ID   RIR1_PSHV1              Reviewed;         811 AA.
AC   Q6UDJ2;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 83.
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=UL39;
OS   Psittacid herpesvirus 1 (isolate Amazon parrot/-/97-0001/1997) (PsHV-1)
OS   (Pacheco's disease virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Iltovirus;
OC   Iltovirus psittacidalpha1; Psittacid alphaherpesvirus 1.
OX   NCBI_TaxID=670426;
OH   NCBI_TaxID=152276; Amazona oratrix (yellow-headed parrot).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16873243; DOI=10.1128/jvi.00134-06;
RA   Thureen D.R., Keeler C.L. Jr.;
RT   "Psittacid herpesvirus 1 and infectious laryngotracheitis virus:
RT   Comparative genome sequence analysis of two avian alphaherpesviruses.";
RL   J. Virol. 80:7863-7872(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   -!- 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; AY372243; AAQ73718.1; -; Genomic_DNA.
DR   RefSeq; NP_944412.1; NC_005264.1.
DR   SMR; Q6UDJ2; -.
DR   GeneID; 2656977; -.
DR   KEGG; vg:2656977; -.
DR   Proteomes; UP000006840; Segment.
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   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; Disulfide bond; DNA replication; Early protein;
KW   Host-virus interaction; Nucleotide-binding; Oxidoreductase;
KW   Reference proteome; Viral latency; Viral reactivation from latency.
FT   CHAIN           1..811
FT                   /note="Ribonucleoside-diphosphate reductase large subunit"
FT                   /id="PRO_0000406807"
FT   ACT_SITE        450
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   ACT_SITE        452
FT                   /note="Cysteine radical intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   ACT_SITE        454
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   BINDING         231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   BINDING         246..247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   BINDING         277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   BINDING         450..454
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   BINDING         636..640
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   SITE            247
FT                   /note="Important for hydrogen atom transfer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   SITE            467
FT                   /note="Important for hydrogen atom transfer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   SITE            781
FT                   /note="Important for electron transfer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   SITE            782
FT                   /note="Important for electron transfer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   SITE            807
FT                   /note="Interacts with thioredoxin/glutaredoxin"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   SITE            810
FT                   /note="Interacts with thioredoxin/glutaredoxin"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT   DISULFID        247..467
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
SQ   SEQUENCE   811 AA;  90420 MW;  92166F6616E4BE9C CRC64;
     MSSATSLVPP AAPDMREHEL GECAAFYAAE TPQRLFENLL HLENALKARG YDTDSAGAPA
     LGPTTLTMEA IADRITLIIN RFKAAVRLDL ELYRLLAELV HIRIRTKTVS MQAWIELRGL
     SRECAEFILE RKNFVCELME RFGEVYPTLS RVGLQSARKF ESMYLGKLKN GRLESVGQFF
     LRIAAEAARG VANNDAFAAA VFRDGTRAPD ANTVFCLFFM ALCRQEIVPP TPVMLFAGTE
     SRSYASCFLL DVRGRHTRDV LTSIAEEIIP VMHSHGGIGL YMDCDSNWDD NSSGMMLALK
     ALDSIIAASN AVSARPSGLC VYVEPWHRDI MKILRCRGVL AGNEETRCDN TFFALWMPDL
     FMKRFEANGT WTLFDGRAAH LSDLYGEEFE KEYELLERKN VGIATYPARD VMFALIKSAV
     STGTPFVMFK HAVNRNYFFD MAGRAMKCSN LCTEIVHMTD DESVGVCNLT SLNLAAFVTR
     RNALPGTPPI GTFDYSSFRD ACAVATVFIN ALMSLSNLPI KRATTGNERL RSIGIGVQGF
     HTACLLQGFG LDSVEACRFN GKLFEALALT TFQTSCRICE LGMNPFRGFS ESKYAKGWLH
     MDGWPARHLY FDGWDRLREN IKAYGLYNCQ LVALMPTASS SQLTEVSEGI HPVFGNIFSK
     ITTTGEDIQL NVALMETIEC LYPNKAERRD ILERLHKNKW STRGAFGAAL PSQHPLTKFD
     TAFEADQEHL LRLSADRAPF VDHSQSTTLY VVEEDDGAVR ASRVAHLLTT AFKYGLKTGM
     YYCKVRKATD NGVFLGTDTC RRDDPTCLAC Q
//