(data stored in ACNUC1104 zone)

SWISSPROT: E6V1B0_VARPE

ID   E6V1B0_VARPE            Unreviewed;       462 AA.
AC   E6V1B0;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 56.
DE   RecName: Full=DNA repair protein RadA {ECO:0000256|HAMAP-Rule:MF_01498, ECO:0000256|RuleBase:RU003555};
GN   Name=radA {ECO:0000256|HAMAP-Rule:MF_01498};
GN   OrderedLocusNames=Varpa_0252 {ECO:0000313|EMBL:ADU34474.1};
OS   Variovorax paradoxus (strain EPS).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34474.1, ECO:0000313|Proteomes:UP000008917};
RN   [1] {ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|Proteomes:UP000008917};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Orwin P.,
RA   Han J.-I.G., Woyke T.;
RT   "Complete sequence of Variovorax paradoxus EPS.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADU34474.1, ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|EMBL:ADU34474.1,
RC   ECO:0000313|Proteomes:UP000008917};
RX   PubMed=24158554;
RA   Han J.I., Spain J.C., Leadbetter J.R., Ovchinnikova G., Goodwin L.A.,
RA   Han C.S., Woyke T., Davenport K.W., Orwin P.M.;
RT   "Genome of the Root-Associated Plant Growth-Promoting Bacterium
RT   Variovorax paradoxus Strain EPS.";
RL   Genome Announc. 1:e00843-13(2013).
CC   -!- FUNCTION: DNA-dependent ATPase involved in processing of
CC       recombination intermediates, plays a role in repairing DNA breaks.
CC       Stimulates the branch migration of RecA-mediated strand transfer
CC       reactions, allowing the 3' invading strand to extend heteroduplex
CC       DNA faster. Binds ssDNA in the presence of ADP but not other
CC       nucleotides, has ATPase activity that is stimulated by ssDNA and
CC       various branched DNA structures, but inhibited by SSB. Does not
CC       have RecA's homology-searching function.
CC       {ECO:0000256|RuleBase:RU003555}.
CC   -!- FUNCTION: Plays a role in repairing double-strand DNA breaks,
CC       probably involving stabilizing or processing branched DNA or
CC       blocked replication forks. {ECO:0000256|HAMAP-Rule:MF_01498}.
CC   -!- DOMAIN: The middle region has homology to RecA with ATPase motifs
CC       including the RadA KNRFG motif, while the C-terminus is homologous
CC       to Lon protease. {ECO:0000256|HAMAP-Rule:MF_01498}.
CC   -!- SIMILARITY: Belongs to the RecA family. RadA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01498, ECO:0000256|RuleBase:RU003555}.
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; CP002417; ADU34474.1; -; Genomic_DNA.
DR   RefSeq; WP_013538720.1; NC_014931.1.
DR   STRING; 595537.Varpa_0252; -.
DR   MEROPS; S16.A04; -.
DR   EnsemblBacteria; ADU34474; ADU34474; Varpa_0252.
DR   GeneID; 29715995; -.
DR   KEGG; vpe:Varpa_0252; -.
DR   eggNOG; ENOG4105DNJ; Bacteria.
DR   eggNOG; COG1066; LUCA.
DR   HOGENOM; HOG000218329; -.
DR   KO; K04485; -.
DR   OMA; SQVREIT; -.
DR   OrthoDB; 505485at2; -.
DR   BioCyc; VPAR595537:G1GQO-254-MONOMER; -.
DR   Proteomes; UP000008917; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0008094; F:DNA-dependent ATPase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0000725; P:recombinational repair; IEA:UniProtKB-UniRule.
DR   CDD; cd01121; Sms; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   HAMAP; MF_01498; RadA_bact; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR004504; DNA_repair_RadA.
DR   InterPro; IPR008269; Lon_proteolytic.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020588; RecA_ATP-bd.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR041166; Rubredoxin_2.
DR   Pfam; PF05362; Lon_C; 1.
DR   Pfam; PF18073; Rubredoxin_2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   TIGRFAMs; TIGR00416; sms; 1.
DR   PROSITE; PS50162; RECA_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; E6V1B0.
DR   SWISS-2DPAGE; E6V1B0.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008917};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008917};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_01498};
KW   Zinc {ECO:0000256|RuleBase:RU003555};
KW   Zinc-finger {ECO:0000256|RuleBase:RU003555}.
FT   DOMAIN       71    220       RECA_2. {ECO:0000259|PROSITE:PS50162}.
FT   NP_BIND     100    107       ATP. {ECO:0000256|HAMAP-Rule:MF_01498}.
FT   REGION      355    462       Lon-protease-like. {ECO:0000256|HAMAP-
FT                                Rule:MF_01498}.
FT   MOTIF       257    261       RadA KNRFG motif. {ECO:0000256|HAMAP-
FT                                Rule:MF_01498}.
SQ   SEQUENCE   462 AA;  48628 MW;  B77E4C5EA3EDA7DC CRC64;
     MAKDKTTFVC SECGGTSPKW LGKCPSCGAW NTLIEQVAGS NAPANNRFGT QFSPLAGVSE
     LATLSEIEAT DIARTPTGID ELDRVLGGGI VSGGVTLIGG DPGIGKSTLL LQAVDALQRA
     GQNALYVTGE ESGAQVALRS RRLGLDHSQV QVLAEIQLEK IIATLDATRP AIAVIDSIQT
     VYSDQLTSAP GSVAQVRECA AHLTRFAKTS GTAVVLVGHV TKEGALAGPR VLEHMVDTVL
     YFEGDTHSSF RLVRAIKNRF GAVNEIGVFA MTERGLKGVA NPSAIFLSQH AEPVPGSVVL
     VTLEGTRPML VEIQALVDNG GPSPRRLSVG LDRDRLAMLL AVLHRHAGVA CMDQDVFVNA
     VGGVRISEPA ADLAVMLAIT SSLRGKPLPK GFIAFGEVGL AGEVRPAPRG QERLREAAKL
     GFSIAVVPKA NAPRKGSKEI EGLTIHPVER IEEAMDVVRR LD
//

If you have problems or comments...

PBIL Back to PBIL home page