ID RIR2_EHV4 Reviewed; 320 AA. AC P50644; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 24-JAN-2024, entry version 104. 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}; 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]. RC STRAIN=1942; 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_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; X75354; CAA53101.1; -; Genomic_DNA. DR SMR; P50644; -. DR IntAct; P50644; 2. DR MINT; P50644; -. 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; Transmembrane; Transmembrane helix; Viral latency; KW Viral reactivation from latency. FT CHAIN 1..320 FT /note="Ribonucleoside-diphosphate reductase small subunit" FT /id="PRO_0000190509" FT TRANSMEM 164..184 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT ACT_SITE 114 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 77 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 107 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 107 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 110 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 170 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 204 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 207 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" SQ SEQUENCE 320 AA; 36172 MW; 7AF3511937730202 CRC64; MALENSKKTD FADELLINAY FYTPECPDIE HLRLLSVANR WLDTDLPISD DLKDVAKLAP AEREFYRFLF AFLSAADDLV NLNLGDLSAL FTQKDILHYY IEQESIEVTH SRVYSAIQLM LFGNDATARA RYVASVVKDV AIDLKVSWLQ AKVRECKSVA EKYILMILIE GVFFASSFAS IAYLRTHNLF VVTCQSNDLI SRDEAIHTNA SCCIYNNYLG GFEKPAPTRI YALFSEAVNI ECEFLLSHAP KSSHLLDIEA IICYVRYSAD RLLGEIGLSP LFNAPKPPPS FPLAFMTVEK HTNFFERRST AYSGTLINDL //