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Database: UniProt
Entry: C7PWS8_CATAD
LinkDB: C7PWS8_CATAD
Original site: C7PWS8_CATAD 
ID   C7PWS8_CATAD            Unreviewed;       362 AA.
AC   C7PWS8;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   RecName: Full=DNA integrity scanning protein DisA {ECO:0000256|HAMAP-Rule:MF_01438};
DE   AltName: Full=Cyclic di-AMP synthase {ECO:0000256|HAMAP-Rule:MF_01438};
DE            Short=c-di-AMP synthase {ECO:0000256|HAMAP-Rule:MF_01438};
DE   AltName: Full=Diadenylate cyclase {ECO:0000256|HAMAP-Rule:MF_01438};
DE            EC=2.7.7.85 {ECO:0000256|HAMAP-Rule:MF_01438};
GN   Name=disA {ECO:0000256|HAMAP-Rule:MF_01438};
GN   OrderedLocusNames=Caci_8362 {ECO:0000313|EMBL:ACU77185.1};
OS   Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL
OS   B-24433 / ID139908).
OC   Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC   Catenulisporaceae; Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU77185.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU77185.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647; DOI=10.4056/sigs.17259;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., Chen F.,
RA   Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Mikhailova N.,
RA   Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Ali Z., Tindall B.J., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
CC   -!- FUNCTION: Has also diadenylate cyclase activity, catalyzing the
CC       condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). c-di-AMP
CC       likely acts as a signaling molecule that may couple DNA integrity with
CC       a cellular process. {ECO:0000256|HAMAP-Rule:MF_01438}.
CC   -!- FUNCTION: Participates in a DNA-damage check-point. DisA forms globular
CC       foci that rapidly scan along the chromosomes searching for lesions.
CC       {ECO:0000256|HAMAP-Rule:MF_01438}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_01438};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01438};
CC   -!- SUBUNIT: Homooctamer. {ECO:0000256|HAMAP-Rule:MF_01438}.
CC   -!- SIMILARITY: Belongs to the DisA family. {ECO:0000256|HAMAP-
CC       Rule:MF_01438}.
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DR   EMBL; CP001700; ACU77185.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7PWS8; -.
DR   STRING; 479433.Caci_8362; -.
DR   KEGG; cai:Caci_8362; -.
DR   eggNOG; COG1623; Bacteria.
DR   HOGENOM; CLU_787128_0_0_11; -.
DR   InParanoid; C7PWS8; -.
DR   OMA; VVRDYVP; -.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0106408; F:diadenylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0019932; P:second-messenger-mediated signaling; IEA:UniProtKB-UniRule.
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; 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; IPR000445; HhH_motif.
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; PF00633; HHH; 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, ECO:0000256|HAMAP-
KW   Rule:MF_01438};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_01438};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_01438};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01438};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01438};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01438};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_01438}; Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01438}.
FT   DOMAIN          8..146
FT                   /note="DAC"
FT                   /evidence="ECO:0000259|PROSITE:PS51794"
FT   BINDING         75
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01438"
FT   BINDING         93
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01438"
FT   BINDING         106..110
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01438"
SQ   SEQUENCE   362 AA;  39031 MW;  6DC0372481946E9D CRC64;
     MTGEASERAA LSAILSTVAP GTVLRDGLER ILRGNTGGLV VFGFDKLVDE MSTGGFVLDV
     EFSPQRLREL CKMDGAVVVS SDGSRIVRAG VQLVPDAAIP TEETGTRHRT ADRVAKQTGF
     PVLSVSQSMR IIALYLRGQR VVLEDSGAIL SKANQALATL ERYKLRLDEV TGTLSALEIE
     DLVTVRDVAA VAQRLEMVTR IADEVAGYVV QLGVDGRLLS LQLDELMAGV DPDRDLIARD
     YLPERTGKKA RTVADVSDDL GSLDRTQLLD LLQVARAMGF GGGVEVLESA VSPRGYRLLA
     KVPRLPGAVI DRLVEHFGGL QKLLAASIDD LQRVEGVGET RARSVREGLS RLAESSILER
     YV
//
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