CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004971
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribonucleoside-diphosphate reductase large chain 1 
Protein Synonyms/Alias
 Ribonucleotide reductase R1 subunit 1; Ribonucleotide reductase large subunit 1 
Gene Name
 RNR1 
Gene Synonyms/Alias
 CRT7; RIR1; SDS12; YER070W 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
10VYKRDGRKEPVQFDKubiquitination[1]
32LCYGLDPKHIDAVKVacetylation[2]
32LCYGLDPKHIDAVKVubiquitination[1]
387GKTIKAQKLWYSILEubiquitination[1, 3]
417CNRKSNQKNLGVIKSubiquitination[1]
849PEVPAPTKNEEKAAPubiquitination[1, 3]
853APTKNEEKAAPIVDDubiquitination[1, 3]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [2] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [3] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047] 
Functional Description
 Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. 
Sequence Annotation
 DOMAIN 1 92 ATP-cone.
 REGION 11 17 Allosteric activator binding (By
 REGION 217 218 Substrate binding.
 REGION 285 288 Allosteric effector binding, determines
 REGION 426 430 Substrate binding.
 REGION 607 611 Substrate binding.
 ACT_SITE 426 426 Proton acceptor.
 ACT_SITE 428 428 Cysteine radical intermediate.
 ACT_SITE 430 430 Proton acceptor.
 BINDING 5 5 Allosteric activator (By similarity).
 BINDING 53 53 Allosteric activator (By similarity).
 BINDING 88 88 Allosteric activator (By similarity).
 BINDING 202 202 Substrate.
 BINDING 247 247 Substrate; via amide nitrogen.
 MOD_RES 227 227 Phosphoserine.
 MOD_RES 837 837 Phosphoserine.
 MOD_RES 887 887 Phosphoserine.
 DISULFID 218 443 Redox-active.  
Keyword
 3D-structure; Allosteric enzyme; ATP-binding; Complete proteome; Cytoplasm; Disulfide bond; DNA replication; Nucleotide-binding; Oxidoreductase; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 888 AA 
Protein Sequence
MYVYKRDGRK EPVQFDKITA RISRLCYGLD PKHIDAVKVT QRIISGVYEG VTTIELDNLA 60
AETCAYMTTV HPDYATLAAR IAISNLHKQT TKQFSKVVED LYRYVNAATG KPAPMISDDV 120
YNIVMENKDK LNSAIVYDRD FQYSYFGFKT LERSYLLRIN GQVAERPQHL IMRVALGIHG 180
RDIEAALETY NLMSLKYFTH ASPTLFNAGT PKPQMSSCFL VAMKEDSIEG IYDTLKECAL 240
ISKTAGGIGL HIHNIRSTGS YIAGTNGTSN GLIPMIRVFN NTARYVDQGG NKRPGAFALY 300
LEPWHADIFD FIDIRKNHGK EEIRARDLFP ALWIPDLFMK RVEENGTWTL FSPTSAPGLS 360
DCYGDEFEAL YTRYEKEGRG KTIKAQKLWY SILEAQTETG TPFVVYKDAC NRKSNQKNLG 420
VIKSSNLCCE IVEYSAPDET AVCNLASVAL PAFIETSEDG KTSTYNFKKL HEIAKVVTRN 480
LNRVIDRNYY PVEEARKSNM RHRPIALGVQ GLADTFMLLR LPFDSEEARL LNIQIFETIY 540
HASMEASCEL AQKDGPYETF QGSPASQGIL QFDMWDQKPY GMWDWDTLRK DIMKHGVRNS 600
LTMAPMPTAS TSQILGYNEC FEPVTSNMYS RRVLSGEFQV VNPYLLRDLV DLGIWDEGMK 660
QYLITQNGSI QGLPNVPQEL KDLYKTVWEI SQKTIINMAA DRSVYIDQSH SLNLFLRAPT 720
MGKLTSMHFY GWKKGLKTGM YYLRTQAASA AIQFTIDQKI ADQATENVAD ISNLKRPSYM 780
PSSASYAASD FVPAAVTANA TIPSLDSSSE ASREASPAPT GSHSLTKGMA ELNVQESKVE 840
VPEVPAPTKN EEKAAPIVDD EETEFDIYNS KVIACAIDNP EACEMCSG 888 
Gene Ontology
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0005971; C:ribonucleoside-diphosphate reductase complex; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0000166; F:nucleotide binding; IDA:SGD.
 GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; ISS:UniProtKB.
 GO:0009263; P:deoxyribonucleotide biosynthetic process; ISS:UniProtKB.
 GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway. 
Interpro
 IPR005144; ATP-cone.
 IPR013346; NrdE_NrdA.
 IPR000788; RNR_lg_C.
 IPR013509; RNR_lsu_N.
 IPR008926; RNR_R1-su_N. 
Pfam
 PF03477; ATP-cone
 PF02867; Ribonuc_red_lgC
 PF00317; Ribonuc_red_lgN 
SMART
  
PROSITE
 PS51161; ATP_CONE
 PS00089; RIBORED_LARGE 
PRINTS
 PR01183; RIBORDTASEM1.