RIR1_HUMAN
ID RIR1_HUMAN Reviewed; 792 AA.
AC P23921; Q9UNN2;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Ribonucleoside-diphosphate reductase large subunit;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleoside-diphosphate reductase subunit M1;
DE AltName: Full=Ribonucleotide reductase large subunit;
GN Name=RRM1; Synonyms=RR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Bone marrow;
RX PubMed=1840662; DOI=10.1093/nar/19.13.3741;
RA Parker N.J., Begley C.G., Fox R.M.;
RT "Human M1 subunit of ribonucleotide reductase: cDNA sequence and expression
RT in stimulated lymphocytes.";
RL Nucleic Acids Res. 19:3741-3741(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary carcinoma;
RX PubMed=1627826; DOI=10.3109/10425179209020807;
RA Pavloff N., Rivard D., Masson S., Shen S.-H., Mes-Masson A.-M.;
RT "Sequence analysis of the large and small subunits of human ribonucleotide
RT reductase.";
RL DNA Seq. 2:227-234(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9933563; DOI=10.1006/geno.1998.5659;
RA Bepler G., O'Briant K.C., Kim Y.-C., Schreiber G., Pitterle D.M.;
RT "A 1.4-Mb high-resolution physical map and contig of chromosome segment
RT 11p15.5 and genes in the LOH11A metastasis suppressor region.";
RL Genomics 55:164-175(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RC TISSUE=Placenta;
RX PubMed=8188248; DOI=10.1006/geno.1994.1017;
RA Parker N.J., Begley C.G., Fox R.M.;
RT "Human R1 subunit of ribonucleotide reductase (RRM1): 5' flanking region of
RT the gene.";
RL Genomics 19:91-96(1994).
RN [6]
RP ACTIVITY REGULATION.
RX PubMed=1867633; DOI=10.1016/0006-2952(91)90033-2;
RA Harrington J.A., Spector T.;
RT "Human ribonucleotide reductase. Activation and inhibition by analogs of
RT ATP.";
RL Biochem. Pharmacol. 42:759-763(1991).
RN [7]
RP INTERACTION WITH RRM2B.
RX PubMed=12615712;
RA Xue L., Zhou B., Liu X., Qiu W., Jin Z., Yen Y.;
RT "Wild-type p53 regulates human ribonucleotide reductase by protein-protein
RT interaction with p53R2 as well as hRRM2 subunits.";
RL Cancer Res. 63:980-986(2003).
RN [8]
RP CATALYTIC ACTIVITY, SUBUNIT, AND ACTIVITY REGULATION.
RX PubMed=16376858; DOI=10.1016/j.bbrc.2005.12.019;
RA Qiu W., Zhou B., Darwish D., Shao J., Yen Y.;
RT "Characterization of enzymatic properties of human ribonucleotide reductase
RT holoenzyme reconstituted in vitro from hRRM1, hRRM2, and p53R2 subunits.";
RL Biochem. Biophys. Res. Commun. 340:428-434(2006).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17 AND LYS-376, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-751, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP ACTIVITY REGULATION, MUTAGENESIS OF ASP-57, AND INTERACTION WITH AHCYL1.
RX PubMed=25237103; DOI=10.1126/science.1251550;
RA Arnaoutov A., Dasso M.;
RT "Enzyme regulation. IRBIT is a novel regulator of ribonucleotide reductase
RT in higher eukaryotes.";
RL Science 345:1512-1515(2014).
RN [13] {ECO:0007744|PDB:2WGH, ECO:0007744|PDB:3HNC, ECO:0007744|PDB:3HND, ECO:0007744|PDB:3HNE, ECO:0007744|PDB:3HNF}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 75-742 IN COMPLEX WITH ALLOSTERIC
RP EFFECTORS ATP; DATP; DTTP; SUBSTRATE GDP AND MAGNESIUM IONS.
RX PubMed=21336276; DOI=10.1038/nsmb.2007;
RA Fairman J.W., Wijerathna S.R., Ahmad M.F., Xu H., Nakano R., Jha S.,
RA Prendergast J., Welin R.M., Flodin S., Roos A., Nordlund P., Li Z.,
RA Walz T., Dealwis C.G.;
RT "Structural basis for allosteric regulation of human ribonucleotide
RT reductase by nucleotide-induced oligomerization.";
RL Nat. Struct. Mol. Biol. 18:316-322(2011).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides.
