ID W8C3W0_CERCA Unreviewed; 797 AA.
AC W8C3W0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
GN Name=RIR1 {ECO:0000313|EMBL:JAB96614.1};
GN ORFNames=CCAP1982_LOCUS6455 {ECO:0000313|EMBL:CAD6997831.1};
OS Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Ceratitis; Ceratitis.
OX NCBI_TaxID=7213 {ECO:0000313|EMBL:JAB96614.1};
RN [1] {ECO:0000313|EMBL:JAB96614.1}
RP NUCLEOTIDE SEQUENCE.
RA Geib S.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB96614.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24495485; DOI=10.1186/1471-2164-15-98;
RA Calla B., Hall B., Hou S., Geib S.M.;
RT "A genomic perspective to assessing quality of mass-reared SIT flies used
RT in Mediterranean fruit fly (Ceratitis capitata) eradication in
RT California.";
RL BMC Genomics 15:98-98(2014).
RN [3] {ECO:0000313|EMBL:CAD6997831.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EGII {ECO:0000313|EMBL:CAD6997831.1};
RA Whitehead M.;
RL Submitted (NOV-2020) 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; CAJHJT010000012; CAD6997831.1; -; Genomic_DNA.
DR EMBL; GAMC01009941; JAB96614.1; -; mRNA.
DR RefSeq; XP_004537904.1; XM_004537847.2.
DR AlphaFoldDB; W8C3W0; -.
DR EnsemblMetazoa; XM_004537847.3; XP_004537904.1; LOC101456426.
DR GeneID; 101456426; -.
DR KEGG; ccat:101456426; -.
DR OrthoDB; 5472715at2759; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000606786; 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 2: Evidence at transcript level;
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:UP000606786}.
FT DOMAIN 6..97
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 797 AA; 90241 MW; F13C6CFEBF05EBFC CRC64;
MKSPKLYVIK RDGRKEDIHF DKITSRVQKL CYGLNMEFVD PVAITLKVIN GLYCGVTTQE
LDNLAAEIAA SLTTQHADYA TLAARIAISN LHKETKKVFS DVISALYNHV SDETGLPTPI
ISDFHYNVVK KHADRLNSAI IYDRDFGYNY FGFKTLERSY LLKLNGKIVE RPQHMLMRVA
IGIHGEDIDA AIDTYNLLSE RYFTHASPTL FAAATKQPQL SSCFLLTMVD DSIDGIFTSA
HQCALISKSA GGIGLNVHCI RAKGTSIAGT NGTSNGLVPM LRVFNNVARY VDQGGGKRPG
AFAIYLEPWH ADIFEFLDLK KNTGKEEHRA RDLFYALWIP DLFMKRVEAN EDWSLMCPHK
CPGLHEVWGE EFEKLYTKYE QEGRANKKVK AQSLWFSIIE SQVETGTPYM LYKDACNRKS
NQQNIGTIKC SNLCTEIVEY SAPDEVAVCN LASIALNMFV TPDKKYDFKR LKEVTKTVTR
NLNKIIDINH YPLPEAKKSN FRHRPIGIGV QGLADALILM RYPYESEQAF LLNQQIFETI
YYGALEASCE LAEKFGPYET YEGSPVSKGI LQYDMWDKKP TELWNWTELK EKIKKHGVRN
SLLLAPMPTA STAQIMGNNE SFEPYTSNIY TRRVLSGEFQ VVNHHLLRDL TELGLWDDDM
KNQIITSRGS IQNIESIPQN IRELYKTVWE ISVKTSIKMA ADRGAFIDQS QSFNIHVAEP
NYGKLTSIHF YGWKAGLKTG MYYLRTKPAA NAIQFTVDKS RKELNDEIKA KPPVENQNLA
DMVCSLENKD ACMSCGS
//
