| Tag | Content |
|---|
| CPLM ID | CPLM-005629 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Recombination repair protein 1 |
Protein Synonyms/Alias | DNA-(apurinic or apyrimidinic site) lyase |
Gene Name | Rrp1 |
Gene Synonyms/Alias | CG3178 |
Created Date | July 27, 2013 |
Organism | Drosophila melanogaster (Fruit fly) |
NCBI Taxa ID | 7227 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 204 | AEPGTISKEKVQKAE | acetylation | [1] | | 353 | KPAKGRKKAPVKAED | acetylation | [1] | | 357 | GRKKAPVKAEDVEDI | acetylation | [1] |
|
Reference | [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation. Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C. Sci Signal. 2011 Jul 26;4(183):ra48. [ PMID: 21791702] |
Functional Description | Could promote homologous recombination at sites of DNA damage. Has apurinic endonuclease and double-stranded DNA 3'- exonuclease activities and carries out single-stranded DNA renaturation in a Mg(2+)-dependent manner. Activity is more efficient in purine-rich regions of dsDNA than in pyrimidine-rich regions. |
Sequence Annotation | REGION 428 679 AP endonuclease.
ACT_SITE 533 533 By similarity.
ACT_SITE 572 572 Proton donor/acceptor (By similarity).
METAL 461 461 Magnesium 1 (By similarity).
METAL 572 572 Magnesium 2 (By similarity).
METAL 574 574 Magnesium 2 (By similarity).
METAL 669 669 Magnesium 1 (By similarity).
MOD_RES 133 133 Phosphothreonine.
MOD_RES 140 140 Phosphothreonine.
MOD_RES 142 142 Phosphoserine.
MOD_RES 258 258 Phosphoserine. |
Keyword | Complete proteome; DNA damage; DNA repair; Lyase; Magnesium; Metal-binding; Nucleus; Phosphoprotein; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 679 AA |
Protein Sequence | MPRVKAVKKQ AEALASEPTD PTPNANGNGV DENADSAAEE LKVPAKGKPR ARKATKTAVS 60
AENSEEVEPQ KAPTAAARGK KKQPKDTDEN GQMEVVAKPK GRAKKATAEA EPEPKVDLPA 120
GKATKPRAKK EPTPAPDEVT SSPPKGRAKA EKPTNAQAKG RKRKELPAEA NGGAEEAAEP 180
PKQRARKEAV PTLKEQAEPG TISKEKVQKA ETAAKRARGT KRLADSEIAA ALDEPEVDEV 240
PPKAASKRAK KGKMVEPSPE TVGDFQSVQE EVESPPKTAA APKKRAKKTT NGETAVELEP 300
KTKAKPTKQR AKKEGKEPAP GKKQKKSADK ENGVVEEEAK PSTETKPAKG RKKAPVKAED 360
VEDIEEAAEE SKPARGRKKA AAKAEEPDVD EESGSKTTKK AKKAETKTTV TLDKDAFALP 420
ADKEFNLKIC SWNVAGLRAW LKKDGLQLID LEEPDIFCLQ ETKCANDQLP EEVTRLPGYH 480
PYWLCMPGGY AGVAIYSKIM PIHVEYGIGN EEFDDVGRMI TAEYEKFYLI NVYVPNSGRK 540
LVNLEPRMRW EKLFQAYVKK LDALKPVVIC GDMNVSHMPI DLENPKNNTK NAGFTQEERD 600
KMTELLGLGF VDTFRHLYPD RKGAYTFWTY MANARARNVG WRLDYCLVSE RFVPKVVEHE 660
IRSQCLGSDH CPITIFFNI 679 |
Gene Ontology | GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. GO:0008408; F:3'-5' exonuclease activity; IDA:FlyBase. GO:0003677; F:DNA binding; IEA:InterPro. GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IDA:FlyBase. GO:0004519; F:endonuclease activity; IEA:InterPro. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0006281; P:DNA repair; IEA:UniProtKB-KW. GO:0006974; P:response to DNA damage stimulus; IMP:FlyBase. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |