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Conserved domains on  [gi|19920498|ref|NP_608575|]
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vacuolar protein sorting 29 [Drosophila melanogaster]

Protein Classification

vacuolar protein sorting-associated protein 29( domain architecture ID 10164674)

vacuolar protein sorting-associated protein 29 acts as component of the retromer cargo-selective complex (CSC), which is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_Vps29 cd07394
Homo sapiens Vps29 and related proteins, metallophosphatase domain; Vps29 (vacuolar sorting ...
 2-179 1.12e-125

Homo sapiens Vps29 and related proteins, metallophosphatase domain; Vps29 (vacuolar sorting protein 29), also known as vacuolar membrane protein Pep11, is a subunit of the retromer complex which is responsible for the retrieval of mannose-6-phosphate receptors (MPRs) from the endosomes for retrograde transport back to the Golgi. Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer complex assembly as well as a phosphatase with specificity for the cytoplasmic tail of the MPR. The retromer includes the following 5 subunits: Vps35, Vps26, Vps29, and a dimer of the sorting nexins Vps5 (Snx1), and Vps17 (Snx2). Vps29 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


:

Pssm-ID: 163637 [Multi-domain]  Cd Length: 178  Bit Score: 350.74  E-value: 1.12e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920498   2 LVLVLGDLHIPHRCSSLPAKFKKLLVPGRIHHILATGNICTKESYDYLKSLANDVHIVRGDFDENLTYPEQKVVTVGQFR 81
Cdd:cd07394   1 LVLVIGDLHIPHRAADLPAKFKKLLVPGKIQHVLCTGNLCSKETYDYLKTIAPDVHIVRGDFDENLNYPETKVITVGQFK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920498  82 IGLCHGHQVVPRGDPEALALIQRQLDVDILITGHTYKFEAYEHGNKFYINPGSATGAFNPLDTNVVPSFVLMDIQSTTVV 161
Cdd:cd07394  81 IGLIHGHQVVPWGDPDSLAALQRQLDVDILISGHTHKFEAFEHEGKFFINPGSATGAFSPLDPNVIPSFVLMDIQGSTVV 160

                       170
                ....*....|....*...
gi 19920498 162 TYVYQLIGDEVKVERIEY 179
Cdd:cd07394 161 TYVYQLIDGEVKVEKIEY 178
 
Name Accession Description Interval E-value
MPP_Vps29 cd07394
Homo sapiens Vps29 and related proteins, metallophosphatase domain; Vps29 (vacuolar sorting ...
 2-179 1.12e-125

Homo sapiens Vps29 and related proteins, metallophosphatase domain; Vps29 (vacuolar sorting protein 29), also known as vacuolar membrane protein Pep11, is a subunit of the retromer complex which is responsible for the retrieval of mannose-6-phosphate receptors (MPRs) from the endosomes for retrograde transport back to the Golgi. Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer complex assembly as well as a phosphatase with specificity for the cytoplasmic tail of the MPR. The retromer includes the following 5 subunits: Vps35, Vps26, Vps29, and a dimer of the sorting nexins Vps5 (Snx1), and Vps17 (Snx2). Vps29 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 163637 [Multi-domain]  Cd Length: 178  Bit Score: 350.74  E-value: 1.12e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920498   2 LVLVLGDLHIPHRCSSLPAKFKKLLVPGRIHHILATGNICTKESYDYLKSLANDVHIVRGDFDENLTYPEQKVVTVGQFR 81
Cdd:cd07394   1 LVLVIGDLHIPHRAADLPAKFKKLLVPGKIQHVLCTGNLCSKETYDYLKTIAPDVHIVRGDFDENLNYPETKVITVGQFK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920498  82 IGLCHGHQVVPRGDPEALALIQRQLDVDILITGHTYKFEAYEHGNKFYINPGSATGAFNPLDTNVVPSFVLMDIQSTTVV 161
Cdd:cd07394  81 IGLIHGHQVVPWGDPDSLAALQRQLDVDILISGHTHKFEAFEHEGKFFINPGSATGAFSPLDPNVIPSFVLMDIQGSTVV 160

