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Conserved domains on  [gi|672085920|ref|XP_008771017|]
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high affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A isoform X1 [Rattus norvegicus]

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;
250-478 7.90e-120

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 352.24  E-value: 7.90e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085920  250 FHNFRHCFCVTQMMYSMVWLCGLQEKFSQMDILVLMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPLENHHCAIAF 329
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085920  330 QILARPECNIFASVPPEGFRQIRQGMITLILATDMARHAEIMDSFKEKME-----NFDYSNEEHLTLLKMILIKCCDISN 404
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLEskktlDFLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672085920  405 EVRPMEVAEPWVDCLLEEYFMQSDREKSEGLPVAPFMDRDK-VTKATAQIGFIKFVLIPMFETVTKLFPIVEETM 478
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKkTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLL 235
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
250-478 7.90e-120

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 352.24  E-value: 7.90e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085920  250 FHNFRHCFCVTQMMYSMVWLCGLQEKFSQMDILVLMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPLENHHCAIAF 329
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085920  330 QILARPECNIFASVPPEGFRQIRQGMITLILATDMARHAEIMDSFKEKME-----NFDYSNEEHLTLLKMILIKCCDISN 404
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLEskktlDFLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672085920  405 EVRPMEVAEPWVDCLLEEYFMQSDREKSEGLPVAPFMDRDK-VTKATAQIGFIKFVLIPMFETVTKLFPIVEETM 478
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKkTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLL 235
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
251-424 5.93e-15

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 71.99  E-value: 5.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085920 251 HNFRHCFCVTQMMYSMvwlcGLQEKFSQMDILVLMTAAICHDLDHPGYNNTYqinartelavrYNDISPLENHHCAIAFQ 330
Cdd:cd00077    2 HRFEHSLRVAQLARRL----AEELGLSEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGAE 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085920 331 ILARPEcnifasvppegFRQIRQGMITLILATDmARHAEIMDSFKEKMENfdysNEEHLTLLKMIlIKCCDISNEVRPM- 409
Cdd:cd00077   67 ILRELL-----------LEEVIKLIDELILAVD-ASHHERLDGLGYPDGL----KGEEITLEARI-VKLADRLDALRRDs 129
                        170
                 ....*....|....*.
gi 672085920 410 -EVAEPWVDCLLEEYF 424
Cdd:cd00077  130 rEKRRRIAEEDLEELL 145
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
248-415 2.38e-09

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: 55.38  E-value: 2.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085920   248 NPFHNFRHCFCVTQMMYSmvwlcgLQEKFSQMDILVLMTAAICHDLDHPGYNNTYQINartelavryndISPLENHHCAI 327
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAA------LAEELGLLDIELLLLAALLHDIGKPGTPDSFLVK-----------TSVLEDHHFIG 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085920   328 AFQILARPECNIFAsvppegfrqirqgmitLILATDMARHaeimdsfkekMENFDYSNEEHLTLLKMIlIKCCDISNEVR 407
Cdd:smart00471  64 AEILLEEEEPRILE----------------EILRTAILSH----------HERPDGLRGEPITLEARI-VKVADRLDALR 116

                   ....*...
gi 672085920   408 PMEVAEPW 415
Cdd:smart00471 117 ADRRYRRV 124
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
250-478 7.90e-120

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 352.24  E-value: 7.90e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085920  250 FHNFRHCFCVTQMMYSMVWLCGLQEKFSQMDILVLMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPLENHHCAIAF 329
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085920  330 QILARPECNIFASVPPEGFRQIRQGMITLILATDMARHAEIMDSFKEKME-----NFDYSNEEHLTLLKMILIKCCDISN 404
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLEskktlDFLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672085920  405 EVRPMEVAEPWVDCLLEEYFMQSDREKSEGLPVAPFMDRDK-VTKATAQIGFIKFVLIPMFETVTKLFPIVEETM 478
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKkTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLL 235
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
251-424 5.93e-15

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 71.99  E-value: 5.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085920 251 HNFRHCFCVTQMMYSMvwlcGLQEKFSQMDILVLMTAAICHDLDHPGYNNTYqinartelavrYNDISPLENHHCAIAFQ 330
Cdd:cd00077    2 HRFEHSLRVAQLARRL----AEELGLSEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGAE 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085920 331 ILARPEcnifasvppegFRQIRQGMITLILATDmARHAEIMDSFKEKMENfdysNEEHLTLLKMIlIKCCDISNEVRPM- 409
Cdd:cd00077   67 ILRELL-----------LEEVIKLIDELILAVD-ASHHERLDGLGYPDGL----KGEEITLEARI-VKLADRLDALRRDs 129
                        170
                 ....*....|....*.
gi 672085920 410 -EVAEPWVDCLLEEYF 424
Cdd:cd00077  130 rEKRRRIAEEDLEELL 145
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
248-415 2.38e-09

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: 55.38  E-value: 2.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085920   248 NPFHNFRHCFCVTQMMYSmvwlcgLQEKFSQMDILVLMTAAICHDLDHPGYNNTYQINartelavryndISPLENHHCAI 327
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAA------LAEELGLLDIELLLLAALLHDIGKPGTPDSFLVK-----------TSVLEDHHFIG 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085920   328 AFQILARPECNIFAsvppegfrqirqgmitLILATDMARHaeimdsfkekMENFDYSNEEHLTLLKMIlIKCCDISNEVR 407
Cdd:smart00471  64 AEILLEEEEPRILE----------------EILRTAILSH----------HERPDGLRGEPITLEARI-VKVADRLDALR 116

                   ....*...
gi 672085920   408 PMEVAEPW 415
Cdd:smart00471 117 ADRRYRRV 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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