ID T1HTV2_RHOPR Unreviewed; 888 AA.
AC T1HTV2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=cGMP-specific 3',5'-cyclic phosphodiesterase {ECO:0000256|ARBA:ARBA00040719};
DE EC=3.1.4.35 {ECO:0000256|ARBA:ARBA00012319};
DE Flags: Fragment;
OS Rhodnius prolixus (Triatomid bug).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX NCBI_TaxID=13249 {ECO:0000313|EnsemblMetazoa:RPRC007472-PA, ECO:0000313|Proteomes:UP000015103};
RN [1] {ECO:0000313|Proteomes:UP000015103}
RP NUCLEOTIDE SEQUENCE.
RA Wilson R.K., Warren W., Dotson E., Oliveira P.L.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:RPRC007472-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746,
CC ChEBI:CHEBI:58115; EC=3.1.4.35;
CC Evidence={ECO:0000256|ARBA:ARBA00000583};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|ARBA:ARBA00001968};
CC -!- SUBUNIT: Interacts with PrBP. {ECO:0000256|ARBA:ARBA00038662}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004342};
CC Lipid-anchor {ECO:0000256|ARBA:ARBA00004342}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004342}. Membrane
CC {ECO:0000256|ARBA:ARBA00004423}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004423}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004423}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000256|ARBA:ARBA00007648}.
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DR EMBL; ACPB03014254; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ACPB03014255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ACPB03014256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ACPB03014257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1HTV2; -.
DR STRING; 13249.T1HTV2; -.
DR EnsemblMetazoa; RPRC007472-RA; RPRC007472-PA; RPRC007472.
DR VEuPathDB; VectorBase:RPRC007472; -.
DR eggNOG; KOG3689; Eukaryota.
DR HOGENOM; CLU_006980_0_2_1; -.
DR InParanoid; T1HTV2; -.
DR OMA; ATIRMFK; -.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000015103; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 3.30.450.40; -; 2.
DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR023088; PDEase.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR11347:SF216; PHOSPHODIESTERASE; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00065; GAF; 2.
DR SUPFAM; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW cGMP {ECO:0000256|ARBA:ARBA00022535};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Prenylation {ECO:0000256|ARBA:ARBA00023289};
KW Reference proteome {ECO:0000313|Proteomes:UP000015103};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
SQ SEQUENCE 888 AA; 101174 MW; A041AE2044649863 CRC64;
KRPSITSELF NLWLTSSPIK RSRSPSRPRA SGEWRRRLDL LDEGELFMEL IRDVSNELDI
DVLCHKILVN VGLLTRADRG SLFLARGSLE AKYLVAKLFD VTVDTELEDA IQKAKAEEIR
IPFGIGVAGV VAQNKKVINI TDAYTDPRFN SEIDMRTGYK TNTILCGPIC NYEGDVIGVA
QIINKTDGAS EFSERDVEVF QRYLTFCGIG IQNAQLFEMS VQEFKRNQIL LNLARSIFEE
QSNLERLVTK IMTEARDLLK CESCAVYLLD HNCGEAIHLE TLGEKAVTSI PERKPLCRRE
SNNLNVNDIL LPKSAMMKFS TIFELRSESH KAIVKTPNQE DMDNSKLSQI ASYVASTGQI
LNIGDLSTWM NQEVTGDGES NDLVARCILC MPIINSQKQV IGVAQLINKE TGHPFTDCDV
SIFEAFAIFC GLGIHNTQMY ENACKLMAKQ KVALECLSYH ATANLDDTLK LCKDTIPSAQ
EYNLFSFKFI DFDLNDDDTC RATIRMFLEC DLVNQYHIPY DVLCRWVLSV KKNYRPVKYH
NWRHALNVAQ TMFAMLKTGK MERFMTDLEV NSRLACIFIF TNHRGTNNAF QTKTESPLAI
LYTTSTMEHH HFDQCVMILN SEGNNIFQAL SPDDYRHVMK VVEHSILSTD LAMYFKKKSS
FIELIENGEF DWQSEGKKEL LCGMMMTGCD VGAIAKPWEV QHKVAKLVAD EFFDQGDLEK
LQLNTQPVAM MDRERKDELP QMQVGFIDVI CLPLYKILSD TFPWILPLYE GTLDNRQRWQ
DLAEKVEMGL TWIDHDTIEK PIEEFSIDQD TKDIEFTVTT LNWDNTGQRK ANGTTMGRFT
SLRKNRALGK SVKSRLSRSL YSRSVSTQSE DNLSIVTQKP KSKLCSLF
//
