ID A8E1H1_MUHVK Unreviewed; 1174 AA. AC A8E1H1; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 27-MAR-2024, entry version 58. DE RecName: Full=Ribonucleoside-diphosphate reductase large subunit-like protein {ECO:0000256|HAMAP-Rule:MF_04027}; GN Name=M45 {ECO:0000313|EMBL:CAP08092.1}; GN Synonyms=RIR1 {ECO:0000256|HAMAP-Rule:MF_04027}; OS Murid herpesvirus 1 (strain K181) (MuHV-1) (Mouse cytomegalovirus). OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes; OC Herpesvirales; Orthoherpesviridae; Betaherpesvirinae; Muromegalovirus; OC Muromegalovirus muridbeta1; Murid herpesvirus 1. OX NCBI_TaxID=69156 {ECO:0000313|EMBL:CAP08092.1, ECO:0000313|Proteomes:UP000158680}; OH NCBI_TaxID=10090; Mus musculus (Mouse). RN [1] {ECO:0000313|EMBL:CAP08092.1, ECO:0000313|Proteomes:UP000158680} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K181 {ECO:0000313|EMBL:CAP08092.1}; RX PubMed=15709020; DOI=10.1128/JVI.79.5.2998-3008.2005; RA Redwood A.J., Messerle M., Harvey N.L., Hardy C.M., Kozinowski U.H., RA Lawson M.A., Shellam G.R.; RT "Use of a murine cytomegalovirus K181-derived bacterial artificial RT chromosome as a vaccine vector for immunocontraception."; RL J. Virol. 79:2998-3008(2005). RN [2] {ECO:0000313|EMBL:CAP08092.1, ECO:0000313|Proteomes:UP000158680} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K181 {ECO:0000313|EMBL:CAP08092.1}; RX PubMed=18417589; DOI=10.1128/JVI.00160-08; RA Smith L.M., McWhorter A.R., Masters L.L., Shellam G.R., Redwood A.J.; RT "Laboratory strains of murine cytomegalovirus are genetically similar to RT but phenotypically distinct from wild strains of virus."; RL J. Virol. 82:6689-6696(2008). 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:0000256|HAMAP-Rule:MF_04027}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|HAMAP-Rule:MF_04027}. Host CC cytoplasm {ECO:0000256|HAMAP-Rule:MF_04027}. CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large CC chain family. {ECO:0000256|ARBA:ARBA00010406, ECO:0000256|HAMAP- CC Rule:MF_04027}. CC -!- CAUTION: Lacks the conserved sequence Asn-x-Cys-x-Glu essential for CC ribonucleotide reductase activity. {ECO:0000256|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; AM886412; CAP08092.1; -; Genomic_DNA. DR SMR; A8E1H1; -. DR IntAct; A8E1H1; 5. DR MINT; A8E1H1; -. DR Proteomes; UP000158680; 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:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR Gene3D; 3.20.70.20; -; 1. DR HAMAP; MF_04027; HSV_RIR1_betahv; 1. DR InterPro; IPR034716; HSV_RIR1_betahv. DR InterPro; IPR025735; RHIM_dom. DR InterPro; IPR000788; RNR_lg_C. DR InterPro; IPR013509; RNR_lsu_N. 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; PF12721; RHIM; 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. PE 3: Inferred from homology; KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200, ECO:0000256|HAMAP- KW Rule:MF_04027}; KW Late protein {ECO:0000256|ARBA:ARBA00022921, ECO:0000256|HAMAP- KW Rule:MF_04027}; Reference proteome {ECO:0000313|Proteomes:UP000158680}; KW Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|HAMAP-Rule:MF_04027}. FT DOMAIN 50..71 FT /note="RHIM" FT /evidence="ECO:0000259|Pfam:PF12721" FT DOMAIN 514..597 FT /note="Ribonucleotide reductase large subunit N-terminal" FT /evidence="ECO:0000259|Pfam:PF00317" FT DOMAIN 649..1135 FT /note="Ribonucleotide reductase large subunit C-terminal" FT /evidence="ECO:0000259|Pfam:PF02867" FT REGION 197..269 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 291..325 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 197..221 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 250..265 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1174 AA; 125127 MW; 449486931C4152D9 CRC64; MDRQPKVYSD PDNGFFFLDV PMPDDGQGGQ QTATTAAGGA FGVGGGHSVP YVRIMNGVSG IQIGNHNAMS IASCWSPSYT DRRRRSYPKT ATNAAADRVA AAVSAANAAV NAAAAAAAAG GGGGANLLAA AVTCANQRGC CGGNGGHSLP PTRAPKTNAT AAAAPAVAVA SNAKSDNNHA NAASGAGSAA ATPAATTSAA AAVENRRPSP SPSTASTAPC DEGSSPRHHR PSHVSVGTQA TPSTPIPIPA PRCSTGQQQQ QPQAKKLKPA KADPLLYAAT MPPPASVTTA AAAAVAPESE SSPAASAPPA AAAMATGGDD EDQSSFSFVS DDVLGEFEDL RIAGLPVRDE MRPPTPTMTV IPVSRPFRAG RDSGRDALFD DAVESVRCYC HGILGNSRFC ALVNEKCSEP AKERMARIRR YAADVTRCGP LALYTAIVSS ANRLIQTDPS CDLDLAECYV ETASKRNAVP LSAFYRDCDR LRDAVAAFFK TYGMVVDAMA QRITERVGPA LGRGLYSTVV MMDRCGNSFQ GREETPISVF ARVAAALAVE CEVDGGVSYK ILSSKPVDAA QAFDAFLSAL CSFAIIPSPR VLAYAGFGGS NPIFDAVSYR AQFYSAESTI NGTLHDICDM VTNGLSVSVS AADLGGDIVA SLHILGQQCK ALRPYARFKT VLRIYFDIWS VDALKIFSFI LDVGREYEGL MAFAVNTPRI FWDRYLDSSG DKMWLMFARR EAAALCGLDL KSFRNVYEKM ERDGRSAITV SPWWAVCQLD ACVARGNTAV VFPHNVKSMI PENIGRPAVC GPGVSVVSGG FVGCTPIHEL CINLENCVLE GAAVESSVDV VLGLGCRFSF KALESLVRDA VVLGNLLIDM TVRTNAYGAG KLLTLYRDLH IGVVGFHAVM NRLGQKFADM ESYDLNQRIA EFIYYTAVRA SVDLCMAGAD PFPKFPKSLY AAGRFYPDLF DDDERGPRRM TKEFLEKLRE DVVKHGIRNA SFITGCSADE AANLAGTTPG FWPRRDNVFL EQTPLMMTPT KDQMLDECVR SVKIEPHRLH EEDLSCLGEN RPVELPVLNS RLRQISKESA TVAVRRGRSA PFYDDSDDED EVACSETGWT VSTDAVIKMC VDRQPFVDHA QSLPVAIGFG GSSVELARHL RRGNALGLSV GVYKCSMPPS VNYR //