ID L0E9M2_THECK Unreviewed; 358 AA.
AC L0E9M2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Putative nucleic-acid-binding protein (Contains the HHH domain) {ECO:0000313|EMBL:AGA56487.1};
GN OrderedLocusNames=Theco_0242 {ECO:0000313|EMBL:AGA56487.1};
OS Thermobacillus composti (strain DSM 18247 / JCM 13945 / KWC4).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Thermobacillus.
OX NCBI_TaxID=717605 {ECO:0000313|EMBL:AGA56487.1, ECO:0000313|Proteomes:UP000010795};
RN [1] {ECO:0000313|Proteomes:UP000010795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18247 / JCM 13945 / KWC4
RC {ECO:0000313|Proteomes:UP000010795};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Anderson I.,
RA Woyke T.;
RT "Complete sequence of chromosome of Thermobacillus composti KWC4.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP = 3',3'-c-di-AMP + 2 diphosphate; Xref=Rhea:RHEA:35655,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:71500; EC=2.7.7.85;
CC Evidence={ECO:0000256|ARBA:ARBA00000877};
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DR EMBL; CP003255; AGA56487.1; -; Genomic_DNA.
DR RefSeq; WP_015253253.1; NC_019897.1.
DR AlphaFoldDB; L0E9M2; -.
DR STRING; 717605.Theco_0242; -.
DR KEGG; tco:Theco_0242; -.
DR eggNOG; COG1623; Bacteria.
DR HOGENOM; CLU_787128_0_0_9; -.
DR OrthoDB; 41841at2; -.
DR Proteomes; UP000010795; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106408; F:diadenylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 1.20.1260.110; DNA integrity scanning linker region; 1.
DR Gene3D; 3.40.1700.10; DNA integrity scanning protein, DisA, N-terminal domain; 1.
DR HAMAP; MF_01438; DisA; 1.
DR InterPro; IPR041663; DisA/LigA_HHH.
DR InterPro; IPR038331; DisA_sf.
DR InterPro; IPR036888; DNA_integrity_DisA_N_sf.
DR InterPro; IPR018906; DNA_integrity_scan_DisA_link.
DR InterPro; IPR003390; DNA_integrity_scan_DisA_N.
DR InterPro; IPR023763; DNA_integrity_scanning_protein.
DR InterPro; IPR010994; RuvA_2-like.
DR PANTHER; PTHR34185; DIADENYLATE CYCLASE; 1.
DR PANTHER; PTHR34185:SF3; DNA INTEGRITY SCANNING PROTEIN DISA; 1.
DR Pfam; PF02457; DAC; 1.
DR Pfam; PF10635; DisA-linker; 1.
DR Pfam; PF12826; HHH_2; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR SUPFAM; SSF143597; YojJ-like; 1.
DR PROSITE; PS51794; DAC; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000010795};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..145
FT /note="DAC"
FT /evidence="ECO:0000259|PROSITE:PS51794"
SQ SEQUENCE 358 AA; 39816 MW; 19B1F81BD94C334E CRC64;
MKPSNPQDVM NRLLQLVAPG TPFREGLENV LRAKTGALIV VGYGPEVAAV VDGGFAIDCE
FTPNNLYELA KMDGAIILSG DLERILYANA QLIPDSSIPS SETGIRHRTA ERVAKQTGKL
VISISQRRGV ITLYQGDLRY ALKDIGVILT KANQAIQTLE HYMTVLRQDF TNLSASEFEE
IVTLAEVASV IQRIERVLRV KAEIQRYIHE LGTEGRLIRM QLEELVGGIE NEYKLLLNDY
AKNVEADKVR EVAASLGRLT IEELLDPAVV VRLLGHPHAQ AGAEEPVRPR GFRLLSKIPR
LPSVIRNNLV QRFGSLPRIL AATIEELDEV DGVGEARARA IRDGLRRLQE QVFIDRHI
//
