ID RIR2_HHV23 Reviewed; 337 AA. AC P69520; P03174; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 24-JAN-2024, entry version 87. 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 Human herpesvirus 2 (strain 333) (HHV-2) (Human herpes simplex virus 2). OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes; OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus; OC Simplexvirus humanalpha2; Human herpesvirus 2. OX NCBI_TaxID=10313; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6321759; DOI=10.1128/jvi.49.3.724-730.1984; RA Galloway D.A., Swain M.A.; RT "Organization of the left-hand end of the herpes simplex virus type 2 BglII RT N fragment."; RL J. Virol. 49:724-730(1984). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6315408; DOI=10.1002/j.1460-2075.1983.tb01684.x; RA McLauchlan J., Clements J.B.; RT "DNA sequence homology between two co-linear loci on the HSV genome which RT have different transforming abilities."; RL EMBO J. 2:1953-1961(1983). RN [3] 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; M12700; AAA45807.1; -; Genomic_DNA. DR EMBL; X00048; CAA24930.1; -; Genomic_DNA. DR PIR; A00528; WMBE32. DR PIR; A00529; WMBEB2. DR RefSeq; YP_009137192.1; NC_001798.2. DR SMR; P69520; -. DR DNASU; 1487327; -. DR GeneID; 1487327; -. DR KEGG; vg:1487327; -. 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; Transmembrane; Transmembrane helix; Viral latency; KW Viral reactivation from latency. FT CHAIN 1..337 FT /note="Ribonucleoside-diphosphate reductase small subunit" FT /id="PRO_0000190505" FT TRANSMEM 177..197 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT REGION 1..22 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 128 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 91 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 121 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 121 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 124 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 184 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 218 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 221 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT CONFLICT 173 FT /note="I -> V (in Ref. 2; CAA24930)" FT /evidence="ECO:0000305" FT CONFLICT 235 FT /note="G -> D (in Ref. 2; CAA24930)" FT /evidence="ECO:0000305" SQ SEQUENCE 337 AA; 37626 MW; 1E27E96599EE2120 CRC64; MDPAVSPAST DPLDTHASGA GAAPIPVCPT PERYFYTSQC PDINHLRSLS ILNRWLETEL VFVGDEEDVS KLSEGELGFY RFLFAFLSAA DDLVTENLGG LSGLFEQKDI LHYYVEQECI EVVHSRVYNI IQLVLFHNND QARRAYVART INHPAIRVKV DWLEARVREC DSIPEKFILM ILIEGVFFAA SFAAIAYLRT NNLLRVTCQS NDLISRDEAV HTTASCYIYN NYLGGHAKPE AARVYRLFRE AVDIEIGFIR SQAPTDSSIL SPGALAAIEN YVRFSADRLL GLIHMQPLYS APAPDASFPL SLMSTDKHTN FFECRSTSYA GAVVNDL //