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Database: UniProt
Entry: Q6BZQ3_YARLI
LinkDB: Q6BZQ3_YARLI
Original site: Q6BZQ3_YARLI 
ID   Q6BZQ3_YARLI            Unreviewed;       892 AA.
AC   Q6BZQ3;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 125.
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=YALI0_F31735g {ECO:0000313|EMBL:CAG78922.1};
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591 {ECO:0000313|EMBL:CAG78922.1, ECO:0000313|Proteomes:UP000001300};
RN   [1] {ECO:0000313|EMBL:CAG78922.1, ECO:0000313|Proteomes:UP000001300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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   -!- PATHWAY: Genetic information processing; DNA replication.
CC       {ECO:0000256|ARBA:ARBA00005160, 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; CR382132; CAG78922.1; -; Genomic_DNA.
DR   RefSeq; XP_506109.1; XM_506109.1.
DR   AlphaFoldDB; Q6BZQ3; -.
DR   STRING; 284591.Q6BZQ3; -.
DR   EnsemblFungi; CAG78922; CAG78922; YALI0_F31735g.
DR   GeneID; 2908285; -.
DR   KEGG; yli:YALI0F31735g; -.
DR   VEuPathDB; FungiDB:YALI0_F31735g; -.
DR   HOGENOM; CLU_000404_1_0_1; -.
DR   InParanoid; Q6BZQ3; -.
DR   OMA; RGSIQNI; -.
DR   OrthoDB; 5472715at2759; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000001300; Chromosome F.
DR   GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IBA:GO_Central.
DR   GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
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:UP000001300}.
FT   DOMAIN          4..95
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
FT   REGION          818..866
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   892 AA;  100993 MW;  CB05C3C8A9FA7735 CRC64;
     MSKLFVIKRD GRKESVQVDK ITARIKRLCY GLDPDHVDPI QITLKIASGI YEGVSTIELD
     NLAAETAAYM TTLHPDYAIL AARIAVSNLH KQTKKQFSQV VYDLYHYVNP RNKKHSPMVS
     KELYDTVQAN ADELNGAILY DRDFTYNYFG FKTLERAYLL RVNGAVAERP QQMIMRVSVG
     IHGDNIARAI ETYNYMSQKY FTHASPTLYN AGTPQPQMSS CFLVNMKDDS IDGIYDTLKT
     CALISKSAGG IGLSIHNIRA TGSYIAGTNG TSNGIVPMLR VYNNTARYVD QGGNKRPGAF
     AMYLEPWHDD IFEFCELRKN HGKEEIRARD LFLALWIPDL FMERVEQNAE WTLMCPNECP
     GLDDVYGDEF KQLYEQYEKE GRGRRTIPAQ KLWYHILDCQ TESGNPFMLY KDSCNRKSNQ
     KNLGTIKSSN LCCEIVEYSS PDEVAVCNLA SIALPTFVTR DDTNSFYDFK KLHDIAKVIV
     RNLNAIIDRN YYPVPEAKKS NMRHRPIALG VQGLADTFMA LRLPFESEEA KKLNIQIFET
     IYHGAVEASY EMALEDGAYE TFQGSPASKG DLQFDLWNVT PSELWEWDDL KAKIMKTGMR
     NSLLVAPMPT ASTSQILGFN ECFEPYTSNI YSRRVLAGEF QIVNPWLLKD LVEVGLWNET
     MKNRIVADNG SVQNIPNIPQ EIKDLYKTVW EISQKRIIEM AADRSPFIDQ SQSLNIHIKD
     PTMGKLTSMH FYGWKKGLKT GMYYLRTMAA AAPIQFTIDQ EALKTIDSST AKAMLNKKPY
     QEINSMANLR SIEDKIAKID LNGGNKENNV MELIRESQEK KEAEKEAKRV PAPVAETKEE
     TQEETKPVEK PAAAEDKPAE DSPIAKSEYD IYADKVLACS LANPESCEMC SG
//
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