| Tag | Content |
|---|
| CPLM ID | CPLM-002534 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Ribonucleoside-diphosphate reductase large subunit |
Protein Synonyms/Alias | Ribonucleoside-diphosphate reductase subunit M1; Ribonucleotide reductase large subunit |
Gene Name | Rrm1 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 471 | EKLAEVTKVIVRNLN | acetylation | [1] |
|
Reference | [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways. Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y. Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [ PMID: 22826441] |
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 (By similarity).
REGION 285 288 Allosteric effector binding, determines
REGION 427 431 Substrate binding (By similarity).
REGION 603 607 Substrate binding (By similarity).
ACT_SITE 427 427 Proton acceptor (By similarity).
ACT_SITE 429 429 Cysteine radical intermediate (By
ACT_SITE 431 431 Proton acceptor (By similarity).
BINDING 5 5 Allosteric activator (By similarity).
BINDING 53 53 Allosteric activator (By similarity).
BINDING 88 88 Allosteric activator (By similarity).
BINDING 247 247 Substrate; via amide nitrogen (By
MOD_RES 17 17 N6-acetyllysine (By similarity).
MOD_RES 376 376 N6-acetyllysine (By similarity).
DISULFID 218 444 Redox-active (By similarity). |
Keyword | Acetylation; Allosteric enzyme; ATP-binding; Complete proteome; Cytoplasm; Disulfide bond; DNA replication; Nucleotide-binding; Oxidoreductase; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 792 AA |
Protein Sequence | MHVIKRDGRQ ERVMFDKITS RIQKLCYGLN MDFVDPAQIT MKVIQGLYSG VTTVELDTLA 60
AETAATLTTK HPDYAILAAR IAVSNLHKET KKVFSDVMED LYNYINPHNG RHSPMVASST 120
LDIVMANKDR LNSAIIYDRD FSYNYFGFKT LERSYLLKIN GKVAERPQHM LMRVSVGIHK 180
EDIDAAIETY NLLSEKWFTH ASPTLFNAGT NRPQLSSCFL LSMKDDSIEG IYDTLKQCAL 240
ISKSAGGIGV AVSCIRATGS YIAGTNGNSN GLVPMLRVYN NTARYVDQGG NKRPGAFAIY 300
LEPWHLDIFE FLDLKKNTGK EEQRARDLFF ALWIPDLFMK RVETNQDWSL MCPNECPGLD 360
EVWGEEFEKL YESYEKQGRV RKVVKAQQLW YAIIESQTET GTPYMLYKDS CNRKSNQQNL 420
GTIKCSNLCT EIVEYTSKDE VAVCNLASLA LNMYVTPEHT YDFEKLAEVT KVIVRNLNKI 480
IDINYYPIPE AHLSNKRHRP IGIGVQGLAD AFILMRYPFE SPEAQLLNKQ IFETIYYGAL 540
EASCELAKEY GPYETYEGSP VSKGILQYDM WNVAPTDLWD WKPLKEKIAK YGIRNSLLIA 600
PMPTASTAQI LGNNESIEPY TSNIYTRRVL SGEFQIVNPH LLKDLTERGL WNEEMKNQII 660
ACNGSIQSIP EIPDDLKQLY KTVWEISQKT VLKMAAERGA FIDQSQSLNI HIAEPNYGKL 720
TSMHFYGWKQ GLKTGMYYLR TRPAANPIQF TLNKEKLKDK EKALKEEEEK ERNTAAMVCS 780
LENREECLMC GS 792 |
Gene Ontology | GO:0005971; C:ribonucleoside-diphosphate reductase complex; IEA:InterPro. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0017076; F:purine nucleotide binding; IDA:MGI. GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IDA:UniProtKB. GO:0009263; P:deoxyribonucleotide biosynthetic process; IDA:UniProtKB. GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway. GO:0051290; P:protein heterotetramerization; IPI:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |