(data stored in SCRATCH zone)

SWISSPROT: A4F6V9_SACEN

ID   A4F6V9_SACEN            Unreviewed;       370 AA.
AC   A4F6V9;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 80.
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=SACE_0435 {ECO:0000313|EMBL:CAL99783.1};
GN   ORFNames=A8924_0832 {ECO:0000313|EMBL:PFG93585.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99783.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99783.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAL99783.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG93585.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93585.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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; AM420293; CAL99783.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93585.1; -; Genomic_DNA.
DR   RefSeq; WP_009947452.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0435; -.
DR   EnsemblBacteria; CAL99783; CAL99783; SACE_0435.
DR   KEGG; sen:SACE_0435; -.
DR   eggNOG; ENOG4105E59; Bacteria.
DR   eggNOG; COG1623; LUCA.
DR   HOGENOM; HOG000236713; -.
DR   KO; K07067; -.
DR   OMA; SKMDGAI; -.
DR   OrthoDB; 1139866at2; -.
DR   BioCyc; SERY405948:SACE_RS02140-MONOMER; -.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
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; A4F6V9.
DR   SWISS-2DPAGE; A4F6V9.
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:UP000006728,
KW   ECO:0000313|Proteomes:UP000225825};
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:UP000006728};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01438,
KW   ECO:0000256|SAAS:SAAS00772224}.
FT   DOMAIN        2    140       DAC. {ECO:0000259|PROSITE:PS51794}.
FT   NP_BIND     100    104       ATP. {ECO:0000256|HAMAP-Rule:MF_01438}.
FT   COILED      147    174       {ECO:0000256|SAM:Coils}.
FT   BINDING      69     69       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01438}.
FT   BINDING      87     87       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01438}.
SQ   SEQUENCE   370 AA;  40685 MW;  5622F622FA922510 CRC64;
     MNEKLRATLA WLAPGTALRD GLERILRGRT GGLVVLGYDE VVESLCDGGF HLDVEFSATR
     LRELSKMDGA VVLSSDATRI VRANVQLVPD ASIRTDESGT RHRSAERTAI HTGYPVVSVS
     QSMSIISLYF QGHRHLLIGS PDILSRANQA LATLERYTAR LAEVAQTLSA LEIEDYVTLR
     DAMTVVQRLE MVRRIADEIE VDVVELGQDG RLIELQLDEL VGAERDTRGT GKRGRTLDRV
     DVDRELIVQE YLPTGGPMPT SEEVAEALAK LDGTELLDLT AIAKAFGYPG TPEVLDQHLQ
     PRGYRLLARV PRLPAVARKQ LVEHFGSLQN LLAATAEDLS VVESVGESRA RQVREGLSRL
     AEASIMDRYA
//

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