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Conserved domains on  [gi|47116962|sp|Q9Z0X4|]
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RecName: Full=cGMP-inhibited 3',5'-cyclic phosphodiesterase 3A; AltName: Full=Cyclic GMP-inhibited phosphodiesterase A; Short=CGI-PDE A

Protein Classification

3',5'-cyclic nucleotide phosphodiesterase( domain architecture ID 10446396)

3',5'-cyclic nucleotide phosphodiesterase catalyzes the hydrolysis of cAMP or cGMP to produce adenosine 5'-phosphate or guanosine 5'-phosphate, respectively

CATH:  1.10.1300.10
EC:  3.1.4.-
Gene Ontology:  GO:0046872|GO:0004114
PubMed:  11008484|9868367
SCOP:  4001423

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
751-1012 2.81e-82

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 267.88  E-value: 2.81e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47116962    751 YHNRIHATDVLHAVWYLttqpipglpsvigdhgsasdsdsdsgFTHGHMGYVFSKmyhvpddkygclsgnipaLELMALY 830
Cdd:pfam00233    1 YHNWRHAFDVTQTMYYL--------------------------LKTGKLKEVLTD------------------LEILALL 36
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47116962    831 VAAAMHDYDHPGRTNAFLVATSAPQAVLYNDRSVLENHHAAAAWNLfMSRPEYNFLVNLDHVEFKHFRFLVIEAILATDL 910
Cdd:pfam00233   37 IAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAFQI-LQDEECNIFSNLSDEEYKEVRKLIISLILATDM 115
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47116962    911 KKHFDFVAKFNAKVNDDVGIDW--TNENDRLLVCQMCIKLADINGPAKCKELHLRWTEGIASEFYEQGDEEASLGLPISP 988
Cdd:pfam00233  116 AKHFELLKKFKSLLESKKTLDFleNEEDRRLLLLSMLIKAADISNPTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSP 195
                          250       260
                   ....*....|....*....|....*
gi 47116962    989 FMDR-SAPQLANLQESFISHIVGPL 1012
Cdd:pfam00233  196 LMDReKKTSLPKSQIGFIDFIVLPL 220
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
751-1012 2.81e-82

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 267.88  E-value: 2.81e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47116962    751 YHNRIHATDVLHAVWYLttqpipglpsvigdhgsasdsdsdsgFTHGHMGYVFSKmyhvpddkygclsgnipaLELMALY 830
Cdd:pfam00233    1 YHNWRHAFDVTQTMYYL--------------------------LKTGKLKEVLTD------------------LEILALL 36
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47116962    831 VAAAMHDYDHPGRTNAFLVATSAPQAVLYNDRSVLENHHAAAAWNLfMSRPEYNFLVNLDHVEFKHFRFLVIEAILATDL 910
Cdd:pfam00233   37 IAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAFQI-LQDEECNIFSNLSDEEYKEVRKLIISLILATDM 115
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47116962    911 KKHFDFVAKFNAKVNDDVGIDW--TNENDRLLVCQMCIKLADINGPAKCKELHLRWTEGIASEFYEQGDEEASLGLPISP 988
Cdd:pfam00233  116 AKHFELLKKFKSLLESKKTLDFleNEEDRRLLLLSMLIKAADISNPTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSP 195
                          250       260
                   ....*....|....*....|....*
gi 47116962    989 FMDR-SAPQLANLQESFISHIVGPL 1012
Cdd:pfam00233  196 LMDReKKTSLPKSQIGFIDFIVLPL 220
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
824-973 4.97e-11

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 61.97  E-value: 4.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47116962  824 LELMALYVAAAMHDYDHPGRTNAFlvatsapqavlYNDRSVLENHHAAAAWNLfmsrpeynflvnLDHVEFKHFRFLVIE 903
Cdd:cd00077   26 EDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGAEI------------LRELLLEEVIKLIDE 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47116962  904 AILATDLKKHfdfvakfnaKVNDDVGIDWTNENDRLLVCQMCIKLADI--NGPAKCKELHLRWTEGIASEFY 973
Cdd:cd00077   83 LILAVDASHH---------ERLDGLGYPDGLKGEEITLEARIVKLADRldALRRDSREKRRRIAEEDLEELL 145
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
817-964 1.65e-07

