(data stored in ACNUC1104 zone)

SWISSPROT: D5USU9_TSUPD

ID   D5USU9_TSUPD            Unreviewed;       360 AA.
AC   D5USU9;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   16-JAN-2019, entry version 60.
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=Tpau_0598 {ECO:0000313|EMBL:ADG77236.1};
OS   Tsukamurella paurometabola (strain ATCC 8368 / DSM 20162 / JCM 10117 /
OS   NBRC 16120 / NCTC 13040) (Corynebacterium paurometabolum).
OC   Bacteria; Actinobacteria; Corynebacteriales; Tsukamurellaceae;
OC   Tsukamurella.
OX   NCBI_TaxID=521096 {ECO:0000313|EMBL:ADG77236.1, ECO:0000313|Proteomes:UP000001213};
RN   [1] {ECO:0000313|Proteomes:UP000001213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040
RC   {ECO:0000313|Proteomes:UP000001213};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Mikhailova N., Munk A.C., Brettin T., Detter J.C.,
RA   Tapia R., Han C., Larimer F., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete chromosome of Tsukamurella paurometabola DSM 20162.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADG77236.1, ECO:0000313|Proteomes:UP000001213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040
RC   {ECO:0000313|Proteomes:UP000001213};
RX   PubMed=21886861;
RA   Munk A.C., Lapidus A., Lucas S., Nolan M., Tice H., Cheng J.F.,
RA   Del Rio T.G., Goodwin L., Pitluck S., Liolios K., Huntemann M.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Tapia R., Han C., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Yasawong M., Brambilla E.M., Rohde M.,
RA   Sikorski J., Goker M., Detter J.C., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Tsukamurella paurometabola type strain
RT   (no. 33).";
RL   Stand. Genomic Sci. 4:342-351(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; CP001966; ADG77236.1; -; Genomic_DNA.
DR   RefSeq; WP_013125278.1; NC_014158.1.
DR   STRING; 521096.Tpau_0598; -.
DR   PRIDE; D5USU9; -.
DR   EnsemblBacteria; ADG77236; ADG77236; Tpau_0598.
DR   KEGG; tpr:Tpau_0598; -.
DR   eggNOG; ENOG4105E59; Bacteria.
DR   eggNOG; COG1623; LUCA.
DR   HOGENOM; HOG000236713; -.
DR   KO; K07067; -.
DR   OMA; SKMDGAI; -.
DR   OrthoDB; 1139866at2; -.
DR   BioCyc; TPAU521096:G1GKO-578-MONOMER; -.
DR   Proteomes; UP000001213; 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; 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   SUPFAM; SSF143597; SSF143597; 1.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   PROSITE; PS51794; DAC; 1.
PE   3: Inferred from homology;
DR   PRODOM; D5USU9.
DR   SWISS-2DPAGE; D5USU9.
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:UP000001213};
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:UP000001213};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01438,
KW   ECO:0000256|SAAS:SAAS00772224}.
FT   DOMAIN       13    151       DAC. {ECO:0000259|PROSITE:PS51794}.
FT   NP_BIND     111    115       ATP. {ECO:0000256|HAMAP-Rule:MF_01438}.
FT   COILED      165    185       {ECO:0000256|SAM:Coils}.
FT   BINDING      80     80       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01438}.
FT   BINDING      98     98       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01438}.
SQ   SEQUENCE   360 AA;  38749 MW;  3D5395CD89F23A87 CRC64;
     MDLDVADRAF AGNAALRETV TRVAPGTGLR DGIERILRGR TGALIVLGYD DTVERICDGG
     FHLDVEFAPT RLRELSKMDG AVVLSTDGSR IVRANVQLVP DPAIPTQESG TRHRSAERTA
     IETGFPVISV SASMSIVHAY VAGVRHVVED AAPILSRANL AIATLERYRH RLDEVLGELS
     RAEIEDVVAV REVAHVVQRL ELVRRLAIEI EQSVLELGTS GRQIALQLED LLGEAVSLRD
     PVLRDYLPGD ADVGEVVARI DGLSDADLLT ASTVAAALGF SDTVEAQDQP VSPRGYRLLG
     SIPRLQRHQI EALVAAFGSL QTLLAASAAD LQGVPGIGAV WARQVREGLS RLSELSVERY
//

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