ID RIR1_EHV1B Reviewed; 790 AA. AC P28846; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 24-JAN-2024, entry version 114. 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}; OrderedLocusNames=21; OS Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus). OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes; OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Varicellovirus; OC Varicellovirus equidalpha1; Equid alphaherpesvirus 1. OX NCBI_TaxID=31520; OH NCBI_TaxID=9796; Equus caballus (Horse). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=1318606; DOI=10.1016/0042-6822(92)90706-u; RA Telford E.A.R., Watson M.S., McBride K., Davison A.J.; RT "The DNA sequence of equine herpesvirus-1."; RL Virology 189:304-316(1992). 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; AY665713; AAT67278.1; -; Genomic_DNA. DR PIR; D36797; WMBEA2. DR RefSeq; YP_053066.1; NC_001491.2. DR SMR; P28846; -. DR GeneID; 1487540; -. DR KEGG; vg:1487540; -. DR Proteomes; UP000001189; Segment. 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; Reference proteome; Viral latency; KW Viral reactivation from latency. FT CHAIN 1..790 FT /note="Ribonucleoside-diphosphate reductase large subunit" FT /id="PRO_0000187241" FT ACT_SITE 436 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" FT ACT_SITE 438 FT /note="Cysteine radical intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" FT ACT_SITE 440 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" FT BINDING 208 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" FT BINDING 223..224 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" FT BINDING 254 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" FT BINDING 436..440 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" FT BINDING 621..625 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" FT SITE 224 FT /note="Important for hydrogen atom transfer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" FT SITE 453 FT /note="Important for hydrogen atom 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 766 FT /note="Important for electron transfer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" FT SITE 785 FT /note="Interacts with thioredoxin/glutaredoxin" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" FT SITE 788 FT /note="Interacts with thioredoxin/glutaredoxin" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" FT DISULFID 224..453 FT /note="Redox-active" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026" SQ SEQUENCE 790 AA; 88399 MW; D8A21677716F5844 CRC64; MALNFLQSDC PLAIIQDVIS RVDAISDYGY ANELSTTLPP RPSRSQVLEY ITRVVDTLKP RCRVDERLYV VCGELVHLRI RTRNVEDLKY WLNSTEIALN EIVEKDILDH LDFIQRTLHA FESSEYRELC ALGLQSALKY EEMYLAKMRG GRIESMGQFF LRLATTATHY TMEEPAMARV LVSGEVGWTY IFKAYFTALA GQVLIPATPI MLFGGRDCGS LASCYLLNPR VTDMNSAMLA LMEEAGPILC NRGGIGLSLQ RFNTPPKEGC SRGVMALLKL IDSMTMAINS DGERPTGVCV YFEPWHADIR AILNMRGMLA RDETVRCDNI FACMWTPDLF FDRYQRYLDG ESGVMWTLFD DTASHLCHMY GKEFEEEYER LEQCGFGVDS IPIQDMAFII VRSAVMTGSP FLMFKDACNK HYHFDLRRKG AIMGSNLCTE IIQHADETQN GVCNLASINL PKCLAIPPPH TAGVPYFDFA ALGRAAATAT IFVNSMMRAG TYPTVKSQRG VDENRSLGLG IQGLHTAFLM LDLDMASPEA RQLNKQIAER LLLNSMKASA TLCRLGMKPF KGFEDSKYSL GELPFDSYPG VTLANRNAWR RLRTEIKQHG LYNSQFVAYM PTVSSSQVTE SSEGFSPVYT NLFSKVTATG EVLRPNLLLM RTIRSIFPRE CARLQALSTL EMAQWSVVGA FGDLPVGHPL SKFKTAFEYD QRTLIDMCAD RAPFVDQSQS MSLFITEPAD GKLPASKIMS LLVHAYKRGL KTGMYYCKIK KATNNGVFVG GDLVCTSCSL //