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Conserved domains on  [gi|157786944|ref|NP_001099402|]
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vacuolar protein sorting-associated protein 29 [Rattus norvegicus]

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 2.39e-129

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: 359.99  E-value: 2.39e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786944   2 LVLVLGDLHIPHRCNSLPAKFKKLLVPGKIQHILCTGNLCTKESYDYLKTLAGDVHIVRGDFDESLNYPEQKVVTVGQFK 81
Cdd:cd07394    1 LVLVIGDLHIPHRAADLPAKFKKLLVPGKIQHVLCTGNLCSKETYDYLKTIAPDVHIVRGDFDENLNYPETKVITVGQFK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786944  82 IGLIHGHQVIPWGDMASLALLQRQFDVDILISGHTHKFEAFEHENKFYINPGSATGAYNALETNIIPSFVLMDIQASTVV 161
Cdd:cd07394   81 IGLIHGHQVVPWGDPDSLAALQRQLDVDILISGHTHKFEAFEHEGKFFINPGSATGAFSPLDPNVIPSFVLMDIQGSTVV 160

                        170
                 ....*....|....*...
gi 157786944 162 TYVYQLIGDDVKVERIEY 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 2.39e-129

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: 359.99  E-value: 2.39e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786944   2 LVLVLGDLHIPHRCNSLPAKFKKLLVPGKIQHILCTGNLCTKESYDYLKTLAGDVHIVRGDFDESLNYPEQKVVTVGQFK 81
Cdd:cd07394    1 LVLVIGDLHIPHRAADLPAKFKKLLVPGKIQHVLCTGNLCSKETYDYLKTIAPDVHIVRGDFDENLNYPETKVITVGQFK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786944  82 IGLIHGHQVIPWGDMASLALLQRQFDVDILISGHTHKFEAFEHENKFYINPGSATGAYNALETNIIPSFVLMDIQASTVV 161
Cdd:cd07394   81 IGLIHGHQVVPWGDPDSLAALQRQLDVDILISGHTHKFEAFEHEGKFFINPGSATGAFSPLDPNVIPSFVLMDIQGSTVV 160

                        170
                 ....*....|....*...
gi 157786944 162 TYVYQLIGDDVKVERIEY 179
Cdd:cd07394  161 TYVYQLIDGEVKVEKIEY 178
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
 1-140 2.84e-30

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: 108.23  E-value: 2.84e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786944    1 MLVLVLGDLHIPHRCNSLPAKFKKLLVpgKIQHILCTGNLCTKESYDYLKTLAGDVHIVRGDFD-ESLNYPEQKVVTVGQ 79
Cdd:TIGR00040   1 MKILVISDTHGPLRATELPVELFNLES--NVDLVIHAGDLTSPFVLKEFEDLAAKVIAVRGNNDgERDELPEEEIFEAEG 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157786944   80 FKIGLIHGHQVIPWGDMASLALLQRQFDVDILISGHTHKFEAFEHENKFYINPGSATGAYN 140
Cdd:TIGR00040  79 IDFGLVHGDLVYPRGDLLVLEYLAKELGVDVLIFGHTHIPVAEELRGILLINPGSLTGPRN 139
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 1-157 8.38e-27

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: 98.92  E-value: 8.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786944    1 MLVLVLGDLHiphRCNSLPAKFKKLLVpGKIQHILCTGNLCTKESYDYLKTLAgDVHIVRGDFDE----SLNYPEQKVVT 76
Cdd:pfam12850   1 MRIGIISDTH---DNLALPEAALERLK-GVVDLIIHAGDIVAPEVLEELLELA-PVLAVRGNNDAaaefATDLPEEAVLE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786944   77 VGQFKIGLIHGHQVipwgDMASLALLQRQFD-VDILISGHTHKFEAFEHENKFYINPGSATGAYNALEtniiPSFVLMDI 155
Cdd:pfam12850  76 LGGVKILLTHGHGV----KDALARLLRRAEEgVAVVVYGHTHVPGVERIGGVLFVNPGSVGGPRFGDP----PTYALLDI 147


