RIR1_EHV2
ID RIR1_EHV2 Reviewed; 799 AA.
AC Q66663;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=61;
OS Equine herpesvirus 2 (strain 86/87) (EHV-2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Percavirus.
OX NCBI_TaxID=82831;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=7783207; DOI=10.1006/jmbi.1995.0314;
RA Telford E.A.R., Watson M.S., Aird H.C., Perry J., Davison A.J.;
RT "The DNA sequence of equine herpesvirus 2.";
RL J. Mol. Biol. 249:520-528(1995).
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; U20824; AAC13849.1; -; Genomic_DNA.
DR PIR; S55656; S55656.
DR RefSeq; NP_042658.1; NC_001650.2.
DR SMR; Q66663; -.
DR GeneID; 1461039; -.
DR KEGG; vg:1461039; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000007083; Genome.
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 GO; GO:0016032; P:viral process; 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.
PE 3: Inferred from homology;
KW ATP-binding; Disulfide bond; DNA replication; Early protein;
KW Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..799
FT /note="Ribonucleoside-diphosphate reductase large subunit"
FT /id="PRO_0000405987"
FT REGION 765..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 408
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT ACT_SITE 410
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT ACT_SITE 412
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 207..208
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 408..412
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 612..616
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 208
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 424
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 743
FT /note="Important for electron transfer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 744
FT /note="Important for electron transfer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 795
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 798
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT DISULFID 208..424
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
SQ SEQUENCE 799 AA; 88581 MW; A88D2540357934F0 CRC64;
MAAAHLGMPV PVYMAEREED LALRKLIDTL KISAGWDLEA NRMAGRLYHF VMGRRAPVDT
RAYVTTFGDK LEKGVHRFLW DNARDIDDLC KDFQNGPEYE RLISRGMLSA KRMYDTYVLR
TEEGGGEGAV YESALQMYAR MAAFFTCQCF AYPSLRKTVS EVEGGSGRME SGLDFFAYFF
KILASQLVSC ATPVMRSAGL RQSYLASCFI MNPDMSTEDK TLSAVFRDLS PLLCSKSGVG
MNLTNFSSGG KNVQSCLRLI NSQVEFCNDK NLRPVSVAAY MELWHEQIEE FLAAKLPENP
ERCQSIFQGV CVPGLFFRLY EQNPDSQWHL FSPKVGGHLA GLYGDKFDEE YARLVRHGLY
SSSLPAKSLM FALISAIIKT GSPYILSKDA INRHHWFETQ GNAISYANLC AEVVQQPHEF
TSTCNLANVC LPACLRARGE GEGAGAAGEG EGADRLSPLT PDLEFCFDTL RAAVRAAVYM
INASILGGVC PTPGVRVMQA ERSAGIGVQG LADVFAKLGR GYMDAESALL DARIFEVMYY
QAVRASNQLV TVGGAPPHAN WKNSKLSRGE FHWESWGVQY DSLFIERQLW EELRESVTKH
GTFNSQFIAL MPTAGTSQLT GLSESFYPFY ANVSSKVSNK EEVMKPNITF LERVSPSDVP
LLKYHGGDVS KLPPPLAAKY RNFLTAFDYS PEDQIRRAAA RSPFVDQSQS FSFFLKEANV
KSASYVKNLI LLGHGLGLKT IMYYCRIQKQ TSLTALECLQ CTESPDSGDG VGGYKGGDEE
PRSPEHAQCE SPDRCLSCQ