                       170
                ....*....|....*...
gi 19920498 162 TYVYQLIGDEVKVERIEY 179
Cdd:cd07394 161 TYVYQLIDGEVKVEKIEY 178
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
 1-155 1.52e-31

phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif approximating DXH(X25)GDXXD(X25)GNHD as found in several phosphoesterases, including the nucleases SbcD and Mre11, and a family of uncharacterized archaeal putative phosphoesterases described by TIGR00024. In this family, the His residue in GNHD portion of the motif is not conserved. The member MJ0936, one of two from Methanococcus jannaschii, was shown () to act on model phosphodiesterase substrates; a divalent cation was required. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272869 [Multi-domain]  Cd Length: 158  Bit Score: 111.31  E-value: 1.52e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920498     1 MLVLVLGDLHIPHRCSSLPAKFKKLLV-PGRIHHilaTGNICTKESYDYLKSLANDVHIVRGDFD-ENLTYPEQKVVTVG 78
Cdd:TIGR00040   1 MKILVISDTHGPLRATELPVELFNLESnVDLVIH---AGDLTSPFVLKEFEDLAAKVIAVRGNNDgERDELPEEEIFEAE 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19920498    79 QFRIGLCHGHQVVPRGDPEALALIQRQLDVDILITGHTYKFEAYEHGNKFYINPGSATGAFNPldtnVVPSFVLMDI 155
Cdd:TIGR00040  78 GIDFGLVHGDLVYPRGDLLVLEYLAKELGVDVLIFGHTHIPVAEELRGILLINPGSLTGPRNG----NTPSYAILDV 150
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 1-157 1.36e-22

Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the Calcineurin-like phosphoesterase superfamily.


Pssm-ID: 432832 [Multi-domain]  Cd Length: 150  Bit Score: 88.14  E-value: 1.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920498     1 MLVLVLGDLHiphRCSSLPAKFKKLLVpGRIHHILATGNICTKESYDYLKSLAnDVHIVRGDFDENL----TYPEQKVVT 76
Cdd:pfam12850   1 MRIGIISDTH---DNLALPEAALERLK-GVVDLIIHAGDIVAPEVLEELLELA-PVLAVRGNNDAAAefatDLPEEAVLE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920498    77 VGQFRIGLCHGHqvvprGDPEALA--LIQRQLDVDILITGHTYKFEAYEHGNKFYINPGSATGAFNPLdtnvVPSFVLMD 154
Cdd:pfam12850  76 LGGVKILLTHGH-----GVKDALArlLRRAEEGVAVVVYGHTHVPGVERIGGVLFVNPGSVGGPRFGD----PPTYALLD 146


                  ...
gi 19920498   155 IQS 157
Cdd:pfam12850 147 IDD 149
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
3-179 2.28e-18

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 78.03  E-value: 2.28e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920498   3 VLVLGDLHiphrcSSLPA--KFKKLLVPGRIHHILATGNIC-----TKESYDYLKSLanDVHIVRG-----DFDENLTYP 70
Cdd:COG0622   2 IAVISDTH-----GNLPAleAVLEDLEREGVDLIVHLGDLVgygpdPPEVLDLLREL--PIVAVRGnhdgaVLRGLRSLP 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920498  71 EQKVVTVGQFRIGLCHGHQ---VVPRGDPEALALIQRQLDVDILITGHTYKFEAYEHGNKFYINPGSATGafnPLDtNVV 147
Cdd:COG0622  75 ETLRLELEGVRILLVHGSPneyLLPDTPAERLRALAAEGDADVVVCGHTHIPFVRRVGGVLLVNPGSVGQ---PRD-GDP 150

                       170       180       190
                ....*....|....*....|....*....|..
gi 19920498 148 PSFVLMDIQSTTVvtyvyqligdEVKVERIEY 179
Cdd:COG0622 151 ASYAILDIDDGEW----------SVEFVRVPY 172
PRK09453 PRK09453
phosphodiesterase; Provisional
 1-136 2.82e-09

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 53.71  E-value: 2.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920498    1 MLVLVLGDLHiphrcSSLPA--KFKKLLVPGRIHHILATGNICTK-------ESYD------YLKSLANDVHIVRGDFDE 65
Cdd:PRK09453   1 MKLMFASDTH-----GSLPAteKALELFAQSGADWLVHLGDVLYHgprnplpEGYApkkvaeLLNAYADKIIAVRGNCDS 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19920498   66 N-----LTYPEQK---VVTVGQFRIGLCHGHQVvprgDPEALALIQrqlDVDILITGHTYKFEAYEHGNKFYINPGSAT 136
Cdd:PRK09453  76 EvdqmlLHFPIMApyqQVLLEGKRLFLTHGHLY----GPENLPALH---DGDVLVYGHTHIPVAEKQGGIILFNPGSVS 147
 
