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Database: UniProt
Entry: A0A2T3W3W6_9DEIO
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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
//
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