ID H2NEH7_PONAB Unreviewed; 792 AA.
AC H2NEH7; A0A2J8R1V6; A0A6D2WI44;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
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:ENSPPYP00000004146.2};
GN ORFNames=CR201_G0054770 {ECO:0000313|EMBL:PNJ02501.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000004146.2, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000004146.2, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PNJ02501.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ02501.1};
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPPYP00000004146.2}
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 EMBL; NDHI03003808; PNJ02501.1; -; Genomic_DNA.
DR Ensembl; ENSPPYT00000004316.3; ENSPPYP00000004146.2; ENSPPYG00000003625.3.
DR GeneTree; ENSGT00910000144246; -.
DR HOGENOM; CLU_000404_1_0_1; -.
DR OMA; QMSSCYL; -.
DR TreeFam; TF300578; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000001595; Chromosome 11.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-EC.
DR GO; GO:0009265; P:2'-deoxyribonucleotide biosynthetic process; IEA:Ensembl.
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:UP000001595}.
FT DOMAIN 1..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 792 AA; 90084 MW; 05DA76676198296A CRC64;
MHVIKRDGRQ ERVMFDKITS RIQKLCYGLN MDFVDPAQIT MKVIQGLYSG VTTVELDTLA
AETAATLTTK HPDYAILAAR IAVSNLHKET KKVFSDVMED LYNYINPHNG KHSPMVAKST
LDIVLANKDR LNSAIIYDRD FSYNYFGFKT LERSYLLKIN GKVAERPQHM LMRVSVGIHK
EDIDAAIETY NLLSERWFTH ASPTLFNAGT NRPQLSSCFL LSMKDDSIEG IYDTLKQCAL
ISKSAGGIGV AVSCIRATGS YIAGTNGNSN GLVPMLRVYN NTARYVDQGG NKRPGAFAIY
LEPWHLDIFE FLDLKKNTGK EEQRARDLFF ALWIPDLFMK RVETNQDWSL MCPNECPGLD
EVWGEEFEKL YASYEKQGRV RKVVKAQQLW YAIIESQTET GTPYMLYKDS CNRKSNQQNL
GTIKCSNLCT EIVEYTSKDE VAVCNLASLA LNMYVTSEHT YDFKKLAEVT KVVVRNLNKI
IDINYYPVPE ACLSNKRHRP IGIGVQGLAD AFILMRYPFE SAEAQLLNKQ IFETIYYGAL
EASCDLAKEQ GPYETYEGSP VSKGILQYDM WNVTPTDLWD WKLLKEKIAK YGIRNSLLIA
PMPTASTAQI LGNNESIEPY TSNIYTRRVL SGEFQIVNPH LLKDLTERGL WHEEMKNQII
ACNGSIQSIP EIPDDLKQLY KTVWEISQKT VLKMAAERGA FIDQSQSLNI HIAEPNYGKL
TSMHFYGWKQ GLKTGMYYLR TRPAANPIQF TLNKEKLKDK EKVSKEEEEK ERNTAAMVCS
LENRDECLMC GS
//
