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Conserved domains on  [gi|1270516733|pdb|5VYD|A]
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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;
65-300 2.37e-97

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 287.14  E-value: 2.37e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VYD_A         65 FHNWRHAVMVLHTTYLLL-TSVATEFITEVELLAMLIAALSHDLDHNGLTNAFHINSRSELALVYNDQSVLENHHSHLAF 143
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLkTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VYD_A        144 EILLEKGCNVVENLDEDEFKRLRAVIINCILNTDMATHHTKLSKMEE-VNRLGGFINLAENNDQRLFVLAVLLHTADLHN 222
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSlLESKKTLDFLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
5VYD_A        223 PIKPFESNKRWSARLQKEFNNQVELEAKMNLPSLPFMRGNDEESLAKGEIGFINFVVKPWHQQLSQAFPKLDFLLDTI 300
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
65-300 2.37e-97

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 287.14  E-value: 2.37e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VYD_A         65 FHNWRHAVMVLHTTYLLL-TSVATEFITEVELLAMLIAALSHDLDHNGLTNAFHINSRSELALVYNDQSVLENHHSHLAF 143
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLkTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VYD_A        144 EILLEKGCNVVENLDEDEFKRLRAVIINCILNTDMATHHTKLSKMEE-VNRLGGFINLAENNDQRLFVLAVLLHTADLHN 222
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSlLESKKTLDFLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
5VYD_A        223 PIKPFESNKRWSARLQKEFNNQVELEAKMNLPSLPFMRGNDEESLAKGEIGFINFVVKPWHQQLSQAFPKLDFLLDTI 300
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
66-241 2.88e-08

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 51.96  E-value: 2.88e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VYD_A       66 HNWRHAVMVLHTTYLLLTSVAtefITEVELLAMLIAALSHDLDHNGLTNAFhinsrselalvYNDQSVLENHHSHLAFEI 145
Cdd:cd00077   2 HRFEHSLRVAQLARRLAEELG---LSEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGAEI 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VYD_A      146 llekgcnvvenLDEDEFKRLRAVIINCILNTDMATHhtklskmeevNRLGGFINLAENNDQRLFVLAVLLHTADLHNPIK 225
Cdd:cd00077  68 -----------LRELLLEEVIKLIDELILAVDASHH----------ERLDGLGYPDGLKGEEITLEARIVKLADRLDALR 126
                       170
                ....*....|....*...
5VYD_A      226 --PFESNKRWSARLQKEF 241
Cdd:cd00077 127 rdSREKRRRIAEEDLEEL 144
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
63-233 6.26e-06

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: 44.98  E-value: 6.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VYD_A          63 NPFHNWRHAVMVLHTTYLLLtsvatEFITEVELLAMLIAALSHDLDHNGLTNAFHINSrselalvyndqSVLENHHSHLA 142
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAALA-----EELGLLDIELLLLAALLHDIGKPGTPDSFLVKT-----------SVLEDHHFIGA 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VYD_A         143 FEILLEKGCNVVENldedefkrlraviincILNTDMATHHtklskmeevnrlggfINLAENNDQRLFVLAVLLHTADLHN 222
Cdd:smart00471  65 EILLEEEEPRILEE----------------ILRTAILSHH---------------ERPDGLRGEPITLEARIVKVADRLD 113
                          170
                   ....*....|.
5VYD_A         223 PIKPFESNKRW 233
Cdd:smart00471 114 ALRADRRYRRV 124
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
65-300 2.37e-97

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 287.14  E-value: 2.37e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VYD_A         65 FHNWRHAVMVLHTTYLLL-TSVATEFITEVELLAMLIAALSHDLDHNGLTNAFHINSRSELALVYNDQSVLENHHSHLAF 143
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLkTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VYD_A        144 EILLEKGCNVVENLDEDEFKRLRAVIINCILNTDMATHHTKLSKMEE-VNRLGGFINLAENNDQRLFVLAVLLHTADLHN 222
Cdd:pfam00233  81 QILQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSlLESKKTLDFLENEEDRRLLLLSMLIKAADISN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
5VYD_A        223 PIKPFESNKRWSARLQKEFNNQVELEAKMNLPSLPFMRGNDEESLAKGEIGFINFVVKPWHQQLSQAFPKLDFLLDTI 300
Cdd:pfam00233 161 PTRPWEISKKWADLVAEEFFRQGDLEKELGLPVSPLMDREKKTSLPKSQIGFIDFIVLPLFEALAKLFPELQPLLDQL 238
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
66-241 2.88e-08

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 51.96  E-value: 2.88e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VYD_A       66 HNWRHAVMVLHTTYLLLTSVAtefITEVELLAMLIAALSHDLDHNGLTNAFhinsrselalvYNDQSVLENHHSHLAFEI 145
Cdd:cd00077   2 HRFEHSLRVAQLARRLAEELG---LSEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGAEI 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VYD_A      146 llekgcnvvenLDEDEFKRLRAVIINCILNTDMATHhtklskmeevNRLGGFINLAENNDQRLFVLAVLLHTADLHNPIK 225
Cdd:cd00077  68 -----------LRELLLEEVIKLIDELILAVDASHH----------ERLDGLGYPDGLKGEEITLEARIVKLADRLDALR 126
                       170
                ....*....|....*...
5VYD_A      226 --PFESNKRWSARLQKEF 241
Cdd:cd00077 127 rdSREKRRRIAEEDLEEL 144
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
63-233 6.26e-06

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: 44.98  E-value: 6.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VYD_A          63 NPFHNWRHAVMVLHTTYLLLtsvatEFITEVELLAMLIAALSHDLDHNGLTNAFHINSrselalvyndqSVLENHHSHLA 142
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAALA-----EELGLLDIELLLLAALLHDIGKPGTPDSFLVKT-----------SVLEDHHFIGA 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VYD_A         143 FEILLEKGCNVVENldedefkrlraviincILNTDMATHHtklskmeevnrlggfINLAENNDQRLFVLAVLLHTADLHN 222
Cdd:smart00471  65 EILLEEEEPRILEE----------------ILRTAILSHH---------------ERPDGLRGEPITLEARIVKVADRLD 113
                          170
                   ....*....|.
5VYD_A         223 PIKPFESNKRW 233
Cdd:smart00471 114 ALRADRRYRRV 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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