ID RIR1_YEAST Reviewed; 888 AA. AC P21524; D3DLX5; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 2. DT 27-MAR-2024, entry version 214. DE RecName: Full=Ribonucleoside-diphosphate reductase large chain 1; DE EC=1.17.4.1; DE AltName: Full=Ribonucleotide reductase R1 subunit 1; DE AltName: Full=Ribonucleotide reductase large subunit 1; GN Name=RNR1; Synonyms=CRT7, RIR1, SDS12; OrderedLocusNames=YER070W; 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169868; RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., RA Botstein D., Davis R.W.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V."; RL Nature 387:78-81(1997). RN [2] 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 [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100 AND 653-682, AND INDUCTION. RX PubMed=2199320; DOI=10.1101/gad.4.5.740; RA Elledge S.J., Davis R.W.; RT "Two genes differentially regulated in the cell cycle and by DNA-damaging RT agents encode alternative regulatory subunits of ribonucleotide RT reductase."; RL Genes Dev. 4:740-751(1990). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 313-384 AND 546-590. RX PubMed=8121398; DOI=10.1007/bf00281793; RA Ozier-Kalogeropoulos O., Adeline M.-T., Yang W.-L., Carman G.M., RA Lacroute F.; RT "Use of synthetic lethal mutants to clone and characterize a novel CTP RT synthetase gene in Saccharomyces cerevisiae."; RL Mol. Gen. Genet. 242:431-439(1994). RN [5] RP INTERACTION WITH SML1, AND ACTIVITY REGULATION. RX PubMed=10593972; DOI=10.1074/jbc.274.51.36679; RA Chabes A., Domkin V., Thelander L.; RT "Yeast Sml1, a protein inhibitor of ribonucleotide reductase."; RL J. Biol. Chem. 274:36679-36683(1999). RN [6] RP SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=10716984; DOI=10.1073/pnas.97.6.2474; RA Chabes A., Domkin V., Larsson G., Liu A., Graeslund A., Wijmenga S., RA Thelander L.; RT "Yeast ribonucleotide reductase has a heterodimeric iron-radical-containing RT subunit."; RL Proc. Natl. Acad. Sci. U.S.A. 97:2474-2479(2000). RN [7] RP FUNCTION, AND MUTAGENESIS OF CYS-428. RX PubMed=11893751; DOI=10.1074/jbc.m201553200; RA Domkin V., Thelander L., Chabes A.; RT "Yeast DNA damage-inducible Rnr3 has a very low catalytic activity strongly RT stimulated after the formation of a cross-talking Rnr1/Rnr3 complex."; RL J. Biol. Chem. 277:18574-18578(2002). RN [8] 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 [9] RP SUBCELLULAR LOCATION. RX PubMed=12732713; DOI=10.1073/pnas.1131932100; RA Yao R., Zhang Z., An X., Bucci B., Perlstein D.L., Stubbe J., Huang M.; RT "Subcellular localization of yeast ribonucleotide reductase regulated by RT the DNA replication and damage checkpoint pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 100:6628-6633(2003). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227; SER-837 AND SER-887, AND RP IDENTIFICATION BY 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-887, 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 [12] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-387 AND LYS-853, AND RP IDENTIFICATION BY MASS 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 [13] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEXES WITH CDP; UDP; TTP; RP GDP; GTP; ADP AND AMPPNP, AND DISULFIDE BOND. RX PubMed=16537479; DOI=10.1073/pnas.0600443103; RA Xu H., Faber C., Uchiki T., Fairman J.W., Racca J., Dealwis C.; RT "Structures of eukaryotic ribonucleotide reductase I provide insights into RT dNTP regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 103:4022-4027(2006). