ID RIR2_BHV1C Reviewed; 314 AA. AC Q01319; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 24-JAN-2024, entry version 114. 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=UL40; OS Bovine herpesvirus 1.1 (strain Cooper) (BoHV-1) (Infectious bovine OS rhinotracheitis virus). OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes; OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Varicellovirus; OC Varicellovirus bovinealpha1. OX NCBI_TaxID=10323; OH NCBI_TaxID=9913; Bos taurus (Bovine). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Cooper / 34; RX PubMed=1325701; DOI=10.1016/0042-6822(92)90907-7; RA Simard C., Bastien N., Trudel M.; RT "Sequencing and 5'- and 3'-end transcript mapping of the gene encoding the RT small subunit of ribonucleotide reductase from bovine herpesvirus type-1."; RL Virology 190:689-701(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7571445; DOI=10.1006/viro.1995.1533; RA Simard C., Langlois I., Styger D., Vogt B., Vlcek C., Chalifour A., RA Trudel M., Schwyzer M.; RT "Sequence analysis of the UL39, UL38, and UL37 homologues of bovine RT herpesvirus 1 and expression studies of UL40 and UL39, the subunits of RT ribonucleotide reductase."; RL Virology 212:734-740(1995). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9010999; DOI=10.1016/s0378-1135(96)01235-7; RA Schwyzer M., Styger D., Vogt B., Lowery D.E., Simard C., LaBoissiere S., RA Misra V., Vlcek C., Paces V.; RT "Gene contents in a 31-kb segment at the left genome end of bovine RT herpesvirus-1."; RL Vet. Microbiol. 53:67-77(1996). RN [4] 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; Z54206; CAA90928.1; -; Genomic_DNA. DR EMBL; M84470; AAA46063.1; -; Genomic_DNA. DR EMBL; Z49078; CAA88899.1; -; Genomic_DNA. DR EMBL; AJ004801; CAA06093.1; -; Genomic_DNA. DR PIR; A43367; WMBEB4. DR RefSeq; NP_045318.1; NC_001847.1. DR SMR; Q01319; -. 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 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; Transmembrane; Transmembrane helix; Viral latency; KW Viral reactivation from latency. FT CHAIN 1..314 FT /note="Ribonucleoside-diphosphate reductase small subunit" FT /id="PRO_0000190507" FT TRANSMEM 160..180 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT ACT_SITE 110 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 73 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 103 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 103 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 106 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 166 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 200 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 203 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" SQ SEQUENCE 314 AA; 35251 MW; 257FB0E91111632E CRC64; MAEAADAATL TRKYKYFYET ECPDLDHLRS LSVANRWLET EFPLADDAKD VARLSGAELE FYRFLFAFLS AADDLVNVNL GDLSELFTQK DILHYYIEQE SIEVVHSRVY SAIQLLLFRN DAVARAGYVE GALGDPAVRR KVDWLERRVA AAESVAEKYV LMILIEGIFF SSSFAAIAYL RTHNLFVVTC QTNDLISRDE AVHTAASCCI FDNYLGGERP PPARIYELFR EAWKLSASLF GCAPRGSHIL DVEAISAYVE YSADRLLAAI QLPPLFGTPP PGTDFPLALM TAEKHTNFFE RRSTNYTGTV INDL //