ID A0A2S7P5N5_9HELO Unreviewed; 905 AA.
AC A0A2S7P5N5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=CJF32_00007117 {ECO:0000313|EMBL:PQE09605.1};
OS Rutstroemia sp. NJR-2017a WRK4.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Rutstroemiaceae; Rutstroemia.
OX NCBI_TaxID=2070412 {ECO:0000313|EMBL:PQE09605.1, ECO:0000313|Proteomes:UP000238813};
RN [1] {ECO:0000313|EMBL:PQE09605.1, ECO:0000313|Proteomes:UP000238813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJR-2017a WRK4 {ECO:0000313|EMBL:PQE09605.1,
RC ECO:0000313|Proteomes:UP000238813};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-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|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:PQE09605.1}.
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DR EMBL; NJPR01000131; PQE09605.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7P5N5; -.
DR STRING; 2070412.A0A2S7P5N5; -.
DR InParanoid; A0A2S7P5N5; -.
DR OrthoDB; 5472715at2759; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000238813; 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:UP000238813}.
FT DOMAIN 1..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 769..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..884
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 905 AA; 101136 MW; 4C6B5CB3F3FBA58A CRC64;
MFVNKRDGRK ERVQFDKITA RVSRLCYGLD ADHVDAAAIT QKVISGVYHG VSTIELDNLA
AETAAYMTVT HPDYAILAAR IAVSNLHKQT KKQFSHVISD LYHYVNPRNN KPSPMISKET
YECVMRHEAE LNSAIVYDRD FNYQYFGFKT LERSYLLRLD GKIAERPQQM IMRVAVGIHG
DDIESAIETY NLMSNKYFTH ASPTLFSAGT PQAQLSSCFL IDMKEDSIDG IYDTLKTCAM
ISKNAGGIGL NIHRIRATGA YIAGTNGNSN GIVPMLRVFN NTARYVDQGG NKRPGAFAVY
LEPWHADVFE FLDLRKNHGK EEVRARDLFY ALWIPDLFMK RVEKNGDWTL MCPNECPGLA
DVYGDEFEAL YESYEKEGRG RKTIKAQKLW YSILEAQTET GNPFMLYKDA CNKKSNQKNL
GTIRSSNLCT EIVEYSAPDE VACCNLASIA LPTFVDMNEG TYDFQKLHEV TQVVVRNLNK
IIDINYYPVP EAKKSNFRHR PIAVGVQGLA DAFLALRLPF ESPEAKHLNV QIFETIYHAA
LTSSVEIAKE LGPYETYEGS PVSKGELQYD MWGVTPTDLW DWDSLKKSIK QHGVRNSLLV
APMPTASTSQ ILGFNECFEP YTSNIYSRRV LAGEFQVVNP WLLKDLVDMG LWSDNMKNRI
IADGGSIQNI PNIPADIKAL YKTVWEISQR TIVQMAADRG AFVDQSQSMN IHMKDPTMGK
ITSMHFAGWK LGLKTGMYYL RTMAASAPIQ FTVDQEALLV ADTNIARERT TKKRSMPTSG
YISSSSATNG AGPRPMYAKQ SSQNKSSSIS APNGVPTPST TPPPSTTAAA KEAHTPIAKV
PFKADMEEGG SPKALATEPV GEPKEEELEV KAKQVEDEGQ GSEEREYDIY AEAKLQFKFP
PATLF
//
