RIR1_BHV1C
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 03-AUG-2022, entry version 88.
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; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
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 -!- PATHWAY: Genetic information processing; DNA replication.
CC {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 PRIDE; P50646; -.
DR GeneID; 1487390; -.
DR KEGG; vg:1487390; -.
DR UniPathway; UPA00326; -.
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 HAMAP; MF_04026; HSV_RIR1; 1.
DR InterPro; IPR034717; HSV_RIR1.
DR InterPro; IPR013346; NrdE_NrdA.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR039718; Rrm1.
DR PANTHER; PTHR11573; PTHR11573; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR TIGRFAMs; TIGR02506; NrdE_NrdA; 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