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEXES WITH GEMCITABINE RP DIPHOSPHATE AND R2 PEPTIDES, AND SUBUNIT. RX PubMed=16537480; DOI=10.1073/pnas.0600440103; RA Xu H., Faber C., Uchiki T., Racca J., Dealwis C.; RT "Structures of eukaryotic ribonucleotide reductase I define gemcitabine RT diphosphate binding and subunit assembly."; RL Proc. Natl. Acad. Sci. U.S.A. 103:4028-4033(2006). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) IN COMPLEX WITH PEPTIDE INHIBITORS, RP AND SUBUNIT. RX PubMed=18610997; DOI=10.1021/jm800350u; RA Xu H., Fairman J.W., Wijerathna S.R., Kreischer N.R., LaMacchia J., RA Helmbrecht E., Cooperman B.S., Dealwis C.; RT "The structural basis for peptidomimetic inhibition of eukaryotic RT ribonucleotide reductase: a conformationally flexible pharmacophore."; RL J. Med. Chem. 51:4653-4659(2008). CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis. CC Catalyzes the biosynthesis of deoxyribonucleotides from the CC corresponding ribonucleotides. {ECO:0000269|PubMed:11893751}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'- CC diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'- CC diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA- CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1; CC -!- ACTIVITY REGULATION: Under complex allosteric control mediated by CC deoxynucleoside triphosphates and ATP binding to separate specificity CC and activation sites on the R1 subunit. The type of nucleotide bound at CC the specificity site determines substrate preference. It seems probable CC that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction CC and dTTP favors GDP reduction. Stimulated by ATP and inhibited by dATP CC binding to the activity site. Inhibited by SML1. CC {ECO:0000269|PubMed:10593972}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC Vmax=2250 nmol/min/mg enzyme for cytidine 5'-diphosphate CC {ECO:0000269|PubMed:10716984}; CC Temperature dependence: CC Optimum temperature is 30 degrees Celsius. CC {ECO:0000269|PubMed:10716984}; CC -!- SUBUNIT: Heterotetramer of two large (R1) and two small (R2) subunits. CC S.cerevisiae has two different R1 subunits (RNR1 and RNR3) and two CC different R2 subunits (RNR2 and RNR4). The functional form of the small CC subunits is a RNR2-RNR4 heterodimer, where RNR2 provides the iron- CC radical center and RNR4 is required for proper folding of RNR2 and CC assembly with the large subunits. Under normal growth conditions, the CC active form of the large subunits is a homodimer of the constitutively CC expressed RNR1. In damaged cells or cells arrested for DNA synthesis, CC the reductase consists of multiple species because of the association CC of the small subunits (RNR2-RNR4) with either the RNR1 homodimer or a CC heterodimer of RNR1 and the damage-inducible RNR3. RNR1 interacts with CC the ribonucleotide reductase inhibitor SML1. CC {ECO:0000269|PubMed:10593972, ECO:0000269|PubMed:10716984, CC ECO:0000269|PubMed:16537480, ECO:0000269|PubMed:18610997}. CC -!