RPA2_YEAST
ID RPA2_YEAST Reviewed; 1203 AA.
AC P22138; D6W421;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=DNA-directed RNA polymerase I subunit RPA135;
DE EC=2.7.7.6 {ECO:0000269|PubMed:18160037, ECO:0000269|PubMed:24153182, ECO:0000269|PubMed:24153184};
DE AltName: Full=DNA-directed RNA polymerase I 135 kDa polypeptide;
DE Short=A135;
DE AltName: Full=DNA-directed RNA polymerase I polypeptide 2;
DE Short=RNA polymerase I subunit 2;
GN Name=RPA135; Synonyms=RPA2, RRN2, SRP3; OrderedLocusNames=YPR010C;
GN ORFNames=YP9531.03C;
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 971-989 AND
RP 1003-1020.
RX PubMed=1990281; DOI=10.1128/mcb.11.2.754-764.1991;
RA Yano R., Nomura M.;
RT "Suppressor analysis of temperature-sensitive mutations of the largest
RT subunit of RNA polymerase I in Saccharomyces cerevisiae: a suppressor gene
RT encodes the second-largest subunit of RNA polymerase I.";
RL Mol. Cell. Biol. 11:754-764(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81 AND SER-1156, AND
RP IDENTIFICATION BY 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
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 [9]
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 [10]
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 [11]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-1104; CYS-1107; CYS-1128 AND
RP CYS-1131.
RX PubMed=14555487; DOI=10.1128/ec.2.5.1046-1052.2003;
RA Naryshkina T., Bruning A., Gadal O., Severinov K.;
RT "Role of second-largest RNA polymerase I subunit Zn-binding domain in
RT enzyme assembly.";
RL Eukaryot. Cell 2:1046-1052(2003).
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 IN COMPLEX WITH
RP ZINC IONS, FUNCTION, 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249;
CC Evidence={ECO:0000305|PubMed:18160037, ECO:0000305|PubMed:24153182,
CC ECO:0000305|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 P22138; P10964: RPA190; NbExp=4; IntAct=EBI-15736, EBI-15730;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14555487,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Three distinct zinc-containing RNA polymerases are found
CC in eukaryotic nuclei: polymerase I for the ribosomal RNA precursor,
CC polymerase II for the mRNA precursor, and polymerase III for 5S and
CC tRNA genes.
CC -!- MISCELLANEOUS: Present with 14100 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000305}.
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DR EMBL; U31900; AAA97589.1; -; Genomic_DNA.
DR EMBL; M62804; AAA34993.1; -; Genomic_DNA.
DR EMBL; Z49919; CAA90154.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA95050.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11437.1; -; Genomic_DNA.
DR PIR; A39607; A39607.
DR RefSeq; NP_015335.1; NM_001184107.1.
DR PDB; 4C2M; X-ray; 2.80 A; B/Q=1-1203.
DR PDB; 4C3H; X-ray; 3.27 A; B=1-1203.
DR PDB; 4C3I; X-ray; 3.00 A; B=1-1203.
DR PDB; 4C3J; X-ray; 3.35 A; B=1-1203.
DR PDB; 4YM7; X-ray; 5.50 A; AB/BB/CB/DB/EB/FB=1-1203.
DR PDB; 5G5L; EM; 4.80 A; B=1-1203.
DR PDB; 5LMX; EM; 4.90 A; B=1-1203.
DR PDB; 5M3F; EM; 3.80 A; B=1-1203.
DR PDB; 5M3M; EM; 4.00 A; B=1-1203.
DR PDB; 5M5W; EM; 3.80 A; B=1-1203.
DR PDB; 5M5X; EM; 4.00 A; B=1-1203.
DR PDB; 5M5Y; EM; 4.00 A; B=1-1203.
DR PDB; 5M64; EM; 4.60 A; B=1-1203.
DR PDB; 5N5Y; EM; 7.70 A; B=1-1203.
DR PDB; 5N5Z; EM; 7.70 A; B=1-1203.
DR PDB; 5N60; EM; 7.70 A; B=1-1203.
DR PDB; 5N61; EM; 3.40 A; B=1-1203.
DR PDB; 5OA1; EM; 4.40 A; B=1-1203.
DR PDB; 5W5Y; EM; 3.80 A; B=1-1203.
DR PDB; 5W64; EM; 4.20 A; B=1-1203.
DR PDB; 5W65; EM; 4.30 A; B=1-1203.
DR PDB; 5W66; EM; 3.90 A; B=1-1203.
DR PDB; 6H67; EM; 3.60 A; B=1-1203.
DR PDB; 6H68; EM; 4.60 A; B=1-1203.
DR PDB; 6HKO; EM; 3.42 A; B=1-1203.
DR PDB; 6HLQ; EM; 3.18 A; B=1-1203.
DR PDB; 6HLR; EM; 3.18 A; B=1-1203.
DR PDB; 6HLS; EM; 3.21 A; B=1-1203.
