ID RIR1_IIV6 Reviewed; 959 AA. AC O55716; DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 27-MAR-2024, entry version 116. DE RecName: Full=Ribonucleoside-diphosphate reductase large subunit; DE EC=1.17.4.1; DE AltName: Full=Ribonucleotide reductase large subunit; DE Contains: DE RecName: Full=IIV-6 RIR1 intein; GN ORFNames=IIV6-085L; OS Invertebrate iridescent virus 6 (IIV-6) (Chilo iridescent virus). OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes; OC Pimascovirales; Iridoviridae; Betairidovirinae; Iridovirus. OX NCBI_TaxID=176652; OH NCBI_TaxID=6997; Acheta domesticus (House cricket). OH NCBI_TaxID=168631; Chilo suppressalis (Asiatic rice borer moth). OH NCBI_TaxID=6999; Gryllus bimaculatus (Two-spotted cricket). OH NCBI_TaxID=58607; Gryllus campestris. OH NCBI_TaxID=7108; Spodoptera frugiperda (Fall armyworm). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11448171; DOI=10.1006/viro.2001.0963; RA Jakob N.J., Mueller K., Bahr U., Darai G.; RT "Analysis of the first complete DNA sequence of an invertebrate iridovirus: RT coding strategy of the genome of Chilo iridescent virus."; RL Virology 286:182-196(2001). RN [2] RP GENOME REANNOTATION. RX PubMed=17239238; DOI=10.1186/1743-422x-4-11; RA Eaton H.E., Metcalf J., Penny E., Tcherepanov V., Upton C., Brunetti C.R.; RT "Comparative genomic analysis of the family Iridoviridae: re-annotating and RT defining the core set of iridovirus genes."; RL Virol. J. 4:11-11(2007). CC -!- FUNCTION: Ribonucleoside-diphosphate reductase holoenzyme provides the CC precursors necessary for viral DNA synthesis. Allows virus growth in CC non-dividing cells. Catalyzes the biosynthesis of deoxyribonucleotides CC from the corresponding ribonucleotides (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'- CC diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'- CC diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA- CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1; CC -!- ACTIVITY REGULATION: Under complex allosteric control mediated by CC deoxynucleoside triphosphates and ATP binding. The type of nucleotide CC bound at the specificity site determines substrate preference. It seems CC probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP CC reduction and dTTP favors GDP reduction (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Heterotetramer composed of a homodimer of the large subunit CC (R1) and a homodimer of the small subunit (R2). Larger multisubunit CC protein complex are also active, composed of (R1)n(R2)n (By CC similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large CC chain family. {ECO:0000305}. 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; AF303741; AAB94427.1; -; Genomic_DNA. DR PIR; T03053; T03053. DR RefSeq; NP_149548.1; NC_003038.1. DR GeneID; 1733256; -. DR KEGG; vg:1733256; -. DR OrthoDB; 2980at10239; -. DR Proteomes; UP000001359; Genome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC. DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro. DR CDD; cd00081; Hint; 1. DR Gene3D; 3.20.70.20; -; 2. DR Gene3D; 3.10.28.10; Homing endonucleases; 1. DR InterPro; IPR003586; Hint_dom_C. DR InterPro; IPR003587; Hint_dom_N. DR InterPro; IPR036844; Hint_dom_sf. DR InterPro; IPR027434; Homing_endonucl. DR InterPro; IPR006142; INTEIN. DR InterPro; IPR004042; Intein_endonuc. DR InterPro; IPR006141; Intein_N. DR InterPro; IPR004860; LAGLIDADG_2. DR InterPro; IPR000788; RNR_lg_C. DR InterPro; IPR013509; RNR_lsu_N. DR InterPro; IPR008926; RNR_R1-su_N. DR InterPro; IPR039718; Rrm1. DR