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O61065

- RIR1_CRYPV

UniProt

O61065 - RIR1_CRYPV

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Protein

Ribonucleoside-diphosphate reductase large chain

Gene

RNR1

Organism
Cryptosporidium parvum
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

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 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 sitei52 – 521Allosteric activatorBy similarity
Binding sitei87 – 871Allosteric activatorBy similarity
Binding sitei200 – 2001SubstrateBy similarity
Sitei216 – 2161Important for hydrogen atom transferBy similarity
Sitei224 – 2241Allosteric effector binding, determines substrate specificityBy similarity
Binding sitei245 – 2451Substrate; via amide nitrogenBy similarity
Sitei254 – 2541Allosteric effector binding, determines substrate specificityBy similarity
Active sitei425 – 4251Proton acceptorBy similarity
Active sitei427 – 4271Cysteine radical intermediateBy similarity
Active sitei429 – 4291Proton acceptorBy similarity
Sitei442 – 4421Important for hydrogen atom transferBy similarity
Sitei737 – 7371Important for electron transferBy similarity
Sitei738 – 7381Important for electron transferBy similarity
Sitei798 – 7981Interacts with thioredoxin/glutaredoxinBy similarity
Sitei801 – 8011Interacts 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 R1 subunit
Gene namesi
Name:RNR1
OrganismiCryptosporidium parvum
Taxonomic identifieri5807 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaConoidasidaCoccidiaEucoccidioridaEimeriorinaCryptosporidiidaeCryptosporidium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 803803Ribonucleoside-diphosphate reductase large chainPRO_0000187196Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi216 ↔ 442Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Heterodimer of a large and a small subunit.

Structurei

3D structure databases

ProteinModelPortaliO61065.
SMRiO61065. Positions 15-789.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9191ATP-conePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 177Allosteric activator bindingBy similarity
Regioni215 – 2162Substrate bindingBy similarity
Regioni283 – 2864Allosteric effector binding, determines substrate specificityBy similarity
Regioni425 – 4295Substrate bindingBy similarity
Regioni603 – 6075Substrate bindingBy similarity

Sequence similaritiesi

Contains 1 ATP-cone domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0209.

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.

O61065-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MYVVNRKGEE EPVSFDQILS RITKLSYGLH PLVDPARVTQ AVINGLYSGI
60 70 80 90 100
KTSELDELAS QTCAYMAATH NDFSKLAARI STSNLHKNTS SDIGDVASQL
110 120 130 140 150
YNFKDNQGCP APLISKPVYD FIMENRERIN SKIDFSKDFE YDYFAFKTLE
160 170 180 190 200
RSYLLKIDNK VVERPQHLLM RVSCGIHCGD IEAALETYEL LSQKYFTHAT
210 220 230 240 250
PTLFNSGTPR PQMSSCFLLR IPEDSINGIF DTLTKCANIS KTAGGLGVAV
260 270 280 290 300
SNIRGTGSYI RGTNGRSNGL IPMLRVYNDT ARYIDQGGGK RKGAIAIYLE
310 320 330 340 350
PWHVDVVEFI EIRKNHGKEE MRCRDLFPAL WVPDLFMERV EKDQDWTLMC
360 370 380 390 400
PDECRGLQDV WGDDFKKLYE EYEKQGRGRK TMKAQKLWFL ILQAQIETGT
410 420 430 440 450
PFICYKDAAN SKSNQKNLGT IVSSNLCTEI IEYTSTDEVA VCNLASIGLP
460 470 480 490 500
KFVDKNNKTF DFDKLKEVTK VITRNLNKLI DVGYYSLKEC KKSNLRHRPL
510 520 530 540 550
GIGIQGLADC FMMLRMPYES EGAKKLNKQI FEVIYYAALD ASCELAEKYG
560 570 580 590 600
PYETYSGSPA SKGILQFDMW GVTPDSGLCD WDLLKDRISK HGIRNSLLIS
610 620 630 640 650
PMPTASTSQI LGNNESFEPF TSNIYHRRVL SGEFFVVNPH LLNDLLELGL
660 670 680 690 700
WDDRLKQNII ANNGSIQNIL TIPEDIRELY KTVWEIKQKT VIDMAADRGP
710 720 730 740 750
YVCQSQSLNI HMENANFAKL SSMHFYGWKK GLKTGIYYLR TQSATRPIQF
760 770 780 790 800
TVDQQLLKSE TKEKDSLETN KRQALEPEAQ KLIACPLRPT NMKDDEECMM

CSG
Length:803
Mass (Da):91,123
Last modified:August 14, 2001 - v2
Checksum:i9DBE7F2AC337F97F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043243 Genomic DNA. Translation: AAC12280.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043243 Genomic DNA. Translation: AAC12280.2 .

3D structure databases

ProteinModelPortali O61065.
SMRi O61065. Positions 15-789.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0209.

Enzyme and pathway databases

UniPathwayi UPA00326 .

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. "Molecular characterization of ribonucleotide reductase from Cryptosporidium parvum."
    Akiyoshi D.E., Balakrishnan R., Huettinger C., Widmer G., Tzipori S.
    DNA Seq. 13:167-172(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: GCH1.

Entry informationi

Entry nameiRIR1_CRYPV
AccessioniPrimary (citable) accession number: O61065
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 14, 2001
Last modified: October 29, 2014
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme

Documents

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

External Data

Dasty 3