(data stored in ACNUC7421 zone)

SWISSPROT: E3J8L9_FRAIE

ID   E3J8L9_FRAIE            Unreviewed;       359 AA.
AC   E3J8L9;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   16-JAN-2019, entry version 59.
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=FraEuI1c_0376 {ECO:0000313|EMBL:ADP78462.1};
OS   Frankia inefficax (strain DSM 45817 / CECT 9037 / EuI1c).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298654 {ECO:0000313|EMBL:ADP78462.1, ECO:0000313|Proteomes:UP000002484};
RN   [1] {ECO:0000313|EMBL:ADP78462.1, ECO:0000313|Proteomes:UP000002484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45817 / CECT 9037 / EuI1c
RC   {ECO:0000313|Proteomes:UP000002484};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Beauchemin N., Sen A., Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.;
RT   "Complete sequence of Frankia sp. EuI1c.";
RL   Submitted (OCT-2010) 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 acts as a signaling molecule that couples DNA integrity
CC       with progression of sporulation. The rise in c-di-AMP level
CC       generated by DisA while scanning the chromosome, operates as a
CC       positive signal that advances sporulation; upon encountering a
CC       lesion, the DisA focus arrests at the damaged site and halts c-di-
CC       AMP synthesis. {ECO:0000256|HAMAP-Rule:MF_01438}.
CC   -!- FUNCTION: Participates in a DNA-damage check-point that is active
CC       prior to asymmetric division when DNA is damaged. DisA forms
CC       globular foci that rapidly scan along the chromosomes during
CC       sporulation, searching for lesions. When a lesion is present, DisA
CC       pauses at the lesion site. This triggers a cellular response that
CC       culminates in a temporary block in sporulation initiation.
CC       {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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002299; ADP78462.1; -; Genomic_DNA.
DR   RefSeq; WP_013421585.1; NC_014666.1.
DR   STRING; 298654.FraEuI1c_0376; -.
DR   EnsemblBacteria; ADP78462; ADP78462; FraEuI1c_0376.
DR   KEGG; fri:FraEuI1c_0376; -.
DR   eggNOG; ENOG4105E59; Bacteria.
DR   eggNOG; COG1623; LUCA.
DR   HOGENOM; HOG000236713; -.
DR   KO; K07067; -.
DR   OMA; SKMDGAI; -.
DR   OrthoDB; 1139866at2; -.
DR   BioCyc; FSP298654:G1GOT-377-MONOMER; -.
DR   Proteomes; UP000002484; 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; E3J8L9.
DR   SWISS-2DPAGE; E3J8L9.
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:UP000002484};
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:UP000002484};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01438,
KW   ECO:0000256|SAAS:SAAS00772224}.
FT   DOMAIN        7    145       DAC. {ECO:0000259|PROSITE:PS51794}.
FT   NP_BIND     105    109       ATP. {ECO:0000256|HAMAP-Rule:MF_01438}.
FT   COILED      149    179       {ECO:0000256|SAM:Coils}.
FT   BINDING      74     74       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01438}.
FT   BINDING      92     92       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01438}.
SQ   SEQUENCE   359 AA;  38850 MW;  CB5C760DB86C6981 CRC64;
     MAGPPGDEAF RTTLAAVAPG TPFRDGLERI LRGHTGALIV LGHDKVVEGV CTGGFQLDVE
     FSATRLRELA KMDGAIVVST DLNRIVRAAV HLVPDPTIPT EESGTRHRTA ERVARQTALP
     VISVSQSMRI IALYVGGRRY VLDDSAAILS RANQALATLE RYKQRLDEVA GTLSALEIED
     LVTVRDAISV LQRLEMVRRI ADEIEGYVVE LGTDGRLLSL QLEELMAGVE TERELTVRDY
     QPVGAKVGSP AEVLTDLAAM SATDLLDLTA LARALGFGSG ADALDRQISP RGYRMLAKIP
     RLPRLIVDRL VDHFTTLQKL LAAGVDDLQA VEGVGETRAK AVREGLSRLA ESSILERYA
//

If you have problems or comments...

PBIL Back to PBIL home page