                  ..
gi 157786944  156 QA 157
Cdd:pfam12850 148 DD 149
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
3-179 5.49e-21

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 84.97  E-value: 5.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786944   3 VLVLGDLHiphrcNSLPA--KFKKLLVPGKIQHILCTG-----NLCTKESYDYLKTLagDVHIVRG-----DFDESLNYP 70
Cdd:COG0622    2 IAVISDTH-----GNLPAleAVLEDLEREGVDLIVHLGdlvgyGPDPPEVLDLLREL--PIVAVRGnhdgaVLRGLRSLP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786944  71 EQKVVTVGQFKIGLIHGHQ---VIPWGDMASLALLQRQFDVDILISGHTHKFEAFEHENKFYINPGSATGAynalETNII 147
Cdd:COG0622   75 ETLRLELEGVRILLVHGSPneyLLPDTPAERLRALAAEGDADVVVCGHTHIPFVRRVGGVLLVNPGSVGQP----RDGDP 150

                        170       180       190
                 ....*....|....*....|....*....|..
gi 157786944 148 PSFVLMDIQASTVvtyvyqligdDVKVERIEY 179
Cdd:COG0622  151 ASYAILDIDDGEW----------SVEFVRVPY 172
PRK09453 PRK09453
phosphodiesterase; Provisional
 1-136 1.70e-11

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 59.88  E-value: 1.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786944   1 MLVLVLGDLHiphrcNSLPA--KFKKLLVPGKIQHILCTGNLCTK-------ESYD------YLKTLAGDVHIVRG---- 61
Cdd:PRK09453   1 MKLMFASDTH-----GSLPAteKALELFAQSGADWLVHLGDVLYHgprnplpEGYApkkvaeLLNAYADKIIAVRGncds 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157786944  62 DFDES-LNYPEQK---VVTVGQFKIGLIHGHQVIPwGDMASLAllqrqfDVDILISGHTHKFEAFEHENKFYINPGSAT 136
Cdd:PRK09453  76 EVDQMlLHFPIMApyqQVLLEGKRLFLTHGHLYGP-ENLPALH------DGDVLVYGHTHIPVAEKQGGIILFNPGSVS 147
 
Name Accession Description Interval E-value
MPP_Vps29 cd07394
Homo sapiens Vps29 and related proteins, metallophosphatase domain; Vps29 (vacuolar sorting ...
 2-179 2.39e-129

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: 359.99  E-value: 2.39e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786944   2 LVLVLGDLHIPHRCNSLPAKFKKLLVPGKIQHILCTGNLCTKESYDYLKTLAGDVHIVRGDFDESLNYPEQKVVTVGQFK 81
Cdd:cd07394    1 LVLVIGDLHIPHRAADLPAKFKKLLVPGKIQHVLCTGNLCSKETYDYLKTIAPDVHIVRGDFDENLNYPETKVITVGQFK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786944  82 IGLIHGHQVIPWGDMASLALLQRQFDVDILISGHTHKFEAFEHENKFYINPGSATGAYNALETNIIPSFVLMDIQASTVV 161
Cdd:cd07394   81 IGLIHGHQVVPWGDPDSLAALQRQLDVDILISGHTHKFEAFEHEGKFFINPGSATGAFSPLDPNVIPSFVLMDIQGSTVV 160

                        170
                 ....*....|....*...
gi 157786944 162 TYVYQLIGDDVKVERIEY 179
Cdd:cd07394  161 TYVYQLIDGEVKVEKIEY 178
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
 1-140 2.84e-30

