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
//