ID RIR2_ALHV1 Reviewed; 305 AA. AC O36410; DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 24-JAN-2024, entry version 105. 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=60; OS Alcelaphine herpesvirus 1 (strain C500) (AlHV-1) (Malignant catarrhal fever OS virus). OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes; OC Herpesvirales; Orthoherpesviridae; Gammaherpesvirinae; Macavirus; OC Macavirus alcelaphinegamma1. OX NCBI_TaxID=654901; OH NCBI_TaxID=9927; Connochaetes taurinus (Blue wildebeest). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=9261371; DOI=10.1128/jvi.71.9.6517-6525.1997; RA Ensser A., Pflanz R., Fleckenstein B.; RT "Primary structure of the alcelaphine herpesvirus 1 genome."; RL J. Virol. 71:6517-6525(1997). 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; AF005370; AAC58107.1; -; Genomic_DNA. DR PIR; T03155; T03155. DR RefSeq; NP_065559.1; NC_002531.1. DR SMR; O36410; -. DR GeneID; 911784; -. DR KEGG; vg:911784; -. DR Proteomes; UP000000941; Segment. DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-UniRule. 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..305 FT /note="Ribonucleoside-diphosphate reductase small subunit" FT /id="PRO_0000405697" FT TRANSMEM 150..170 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT ACT_SITE 101 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 64 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 94 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 94 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 97 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 157 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 191 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 194 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" SQ SEQUENCE 305 AA; 35524 MW; 6431D1DD2F129473 CRC64; MDFIKKYLYV CDHPGFFELT QETFQNRWFP AQINLSVDVK CLSLMSEADV NFYKYLFTFL GMAETLVNFN IDELLVDFEC HDIKHYYCEQ MAMECVHGKV YFNILNMLFK NNLAATWEFA EAVLKDEALQ KKLEWLESKI KMAKTKAEKV LIFYLIEGVF FISSFYCIGL LRVKGVMPGV CMANDYISRD ELLHTRAAAL LYNTMIPKEE RPSSEWVVSL FKEAVEIECA FIEAKTKQVT FVSMDDIRAF LEATADRLLN SIELPRYYKS DPPQSCPLTY TGCIKNVSFF ERESTEYSSF IINDL //