ID RIR1_EHV4 Reviewed; 789 AA. AC P50642; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 24-JAN-2024, entry version 83. DE RecName: Full=Ribonucleoside-diphosphate reductase large subunit {ECO:0000255|HAMAP-Rule:MF_04026}; DE Short=R1 {ECO:0000255|HAMAP-Rule:MF_04026}; DE EC=1.17.4.1 {ECO:0000255|HAMAP-Rule:MF_04026}; DE AltName: Full=Ribonucleotide reductase large subunit {ECO:0000255|HAMAP-Rule:MF_04026}; GN Name=RIR1 {ECO:0000255|HAMAP-Rule:MF_04026}; OS Equine herpesvirus 4 (strain 1942) (EHV-4) (Equine rhinopneumonitis virus). OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes; OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Varicellovirus; OC Varicellovirus equidalpha4; Equid alphaherpesvirus 4. OX NCBI_TaxID=10333; OH NCBI_TaxID=9796; Equus caballus (Horse). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8206376; DOI=10.1016/0378-1119(94)90099-x; RA Riggio M.P., Onions D.E.; RT "Sequences of the ribonucleotide reductase-encoding genes of equine RT herpesvirus 4."; RL Gene 143:217-222(1994). RN [2] RP REVIEW. RX PubMed=18990579; DOI=10.1016/j.tibs.2008.09.008; RA Lembo D., Brune W.; RT "Tinkering with a viral ribonucleotide reductase."; RL Trends Biochem. Sci. 34:25-32(2009). CC -!- FUNCTION: Ribonucleoside-diphosphate reductase holoenzyme provides the CC precursors necessary for viral DNA synthesis. Allows virus growth in CC non-dividing cells, as well as reactivation from latency in infected CC hosts. Catalyzes the biosynthesis of deoxyribonucleotides from the CC corresponding ribonucleotides. {ECO:0000255|HAMAP-Rule:MF_04026}. 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:0000255|HAMAP-Rule:MF_04026}; 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. CC {ECO:0000255|HAMAP-Rule:MF_04026}. CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large CC chain family. {ECO:0000255|HAMAP-Rule:MF_04026}. 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; X75354; CAA53100.1; -; Genomic_DNA. DR SMR; P50642; -. DR IntAct; P50642; 2. DR MINT; P50642; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-UniRule. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule. DR GO; GO:0019046; P:release from viral latency; IEA:UniProtKB-KW. DR Gene3D; 3.20.70.20; -; 1. DR HAMAP; MF_04026; HSV_RIR1; 1. DR InterPro; IPR034717; HSV_RIR1. DR InterPro; IPR013346; NrdE_NrdA_C. DR InterPro; IPR000788; RNR_lg_C. DR InterPro; IPR013509; RNR_lsu_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 PROSITE; PS00089; RIBORED_LARGE; 1. PE 3: Inferred from homology; KW ATP-binding; Disulfide bond; DNA replication; Early protein; KW Nucleotide-binding; Oxidoreductase; Viral latency; KW Viral reactivation from latency. FT CHAIN 1..789 FT /note="Ribonucleoside-diphosphate reductase large subunit" FT /id="PRO_0000187242" FT ACT_SITE 435 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" FT ACT_SITE 437 FT /note="Cysteine radical intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" FT ACT_SITE 439 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" FT BINDING 207 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" FT BINDING 222..223 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" FT BINDING 253 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" FT BINDING 435..439 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" FT BINDING 620..624 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" FT SITE 223 FT /note="Important for hydrogen atom transfer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" FT SITE 452 FT /note="Important for hydrogen atom transfer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" FT SITE 764 FT /note="Important for electron transfer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" FT SITE 765 FT /note="Important for electron transfer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" FT SITE 784 FT /note="Interacts with thioredoxin/glutaredoxin" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" FT SITE 787 FT /note="Interacts with thioredoxin/glutaredoxin" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" FT DISULFID 223..452 FT /note="Redox-active" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" SQ SEQUENCE 789 AA; 88047 MW; 7CD9A24F3147988B CRC64; MALDFLSTDC PLGIVSDIIS NVNTIKEYGY SSELSTTLAP RPSREQVLEY ITRVVDKLKP LCRVDERLYI ACGELVHLRI KARNTDLKYW LKSSEIDLSD VVEQAILEHI DFVQKTLNSF ETSEYRDLCS LGLQSALKYE EMYLAKMRGG RLESMGQFFL RLATTATHYT MEQPAMARVL VSGEVGWTYI FRAFFTALAG QVVIPATPIM LFGGRDCGSM ASCYLLNPRV TDMNSAIPAL MEEVGPILCN RGGIGLSLQR FNTPPTEGCS RGVMALLKLL DSMTMAINSD GERPTGVCVY FEPWHADIRA ILNMRGMLAR DETVRCDNIF ACMWTPDLFF DRYQRYVDGE SGIMWTLFDD TASHLCHMYG NDFTREYERL ERCGFGIDAI PIQDMAFIIV RSAVMTGSPF LMFKDACNRH YHFDMRQRGA IMGSNLCTEI IQHADETQNG VCNLASINLP KCLALPPPNI AGVPYFDFAA LGRAAATATI FVNAMMCAST YPTVKSQKGV EENRSLGLGI QGLHTTFLML DLDMASPEAH QLNKQIAERL LLNSMKASAT LCKLGMQPFK GFEDSKYSRG ELPFDAYPNV TLTNRNAWRR LRTDIKQYGL YNSQFVAYMP TVSSSQVTES SEGFSPVYTN LFSKVTATGE VLRPNVLLMR TIRSIFPQEC ARLQALSTLE AAKWSVVGAF GDLPVGHPLS KFKTAFEYDQ TMLINMCADR AAFVDQSQSM SLFITEPADG KLPASRIMNL LVHAYKRGLK TGMYYCKIKK ATNNGVFVGG DLVCTSCSL //