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Description:
DNA repair and recombination protein radA.
Molecular weight: 35867
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 2.
07-MAR-2006, entry version 39.
Phylogenetic order:
Archaea Crenarchaeota Thermoprotei Sulfolobales Sulfolobaceae Sulfolobus.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein RADA_SULSO:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | U45310 | AAC44123.1 | - |
| EMBL | AE006661 | AAK40589.1 | - |
| PIR | F90166 | F90166. | |
| PIR | S71093 | S71093. | |
| PDB | 2BKE | X-ray | A=1-324. |
| GenomeReviews | AE006641_GR | SSO0250.1 | |
| BioCyc | SSOL2287:SSO0250-MONOMER | -.1 | |
| HAMAP | MF_00348 | - | 1. |
| InterPro | IPR003593 | AAA_ATPase. | |
| InterPro | IPR001553 | RecA_bac. | |
| InterPro | IPR011938 | Recomb_radA. | |
| PRINTS | PR00142 | RECA. | |
| ProDom | PD000229 | RecA | 1. |
| SMART | SM00382 | AAA | 1. |
| TIGRFAMs | TIGR02236 | recomb_radA | 1. |
| PROSITE | PS50162 | RECA_2 | 1. |
| PROSITE | PS50163 | RECA_3 | 1. |
Keywords:
3D-structure; ATP-binding; Complete proteome; DNA damage; DNA recombination; DNA-binding; Nucleotide-binding.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX MEDLINE=96251095; PubMed=8668545; DOI=10.1093/nar/24.11.2125;
RA Sandler S.J., Satin L.H., Samra H.S., Clark A.J.;
RT "recA-like genes from three archaean species with putative protein
RT products similar to Rad51 and Dmc1 proteins of the yeast Saccharomyces
RT cerevisiae.";
RL Nucleic Acids Res. 24:2125-2132(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / P2;
RX MEDLINE=21332296; PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G.,
RA Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A.,
RA De Moors A., Erauso G., Fletcher C., Gordon P.M.K.,
RA Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X.,
RA Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N.,
RA Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [3]
RP CHARACTERIZATION.
RX MEDLINE=98241482; PubMed=9573041;
RA Seitz E.M., Brockman J.P., Sandler S.J., Clark A.J.,
RA Kowalczykowski S.C.;
RT "RadA protein is an archaeal RecA protein homolog that catalyzes DNA
RT strand exchange.";
RL Genes Dev. 12:1248-1253(1998).
RN [4]
RP CHARACTERIZATION.
RX MEDLINE=20392210; PubMed=10931349;
RA Seitz E.M., Kowalczykowski S.C.;
RT "The DNA binding and pairing preferences of the archaeal RadA protein
RT demonstrate a universal characteristic of DNA strand exchange
RT proteins.";
RL Mol. Microbiol. 37:555-560(2000).
Feature:
CHAIN 1 324 DNA repair and recombination protein
radA.
/FTId=PRO_0000150107.
NP_BIND 114 121 ATP (Potential).
CONFLICT 225 225 N -> I (in Ref. 1).
Comments:
-!- FUNCTION: Involved in DNA repair and in homologous recombination.
Binds and assemble on single-stranded DNA to form a nucleoprotein
filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes
DNA strand exchange between homologous DNA molecules.
-!- SIMILARITY: Belongs to the eukaryotic recA-like protein family.
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Sequence length: 324
MSNEVEQKKN IKTINDLPGI SQTVINKLIE AGYSSLETLA VASPQDLSVA AGIPLSTAQK
IIKEARDALD IRFKTALEVK KERMNVKKIS TGSQALDGLL AGGIETRTMT EFFGEFGSGK
TQLCHQLSVN VQLPPEKGGL SGKAVYIDTE GTFRWERIEN MAKALGLDID NVMNNIYYIR
AINTDHQIAI VDDLQELVSK DPSIKLIVVD SVTSHFRAEY PGRENLAVRQ QKLNKHLHQL
TRLAEVYDIA VIITNQVMAR PDMFYGDPTV AVGGHTLYHV PGIRIQLKKS RGNRRIARVV
DAPHLPEGEV VFALTEEGIR DAEE