DR PDB; 6RQH; EM; 3.70 A; B=1-1203.
DR PDB; 6RQL; EM; 2.90 A; B=1-1203.
DR PDB; 6RQT; EM; 4.00 A; B=1-1203.
DR PDB; 6RRD; EM; 3.10 A; B=1-1203.
DR PDB; 6RUI; EM; 2.70 A; B=1-1203.
DR PDB; 6RUO; EM; 3.50 A; B=1-1203.
DR PDB; 6RWE; EM; 3.00 A; B=1-1203.
DR PDB; 6TPS; EM; 3.54 A; B=1-1203.
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; P22138; -.
DR SMR; P22138; -.
DR BioGRID; 36188; 186.
DR ComplexPortal; CPX-1664; DNA-directed RNA Polymerase I complex.
DR DIP; DIP-135N; -.
DR IntAct; P22138; 60.
DR MINT; P22138; -.
DR STRING; 4932.YPR010C; -.
DR iPTMnet; P22138; -.
DR MaxQB; P22138; -.
DR PaxDb; P22138; -.
DR PRIDE; P22138; -.
DR EnsemblFungi; YPR010C_mRNA; YPR010C; YPR010C.
DR GeneID; 856119; -.
DR KEGG; sce:YPR010C; -.
DR SGD; S000006214; RPA135.
DR VEuPathDB; FungiDB:YPR010C; -.
DR eggNOG; KOG0216; Eukaryota.
DR GeneTree; ENSGT00950000183132; -.
DR HOGENOM; CLU_000524_5_1_1; -.
DR InParanoid; P22138; -.
DR OMA; FFGVVHY; -.
DR BioCyc; YEAST:G3O-34172-MON; -.
DR Reactome; R-SCE-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-SCE-73772; RNA Polymerase I Promoter Escape.
DR PRO; PR:P22138; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P22138; protein.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0001054; F:RNA polymerase I activity; IDA:UniProtKB.
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 CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR InterPro; IPR009674; Rpa2_dom_4.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF06883; RNA_pol_Rpa2_4; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing;
KW DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW Nucleus; Phosphoprotein; Reference proteome; Ribosome biogenesis;
KW Transcription; Transferase; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1203
FT /note="DNA-directed RNA polymerase I subunit RPA135"
FT /id="PRO_0000048080"
FT ZN_FING 1104..1131
FT /note="C4-type"
FT /evidence="ECO:0000305|PubMed:14555487"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 1104
FT /note="C->A: No effect; when associated with A-1107; A-1128
FT and A-1131."
FT /evidence="ECO:0000269|PubMed:14555487"
FT MUTAGEN 1107
FT /note="C->A: Lethal. Abolishes recruitment of RPA1 to Pol
FT I. No effect; when associated with A-1104; A-1128 and A-
FT 1131."
FT /evidence="ECO:0000269|PubMed:14555487"
FT MUTAGEN 1127
FT /note="C->R: Responsible of suppression of RPA190-5 and
FT RPA190-1 mutations."
FT MUTAGEN 1128
FT /note="C->A: No effect; when associated with A-1104; A-1107
FT and A-1131."
FT /evidence="ECO:0000269|PubMed:14555487"
FT MUTAGEN 1131
FT /note="C->A: No effect; when associated with A-1104; A-1107
FT and A-1128."
FT /evidence="ECO:0000269|PubMed:14555487"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:6HLQ"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:6RQL"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 60..64
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:6RWE"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 94..104
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:4C3I"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:4C3I"
FT HELIX 123..129
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 134..145
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 146..149
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:6RWE"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 177..182
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:5N61"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 229..239
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:6RUO"
FT STRAND 245..253
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 258..266
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 273..280
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 285..292
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:6RQL"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:5N61"
FT HELIX 300..316
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 323..333
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 334..339
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:4C3I"
FT HELIX 346..356
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 357..361
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:5N61"
FT HELIX 367..385
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:4C3I"
FT STRAND 396..403
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 405..432
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 433..435
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 443..450
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 457..467
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:6RRD"
FT STRAND 485..487
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 493..497
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 498..500
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 501..504
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 507..509
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 515..518
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 522..524
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 525..527
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 537..541
FT /evidence="ECO:0007829|PDB:4C2M"
FT STRAND 542..545
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 558..560
FT /evidence="ECO:0007829|PDB:4C3I"
FT HELIX 561..567
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 573..575
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 583..588
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 591..596
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 598..613
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 614..616
FT /evidence="ECO:0007829|PDB:6RWE"
FT STRAND 618..620
FT /evidence="ECO:0007829|PDB:4C3I"
FT STRAND 625..629
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 633..636
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 639..643
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 645..647
FT /evidence="ECO:0007829|PDB:5N61"
FT STRAND 649..655
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 656..659
