ID F6YYG9_HORSE Unreviewed; 804 AA.
AC F6YYG9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
GN Name=RRM1 {ECO:0000313|Ensembl:ENSECAP00000021481.2,
GN ECO:0000313|VGNC:VGNC:22582};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000021481.2, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000021481.2, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000021481.2,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000021481.2}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000021481.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00000206,
CC 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 AlphaFoldDB; F6YYG9; -.
DR STRING; 9796.ENSECAP00000021481; -.
DR PaxDb; 9796-ENSECAP00000021481; -.
DR Ensembl; ENSECAT00000025802.3; ENSECAP00000021481.2; ENSECAG00000023847.4.
DR CTD; 6240; -.
DR VGNC; VGNC:22582; RRM1.
DR GeneTree; ENSGT00910000144246; -.
DR HOGENOM; CLU_000404_1_0_1; -.
DR InParanoid; F6YYG9; -.
DR OMA; QMSSCYL; -.
DR OrthoDB; 5472715at2759; -.
DR TreeFam; TF300578; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000002281; Chromosome 7.
DR Bgee; ENSECAG00000023847; Expressed in bone marrow and 23 other cell types or tissues.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
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:0097718; F:disordered domain specific binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IBA:GO_Central.
DR GO; GO:0009265; P:2'-deoxyribonucleotide biosynthetic process; IEA:Ensembl.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:Ensembl.
DR GO; GO:0006264; P:mitochondrial DNA replication; IEA:Ensembl.
DR GO; GO:0070318; P:positive regulation of G0 to G1 transition; IEA:Ensembl.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0051290; P:protein heterotetramerization; IEA:Ensembl.
DR GO; GO:0009185; P:ribonucleoside diphosphate metabolic process; IEA:Ensembl.
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:UP000002281}.
FT DOMAIN 4..104
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 804 AA; 91613 MW; CB5F2AAAB0ACB7F7 CRC64;
MILTLILKEK INHYWKFSDG RQERVMFDKI TSRIQKLCYG LNMDFVDPAQ ITMKVIQGLY
SGVTTVELDT LAAETAATLT TKHPDYAILA ARIAVSNLHK ETKKVFSDVM EDLYNYINPH
NGKHSPMVAK PTLDIVLANK DRLNSAIIYD RDFSYNYFGF KTLERSYLLK INGKVAERPQ
HMLMRVSVGI HSEDIDAAIE TYNLLSEKWF THASPTLFNA GTNRPQLSSC FLLSMKDDSI
EGIYDTLKQC ALISKSAGGI GVAVSCIRAT GSYIAGTNGN SNGLVPMLRV YNNTARYVDQ
GGNKRPGAFA IYLEPWHLDI FEFLDLKKNT GKEEQRARDL FFALWIPDLF MKRVESNQDW
SLMCPNECPG LDEVWGEEFE KLYESYEKQG RVRKVVKAQQ LWYAIIESQT ETGTPYMLYK
DSCNRKSNQQ NLGTIKCSNL CTEIVEYTSK DEVAVCNLAS LALNMFVTSE HTYDFQKLAE
VTKVIVRNLN KIIDINYYPI PEACLSNKRH RPIGIGVQGL ADAFILMRYP FESPEAQLLN
KQIFETIYYG ALEASCDLSR EDGPYETYEG SPVSKGILQY DMWNVTPTDL WDWKLLKEKI
AKYGVRNSLL IAPMPTASTA QILGNNESIE PYTSNIYTRR VLSGEFQIVN PHLLKDLTER
GLWNEEMKNQ IIACNGSIQS IQEIPDDLKQ LYKTVWEISQ KTILKMAAER GAFIDQSQSL
NIHIAEPNYG KLTSMHFYGW KQGLKTGMYY LRTRPAANPI QFTLNKEKLK DKEKASKEEE
EKERNTAAMV CSLENRDECL MCGS
//
