ID   RIR1_BHV1C              Reviewed;         787 AA.
AC   P50646;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, entry version 95.
DE   RecName: Full=Ribonucleoside-diphosphate reductase large subunit {ECO:0000255|HAMAP-Rule:MF_04026};
DE            Short=R1 {ECO:0000255|HAMAP-Rule:MF_04026};
DE            EC=1.17.4.1 {ECO:0000255|HAMAP-Rule:MF_04026};
DE   AltName: Full=Ribonucleotide reductase large subunit {ECO:0000255|HAMAP-Rule:MF_04026};
GN   Name=RIR1 {ECO:0000255|HAMAP-Rule:MF_04026}; OrderedLocusNames=UL39;
OS   Bovine herpesvirus 1.1 (strain Cooper) (BoHV-1) (Infectious bovine
OS   rhinotracheitis virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Varicellovirus;
OC   Varicellovirus bovinealpha1.
OX   NCBI_TaxID=10323;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7571445; DOI=10.1006/viro.1995.1533;
RA   Simard C., Langlois I., Styger D., Vogt B., Vlcek C., Chalifour A.,
RA   Trudel M., Schwyzer M.;
RT   "Sequence analysis of the UL39, UL38, and UL37 homologues of bovine
RT   herpesvirus 1 and expression studies of UL40 and UL39, the subunits of
RT   ribonucleotide reductase.";
RL   Virology 212:734-740(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9010999; DOI=10.1016/s0378-1135(96)01235-7;
RA   Schwyzer M., Styger D., Vogt B., Lowery D.E., Simard C., LaBoissiere S.,
RA   Misra V., Vlcek C., Paces V.;
RT   "Gene contents in a 31-kb segment at the left genome end of bovine
RT   herpesvirus-1.";
RL   Vet. Microbiol. 53:67-77(1996).
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_04026}.
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_04026};
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_04026}.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC       chain family. {ECO:0000255|HAMAP-Rule:MF_04026}.
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DR   EMBL; Z54206; CAA90929.1; -; Genomic_DNA.
DR   EMBL; Z49078; CAA88900.1; -; Genomic_DNA.
DR   EMBL; AJ004801; CAA06094.1; -; Genomic_DNA.
DR   RefSeq; NP_045319.1; NC_001847.1.
DR   SMR; P50646; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.70.20; -; 1.
DR   HAMAP; MF_04026; HSV_RIR1; 1.
DR   InterPro; IPR034717; HSV_RIR1.
DR   InterPro; IPR013346; NrdE_NrdA_C.
DR   InterPro; IPR000788; RNR_lg_C.
DR   InterPro; IPR013509; RNR_lsu_N.
DR   InterPro; IPR039718; Rrm1.
DR   NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR   PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR   PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR   Pfam; PF02867; Ribonuc_red_lgC; 1.
DR   Pfam; PF00317; Ribonuc_red_lgN; 1.
DR   PRINTS; PR01183; RIBORDTASEM1.
DR   SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR   PROSITE; PS00089; RIBORED_LARGE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Disulfide bond; DNA replication; Early protein;
KW   Nucleotide-binding; Oxidoreductase; Viral latency;
KW   Viral reactivation from latency.
FT   CHAIN           1..787
FT                   /note="Ribonucleoside-diphosphate reductase large subunit"
FT                   /id="PRO_0000187240"
FT   ACT_SITE        436
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   ACT_SITE        438
FT                   /note="Cysteine radical intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   ACT_SITE        440
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   BINDING         209
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   BINDING         224..225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   BINDING         255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   BINDING         436..440
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   BINDING         618..622
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   SITE            225
FT                   /note="Important for hydrogen atom transfer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   SITE            453
FT                   /note="Important for hydrogen atom transfer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   SITE            762
FT                   /note="Important for electron transfer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   SITE            763
FT                   /note="Important for electron transfer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   SITE            782
FT                   /note="Interacts with thioredoxin/glutaredoxin"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   SITE            785
FT                   /note="Interacts with thioredoxin/glutaredoxin"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   DISULFID        225..453
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
SQ   SEQUENCE   787 AA;  86010 MW;  8DB0F6327862333E CRC64;
     MASDAFMQTA CPADAAEQLE AEHAEWAQLG CGAVPPPPAA ASRPSRAAVA AYVGEVVDRM
     RAQSRADERV YVKCGQLVHL RVRARSVPLD DWLTSAELAL VSEVAEPVRA NRAFVEVSLR
     YFELTEYATL RALGLQSALK YEEMYLAKLE GGAIESMGQF FVRIAATAAT WTMREPAFGR
     ALVGEGATWC AVFNAYLTAL YRQLVVPATP IMLFAGRARG SLASCYLLNP QVSSSTEAVE
     AITTEVARIL LNRGGIGISF QSFDRAVSRD CKRGIMGALK LLDSMAMAIN SDSERPTGIC
     VYLEPWHCDV RAVLNMRGLL ARDESTRCDN LFSCLWVPDL LFDRYLAHLE GREGVVWTLF
     DDRASHLSRL HGPAFTAEYE RLEREGLGVE TVPVQDLAFL IVRSIVMTGS PFVMFKDACN
     RHYHMDTAGD ALTGSNLCTE IVQRASPDAH GVCNLASVNL PRCVREGEGG ALAFDFAALS
     TAAATAAIFV NAMMLGGQYP TEKAARGVAR HRSLGIGFQG LHTLLLELGM DMLSPAARRL
     NVEIAERLLL AVMATSATLC EYGCAPFEDF ARSKFARGLM PFDGYEGVVL SLPRAWARLR
     EKVARHGLYN AQFVALMPTV SSSQVTEGSE GFSPVFTNMF SKVTMSGELL RPNLPLMRAL
     RKHFTREASR LGAVRALDRE QWSVAAALGD LAPGHPLAKF KTAFEYDQER LIDLCADRAP
     FVDQSQSMSL FVTEPMDGKV PASQIMNLLV YAYKKGLKTG LYYCKIRKAT NNGVFTGGDL
     VCSGCHL
//