RIR1_HCMVA
ID RIR1_HCMVA Reviewed; 906 AA.
AC P16782; Q7M6P0;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 101.
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 AD169) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=10360;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2161319; DOI=10.1007/978-3-642-74980-3_6;
RA Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R.,
RA Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A.,
RA Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.;
RT "Analysis of the protein-coding content of the sequence of human
RT cytomegalovirus strain AD169.";
RL Curr. Top. Microbiol. Immunol. 154:125-169(1990).
RN [2]
RP GENOME REANNOTATION.
RX PubMed=12533697; DOI=10.1099/vir.0.18606-0;
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RT "The human cytomegalovirus genome revisited: comparison with the chimpanzee
RT cytomegalovirus genome.";
RL J. Gen. Virol. 84:17-28(2003).
RN [3]
RP ERRATUM OF PUBMED:12533697.
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RL J. Gen. Virol. 84:1053-1053(2003).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND PROBABLE ABSENCE OF RIBONUCLEOTIDE
RP REDUCTASE ACTIVITY.
RX PubMed=14645917; DOI=10.1099/vir.0.19452-0;
RA Patrone M., Percivalle E., Secchi M., Fiorina L., Pedrali-Noy G., Zoppe M.,
RA Baldanti F., Hahn G., Koszinowski U.H., Milanesi G., Gallina A.;
RT "The human cytomegalovirus UL45 gene product is a late, virion-associated
RT protein and influences virus growth at low multiplicities of infection.";
RL J. Gen. Virol. 84:3359-3370(2003).
RN [5]
RP IDENTIFICATION.
RX PubMed=15452216; DOI=10.1128/jvi.78.20.10960-10966.2004;
RA Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
RA Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
RA Shenk T., Smith R.D., Nelson J.A.;
RT "Identification of proteins in human cytomegalovirus (HCMV) particles: the
RT HCMV proteome.";
RL J. Virol. 78:10960-10966(2004).
RN [6]
RP ERRATUM OF PUBMED:15452216.
RA Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
RA Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
RA Shenk T., Smith R.D., Nelson J.A.;
RL J. Virol. 78:13395-13395(2004).
RN [7]
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 ECO:0000269|PubMed:14645917}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04027,
CC ECO:0000269|PubMed:14645917}. Host cytoplasm {ECO:0000255|HAMAP-
CC 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}.
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; X17403; CAA35404.1; -; Genomic_DNA.
DR EMBL; BK000394; DAA00148.1; -; Genomic_DNA.
DR PIR; S09808; WMBEV3.
DR SMR; P16782; -.
DR Proteomes; UP000008991; Genome.
DR Proteomes; UP000008992; 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..906
FT /note="Ribonucleoside-diphosphate reductase large subunit-
FT like protein"
FT /id="PRO_0000187235"
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; 101668 MW; EE05E44B2DDEA6F9 CRC64;
MNPADADEEQ RVSSVPAHRC RPGRIPSRSA ETETEESSAE VAADTIGGDD SELEEGPLPG
GDKEASAGNT NVSSGVACVA GFTSGGGVVS WRPESPSPDG TPSVLSLTRD SGPAVPSRGG
RVSSGLSTFN PAGATRMELD SVEEEDDFGA SLCKVSPPIQ ATRMLMGKKC 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