NCBIfam; TIGR01445; intein_Nterm; 1. DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1. DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1. DR Pfam; PF14528; LAGLIDADG_3; 1. DR Pfam; PF02867; Ribonuc_red_lgC; 2. DR Pfam; PF00317; Ribonuc_red_lgN; 1. DR PRINTS; PR00379; INTEIN. DR SMART; SM00305; HintC; 1. DR SMART; SM00306; HintN; 1. DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1. DR SUPFAM; SSF55608; Homing endonucleases; 1. DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1. DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1. DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1. DR PROSITE; PS50817; INTEIN_N_TER; 1. PE 3: Inferred from homology; KW Autocatalytic cleavage; Deoxyribonucleotide synthesis; Disulfide bond; KW Oxidoreductase; Protein splicing; Reference proteome. FT CHAIN 1..271 FT /note="Ribonucleoside-diphosphate reductase large subunit, FT 1st part" FT /id="PRO_0000376951" FT CHAIN 272..611 FT /note="IIV-6 RIR1 intein" FT /evidence="ECO:0000255" FT /id="PRO_0000376952" FT CHAIN 612..959 FT /note="Ribonucleoside-diphosphate reductase large subunit, FT 2nd part" FT /id="PRO_0000377536" FT DOMAIN 378..508 FT /note="DOD-type homing endonuclease" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00273" FT ACT_SITE 270 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 611 FT /note="Cysteine radical intermediate" FT /evidence="ECO:0000250" FT ACT_SITE 613 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 68 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 83..84 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 112 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 751..755 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 84 FT /note="Important for hydrogen atom transfer" FT /evidence="ECO:0000250" FT SITE 91 FT /note="Allosteric effector binding" FT /evidence="ECO:0000250" FT SITE 120 FT /note="Allosteric effector binding" FT /evidence="ECO:0000250" FT SITE 626 FT /note="Important for hydrogen atom transfer" FT /evidence="ECO:0000250" FT SITE 890 FT /note="Important for electron transfer" FT /evidence="ECO:0000250" FT SITE 891 FT /note="Important for electron transfer" FT /evidence="ECO:0000250" FT SITE 955 FT /note="Interacts with thioredoxin/glutaredoxin" FT /evidence="ECO:0000250" FT SITE 958 FT /note="Interacts with thioredoxin/glutaredoxin" FT /evidence="ECO:0000250" FT DISULFID 84..626 FT /note="Redox-active" FT /evidence="ECO:0000250" SQ SEQUENCE 959 AA; 108770 MW; CA051A57E685F419 CRC64; MSDIIIDLSR DSKFDELGLK RLRESYMMRE ETSPQERFAY VCKQVGTDRD HSQRLYEYTS KHWLSLSTPI LSFGKANHGL PISCYLSWIE DTKEGLIDTL SEVNQLSMLG GGVGVGVGIR TSDNKSTGVM SHLNTYDACS LAYKQDGVRR GSYAMYLNNN HPDVLQFIEM RKPTGDHNIR CLNLHHGLNI SDEFMELIEK CDGGGNIDDT WNLIDPHTKK ITTVGARDLW QRILETRMKT GEPYICFIDT CNKHMYDFQK KKGLTIKQSN LCVAPETMIL TEDGQFPIKD LEGKIIKVWN GNEFSSVTVV KTGTEKELLE VELSNGCTLS CTPEHKFIIV KSYTEAKKQK TDDNAIANAE RVDAQDLKPR MKLIKFDLPT LFGNSEHDIK YPYTHGFFCG DGTYTKYGKP QLSLYGDKKE LLTYLDVRTM TGLEDASGRL NTWLPLDLAP KFDVPINSSL ECRMEWLAGY LDADGCVFRN GTNESIQVSC IHLDFLKRIQ LLLIGMGVTS KITKLHDEKI TTMPDGKGGQ KPYSCKPIWR LFISSSGLYH LSEQGFETRR LKWEPRQPQR NAERFVEVLK VNKTGRVDDT YCFTEPINHA GVFNGILTGQ CSEIILPTDS TRTAVCCLSS LNLEYYDEWK DNDLFIKDVM EMLDNALTIF IEKAPPTISR AVNSAKKERS IGIGVLGFHS FLQQKNISFE SDEAAKLNID IFTKLRSKID TFNLVLGSLR GSPEDAEGTG RRFCCTMAVA PTATSSIIMG NTSPSVEPFR ANAYRQDTLS GSFLNKNRYL SRILSQRLNV KEINEVWSNI VSNGGSVQQL PNNLLSEQEK QVFKTAFEIN QKWVIKHAAD RQKYIDQSQS INLFLKPDIH KRELHSLHLN AWKSGLKTLY YLRSEKIADA DKISSNHMIN SINFTNIKES IKDSIKVSIL EVRNKEKNYE EKICKLTNGR RLSGCFACE //