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 51.14  E-value: 1.65e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47116962     817 LSGNIPALELMALYVAAAMHDYDHPGRTNAFLVATsapqavlyndrSVLENHHAAAAWnLFMSRPEYNFLVNldhvefkh 896
Cdd:smart00471   19 LAEELGLLDIELLLLAALLHDIGKPGTPDSFLVKT-----------SVLEDHHFIGAE-ILLEEEEPRILEE-------- 78
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47116962     897 frflvieaILATDLKKHFDFvakfnakvnddvgiDWTNENDRLLVCQMCIKLADINGPAKCKELHLRW 964
Cdd:smart00471   79 --------ILRTAILSHHER--------------PDGLRGEPITLEARIVKVADRLDALRADRRYRRV 124
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
751-1012 2.81e-82

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 267.88  E-value: 2.81e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47116962    751 YHNRIHATDVLHAVWYLttqpipglpsvigdhgsasdsdsdsgFTHGHMGYVFSKmyhvpddkygclsgnipaLELMALY 830
Cdd:pfam00233    1 YHNWRHAFDVTQTMYYL--------------------------LKTGKLKEVLTD------------------LEILALL 36
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47116962    831 VAAAMHDYDHPGRTNAFLVATSAPQAVLYNDRSVLENHHAAAAWNLfMSRPEYNFLVNLDHVEFKHFRFLVIEAILATDL 910
Cdd:pfam00233   37 IAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAFQI-LQDEECNIFSNLSDEEYKEVRKLIISLILATDM 115
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47116962    911 KKHFDFVAKFNAKVNDDVGIDW--TNENDRLLVCQMCIKLADINGPAKCKELHLRWTEGIASEFYEQGDEEASLGLPISP 988
Cdd:pfam00233  116 AKHFELLKKFKSLLESKKTLDFleNEEDRRLLLLSMLIKAADISNPTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSP 195
                          250       260
                   ....*....|....*....|....*
gi 47116962    989 FMDR-SAPQLANLQESFISHIVGPL 1012
Cdd:pfam00233  196 LMDReKKTSLPKSQIGFIDFIVLPL 220
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
824-973 4.97e-11

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 61.97  E-value: 4.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47116962  824 LELMALYVAAAMHDYDHPGRTNAFlvatsapqavlYNDRSVLENHHAAAAWNLfmsrpeynflvnLDHVEFKHFRFLVIE 903
Cdd:cd00077   26 EDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGAEI------------LRELLLEEVIKLIDE 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47116962  904 AILATDLKKHfdfvakfnaKVNDDVGIDWTNENDRLLVCQMCIKLADI--NGPAKCKELHLRWTEGIASEFY 973
Cdd:cd00077   83 LILAVDASHH---------ERLDGLGYPDGLKGEEITLEARIVKLADRldALRRDSREKRRRIAEEDLEELL 145
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
817-964 1.65e-07

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 51.14  E-value: 1.65e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47116962     817 LSGNIPALELMALYVAAAMHDYDHPGRTNAFLVATsapqavlyndrSVLENHHAAAAWnLFMSRPEYNFLVNldhvefkh 896
Cdd:smart00471   19 LAEELGLLDIELLLLAALLHDIGKPGTPDSFLVKT-----------SVLEDHHFIGAE-ILLEEEEPRILEE-------- 78
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47116962     897 frflvieaILATDLKKHFDFvakfnakvnddvgiDWTNENDRLLVCQMCIKLADINGPAKCKELHLRW 964
Cdd:smart00471   79 --------ILRTAILSHHER--------------PDGLRGEPITLEARIVKVADRLDALRADRRYRRV 124
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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