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Database: UniProt
Entry: M0EA94_9EURY
LinkDB: M0EA94_9EURY
Original site: M0EA94_9EURY 
ID   M0EA94_9EURY            Unreviewed;       269 AA.
AC   M0EA94;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Diadenylate cyclase {ECO:0000256|HAMAP-Rule:MF_00840};
DE            Short=DAC {ECO:0000256|HAMAP-Rule:MF_00840};
DE            EC=2.7.7.85 {ECO:0000256|HAMAP-Rule:MF_00840};
DE   AltName: Full=Cyclic-di-AMP synthase {ECO:0000256|HAMAP-Rule:MF_00840};
DE            Short=c-di-AMP synthase {ECO:0000256|HAMAP-Rule:MF_00840};
GN   Name=dacZ {ECO:0000256|HAMAP-Rule:MF_00840};
GN   ORFNames=C463_06942 {ECO:0000313|EMBL:ELZ44675.1};
OS   Halorubrum californiense DSM 19288.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halorubrum.
OX   NCBI_TaxID=1227465 {ECO:0000313|EMBL:ELZ44675.1, ECO:0000313|Proteomes:UP000011586};
RN   [1] {ECO:0000313|EMBL:ELZ44675.1, ECO:0000313|Proteomes:UP000011586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19288 {ECO:0000313|EMBL:ELZ44675.1,
RC   ECO:0000313|Proteomes:UP000011586};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- FUNCTION: Diadenylate cyclase that catalyzes the condensation of 2 ATP
CC       molecules into cyclic di-AMP (c-di-AMP). c-di-AMP is a second messenger
CC       for intracellular signal transduction involved in the control of
CC       important regulatory processes such as osmoregulation.
CC       {ECO:0000256|HAMAP-Rule:MF_00840}.
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_00840};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00840};
CC   -!- SIMILARITY: Belongs to the adenylate cyclase family. DacZ subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00840}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ELZ44675.1}.
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DR   EMBL; AOJK01000036; ELZ44675.1; -; Genomic_DNA.
DR   RefSeq; WP_008442302.1; NZ_AOJK01000036.1.
DR   AlphaFoldDB; M0EA94; -.
DR   STRING; 1227465.C463_06942; -.
DR   PATRIC; fig|1227465.4.peg.1357; -.
DR   OrthoDB; 85944at2157; -.
DR   Proteomes; UP000011586; Unassembled WGS sequence.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0106408; F:diadenylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019932; P:second-messenger-mediated signaling; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1700.10; DNA integrity scanning protein, DisA, N-terminal domain; 1.
DR   HAMAP; MF_00840; DacZ; 1.
DR   InterPro; IPR014499; DAC_DacZ.
DR   InterPro; IPR045586; DacZ_N.
DR   InterPro; IPR036888; DNA_integrity_DisA_N_sf.
DR   InterPro; IPR003390; DNA_integrity_scan_DisA_N.
DR   NCBIfam; NF041371; Diadnylcyc_Halo; 1.
DR   PANTHER; PTHR34185; DIADENYLATE CYCLASE; 1.
DR   PANTHER; PTHR34185:SF1; DIADENYLATE CYCLASE; 1.
DR   Pfam; PF02457; DAC; 1.
DR   Pfam; PF19294; DACZ_N; 1.
DR   PIRSF; PIRSF019073; UCP019073; 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_00840}; Manganese {ECO:0000256|HAMAP-Rule:MF_00840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00840};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_00840};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00840}.
FT   DOMAIN          109..266
FT                   /note="DAC"
FT                   /evidence="ECO:0000259|PROSITE:PS51794"
SQ   SEQUENCE   269 AA;  28698 MW;  AA1AE9E986605BD5 CRC64;
     MASLTDHLAD LVAEVDAALL FSPTSSFYER FADDGSEVVV VAPDNDVDAE TFVDLPLPFD
     NVKDRIRFGI EGAMDADLVS EGDEVACVAS VFDGGSDAVI RATVDQGVHT GIYDLFANSR
     AEPSVIRDVF EVAIELGQKG QKGKPVGALF VVGDAGKVMN KSRPLSYNPF EKSHVHVGDP
     IVNVMLKEFS RLDGAFVVSD SGKIVSAYRY LEPAAEGVDI PKGLGARHMS GAAITRDTNS
     TAIVLSESDG LVRAFKAGEL VLEIDPEEY
//
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