ID D3YPA3_HHV1 Unreviewed; 1137 AA.
AC D3YPA3;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
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:ADD60038.1};
GN Synonyms=RIR1 {ECO:0000256|HAMAP-Rule:MF_04026};
OS Human herpesvirus 1 (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus;
OC Simplexvirus humanalpha1.
OX NCBI_TaxID=10298 {ECO:0000313|EMBL:ADD60038.1, ECO:0000313|Proteomes:UP000121444};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ADD60038.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F {ECO:0000313|EMBL:ADD60038.1};
RX PubMed=20219902; DOI=10.1128/JVI.00312-10;
RA Szpara M.L., Parsons L., Enquist L.W.;
RT "Sequence variability in clinical and laboratory isolates of herpes simplex
RT virus 1 reveals new mutations.";
RL J. Virol. 84:5303-5313(2010).
RN [2] {ECO:0000313|EMBL:AJE60270.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=F {ECO:0000313|EMBL:AJE60270.1};
RX PubMed=25827418;
RA Parsons L.R., Tafuri Y.R., Shreve J.T., Bowen C.D., Shipley M.M.,
RA Enquist L.W., Szpara M.L.;
RT "Rapid genome assembly and comparison decode intrastrain variation in human
RT alphaherpesviruses.";
RL MBio 6:e02213-14(2015).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GU734771; ADD60038.1; -; Genomic_DNA.
DR EMBL; KM222725; AJE60270.1; -; Genomic_DNA.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000121444; 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: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 946..968
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 791
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT ACT_SITE 793
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT ACT_SITE 795
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT BINDING 566
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT BINDING 581..582
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT BINDING 612
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT BINDING 791..795
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT BINDING 968..972
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT SITE 582
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT SITE 808
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT SITE 1111
FT /note="Important for electron transfer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT SITE 1112
FT /note="Important for electron transfer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT SITE 1132
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT SITE 1135
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
FT DISULFID 582..808
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04026"
SQ SEQUENCE 1137 AA; 123941 MW; 0392F8294ED73428 CRC64;
MASRPAASSP VEARAPVGGQ EAGGPSAATQ GEAAGAPLAH GHHVYCQRVN GVMVLSDKTP
GSASYRISDS NFVQCGSNCT MIIDGDVVRG RPQDPGAAAS PAPFVAVTNI GAGSDGGTAV
VAFGGTPRRS AGTSTGTQTA DVPAEALGGP PPPPRFTLGG GCCSCRDTRR RSAVFGGEGD
PVGPAEFVSD DRSSDSDSDD SEDTDSETLS HASSDVSGGA TYDDALDSDS SSDDSLQIDG
PVCRPWSNDT APLDVCPGTP GPGADAGGPS AVDPHAPTTG AGAGLAADPA VARDDAEGLS
DPRPRLGTGT AYPVPLELTP ENAEAVARFL GDAVNREPAL MLEYFCRCAR EETKRVPPRT
FCSPPRLTED DFGLLNYALV EMQRLCLDVP PVPPNAYMPY YLREYVTRLV NGFKPLVSRS
ARLYRILGVL VHLRIRTREA SFEEWLRSKE VALDFGLTER LREHEAQLVI LAQALDHYDC
LIHSTPHTLV ERGLQSALKY EEFYLKRFGG HYMESVFQMY TRIAGFLACR ATRGMRHIAL
GREGSWWEMF KFFFHRLYDH QIVPSTPAML NLGTRNYYTS SCYLVNPQAT TNKATLRAIT
SNVSAILARN GGIGLCVQAF NDSGPGTASV MPALKVLDSL VAAHNKESAR PTGACVYLEP
WHTDVRAVLR MKGVLAGEEA QRCDNIFSAL WMPDLFFKRL IRHLDGEKNV TWTLFDRDTS
MSLADFHGEE FEKLYQHLEV MGFGEQIPIQ ELAYGIVRSA ATTGSPFVMF KDAVNRHYIY
DTQGAAIAGS NLCTEIVHPA SKRSSGVCNL GSVNLARCVS RQTFDFGRLR DAVQACVLMV
NIMIDSTLQP TPQCTRGNDN LRSMGIGMQG LHTACLKLGL DLESAEFQDL NKHIAEVMLL
SAMKTSNALC VRGARPFNHF KRSMYRAGRF HWERFPDARP RYEGEWEMLR QSMMKHGLRN
SQFVALMPTA ASAQISDVSE GFAPLFTNLF SKVTRDGETL RPNTLLLKEL ERTFSGKRLL
EVMDSLDAKQ WSVAQALPCL EPTHPLRRFK TAFDYDQKLL IDLCADRAPY VDHSQSMTLY
VTEKADGTLP ASTLVRLLVH AYKRGLKTGM YYCKVRKATN SGVFGGDDNI VCTSCAL
//
