ID A0A2T3W3W6_9DEIO Unreviewed; 1372 AA.
AC A0A2T3W3W6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
GN ORFNames=C8263_17155 {ECO:0000313|EMBL:PTA66562.1};
OS Deinococcus arcticus.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=2136176 {ECO:0000313|EMBL:PTA66562.1, ECO:0000313|Proteomes:UP000240317};
RN [1] {ECO:0000313|EMBL:PTA66562.1, ECO:0000313|Proteomes:UP000240317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OD32 {ECO:0000313|EMBL:PTA66562.1,
RC ECO:0000313|Proteomes:UP000240317};
RA Wang X.-P., Du Z.-J.;
RT "Draft genome of Deinococcus sp. OD32.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Genetic information processing; DNA replication.
CC {ECO:0000256|RuleBase:RU003410}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|RuleBase:RU003410}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PTA66562.1}.
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DR EMBL; PYSV01000025; PTA66562.1; -; Genomic_DNA.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000240317; Unassembled WGS sequence.
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:UniProtKB-UniPathway.
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 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}.
FT DOMAIN 577..717
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 806..828
FT /note="Intein C-terminal splicing"
FT /evidence="ECO:0000259|PROSITE:PS50818"
FT REGION 1144..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1372 AA; 148051 MW; F173C15D5360F680 CRC64;
MTIPTAPTLT NFDENAHHIA KRQYLQAGDG DLGGMFRRIA TWVAGAEAPE ARAHWAQQYF
DLMAEKKFCP GGRVLAGAGT AHGNVLNCFV QGATEHAPSS FEGVMEVARK LALVTKVGGG
NGVNLDVYTP RAQGSRPDAG VRGWAYMSAA HADVTDFIEG LMRPPTQPDG DKQPVAVRNW
TRVVYGQVIR PEIVALARAN GVAVVAALPE GVQTVPDDMG GIIDAARKVA DDAKLGLEPR
IDLSTMRPEG APIRGSGGTS SGPVSFLLEI FDNFLEWANR GAETSGPVNT LRFVYSPVLR
VVRQGGTRRG AGMATISIGH PDVLDFLTAK DLDREAAEGD ISTFNISILV STAFWDTLQQ
GGLWPVQAQE VPGKYYLAPQ TGAFKGEWPE LPVRAEDDAQ GVPVYALKKG QSGIPARWLW
DQIAQHAWST GEPGLIFVDR INEYSALKNL GERYQIRSTN PCVTADTWVS TAMGARQVSQ
LIGKDFCAVV DGQSYSAQGG FWLTGVKPVL RVTTRRGYEL RLTDNHQLLK VVSQTRDVQD
TAWVETGTLV PGDRIMLSDH RDVTPWAGVG NRSEGWLLGN LIGDGTFQTD KARPMAALGF
WGETRHVMAD AAQELLAKMG AVKKLWRSND EVRARVRLSS EALAELAARY GVTPGHKTLT
DQIEQGGYEL YRGVLQGLFD ADGSVQGDQR KGVSVRLAQS DLPLLKRAQR MLARLGILST
LYPERRPEGL KLLPDGQGGH AEYATRAQHE LVISGSNLRT FMQVVNFRDA HKAGRLAQAL
STYTRNLNRE RFSDEIVSIQ PDGEEAVYDV TVQQVHAFDA NGIKAHNCGE IPLTVGEPCD
LGAINLAAYV KGSAFDYATF RADVRTCVRF LDDVLDVNVF ALEDNRVASQ DLRRLGLGVM
GLADALIKLG LRYDSEAGRD TIYDIMSALR EEAVAESERL GQERGIYPVY TRHEGQIPHA
PRRNVAVLTV APTGTTSMLM GVSSGIEPIF SPFIWRKIGS EYRALLAPLF VELLETYPAP
QGMGKDGNGA GNETRPGWDW DKVTEAVSEN HGSVVGLPFI PEALQQVFVC AHDIKPADHV
RMQGAVQRAF DAEGYAANSL SKTINLPNEA TVQDVQDAYS EAYTTGCKGI TVYRDGSRQF
QVLSTSKKKK ESTEQPAQAA AEVMGEQGET PAPAAPALAL PAVPAPAARS AMPSKPQYER
PTRLSGITDM VKLTDPTSGH RRSFLVTVNQ LNGKPVEVMV ISGRAGDEAN ADSEALGRVV
SIALQHGVPA QAIIKTLRGI NGGLYGSYNG RLVGSKADLI AVALETFQKD MEGAQLPPLA
GGSTDAVAPS PAPAGVSVDG MARERCPVCE EKAVIREEGC LKCQACGYSK CG
//