- INTERACTION: CC P21524; P21524: RNR1; NbExp=6; IntAct=EBI-15234, EBI-15234; CC P21524; P09938: RNR2; NbExp=5; IntAct=EBI-15234, EBI-15240; CC P21524; P49723: RNR4; NbExp=5; IntAct=EBI-15234, EBI-15251; CC P21524; Q04964: SML1; NbExp=4; IntAct=EBI-15234, EBI-27834; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12732713}. CC -!- INDUCTION: Cell cycle-regulated with highest activity in S phase. CC Moderately induced by DNA-damage. {ECO:0000269|PubMed:2199320}. CC -!- MISCELLANEOUS: Two distinct regulatory sites have been defined: the CC specificity site, which controls substrate specificity, and the CC activity site which regulates overall catalytic activity. A substrate- CC binding catalytic site, located on R1, is formed only in the presence CC of the second subunit R2 (By similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: Present with 293000 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large CC chain 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; U18813; AAB64606.1; -; Genomic_DNA. DR EMBL; X69216; CAA49150.1; -; Genomic_DNA. DR EMBL; X69217; CAA49151.1; -; Genomic_DNA. DR EMBL; BK006939; DAA07729.1; -; Genomic_DNA. DR PIR; S50573; S50573. DR RefSeq; NP_010993.1; NM_001178961.1. DR PDB; 1ZYZ; X-ray; 2.90 A; A/B=1-888. DR PDB; 1ZZD; X-ray; 2.60 A; A=1-888. DR PDB; 2CVS; X-ray; 2.60 A; A=1-888. DR PDB; 2CVT; X-ray; 3.20 A; A=1-888. DR PDB; 2CVU; X-ray; 2.90 A; A=1-888. DR PDB; 2CVV; X-ray; 2.90 A; A=1-888. DR PDB; 2CVW; X-ray; 2.40 A; A=1-888. DR PDB; 2CVX; X-ray; 2.20 A; A=1-888. DR PDB; 2CVY; X-ray; 2.40 A; A=1-888. DR PDB; 2EUD; X-ray; 2.30 A; A=1-888. DR PDB; 2ZLF; X-ray; 2.59 A; A=1-888. DR PDB; 2ZLG; X-ray; 2.52 A; A=1-888. DR PDB; 3K8T; X-ray; 2.10 A; A=1-888. DR PDB; 3PAW; X-ray; 6.61 A; A/B/C/D=1-888. DR PDB; 3RSR; X-ray; 2.30 A; A=1-888. DR PDB; 3S87; X-ray; 2.25 A; A=1-888. DR PDB; 3S8A; X-ray; 2.90 A; A=1-888. DR PDB; 3S8B; X-ray; 2.80 A; A=1-888. DR PDB; 3S8C; X-ray; 2.77 A; A=1-888. DR PDB; 3TB9; X-ray; 2.53 A; A=1-888. DR PDB; 3TBA; X-ray; 2.80 A; A=1-888. DR PDBsum; 1ZYZ; -. DR PDBsum; 1ZZD; -. DR PDBsum; 2CVS; -. DR PDBsum; 2CVT; -. DR PDBsum; 2CVU; -. DR PDBsum; 2CVV; -. DR PDBsum; 2CVW; -. DR PDBsum; 2CVX; -. DR PDBsum; 2CVY; -. DR PDBsum; 2EUD; -. DR PDBsum; 2ZLF; -. DR PDBsum; 2ZLG; -. DR PDBsum; 3K8T; -. DR PDBsum; 3PAW; -. DR PDBsum; 3RSR; -. DR PDBsum; 3S87; -. DR PDBsum; 3S8A; -. DR PDBsum; 3S8B; -. DR PDBsum; 3S8C; -. DR PDBsum; 3TB9; -. DR PDBsum; 3TBA; -. DR AlphaFoldDB; P21524; -. DR SMR; P21524; -. DR BioGRID; 36813; 256. DR ComplexPortal; CPX-1102; Ribonucleoside-diphosphate reductase variant 1. DR ComplexPortal; CPX-1103; Ribonucleoside-diphosphate reductase variant 2. DR DIP; DIP-6299N; -. DR IntAct; P21524; 13. DR MINT; P21524; -. DR STRING; 4932.YER070W; -. DR iPTMnet; P21524; -. DR MaxQB; P21524; -. DR PaxDb; 4932-YER070W; -. DR PeptideAtlas; P21524; -. DR EnsemblFungi; YER070W_mRNA; YER070W; YER070W. DR GeneID; 856801; -. DR KEGG; sce:YER070W; -. DR AGR; SGD:S000000872; -. DR SGD; S000000872; RNR1. DR VEuPathDB; FungiDB:YER070W; -. DR eggNOG; KOG1112; Eukaryota. DR GeneTree; ENSGT00910000144246; -. DR HOGENOM; CLU_000404_1_0_1; -. DR InParanoid; P21524; -. DR OMA; QMSSCYL; -. DR OrthoDB; 5472715at2759; -. DR BioCyc; MetaCyc:YER070W-MONOMER; -. DR BioCyc; YEAST:YER070W-MONOMER; -. DR BRENDA; 1.17.4.1; 984. DR BioGRID-ORCS; 856801; 0 hits in 10 CRISPR screens. DR EvolutionaryTrace; P21524; -. DR PRO; PR:P21524; -. DR Proteomes; UP000002311; Chromosome V. DR RNAct; P21524; Protein. