829|PDB:6HKO"
FT HELIX 977..979
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 986..988
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 992..1009
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1010..1012
FT /evidence="ECO:0007829|PDB:6RQL"
FT STRAND 1013..1016
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1017..1026
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1027..1029
FT /evidence="ECO:0007829|PDB:6HLQ"
FT STRAND 1036..1039
FT /evidence="ECO:0007829|PDB:4C3I"
FT STRAND 1041..1043
FT /evidence="ECO:0007829|PDB:6HKO"
FT STRAND 1045..1049
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1050..1052
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1057..1059
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1061..1064
FT /evidence="ECO:0007829|PDB:6RQL"
FT HELIX 1066..1071
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1073..1079
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1083..1085
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1088..1090
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1093..1107
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 1108..1110
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1113..1115
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1123..1126
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 1129..1131
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1138..1149
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1152..1155
FT /evidence="ECO:0007829|PDB:4C2M"
FT STRAND 1157..1160
FT /evidence="ECO:0007829|PDB:4C2M"
FT HELIX 1164..1175
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1185..1194
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 1195..1197
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1218..1225
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 1226..1228
FT /evidence="ECO:0007829|PDB:4C3I"
FT STRAND 1237..1242
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1244..1246
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1248..1256
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1259..1262
FT /evidence="ECO:0007829|PDB:5N61"
FT HELIX 1263..1266
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1267..1275
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1289..1296
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1299..1306
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1310..1317
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 1318..1320
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1321..1337
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1344..1346
FT /evidence="ECO:0007829|PDB:4C3I"
FT STRAND 1355..1360
FT /evidence="ECO:0007829|PDB:6RQL"
FT HELIX 1364..1366
FT /evidence="ECO:0007829|PDB:4C2M"
FT HELIX 1369..1378
FT /evidence="ECO:0007829|PDB:4C2M"
FT STRAND 1382..1384
FT /evidence="ECO:0007829|PDB:4C2M"
FT HELIX 1389..1394
FT /evidence="ECO:0007829|PDB:4C2M"
FT STRAND 1403..1406
FT /evidence="ECO:0007829|PDB:6RQL"
FT HELIX 1441..1453
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1454..1456
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1460..1462
FT /evidence="ECO:0007829|PDB:6RQL"
FT TURN 1464..1466
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1469..1475
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1478..1480
FT /evidence="ECO:0007829|PDB:6HLQ"
FT HELIX 1485..1493
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1497..1499
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1506..1508
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1513..1515
FT /evidence="ECO:0007829|PDB:6RRD"
FT STRAND 1518..1523
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1526..1529
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1530..1532
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 1533..1535
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1538..1540
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1542..1544
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1546..1552
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1555..1571
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 1572..1574
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1579..1589
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 1590..1592
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1600..1603
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1609..1615
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1618..1626
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 1627..1629
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1637..1643
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1648..1650
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1653..1660
FT /evidence="ECO:0007829|PDB:6RUI"
SQ SEQUENCE 1664 AA; 186432 MW; DF65A7AA459D5E6D CRC64;
MDISKPVGSE ITSVDFGILT AKEIRNLSAK QITNPTVLDN LGHPVSGGLY DLALGAFLRN
LCSTCGLDEK FCPGHQGHIE LPVPCYNPLF FNQLYIYLRA SCLFCHHFRL KSVEVHRYAC
KLRLLQYGLI DESYKLDEIT LGSLNSSMYT DDEAIEDNED EMDGEGSKQS KDISSTLLNE
LKSKRSEYVD MAIAKALSDG RTTERGSFTA TVNDERKKLV HEFHKKLLSR GKCDNCGMFS
PKFRKDGFTK IFETALNEKQ ITNNRVKGFI RQDMIKKQKQ AKKLDGSNEA SANDEESFDV
GRNPTTRPKT GSTYILSTEV KNILDTVFRK EQCVLQYVFH SRPNLSRKLV KADSFFMDVL
VVPPTRFRLP SKLGEEVHEN SQNQLLSKVL TTSLLIRDLN DDLSKLQKDK VSLEDRRVIF
SRLMNAFVTI QNDVNAFIDS TKAQGRTSGK VPIPGVKQAL EKKEGLFRKH MMGKRVNYAA
RSVISPDPNI ETNEIGVPPV FAVKLTYPEP VTAYNIAELR QAVINGPDKW PGATQIQNED
GSLVSLIGMS VEQRKALANQ LLTPSSNVST HTLNKKVYRH IKNRDVVLMN RQPTLHKASM
MGHKVRVLPN EKTLRLHYAN TGAYNADFDG DEMNMHFPQN ENARAEALNL ANTDSQYLTP
TSGSPVRGLI QDHISAGVWL TSKDSFFTRE QYQQYIYGCI RPEDGHTTRS KIVTLPPTIF
KPYPLWTGKQ IITTVLLNVT PPDMPGINLI SKNKIKNEYW GKGSLENEVL FKDGALLCGI
LDKSQYGASK YGIVHSLHEV YGPEVAAKVL SVLGRLFTNY ITATAFTCGM DDLRLTAEGN
KWRTDILKTS VDTGREAAAE VTNLDKDTPA DDPELLKRLQ EILRDNNKSG ILDAVTSSKV
NAITSQVVSK CVPDGTMKKF PCNSMQAMAL SGAKGSNVNV SQIMCLLGQQ ALEGRRVPVM
VSGKTLPSFK PYETDAMAGG YVKGRFYSGI KPQEYYFHCM AGREGLIDTA VKTSRSGYLQ
RCLTKQLEGV HVSYDNSIRD ADGTLVQFMY GGDAIDITKE SHMTQFEFCL DNYYALLKKY
NPSALIEHLD VESALKYSKK TLKYRKKHSK EPHYKQSVKY DPVLAKYNPA KYLGSVSENF
QDKLESFLDK NSKLFKSSDG VNEKKFRALM QLKYMRSLIN PGEAVGIIAS QSVGEPSTQM
TLNTFHFAGH GAANVTLGIP RLREIVMTAS AAIKTPQMTL PIWNDVSDEQ ADTFCKSISK
VLLSEVIDKV IVTETTGTSN TAGGNAARSY VIHMRFFDNN EYSEEYDVSK EELQNVISNQ
FIHLLEAAIV KEIKKQKRTT GPDIGVAVPR LQTDVANSSS NSKRLEEDND EEQSHKKTKQ
AVSYDEPDED EIETMREAEK SSDEEGIDSD KESDSDSEDE DVDMNEQINK SIVEANNNMN
KVQRDRQSAI ISHHRFITKY NFDDESGKWC EFKLELAADT EKLLMVNIVE EICRKSIIRQ
IPHIDRCVHP EPENGKRVLV TEGVNFQAMW DQEAFIDVDG ITSNDVAAVL KTYGVEAARN
TIVNEINNVF SRYAISVSFR HLDLIADMMT RQGTYLAFNR QGMETSTSSF MKMSYETTCQ
FLTKAVLDNE REQLDSPSAR IVVGKLNNVG TGSFDVLAKV PNAA