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 Evidence={ECO:0000269|PubMed:16376858};
CC -!- ACTIVITY REGULATION: Under complex allosteric control mediated by
CC deoxynucleoside triphosphates and ATP binding to separate specificity
CC and activation sites on the M1 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, the dATP inhibition is mediated by AHCYL1
CC which stabilizes dATP in the site. {ECO:0000269|PubMed:16376858,
CC ECO:0000269|PubMed:1867633, ECO:0000269|PubMed:25237103}.
CC -!- PATHWAY: Genetic information processing; DNA replication.
CC -!- SUBUNIT: Heterodimer of a large and a small subunit. Heterodimer with
CC small subunit RRM2 or RRM2B. The heterodimer with RRM2 has higher
CC catalytic activity than the heterodimer with RRM2B. Interacts with
CC AHCYL1 which inhibits its activity. {ECO:0000269|PubMed:16376858,
CC ECO:0000269|PubMed:21336276, ECO:0000269|PubMed:25237103}.
CC -!- INTERACTION:
CC P23921; P23921: RRM1; NbExp=5; IntAct=EBI-717006, EBI-717006;
CC P23921; P31350: RRM2; NbExp=6; IntAct=EBI-717006, EBI-2339245;
CC P23921; Q8N720: ZNF655; NbExp=3; IntAct=EBI-717006, EBI-625509;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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 M1, is formed only in the presence
CC of the second subunit M2.
CC -!- MISCELLANEOUS: The level of the enzyme activity is closely correlated
CC with the growth rate of a cell and appears to vary with the cell cycle.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Ribonucleotide reductase entry;
CC URL="https://en.wikipedia.org/wiki/Ribonucleotide_reductase";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RRM1ID42174ch11p15.html";
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DR EMBL; X59543; CAA42118.1; -; mRNA.
DR EMBL; X59617; CAA42180.1; -; mRNA.
DR EMBL; AF107045; AAD37491.1; -; Genomic_DNA.
DR EMBL; BC006498; AAH06498.1; -; mRNA.
DR EMBL; L10342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS7750.1; -.
DR PIR; S16680; S16680.
DR RefSeq; NP_001024.1; NM_001033.4.
DR RefSeq; NP_001304993.1; NM_001318064.1.
DR RefSeq; NP_001304994.1; NM_001318065.1.
DR PDB; 2WGH; X-ray; 2.30 A; A/B=75-742.
DR PDB; 3HNC; X-ray; 2.41 A; A/B=1-792.
DR PDB; 3HND; X-ray; 3.21 A; A/B=1-792.
DR PDB; 3HNE; X-ray; 3.11 A; A/B=1-792.
DR PDB; 3HNF; X-ray; 3.16 A; A/B=1-792.
DR PDB; 4X3V; X-ray; 3.70 A; A/B=1-792.
DR PDB; 5D1Y; X-ray; 9.01 A; A/B=1-792.
DR PDB; 5TUS; X-ray; 2.66 A; A/B=1-792.
DR PDB; 6AUI; EM; 3.30 A; A/B/C/D/E/F=1-792.
DR PDB; 6L3R; X-ray; 2.00 A; A/E=75-742.
DR PDB; 6L7L; X-ray; 2.17 A; A/E=75-742.
DR PDB; 6LKM; X-ray; 2.55 A; A/B=75-742.
DR PDBsum; 2WGH; -.
DR PDBsum; 3HNC; -.
DR PDBsum; 3HND; -.
DR PDBsum; 3HNE; -.
DR PDBsum; 3HNF; -.
DR PDBsum; 4X3V; -.
DR PDBsum; 5D1Y; -.
DR PDBsum; 5TUS; -.
DR PDBsum; 6AUI; -.
DR PDBsum; 6L3R; -.
DR PDBsum; 6L7L; -.
DR PDBsum; 6LKM; -.
DR AlphaFoldDB; P23921; -.
DR SMR; P23921; -.
DR BioGRID; 112154; 95.
DR ComplexPortal; CPX-2194; Ribonucleoside-diphosphate reductase RR1 complex, RRM2 variant.
DR ComplexPortal; CPX-369; Ribonucleoside-diphosphate reductase RR1 complex, RRM2B variant.
DR DIP; DIP-24233N; -.
DR IntAct; P23921; 26.
