ID RIR1_ASFWA Reviewed; 778 AA. AC P0C8H9; DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 1. DT 27-MAR-2024, entry version 46. DE RecName: Full=Ribonucleoside-diphosphate reductase large subunit; DE EC=1.17.4.1; DE AltName: Full=Ribonucleotide reductase large subunit; GN OrderedLocusNames=War-055; OS African swine fever virus (isolate Warthog/Namibia/Wart80/1980) (ASFV). OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes; OC Asfuvirales; Asfarviridae; Asfivirus; African swine fever virus. OX NCBI_TaxID=561444; OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks). OH NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog). OH NCBI_TaxID=41426; Phacochoerus africanus (Warthog). OH NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig). OH NCBI_TaxID=9823; Sus scrofa (Pig). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Kutish G.F., Rock D.L.; RT "African swine fever virus genomes."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Ribonucleoside-diphosphate reductase holoenzyme provides the CC precursors necessary for viral DNA synthesis. Allows virus growth in CC non-dividing cells. Catalyzes the biosynthesis of deoxyribonucleotides CC from the corresponding ribonucleotides (By similarity). {ECO:0000250}. 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. The type of nucleotide CC bound at the specificity site determines substrate preference. It seems CC probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP CC reduction and dTTP favors GDP reduction (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Heterotetramer composed of a homodimer of the large subunit CC (R1) and a homodimer of the small subunit (R2). Larger multisubunit CC protein complex are also active, composed of (R1)n(R2)n (By CC similarity). {ECO:0000250}. CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle. CC {ECO:0000305}. 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; AY261366; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR SMR; P0C8H9; -. DR Proteomes; UP000000858; Genome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC. DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR Gene3D; 3.20.70.20; -; 1. 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; 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; PS00089; RIBORED_LARGE; 1. PE 3: Inferred from homology; KW Allosteric enzyme; ATP-binding; Deoxyribonucleotide synthesis; KW Disulfide bond; Early protein; Nucleotide-binding; Oxidoreductase. FT CHAIN 1..778 FT /note="Ribonucleoside-diphosphate reductase large subunit" FT /id="PRO_0000355221" FT ACT_SITE 419 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 421 FT /note="Cysteine radical intermediate" FT /evidence="ECO:0000250" FT ACT_SITE 423 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 177 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 192..193 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 221 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 419..423 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 613..617 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 193 FT /note="Important for hydrogen atom transfer" FT /evidence="ECO:0000250" FT SITE 200 FT /note="Allosteric effector binding" FT /evidence="ECO:0000250" FT SITE 230 FT /note="Allosteric effector binding" FT /evidence="ECO:0000250" FT SITE 439 FT /note="Important for hydrogen atom transfer" FT /evidence="ECO:0000250" FT SITE 747 FT /note="Important for electron transfer" FT /evidence="ECO:0000250" FT SITE 748 FT /note="Important for electron transfer" FT /evidence="ECO:0000250" FT SITE 773 FT /note="Interacts with thioredoxin/glutaredoxin" FT /evidence="ECO:0000250" FT SITE 776 FT /note="Interacts with thioredoxin/glutaredoxin" FT /evidence="ECO:0000250" FT DISULFID 193..439 FT /note="Redox-active" FT /evidence="ECO:0000250" SQ SEQUENCE 778 AA; 87402 MW; 5F0D50259308371F CRC64; METFCIETLA SDTYGKALNV DLDRLSQAQI KYTLQELISY CSALTILHYD YSTLAARLSV YQLHQSTASS FSKAVRLQAA QSCSRLSPQF VDVVYKYKAI FDSYIDYNRD YKLSLLGIET MKNSYLLKNK DGVIMERPQD AYMRVAIMIY GMGKVVNIKM ILLTYDLLSQ HIITHASPTM FNAGTKKPQL SSCFLLNVND NLENLYDMVK TAGIISGGGG GIGLCLSGIR AKNSFISGSG LRSNGIQNYI MLQNASQCYA NQGGLRPGAY AVYLELWHQD IFTFLEMPRL KGQMAEQRLN APNLKYGLWV PDLFMEILED QIHNRGDGRW YLFSPDQAPN LHKVFDLERS QHENAHREFK KLYYQYVAEK RYTGVTTAKE IIKAWFKTVI QVGNPYIGFK DAINRKSNLS HVGTITNSNL CIEVTIPCWE GDKAEQGVCN LAAVNLAAFI RENGYDYRGL IEASGNVTEN LDNIIDNGYY PTEATRRSNM RHRPIGIGVF GLADVFASLK IKFGSPEAIA MDEAIHAALY YGAMRRSIEL AKEKGSHPSF PGSAASKGLL QPDLWVRCGD LIPSWEERVA QTTQGVLTRK SWRQLRLAAI QGVRNGYLTA LMPTATSSNS TGKNECFEPF TSNLYTRRTL SGEFIVLNKY LIDDLKEINL WTEAIQLQLL NAGGSIQHIL DIPAEIRDRY KTSREMNQKI LTKHAAARNP FVSQSMSLNY YFYEPELSQV LTVLVLGWKK GLTTGSYYCH FSPGAGTQKK IIRNSEKACN ADCEACLL //