Name Accession Description Interval E-value
MPP_Vps29 cd07394
Homo sapiens Vps29 and related proteins, metallophosphatase domain; Vps29 (vacuolar sorting ...
 2-179 1.12e-125

Homo sapiens Vps29 and related proteins, metallophosphatase domain; Vps29 (vacuolar sorting protein 29), also known as vacuolar membrane protein Pep11, is a subunit of the retromer complex which is responsible for the retrieval of mannose-6-phosphate receptors (MPRs) from the endosomes for retrograde transport back to the Golgi. Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer complex assembly as well as a phosphatase with specificity for the cytoplasmic tail of the MPR. The retromer includes the following 5 subunits: Vps35, Vps26, Vps29, and a dimer of the sorting nexins Vps5 (Snx1), and Vps17 (Snx2). Vps29 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 163637 [Multi-domain]  Cd Length: 178  Bit Score: 350.74  E-value: 1.12e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920498   2 LVLVLGDLHIPHRCSSLPAKFKKLLVPGRIHHILATGNICTKESYDYLKSLANDVHIVRGDFDENLTYPEQKVVTVGQFR 81
Cdd:cd07394   1 LVLVIGDLHIPHRAADLPAKFKKLLVPGKIQHVLCTGNLCSKETYDYLKTIAPDVHIVRGDFDENLNYPETKVITVGQFK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920498  82 IGLCHGHQVVPRGDPEALALIQRQLDVDILITGHTYKFEAYEHGNKFYINPGSATGAFNPLDTNVVPSFVLMDIQSTTVV 161
Cdd:cd07394  81 IGLIHGHQVVPWGDPDSLAALQRQLDVDILISGHTHKFEAFEHEGKFFINPGSATGAFSPLDPNVIPSFVLMDIQGSTVV 160

                       170
                ....*....|....*...
gi 19920498 162 TYVYQLIGDEVKVERIEY 179
Cdd:cd07394 161 TYVYQLIDGEVKVEKIEY 178
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
 1-155 1.52e-31

phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif approximating DXH(X25)GDXXD(X25)GNHD as found in several phosphoesterases, including the nucleases SbcD and Mre11, and a family of uncharacterized archaeal putative phosphoesterases described by TIGR00024. In this family, the His residue in GNHD portion of the motif is not conserved. The member MJ0936, one of two from Methanococcus jannaschii, was shown () to act on model phosphodiesterase substrates; a divalent cation was required. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272869 [Multi-domain]  Cd Length: 158  Bit Score: 111.31  E-value: 1.52e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920498     1 MLVLVLGDLHIPHRCSSLPAKFKKLLV-PGRIHHilaTGNICTKESYDYLKSLANDVHIVRGDFD-ENLTYPEQKVVTVG 78
Cdd:TIGR00040   1 MKILVISDTHGPLRATELPVELFNLESnVDLVIH---AGDLTSPFVLKEFEDLAAKVIAVRGNNDgERDELPEEEIFEAE 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19920498    79 QFRIGLCHGHQVVPRGDPEALALIQRQLDVDILITGHTYKFEAYEHGNKFYINPGSATGAFNPldtnVVPSFVLMDI 155
Cdd:TIGR00040  78 GIDFGLVHGDLVYPRGDLLVLEYLAKELGVDVLIFGHTHIPVAEELRGILLINPGSLTGPRNG----NTPSYAILDV 150
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 1-157 1.36e-22

Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the Calcineurin-like phosphoesterase superfamily.


Pssm-ID: 432832 [Multi-domain]  Cd Length: 150  Bit Score: 88.14  E-value: 1.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920498     1 MLVLVLGDLHiphRCSSLPAKFKKLLVpGRIHHILATGNICTKESYDYLKSLAnDVHIVRGDFDENL----TYPEQKVVT 76
Cdd:pfam12850   1 MRIGIISDTH---DNLALPEAALERLK-GVVDLIIHAGDIVAPEVLEELLELA-PVLAVRGNNDAAAefatDLPEEAVLE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920498    77 VGQFRIGLCHGHqvvprGDPEALA--LIQRQLDVDILITGHTYKFEAYEHGNKFYINPGSATGAFNPLdtnvVPSFVLMD 154
Cdd:pfam12850  76 LGGVKILLTHGH-----GVKDALArlLRRAEEGVAVVVYGHTHVPGVERIGGVLFVNPGSVGGPRFGD----PPTYALLD 146


