ID A0A0L0GAS0_9EUKA Unreviewed; 799 AA.
AC A0A0L0GAS0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=SARC_01762 {ECO:0000313|EMBL:KNC86070.1};
OS Sphaeroforma arctica JP610.
OC Eukaryota; Ichthyosporea; Ichthyophonida; Sphaeroforma.
OX NCBI_TaxID=667725 {ECO:0000313|EMBL:KNC86070.1, ECO:0000313|Proteomes:UP000054560};
RN [1] {ECO:0000313|EMBL:KNC86070.1, ECO:0000313|Proteomes:UP000054560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP610 {ECO:0000313|EMBL:KNC86070.1,
RC ECO:0000313|Proteomes:UP000054560};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Young S.K., Zeng Q., Gargeya S., Alvarado L., Berlin A.,
RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Howarth C., Mehta T., Neiman D.,
RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., White J., Yandava C., Burger G., Gray M.W., Holland P.W.H.,
RA King N., Lang F.B.F., Roger A.J., Ruiz-Trillo I., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Sphaeroforma arctica JP610.";
RL Submitted (FEB-2011) 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|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}.
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DR EMBL; KQ241669; KNC86070.1; -; Genomic_DNA.
DR RefSeq; XP_014159972.1; XM_014304497.1.
DR AlphaFoldDB; A0A0L0GAS0; -.
DR STRING; 667725.A0A0L0GAS0; -.
DR EnsemblProtists; KNC86070; KNC86070; SARC_01762.
DR GeneID; 25902266; -.
DR eggNOG; KOG1112; Eukaryota.
DR OrthoDB; 5472715at2759; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000054560; 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:UP000054560}.
FT DOMAIN 5..96
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 799 AA; 90048 MW; 84B6EA026E09F0BA CRC64;
MAPKLYVTKR DGRKEAVLFD KITSRISRLC YGLNEEFVDP TDVTMKIVSG IYAGVTTVEL
DTLAAETCAY MTTTHPDYAI LAARIAMSNL HKETKKVFSE VMNDLATYVN PKNDKQSPLV
SEEFIQRVRA NSEKLNSAIV YDRDFNYQYF GFKTLERSYL LRLDGKVAER PQHMLMRVSV
GIHGDDIDGA IETYNNLSQG WFTHASPTLF NAGTRRPQLS SCFLLTIEDD SIEGIYNTLK
TCAMISKSAG GIGLNVHKIR SKESYIAGTN GNSNGLVPML RVFNNTARYV DQGGNKRPGA
FAMYLEPWHA DIFEFLDLKK NTGSEEMRAR DLFFGLWIND LFMERCEADG EWSLFSPSDA
PGLDDVWGKE FEDLYHKYER EGRAKRVIKA QQLWFAILEA QTETGTPYML YKDACNRKSN
QQNLGTIKCS NLCCEIVEYS SPDEVAVCNL ASLALPKYVK TDGANGPEFD FVKLEEVTRI
ATRNLNKIID VNYYPVPEAE KSNKRHRPIG LGVQGLADAF ILMRLPFDSP DARVLNKHIF
ETIYYSAVTE SIAIAKREGP YETYAGSPAS KGILQFDMWD VVPSDRHDWA KVKENMALYG
LRNSLLVAPM PTASTAQILG NNESIEPYTS NIYTRRVLSG EFQIVNQHLL KDLTDLGLWD
TDMKNQLIAS GGSIQNITRI PEQLRDIYRT VWEMSQKSLI DMAADRGAYV CQSQSFNLFI
AEPNFGKLTS MHFYAYKKGL KTGMYYLRTR PAVNAIQFTV DTEKLAAAVK TASLRTAEEN
EEALLCSINN KDDCTMCSG
//
