ID Q89942_9ALPH Unreviewed; 820 AA.
AC Q89942;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Ribonucleoside-diphosphate reductase large subunit {ECO:0000256|HAMAP-Rule:MF_04026};
DE Short=R1 {ECO:0000256|HAMAP-Rule:MF_04026};
DE EC=1.17.4.1 {ECO:0000256|HAMAP-Rule:MF_04026};
DE AltName: Full=Ribonucleotide reductase large subunit {ECO:0000256|HAMAP-Rule:MF_04026};
GN Name=UL39 {ECO:0000313|EMBL:AAA80556.1};
GN Synonyms=RIR1 {ECO:0000256|HAMAP-Rule:MF_04026};
OS Gallid alphaherpesvirus 2.
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Mardivirus;
OC Mardivirus gallidalpha2.
OX NCBI_TaxID=10390 {ECO:0000313|EMBL:AAA80556.1};
RN [1] {ECO:0000313|EMBL:AAA80556.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=7645252; DOI=10.1006/viro.1995.1430;
RA Darteil R., Bublot M., Laplace E., Bouquet J.F., Audonnet J.C., Riviere M.;
RT "Herpesvirus of turkey recombinant viruses expressing infectious bursal
RT disease virus (IBDV) VP2 immunogen induce protection against an IBDV
RT virulent challenge in chickens.";
RL Virology 211:481-490(1995).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}.
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:0000256|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:0000256|HAMAP-Rule:MF_04026,
CC ECO:0000256|RuleBase:RU003410};
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:0000256|HAMAP-Rule:MF_04026}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406, ECO:0000256|HAMAP-
CC Rule:MF_04026, ECO:0000256|RuleBase:RU003410}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_04026}.
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DR EMBL; L40429; AAA80556.1; -; Genomic_DNA.
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:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0016032; P:viral process; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_04026};
KW Deoxyribonucleotide synthesis {ECO:0000256|RuleBase:RU003410};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW Rule:MF_04026}; DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Early protein {ECO:0000256|ARBA:ARBA00022518, ECO:0000256|HAMAP-
KW Rule:MF_04026};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_04026};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_04026,
KW ECO:0000256|RuleBase:RU003410}.
FT DOMAIN 627..649
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
FT ACT_SITE 468
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT ACT_SITE 470
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT ACT_SITE 472
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT BINDING 262..263
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT BINDING 468..472
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT BINDING 649..653
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT SITE 263
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT SITE 485
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT SITE 794
FT /note="Important for electron transfer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT SITE 795
FT /note="Important for electron transfer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT SITE 815
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT SITE 818
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
SQ SEQUENCE 820 AA; 91483 MW; A1494208EC702CF9 CRC64;
MFDESDGYSG PGKIHARGIE APGTGQIHVV DASTASRKLN DMQMSSSVAT ELYSIERQLL
SMDYLSDSDL YMIDVRKYPE TIPSISDMRA HITRLVNKMK PICRFDERLY SVCGELVHLR
IASSETTFDA WLTSKKLNLK ADVLDNLRRY RAHIEMDMLR FYGNIYPQLK RLGLQSALKY
EEYLVELEGG KKESLCQFFI RLAAAAATEA LHRKPLIASL TNGSANWRTA FTSFFLALAH
QLFVPSTPCM LFLGREGYST ASCYLMDPRT TTTQDTIKVI TNDVVPHLLA RGGIGISLQH
VNQKSGLMHV LKLIDSLIVA TNVNESRPTG VCVYLEPWHS DIMSALTMRG MMAAEESRRC
DNVFLALWAC DLLFKRYLRY VNGEKNVMWT LFDSRASILS KLYGDKFEVE YERLEKEGIG
VAQIPIRDMM FAIIKSAAST GSPFILFKDA CNRHYITDTQ GDAIAGSNLC TEIIQKTNES
TNGVCTLASI NLARCVRRVN VNVNSILMPL GMPFRLATVF TNAIMDGSDV PTVKSQSGRD
RNRSIGIGVQ GFHTAMLSLG LDLEDGAVRA LNKQIFELML LEAMTVSCEF CERGLPPFPD
FSDSYYAQGR LHFDGWDSVE LTAPEEWGVL RGRIMSSGLY NAQFIALMPT AASAQVTEVS
EGFAPLFSNM FSKVTSAGEL LRPNSQLMRD VRQIYPDNEQ RRLSAITALE STAWCVKEAL
GDRPECTRLL KYKTAFEYDQ SLLIDLCADR APFVDQSQSM TLFVTETADG TLLASRVMNL
LLHAYKAGLK TGMYYCKIRK ATNTGIFSGD GELTCSSCVL
//