                  ...
gi 19920498   155 IQS 157
Cdd:pfam12850 147 IDD 149
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
3-179 2.28e-18

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 78.03  E-value: 2.28e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920498   3 VLVLGDLHiphrcSSLPA--KFKKLLVPGRIHHILATGNIC-----TKESYDYLKSLanDVHIVRG-----DFDENLTYP 70
Cdd:COG0622   2 IAVISDTH-----GNLPAleAVLEDLEREGVDLIVHLGDLVgygpdPPEVLDLLREL--PIVAVRGnhdgaVLRGLRSLP 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920498  71 EQKVVTVGQFRIGLCHGHQ---VVPRGDPEALALIQRQLDVDILITGHTYKFEAYEHGNKFYINPGSATGafnPLDtNVV 147
Cdd:COG0622  75 ETLRLELEGVRILLVHGSPneyLLPDTPAERLRALAAEGDADVVVCGHTHIPFVRRVGGVLLVNPGSVGQ---PRD-GDP 150

                       170       180       190
                ....*....|....*....|....*....|..
gi 19920498 148 PSFVLMDIQSTTVvtyvyqligdEVKVERIEY 179
Cdd:COG0622 151 ASYAILDIDDGEW----------SVEFVRVPY 172
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 2-137 6.59e-17

Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a manganase-dependent metallophosphatase, found in bacteria and archaea, that cleaves bis-p-nitrophenyl phosphate, thymidine 5'-monophosphate-p-nitrophenyl ester, and p-nitrophenyl phosphorylcholine, but is unable to hydrolyze 2',3 ' or 3',5' cyclic nucleic phosphodiesters, and various phosphomonoesters, including p-nitrophenyl phosphate. This family also includes the Bacilus subtilis YsnB and Methanococcus jannaschii MJ0936 proteins. This domain family belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277320 [Multi-domain]  Cd Length: 156  Bit Score: 73.46  E-value: 6.59e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920498   2 LVLVLGDLHIPhrcSSLPAKFKKLLVpGRIHHILATGNICTKESYDYLKSLANDVHIVRG--DFD-----ENLTYPEQKV 74
Cdd:cd00841   1 KIGVISDTHGN---LEAIEKALELFE-DGVDAVIHAGDFVSPFVLNALLELKAPLIAVRGnnDGEvdqllGRPILPEFLT 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19920498  75 VTVGQFRIGLCHGHQvvprGDPEALALIQRQLDVDILITGHTYKFEAYEHGNKFYINPGSATG 137
Cdd:cd00841  77 LEIGGLRILLTHGHL----FGVLEALYLAKEGGADVVVFGHTHVPVIERVGGTLLLNPGSVSG 135
PRK09453 PRK09453
phosphodiesterase; Provisional
 1-136 2.82e-09

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 53.71  E-value: 2.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920498    1 MLVLVLGDLHiphrcSSLPA--KFKKLLVPGRIHHILATGNICTK-------ESYD------YLKSLANDVHIVRGDFDE 65
Cdd:PRK09453   1 MKLMFASDTH-----GSLPAteKALELFAQSGADWLVHLGDVLYHgprnplpEGYApkkvaeLLNAYADKIIAVRGNCDS 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19920498   66 N-----LTYPEQK---VVTVGQFRIGLCHGHQVvprgDPEALALIQrqlDVDILITGHTYKFEAYEHGNKFYINPGSAT 136
Cdd:PRK09453  76 EvdqmlLHFPIMApyqQVLLEGKRLFLTHGHLY----GPENLPALH---DGDVLVYGHTHIPVAEKQGGIILFNPGSVS 147
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 1-92 5.88e-04

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 37.96  E-value: 5.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920498     1 MLVLVLGDLHIPHRCSSLPAKFKKLLVPGRIHHILATGNIC-----TKESYDYLKSLAN--DVHIVRG----DFDENLTY 69
Cdd:pfam00149   1 MRILVIGDLHLPGQLDDLLELLKKLLEEGKPDLVLHAGDLVdrgppSEEVLELLERLIKyvPVYLVRGnhdfDYGECLRL 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 19920498    70 PEQKVVTVGQFR-----------IGLCHGHQVVP 92
Cdd:pfam00149  81 YPYLGLLARPWKrflevfnflplAGILSGHTHVP 114
 
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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