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Conserved domains on  [gi|170295853|ref|NP_032828|]
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high affinity 3',5'-cyclic-AMP phosphodiesterase 7A isoform 1 [Mus musculus]

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
185-405 5.17e-97

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 291.38  E-value: 5.17e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295853  185 YHNAVHAADVTQAMHCYLKEPKLASSVTPWDILLSLIAAATHDLDHPGVNQPFLIKTNHYLATLYKNSSVLENHHWRSAV 264
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295853  265 GLLRESG--LFSHLPLESRQEMEAQIGALILATDISRQNEYLSLFRSHLDKGDLHL---DDGRHRHLVLQMALKCADICN 339
Cdd:pfam00233  81 QILQDEEcnIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTLDfleNEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170295853  340 PCRNWELSKQWSEKVTEEFFHQGDIEKKYHLGVSPLCDRQ-TESIANIQIGFMTYLVEPLFTEWARF 405
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREkKTSLPKSQIGFIDFIVLPLFEALAKL 227
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
185-405 5.17e-97

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 291.38  E-value: 5.17e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295853  185 YHNAVHAADVTQAMHCYLKEPKLASSVTPWDILLSLIAAATHDLDHPGVNQPFLIKTNHYLATLYKNSSVLENHHWRSAV 264
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295853  265 GLLRESG--LFSHLPLESRQEMEAQIGALILATDISRQNEYLSLFRSHLDKGDLHL---DDGRHRHLVLQMALKCADICN 339
Cdd:pfam00233  81 QILQDEEcnIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTLDfleNEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170295853  340 PCRNWELSKQWSEKVTEEFFHQGDIEKKYHLGVSPLCDRQ-TESIANIQIGFMTYLVEPLFTEWARF 405
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREkKTSLPKSQIGFIDFIVLPLFEALAKL 227
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
183-350 7.90e-12

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: 62.31  E-value: 7.90e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295853   183 NPYHNAVHAADVTQAMHCYLKEPKLassvtpWDILLSLIAAATHDLDHPGVNQPFLIKTnhylatlyknsSVLENHHWRS 262
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAALAEELGL------LDIELLLLAALLHDIGKPGTPDSFLVKT-----------SVLEDHHFIG 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295853   263 AVGLLRESglfshlplesrqemEAQIGALILATDIsrqneylslfRSHLDKGDlhlDDGRHRHLVLQMALKCADICNPCR 342
Cdd:smart00471  64 AEILLEEE--------------EPRILEEILRTAI----------LSHHERPD---GLRGEPITLEARIVKVADRLDALR 116

                   ....*...
gi 170295853   343 NWELSKQW 350
Cdd:smart00471 117 ADRRYRRV 124
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
185-359 3.60e-11

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 60.82  E-value: 3.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295853 185 YHNAVHAADVTQAMHCYLKEPKLassvTPWDILLSLIAAATHDLDHPGVNQPFliktnhylatlYKNSSVLENHHWRSAV 264
Cdd:cd00077    1 EHRFEHSLRVAQLARRLAEELGL----SEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGA 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295853 265 GLLREsglfshlplESRQEMEAQIGALILATDisrqneylSLFRSHLDKGDLHLDDGRHRHLVLQMALKCADICNPCRN- 343
Cdd:cd00077   66 EILRE---------LLLEEVIKLIDELILAVD--------ASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRRd 128
                        170
                 ....*....|....*..
gi 170295853 344 -WELSKQWSEKVTEEFF 359
Cdd:cd00077  129 sREKRRRIAEEDLEELL 145
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
185-405 5.17e-97

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 291.38  E-value: 5.17e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295853  185 YHNAVHAADVTQAMHCYLKEPKLASSVTPWDILLSLIAAATHDLDHPGVNQPFLIKTNHYLATLYKNSSVLENHHWRSAV 264
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295853  265 GLLRESG--LFSHLPLESRQEMEAQIGALILATDISRQNEYLSLFRSHLDKGDLHL---DDGRHRHLVLQMALKCADICN 339
Cdd:pfam00233  81 QILQDEEcnIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTLDfleNEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170295853  340 PCRNWELSKQWSEKVTEEFFHQGDIEKKYHLGVSPLCDRQ-TESIANIQIGFMTYLVEPLFTEWARF 405
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREkKTSLPKSQIGFIDFIVLPLFEALAKL 227
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
183-350 7.90e-12

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: 62.31  E-value: 7.90e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295853   183 NPYHNAVHAADVTQAMHCYLKEPKLassvtpWDILLSLIAAATHDLDHPGVNQPFLIKTnhylatlyknsSVLENHHWRS 262
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAALAEELGL------LDIELLLLAALLHDIGKPGTPDSFLVKT-----------SVLEDHHFIG 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295853   263 AVGLLRESglfshlplesrqemEAQIGALILATDIsrqneylslfRSHLDKGDlhlDDGRHRHLVLQMALKCADICNPCR 342
Cdd:smart00471  64 AEILLEEE--------------EPRILEEILRTAI----------LSHHERPD---GLRGEPITLEARIVKVADRLDALR 116

                   ....*...
gi 170295853   343 NWELSKQW 350
Cdd:smart00471 117 ADRRYRRV 124
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
185-359 3.60e-11

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 60.82  E-value: 3.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295853 185 YHNAVHAADVTQAMHCYLKEPKLassvTPWDILLSLIAAATHDLDHPGVNQPFliktnhylatlYKNSSVLENHHWRSAV 264
Cdd:cd00077    1 EHRFEHSLRVAQLARRLAEELGL----SEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGA 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295853 265 GLLREsglfshlplESRQEMEAQIGALILATDisrqneylSLFRSHLDKGDLHLDDGRHRHLVLQMALKCADICNPCRN- 343
Cdd:cd00077   66 EILRE---------LLLEEVIKLIDELILAVD--------ASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRRd 128
                        170
                 ....*....|....*..
gi 170295853 344 -WELSKQWSEKVTEEFF 359
Cdd:cd00077  129 sREKRRRIAEEDLEELL 145
 
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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