| Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | DNA double-strand break repair Rad50 ATPase |
Protein Synonyms/Alias | |
Gene Name | rad50 |
Gene Synonyms/Alias | Saci_0051 |
Created Date | 3-June-2014 |
Organism | Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) |
NCBI Taxa ID | 330779 |
Phosphorylation | Position | Peptide | Code | Type | References | | 364 | EIEKRLTYVLKNIER | Y | HTP | [1] | | 655 | DALLNRISELGYSEK | S | HTP | [1] | | 95 | VGETSRDTISLLKEG | T | HTP | [1] | | 660 | RISELGYSEKRYKQL | S | HTP | [1] | | 553 | LIDYHEEYLKNSDIL | Y | HTP | [1] | | 363 | EEIEKRLTYVLKNIE | T | HTP | [1] | |
Reference | [1]Archaeal signal transduction: impact of protein phosphatase deletions on cell size, motility, and energy metabolism in Sulfolobus acidocaldarius. Reimann J,Esser D,Orell A,Amman F,Pham TK,Noirel J,Lindås AC,Bernander R,Wright PC,Siebers B,Albers SV Mol. Cell Proteomics 2013, Dec;12(12):3908-23. [ PMID:24078887] |
Functional Description From UniProt | FUNCTION: Involved in DNA double-strand break repair (DSBR). The Rad50/Mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific 3'-5' exonuclease activity. Rad50 provides an ATP-dependent control of Mre11 by unwinding and/or repositioning DNA ends into the Mre11 active site (By similarity) |
| COILED 174 345 Potential
COILED 391 429 Potential
COILED 461 489 Potential
COILED 532 727 Potential |
| ATP-binding; Coiledcoil; Completeproteome; DNAdamage; DNArepair; Hydrolase; Metal-binding; Nucleotide-binding; Zinc |
Protein Sequence | MIIREIRLQN FLSHEDTTVK FEGSINVIIG NNGAGKSSII DGILFGLFKR TNRDIGKNEE 60
LIKKGKKSGQ VSIKFEINGD TYLIDRNVGE TSRDTISLLK EGKIITLARQ STTVNNKIKE 120
ILGFDHKILM STTIIGQGSV ESVFSDFPEV MKELLKINKL EMLRESNGPI HSLIKVLTDR 180
IRSLQSIKDI LKREEAEIDR LKKEIEEIKV KLENIEREAK EKEDELNQYN TEFNRIKEIK 240
VQYDILSGEL SVVNKKIEEI ALRLKDFEEK EKRYNKIETE VKELDENREK INTISSFKSI 300
LVQIDSLKSQ INVVENDLKR KKEKLKRKKE LEEKEKQYEE IEKRKKELEE KEKQYEEIEK 360
RLTYVLKNIE RQKNEIEKLN YVDTQDLENK IKDVSDRINQ IDNELKGLLD RRGDLNGRKE 420
QTLKIYNNLN SIEDDRCPIC GRPLDSEHKA KIREEIKVQL LELNKQITAL QARINSLIKE 480
REELEATRNK LQLELQKRSK EKGIYEAKLK ELQRLEEEKN KLQNEILSLL SYHQEFENIA 540
EKEKELIDYH EEYLKNSDIL EEDIQEQEQR LNELNSKLSE LEKSYNDYKA KYQFLPADLK 600
SLVSLEERIR RRISELEKLK IEYERLKEEI TRMKGLKEEY EKLKEEEDAL LNRISELGYS 660
EKRYKQLEEI IDKLSKILSG IEADKGKIKG SLEEKIKNIE EKERNIEELR NKMNEESKLN 720
LGISKLQKLR EVLDNKHLQS HIMNIVRNQI ENNVNEVIAK FDLSFSAVEI DFVGKSELYV 780
YTASGQKIHI NALSGGERIS IALALRLAIA KALMNQFSTL ILDEPTVNLD EYRRKELIDV 840
IRSAIEIVPQ IILVTHDQEL IQAGDYIIRV EKKGDTSKVE VSSYDR 886 |
| GO:0005524 F:ATP binding IEA:UniProtKB-HAMAP GO:0016887 F:ATPase activity IEA:UniProtKB-HAMAP GO:0004519 F:endonuclease activity IEA:UniProtKB-HAMAP GO:0004527 F:exonuclease activity IEA:UniProtKB-HAMAP GO:0008270 F:zinc ion binding IEA:UniProtKB-HAMAP GO:0006302 P:double-strand break repair IEA:UniProtKB-HAMAP |
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