O61065 (RIR1_CRYPV) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonucleoside-diphosphate reductase large chain
EC=1.17.4.1

Alternative name(s):
Ribonucleotide reductase R1 subunit

Gene names

Name:

RNR1

Organism

Cryptosporidium parvum

Taxonomic identifier

5807 [NCBI]

Taxonomic lineage

Eukaryota › Alveolata › Apicomplexa › Coccidia › Eucoccidiorida › Eimeriorina › Cryptosporidiidae › Cryptosporidium

Protein attributes

Sequence length	803 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Catalytic activity	2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.
Enzyme regulation	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.
Pathway	Genetic information processing; DNA replication.
Subunit structure	Heterodimer of a large and a small subunit.
Sequence similarities	Belongs to the ribonucleoside diphosphate reductase large chain family. Contains 1 ATP-cone domain.

Ontologies

Keywords
Biological process	DNA replication
Ligand	ATP-binding Nucleotide-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Allosteric enzyme
Gene Ontology (GO)
Biological process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW deoxyribonucleotide biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	ribonucleoside-diphosphate reductase complex Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ribonucleoside-diphosphate reductase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 803	803	Ribonucleoside-diphosphate reductase large chain		PRO_0000187196
Regions
	Domain	1 – 91	91	ATP-cone
	Region	11 – 17	7	Allosteric activator binding By similarity
	Region	215 – 216	2	Substrate binding By similarity
	Region	283 – 286	4	Allosteric effector binding, determines substrate specificity By similarity
	Region	425 – 429	5	Substrate binding By similarity
	Region	603 – 607	5	Substrate binding By similarity
Sites
	Active site	425	1	Proton acceptor By similarity
	Active site	427	1	Cysteine radical intermediate By similarity
	Active site	429	1	Proton acceptor By similarity
	Binding site	52	1	Allosteric activator By similarity
	Binding site	87	1	Allosteric activator By similarity
	Binding site	200	1	Substrate By similarity
	Binding site	245	1	Substrate; via amide nitrogen By similarity
	Site	216	1	Important for hydrogen atom transfer By similarity
	Site	224	1	Allosteric effector binding, determines substrate specificity By similarity
	Site	254	1	Allosteric effector binding, determines substrate specificity By similarity
	Site	442	1	Important for hydrogen atom transfer By similarity
	Site	737	1	Important for electron transfer By similarity
	Site	738	1	Important for electron transfer By similarity
	Site	798	1	Interacts with thioredoxin/glutaredoxin By similarity
	Site	801	1	Interacts with thioredoxin/glutaredoxin By similarity
Amino acid modifications
	Disulfide bond	216 ↔ 442		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	O61065 [UniParc]. Last modified August 14, 2001. Version 2. Checksum: 9DBE7F2AC337F97F	FASTA	803	91,123
	10 20 30 40 50 60 MYVVNRKGEE EPVSFDQILS RITKLSYGLH PLVDPARVTQ AVINGLYSGI KTSELDELAS 70 80 90 100 110 120 QTCAYMAATH NDFSKLAARI STSNLHKNTS SDIGDVASQL YNFKDNQGCP APLISKPVYD 130 140 150 160 170 180 FIMENRERIN SKIDFSKDFE YDYFAFKTLE RSYLLKIDNK VVERPQHLLM RVSCGIHCGD 190 200 210 220 230 240 IEAALETYEL LSQKYFTHAT PTLFNSGTPR PQMSSCFLLR IPEDSINGIF DTLTKCANIS 250 260 270 280 290 300 KTAGGLGVAV SNIRGTGSYI RGTNGRSNGL IPMLRVYNDT ARYIDQGGGK RKGAIAIYLE 310 320 330 340 350 360 PWHVDVVEFI EIRKNHGKEE MRCRDLFPAL WVPDLFMERV EKDQDWTLMC PDECRGLQDV 370 380 390 400 410 420 WGDDFKKLYE EYEKQGRGRK TMKAQKLWFL ILQAQIETGT PFICYKDAAN SKSNQKNLGT 430 440 450 460 470 480 IVSSNLCTEI IEYTSTDEVA VCNLASIGLP KFVDKNNKTF DFDKLKEVTK VITRNLNKLI 490 500 510 520 530 540 DVGYYSLKEC KKSNLRHRPL GIGIQGLADC FMMLRMPYES EGAKKLNKQI FEVIYYAALD 550 560 570 580 590 600 ASCELAEKYG PYETYSGSPA SKGILQFDMW GVTPDSGLCD WDLLKDRISK HGIRNSLLIS 610 620 630 640 650 660 PMPTASTSQI LGNNESFEPF TSNIYHRRVL SGEFFVVNPH LLNDLLELGL WDDRLKQNII 670 680 690 700 710 720 ANNGSIQNIL TIPEDIRELY KTVWEIKQKT VIDMAADRGP YVCQSQSLNI HMENANFAKL 730 740 750 760 770 780 SSMHFYGWKK GLKTGIYYLR TQSATRPIQF TVDQQLLKSE TKEKDSLETN KRQALEPEAQ 790 800 KLIACPLRPT NMKDDEECMM CSG

References

[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: 12391728] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: GCH1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF043243 Genomic DNA. Translation: AAC12280.2.
3D structure databases
ProteinModelPortal	O61065.
SMR	O61065. Positions 15-789.
ModBase	Search...
Protein-protein interaction databases
STRING	O61065.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	KOG1112.
Family and domain databases
InterPro	IPR005144. ATP-cone. IPR013346. NrdE_NrdA. IPR013509. Ribncl_Rdtase_lsu_N. IPR000788. Ribncl_red_lg_C. IPR008926. Ribnucl_Rdtase_R1-su_N. [Graphical view]
Pfam	PF03477. ATP-cone. 1 hit. PF02867. Ribonuc_red_lgC. 1 hit. PF00317. Ribonuc_red_lgN. 1 hit. [Graphical view]
PRINTS	PR01183. RIBORDTASEM1.
SUPFAM	SSF48168. Ribonucleo_red_N. 1 hit.
TIGRFAMs	TIGR02506. NrdE_NrdA. 1 hit.
PROSITE	PS51161. ATP_CONE. 1 hit. PS00089. RIBORED_LARGE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RIR1_CRYPV

Accession

Primary (citable) accession number: O61065

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	August 14, 2001
Last modified:	December 14, 2011
This is version 65 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)