ID   RIR1_HHV6Z              Reviewed;         804 AA.
AC   Q9QJ39;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 91.
DE   RecName: Full=Ribonucleoside-diphosphate reductase large subunit-like protein {ECO:0000255|HAMAP-Rule:MF_04027};
GN   Name=RIR1 {ECO:0000255|HAMAP-Rule:MF_04027}; Synonyms=U28;
OS   Human herpesvirus 6B (strain Z29) (HHV-6 variant B) (Human B lymphotropic
OS   virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Betaherpesvirinae; Roseolovirus;
OC   Roseolovirus humanbeta6b; Human herpesvirus 6B.
OX   NCBI_TaxID=36351;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10482553; DOI=10.1128/jvi.73.10.8040-8052.1999;
RA   Dominguez G., Dambaugh T.R., Stamey F.R., Dewhurst S., Inoue N.,
RA   Pellett P.E.;
RT   "Human herpesvirus 6B genome sequence: coding content and comparison with
RT   human herpesvirus 6A.";
RL   J. Virol. 73:8040-8052(1999).
CC   -!- FUNCTION: Does not possess a ribonucleotide reductase activity.
CC       Betaherpesviruses probably use another strategy to expand the dNTP pool
CC       in a quiescent host cell. {ECO:0000255|HAMAP-Rule:MF_04027}.
CC   -!- SUBUNIT: The genome of human herpesvirus-6 does not code for a
CC       ribonucleotide reductase small subunit.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04027}. Host
CC       cytoplasm {ECO:0000255|HAMAP-Rule:MF_04027}.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC       chain family. {ECO:0000255|HAMAP-Rule:MF_04027}.
CC   -!- CAUTION: Lacks the conserved sequence Asn-x-Cys-x-Glu essential for
CC       ribonucleotide reductase activity. {ECO:0000255|HAMAP-Rule:MF_04027}.
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DR   EMBL; AF157706; AAD49642.1; -; Genomic_DNA.
DR   RefSeq; NP_050209.1; NC_000898.1.
DR   SMR; Q9QJ39; -.
DR   DNASU; 1497030; -.
DR   GeneID; 1497030; -.
DR   KEGG; vg:1497030; -.
DR   Proteomes; UP000006930; Segment.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0044423; C:virion component; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.70.20; -; 1.
DR   HAMAP; MF_04027; HSV_RIR1_betahv; 1.
DR   InterPro; IPR034716; HSV_RIR1_betahv.
DR   InterPro; IPR013346; NrdE_NrdA_C.
DR   InterPro; IPR000788; RNR_lg_C.
DR   InterPro; IPR039718; Rrm1.
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   PRINTS; PR01183; RIBORDTASEM1.
DR   SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR   PROSITE; PS00089; RIBORED_LARGE; 1.
PE   3: Inferred from homology;
KW   Host cytoplasm; Late protein; Reference proteome; Virion.
FT   CHAIN           1..804
FT                   /note="Ribonucleoside-diphosphate reductase large subunit-
FT                   like protein"
FT                   /id="PRO_0000408414"
SQ   SEQUENCE   804 AA;  93283 MW;  39C240FDA8F19E1D CRC64;
     MKRKERRINK DFGYNRKCVC HYEASQKRFC YSQYSCASVL YERVRDIAKI MDRLDSGLDA
     WCLRDAIISV LRATHCVPRV DRMLGRWYLK TSIFYDFCPD DLILSCPNVI MPNVLNFVKK
     YRDFIRSVLY KVSVSWKNQY MPGVLGASRF LEEISNSLNG VEESIPCIYL RMCATLTEIV
     LRNGYLREIY QENPYVIFEE LAFSLFTQKW VLPFSCMTNL GLVEKANSTV FDVAIYNTCL
     YSLADFITVN GEHLFPALLN GSNISMNVTR YQQEAKNIFE ILLSQIQVVE RDTDKTVQLT
     VYVEVWHVSA LTWLDLYQVL PETSRVTFCL IIPGIFMDRY ELKRAQWSLF HKNIAFELGK
     CDEVTFSTKY LEFERTTDHA KITMASFVEK ICRCLKRGRM GLIFRKNVYQ YSMIPHVPLY
     CGGDFLDVLP VRDGINTCLR MLLNVVHFLG DEVSDELTEE IDFVRLQCKF FMFNELRRVV
     RKMVLVANAV IDYAVDNKDF LREGIVDGRS LGICITGLHS VFMTVGLSYA HPDACRLYRM
     MCEHIYYTCV RTSVDCCMKG AEPCNLFDRS KYALGMLYFD QFDNVECTLP EELWTTLRKD
     VLMHGVRNIH FTAGTAMQKE FDIINSSESF WPMEDNKILR RSNIKVVIGK DGLNDVTSVY
     SSELKSLYIP VYNNLLLNRF NKHQQYLKTV GYRVLNVDTN LFTDKELDDL AVFKDGFSYP
     LNDLIEMYKS GLPFLDQGQA NVFYFNDTVS LKHLLPLLYK TGFKVAMYKV LCSSEMYKHL
     DLSNPLPLIG KCSDGVVMHV KNIL
//