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Conserved domains on  [gi|2069507063|ref|XP_042298116|]
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vacuolar protein sorting-associated protein 29 isoform X1 [Sceloporus undulatus]

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 ...
 12-189 5.01e-127

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: 354.59  E-value: 5.01e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069507063  12 LVLVLGDLHIPHRCNSLPAKFKKLLVPGKIQHILCTGNLCTKESYDYLKTLAGDVHVVRGDFDENLNYPEQKVVTVGQFK 91
Cdd:cd07394     1 LVLVIGDLHIPHRAADLPAKFKKLLVPGKIQHVLCTGNLCSKETYDYLKTIAPDVHIVRGDFDENLNYPETKVITVGQFK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069507063  92 IGLIHGHQVIPWGDVASLALLQRQFDVDILISGHTHKFEAFEHENKFYINPGSATGAYSALENNIISSFVLMDIQASTVV 171
Cdd:cd07394    81 IGLIHGHQVVPWGDPDSLAALQRQLDVDILISGHTHKFEAFEHEGKFFINPGSATGAFSPLDPNVIPSFVLMDIQGSTVV 160

                         170
                  ....*....|....*...
gi 2069507063 172 TYVYQLIGDDVKVERIEY 189
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 ...
 12-189 5.01e-127

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: 354.59  E-value: 5.01e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069507063  12 LVLVLGDLHIPHRCNSLPAKFKKLLVPGKIQHILCTGNLCTKESYDYLKTLAGDVHVVRGDFDENLNYPEQKVVTVGQFK 91
Cdd:cd07394     1 LVLVIGDLHIPHRAADLPAKFKKLLVPGKIQHVLCTGNLCSKETYDYLKTIAPDVHIVRGDFDENLNYPETKVITVGQFK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069507063  92 IGLIHGHQVIPWGDVASLALLQRQFDVDILISGHTHKFEAFEHENKFYINPGSATGAYSALENNIISSFVLMDIQASTVV 171
Cdd:cd07394    81 IGLIHGHQVVPWGDPDSLAALQRQLDVDILISGHTHKFEAFEHEGKFFINPGSATGAFSPLDPNVIPSFVLMDIQGSTVV 160

                         170
                  ....*....|....*...
gi 2069507063 172 TYVYQLIGDDVKVERIEY 189
Cdd:cd07394   161 TYVYQLIDGEVKVEKIEY 178
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
 12-148 5.95e-28

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: 102.45  E-value: 5.95e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069507063  12 LVLVLGDLHIPHRCNSLPAKFKKLLVpgKIQHILCTGNLCTKESYDYLKTLAGDVHVVRGDFD-ENLNYPEQKVVTVGQF 90
Cdd:TIGR00040   2 KILVISDTHGPLRATELPVELFNLES--NVDLVIHAGDLTSPFVLKEFEDLAAKVIAVRGNNDgERDELPEEEIFEAEGI 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2069507063  91 KIGLIHGHQVIPWGDVASLALLQRQFDVDILISGHTHKFEAFEHENKFYINPGSATGA 148
Cdd:TIGR00040  80 DFGLVHGDLVYPRGDLLVLEYLAKELGVDVLIFGHTHIPVAEELRGILLINPGSLTGP 137
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 12-167 3.67e-23

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: 90.06  E-value: 3.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069507063  12 LVLVLGDLHiphRCNSLPAKFKKLLVpGKIQHILCTGNLCTKESYDYLKTLAgDVHVVRGDFDENL----NYPEQKVVTV 87
Cdd:pfam12850   2 RIGIISDTH---DNLALPEAALERLK-GVVDLIIHAGDIVAPEVLEELLELA-PVLAVRGNNDAAAefatDLPEEAVLEL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069507063  88 GQFKIGLIHGHqvipwGDVASLALLQRQF--DVDILISGHTHKFEAFEHENKFYINPGSATGAYSALEnniiSSFVLMDI 165
Cdd:pfam12850  77 GGVKILLTHGH-----GVKDALARLLRRAeeGVAVVVYGHTHVPGVERIGGVLFVNPGSVGGPRFGDP----PTYALLDI 147


                  ..
gi 2069507063 166 QA 167
Cdd:pfam12850 148 DD 149
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
13-189 5.52e-20

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 82.66  E-value: 5.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069507063  13 VLVLGDLHiphrcNSLPA--KFKKLLVPGKIQHILCTG-----NLCTKESYDYLKTLagDVHVVRG-----DFDENLNYP 80
Cdd:COG0622     2 IAVISDTH-----GNLPAleAVLEDLEREGVDLIVHLGdlvgyGPDPPEVLDLLREL--PIVAVRGnhdgaVLRGLRSLP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069507063  81 EQKVVTVGQFKIGLIHGHQ---VIPWGDVASLALLQRQFDVDILISGHTHKFEAFEHENKFYINPGSATGAysalENNII 157
Cdd:COG0622    75 ETLRLELEGVRILLVHGSPneyLLPDTPAERLRALAAEGDADVVVCGHTHIPFVRRVGGVLLVNPGSVGQP----RDGDP 150

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2069507063 158 SSFVLMDIQASTVvtyvyqligdDVKVERIEY 189
Cdd:COG0622   151 ASYAILDIDDGEW----------SVEFVRVPY 172
PRK09453 PRK09453
phosphodiesterase; Provisional
 13-146 1.27e-09