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0005634; C:nucleus; HDA:SGD. DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IDA:SGD. DR GO; GO:0005524; F:ATP binding; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0000166; F:nucleotide binding; IDA:SGD. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IDA:SGD. DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IDA:SGD. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR CDD; cd01679; RNR_I; 1. DR Gene3D; 3.20.70.20; -; 1. DR InterPro; IPR005144; ATP-cone_dom. DR InterPro; IPR013346; NrdE_NrdA_C. DR InterPro; IPR000788; RNR_lg_C. DR InterPro; IPR013509; RNR_lsu_N. DR InterPro; IPR008926; RNR_R1-su_N. DR InterPro; IPR039718; Rrm1. DR NCBIfam; TIGR02506; NrdE_NrdA; 1. DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1. DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1. DR Pfam; PF03477; ATP-cone; 1. DR Pfam; PF02867; Ribonuc_red_lgC; 1. DR Pfam; PF00317; Ribonuc_red_lgN; 1. DR PRINTS; PR01183; RIBORDTASEM1. DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1. DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1. DR PROSITE; PS51161; ATP_CONE; 1. DR PROSITE; PS00089; RIBORED_LARGE; 1. PE 1: Evidence at protein level; KW 3D-structure; Allosteric enzyme; ATP-binding; Cytoplasm; KW Deoxyribonucleotide synthesis; Disulfide bond; Isopeptide bond; KW Nucleotide-binding; Oxidoreductase; Phosphoprotein; Reference proteome; KW Ubl conjugation. FT CHAIN 1..888 FT /note="Ribonucleoside-diphosphate reductase large chain 1" FT /id="PRO_0000187203" FT DOMAIN 1..92 FT /note="ATP-cone" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00492" FT REGION 804..825 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 839..861 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 426 FT /note="Proton acceptor" FT ACT_SITE 428 FT /note="Cysteine radical intermediate" FT ACT_SITE 430 FT /note="Proton acceptor" FT BINDING 5..6 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:P23921" FT BINDING 11..17 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:P23921" FT BINDING 53 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:P23921" FT BINDING 57 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:P23921" FT BINDING 202 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:P23921" FT BINDING 217 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:P23921" FT BINDING 226..228 FT /ligand="dTTP" FT /ligand_id="ChEBI:CHEBI:37568" FT /ligand_note="allosteric effector that controls substrate FT specificity" FT /evidence="ECO:0000250|UniProtKB:P23921" FT BINDING 243 FT /ligand="dTTP" FT /ligand_id="ChEBI:CHEBI:37568" FT /ligand_note="allosteric effector that controls substrate FT specificity" FT /evidence="ECO:0000250|UniProtKB:P23921" FT BINDING 256 FT /ligand="dTTP" FT /ligand_id="ChEBI:CHEBI:37568" FT /ligand_note="allosteric effector that controls substrate FT specificity" FT /evidence="ECO:0000250|UniProtKB:P23921" FT BINDING 263..264 FT /ligand="dTTP" FT /ligand_id="ChEBI:CHEBI:37568" FT /ligand_note="allosteric effector that controls substrate FT specificity" FT /evidence="ECO:0000250|UniProtKB:P23921" FT BINDING 426 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:P23921" FT BINDING 430 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:P23921" FT BINDING 