ID R7FG52_9CLOT Unreviewed; 672 AA.
AC R7FG52;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN ORFNames=BN670_00155 {ECO:0000313|EMBL:CDE13820.1};
OS Clostridium sp. CAG:470.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262812 {ECO:0000313|EMBL:CDE13820.1, ECO:0000313|Proteomes:UP000018084};
RN [1] {ECO:0000313|EMBL:CDE13820.1, ECO:0000313|Proteomes:UP000018084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:470 {ECO:0000313|Proteomes:UP000018084};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDE13820.1}.
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; CBII010000007; CDE13820.1; -; Genomic_DNA.
DR AlphaFoldDB; R7FG52; -.
DR Proteomes; UP000018084; 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}.
FT DOMAIN 358..512
FT /note="DDH"
FT /evidence="ECO:0000259|Pfam:PF01368"
FT DOMAIN 541..659
FT /note="DHHA1"
FT /evidence="ECO:0000259|Pfam:PF02272"
SQ SEQUENCE 672 AA; 76407 MW; 8B48846B244041BC CRC64;
MQTSNKKIFD NLVSRTKIYL VIILILLIGI SWQNKILIIP SVILYALILG YTYFANNKRK
SEISETLQDL TLTVDSAAKT SLINSPFPLI ILETDGNVVW KSSKFATEFE DIDINTFVND
LIYDLKDEIK NKKNSTDKSI LKNIQVNKRQ YRMVGKFVNS KRYSKNEKNE YMAILYFIDE
TENIKLQNEY NDSKSCVGII MIDNYEENMQ MLESEEKAQY IAEIDKVIYE WTNETNGILI
KSDRDRYIYI FEQRYLEKIK EDKFSILDKI KDLDPKQKVQ FTLSIAISNE GEVDKDKYKS
AQTAMDIVLG RGGDQAVVRQ NDIYKFFGGR SQEVEKRTKV KARVVAHALE NLIKESSKVM
VMGHTNPDID AIGSAIGVYR LAKSLDKNAY IISNKRPALQ NFMESLKEEP EYEDVIISKE
VAEENIDEDT LLVVVDTHKV TYVESEEVLK KASKIVIIDH HRRSADYIEN ATLTFQEVYA
SSAAELVTEL LQYAEVNVEL KKIEAEALYA GIMMDTKSFT FKTGVRTFEA AAYLRKCGVD
IIRVKKWFQS DLESFNKIAD IVKKAEIVND SIAIALCENE KSKDISLLCA KAADELLTIS
DVTASFVLGD TGEKICISGR SIGDINVQVI LEKLGGGGHI TLAGAQVEGM TIEEVKQELI
IRINEYFTEI EN
//
