RIR1_HCMVM
ID RIR1_HCMVM Reviewed; 906 AA.
AC Q6SW87; D2K3L2;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 23-FEB-2022, entry version 67.
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=UL45;
OS Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=295027;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15105547; DOI=10.1099/vir.0.79888-0;
RA Dolan A., Cunningham C., Hector R.D., Hassan-Walker A.F., Lee L.,
RA Addison C., Dargan D.J., McGeoch D.J., Gatherer D., Emery V.C.,
RA Griffiths P.D., Sinzger C., McSharry B.P., Wilkinson G.W.G., Davison A.J.;
RT "Genetic content of wild-type human cytomegalovirus.";
RL J. Gen. Virol. 85:1301-1312(2004).
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; AY446894; AAR31609.1; -; Genomic_DNA.
DR RefSeq; YP_081503.1; NC_006273.2.
DR SMR; Q6SW87; -.
DR BioGRID; 1677997; 3.
DR PRIDE; Q6SW87; -.
DR DNASU; 3077444; -.
DR GeneID; 3077444; -.
DR KEGG; vg:3077444; -.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Proteomes; UP000000938; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019033; C:viral tegument; TAS:Reactome.
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..906
FT /note="Ribonucleoside-diphosphate reductase large subunit-
FT like protein"
FT /id="PRO_0000418312"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 906 AA; 101698 MW; B99A2500AB30F063 CRC64;
MNPADADEEQ RVSSVPAHRC RPGRIPSRSA ETETEESSAE VAADTIGGDD SELEEGPLPG
GDKEASAGNT NVSSGVACVA GFTSGGGVVS WRPESPSPDG TPSVLSLTRD SGPAVPSRGG
RVSSGLSTFN PAGATRMELD SVEEEDDFGA SLCKVSPPIQ AMRMLMGKKC HCHGYWGKFR
FCGVQEPARE LPSDRNALWR EMDTVSRHSA GLGSFRLFQL IMRHGPCLIR HSPRCDLLLG
RFYFKANWAR ESRTPLCYAS ELCDESVRRF VLRHMEDLPK LAEETARFVE LAGCWGLYAA
ILCLDKVCRQ LHGQDESPGG VFLRIAVALT AAIENSRHSR IYRFHLDARF EGEVLESVLK
RCRDGQLSLS TFTMSTVGFD RVPQYDFLIS ADPFSRDASW AAMCKWMSTL SCGVSVSVNV
TRLNADVNSV IRCLGGYCDL IREKEVHRPV VRVFVDMWDV AAIRVINFIL KESTSELTGV
CYAFNVPSVL MKRYRAREQR YSLFGRPVSR RLSDLGQESA FEKEYSRCEQ SCPKVVVNTD
DFLKKMLLCA LKGRASVVFV HHVVKYSIMA DSVCLPPCLS PDMASCHFGE CDMPVQRLTV
NVARCVFARS DEQKLHLPDV VLGNTRRYFD LSVLRELVTE AVVWGNARLD ALMSASEWWV
ESALEKLRPL HIGVAGLHTA LMRLGFTYFA SWDLIERIFE HMYFAAVRAS VDLCKSGLPR
CEWFERTIYQ EGKFIFELYR LPRLSIASAR WEALRADMLE FGLRNCQFLA VGPDDEVAHL
WGVTPSVWAS RGTVFEEETV WSLCPPNREC YFPTVVRRPL RVPVVNYAWL EQHQEEGKAT
QCLFQAAPAI QNDVEMAAVN LSVFVDQCVA LVFYYDSGMT PDVLLARMLK WYHWRFKVGV
YKYCAS