Reviewed, UniProtKB/Swiss-Prot Q5R919 (RIR1_PONAB)

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

Gene names

Name:

RRM1

Organism

Pongo abelii (Sumatran orangutan)

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length	792 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 By similarity.
Catalytic activity	2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.
Enzyme regulation	Under complex allosteric control mediated by the binding of deoxynucleoside triphosphates and ATP to binding sites on the M1 subunit By similarity.
Pathway	Genetic information processing; DNA replication.
Subunit structure	Heterodimer of a large and a small subunit. Interacts with RRM2B By similarity.
Subcellular location	Cytoplasm By similarity.
Miscellaneous	Two distinct regulatory sites have been defined: the specificity site, which controls substrate specificity, and the activity site which regulates overall catalytic activity. A substrate-binding catalytic site, located on M1, is formed only in the presence of the second subunit M2 By similarity.
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	Acetylation
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 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 – 792	792	Ribonucleoside-diphosphate reductase large subunit		PRO_0000290352
Regions
	Domain	1 – 92	92	ATP-cone
Sites
	Active site	218	1	Hydrogen atom transfer By similarity
	Active site	427	1	Proton acceptor By similarity
	Active site	429	1	Proton acceptor By similarity
	Active site	431	1	Proton acceptor By similarity
	Active site	444	1	Hydrogen atom transfer By similarity
	Active site	737	1	Electron transfer By similarity
	Active site	738	1	Electron transfer By similarity
	Site	226	1	Allosteric effector binding By similarity
	Site	256	1	Allosteric effector binding By similarity
	Site	787	1	Interacts with thioredoxin/glutaredoxin By similarity
	Site	790	1	Interacts with thioredoxin/glutaredoxin By similarity
Amino acid modifications
	Modified residue	17	1	N6-acetyllysine By similarity
	Modified residue	376	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5R919-1 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 93AC48CB6CEEC044	FASTA	792	90,027
	10 20 30 40 50 60 MHVIKRDGRQ ERVMFDKITS RIQKLCYGLN MDFVDPAQIT MKVIQGLYSG VTTVELDTLA 70 80 90 100 110 120 AETAATLTTK HPDYAILAAR IAVSNLHKEA KKVFSDVMED LYNYINPHNG KHSPMVAKST 130 140 150 160 170 180 LDIVLANKDR LNSAIIYDRD FSYNYFGFKT LERSYLLKIN GKVAERPQHM LMRVSVGIHK 190 200 210 220 230 240 EDIDAAIETY NLLSERWFTH ASPTLFNAGT NRPQLSSCFL LSMKDDSIEG IYDTLKQCAL 250 260 270 280 290 300 ISKSAGGIGV AVSCIRATGS YIAGTNGNSN GLVPMLRVYN NTARYVDQGG NKRPGAFAIY 310 320 330 340 350 360 LEPWHLDIFE FLDLKKNTGK EEQRARDLFF ALWIPDLFMK RVETNQDWSL MCPNECPGLD 370 380 390 400 410 420 EVWGEEFEKL YASYEKQGRV RKVVKAQQLW YAIIESQTET GTPYMLYKDS CNRKSNQQNL 430 440 450 460 470 480 GTIKCSSLCT EIVEYTSKDE VAVCNLASLA LNMYVTSEHT YDFKKLAEVT KVVVRNLNKI 490 500 510 520 530 540 IDINYYPVPE ACLSNKRHRP IGIGVQGLAD AFILMRYPFE SAEAQLLNKQ IFETIYYGAL 550 560 570 580 590 600 EASCDLAKEQ GPYETYEGSP VSKGILQYDM WNVTPTDLWD WKLLKEKIAK YGIRNSLLIA 610 620 630 640 650 660 PMPTASTAQI LGNNESIEPY TSNIYTRRVL SGEFQIVNPH LLKDLTERGL WHEEMKNQII 670 680 690 700 710 720 ACNGSIQSIP EIPDDLKQLY KTVWEISQKT VLKMAAERGA FIDQSQSLNI HIAEPNYGKL 730 740 750 760 770 780 TSMHFYGWKQ GLKTGMYYLR TRPAANPIQF TLNKEKLKDK EKVSKEEEEK ERNTAAMVCS 790 LENRDECLMC GS

References

[1]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Heart.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR859577 mRNA. Translation: CAH91741.1.
RefSeq	NP_001126012.1.
UniGene	Pab.9179
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	100172956.
Organism-specific databases
CTD	100172956.
Phylogenomic databases
HOVERGEN	Q5R919.
Enzyme and pathway databases
BRENDA	1.17.4.1. 269192.
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_PONAB

Accession

Primary (citable) accession number: Q5R919

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 12, 2007
Last sequence update:	December 21, 2004
Last modified:	October 13, 2009
This is version 25 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)