ID RIR1_ASFM2 Reviewed; 779 AA. AC P26685; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 27-MAR-2024, entry version 93. DE RecName: Full=Ribonucleoside-diphosphate reductase large subunit; DE EC=1.17.4.1; DE AltName: Full=Ribonucleotide reductase large subunit; GN OrderedLocusNames=Mal-053; OS African swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV). OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes; OC Asfuvirales; Asfarviridae; Asfivirus; African swine fever virus. OX NCBI_TaxID=10500; 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 [GENOMIC DNA]. RX PubMed=1871976; DOI=10.1016/0042-6822(91)90860-e; RA Boursnell M., Shaw K., Yanez R.J., Vinuela E., Dixon L.; RT "The sequences of the ribonucleotide reductase genes from African swine RT fever virus show considerable homology with those of the orthopoxvirus, RT vaccinia virus."; RL Virology 184:411-416(1991). RN [2] 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; M64728; AAA42732.1; -; Genomic_DNA. DR PIR; A40568; WMVZAL. DR SMR; P26685; -. 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..779 FT /note="Ribonucleoside-diphosphate reductase large subunit" FT /id="PRO_0000187228" FT ACT_SITE 420 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 422 FT /note="Cysteine radical intermediate" FT /evidence="ECO:0000250" FT ACT_SITE 424 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 178 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 193..194 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 222 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 420..424 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 614..618 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 194 FT /note="Important for hydrogen atom transfer" FT /evidence="ECO:0000250" FT SITE 201 FT /note="Allosteric effector binding" FT /evidence="ECO:0000250" FT SITE 231 FT /note="Allosteric effector binding" FT /evidence="ECO:0000250" FT SITE 440 FT /note="Important for hydrogen atom transfer" FT /evidence="ECO:0000250" FT SITE 748 FT /note="Important for electron transfer" FT /evidence="ECO:0000250" FT SITE 749 FT /note="Important for electron transfer" FT /evidence="ECO:0000250" FT SITE 774 FT /note="Interacts with thioredoxin/glutaredoxin" FT /evidence="ECO:0000250" FT SITE 777 FT /note="Interacts with thioredoxin/glutaredoxin" FT /evidence="ECO:0000250" FT DISULFID 194..440 FT /note="Redox-active" FT /evidence="ECO:0000250" SQ SEQUENCE 779 AA; 87388 MW; 88A3D0C8D5D10819 CRC64; MENFFIVKKL ASATYGKALN VDLNKLLQAL NHHSLQGLIS YCSALTILHY DYSTLAARLS VYLLHQSTAS SFSKAVSLQA AQSCSRLSSH FVDVVYKYKA IFDSYIDYSR DYKLSLLGIE TMKNSYLLKN KDGVIMERPQ DAYMRVAIMI HGMGRVVNMK MILLTYDLLS RHVITHASPT MFNAGTKKPQ LSSCFLLNVN DNLENLYDMV KTAGIISGGG GGIGLCLSGI RAKNSFISGS GLRSNGIQNY IVLQNASQCY ANQGGLRPGA YAVYLELWHQ DIFTFLQMPR LKGQMAEQRL NAPNLKYGLW VPDLFMEILE DQIHNRGDGT WYLFSPDQAP NLHKVFDLER SQHENAHREF KKLYYQYVAE KRYTGVTTAK EIIKEWFKTV VQVGNPYIGF KDAINRKSNL SHVGTITNSN LCIEITIPCW EGNEAEQGVC NLAAVNLAAF IRESSYDYRG LIEAAGNVTE NLDNIIDNGY YPTEATRRSN MRHRPIGIGV FGLADVFASL KMKFGSPEAI AIDEAIHAAL YYGAMRRSIE LAKEKGSHPS FPGSAASKGL LQPDLWVRCG DLIPSWENRV AQTTQGVLTP KKWWQLRLAA IQGVRNGYLT ALMPTATSSN STGKNECFEP FTSNLYTRRT LSGEFIILNK YLMDDLEEIN LWSEDIQQQL LNAGGSIQHI LDIPAEIRER YKTSREMNQK ILTKHAAARN PFVSQSMSLN YYFYEPELSQ VLTVLVLGWK KGLTTGSYYC HFSPGAGTQK KIIRNSEKAC NADCEACLL //