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Conserved domains on  [gi|4505675|ref|NP_002597|]
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high affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A isoform a [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;
311-539 4.10e-121

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 425542  Cd Length: 235  Bit Score: 357.61  E-value: 4.10e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505675    311 FHNFRHCFCVAQMMYSMVWLCSLQEKFSQTDILILMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPLENHHCAVAF 390
Cdd:pfam00233   1 YHNFRHAADVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLINTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505675    391 QILAEPECNIFSNIPPDGFKQIRQGMITLILATDMARHAEIMDSFKEKMEN--FDYSNEEHMTLLKMILIKCCDISNEVR 468
Cdd:pfam00233  81 QILSSEECNIFSNLSKEEYKEVRKLIISLILATDMAKHFELLKKFKSLLDKtlDLENEEDRRLLLLQMLIKAADISNPTR 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4505675    469 PMEVAEPWVDCLLEEYFMQSDREKSEGLPVAPFMDRDK-VTKATAQIGFIKFVLIPMFETVTKLFPMVEEIM 539
Cdd:pfam00233 161 PWEISKKWAERVAEEFFRQGDLEKELGLPVSPLMDREKkTSLPKSQIGFIDFIVLPLFEALARLLPELQPLL 232
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
311-539 4.10e-121

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 425542  Cd Length: 235  Bit Score: 357.61  E-value: 4.10e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505675    311 FHNFRHCFCVAQMMYSMVWLCSLQEKFSQTDILILMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPLENHHCAVAF 390
Cdd:pfam00233   1 YHNFRHAADVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLINTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505675    391 QILAEPECNIFSNIPPDGFKQIRQGMITLILATDMARHAEIMDSFKEKMEN--FDYSNEEHMTLLKMILIKCCDISNEVR 468
Cdd:pfam00233  81 QILSSEECNIFSNLSKEEYKEVRKLIISLILATDMAKHFELLKKFKSLLDKtlDLENEEDRRLLLLQMLIKAADISNPTR 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4505675    469 PMEVAEPWVDCLLEEYFMQSDREKSEGLPVAPFMDRDK-VTKATAQIGFIKFVLIPMFETVTKLFPMVEEIM 539
Cdd:pfam00233 161 PWEISKKWAERVAEEFFRQGDLEKELGLPVSPLMDREKkTSLPKSQIGFIDFIVLPLFEALARLLPELQPLL 232
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
312-485 7.39e-16

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 74.68  E-value: 7.39e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505675  312 HNFRHCFCVAQMMYSMvwlcSLQEKFSQTDILILMTAAICHDLDHPGYNNTYqinartelavrYNDISPLENHHCAVAFQ 391
Cdd:cd00077   2 HRFEHSLRVAQLARRL----AEELGLSEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGAE 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505675  392 ILAEPEcnifsnippdgFKQIRQGMITLILATDmARHAEIMDSFKEKMENfdysNEEHMTLLKMIlIKCCDISNEVRPM- 470
Cdd:cd00077  67 ILRELL-----------LEEVIKLIDELILAVD-ASHHERLDGLGYPDGL----KGEEITLEARI-VKLADRLDALRRDs 129
                       170
                ....*....|....*.
gi 4505675  471 -EVAEPWVDCLLEEYF 485
Cdd:cd00077 130 rEKRRRIAEEDLEELL 145
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
309-476 5.60e-11

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: 60.00  E-value: 5.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505675     309 NPFHNFRHCFCVAQMMYSmvwlcsLQEKFSQTDILILMTAAICHDLDHPGYNNTYQINartelavryndISPLENHHCAV 388
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAA------LAEELGLLDIELLLLAALLHDIGKPGTPDSFLVK-----------TSVLEDHHFIG 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505675     389 AFQILAEPECNIFSNippdgfkqirqgmitlILATDMARHaeimdsfkekMENFDYSNEEHMTLLKMIlIKCCDISNEVR 468
Cdd:smart00471  64 AEILLEEEEPRILEE----------------ILRTAILSH----------HERPDGLRGEPITLEARI-VKVADRLDALR 116

                   ....*...
gi 4505675     469 PMEVAEPW 476
Cdd:smart00471 117 ADRRYRRV 124
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
311-539 4.10e-121

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 425542  Cd Length: 235  Bit Score: 357.61  E-value: 4.10e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505675    311 FHNFRHCFCVAQMMYSMVWLCSLQEKFSQTDILILMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPLENHHCAVAF 390
Cdd:pfam00233   1 YHNFRHAADVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLINTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505675    391 QILAEPECNIFSNIPPDGFKQIRQGMITLILATDMARHAEIMDSFKEKMEN--FDYSNEEHMTLLKMILIKCCDISNEVR 468
Cdd:pfam00233  81 QILSSEECNIFSNLSKEEYKEVRKLIISLILATDMAKHFELLKKFKSLLDKtlDLENEEDRRLLLLQMLIKAADISNPTR 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4505675    469 PMEVAEPWVDCLLEEYFMQSDREKSEGLPVAPFMDRDK-VTKATAQIGFIKFVLIPMFETVTKLFPMVEEIM 539
Cdd:pfam00233 161 PWEISKKWAERVAEEFFRQGDLEKELGLPVSPLMDREKkTSLPKSQIGFIDFIVLPLFEALARLLPELQPLL 232
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
312-485 7.39e-16

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 74.68  E-value: 7.39e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505675  312 HNFRHCFCVAQMMYSMvwlcSLQEKFSQTDILILMTAAICHDLDHPGYNNTYqinartelavrYNDISPLENHHCAVAFQ 391
Cdd:cd00077   2 HRFEHSLRVAQLARRL----AEELGLSEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGAE 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505675  392 ILAEPEcnifsnippdgFKQIRQGMITLILATDmARHAEIMDSFKEKMENfdysNEEHMTLLKMIlIKCCDISNEVRPM- 470
Cdd:cd00077  67 ILRELL-----------LEEVIKLIDELILAVD-ASHHERLDGLGYPDGL----KGEEITLEARI-VKLADRLDALRRDs 129
                       170
                ....*....|....*.
gi 4505675  471 -EVAEPWVDCLLEEYF 485
Cdd:cd00077 130 rEKRRRIAEEDLEELL 145
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
309-476 5.60e-11

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: 60.00  E-value: 5.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505675     309 NPFHNFRHCFCVAQMMYSmvwlcsLQEKFSQTDILILMTAAICHDLDHPGYNNTYQINartelavryndISPLENHHCAV 388
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAA------LAEELGLLDIELLLLAALLHDIGKPGTPDSFLVK-----------TSVLEDHHFIG 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505675     389 AFQILAEPECNIFSNippdgfkqirqgmitlILATDMARHaeimdsfkekMENFDYSNEEHMTLLKMIlIKCCDISNEVR 468
Cdd:smart00471  64 AEILLEEEEPRILEE----------------ILRTAILSH----------HERPDGLRGEPITLEARI-VKVADRLDALR 116

                   ....*...
gi 4505675     469 PMEVAEPW 476
Cdd:smart00471 117 ADRRYRRV 124
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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