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 660..664
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 666..668
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 669..671
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 674..677
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 678..680
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 683..685
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 687..689
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 693..696
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 702..704
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 707..709
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 712..721
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 722..724
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 733..735
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 739..746
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 751..753
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 756..759
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 762..764
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 768..775
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 779..781
FT /evidence="ECO:0007829|PDB:4C2M"
FT STRAND 784..790
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 791..795
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 796..799
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 801..814
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 817..819
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 823..826
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 829..831
FT /evidence="ECO:0007829|PDB:6RQL"
FT HELIX 836..838
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 844..846
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 856..863
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 864..867
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 868..873
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 876..878
FT /evidence="ECO:0007829|PDB:6RWE"
FT STRAND 880..888
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 891..893
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 894..896
FT /evidence="ECO:0007829|PDB:6RUO"
FT STRAND 900..909
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 916..919
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 920..922
FT /evidence="ECO:0007829|PDB:6HLQ"
FT STRAND 924..931
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 933..935
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 938..941
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 946..949
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 951..953
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 955..957
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 961..975
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 978..980
FT /evidence="ECO:0007829|PDB:6RQL"
FT STRAND 985..987
FT /evidence="ECO:0007829|PDB:6RQL"
FT STRAND 988..990
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 992..1003
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1009..1011
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 1016..1018
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1026..1037
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1041..1043
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1045..1049
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 1054..1056
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 1063..1066
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1069..1071
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1073..1081
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1085..1092
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 1093..1096
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1098..1104
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 1105..1108
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1109..1112
FT /evidence="ECO:0007829|PDB:6HLQ"
FT STRAND 1113..1115
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1120..1122
FT /evidence="ECO:0007829|PDB:4C3I"
FT STRAND 1126..1129
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1133..1136
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1155..1160
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1162..1164
FT /evidence="ECO:0007829|PDB:6HLQ"
FT STRAND 1166..1168
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1173..1179
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 1181..1190
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 1191..1193
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1194..1198
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 1199..1201
FT /evidence="ECO:0007829|PDB:6HLS"
SQ SEQUENCE 1203 AA; 135742 MW; 72FA95B66F98C5F8 CRC64;
MSKVIKPPGQ ARTADFRTLE RESRFINPPK DKSAFPLLQE AVQPHIGSFN ALTEGPDGGL
LNLGVKDIGE KVIFDGKPLN SEDEISNSGY LGNKLSVSVE QVSIAKPMSN DGVSSAVERK
VYPSESRQRL TSYRGKLLLK LKWSVNNGEE NLFEVRDCGG LPVMLQSNRC HLNKMSPYEL
VQHKEESDEI GGYFIVNGIE KLIRMLIVQR RNHPMAIIRP SFANRGASYS HYGIQIRSVR
PDQTSQTNVL HYLNDGQVTF RFSWRKNEYL VPVVMILKAL CHTSDREIFD GIIGNDVKDS
FLTDRLELLL RGFKKRYPHL QNRTQVLQYL GDKFRVVFQA SPDQSDLEVG QEVLDRIVLV
HLGKDGSQDK FRMLLFMIRK LYSLVAGECS PDNPDATQHQ EVLLGGFLYG MILKEKIDEY
LQNIIAQVRM DINRGMAINF KDKRYMSRVL MRVNENIGSK MQYFLSTGNL VSQSGLDLQQ
VSGYTVVAEK INFYRFISHF RMVHRGSFFA QLKTTTVRKL LPESWGFLCP VHTPDGSPCG
LLNHFAHKCR ISTQQSDVSR IPSILYSLGV APASHTFAAG PSLCCVQIDG KIIGWVSHEQ
GKIIADTLRY WKVEGKTPGL PIDLEIGYVP PSTRGQYPGL YLFGGHSRML RPVRYLPLDK
EDIVGPFEQV YMNIAVTPQE IQNNVHTHVE FTPTNILSIL ANLTPFSDFN QSPRNMYQCQ
MGKQTMGTPG VALCHRSDNK LYRLQTGQTP IVKANLYDDY GMDNFPNGFN AVVAVISYTG
YDMDDAMIIN KSADERGFGY GTMYKTEKVD LALNRNRGDP ITQHFGFGND EWPKEWLEKL
DEDGLPYIGT YVEEGDPICA YFDDTLNKTK IKTYHSSEPA YIEEVNLIGD ESNKFQELQT
VSIKYRIRRT PQIGDKFSSR HGQKGVCSRK WPTIDMPFSE TGIQPDIIIN PHAFPSRMTI
GMFVESLAGK AGALHGIAQD STPWIFNEDD TPADYFGEQL AKAGYNYHGN EPMYSGATGE
ELRADIYVGV VYYQRLRHMV NDKFQVRSTG PVNSLTMQPV KGRKRHGGIR VGEMERDALI
GHGTSFLLQD RLLNSSDYTQ ASVCRECGSI LTTQQSVPRI GSISTVCCRR CSMRFEDAKK
LLTKSEDGEK IFIDDSQIWE DGQGNKFVGG NETTTVAIPF VLKYLDSELS AMGIRLRYNV
EPK
