ID F1SUZ5_PIG Unreviewed; 776 AA.
AC F1SUZ5;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 5.
DT 27-MAR-2024, entry version 79.
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:ENSSSCP00000015710.5,
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:ENSSSCP00000015710.5, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000015710.5, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000015710.5,
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:ENSSSCP00000015710.5}
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; F1SUZ5; -.
DR PaxDb; 9823-ENSSSCP00000015710; -.
DR PeptideAtlas; F1SUZ5; -.
DR Ensembl; ENSSSCT00000016142.5; ENSSSCP00000015710.5; ENSSSCG00000014791.5.
DR VGNC; VGNC:92461; RRM1.
DR GeneTree; ENSGT00910000144246; -.
DR HOGENOM; CLU_000404_1_0_1; -.
DR TreeFam; TF300578; -.
DR Proteomes; UP000008227; Chromosome 9.
DR Bgee; ENSSSCG00000014791; Expressed in hindlimb bud and 43 other cell types or tissues.
DR ExpressionAtlas; F1SUZ5; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:InterPro.
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 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:F1SUZ5};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT DOMAIN 1..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 776 AA; 88257 MW; CF77E04BC2D6CB88 CRC64;
MHVIKRDGRQ ERVMFDKITS RIQKLCYGLN MDFVDPAQIT MKVIQGLYSG VTTVELDTLA
AETAATLTTK HPDYAILAAR IAVSNLHKET KKVFSDVMED LFNYINPHNG KHSPMVASTL
DIVLANKDRL NSAIIYDRDF SYNYFGFKAE RPQHMLMRVS VGIHKEDIDA AIETYNLLSE
KWFTHASPTL FNAGTNRPQL SSCFLLSMKD DSIEGIYDTL KQCALISKSA GGIGVAVSCI
RATGSYIAGT NGNSNGLVPM LRVYNNTARY VDQGGNKRPG AFAIYLEPWH LDIFEFLDLK
KNTGKEEQRA RDLFFALWIP DLFMKRVETN QDWSLMCPNE CPGLDEVWGE EFEKLYESYE
RQGHVRKVVK AQQLWYAIIE SQTETGTPYM LYKDSCNRKS NQQNLGTIKC SNLCTEIVEY
TSKDEVAVCN LASLALNMYV TSEHTYDFTK LAEVTKVIVR NLNKIIDINY YPIPEASLSN
KRHRPIGIGV QGLADAFILM RYPFESPEAQ LLNKQIFETI YYGALEASCD LAKEYGPYET
YEGSPVSKGI LQYDMWNVTP TDLWDWKLLK EKIAKYGIRN SLLIAPMPTA STAQILGNNE
SIEPYTSNIY TRRVLSGEFQ IVNPHLLKDL TERGLWNEEM KNQIIACNGS IQSIPEIPDD
LKQLYKTVWE ISQKTVLKMA AERGAFIDQS QSLNIHIAEP NYGKLTSMHF YGWKQGLKTG
MYYLRTRPAA NPIQFTLNKE KLKDKEKVSK EEEKERNTAA MVCSLENRDE CLMCGS
//
