RIR2_EBVG
ID RIR2_EBVG Reviewed; 302 AA.
AC P0C701; Q777G0;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 02-JUN-2021, entry version 62.
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=BaRF1;
OS Epstein-Barr virus (strain GD1) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=10376;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16306603; DOI=10.1128/jvi.79.24.15323-15330.2005;
RA Zeng M.-S., Li D.-J., Liu Q.-L., Song L.-B., Li M.-Z., Zhang R.-H.,
RA Yu X.-J., Wang H.-M., Ernberg I., Zeng Y.-X.;
RT "Genomic sequence analysis of Epstein-Barr virus strain GD1 from a
RT nasopharyngeal carcinoma patient.";
RL J. Virol. 79:15323-15330(2005).
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 -!- INTERACTION:
CC P0C701; Q66542: BNRF1; NbExp=2; IntAct=EBI-2621366, EBI-2621061;
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; AY961628; AAY41106.1; -; Genomic_DNA.
DR RefSeq; YP_401656.1; NC_007605.1.
DR SMR; P0C701; -.
DR IntAct; P0C701; 5.
DR DNASU; 3783683; -.
DR GeneID; 3783683; -.
DR KEGG; vg:3783683; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000007641; 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 1: Evidence at protein level;
KW DNA replication; Host membrane; Iron; Membrane; Metal-binding;
KW Oxidoreductase; Transmembrane; Transmembrane helix; Viral latency;
KW Viral reactivation from latency.
FT CHAIN 1..302
FT /note="Ribonucleoside-diphosphate reductase small subunit"
FT /id="PRO_0000375968"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04028"
SQ SEQUENCE 302 AA; 34359 MW; 473BF0BDFB7F0637 CRC64;
MSKLLYVRDH EGFACLTVET HRNRWFAAHI VLTKDCGCLK LLNERDLEFY KFLFTFLAMA
EKLVNFNIDE LVTSFESHDI DHYYTEQKAM ENVHGETYAN ILNMLFDGDR AAMNAYAEAI
MADEALQAKI SWLRDKVAAA VTLPEKILVF LLIEGIFFIS SFYSIALLRV RGLMPGICLA
NNYISRDELL HTRAASLLYN SMTAKADRPR ATWIQELFRT AVEVETAFIE ARGEGVTLVD
VRAIKQFLEA TADRILGDIG QAPLYGTPPP KDCPLTYMTS IKQTNFFEQE SSDYTMLVVD
DL