608..611 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:P23921" FT SITE 218 FT /note="Important for hydrogen atom transfer" FT /evidence="ECO:0000250" FT SITE 443 FT /note="Important for hydrogen atom transfer" FT /evidence="ECO:0000250" FT SITE 741 FT /note="Important for electron transfer" FT /evidence="ECO:0000250" FT SITE 742 FT /note="Important for electron transfer" FT /evidence="ECO:0000250" FT SITE 883 FT /note="Interacts with thioredoxin/glutaredoxin" FT /evidence="ECO:0000250" FT SITE 886 FT /note="Interacts with thioredoxin/glutaredoxin" FT /evidence="ECO:0000250" FT MOD_RES 227 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 816 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P21672" FT MOD_RES 837 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 887 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT DISULFID 218..443 FT /note="Redox-active" FT /evidence="ECO:0000269|PubMed:16537479" FT CROSSLNK 387 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT CROSSLNK 853 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT MUTAGEN 428 FT /note="C->A: Completely abolishes reductase activity." FT /evidence="ECO:0000269|PubMed:11893751" FT CONFLICT 329 FT /note="F -> L (in Ref. 4; CAA49151)" FT /evidence="ECO:0000305" FT CONFLICT 587..589 FT /note="TLR -> NLK (in Ref. 4; CAA49150)" FT /evidence="ECO:0000305" FT CONFLICT 666 FT /note="Q -> E (in Ref. 3; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 679 FT /note="E -> Q (in Ref. 3; no nucleotide entry)" FT /evidence="ECO:0000305" FT HELIX 19..23 FT /evidence="ECO:0007829|PDB:1ZYZ" FT TURN 31..33 FT /evidence="ECO:0007829|PDB:1ZYZ" FT HELIX 36..41 FT /evidence="ECO:0007829|PDB:1ZYZ" FT HELIX 53..66 FT /evidence="ECO:0007829|PDB:1ZYZ" FT TURN 67..70 FT /evidence="ECO:0007829|PDB:1ZYZ" FT HELIX 79..89 FT /evidence="ECO:0007829|PDB:2CVX" FT HELIX 94..102 FT /evidence="ECO:0007829|PDB:3K8T" FT TURN 107..110 FT /evidence="ECO:0007829|PDB:3K8T" FT HELIX 118..126 FT /evidence="ECO:0007829|PDB:3K8T" FT HELIX 128..132 FT /evidence="ECO:0007829|PDB:3K8T" FT HELIX 137..142 FT /evidence="ECO:0007829|PDB:3K8T" FT HELIX 145..154 FT /evidence="ECO:0007829|PDB:3K8T" FT STRAND 158..163 FT /evidence="ECO:0007829|PDB:2CVX" FT HELIX 167..179 FT /evidence="ECO:0007829|PDB:3K8T" FT HELIX 183..194 FT /evidence="ECO:0007829|PDB:3K8T" FT STRAND 197..200 FT /evidence="ECO:0007829|PDB:3K8T" FT HELIX 202..207 FT /evidence="ECO:0007829|PDB:3K8T" FT STRAND 210..212 FT /evidence="ECO:0007829|PDB:3K8T" FT STRAND 218..222 FT /evidence="ECO:0007829|PDB:3K8T" FT HELIX 228..242 FT /evidence="ECO:0007829|PDB:3K8T" FT TURN 243..245 FT /evidence="ECO:0007829|PDB:3S8A" FT STRAND 247..251 FT /evidence="ECO:0007829|PDB:3K8T" FT TURN 263..266 FT /evidence="ECO:0007829|PDB:3K8T" FT HELIX 272..285 FT /evidence="ECO:0007829|PDB:3K8T" FT TURN 288..291 FT /evidence="ECO:0007829|PDB:2CVX" FT STRAND 297..301 FT /evidence="ECO:0007829|PDB:3K8T" FT HELIX 308..311 FT /evidence="ECO:0007829|PDB:3K8T" FT TURN 312..315 FT /evidence="ECO:0007829|PDB:3K8T" FT STRAND 317..319 FT /evidence="ECO:0007829|PDB:3K8T" FT HELIX 321..323 FT /evidence="ECO:0007829|PDB:2CVX" FT STRAND 328..334 FT /evidence="ECO:0007829|PDB:3K8T" FT HELIX 336..343 FT /evidence="ECO:0007829|PDB:3K8T" FT STRAND 347..351 FT /evidence="ECO:0007829|PDB:3K8T" FT TURN 353..355 FT /evidence="ECO:0007829|PDB:3K8T" FT HELIX 359..361 FT /evidence="ECO:0007829|PDB:3K8T" FT HELIX 364..376 FT /evidence="ECO:0007829|PDB:3K8T" FT STRAND 380..384 FT /evidence="ECO:0007829|PDB:3K8T" FT HELIX 385..399 FT /evidence="ECO:0007829|PDB:3K8T" FT STRAND 403..406 FT /evidence="ECO:0007829|PDB:3K8T" FT HELIX 407..412 FT /evidence="ECO:0007829|PDB:3K8T" FT TURN 415..419 FT /evidence="ECO:0007829|PDB:3K8T" FT STRAND 427..429 FT /evidence="ECO:0007829|PDB:1ZYZ" FT STRAND 441..443 FT /evidence="ECO:0007829|PDB:3K8T" FT STRAND 445..449 FT /evidence="ECO:0007829|PDB:3K8T" FT HELIX 450..453 FT /evidence="ECO:0007829|PDB:3K8T" FT STRAND 454..456 FT /evidence="ECO:0007829|PDB:2CVX" FT STRAND 458..462 FT /evidence="ECO:0007829|PDB:2EUD" FT STRAND 463..465 FT /evidence="ECO:0007829|PDB:2CVX" FT HELIX 467..487 FT /evidence="ECO:0007829|PDB:3K8T" FT HELIX 493..502 FT /evidence="ECO:0007829|PDB:3K8T" FT STRAND 506..510 FT /evidence="ECO:0007829|PDB:3K8T" FT HELIX 512..519 FT /evidence="ECO:0007829|PDB:3K8T" FT HELIX 526..554 FT /evidence="ECO:0007829|PDB:3K8T" FT HELIX 564..567 FT /evidence="ECO:0007829|PDB:3K8T" FT HELIX 571..574 FT /evidence="ECO:0007829|PDB:3K8T" FT STRAND 581..583 FT /evidence="ECO:0007829|PDB:2ZLG" FT HELIX 585..595 FT /evidence="ECO:0007829|PDB:3K8T" FT HELIX 611..615 FT /evidence="ECO:0007829|PDB:3K8T" FT STRAND 619..622 FT /evidence="ECO:0007829|PDB:2CVS" FT STRAND 627..629 FT /evidence="ECO:0007829|PDB:2CVX" FT STRAND 634..636 FT /evidence="ECO:0007829|PDB:1ZYZ" FT STRAND 638..641 FT /evidence="ECO:0007829|PDB:1ZYZ" FT HELIX 643..651 FT /evidence="ECO:0007829|PDB:3K8T" FT HELIX 657..664 FT /evidence="ECO:0007829|PDB:3K8T" FT TURN 665..668 FT /evidence="ECO:0007829|PDB:3K8T" FT HELIX 678..683 FT /evidence="ECO:0007829|PDB:3K8T" FT HELIX 687..689 FT /evidence="ECO:0007829|PDB:3K8T" FT HELIX 692..703 FT /evidence="ECO:0007829|PDB:3K8T" FT STRAND 714..718 FT /evidence="ECO:0007829|PDB:2CVX" FT HELIX 721..734 FT /evidence="ECO:0007829|PDB:3K8T" FT STRAND 737..741 FT /evidence="ECO:0007829|PDB:3K8T" FT STRAND 743..745 FT /evidence="ECO:0007829|PDB:2CVX" FT TURN 748..751 FT /evidence="ECO:0007829|PDB:1ZYZ" FT HELIX 760..763 FT /evidence="ECO:0007829|PDB:1ZYZ" FT HELIX 764..766 FT /evidence="ECO:0007829|PDB:1ZYZ" FT TURN 789..791 FT /evidence="ECO:0007829|PDB:1ZYZ" SQ SEQUENCE 888 AA; 99561 MW; 56BE1B077916E419 CRC64; MYVYKRDGRK EPVQFDKITA RISRLCYGLD PKHIDAVKVT QRIISGVYEG VTTIELDNLA AETCAYMTTV HPDYATLAAR IAISNLHKQT TKQFSKVVED LYRYVNAATG KPAPMISDDV YNIVMENKDK LNSAIVYDRD FQYSYFGFKT LERSYLLRIN GQVAERPQHL IMRVALGIHG RDIEAALETY NLMSLKYFTH ASPTLFNAGT PKPQMSSCFL VAMKEDSIEG IYDTLKECAL ISKTAGGIGL HIHNIRSTGS YIAGTNGTSN GLIPMIRVFN NTARYVDQGG NKRPGAFALY LEPWHADIFD FIDIRKNHGK EEIRARDLFP ALWIPDLFMK RVEENGTWTL FSPTSAPGLS DCYGDEFEAL YTRYEKEGRG KTIKAQKLWY SILEAQTETG TPFVVYKDAC NRKSNQKNLG VIKSSNLCCE IVEYSAPDET AVCNLASVAL PAFIETSEDG KTSTYNFKKL HEIAKVVTRN LNRVIDRNYY PVEEARKSNM RHRPIALGVQ GLADTFMLLR LPFDSEEARL LNIQIFETIY HASMEASCEL AQKDGPYETF QGSPASQGIL QFDMWDQKPY GMWDWDTLRK DIMKHGVRNS LTMAPMPTAS TSQILGYNEC FEPVTSNMYS RRVLSGEFQV VNPYLLRDLV DLGIWDEGMK QYLITQNGSI QGLPNVPQEL KDLYKTVWEI SQKTIINMAA DRSVYIDQSH SLNLFLRAPT MGKLTSMHFY GWKKGLKTGM YYLRTQAASA AIQFTIDQKI ADQATENVAD ISNLKRPSYM PSSASYAASD FVPAAVTANA TIPSLDSSSE ASREASPAPT GSHSLTKGMA ELNVQESKVE VPEVPAPTKN EEKAAPIVDD EETEFDIYNS KVIACAIDNP EACEMCSG //