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Database: UniProt
Entry: A0A0G2HLB1_9SYNE
LinkDB: A0A0G2HLB1_9SYNE
Original site: A0A0G2HLB1_9SYNE 
ID   A0A0G2HLB1_9SYNE        Unreviewed;       476 AA.
AC   A0A0G2HLB1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   08-NOV-2023, entry version 37.
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   ORFNames=TE42_07105 {ECO:0000313|EMBL:KKZ11737.1};
OS   Candidatus Synechococcus spongiarum SP3.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1604020 {ECO:0000313|EMBL:KKZ11737.1, ECO:0000313|Proteomes:UP000035067};
RN   [1] {ECO:0000313|EMBL:KKZ11737.1, ECO:0000313|Proteomes:UP000035067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP3 {ECO:0000313|EMBL:KKZ11737.1};
RA   Burgsdorf I., Slaby B.M., Handley K.M., Haber M., Blom J., Marshall C.W.,
RA   Gilbert J.A., Hentschel U., Steindler L.;
RT   "Lifestyle Evolution in Cyanobacterial Symbionts of Sponges.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-dependent ATPase involved in processing of recombination
CC       intermediates, plays a role in repairing DNA breaks. Stimulates the
CC       branch migration of RecA-mediated strand transfer reactions, allowing
CC       the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA
CC       in the presence of ADP but not other nucleotides, has ATPase activity
CC       that is stimulated by ssDNA and various branched DNA structures, but
CC       inhibited by SSB. Does not have RecA's homology-searching function.
CC       {ECO:0000256|RuleBase:RU003555}.
CC   -!- FUNCTION: Plays a role in repairing double-strand DNA breaks, probably
CC       involving stabilizing or processing branched DNA or blocked replication
CC       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 to
CC       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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKZ11737.1}.
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DR   EMBL; JXQG01000042; KKZ11737.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2HLB1; -.
DR   PATRIC; fig|1604020.3.peg.1274; -.
DR   Proteomes; UP000035067; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000725; P:recombinational repair; IEA:UniProtKB-UniRule.
DR   CDD; cd01121; RadA_SMS_N; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_01498; RadA_bact; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR004504; DNA_repair_RadA.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020588; RecA_ATP-bd.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR041166; Rubredoxin_2.
DR   NCBIfam; TIGR00416; sms; 1.
DR   PANTHER; PTHR32472; DNA REPAIR PROTEIN RADA; 1.
DR   PANTHER; PTHR32472:SF10; DNA REPAIR PROTEIN RADA-LIKE PROTEIN; 1.
DR   Pfam; PF13481; AAA_25; 1.
DR   Pfam; PF18073; Rubredoxin_2; 1.
DR   PRINTS; PR01874; DNAREPAIRADA.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS50162; RECA_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01498};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW   Rule:MF_01498}; Zinc {ECO:0000256|RuleBase:RU003555};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU003555}.
FT   DOMAIN          67..226
FT                   /note="RecA family profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50162"
FT   REGION          361..476
FT                   /note="Lon-protease-like"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT   MOTIF           263..267
FT                   /note="RadA KNRFG motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT   BINDING         96..103
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
SQ   SEQUENCE   476 AA;  50713 MW;  505F3B711DD37642 CRC64;
     MARVQPVYRC QACGSQAHQF FGRCPSCGAW NTLLEELPAE RSLTSQRCPS SSTRQRSQPI
     GAVEPMAEVR INTGSSELDR VLGGGLVRGS LVLVGGDPGI GKSTLLLQTA HHMAQQVCVL
     YVSAEESAQQ VRLRWSRLCS GHPETSDHDS SIAMGLRLQA ETSLRLVLQE LERLAPDVAV
     IDSIQALHNP DLSSAAGSVA QVRECAAALR QLAKTMNIAT LLVGHVTKEG MLAGPKTLEH
     LVDAVLSFEG DRFASHRLLR SLKNRFGATF ELGVFEMGDR GLREVANPSQ LFLSQGDPTS
     GTAAIVACEG TRPLVVELQA LISPSSYASP RRSATGIANN RLHQILAVLE KQLGLPLSRF
     DCYLAVAGGL EVTEPAADVG VAVAVASSYR DLLIPPGTLC IGELGLGGQL RPVARMEQRL
     QEGQRLGFHR ALVPAGSEIT PPATMTIIEA GTIRQVLVAA LQNNLAVADE EIPSQA
//
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