RIR1_EHV4
ID RIR1_EHV4 Reviewed; 789 AA.
AC P50642;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 77.
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};
OS Equine herpesvirus 4 (strain 1942) (EHV-4) (Equine rhinopneumonitis virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10333;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8206376; DOI=10.1016/0378-1119(94)90099-x;
RA Riggio M.P., Onions D.E.;
RT "Sequences of the ribonucleotide reductase-encoding genes of equine
RT herpesvirus 4.";
RL Gene 143:217-222(1994).
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; X75354; CAA53100.1; -; Genomic_DNA.
DR SMR; P50642; -.
DR IntAct; P50642; 2.
DR MINT; P50642; -.
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 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; Viral latency;
KW Viral reactivation from latency.
FT CHAIN 1..789
FT /note="Ribonucleoside-diphosphate reductase large subunit"
FT /id="PRO_0000187242"
FT ACT_SITE 435
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT ACT_SITE 437
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT ACT_SITE 439
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 222..223
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 435..439
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 620..624
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 223
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 452
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 764
FT /note="Important for electron 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 784
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 787
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT DISULFID 223..452
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
SQ SEQUENCE 789 AA; 88047 MW; 7CD9A24F3147988B CRC64;
MALDFLSTDC PLGIVSDIIS NVNTIKEYGY SSELSTTLAP RPSREQVLEY ITRVVDKLKP
LCRVDERLYI ACGELVHLRI KARNTDLKYW LKSSEIDLSD VVEQAILEHI DFVQKTLNSF
ETSEYRDLCS LGLQSALKYE EMYLAKMRGG RLESMGQFFL RLATTATHYT MEQPAMARVL
VSGEVGWTYI FRAFFTALAG QVVIPATPIM LFGGRDCGSM ASCYLLNPRV TDMNSAIPAL
MEEVGPILCN RGGIGLSLQR FNTPPTEGCS RGVMALLKLL DSMTMAINSD GERPTGVCVY
FEPWHADIRA ILNMRGMLAR DETVRCDNIF ACMWTPDLFF DRYQRYVDGE SGIMWTLFDD
TASHLCHMYG NDFTREYERL ERCGFGIDAI PIQDMAFIIV RSAVMTGSPF LMFKDACNRH
YHFDMRQRGA IMGSNLCTEI IQHADETQNG VCNLASINLP KCLALPPPNI AGVPYFDFAA
LGRAAATATI FVNAMMCAST YPTVKSQKGV EENRSLGLGI QGLHTTFLML DLDMASPEAH
QLNKQIAERL LLNSMKASAT LCKLGMQPFK GFEDSKYSRG ELPFDAYPNV TLTNRNAWRR
LRTDIKQYGL YNSQFVAYMP TVSSSQVTES SEGFSPVYTN LFSKVTATGE VLRPNVLLMR
TIRSIFPQEC ARLQALSTLE AAKWSVVGAF GDLPVGHPLS KFKTAFEYDQ TMLINMCADR
AAFVDQSQSM SLFITEPADG KLPASRIMNL LVHAYKRGLK TGMYYCKIKK ATNNGVFVGG
DLVCTSCSL
