Reviewed, UniProtKB/Swiss-Prot P50647 (RIR1_PLAFG)

Names and origin

Protein names

Recommended name:
    Ribonucleoside-diphosphate reductase large subunit
    EC=1.17.4.1
Alternative name(s):
    Ribonucleotide reductase R1 subunit

Gene names

Name:

RNR1

Organism

Plasmodium falciparum (isolate FCR-3 / Gambia)

Taxonomic identifier

5838 [NCBI]

Taxonomic lineage

Eukaryota › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodium › Plasmodium (Laverania)

Protein attributes

Sequence length	804 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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
Technical term	Allosteric enzyme
Gene Ontology (GO)
Biological process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	ribonucleoside-diphosphate reductase complex Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from electronic annotation. Source: InterPro ribonucleoside-diphosphate reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 804	804	Ribonucleoside-diphosphate reductase large subunit		PRO_0000187197
Regions
	Domain	1 – 92	92	ATP-cone
Sites
	Active site	217	1	Hydrogen atom transfer By similarity
	Active site	425	1	Proton acceptor By similarity
	Active site	427	1	Proton acceptor By similarity
	Active site	429	1	Proton acceptor By similarity
	Active site	442	1	Hydrogen atom transfer By similarity
	Active site	736	1	Electron transfer By similarity
	Active site	737	1	Electron transfer By similarity
	Site	225	1	Allosteric effector binding By similarity
	Site	255	1	Allosteric effector binding By similarity
	Site	799	1	Interacts with thioredoxin/glutaredoxin By similarity
	Site	802	1	Interacts with thioredoxin/glutaredoxin By similarity

Sequences

	Sequence		Length	Mass (Da)
	P50647-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 8D3C70EA2ED0A6E9	FASTA	804	92,403
	10 20 30 40 50 60 MYVLNRKGEE EDISFDQILK RIQRLSYGLH KLGEYPACVT QGVINGMYSS IKTCELDELA 70 80 90 100 110 120 AQTCAYMATT HPDFSILAAR ITTDNLHKNT SDDVAEVAEA LYTYKDGRGR PASLISKEVY 130 140 150 160 170 180 DFILLHKVRL NKEIDYTTHF NYDYFGFKTL ERSYLLRINN KIIERPQHLL MRVSIGIHID 190 200 210 220 230 240 DIDKALETYH LMSQKYFTHA TPTLFNSGTP RPQMSSCFLL SMKADSIEGI FETLKQCALI 250 260 270 280 290 300 SKTAGGIGVA VQDIRGQNSY IRGTNGISNG LVPMLRVFND TARYVDQGGG KRKGSYAVYI 310 320 330 340 350 360 EPWHSDIFEF LDLRKNHGKE ELRARDLFYA VWVPDLFMKR VKENKNWTLM CPNECPGLSE 370 380 390 400 410 420 TWGEEFEKLY TKYEEENMGK KTVLAQDLWF AILQSQIETG VPIYLYKDSC NAKPIKNLGT 430 440 450 460 470 480 IKCSNLCCEI IEYTSPDEVA VCNLASIALC KFVDLEKKEF NFKKLYEITK IITRNLDKII 490 500 510 520 530 540 ERNYYPVKEA KTSNTRHRPI GIGVQGLADT FMLLRYLYES DAAKELNKRI YETMYYAALE 550 560 570 580 590 600 MSVDWLQSGP YESYQGSPGS QGILQFDMWN AKVDNKYWDW DELKLKIAKT GLRNLLLLAP 610 620 630 640 650 660 MPTASTSQIL GNNESFEPYT SNIYYRRVLS GEFFVVNPHL LKDLFDRGLW DEDMKQQLIA 670 680 690 700 710 720 HNGSIQYISE IPDDLKELYK TVWEIKQKNI IDMAADRGYF IDQSQSLNIY IQKPTFAKLS 730 740 750 760 770 780 SMHFYGWEKG LKTGAYYLRT QAATDAIKFT VDTHVAKNAV KLKNADGVQI TREVSRETIQ 790 800 LNQRYSKCVS FKSNNDEQCL MCSG

References

[1]

"Cloning, sequence determination, and regulation of the ribonucleotide reductase subunits from Plasmodium falciparum: a target for antimalarial therapy." Rubin H., Salem J.S., Li L.S., Yang F.D., Mama S., Wang Z.M., Fisher A., Hamann C.S., Cooperman B.S. Proc. Natl. Acad. Sci. U.S.A. 90:9280-9284(1993) [PubMed: 8415692] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF205580 Genomic DNA. Translation: AAA29755.1.
PIR	B48687.
3D structure databases
ModBase	Search...
Family and domain databases
InterPro	IPR005144. ATP-cone. IPR013346. NrdE_NrdA. IPR013509. Ribncl_Rdtase_lsu_N. IPR000788. Ribncl_red_lg_C. [Graphical view]
PANTHER	PTHR11573. Ribncl_red_lg_C. 1 hit.
Pfam	PF03477. ATP-cone. 1 hit. PF02867. Ribonuc_red_lgC. 1 hit. PF00317. Ribonuc_red_lgN. 1 hit. [Graphical view]
PRINTS	PR01183. RIBORDTASEM1.
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_PLAFG

Accession

Primary (citable) accession number: P50647

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)