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: 108.23  E-value: 2.84e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786944    1 MLVLVLGDLHIPHRCNSLPAKFKKLLVpgKIQHILCTGNLCTKESYDYLKTLAGDVHIVRGDFD-ESLNYPEQKVVTVGQ 79
Cdd:TIGR00040   1 MKILVISDTHGPLRATELPVELFNLES--NVDLVIHAGDLTSPFVLKEFEDLAAKVIAVRGNNDgERDELPEEEIFEAEG 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157786944   80 FKIGLIHGHQVIPWGDMASLALLQRQFDVDILISGHTHKFEAFEHENKFYINPGSATGAYN 140
Cdd:TIGR00040  79 IDFGLVHGDLVYPRGDLLVLEYLAKELGVDVLIFGHTHIPVAEELRGILLINPGSLTGPRN 139
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 1-157 8.38e-27

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: 98.92  E-value: 8.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786944    1 MLVLVLGDLHiphRCNSLPAKFKKLLVpGKIQHILCTGNLCTKESYDYLKTLAgDVHIVRGDFDE----SLNYPEQKVVT 76
Cdd:pfam12850   1 MRIGIISDTH---DNLALPEAALERLK-GVVDLIIHAGDIVAPEVLEELLELA-PVLAVRGNNDAaaefATDLPEEAVLE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786944   77 VGQFKIGLIHGHQVipwgDMASLALLQRQFD-VDILISGHTHKFEAFEHENKFYINPGSATGAYNALEtniiPSFVLMDI 155
Cdd:pfam12850  76 LGGVKILLTHGHGV----KDALARLLRRAEEgVAVVVYGHTHVPGVERIGGVLFVNPGSVGGPRFGDP----PTYALLDI 147


                  ..
gi 157786944  156 QA 157
Cdd:pfam12850 148 DD 149
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
3-179 5.49e-21

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 84.97  E-value: 5.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786944   3 VLVLGDLHiphrcNSLPA--KFKKLLVPGKIQHILCTG-----NLCTKESYDYLKTLagDVHIVRG-----DFDESLNYP 70
Cdd:COG0622    2 IAVISDTH-----GNLPAleAVLEDLEREGVDLIVHLGdlvgyGPDPPEVLDLLREL--PIVAVRGnhdgaVLRGLRSLP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786944  71 EQKVVTVGQFKIGLIHGHQ---VIPWGDMASLALLQRQFDVDILISGHTHKFEAFEHENKFYINPGSATGAynalETNII 147
Cdd:COG0622   75 ETLRLELEGVRILLVHGSPneyLLPDTPAERLRALAAEGDADVVVCGHTHIPFVRRVGGVLLVNPGSVGQP----RDGDP 150

                        170       180       190
                 ....*....|....*....|....*....|..
gi 157786944 148 PSFVLMDIQASTVvtyvyqligdDVKVERIEY 179
Cdd:COG0622  151 ASYAILDIDDGEW----------SVEFVRVPY 172
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 2-137 1.85e-18

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: 77.70  E-value: 1.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786944   2 LVLVLGDLHIPhrcNSLPAKFKKLLVpGKIQHILCTGNLCTKESYDYLKTLAGDVHIVRG--DFD-----ESLNYPEQKV 74
Cdd:cd00841    1 KIGVISDTHGN---LEAIEKALELFE-DGVDAVIHAGDFVSPFVLNALLELKAPLIAVRGnnDGEvdqllGRPILPEFLT 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157786944  75 VTVGQFKIGLIHGHQVIPwGDMASLAllqRQFDVDILISGHTHKFEAFEHENKFYINPGSATG 137
Cdd:cd00841   77 LEIGGLRILLTHGHLFGV-LEALYLA---KEGGADVVVFGHTHVPVIERVGGTLLLNPGSVSG 135
PRK09453 PRK09453
phosphodiesterase; Provisional
 1-136 1.70e-11

