RIR1_HHV7J
ID RIR1_HHV7J Reviewed; 806 AA.
AC P50641;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
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 7 (strain JI) (HHV-7) (Human T lymphotropic virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=57278;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8709220; DOI=10.1128/jvi.70.9.5975-5989.1996;
RA Nicholas J.;
RT "Determination and analysis of the complete nucleotide sequence of human
RT herpesvirus.";
RL J. Virol. 70:5975-5989(1996).
RN [2]
RP LACK OF RIBONUCLEOTIDE REDUCTASE ACTIVITY.
RX PubMed=10573165; DOI=10.1099/0022-1317-80-10-2713;
RA Sun Y., Conner J.;
RT "The U28 ORF of human herpesvirus-7 does not encode a functional
RT ribonucleotide reductase R1 subunit.";
RL J. Gen. Virol. 80:2713-2718(1999).
RN [3]
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: 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 -!- 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; U43400; AAC54690.1; -; Genomic_DNA.
DR PIR; T41930; T41930.
DR RefSeq; YP_073768.1; NC_001716.2.
DR SMR; P50641; -.
DR PRIDE; P50641; -.
DR DNASU; 3289486; -.
DR GeneID; 3289486; -.
DR KEGG; vg:3289486; -.
DR Proteomes; UP000009246; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044423; C:virion component; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR HAMAP; MF_04027; HSV_RIR1_betahv; 1.
DR InterPro; IPR034716; HSV_RIR1_betahv.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR039718; Rrm1.
DR PANTHER; PTHR11573; PTHR11573; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Host cytoplasm; Late protein; Reference proteome; Virion.
FT CHAIN 1..806
FT /note="Ribonucleoside-diphosphate reductase large subunit-
FT like protein"
FT /id="PRO_0000187239"
SQ SEQUENCE 806 AA; 93070 MW; 4BA516084FCCDCC0 CRC64;
MDPNNKVSIN KNMGLLRKCL CHDEYNKKRF CYSRFHHKTL LYKQLYEISK ILRRLNSGLD
MWCLRDAIIS ALGAMHDAPH VDRLLGQFYL KTNSASEFDS ISLILESENI LQKELIEFVR
DSKVELEKIL QAAIHVWRAK FSPGVLAASR FLDEISNSFN GIEENIPTIF LRISVTLASQ
IKKIEYLQKS FVSHKCPLVE EILILLYKRV CMLPFPCMSN LGLVSEKKSV FDTVFHNVSN
FSLEDFLDIN SGFFLPAMLN GSYVSVNLTR YHYEAESLME LLLSQLQIVE KDTNKTTGLT
IYLEIWHLSL LMWLDFCEIL PTTVQVKFCL ILPEIFMERL KTENSYWSVF HKALAINLGL
YDESDFTSKY LECERTAEHA RIKTETLLDN ICRCLRRGQM GFIFRKNIHK YSMLPQIASY
CLGNSMDVIP FEYGLNTAFR IALNLSYFVE NVSEEQKSHT NIDMFHYRDK IFNLKKMRKT
VTELVLIGNA VIDYALENRD FLMDGIVNAR SLAICVTGLH SALMSMNLPF NSQLGCQLYR
IVCENIYYSS VRTSMNCCKK GAEPCSFFQR SKYAQGILHC DLYDNVEYTL PNVLWTNLRS
DIKKYGLRNL TFVSGSAMSK EFDLLNCSQS FCPIEGNKIL KRSSIKVLHP NPVFHSDLSV
YSTELQTLYI PVYNGLFLNR FKNHLEYLSS VNYDVSKVNK NLFSEEEMQE MTIFLNAFDY
SVNEMLNMYV GALPFTDHGQ ANVFFINKTE NMRDILVCLY QNGFKTGIYQ AVYKNQKCDG
VNPSKKFDLL SGFSDGVVMS TMHVFQ