ID Q9RRW1_DEIRA Unreviewed; 1418 AA.
AC Q9RRW1;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 150.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
GN OrderedLocusNames=DR_2374 {ECO:0000313|EMBL:AAF11919.1};
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230 {ECO:0000313|EMBL:AAF11919.1, ECO:0000313|Proteomes:UP000002524};
RN [1] {ECO:0000313|EMBL:AAF11919.1, ECO:0000313|Proteomes:UP000002524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC NCIMB 9279 / R1 / VKM B-1422 {ECO:0000313|Proteomes:UP000002524};
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L., Utterback T., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}.
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 Evidence={ECO:0000256|RuleBase:RU003410};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|RuleBase:RU003410}.
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; AE000513; AAF11919.1; -; Genomic_DNA.
DR PIR; D75281; D75281.
DR RefSeq; NP_296095.1; NC_001263.1.
DR STRING; 243230.DR_2374; -.
DR PaxDb; 243230-DR_2374; -.
DR EnsemblBacteria; AAF11919; AAF11919; DR_2374.
DR KEGG; dra:DR_2374; -.
DR PATRIC; fig|243230.17.peg.2610; -.
DR eggNOG; COG0209; Bacteria.
DR eggNOG; COG1372; Bacteria.
DR HOGENOM; CLU_000404_2_1_0; -.
DR InParanoid; Q9RRW1; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IBA:GO_Central.
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; -; 3.
DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 1.
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; IPR030934; Intein_C.
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 NCBIfam; TIGR01443; intein_Cterm; 1.
DR NCBIfam; TIGR01445; intein_Nterm; 1.
DR PANTHER; PTHR43371:SF1; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR43371; VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE; 1.
DR Pfam; PF14890; Intein_splicing; 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; 2.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Protein splicing {ECO:0000256|ARBA:ARBA00023000};
KW Reference proteome {ECO:0000313|Proteomes:UP000002524}.
FT DOMAIN 640..780
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 869..891
FT /note="Intein C-terminal splicing"
FT /evidence="ECO:0000259|PROSITE:PS50818"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1418 AA; 152909 MW; 6736098DE6EA95B4 CRC64;
MPVSQHGGKV GHRSTSSCLT RDHQRTPCCP FRRRDGFPCC AGALAASPSS PSPPPSARSS
MTTAPDRSAP ARTDKTTQHF DENAQHIAKR QYLQGNDGDI SGMFWRIADW VAGAEAPEAR
QGWAQQYYDL MAEKKFCPGG RVLAGAGTQH GNVLNCFVQG ATEHDPSSFE GVMEVAKKLA
LVTKVGGGNG VNLDVYRPRA QSSRSDNGVR GWVYMSAEHA DVQDFIEGLM RPPTQPDGEK
QPVSVRNWTR VVYGQAISPE LVASARANGV QIVRTLPEGV TAVADDMGGI IDAARQVAEI
AKLNIEPRID LSAMRPEGAP IKGSGGTSSG PVSFLMEIFD NFIEWANRGA EDSGPINTLR
YVYAPVLRVV RQGGTRRGAG MATISIGHPD VLDFLTAKDL DREAAEGDIS TFNISILVDT
KFWDTLQADG VWTIDAQDVP GKYFPVPQEG EYAGTFPELP TRAEDGAKGV PVYGSGIPAR
WLWDQIAQHA WSTGEPGLIF NDRVNEYSAL KNLGERYEIR STNPCVTADT WVSTAFGARQ
VQDLIGKDFC ATVNGESFSA RGGFWLTGVK SVLKVTTRRG YELRLTGNHQ LLKVTHQTRK
VQQTAWVETA TLAAGDRIML NDHRTVKPWA GAGNFSEGWL LGSLIGDGTF LTDKARPMAA
LGFWGEERQA QADSAQARLS KLGAVKKLWR SNDEQRQRVR LSSEALAELG AKYGVVHGHK
TLTDKVEQGG YEFYRGVLQG LFDADGSVQG TQSKGVSVRL AQSDLSLLKR AQRMLSRLGI
MSSLYAERRL AGTSTLPDGK GGSAEYPTQA QHELIISGSN LAVFAERVGF SEAGKAARLA
EKLAGYARNL NRERFSDEIV SIVPDGEEAV YDVTVEQVHA FDANGVLAHN CGEIPLTVGE
PCDLGAINLA AYVRGSDFDF AAFRADVRTC VRFLDDVLDV NVFALEDNRV ASQDLRRLGL
GVMGLADALI KMGLRYDNES GRQAIYDIMS ALREEAVAES ERLGQERGFY PVYERNREQV
PHDPRRNVAV LTVAPTGTTS MLMGVSSGIE PVFSPFIWRK IGSEYRALLA PLFVELLESY
PAPKGMEKDG GWDWDKVTEA VSENHGSVVG LSFIPDALQQ VFVCAHDISP VDHVRMQGTV
QRAFDDGGQL AANSLSKTIN LPNSASVDDV KSAYEEAYRT GCKGITVYRD GSRQFQVLST
SKKKAKTEER GSAEPLADSK PAEAPAVTAP VSAPAAAAQP QPHYERPGRL HGITDMVKLT
DPTSGHRRSF LVTVNHLNGN PVEVMVISGR AGDEANADSE ALGRVVSIAL QHGVPASALI
HTLRGINGGL YGSYNGRLVG SKADLIAVAL DTFQKDMAAA PLPPLAGGSG EVAPSAPAST
GVSVDGLGQE RCPVCEEKAV IREEGCLKCQ ACGYSKCG
//
