Reviewed, UniProtKB/Swiss-Prot P79732 (RIR1_DANRE)

Names and origin

Protein names

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 names

Name:

rrm1

Organism

Danio rerio (Zebrafish) (Brachydanio rerio)

Taxonomic identifier

7955 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Ostariophysi › Cypriniformes › Cyprinidae › Danio

Protein attributes

Sequence length	794 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

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 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.
Pathway	Genetic information processing; DNA replication.
Subunit structure	Heterodimer of a large and a small subunit.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the ribonucleoside diphosphate reductase large chain family. Contains 1 ATP-cone domain.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Cytoplasm
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 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 – 794	794	Ribonucleoside-diphosphate reductase large subunit		PRO_0000187192
Regions
	Domain	1 – 92	92	ATP-cone
	Region	11 – 17	7	Allosteric activator binding By similarity
	Region	217 – 218	2	Substrate binding By similarity
	Region	285 – 288	4	Allosteric effector binding, determines substrate specificity By similarity
	Region	427 – 431	5	Substrate binding By similarity
	Region	603 – 607	5	Substrate binding By similarity
Sites
	Active site	427	1	Proton acceptor By similarity
	Active site	429	1	Cysteine radical intermediate By similarity
	Active site	431	1	Proton acceptor By similarity
	Binding site	5	1	Allosteric activator By similarity
	Binding site	53	1	Allosteric activator By similarity
	Binding site	88	1	Allosteric activator By similarity
	Binding site	202	1	Substrate By similarity
	Binding site	247	1	Substrate; via amide nitrogen By similarity
	Site	218	1	Important for hydrogen atom transfer By similarity
	Site	226	1	Allosteric effector binding, determines substrate specificity By similarity
	Site	256	1	Allosteric effector binding, determines substrate specificity By similarity
	Site	444	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	789	1	Interacts with thioredoxin/glutaredoxin By similarity
	Site	792	1	Interacts with thioredoxin/glutaredoxin By similarity
Amino acid modifications
	Disulfide bond	218 ↔ 444		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P79732-1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 128355C073B3908C	FASTA	794	89,816
	10 20 30 40 50 60 MHVIKRDGGQ EGVMFDKITS RIQKLCYGLN SDFVDPTQIT MKVIQGLYSG VTTVELDTLA 70 80 90 100 110 120 AETAATSTTK HPDYAILAAR IAVSNLHKET KKVFSEVMED LYNYVNPLNS RHSPMISKET 130 140 150 160 170 180 LDIVLANKDR LNSAIIYDRD FSYNFFGFKT LERSYLLKIN GKVAERPQHM LMRVSVGIHK 190 200 210 220 230 240 EDIAAAIETY NLLSEKWFTH ASPTLFNAGT NRPQLSSCFL LAMKDDSIEG IYDTLKQCAL 250 260 270 280 290 300 ISKSAGGIGV AVSCIRATGR YIAGTNGNSN GLVPMLRVNN NTARYVDQGG NKRPGAFAMY 310 320 330 340 350 360 LEPWHFDIFD FLELKKNTGK EEQRARDLFY ALWIPDLFMK RVETNGDWSL MCPNDCPGLD 370 380 390 400 410 420 ECWGEEFEKL YAKYEQEGRA KRVVKAQQLW YAIIESQTET GTPYMLYKDA CNRKSNRQNL 430 440 450 460 470 480 GTIKCSNLCT EIVEYTSADE VAVCNLASIA LNMYVTSERT FDFQKLASVT KVIVKNLNKI 490 500 510 520 530 540 IDINYYPVKE AENSNKRHRP IGIGVQGLAD AFILMRFPFE STEAQLLNTQ IFETIYYAAL 550 560 570 580 590 600 ESSCELAAEY GPYQTYAGCP VSKGILQYDM WEKTPTDLWD WAALKEKIAN DGVRNSLLLA 610 620 630 640 650 660 PMPTASTAQI LGNNESIEPY TSNIYHRRVL SGEFQIVNPH LLKDLTERGL WNEEMKNQII 670 680 690 700 710 720 AQNGSIQTIP AIPDDLKELY KTVWEISQKT ILKMAADRGA YIDQSQSLNI HIAEPNYGKL 730 740 750 760 770 780 TSMHFYGWKQ GLKTGMYYLR TKPGANPIQF TLNKEKLKET QKTTSSEDEE TKERNKAAMV 790 CSLENRHECL MCGS

References

[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: 8983196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	U57964 mRNA. Translation: AAB37102.1.
IPI	IPI00482388.
RefSeq	NP_571530.1.
UniGene	Dr.33356
3D structure databases
SMR	P79732. Positions 15-755.
ModBase	Search...
Protein-protein interaction databases
STRING	P79732.
Proteomic databases
PRIDE	P79732.
Genome annotation databases
Ensembl	ENSDART00000012091; ENSDARP00000010800; ENSDARG00000014017; Danio rerio. [Genome view]
GeneID	30740.
KEGG	dre:30740.
Organism-specific databases
CTD	30740.
ZFIN	ZDB-GENE-990415-247. rrm1.
Phylogenomic databases
eggNOG	fiNOG11747.
HOGENOM	HBG296647.
HOVERGEN	P79732.
InParanoid	P79732.
PhylomeDB	P79732.
Enzyme and pathway databases
BRENDA	1.17.4.1. 96826.
Gene expression databases
ArrayExpress	P79732.
Bgee	P79732.
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]
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_DANRE

Accession

Primary (citable) accession number: P79732

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	May 1, 1997
Last modified:	February 9, 2010
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Zebrafish annotation project