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Protein

Ribonucleoside-diphosphate reductase large chain

Gene

ECU10_0920

Organism
Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity).By similarity

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 large 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).By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei196 – 1961SubstrateBy similarity
Sitei212 – 2121Important for hydrogen atom transferBy similarity
Sitei220 – 2201Allosteric effector binding, determines substrate specificityBy similarity
Binding sitei241 – 2411Substrate; via amide nitrogenBy similarity
Sitei250 – 2501Allosteric effector binding, determines substrate specificityBy similarity
Active sitei420 – 4201Proton acceptorBy similarity
Active sitei422 – 4221Cysteine radical intermediateBy similarity
Active sitei424 – 4241Proton acceptorBy similarity
Sitei437 – 4371Important for hydrogen atom transferBy similarity
Sitei729 – 7291Important for electron transferBy similarity
Sitei730 – 7301Important for electron transferBy similarity
Sitei763 – 7631Interacts with thioredoxin/glutaredoxinBy similarity
Sitei766 – 7661Interacts with thioredoxin/glutaredoxinBy 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. deoxyribonucleotide biosynthetic process Source: UniProtKB
  2. DNA replication Source: UniProtKB-UniPathway
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 chain (EC:1.17.4.1)
Alternative name(s):
Ribonucleotide reductase
Gene namesi
Ordered Locus Names:ECU10_0920
OrganismiEncephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)
Taxonomic identifieri284813 [NCBI]
Taxonomic lineageiEukaryotaFungiMicrosporidiaUnikaryonidaeEncephalitozoon
ProteomesiUP000000819 Componenti: Chromosome X

Organism-specific databases

EuPathDBiMicrosporidiaDB:ECU10_0920.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 768768Ribonucleoside-diphosphate reductase large chainPRO_0000187200Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi212 ↔ 437Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ8SR37.

Interactioni

Subunit structurei

Heterodimer of a large and a small subunit.By similarity

Protein-protein interaction databases

STRINGi6035.ECU10_0920.

Structurei

3D structure databases

ProteinModelPortaliQ8SR37.
SMRiQ8SR37. Positions 79-734.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni211 – 2122Substrate bindingBy similarity
Regioni279 – 2824Allosteric effector binding, determines substrate specificityBy similarity
Regioni420 – 4245Substrate bindingBy similarity
Regioni595 – 5995Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0209.
HOGENOMiHOG000057035.
InParanoidiQ8SR37.
KOiK10807.
OMAiYELLWQM.
OrthoDBiEOG7C5MHR.

Family and domain databases

InterProiIPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamiPF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSiPR01183. RIBORDTASEM1.
SUPFAMiSSF48168. SSF48168. 1 hit.
TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
PROSITEiPS00089. RIBORED_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8SR37-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENFSNSKRI KSEKLGIDLI RSRIEGYVKD LKLRHVDVDE LVERIVSGWC
60 70 80 90 100
EDMTRKETID YCSETAASMI TKHPEYGQIS SRIIVSYIHE ITMDSFVEKI
110 120 130 140 150
KYIQKHRGMV SEEMYGIILE HGETIEGMIN YENDFLFSYF GILTLMKSYL
160 170 180 190 200
IKVGEEIIER PQDMFMRVAL QIHKTDFEKV REVYNLLSGH YFTHATPTLY
210 220 230 240 250
NSCLKNPQLA SCFLITPRED SIEGVYHMIN QAAIITKYSG GIGLNLHGIR
260 270 280 290 300
SKGSSLRSTG GRSNGIIPLI QVLNATKRYI NQGAERRPGS IAIFLEPWHM
310 320 330 340 350
EIFDFLELRK NTGPEEFRAR DIFTALWIND LFMERVKNNE EWSLFCPSQA
360 370 380 390 400
VGLSDVWGEE FNALYCKYEK TISRTVVPAQ KLWKAIIEAQ IETGTPYMCY
410 420 430 440 450
KDACNRLSNQ QHLGTIKSSN LCAEIVEYSS GEETSVCNLA SICLPMFVKD
460 470 480 490 500
GWFDFEAFRR VVKILTVNLN RVIDFNYYPV EEARRSNMRN RPIGIGVQGL
510 520 530 540 550
ADLFAILRLA FESDGARSLN QDIFEAMYYS AMEASCELAE KEGPFPSYEG
560 570 580 590 600
SPISKGIFHF ELAGRKASGN WDWEGLRERI RRHGVRNSLL IALMPTAGTS
610 620 630 640 650
QIFGNNEAFE PHASNIYTRR THAGEFQIVN QHLVNDLVRL GLWSYEMKNL
660 670 680 690 700
VIENEGSIQN ITSIPHEIRE IYKTAWEIKM KSVIDLAADR QVFVDQSQSL
710 720 730 740 750
NIFIAKPTYS QLTSMHFYGY HCGLKTGMYY LRTRPITSAI KFTVDKKLAE
760
KTLSSMNDTD DPCSMCSS
Length:768
Mass (Da):87,941
Last modified:May 31, 2002 - v1
Checksum:i3E6BF6826805E20D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL590449 Genomic DNA. Translation: CAD25811.1.
RefSeqiNP_586207.1. NM_001042040.1.

Genome annotation databases

GeneIDi859856.
KEGGiecu:ECU10_0920.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL590449 Genomic DNA. Translation: CAD25811.1.
RefSeqiNP_586207.1. NM_001042040.1.

3D structure databases

ProteinModelPortaliQ8SR37.
SMRiQ8SR37. Positions 79-734.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6035.ECU10_0920.

Proteomic databases

PRIDEiQ8SR37.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi859856.
KEGGiecu:ECU10_0920.

Organism-specific databases

EuPathDBiMicrosporidiaDB:ECU10_0920.

Phylogenomic databases

eggNOGiCOG0209.
HOGENOMiHOG000057035.
InParanoidiQ8SR37.
KOiK10807.
OMAiYELLWQM.
OrthoDBiEOG7C5MHR.

Enzyme and pathway databases

UniPathwayiUPA00326.

Family and domain databases

InterProiIPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamiPF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSiPR01183. RIBORDTASEM1.
SUPFAMiSSF48168. SSF48168. 1 hit.
TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
PROSITEiPS00089. RIBORED_LARGE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: GB-M1.

Entry informationi

Entry nameiRIR1_ENCCU
AccessioniPrimary (citable) accession number: Q8SR37
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2004
Last sequence update: May 31, 2002
Last modified: January 6, 2015
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.