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Conserved domains on  [gi|159474548|ref|XP_001695387|]
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3',5'-cyclic-nucleotide phosphodiesterase, partial [Chlamydomonas reinhardtii]

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
69-287 3.05e-94

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 306695  Cd Length: 232  Bit Score: 281.74  E-value: 3.05e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159474548   69 YHSATHAADVLQTLHVIIHGAQLHvHYLDALGLFAAYFAAIVHDYGHPGLTNDFLIATSDPLAVRYNDKSPLENHHAAAA 148
Cdd:pfam00233   1 YHNWRHAADVAQTMYYLLKKGGLK-EVLTDLEILALLIAALCHDVDHPGTNNAFLINTKSPLAILYNDKSVLENHHCATA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159474548  149 FSVLRRSEVDVLSTLTLQERNTFRKQVIEMVLATDMKQHFTTLSHFQTMHRLASFQQVQQAAG----LPVAMKAADLGHL 224
Cdd:pfam00233  80 FKILSKEECNILSNLSADEYQEFRKLIIDLILATDMSKHFELLKKFKELVKISEKNLLNTEEDrlllLQLLIKAADISNP 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 159474548  225 GEELEVHKRWLAGLEEEFFNQGDREKELGIPISPLFDRAKQGVSKSQVGFYDFVALPLVHALT 287
Cdd:pfam00233 160 TRPWEISKKWAERVMEEFFRQGDLEKELGLPVSPLMDREKTDVPKSQIGFIDFIVLPLFEALA 222
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
69-287 3.05e-94

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 306695  Cd Length: 232  Bit Score: 281.74  E-value: 3.05e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159474548   69 YHSATHAADVLQTLHVIIHGAQLHvHYLDALGLFAAYFAAIVHDYGHPGLTNDFLIATSDPLAVRYNDKSPLENHHAAAA 148
Cdd:pfam00233   1 YHNWRHAADVAQTMYYLLKKGGLK-EVLTDLEILALLIAALCHDVDHPGTNNAFLINTKSPLAILYNDKSVLENHHCATA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159474548  149 FSVLRRSEVDVLSTLTLQERNTFRKQVIEMVLATDMKQHFTTLSHFQTMHRLASFQQVQQAAG----LPVAMKAADLGHL 224
Cdd:pfam00233  80 FKILSKEECNILSNLSADEYQEFRKLIIDLILATDMSKHFELLKKFKELVKISEKNLLNTEEDrlllLQLLIKAADISNP 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 159474548  225 GEELEVHKRWLAGLEEEFFNQGDREKELGIPISPLFDRAKQGVSKSQVGFYDFVALPLVHALT 287
Cdd:pfam00233 160 TRPWEISKKWAERVMEEFFRQGDLEKELGLPVSPLMDREKTDVPKSQIGFIDFIVLPLFEALA 222
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
69-187 1.50e-05

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032  Cd Length: 145  Bit Score: 43.87  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159474548  69 YHSATHAADVLQTLHVIihGAQLHVHYLDALglfAAYFAAIVHDYGHPGLTNDFliatsdplavrYNDKSPLENHHAAAA 148
Cdd:cd00077    1 EHRFEHSLRVAQLARRL--AEELGLSEEDIE---LLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVG 64
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 159474548 149 FSVLRRSevdvlstltlqERNTFRKQVIEMVLATDMKQH 187
Cdd:cd00077   65 AEILREL-----------LLEEVIKLIDELILAVDASHH 92
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
67-160 7.92e-05

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  Cd Length: 124  Bit Score: 41.51  E-value: 7.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159474548    67 NPYHSATHAADVLQTLHVIihgaqlhVHYLDALGLFAAYFAAIVHDYGHPGLTNDFLIATsdplavryndkSPLENHHAA 146
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAAL-------AEELGLLDIELLLLAALLHDIGKPGTPDSFLVKT-----------SVLEDHHFI 62
                           90
                   ....*....|....
gi 159474548   147 AAFSVLRRSEVDVL 160
Cdd:smart00471  63 GAEILLEEEEPRIL 76
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
69-287 3.05e-94

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 306695  Cd Length: 232  Bit Score: 281.74  E-value: 3.05e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159474548   69 YHSATHAADVLQTLHVIIHGAQLHvHYLDALGLFAAYFAAIVHDYGHPGLTNDFLIATSDPLAVRYNDKSPLENHHAAAA 148
Cdd:pfam00233   1 YHNWRHAADVAQTMYYLLKKGGLK-EVLTDLEILALLIAALCHDVDHPGTNNAFLINTKSPLAILYNDKSVLENHHCATA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159474548  149 FSVLRRSEVDVLSTLTLQERNTFRKQVIEMVLATDMKQHFTTLSHFQTMHRLASFQQVQQAAG----LPVAMKAADLGHL 224
Cdd:pfam00233  80 FKILSKEECNILSNLSADEYQEFRKLIIDLILATDMSKHFELLKKFKELVKISEKNLLNTEEDrlllLQLLIKAADISNP 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 159474548  225 GEELEVHKRWLAGLEEEFFNQGDREKELGIPISPLFDRAKQGVSKSQVGFYDFVALPLVHALT 287
Cdd:pfam00233 160 TRPWEISKKWAERVMEEFFRQGDLEKELGLPVSPLMDREKTDVPKSQIGFIDFIVLPLFEALA 222
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
69-187 1.50e-05

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032  Cd Length: 145  Bit Score: 43.87  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159474548  69 YHSATHAADVLQTLHVIihGAQLHVHYLDALglfAAYFAAIVHDYGHPGLTNDFliatsdplavrYNDKSPLENHHAAAA 148
Cdd:cd00077    1 EHRFEHSLRVAQLARRL--AEELGLSEEDIE---LLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVG 64
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 159474548 149 FSVLRRSevdvlstltlqERNTFRKQVIEMVLATDMKQH 187
Cdd:cd00077   65 AEILREL-----------LLEEVIKLIDELILAVDASHH 92
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
67-160 7.92e-05

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  Cd Length: 124  Bit Score: 41.51  E-value: 7.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159474548    67 NPYHSATHAADVLQTLHVIihgaqlhVHYLDALGLFAAYFAAIVHDYGHPGLTNDFLIATsdplavryndkSPLENHHAA 146
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAAL-------AEELGLLDIELLLLAALLHDIGKPGTPDSFLVKT-----------SVLEDHHFI 62
                           90
                   ....*....|....
gi 159474548   147 AAFSVLRRSEVDVL 160
Cdd:smart00471  63 GAEILLEEEEPRIL 76
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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