ID RIR2_SUHVK Reviewed; 303 AA. AC P50645; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 24-JAN-2024, entry version 103. 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=RR2, UL40; OS Suid herpesvirus 1 (strain Kaplan) (SuHV-1) (Pseudorabies virus (strain OS Kaplan)). OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes; OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Varicellovirus; OC Varicellovirus suidalpha1; Suid alphaherpesvirus 1. OX NCBI_TaxID=33703; OH NCBI_TaxID=9823; Sus scrofa (Pig). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8086454; DOI=10.1016/0167-4781(94)90259-3; RA Kaliman A., Boldogkoi Z., Fodor I.; RT "Large and small subunits of the Aujeszky's disease virus ribonucleotide RT reductase: nucleotide sequence and putative structure."; RL Biochim. Biophys. Acta 1219:151-156(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; X72087; CAA50977.1; -; Genomic_DNA. DR EMBL; X80797; CAA56776.1; -; Genomic_DNA. DR PIR; S47526; S47526. DR RefSeq; YP_068343.1; NC_006151.1. DR SMR; P50645; -. DR GeneID; 2952536; -. DR KEGG; vg:2952536; -. 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..303 FT /note="Ribonucleoside-diphosphate reductase small subunit" FT /id="PRO_0000190511" FT TRANSMEM 147..167 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT ACT_SITE 97 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 60 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 90 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 90 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 93 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 153 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 187 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" FT BINDING 190 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028" SQ SEQUENCE 303 AA; 34375 MW; 560F19FDE6C7A9C3 CRC64; MEYFYTSQCP DMDHLRSLSV ANRWLETDLP LGDDAKDVAA LSEPELEFYR FLFAFLSAAD DLVNVNLGSL SELFTQKDIL HYYIEQECIE VVHSRVYSAI QLMLFRGDAA ARERYVRAAL RDEAIRRKVE WLDSRVAECA SVAEKYLLMI LIEGIFFASS FASISYLRTH NLFVVTCQSN DFISRDEAIH TSASCCIYNN YLGDAPRPDE ARIHQLFAEA VEIECEFLRA RAPRDSLLLD LPAIISYVRY SADRLLQAIG ASPLFGAPAP AADFPMALMV AEKHTNFFER RSTNYTGTVV NDL //