RIR1_IIV6
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 03-AUG-2022, entry version 111.
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 -!- PATHWAY: Genetic information processing; DNA replication.
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 UniPathway; UPA00326; -.
DR Proteomes; UP000001359; Genome.
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:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR Gene3D; 3.10.28.10; -; 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; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR PANTHER; PTHR11573; PTHR11573; 2.
DR Pfam; PF14528; LAGLIDADG_3; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 2.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF48168; SSF48168; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR SUPFAM; SSF55608; SSF55608; 1.
DR TIGRFAMs; TIGR01445; intein_Nterm; 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
