ID RADA_HALSA STANDARD; PRT; 343 AA. AC Q9HMM4; O93747; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 13-SEP-2005 (Rel. 48, Last annotation update) DE DNA repair and recombination protein radA. GN Name=radA; Synonyms=radA1; OrderedLocusNames=VNG2473G; OS Halobacterium salinarium (Halobacterium halobium). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Halobacterium. OX NCBI_TaxID=2242; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=99121030; PubMed=9922255; RA Sandler S.J., Hugenholtz P., Schleper C., DeLong E.F., Pace N.R., RA Clark A.J.; RT "Diversity of radA genes from cultured and uncultured archaea: RT comparative analysis of putative RadA proteins and their use as a RT phylogenetic marker."; RL J. Bacteriol. 181:907-915(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRC-1 / ATCC 700922 / JCM 11081; RX MEDLINE=20504483; PubMed=11016950; DOI=10.1073/pnas.190337797; RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., RA Shukla H.D., Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., RA Swartzell S., Weir D., Hall J., Dahl T.A., Welti R., Goo Y.A., RA Leithauser B., Keller K., Cruz R., Danson M.J., Hough D.W., RA Maddocks D.G., Jablonski P.E., Krebs M.P., Angevine C.M., Dale H., RA Isenbarger T.A., Peck R.F., Pohlschroder M., Spudich J.L., Jung K.-H., RA Alam M., Freitas T., Hou S., Daniels C.J., Dennis P.P., Omer A.D., RA Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L., DasSarma S.; RT "Genome sequence of Halobacterium species NRC-1."; RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000). CC -!- FUNCTION: Involved in DNA repair and in homologous recombination. CC Binds and assemble on single-stranded DNA to form a nucleoprotein CC filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes CC DNA strand exchange between homologous DNA molecules (By CC similarity). CC -!- SIMILARITY: Belongs to the eukaryotic recA-like protein family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF090196; AAD16062.1; -; Genomic_DNA. DR EMBL; AE005125; AAG20547.1; ALT_INIT; Genomic_DNA. DR PIR; T43802; T43802. DR HSSP; Q06609; 1N0W. DR HAMAP; MF_00348; -; 1. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR000445; HhH. DR InterPro; IPR003583; HHH1_bd. DR InterPro; IPR001553; RecA. DR InterPro; IPR011938; Recomb_radA. DR ProDom; PD000229; RecA; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00278; HhH1; 2. DR TIGRFAMs; TIGR02236; recomb_radA; 1. DR PROSITE; PS50162; RECA_2; 1. DR PROSITE; PS50163; RECA_3; 1. KW ATP-binding; Complete proteome; DNA damage; DNA recombination; KW DNA-binding; Nucleotide-binding. FT NP_BIND 107 114 ATP (Potential). FT CONFLICT 1 2 MP -> MRGAPPTRRYIS (in Ref. 1). FT CONFLICT 8 8 E -> D (in Ref. 1). FT CONFLICT 15 17 ATA -> PTT (in Ref. 1). FT CONFLICT 23 23 N -> S (in Ref. 1). FT CONFLICT 30 32 SLA -> ILT (in Ref. 1). FT CONFLICT 75 75 R -> P (in Ref. 1). FT CONFLICT 132 132 G -> A (in Ref. 1). FT CONFLICT 263 263 K -> P (in Ref. 1). FT CONFLICT 266 266 N -> D (in Ref. 1). SQ SEQUENCE 343 AA; 37423 MW; 847D17052968EF2D CRC64; MPESDLEELP GVGPATAEKL RDNGFDAFQS LAVANSAELS NTADIGESTA ADVIQAAREA ADVGGFETGA TVLERREQIG KLTWNIPEVD DLLGGGVETQ SITEVYGEFG AGKSQVTHQL AVNVQLPTEY GGLHGRAVFI DSEDTFRPER IDDMVRGLSD ETLQAAMEAH EIEGSTDDED TLTELVDAFL DKIHVAKGFN SNHQMLLAEK AKEIASEHED GDWPVRMLTV DSLTAHFRAE YVGRGELADR QQKLNKHLHD LEKVGNLYNA AVLVTNQVQS NPDAFFGDPT KPIGGNILGH KSTFRMYLRK SKNDKRIVKL VDAPNLADGE AVMRVQDEGL KPE //