ID A0A2P7MT30_9CYAN Unreviewed; 489 AA.
AC A0A2P7MT30;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DNA repair protein RadA {ECO:0000256|HAMAP-Rule:MF_01498};
GN Name=radA {ECO:0000256|HAMAP-Rule:MF_01498};
GN ORFNames=C7K55_10285 {ECO:0000313|EMBL:PSJ04393.1};
OS Cyanobium usitatum str. Tous.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Cyanobium.
OX NCBI_TaxID=2116684 {ECO:0000313|EMBL:PSJ04393.1, ECO:0000313|Proteomes:UP000243002};
RN [1] {ECO:0000313|EMBL:PSJ04393.1, ECO:0000313|Proteomes:UP000243002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tous {ECO:0000313|EMBL:PSJ04393.1,
RC ECO:0000313|Proteomes:UP000243002};
RX PubMed=30117250; DOI=.1111/1462-2920.14377;
RA Cabello-Yeves P.J., Picazo A., Camacho A., Callieri C., Rosselli R.,
RA Roda-Garcia J.J., Coutinho F.H., Rodriguez-Valera F.;
RT "Ecological and genomic features of two widespread freshwater
RT picocyanobacteria.";
RL Environ. Microbiol. 20:3757-3771(2018).
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}.
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:PSJ04393.1}.
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DR EMBL; PXXO01000012; PSJ04393.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P7MT30; -.
DR OrthoDB; 9803906at2; -.
DR Proteomes; UP000243002; 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 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 DNA damage {ECO:0000256|HAMAP-Rule:MF_01498};
KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01498};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01498};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01498}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01498};
KW Reference proteome {ECO:0000313|Proteomes:UP000243002};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_01498}; Zinc {ECO:0000256|ARBA:ARBA00022771};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 77..242
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT REGION 39..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..489
FT /note="Lon-protease-like"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT MOTIF 279..283
FT /note="RadA KNRFG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT BINDING 106..113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
SQ SEQUENCE 489 AA; 50926 MW; DA0FC44EACBEF101 CRC64;
MAKPSTFFVC TSCGAQARQF FGKCASCGSW NTLVEQKAAP AADSRRRRPV AEAPAAEAVV
AGQPRRSEPI QAVGERALQR LSSGYGEFDR VLGGGLVPGS LVLVGGDPGI GKSTLLLQSA
RAMAGRASVL YVSAEESAQQ VKLRWRRLAE ASPAQPEAGE LEAGESKAGA DFQLLAETDL
ELVLQELEAL RPAVAIIDSI QALHDAELGS APGSVSQVRE CAAALARIAK RQDTALLLVG
HVTKEGALAG PKVLEHLVDA VLTFEGDRFA SHRLLRAVKN RFGATHELGV FEMRDRGLAE
VTNPSELFLG GDEPSAGTAT IVACEGTRPL VVEMQALVST TSYASPRRSA TGIAVNRLHQ
ILAVLEKHLG LPLSRFDCYL AVAGGLEVEE PAADLGVAAA VVASYRDLTL PPGTVLVGEL
GLGGQLRPVG QLELRLQEAA RLGFTRAVVP RGTGLAKAAA GFGLQLLEAG GVAEALVAAL
GVNPADDRG
//