DR MINT; P23921; -.
DR STRING; 9606.ENSP00000300738; -.
DR BindingDB; P23921; -.
DR ChEMBL; CHEMBL1830; -.
DR DrugBank; DB00242; Cladribine.
DR DrugBank; DB00631; Clofarabine.
DR DrugBank; DB01073; Fludarabine.
DR DrugBank; DB05420; Gallium maltolate.
DR DrugBank; DB00441; Gemcitabine.
DR DrugBank; DB01005; Hydroxyurea.
DR DrugBank; DB05003; Imexon.
DR DrugBank; DB06433; Tezacitabine.
DR DrugCentral; P23921; -.
DR GuidetoPHARMACOLOGY; 2630; -.
DR GlyGen; P23921; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; P23921; -.
DR MetOSite; P23921; -.
DR PhosphoSitePlus; P23921; -.
DR SwissPalm; P23921; -.
DR BioMuta; RRM1; -.
DR DMDM; 132608; -.
DR EPD; P23921; -.
DR jPOST; P23921; -.
DR MassIVE; P23921; -.
DR MaxQB; P23921; -.
DR PaxDb; P23921; -.
DR PeptideAtlas; P23921; -.
DR PRIDE; P23921; -.
DR ProteomicsDB; 54166; -.
DR Antibodypedia; 10853; 671 antibodies from 38 providers.
DR DNASU; 6240; -.
DR Ensembl; ENST00000300738.10; ENSP00000300738.5; ENSG00000167325.15.
DR GeneID; 6240; -.
DR KEGG; hsa:6240; -.
DR MANE-Select; ENST00000300738.10; ENSP00000300738.5; NM_001033.5; NP_001024.1.
DR UCSC; uc001lyw.5; human.
DR CTD; 6240; -.
DR DisGeNET; 6240; -.
DR GeneCards; RRM1; -.
DR HGNC; HGNC:10451; RRM1.
DR HPA; ENSG00000167325; Low tissue specificity.
DR MIM; 180410; gene.
DR neXtProt; NX_P23921; -.
DR OpenTargets; ENSG00000167325; -.
DR PharmGKB; PA298; -.
DR VEuPathDB; HostDB:ENSG00000167325; -.
DR eggNOG; KOG1112; Eukaryota.
DR GeneTree; ENSGT00910000144246; -.
DR HOGENOM; CLU_000404_1_0_1; -.
DR InParanoid; P23921; -.
DR OMA; RGSIQNI; -.
DR OrthoDB; 156716at2759; -.
DR PhylomeDB; P23921; -.
DR TreeFam; TF300578; -.
DR BioCyc; MetaCyc:HS09541-MON; -.
DR BRENDA; 1.17.4.1; 2681.
DR PathwayCommons; P23921; -.
DR Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates.
DR SignaLink; P23921; -.
DR SIGNOR; P23921; -.
DR UniPathway; UPA00326; -.
DR BioGRID-ORCS; 6240; 810 hits in 1084 CRISPR screens.
DR ChiTaRS; RRM1; human.
DR EvolutionaryTrace; P23921; -.
DR GeneWiki; RRM1; -.
DR GenomeRNAi; 6240; -.
DR Pharos; P23921; Tclin.
DR PRO; PR:P23921; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P23921; protein.
DR Bgee; ENSG00000167325; Expressed in ventricular zone and 215 other tissues.
DR ExpressionAtlas; P23921; baseline and differential.
DR Genevisible; P23921; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IPI:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0061731; F:ribonucleoside-diphosphate reductase activity; IMP:CACAO.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; ISS:UniProtKB.
DR GO; GO:0009265; P:2'-deoxyribonucleotide biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IDA:ComplexPortal.
DR GO; GO:0000731; P:DNA synthesis involved in DNA repair; IC:ComplexPortal.
DR GO; GO:0006264; P:mitochondrial DNA replication; IMP:ComplexPortal.
DR GO; GO:0070318; P:positive regulation of G0 to G1 transition; IDA:ComplexPortal.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IDA:ComplexPortal.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IDA:ComplexPortal.
DR GO; GO:0051290; P:protein heterotetramerization; IEA:Ensembl.
DR GO; GO:0009185; P:ribonucleoside diphosphate metabolic process; IDA:ComplexPortal.
