ID W9XBS5_9EURO Unreviewed; 911 AA.
AC W9XBS5;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=A1O3_09912 {ECO:0000313|EMBL:EXJ77683.1};
OS Capronia epimyces CBS 606.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ77683.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ77683.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ77683.1,
RC ECO:0000313|Proteomes:UP000019478};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL Submitted (MAR-2013) 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:EXJ77683.1}.
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DR EMBL; AMGY01000010; EXJ77683.1; -; Genomic_DNA.
DR RefSeq; XP_007738193.1; XM_007740003.1.
DR AlphaFoldDB; W9XBS5; -.
DR STRING; 1182542.W9XBS5; -.
DR GeneID; 19173993; -.
DR eggNOG; KOG1112; Eukaryota.
DR HOGENOM; CLU_000404_1_2_1; -.
DR OrthoDB; 5472715at2759; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000019478; 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:UP000019478}.
FT DOMAIN 1..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 799..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..886
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 911 AA; 102102 MW; 304E191F1BB849AA CRC64;
MFVFKRDGRK ERVQFDKITA RVSRLCYGLD PEHVDAAAIT QKVISGVYQG VTTFELDNLA
AETAAYMTVT HPDYAILAAR IAVSNLHKQT KKQFSSVISD LYHYINPKNN KPSPMISDET
YECVMRHADE LNSAIVYDRD FNYQYFGFKT LERSYLLKIG NQVAERPQHL LMRVAVGIHG
DDVEKAIETY NLMSQKCFTH ASPTLFNAGT PQPQLSSCFL IDMKEDSIDG IYDTLKTCAL
ISKTAGGIGL NAHCIRATGS YIAGTNGTSN GLIPMLRVFN NTARYVDQGG NKRPGAFAIY
LEPWHADVFE WLNLRKNHGK EEVRARDLFY ALWTPDLFMQ RVEKNQDWTL FCPHEAPGLA
DVYGDEFVAL FEKYEREGRG RQTIKAQKLW YAILEAQTET GTPFMLYKDA CNNKSNQKNL
GTIRNSNLCT EIVEYCAPDE VAVCNLASLA LPTFVDQARG EYDFGRLHEV VQVVTRNLNK
IIDINYYPVP EAKKSNFRHR PIGLGVQGLA DAFLALRLPF DSPEARQLNI QIFETIYHAA
LTASCELARE QGTYETYEGS PVSQGILQYD MWNVTPTDLW DWDSLKAEIA KYGVRNSLLV
APMPTASTSQ ILGNNECFEP YTSNIYSRRV LAGEFQVVNP WLLKDLVDLG LWSDNMKNRI
IADGGSIQNI PNIPADIKAL YKTVWEISQR TILQMAADRG AFIDQSQSLN IHLKEPTMGK
LTSMHFAGWK MGLKTGMYYL RTMAASAPIQ FTVDQEQLKV TDTNVARERS LPKKRTSLGF
GQSYTSVPRP MYATKTPNFV GSSSTTSLNG IPTPTSTPPP SEDKNLELVN KLAKTRLSEG
SSSEEPSPKV LPTDPIGTPI VEESLENREQ VKRVQEEDAQ SDSAEREVDI YSQKVLACSI
ENGDACVMCS G
//
