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Conserved domains on  [gi|2306764|gb|AAB65772|]
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cAMP phosphodiesterase PDE7 [Homo sapiens]

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;
185-405 1.14e-96

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 290.61  E-value: 1.14e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306764    185 YHNAVHAADVTQAMHCYLKEPKLANSVTPWDILLSLIAAATHDLDHPGVNQPFLIKTNHYLATLYKNTSVLENHHWRSAV 264
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306764    265 GLLRESG--LFSHLPLESRQQMETQIGALILATDISRQNEYLSLFRSHLDRGDL---CLEDTRHRHLVLQMALKCADICN 339
Cdd:pfam00233  81 QILQDEEcnIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTldfLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2306764    340 PCRTWELSKQWSEKVTEEFFHQGDIEKKYHLGVSPLCDRH-TESIANIQIGFMTYLVEPLFTEWARF 405
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREkKTSLPKSQIGFIDFIVLPLFEALAKL 227
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
185-405 1.14e-96

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 290.61  E-value: 1.14e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306764    185 YHNAVHAADVTQAMHCYLKEPKLANSVTPWDILLSLIAAATHDLDHPGVNQPFLIKTNHYLATLYKNTSVLENHHWRSAV 264
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306764    265 GLLRESG--LFSHLPLESRQQMETQIGALILATDISRQNEYLSLFRSHLDRGDL---CLEDTRHRHLVLQMALKCADICN 339
Cdd:pfam00233  81 QILQDEEcnIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTldfLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2306764    340 PCRTWELSKQWSEKVTEEFFHQGDIEKKYHLGVSPLCDRH-TESIANIQIGFMTYLVEPLFTEWARF 405
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREkKTSLPKSQIGFIDFIVLPLFEALAKL 227
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
183-350 3.60e-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: 63.08  E-value: 3.60e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306764     183 NPYHNAVHAADVTQAMHcylkepKLANSVTPWDILLSLIAAATHDLDHPGVNQPFLIKtnhylatlyknTSVLENHHWRS 262
Cdd:smart00471   1 SDYHVFEHSLRVAQLAA------ALAEELGLLDIELLLLAALLHDIGKPGTPDSFLVK-----------TSVLEDHHFIG 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306764     263 AVGLLRESglfshlplesrqqmETQIGALILATDIsrqneylslfRSHLDRGDLcleDTRHRHLVLQMALKCADICNPCR 342
Cdd:smart00471  64 AEILLEEE--------------EPRILEEILRTAI----------LSHHERPDG---LRGEPITLEARIVKVADRLDALR 116

                   ....*...
gi 2306764     343 TWELSKQW 350
Cdd:smart00471 117 ADRRYRRV 124
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
185-359 1.19e-10

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 59.66  E-value: 1.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306764  185 YHNAVHAADVTQAMHCYLKEPKLansvTPWDILLSLIAAATHDLDHPGVNQPFliktnhylatlYKNTSVLENHHWRSAV 264
Cdd:cd00077   1 EHRFEHSLRVAQLARRLAEELGL----SEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGA 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306764  265 GLLREsglfshlplESRQQMETQIGALILATDisrqneylSLFRSHLDRGDLCLEDTRHRHLVLQMALKCADICNPCRT- 343
Cdd:cd00077  66 EILRE---------LLLEEVIKLIDELILAVD--------ASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRRd 128
                       170
                ....*....|....*..
gi 2306764  344 -WELSKQWSEKVTEEFF 359
Cdd:cd00077 129 sREKRRRIAEEDLEELL 145
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
185-405 1.14e-96

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 290.61  E-value: 1.14e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306764    185 YHNAVHAADVTQAMHCYLKEPKLANSVTPWDILLSLIAAATHDLDHPGVNQPFLIKTNHYLATLYKNTSVLENHHWRSAV 264
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306764    265 GLLRESG--LFSHLPLESRQQMETQIGALILATDISRQNEYLSLFRSHLDRGDL---CLEDTRHRHLVLQMALKCADICN 339
Cdd:pfam00233  81 QILQDEEcnIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTldfLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2306764    340 PCRTWELSKQWSEKVTEEFFHQGDIEKKYHLGVSPLCDRH-TESIANIQIGFMTYLVEPLFTEWARF 405
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREkKTSLPKSQIGFIDFIVLPLFEALAKL 227
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
183-350 3.60e-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: 63.08  E-value: 3.60e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306764     183 NPYHNAVHAADVTQAMHcylkepKLANSVTPWDILLSLIAAATHDLDHPGVNQPFLIKtnhylatlyknTSVLENHHWRS 262
Cdd:smart00471   1 SDYHVFEHSLRVAQLAA------ALAEELGLLDIELLLLAALLHDIGKPGTPDSFLVK-----------TSVLEDHHFIG 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306764     263 AVGLLRESglfshlplesrqqmETQIGALILATDIsrqneylslfRSHLDRGDLcleDTRHRHLVLQMALKCADICNPCR 342
Cdd:smart00471  64 AEILLEEE--------------EPRILEEILRTAI----------LSHHERPDG---LRGEPITLEARIVKVADRLDALR 116

                   ....*...
gi 2306764     343 TWELSKQW 350
Cdd:smart00471 117 ADRRYRRV 124
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
185-359 1.19e-10

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 59.66  E-value: 1.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306764  185 YHNAVHAADVTQAMHCYLKEPKLansvTPWDILLSLIAAATHDLDHPGVNQPFliktnhylatlYKNTSVLENHHWRSAV 264
Cdd:cd00077   1 EHRFEHSLRVAQLARRLAEELGL----SEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGA 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306764  265 GLLREsglfshlplESRQQMETQIGALILATDisrqneylSLFRSHLDRGDLCLEDTRHRHLVLQMALKCADICNPCRT- 343
Cdd:cd00077  66 EILRE---------LLLEEVIKLIDELILAVD--------ASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRRd 128
                       170
                ....*....|....*..
gi 2306764  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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