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; Acetylation; Allosteric enzyme; ATP-binding; Cytoplasm;
KW Deoxyribonucleotide synthesis; Disulfide bond; Nucleotide-binding;
KW Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..792
FT /note="Ribonucleoside-diphosphate reductase large subunit"
FT /id="PRO_0000187190"
FT DOMAIN 1..92
FT /note="ATP-cone"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00492"
FT ACT_SITE 427
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 429
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 431
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 5..6
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0007744|PDB:3HNE"
FT BINDING 11..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0007744|PDB:3HNE"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0007744|PDB:3HNE"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0007744|PDB:3HNE"
FT BINDING 202
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0007744|PDB:3HND"
FT BINDING 217
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0007744|PDB:3HND"
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:0007744|PDB:3HNE"
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:0007744|PDB:3HNE"
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:0007744|PDB:3HNE"
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:0007744|PDB:3HNE"
FT BINDING 427
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0007744|PDB:3HND"
FT BINDING 431
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0007744|PDB:3HND"
FT BINDING 604..607
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0007744|PDB:3HND"
FT SITE 218
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 444
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 737
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 738
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 787
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT SITE 790
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 376
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 751
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT DISULFID 218..444
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT VARIANT 590
FT /note="K -> Q (in dbSNP:rs2228123)"
FT /id="VAR_052052"
FT VARIANT 778
FT /note="V -> A (in dbSNP:rs2229196)"
FT /id="VAR_052053"
FT MUTAGEN 57
FT /note="D->N: Severely decreases interaction with AHCYL1 in
FT the presence of dATP."
FT /evidence="ECO:0000269|PubMed:25237103"
FT CONFLICT 6
FT /note="R -> Q (in Ref. 3; AAD37491)"
FT /evidence="ECO:0000305"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:3HNC"
FT TURN 6..8
FT /evidence="ECO:0007829|PDB:6AUI"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:3HNC"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:3HNC"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:6AUI"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:3HNC"
FT HELIX 36..44
FT /evidence="ECO:0007829|PDB:3HNC"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:3HND"
FT HELIX 53..66
FT /evidence="ECO:0007829|PDB:3HNC"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:3HNC"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:6L3R"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:6L3R"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:6L3R"
FT HELIX 118..126
FT /evidence="ECO:0007829|PDB:6L3R"
FT HELIX 128..134
FT /evidence="ECO:0007829|PDB:6L3R"
FT HELIX 137..142
FT /evidence="ECO:0007829|PDB:6L3R"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:6L3R"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:3HNF"
FT HELIX 167..179
FT /evidence="ECO:0007829|PDB:6L3R"
FT HELIX 183..194
FT /evidence="ECO:0007829|PDB:6L3R"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:6L3R"
FT HELIX 202..207
FT /evidence="ECO:0007829|PDB:6L3R"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:6L3R"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:6L3R"
FT HELIX 228..243
