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RIR2_HHV2H
ID   RIR2_HHV2H              Reviewed;         337 AA.
AC   P69521; P03174;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 90.
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}; ORFNames=UL40;
OS   Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10315;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9499055; DOI=10.1128/jvi.72.3.2010-2021.1998;
RA   Dolan A., Jamieson F.E., Cunningham C., Barnett B.C., McGeoch D.J.;
RT   "The genome sequence of herpes simplex virus type 2.";
RL   J. Virol. 72:2010-2021(1998).
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;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_04028};
CC   -!- PATHWAY: Genetic information processing; DNA replication.
CC       {ECO:0000255|HAMAP-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}.
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DR   EMBL; Z86099; CAB06726.1; -; Genomic_DNA.
DR   RefSeq; YP_009137192.1; NC_001798.2.
DR   SMR; P69521; -.
DR   PRIDE; P69521; -.
DR   DNASU; 1487327; -.
DR   GeneID; 1487327; -.
DR   KEGG; vg:1487327; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000001874; Genome.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of 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; -; 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; PTHR23409; 1.
DR   Pfam; PF00268; Ribonuc_red_sm; 1.
DR   SUPFAM; SSF47240; SSF47240; 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..337
FT                   /note="Ribonucleoside-diphosphate reductase small subunit"
FT                   /id="PRO_0000190506"
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"
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
 
 
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