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 59.88  E-value: 1.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786944   1 MLVLVLGDLHiphrcNSLPA--KFKKLLVPGKIQHILCTGNLCTK-------ESYD------YLKTLAGDVHIVRG---- 61
Cdd:PRK09453   1 MKLMFASDTH-----GSLPAteKALELFAQSGADWLVHLGDVLYHgprnplpEGYApkkvaeLLNAYADKIIAVRGncds 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157786944  62 DFDES-LNYPEQK---VVTVGQFKIGLIHGHQVIPwGDMASLAllqrqfDVDILISGHTHKFEAFEHENKFYINPGSAT 136
Cdd:PRK09453  76 EVDQMlLHFPIMApyqQVLLEGKRLFLTHGHLYGP-ENLPALH------DGDVLVYGHTHIPVAEKQGGIILFNPGSVS 147
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 1-119 2.11e-07

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: 47.21  E-value: 2.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786944    1 MLVLVLGDLHIPHRCNSLPAKFKKLLVPGKIQHILCTGNL--CTKESYDYLKTLA-----GDVHIVRGDFDESLNYPEQK 73
Cdd:pfam00149   1 MRILVIGDLHLPGQLDDLLELLKKLLEEGKPDLVLHAGDLvdRGPPSEEVLELLErlikyVPVYLVRGNHDFDYGECLRL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 157786944   74 VVTVGQFKIGLIHGHQVIPWgdmaslallqrqFDVDILISGHTHKF 119
Cdd:pfam00149  81 YPYLGLLARPWKRFLEVFNF------------LPLAGILSGHTHVP 114
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 4-133 1.03e-05

metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing 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. This superfamily includes: the phosphoprotein phosphatases (PPPs), 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: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 43.02  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786944   4 LVLGDLHIPHRCNSLPAKfKKLLVPGKIQHILCTGNLCTK--------ESYDYLKTLAGDVHIVRGDFDeslnypeqkvv 75
Cdd:cd00838    1 LVISDIHGNLEALEAVLE-AALAKAEKPDLVICLGDLVDYgpdpeeveLKALRLLLAGIPVYVVPGNHD----------- 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157786944  76 tvgqfkIGLIHGHQVIP--------WGDMASLALLQRQFDVDILISGHTHKFEAFEHE--NKFYINPG 133
Cdd:cd00838   69 ------ILVTHGPPYDPldegspgeDPGSEALLELLDKYGPDLVLSGHTHVPGRREVDkgGTLVVNPG 130
MPP_YbbF-LpxH cd07398
Escherichia coli YbbF/LpxH and related proteins, metallophosphatase domain; YbbF/LpxH is an ...
 99-134 4.77e-04

Escherichia coli YbbF/LpxH and related proteins, metallophosphatase domain; YbbF/LpxH is an Escherichia coli UDP-2,3-diacylglucosamine hydrolase thought to catalyze the fourth step of lipid A biosynthesis, in which a precursor UDP-2,3-diacylglucosamine is hydrolyzed to yield 2,3-diacylglucosamine 1-phosphate and UMP. YbbF 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: 277343 [Multi-domain]  Cd Length: 217  Bit Score: 39.26  E-value: 4.77e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 157786944  99 LALLQRQFDVDILISGHTHKFEAFEHENKFYINPGS 134
Cdd:cd07398  181 VARLARHRGVDGVICGHTHRPAIHRLDGILYINLGD 216
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
79-167 6.47e-04

3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 38.90  E-value: 6.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786944  79 QFKIGLIHgHQVIPWG---------DMASLALLQRQFDVDILISGHTHKFEAFEHENKFYINPGSATGaynalETNIIPS 149
Cdd:COG1409  140 KPVIVFLH-HPPYSTGsgsdriglrNAEELLALLARYGVDLVLSGHVHRYERTRRDGVPYIVAGSTGG-----QVRLPPG 213

                         90
                 ....*....|....*...
gi 157786944 150 FVLMDIQASTVVTYVYQL 167
Cdd:COG1409  214 YRVIEVDGDGLTVEVRRV 231
 
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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