ID D0YY24_PHODD Unreviewed; 511 AA.
AC D0YY24;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=cyclic-guanylate-specific phosphodiesterase {ECO:0000256|ARBA:ARBA00012282};
DE EC=3.1.4.52 {ECO:0000256|ARBA:ARBA00012282};
GN ORFNames=VDA_002187 {ECO:0000313|EMBL:EEZ41155.1};
OS Photobacterium damselae subsp. damselae CIP 102761.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=675817 {ECO:0000313|EMBL:EEZ41155.1, ECO:0000313|Proteomes:UP000003579};
RN [1] {ECO:0000313|EMBL:EEZ41155.1, ECO:0000313|Proteomes:UP000003579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 102761 {ECO:0000313|EMBL:EEZ41155.1,
RC ECO:0000313|Proteomes:UP000003579};
RG Los Alamos National Laboratory (LANL);
RG National Microbial Pathogen Data Resource (NMPDR);
RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA Brettin T.S., Colwell R., Huq A., Grim C.J., Hasan N.A., Vonstein V.,
RA Bartels D.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',3'-c-di-GMP + H2O = 5'-phosphoguanylyl(3'->5')guanosine +
CC H(+); Xref=Rhea:RHEA:24902, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58754, ChEBI:CHEBI:58805; EC=3.1.4.52;
CC Evidence={ECO:0000256|ARBA:ARBA00034290};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; ADBS01000001; EEZ41155.1; -; Genomic_DNA.
DR RefSeq; WP_005299612.1; NZ_ADBS01000001.1.
DR AlphaFoldDB; D0YY24; -.
DR eggNOG; COG2200; Bacteria.
DR Proteomes; UP000003579; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0071111; F:cyclic-guanylate-specific phosphodiesterase activity; IEA:UniProtKB-EC.
DR CDD; cd01948; EAL; 1.
DR Gene3D; 3.20.20.450; EAL domain; 1.
DR InterPro; IPR024744; CSS-motif_dom.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR PANTHER; PTHR33121; CYCLIC DI-GMP PHOSPHODIESTERASE PDEF; 1.
DR PANTHER; PTHR33121:SF80; CYCLIC DI-GMP PHOSPHODIESTERASE PDEL-RELATED; 1.
DR Pfam; PF12792; CSS-motif; 1.
DR Pfam; PF00563; EAL; 1.
DR SMART; SM00052; EAL; 1.
DR SUPFAM; SSF141868; EAL domain-like; 1.
DR PROSITE; PS50883; EAL; 1.
PE 4: Predicted;
KW c-di-GMP {ECO:0000256|ARBA:ARBA00022636};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000003579};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 249..504
FT /note="EAL"
FT /evidence="ECO:0000259|PROSITE:PS50883"
SQ SEQUENCE 511 AA; 59348 MW; E7C85D20F95C6662 CRC64;
MSKSKTILLF ICSVIIGLAV NLIWIRFQVN HQTEEMLSTI DTATTQYLNR MTNEIKFLHS
TAPICSETFI NHLESTVLKS MSIQEITYIN KNQFICSDRG MQEQAQTINI EQLNKYKDNN
GYIIYRGRSL RYDIDGLYIM LPVAKQTWYR FLINDAFLKF WLEQHLLDKH IHACVNSLGQ
TIVCTGPHES QYQHTYHRYS ENYNLHFTAS FDNEIYWCYF KYNLPYTIIL LTIFSSLCLV
LAHNYYHRRQ SLSAEIQRGI DNHEFIGYYQ PIISAKNNRW CGAELLVRWN HPKAGLIPPD
QFIHIAERSE LIHQMTLDLI KQIALQKTYI EQLVPHSYFS INMTPSMIAN TQFVTKLVQI
LQMNPDLQHG LVIELTEREP FSPAKLLKLK QGMDLLRSYG VKWALDDFGT GYSGLATLQQ
LSFDILKIDR TFINLSSNDA ISLSILDNIA QMGHKLHCSL VAEGVETKEQ AQYAKKIGIE
ACQGYYYAKP MTFDDYYHAL KNHLGNRFIP L
//
