RIR1_SUHVK
ID RIR1_SUHVK Reviewed; 835 AA.
AC P50643;
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}; OrderedLocusNames=RR1, UL39;
OS Suid herpesvirus 1 (strain Kaplan) (SuHV-1) (Pseudorabies virus (strain
OS Kaplan)).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=33703;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8086454; DOI=10.1016/0167-4781(94)90259-3;
RA Kaliman A., Boldogkoi Z., Fodor I.;
RT "Large and small subunits of the Aujeszky's disease virus ribonucleotide
RT reductase: nucleotide sequence and putative structure.";
RL Biochim. Biophys. Acta 1219:151-156(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; X72087; CAA50976.1; -; Genomic_DNA.
DR EMBL; X80797; CAA56775.1; -; Genomic_DNA.
DR PIR; S47345; S40140.
DR SMR; P50643; -.
DR PRIDE; P50643; -.
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..835
FT /note="Ribonucleoside-diphosphate reductase large subunit"
FT /id="PRO_0000187244"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 489
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT ACT_SITE 491
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT ACT_SITE 493
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 277..278
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 489..493
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 666..670
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 278
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 506
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 810
FT /note="Important for electron transfer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 811
FT /note="Important for electron transfer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 830
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 833
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT DISULFID 278..506
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
SQ SEQUENCE 835 AA; 91060 MW; 20D4AF7366667EBA CRC64;
MPPRAPRPAG AVSPPFPPLA GPPLKARAPR ARDSPLTSPC RAHAAMASVV APAASSSAAA
PGADAFLDAA CPEDVARALA AELEALRALG HDVGAPAPGA SRREAALFIT RAVDGLKAFS
RVDERVYVAC GKLVHLRVRS READLDAWLA SPELALIPAV AAAVRRHRAR VEAALRWFWR
EAYPALYARG LQSALKYEEM YLARLEHGRC EAMDQFFVRL AAAAATATRR PMALVLCGSD
AWPEVFDAYF RALATQAIVP ATPLMLFAGR ARGSLASCYL LNPLPRTTEE AVRAITDEVA
PILLRRGGVG LSLQSFNRTP SGDCTRGIMA VLKALDSMTA AINSDSERPT GVCVYVEPWH
ADVRAVLNMR GMLAADESLR CDNIFSCLWT PDLFFQRYQR HLDGERAVKW TLFDDRASHL
ASLHGPDFAR EYERLERLGL GVESLPIQDM AFLIVRSAVM TGSPFLMMKD ACNRHFHTDT
RGAALATSNL CTEIVQRATP GENGVCNLAS VNLPACLAGG AFDFAALRRA ARVAAVFVNA
MMRIGNYPTG ASVEGVRRSR SLGIGLQGLH TTVLALDMDM ADPAARRLNA AIAEELLYGV
MDASVELCER GLRPFDGFEH SRYARGVMPF DAYERVSLRE PMRWDALRVR IAEHGVYNAQ
FVALMPTVSS SQVTESSEGF SPTFTNMFSK VTISGELLRP NLPLMETLRR LFPRECARRD
AVARLERAQW SVAAAFGELP AGHPLAKFKT AFEYDQELLI DMCADRAPFV DHSQSMSLFL
TEPADGKLHA SRVMGLLMRA YNLGLKTGMY YCKIRKATNN GVFTGGDLVC TSCHL
