RIR1_HHV8P
ID RIR1_HHV8P Reviewed; 792 AA.
AC Q2HR67;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=ORF61;
OS Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS sarcoma-associated herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=868565;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10400794; DOI=10.1128/jvi.73.8.6953-6963.1999;
RA Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.;
RT "Identification of a spliced gene from Kaposi's sarcoma-associated
RT herpesvirus encoding a protein with similarities to latent membrane
RT proteins 1 and 2A of Epstein-Barr virus.";
RL J. Virol. 73:6953-6963(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL J. Gen. Virol. 87:1781-1804(2006).
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; AF148805; ABD28916.1; -; Genomic_DNA.
DR RefSeq; YP_001129418.1; NC_009333.1.
DR SMR; Q2HR67; -.
DR PRIDE; Q2HR67; -.
DR DNASU; 4961490; -.
DR GeneID; 4961490; -.
DR KEGG; vg:4961490; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000000942; 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; IPR008926; RNR_R1-su_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 SUPFAM; SSF48168; SSF48168; 1.
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 Host-virus interaction; Nucleotide-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..792
FT /note="Ribonucleoside-diphosphate reductase large subunit"
FT /id="PRO_0000423783"
FT REGION 758..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 415
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT ACT_SITE 417
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT ACT_SITE 419
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 215..216
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 415..419
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 606..610
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 216
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 431
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 737
FT /note="Important for electron transfer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 738
FT /note="Important for electron transfer"
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 SITE 791
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT DISULFID 216..431
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
SQ SEQUENCE 792 AA; 88806 MW; F6F23551FE8A90DC CRC64;
MSVRTFCQVH LGAVPPERRG SQVSAGQLSD FDMCAQSLID FLKVRVGWDV RANAMAGRLW
HQIMEARCPA TLKQYLGIFR GVLGHRVESF IQKNIDALED MLCAYRRSKA YEDTLNCGYL
SAVRLYDTYV LRTMGTEPVY ESVAQMFMRV SVFVACQCLE HECLYWLARD LIEDAKSVSE
MAIVEYVFGY LAAQHVCCAT PILRSAGVEG GQLASCFILQ PSMMNEPGTL DALYHDMSPL
LASKSGVGLD VTSFSHQKNI ASCLKLVDAQ VHYFNDNNIR PVGASAYMEL WHSQICDFLN
AKLPENPDRC HSLFQGVCIP TLFFRMYEKD PSKLWYLFDP ATAPNLIKLY GAAFDNEYER
LVRAGKYVSC MPLKSMMFTL IHTIIKTGSP YVLLKEALNE HHWTDTQGMA INCSNLCAEI
VQLPGRNTSV CNLANICLPK CLRTVESARV GTTDANRPFF CFEALGDAVR VAVLVINACI
LGGSHPTPGV ERGQKERSMG IGVQGLADVF AELGYGYLDA ESAELDKNIF QSMYYTAVET
SHNLVLEGQG VPFHGWEVSN FAKGRFHWQT WEGEDASFVP RHRWDALGKS IAEHGIFNSQ
FLAVMPTAGT SQVTGYAESV YPFFANISSK VTNKEEVLRP NVTFFKKVLP DDLRVVRQYG
GDVSTFPKHH RERYRVFLTA FDYCPFKLLD RARARAPFVD QSQSMSFFLK EDRVRNASYL
RDLLLHGYRL GLKTLMYYCR VQKQSSLTAL QCLADPGSPP HSGMKQDGAW LPGPKNPEEE
SCAADPECLV CQ
