ID A0A1Y4EYR9_9FIRM Unreviewed; 680 AA.
AC A0A1Y4EYR9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN ORFNames=B5F53_16670 {ECO:0000313|EMBL:OUO76624.1};
OS Blautia sp. An249.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=1965603 {ECO:0000313|EMBL:OUO76624.1, ECO:0000313|Proteomes:UP000195974};
RN [1] {ECO:0000313|Proteomes:UP000195974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An249 {ECO:0000313|Proteomes:UP000195974};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUO76624.1}.
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; NFJL01000023; OUO76624.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4EYR9; -.
DR OrthoDB; 9759476at2; -.
DR Proteomes; UP000195974; 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:UP000195974};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 41..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 365..521
FT /note="DDH"
FT /evidence="ECO:0000259|Pfam:PF01368"
FT DOMAIN 599..672
FT /note="DHHA1"
FT /evidence="ECO:0000259|Pfam:PF02272"
SQ SEQUENCE 680 AA; 76422 MW; 97667F46C991821A CRC64;
MEEKFKLRGR LKQFMRWPFI LSILLILVNV PVYALNIHAG ILLSLITAAY IILSLALFTY
NRPVIMNELL AFASQYEQIE KQMLDNLTMP CALIDEEGNM IWSNKKFLEL TKVDSGYKKN
ISLLFPEINK ELLSGKNESQ EKQIHYGDRI FNATFRRISL GNLAESTNMI EGLDDKTSVV
AVYLLDKTEL AEYIQEIEDN KLVVALAYLD NYDEALESVE EVRRSLLIAL IDRKITKYFS
NYDGMVRKLE KDKYFLIMRQ SSLKKLKEQK FPILDEVKTV NIGNEMSVTL SIGIGINAST
YIQDYEYSRI AIEMALGRGG DQVVIKDGDT ITYFGGKSQQ MEKTTRVKAR VKAQALKEFI
STRDRVVVMG HKITDVDAFG AAVGIYRAAK TLGKPAHIVV NDPTTSIRPL MAGFVESSDY
ADDMFLSSQE AKELVDNRCV VVVVDTNKPS YTECEDLLYK TKTIVVLDHH RRGSEVIQNA
VLSYVEPYAS STCEMVAEIL QYFSDGIRIR NIEADSIYAG IMIDTNNFTT RAGVRTFEAA
AFLRRCGADV TRVRKMLRDD MDSYRARAET ICNAIVYKTS FVIGVCPSEG LKSPTVVGAQ
AANELLNIDG VKASFVLTKY KGIIYISARA IDEVNVQVMM ERLGGGGHMN VSGAQISGRS
VEDVVQMIKD IIDDLNQEEV
//