FT /evidence="ECO:0007829|PDB:6L3R"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:6L3R"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:3HNE"
FT TURN 263..266
FT /evidence="ECO:0007829|PDB:6L3R"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:3HNE"
FT HELIX 272..285
FT /evidence="ECO:0007829|PDB:6L3R"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:6AUI"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:6LKM"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:6L3R"
FT HELIX 308..311
FT /evidence="ECO:0007829|PDB:6L3R"
FT TURN 312..315
FT /evidence="ECO:0007829|PDB:6L3R"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:6L3R"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:6L3R"
FT STRAND 328..334
FT /evidence="ECO:0007829|PDB:6L3R"
FT HELIX 336..343
FT /evidence="ECO:0007829|PDB:6L3R"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:6L3R"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:6L3R"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:6L3R"
FT HELIX 364..376
FT /evidence="ECO:0007829|PDB:6L3R"
FT STRAND 381..385
FT /evidence="ECO:0007829|PDB:6L3R"
FT HELIX 386..400
FT /evidence="ECO:0007829|PDB:6L3R"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:6L3R"
FT HELIX 408..413
FT /evidence="ECO:0007829|PDB:6L3R"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:6L3R"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:3HNC"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:6L3R"
FT STRAND 446..450
FT /evidence="ECO:0007829|PDB:6L3R"
FT HELIX 451..454
FT /evidence="ECO:0007829|PDB:6L3R"
FT STRAND 459..461
FT /evidence="ECO:0007829|PDB:3HND"
FT HELIX 463..483
FT /evidence="ECO:0007829|PDB:6L3R"
FT HELIX 489..498
FT /evidence="ECO:0007829|PDB:6L3R"
FT STRAND 502..506
FT /evidence="ECO:0007829|PDB:6L3R"
FT HELIX 508..514
FT /evidence="ECO:0007829|PDB:6L3R"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:6LKM"
FT HELIX 522..550
FT /evidence="ECO:0007829|PDB:6L3R"
FT HELIX 554..556
FT /evidence="ECO:0007829|PDB:3HNE"
FT HELIX 561..563
FT /evidence="ECO:0007829|PDB:6L3R"
FT HELIX 567..570
FT /evidence="ECO:0007829|PDB:6L3R"
FT STRAND 577..579
FT /evidence="ECO:0007829|PDB:2WGH"
FT HELIX 581..591
FT /evidence="ECO:0007829|PDB:6L3R"
FT HELIX 605..611
FT /evidence="ECO:0007829|PDB:6L3R"
FT STRAND 615..618
FT /evidence="ECO:0007829|PDB:6AUI"
FT STRAND 623..625
FT /evidence="ECO:0007829|PDB:6L3R"
FT STRAND 632..637
FT /evidence="ECO:0007829|PDB:3HNC"
FT HELIX 639..647
FT /evidence="ECO:0007829|PDB:6L3R"
FT HELIX 655..661
FT /evidence="ECO:0007829|PDB:6L3R"
FT TURN 662..664
FT /evidence="ECO:0007829|PDB:6L3R"
FT HELIX 666..668
FT /evidence="ECO:0007829|PDB:6AUI"
FT STRAND 670..672
FT /evidence="ECO:0007829|PDB:6L7L"
FT HELIX 674..679
FT /evidence="ECO:0007829|PDB:6L3R"
FT HELIX 683..685
FT /evidence="ECO:0007829|PDB:6L3R"
FT HELIX 688..699
FT /evidence="ECO:0007829|PDB:6L3R"
FT STRAND 709..711
FT /evidence="ECO:0007829|PDB:6AUI"
FT HELIX 717..729
FT /evidence="ECO:0007829|PDB:6L3R"
FT STRAND 733..737
FT /evidence="ECO:0007829|PDB:6L3R"
SQ SEQUENCE 792 AA; 90070 MW; 4470A76C61E8F86A CRC64;
MHVIKRDGRQ ERVMFDKITS RIQKLCYGLN MDFVDPAQIT MKVIQGLYSG VTTVELDTLA
AETAATLTTK HPDYAILAAR IAVSNLHKET KKVFSDVMED LYNYINPHNG KHSPMVAKST
LDIVLANKDR LNSAIIYDRD FSYNYFGFKT LERSYLLKIN GKVAERPQHM LMRVSVGIHK
EDIDAAIETY NLLSERWFTH ASPTLFNAGT NRPQLSSCFL LSMKDDSIEG IYDTLKQCAL
ISKSAGGIGV AVSCIRATGS YIAGTNGNSN GLVPMLRVYN NTARYVDQGG NKRPGAFAIY
LEPWHLDIFE FLDLKKNTGK EEQRARDLFF ALWIPDLFMK RVETNQDWSL MCPNECPGLD
EVWGEEFEKL YASYEKQGRV RKVVKAQQLW YAIIESQTET GTPYMLYKDS CNRKSNQQNL
GTIKCSNLCT EIVEYTSKDE VAVCNLASLA LNMYVTSEHT YDFKKLAEVT KVVVRNLNKI
IDINYYPVPE ACLSNKRHRP IGIGVQGLAD AFILMRYPFE SAEAQLLNKQ IFETIYYGAL
EASCDLAKEQ GPYETYEGSP VSKGILQYDM WNVTPTDLWD WKVLKEKIAK YGIRNSLLIA
PMPTASTAQI LGNNESIEPY TSNIYTRRVL SGEFQIVNPH LLKDLTERGL WHEEMKNQII
ACNGSIQSIP EIPDDLKQLY KTVWEISQKT VLKMAAERGA FIDQSQSLNI HIAEPNYGKL
TSMHFYGWKQ GLKTGMYYLR TRPAANPIQF TLNKEKLKDK EKVSKEEEEK ERNTAAMVCS
LENRDECLMC GS
