ID A0A369GR44_9HYPO Unreviewed; 911 AA.
AC A0A369GR44;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
GN ORFNames=CP532_1248 {ECO:0000313|EMBL:RDA85352.1};
OS Ophiocordyceps camponoti-leonardi (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2039875 {ECO:0000313|EMBL:RDA85352.1, ECO:0000313|Proteomes:UP000252748};
RN [1] {ECO:0000313|EMBL:RDA85352.1, ECO:0000313|Proteomes:UP000252748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 80369 {ECO:0000313|EMBL:RDA85352.1,
RC ECO:0000313|Proteomes:UP000252748};
RA Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA Luangsa-Ard J.-J., Giraud T.;
RT "A genome scan of diversifying selection in the zombie-ant fungus
RT Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT coevolution and host-specificity.";
RL Submitted (OCT-2017) 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|RuleBase:RU003410};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406,
CC 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:RDA85352.1}.
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DR EMBL; PDHP01000080; RDA85352.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369GR44; -.
DR STRING; 2039875.A0A369GR44; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000252748; 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:UP000252748}.
FT DOMAIN 1..97
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 808..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 911 AA; 102385 MW; EE103BB7B166CA5F CRC64;
MYVKKRDGRQ ERVQFDKITA RVSRLCYGLD SEHVDPVAIS QKVISGVYGG VTTIQLDDLI
DSLQAAETAA YMTVTHPDYA ILAARIAVSN LHKQTKKQWS SVVNDLYHYV SPKNKRASPR
ISKETYECVM RHKEELDSAI VYDRDFNYQY FGFKTLERSY LLRLDGKVVE RPQHMIMRVA
IGIWGDNIER VIETYNLMSN KFFTHASPTL FNAGIPNGQL SSCFLVDMKE DSIEGIYDTL
KTTAIISKMA GGIGLNVHRI RATGSDIAGT NGTSNGIVPM LRVFNYTSRY VDQGGNKRPG
AFAIYLEPWH ADIFDFLELR KNHGKEEMRA RDLFLALWIP DLFMKRVKEN GDWTLMCPNE
CPGLADCYGD EFEALYEKYE REGRGRATIR AQKLWYSILE AQTETGNPFM LYKDHCNRKS
NQKNLGTIRS SNLCTEIIEY SAPDEVAVCN LASLALPAFV DYDQGCYDFK KLHDVTQVVV
RNLNRIIDVN HYPVPEAYNS NMRHRPIGVG VQGLADAFLA LRMPFESPEA QQLNKQIFET
IYHASLTASM ELAKEQGTYS SYEGSPVSQG ILQFDMWDVK PSELWDWEPL RAQIKEHGVR
NSLLVAPMPT ASTSQILGNN ECFEPYTSNI YQRRVLAGEF QVVNPWLLKD LVDMGLWSDA
MKNRIIAENG SIQNIPNIPA EIKALYKTVW EISQRQVVQM AADRGAFIDQ SQSLNIHMKD
PTMGKITSMH FAGWKLGLKT GMYYLRTQAA AAPIQFTVDQ EALLVADTNV GRERMPKKRT
APAGTSYMAM PVMVSRPAEA RPVQNVVIVD PNGIPTPNTT PPREVKGADA STPRPLASPS
KPPAIKAEKV EGDSPRVLPT EPSSEGIKDG EAEEQTEDKE EASEEREQDI YSDAVLACSI
ENPQACEMCS G
//
