ID RIR2_EHV1B Reviewed; 321 AA. AC P28847; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 24-JAN-2024, entry version 126. DE RecName: Full=Ribonucleoside-diphosphate reductase small subunit {ECO:0000255|HAMAP-Rule:MF_04028}; DE EC=1.17.4.1 {ECO:0000255|HAMAP-Rule:MF_04028}; DE AltName: Full=Ribonucleotide reductase small subunit {ECO:0000255|HAMAP-Rule:MF_04028}; GN Name=RIR2 {ECO:0000255|HAMAP-Rule:MF_04028}; Synonyms=20; 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_04028}. 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_04028}; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|HAMAP- CC Rule:MF_04028}; 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_04028}. CC -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000255|HAMAP-Rule:MF_04028}; CC Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04028}. CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small CC chain family. {ECO:0000255|HAMAP-Rule:MF_04028}. 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; AAT67277.1; -; Genomic_DNA. DR PIR; C36797; WMBEA1. DR RefSeq; YP_053065.1; NC_001491.2. DR SMR; P28847; -. DR GeneID; 1487524; -. DR KEGG; vg:1487524; -. DR Proteomes; UP000001189; Segment. DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-UniRule. DR GO; GO:0009186; P:deoxyribonucleoside diphosphate metabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule. DR GO; GO:0019046; P:release from viral latency; IEA:UniProtKB-KW. DR CDD; cd01049; RNRR2; 1. DR Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 1. DR HAMAP; MF_04028; HSV_RIR2; 1. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR034715; HSV_RIR2. DR InterPro; IPR012348; RNR-like. DR InterPro; IPR033909; RNR_small. DR InterPro; IPR030475; RNR_small_AS. DR InterPro; IPR000358; RNR_small_fam. DR PANTHER; PTHR23409; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN; 1. DR PANTHER; PTHR23409:SF18; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2; 1. DR Pfam; PF00268; Ribonuc_red_sm; 1. DR SUPFAM; SSF47240; Ferritin-like; 1. DR PROSITE; PS00368; RIBORED_SMALL; 1. PE 3: Inferred from homology; KW DNA replication; Host membrane; Iron; Membrane; Metal-binding; KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix; KW Viral latency; Viral reactivation from latency. FT CHAIN 1..321 FT /note="Ribonucleoside-diphosphate reductase small subunit" FT /id="PRO_0000190508" FT TRANSMEM 165..185 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT ACT_SITE 115 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 78 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 108 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 108 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 111 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 171 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 205 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 208 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" SQ SEQUENCE 321 AA; 36017 MW; 81E1FF57B12B84A4 CRC64; MSIENSKEAA LTAELSLAGA FFYTPECPDI EHLRSLSVAN RWLDTDLPIS DDLKDVAKLT PAEREFYRFL FAFLSAADDL VNLNLGDLSA LFTQKDILHY YIEQESIEVT HSRVYSAIQL MLFGNDAAAR ARYVASIIGD AAIGRKVAWL QAKVRECGSV AEKYILMILI EGLFFASSFA SIAYLRTHNL FVVTCQSNDL ISRDEAIHTR ASCCIYNNYL GGFEKPEPKR IYELFSEAVN IECEFLLSHA PQYSHLLDIG AIISYVRYSA DRLLGEIGLS PLFNAPKPSP SFPLAFMTVE KHTNFFERRS TAYSGTLIND L //