ID A0A091QX93_MERNU Unreviewed; 778 AA.
AC A0A091QX93;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
DE Flags: Fragment;
GN ORFNames=N331_11038 {ECO:0000313|EMBL:KFQ32190.1};
OS Merops nubicus (Northern carmine bee-eater).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Meropidae; Merops.
OX NCBI_TaxID=57421 {ECO:0000313|EMBL:KFQ32190.1, ECO:0000313|Proteomes:UP000052967};
RN [1] {ECO:0000313|EMBL:KFQ32190.1, ECO:0000313|Proteomes:UP000052967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N331 {ECO:0000313|EMBL:KFQ32190.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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|ARBA:ARBA00024942,
CC 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|ARBA:ARBA00000206,
CC ECO:0000256|RuleBase:RU003410};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406,
CC ECO:0000256|RuleBase:RU003410}.
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DR EMBL; KK709082; KFQ32190.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091QX93; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000052967; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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 CDD; cd01679; RNR_I; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR013346; NrdE_NrdA_C.
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; TIGR02506; NrdE_NrdA; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF03477; ATP-cone; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000052967}.
FT DOMAIN 1..86
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 586..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ32190.1"
FT NON_TER 778
FT /evidence="ECO:0000313|EMBL:KFQ32190.1"
SQ SEQUENCE 778 AA; 88687 MW; D2F851C3C7E889DB CRC64;
DGRQERVMFD KITSRIQKLC YGLNADFVDP AQITMKVIQG LYSGVTTVEL DTLAAETAAT
LTTKHPDYAI LAARIAVSNL HKETKKVFSD VMDDLYNYVN PHNGKHSPMI SKETLDIVLA
NKDRLNSAII YDRDFSYNYF GFKTLERSYL LKINSKVAER PQHMLMRVSV GIHKTDIEAA
IETYNLLSER WFTHASPTLF NAGTSRPQLS SCFLLCMKDD SIEGIYDTLK QCALISKSAG
GIGLAVSCIR ATGREGLGTN GNSNGLVPML RVYNNTARYV DQGGNKRPGA FAIYLEPWHL
DIFEFLDLKK NTGKEEQRAR DLFFALWIPD LFMKRVETNQ DWSLMCPNEC PGLDEVWGEE
FEKLYESYER QGRARRVVRA QQLWYAIIES QTETGTPYML YKDSCNRKSN QQNLGTIKCS
NLCTEIVEYT SKDEVAVCNL ASIALNMYVT SEHTYDFKKL AEVTKVIVRN LNKIIDINYY
PVPEAERSNR RHRPIGIGVQ GLADAFILMR FPFESPEAQR LNQQIFETIY YGALEASCEL
AKEQGPYETY EGSPVSKGVL QYDMWNVTPS DLWDWKALKE KIARSWATTN PSSPTPATST
HAESSQESFR VDSTFVLCLL QVVNPHLLKD LTERGLWNEE MKNQIIAHNG SIQNIPEIPD
DLKQLYKTVW EISQKTILKM AADRGAFIDQ SQSLNIHIAE PNYGKLTSMH FYGWKQGLKT
GMYYLRTKPA ANPIQFTLNK EKLREREKAS KEEEEKERNK AAMVCSLENR EECMMCGS
//
