ID   A0A3A9SFA3_9FIRM        Unreviewed;       683 AA.
AC   A0A3A9SFA3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE            EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN   ORFNames=D6855_14870 {ECO:0000313|EMBL:RKM56141.1};
OS   Butyrivibrio sp. CB08.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=2364879 {ECO:0000313|EMBL:RKM56141.1, ECO:0000313|Proteomes:UP000281491};
RN   [1] {ECO:0000313|Proteomes:UP000281491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB08 {ECO:0000313|Proteomes:UP000281491};
RA   Hivarkar S., Lanjekar V.B., Dhakephalkar P.K., Dagar S.;
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has phosphodiesterase (PDE) activity against cyclic-di-AMP
CC       (c-di-AMP). {ECO:0000256|PIRNR:PIRNR026583}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3',3'-c-di-AMP + H2O = 5'-O-phosphonoadenylyl-(3'->5')-
CC         adenosine + H(+); Xref=Rhea:RHEA:54420, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:71500, ChEBI:CHEBI:138171;
CC         Evidence={ECO:0000256|PIRNR:PIRNR026583};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR026583}.
CC   -!- SIMILARITY: Belongs to the GdpP/PdeA phosphodiesterase family.
CC       {ECO:0000256|PIRNR:PIRNR026583}.
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:RKM56141.1}.
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DR   EMBL; RAIR01000010; RKM56141.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A9SFA3; -.
DR   OrthoDB; 9759476at2; -.
DR   Proteomes; UP000281491; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0106409; F:cyclic-di-AMP phosphodiesterase activity; IEA:RHEA.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.310.30; -; 1.
DR   Gene3D; 3.90.1640.10; inorganic pyrophosphatase (n-terminal core); 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR001667; DDH_dom.
DR   InterPro; IPR038763; DHH_sf.
DR   InterPro; IPR003156; DHHA1_dom.
DR   InterPro; IPR014528; GdpP/PdeA.
DR   PANTHER; PTHR47618; BIFUNCTIONAL OLIGORIBONUCLEASE AND PAP PHOSPHATASE NRNA; 1.
DR   PANTHER; PTHR47618:SF2; CYCLIC-DI-AMP PHOSPHODIESTERASE GDPP; 1.
DR   Pfam; PF01368; DHH; 1.
DR   Pfam; PF02272; DHHA1; 1.
DR   PIRSF; PIRSF026583; YybT; 1.
DR   SUPFAM; SSF64182; DHH phosphoesterases; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|PIRNR:PIRNR026583};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR026583};
KW   Membrane {ECO:0000256|PIRNR:PIRNR026583, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000281491};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        16..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          367..523
FT                   /note="DDH"
FT                   /evidence="ECO:0000259|Pfam:PF01368"
FT   DOMAIN          553..673
FT                   /note="DHHA1"
FT                   /evidence="ECO:0000259|Pfam:PF02272"
SQ   SEQUENCE   683 AA;  76285 MW;  A8AC829BC6493B84 CRC64;
     MANKNRVRLK GRLRSYFRVF TYLGILLLLV NAAVFTVNFT AGLILLAFTG LYFIAILYMN
     FYSKPIIMNE LVSFATEYGQ IQKKLLRELE LPHAVLDDSG KVVWTNIAFE KVVHQDKGFR
     KTIFSLFPSI TMDKFPQGAE EVSYELEYEN SNYTIKMKRI SLKEMATNSD IIDAESYEGS
     LIAVYLFDET ALKLAIQEVD NQSLAAGLIY LDNYEEALDS VEEVRRSLLT ALIDRKVNKY
     IASCNGISKK IEKDKYFVVM PKKSCELLKE QKFDILEDVK TVNIGNEMAV TLSIGIGLNG
     LSYAQNYEFA RNAIDVALGR GGDQAVVKSA DNISYYGGKS QQIEKSTRVK ARVKAHALRE
     IISGKDNVIV MGHRIGDVDS FGSSVGIYRI AKTLDRKCHI VLNDVTTSMQ PLVDLFKNNP
     EYEDDMIITN QQAIDIAGNN TVLVVVDVNK PSITECPELL RFCKTIVVLD HHRQGTEVVE
     NATLSYVEPY ASSACEMVSE ILQYIGENVK IHNEEADSLY SGIMVDTNNF MNKTGVRTFE
     AAAFLRRNGA DVTRVRKLFR EDAGEYKAKA DTVSQAEIYR SKFAISILSN EEIQSPTIVG
     AQAANELLNI KGVRASFVCT DYQNQIYVSA RSIDEVNVQV IMEKLGGGGH MSSAGCQMDG
     VTTEEAIATL KRTLDQMIDE GEL
//