ID A0A0P5ESK7_9CRUS Unreviewed; 806 AA.
AC A0A0P5ESK7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
GN ORFNames=APZ42_027762 {ECO:0000313|EMBL:KZS08302.1};
OS Daphnia magna.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=35525 {ECO:0000313|EMBL:JAJ86404.1};
RN [1] {ECO:0000313|EMBL:JAJ86404.1}
RP NUCLEOTIDE SEQUENCE.
RA Gilbert D.G.;
RT "EvidentialGene: Evidence-directed Construction of Complete mRNA
RT Transcriptomes without Genomes.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KZS08302.1, ECO:0000313|Proteomes:UP000076858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xinb3 {ECO:0000313|EMBL:KZS08302.1,
RC ECO:0000313|Proteomes:UP000076858};
RC TISSUE=Complete organism {ECO:0000313|EMBL:KZS08302.1};
RA Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL Submitted (MAR-2016) 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; GDIQ01265320; JAJ86404.1; -; Transcribed_RNA.
DR EMBL; LRGB01002244; KZS08302.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P5ESK7; -.
DR STRING; 35525.A0A0P5ESK7; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000076858; 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.
DR PROSITE; PS00089; RIBORED_LARGE; 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:UP000076858}.
FT DOMAIN 9..100
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 806 AA; 90704 MW; 50DFB53D40673497 CRC64;
MVGGGCKKMF VLKRGGRQED VHFDKITSRI QKLCYGLNMD FVDPTAITMK VINGLYPGVT
TVELDNLAAE TAATMTTKHP DYAILAARIA VSNLHKETKK VFSEVIDDLY NMKDAKTKKP
TPMISEFHHD VIMKHSDKLN SAIIYDRDFN FNYFGFKTLE RSYLLKISGK PVERPQHMMM
RVSVGIHGDD LEAAIETYNL LSEKWFTHAS PTLFNAATPR PQLSSCFLLT MKDDSIDGIY
ETLKQCAIIS KSAGGIGLNI HCIRATGSYI AGTNGISNGL VPMLRVYNNT ARYVDQGGNK
RPGAFAIYLE PWHSDVFEFL DLKKNTGKEE NRARDLFYAL WIPDLFMQRV ESDGEWSLMC
PNECPGLADA WGEEFEALYT KYEESGLYRR KVKAQQLWFA VIESQIETGT PYILYKDACN
RKSNQQNLGT IKCSNLCTEI VEYSSPDEVA VCNLASIALN MFVKPDRAYD LPKLKEITKV
ITRNLNKIID VNYYPVPEAK LSNFRHRPIG IGVQGLADAF ILMRYPFDSE EAQLLNKQIF
ETIYYGALES SCELAQQFGP YESYPGCPVS KGILQYDMWG VTPTDLWDWA SLKKKIAEFG
VRNSLLLAPM PTASTAQILG NNESIEAYTS NIYVRRVLSG EFQVVNHHLL RDLTEGGLWN
EDVKNGIIAH NGSIQEIDGI PDDVKALYKT VWEIPQRVII KMAADRGAFI DQSQSLNIHI
AEPNYGKLTS MHFYAWKLGL KTGMYYLRTK PAASAIQFTV DKSKLKISSD VDNSSAAAKS
AEEERKNREA MVCSLQNKDD CLMCGS
//
