RIR1_YEAST
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 03-AUG-2022, entry version 207.
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 -!- PATHWAY: Genetic information processing; DNA replication.
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}.
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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; 89.
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; P21524; -.
DR PRIDE; P21524; -.
DR EnsemblFungi; YER070W_mRNA; YER070W; YER070W.
DR GeneID; 856801; -.
DR KEGG; sce:YER070W; -.
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; RGSIQNI; -.
DR BioCyc; MetaCyc:YER070W-MON; -.
DR BioCyc; YEAST:YER070W-MON; -.
DR BRENDA; 1.17.4.1; 984.
DR UniPathway; UPA00326; -.
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:UniProtKB-UniPathway.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR013346; NrdE_NrdA.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR PANTHER; PTHR11573; PTHR11573; 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; SSF48168; SSF48168; 1.
DR TIGRFAMs; TIGR02506; NrdE_NrdA; 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
