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P79732

- RIR1_DANRE

UniProt

P79732 - RIR1_DANRE

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Protein
Ribonucleoside-diphosphate reductase large subunit
Gene
rrm1
Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.

Catalytic activityi

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.

Enzyme regulationi

Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding to separate specificity and activation sites on the M1 subunit. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction. Stimulated by ATP and inhibited by dATP binding to the activity site By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei5 – 51Allosteric activator By similarity
Binding sitei53 – 531Allosteric activator By similarity
Binding sitei88 – 881Allosteric activator By similarity
Binding sitei202 – 2021Substrate By similarity
Sitei218 – 2181Important for hydrogen atom transfer By similarity
Sitei226 – 2261Allosteric effector binding, determines substrate specificity By similarity
Binding sitei247 – 2471Substrate; via amide nitrogen By similarity
Sitei256 – 2561Allosteric effector binding, determines substrate specificity By similarity
Active sitei427 – 4271Proton acceptor By similarity
Active sitei429 – 4291Cysteine radical intermediate By similarity
Active sitei431 – 4311Proton acceptor By similarity
Sitei444 – 4441Important for hydrogen atom transfer By similarity
Sitei737 – 7371Important for electron transfer By similarity
Sitei738 – 7381Important for electron transfer By similarity
Sitei789 – 7891Interacts with thioredoxin/glutaredoxin By similarity
Sitei792 – 7921Interacts with thioredoxin/glutaredoxin By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Source: UniProtKB

GO - Biological processi

  1. DNA replication Source: UniProtKB-UniPathway
  2. deoxyribonucleotide biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00326.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonucleoside-diphosphate reductase large subunit (EC:1.17.4.1)
Alternative name(s):
Ribonucleoside-diphosphate reductase subunit M1
Ribonucleotide reductase large subunit
Ribonucleotide reductase protein R1 class I
Gene namesi
Name:rrm1
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
ProteomesiUP000000437: Unplaced

Organism-specific databases

ZFINiZDB-GENE-990415-247. rrm1.

Subcellular locationi

GO - Cellular componenti

  1. ribonucleoside-diphosphate reductase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 794794Ribonucleoside-diphosphate reductase large subunit
PRO_0000187192Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi218 ↔ 444Redox-active By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP79732.

Interactioni

Subunit structurei

Heterodimer of a large and a small subunit.

Protein-protein interaction databases

STRINGi7955.ENSDARP00000010800.

Structurei

3D structure databases

ProteinModelPortaliP79732.
SMRiP79732. Positions 15-755.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9292ATP-cone
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 177Allosteric activator binding By similarity
Regioni217 – 2182Substrate binding By similarity
Regioni285 – 2884Allosteric effector binding, determines substrate specificity By similarity
Regioni427 – 4315Substrate binding By similarity
Regioni603 – 6075Substrate binding By similarity

Sequence similaritiesi

Contains 1 ATP-cone domain.

Phylogenomic databases

eggNOGiCOG0209.
HOGENOMiHOG000057035.
HOVERGENiHBG003447.
InParanoidiP79732.
PhylomeDBiP79732.

Family and domain databases

InterProiIPR005144. ATP-cone.
IPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamiPF03477. ATP-cone. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSiPR01183. RIBORDTASEM1.
SUPFAMiSSF48168. SSF48168. 1 hit.
TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
PROSITEiPS51161. ATP_CONE. 1 hit.
PS00089. RIBORED_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P79732-1 [UniParc]FASTAAdd to Basket

« Hide

MHVIKRDGGQ EGVMFDKITS RIQKLCYGLN SDFVDPTQIT MKVIQGLYSG    50
VTTVELDTLA AETAATSTTK HPDYAILAAR IAVSNLHKET KKVFSEVMED 100
LYNYVNPLNS RHSPMISKET LDIVLANKDR LNSAIIYDRD FSYNFFGFKT 150
LERSYLLKIN GKVAERPQHM LMRVSVGIHK EDIAAAIETY NLLSEKWFTH 200
ASPTLFNAGT NRPQLSSCFL LAMKDDSIEG IYDTLKQCAL ISKSAGGIGV 250
AVSCIRATGR YIAGTNGNSN GLVPMLRVNN NTARYVDQGG NKRPGAFAMY 300
LEPWHFDIFD FLELKKNTGK EEQRARDLFY ALWIPDLFMK RVETNGDWSL 350
MCPNDCPGLD ECWGEEFEKL YAKYEQEGRA KRVVKAQQLW YAIIESQTET 400
GTPYMLYKDA CNRKSNRQNL GTIKCSNLCT EIVEYTSADE VAVCNLASIA 450
LNMYVTSERT FDFQKLASVT KVIVKNLNKI IDINYYPVKE AENSNKRHRP 500
IGIGVQGLAD AFILMRFPFE STEAQLLNTQ IFETIYYAAL ESSCELAAEY 550
GPYQTYAGCP VSKGILQYDM WEKTPTDLWD WAALKEKIAN DGVRNSLLLA 600
PMPTASTAQI LGNNESIEPY TSNIYHRRVL SGEFQIVNPH LLKDLTERGL 650
WNEEMKNQII AQNGSIQTIP AIPDDLKELY KTVWEISQKT ILKMAADRGA 700
YIDQSQSLNI HIAEPNYGKL TSMHFYGWKQ GLKTGMYYLR TKPGANPIQF 750
TLNKEKLKET QKTTSSEDEE TKERNKAAMV CSLENRHECL MCGS 794
Length:794
Mass (Da):89,816
Last modified:May 1, 1997 - v1
Checksum:i128355C073B3908C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U57964 mRNA. Translation: AAB37102.1.
UniGeneiDr.33356.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U57964 mRNA. Translation: AAB37102.1 .
UniGenei Dr.33356.

3D structure databases

ProteinModelPortali P79732.
SMRi P79732. Positions 15-755.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 7955.ENSDARP00000010800.

Proteomic databases

PRIDEi P79732.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

ZFINi ZDB-GENE-990415-247. rrm1.

Phylogenomic databases

eggNOGi COG0209.
HOGENOMi HOG000057035.
HOVERGENi HBG003447.
InParanoidi P79732.
PhylomeDBi P79732.

Enzyme and pathway databases

UniPathwayi UPA00326 .

Miscellaneous databases

NextBioi 20807088.
PROi P79732.

Family and domain databases

InterProi IPR005144. ATP-cone.
IPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view ]
Pfami PF03477. ATP-cone. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view ]
PRINTSi PR01183. RIBORDTASEM1.
SUPFAMi SSF48168. SSF48168. 1 hit.
TIGRFAMsi TIGR02506. NrdE_NrdA. 1 hit.
PROSITEi PS51161. ATP_CONE. 1 hit.
PS00089. RIBORED_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and sequencing of cDNAs encoding ribonucleotide reductase from zebrafish Danio rerio."
    Mathews C.Z., Sjoeberg B.-M., Karlsson M.
    Mol. Mar. Biol. Biotechnol. 5:284-287(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiRIR1_DANRE
AccessioniPrimary (citable) accession number: P79732
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 1, 1997
Last modified: June 11, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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