ID A0A287A8J7_PIG Unreviewed; 790 AA.
AC A0A287A8J7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 32.
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:ENSSSCP00000040138.2,
GN ECO:0000313|VGNC:VGNC:92461};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000040138.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000040138.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000040138.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000040138.2}
RP IDENTIFICATION.
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; A0A287A8J7; -.
DR SMR; A0A287A8J7; -.
DR STRING; 9823.ENSSSCP00000040138; -.
DR PaxDb; 9823-ENSSSCP00000022494; -.
DR Ensembl; ENSSSCT00000050049.3; ENSSSCP00000040138.2; ENSSSCG00000014791.5.
DR VGNC; VGNC:92461; RRM1.
DR eggNOG; KOG1112; Eukaryota.
DR GeneTree; ENSGT00910000144246; -.
DR InParanoid; A0A287A8J7; -.
DR Reactome; R-SSC-499943; Interconversion of nucleotide di- and triphosphates.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000008227; Chromosome 9.
DR Bgee; ENSSSCG00000014791; Expressed in hindlimb bud and 43 other cell types or tissues.
DR ExpressionAtlas; A0A287A8J7; baseline and differential.
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 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:A0A287A8J7};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT DOMAIN 1..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 790 AA; 89846 MW; 34C79972DCCB4B34 CRC64;
MHVIKRDGRQ ERVMFDKITS RIQKLCYGLN MDFVDPAQIT MKVIQGLYSG VTTVELDTLA
AETAATLTTK HPDYAILAAR IAVSNLHKET KKVFSDVMED LFNYINPHNG KHSPMVASTL
DIVLANKDRL NSAIIYDRDF SYNYFGFKTL ERSYLLKISG KVAERPQHML MRVSVGIHKE
DIDAAIETYN LLSEKWFTHA SPTLFNAGTN RPQLSSCFLL SMKDDSIEGI YDTLKQCALI
SKSAGGIGVA VSCIRATGSY IAGTNGNSNG LVPMLRVYNN TARYVDQGGN KRPGAFAIYL
EPWHLDIFEF LDLKKNTGKE EQRARDLFFA LWIPDLFMKR VETNQDWSLM CPNECPGLDE
VWGEEFEKLY ESYERQGHVR KVVKAQQLWY AIIESQTETG TPYMLYKDSC NRKSNQQNLG
TIKCSNLCTE IVEYTSKDEV AVCNLASLAL NMYVTSEHTY DFTKLAEVTK VIVRNLNKII
DINYYPIPEA SLSNKRHRPI GIGVQGLADA FILMRYPFES PEAQLLNKQI FETIYYGALE
ASCDLAKEYG PYETYEGSPV SKGILQYDMW NVTPTDLWDW KLLKEKIAKY GIRNSLLIAP
MPTASTAQIL GNNESIEPYT SNIYTRRVLS GEFQIVNPHL LKDLTERGLW NEEMKNQIIA
CNGSIQSIPE IPDDLKQLYK TVWEISQKTV LKMAAERGAF IDQSQSLNIH IAEPNYGKLT
SMHFYGWKQG LKTGMYYLRT RPAANPIQFT LNKEKLKDKE KVSKEEEKER NTAAMVCSLE
NRDECLMCGS
//
