RIR1_EHV1B
ID RIR1_EHV1B Reviewed; 790 AA.
AC P28846;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=21;
OS Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=31520;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=1318606; DOI=10.1016/0042-6822(92)90706-u;
RA Telford E.A.R., Watson M.S., McBride K., Davison A.J.;
RT "The DNA sequence of equine herpesvirus-1.";
RL Virology 189:304-316(1992).
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_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; AY665713; AAT67278.1; -; Genomic_DNA.
DR PIR; D36797; WMBEA2.
DR RefSeq; YP_053066.1; NC_001491.2.
DR SMR; P28846; -.
DR PRIDE; P28846; -.
DR GeneID; 1487540; -.
DR KEGG; vg:1487540; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000001189; 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:0019046; P:release from viral latency; IEA:UniProtKB-KW.
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; Reference proteome; Viral latency;
KW Viral reactivation from latency.
FT CHAIN 1..790
FT /note="Ribonucleoside-diphosphate reductase large subunit"
FT /id="PRO_0000187241"
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 208
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 223..224
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 254
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 621..625
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 224
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 765
FT /note="Important for electron transfer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 766
FT /note="Important for electron transfer"
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 SITE 788
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT DISULFID 224..453
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
SQ SEQUENCE 790 AA; 88399 MW; D8A21677716F5844 CRC64;
MALNFLQSDC PLAIIQDVIS RVDAISDYGY ANELSTTLPP RPSRSQVLEY ITRVVDTLKP
RCRVDERLYV VCGELVHLRI RTRNVEDLKY WLNSTEIALN EIVEKDILDH LDFIQRTLHA
FESSEYRELC ALGLQSALKY EEMYLAKMRG GRIESMGQFF LRLATTATHY TMEEPAMARV
LVSGEVGWTY IFKAYFTALA GQVLIPATPI MLFGGRDCGS LASCYLLNPR VTDMNSAMLA
LMEEAGPILC NRGGIGLSLQ RFNTPPKEGC SRGVMALLKL IDSMTMAINS DGERPTGVCV
YFEPWHADIR AILNMRGMLA RDETVRCDNI FACMWTPDLF FDRYQRYLDG ESGVMWTLFD
DTASHLCHMY GKEFEEEYER LEQCGFGVDS IPIQDMAFII VRSAVMTGSP FLMFKDACNK
HYHFDLRRKG AIMGSNLCTE IIQHADETQN GVCNLASINL PKCLAIPPPH TAGVPYFDFA
ALGRAAATAT IFVNSMMRAG TYPTVKSQRG VDENRSLGLG IQGLHTAFLM LDLDMASPEA
RQLNKQIAER LLLNSMKASA TLCRLGMKPF KGFEDSKYSL GELPFDSYPG VTLANRNAWR
RLRTEIKQHG LYNSQFVAYM PTVSSSQVTE SSEGFSPVYT NLFSKVTATG EVLRPNLLLM
RTIRSIFPRE CARLQALSTL EMAQWSVVGA FGDLPVGHPL SKFKTAFEYD QRTLIDMCAD
RAPFVDQSQS MSLFITEPAD GKLPASKIMS LLVHAYKRGL KTGMYYCKIK KATNNGVFVG
GDLVCTSCSL
