(data stored in ACNUC1104 zone)

SWISSPROT: A1SDX6_NOCSJ

ID   A1SDX6_NOCSJ            Unreviewed;       360 AA.
AC   A1SDX6;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   10-APR-2019, entry version 83.
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=Noca_0469 {ECO:0000313|EMBL:ABL80011.1};
OS   Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Nocardioides.
OX   NCBI_TaxID=196162 {ECO:0000313|EMBL:ABL80011.1, ECO:0000313|Proteomes:UP000000640};
RN   [1] {ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Mattes T., Gossett J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABL80011.1, ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RX   PubMed=21551312; DOI=10.1128/JB.05109-11;
RA   Coleman N.V., Wilson N.L., Barry K., Brettin T.S., Bruce D.C.,
RA   Copeland A., Dalin E., Detter J.C., Del Rio T.G., Goodwin L.A.,
RA   Hammon N.M., Han S., Hauser L.J., Israni S., Kim E., Kyrpides N.,
RA   Land M.L., Lapidus A., Larimer F.W., Lucas S., Pitluck S.,
RA   Richardson P., Schmutz J., Tapia R., Thompson S., Tice H.N.,
RA   Spain J.C., Gossett J.G., Mattes T.E.;
RT   "Genome Sequence of the ethene- and vinyl chloride-oxidizing
RT   actinomycete Nocardioides sp. strain JS614.";
RL   J. Bacteriol. 193:3399-3400(2011).
CC   -!- FUNCTION: Has also diadenylate cyclase activity, catalyzing the
CC       condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). c-
CC       di-AMP likely acts as a signaling molecule that may couple DNA
CC       integrity with a cellular process. {ECO:0000256|HAMAP-
CC       Rule:MF_01438}.
CC   -!- FUNCTION: Participates in a DNA-damage check-point. DisA forms
CC       globular foci that rapidly scan along the chromosomes searching
CC       for lesions. {ECO:0000256|HAMAP-Rule:MF_01438}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP = c-di-AMP + 2 diphosphate; Xref=Rhea:RHEA:35655,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:71500;
CC         EC=2.7.7.85; Evidence={ECO:0000256|HAMAP-Rule:MF_01438,
CC         ECO:0000256|SAAS:SAAS01115408};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01438, ECO:0000256|SAAS:SAAS00724644};
CC   -!- SUBUNIT: Homooctamer. {ECO:0000256|HAMAP-Rule:MF_01438}.
CC   -!- SIMILARITY: Belongs to the DisA family. {ECO:0000256|HAMAP-
CC       Rule:MF_01438, ECO:0000256|SAAS:SAAS00724629}.
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DR   EMBL; CP000509; ABL80011.1; -; Genomic_DNA.
DR   RefSeq; WP_011753962.1; NC_008699.1.
DR   STRING; 196162.Noca_0469; -.
DR   EnsemblBacteria; ABL80011; ABL80011; Noca_0469.
DR   KEGG; nca:Noca_0469; -.
DR   eggNOG; ENOG4105E59; Bacteria.
DR   eggNOG; COG1623; LUCA.
DR   HOGENOM; HOG000236713; -.
DR   KO; K07067; -.
DR   OMA; SKMDGAI; -.
DR   OrthoDB; 1139866at2; -.
DR   Proteomes; UP000000640; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; 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; 1.20.1260.110; -; 1.
DR   Gene3D; 3.40.1700.10; -; 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   Pfam; PF10635; DisA-linker; 1.
DR   Pfam; PF02457; DisA_N; 1.
DR   Pfam; PF12826; HHH_2; 1.
DR   SUPFAM; SSF143597; SSF143597; 1.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   PROSITE; PS51794; DAC; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1SDX6.
DR   SWISS-2DPAGE; A1SDX6.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01438,
KW   ECO:0000256|SAAS:SAAS00772210}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000640};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_01438,
KW   ECO:0000256|SAAS:SAAS00724631};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_01438,
KW   ECO:0000256|SAAS:SAAS00724636};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01438,
KW   ECO:0000256|SAAS:SAAS00724650};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01438,
KW   ECO:0000256|SAAS:SAAS00724630};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01438,
KW   ECO:0000256|SAAS:SAAS00772222};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01438,
KW   ECO:0000256|SAAS:SAAS00772249};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000640};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01438,
KW   ECO:0000256|SAAS:SAAS00772224}.
FT   DOMAIN        9    147       DAC. {ECO:0000259|PROSITE:PS51794}.
FT   NP_BIND     107    111       ATP. {ECO:0000256|HAMAP-Rule:MF_01438}.
FT   COILED      161    181       {ECO:0000256|SAM:Coils}.
FT   BINDING      76     76       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01438}.
FT   BINDING      94     94       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01438}.
SQ   SEQUENCE   360 AA;  39196 MW;  3169A4B829CFBEC0 CRC64;
     MATDRSDDIL RLRATLATIA PGTPLRDGLE RILRGRTGAL IVLGHDKVVE SISTGGFTLD
     VPFTATGLRE LAKMDGAIIV DRDVTRIQRA AVHLMPDHTI PSEETGTRHR TADRVARQTG
     FPVISVSQSM QIIAAYVGET RHVLEDSGQI LSRANQALAT LERYKLRLDE VSSTLSALEI
     EDLVTVRDVA VVAQRLEMVT RIASEIEDYV LELGTDGRLL SLQLEELITG VDTERELVIR
     DYLPAGRRSK SPEALLNRLE SLSSTELVDP AAAARALGLG NGEHLDGAVA PRGFRLLAKV
     PRLPATVVDR LVDHFGTLQK LLSAGVDDLQ AVEGVGELRA RSVREGLSRL AESTILERYV
//

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