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 54.87  E-value: 1.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069507063  13 VLVLGDLHiphrcNSLPA--KFKKLLVPGKIQHILCTGNLCTK-------ESYD------YLKTLAGDVHVVRGDFDEN- 76
Cdd:PRK09453    3 LMFASDTH-----GSLPAteKALELFAQSGADWLVHLGDVLYHgprnplpEGYApkkvaeLLNAYADKIIAVRGNCDSEv 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2069507063  77 ----LNYPEQK---VVTVGQFKIGLIHGHQVIPwGDVASLAllqrqfDVDILISGHTHKFEAFEHENKFYINPGSAT 146
Cdd:PRK09453   78 dqmlLHFPIMApyqQVLLEGKRLFLTHGHLYGP-ENLPALH------DGDVLVYGHTHIPVAEKQGGIILFNPGSVS 147
 
Name Accession Description Interval E-value
MPP_Vps29 cd07394
Homo sapiens Vps29 and related proteins, metallophosphatase domain; Vps29 (vacuolar sorting ...
 12-189 5.01e-127

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: 354.59  E-value: 5.01e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069507063  12 LVLVLGDLHIPHRCNSLPAKFKKLLVPGKIQHILCTGNLCTKESYDYLKTLAGDVHVVRGDFDENLNYPEQKVVTVGQFK 91
Cdd:cd07394     1 LVLVIGDLHIPHRAADLPAKFKKLLVPGKIQHVLCTGNLCSKETYDYLKTIAPDVHIVRGDFDENLNYPETKVITVGQFK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069507063  92 IGLIHGHQVIPWGDVASLALLQRQFDVDILISGHTHKFEAFEHENKFYINPGSATGAYSALENNIISSFVLMDIQASTVV 171
Cdd:cd07394    81 IGLIHGHQVVPWGDPDSLAALQRQLDVDILISGHTHKFEAFEHEGKFFINPGSATGAFSPLDPNVIPSFVLMDIQGSTVV 160

                         170
                  ....*....|....*...
gi 2069507063 172 TYVYQLIGDDVKVERIEY 189
Cdd:cd07394   161 TYVYQLIDGEVKVEKIEY 178
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
 12-148 5.95e-28

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: 102.45  E-value: 5.95e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069507063  12 LVLVLGDLHIPHRCNSLPAKFKKLLVpgKIQHILCTGNLCTKESYDYLKTLAGDVHVVRGDFD-ENLNYPEQKVVTVGQF 90
Cdd:TIGR00040   2 KILVISDTHGPLRATELPVELFNLES--NVDLVIHAGDLTSPFVLKEFEDLAAKVIAVRGNNDgERDELPEEEIFEAEGI 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2069507063  91 KIGLIHGHQVIPWGDVASLALLQRQFDVDILISGHTHKFEAFEHENKFYINPGSATGA 148
Cdd:TIGR00040  80 DFGLVHGDLVYPRGDLLVLEYLAKELGVDVLIFGHTHIPVAEELRGILLINPGSLTGP 137
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 12-167 3.67e-23

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: 90.06  E-value: 3.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069507063  12 LVLVLGDLHiphRCNSLPAKFKKLLVpGKIQHILCTGNLCTKESYDYLKTLAgDVHVVRGDFDENL----NYPEQKVVTV 87
Cdd:pfam12850   2 RIGIISDTH---DNLALPEAALERLK-GVVDLIIHAGDIVAPEVLEELLELA-PVLAVRGNNDAAAefatDLPEEAVLEL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069507063  88 GQFKIGLIHGHqvipwGDVASLALLQRQF--DVDILISGHTHKFEAFEHENKFYINPGSATGAYSALEnniiSSFVLMDI 165
Cdd:pfam12850  77 GGVKILLTHGH-----GVKDALARLLRRAeeGVAVVVYGHTHVPGVERIGGVLFVNPGSVGGPRFGDP----PTYALLDI 147


                  ..
gi 2069507063 166 QA 167
Cdd:pfam12850 148 DD 149
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
13-189 5.52e-20

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 82.66  E-value: 5.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069507063  13 VLVLGDLHiphrcNSLPA--KFKKLLVPGKIQHILCTG-----NLCTKESYDYLKTLagDVHVVRG-----DFDENLNYP 80
Cdd:COG0622     2 IAVISDTH-----GNLPAleAVLEDLEREGVDLIVHLGdlvgyGPDPPEVLDLLREL--PIVAVRGnhdgaVLRGLRSLP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069507063  81 EQKVVTVGQFKIGLIHGHQ---VIPWGDVASLALLQRQFDVDILISGHTHKFEAFEHENKFYINPGSATGAysalENNII 157
Cdd:COG0622    75 ETLRLELEGVRILLVHGSPneyLLPDTPAERLRALAAEGDADVVVCGHTHIPFVRRVGGVLLVNPGSVGQP----RDGDP 150

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2069507063 158 SSFVLMDIQASTVvtyvyqligdDVKVERIEY 189
Cdd:COG0622   151 ASYAILDIDDGEW----------SVEFVRVPY 172
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 12-147 2.99e-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: 77.31  E-value: 2.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069507063  12 LVLVLGDLHIPhrcNSLPAKFKKLLVpGKIQHILCTGNLCTKESYDYLKTLAGDVHVVRG--DFD-----ENLNYPEQKV 84
Cdd:cd00841     1 KIGVISDTHGN---LEAIEKALELFE-DGVDAVIHAGDFVSPFVLNALLELKAPLIAVRGnnDGEvdqllGRPILPEFLT 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2069507063  85 VTVGQFKIGLIHGHQvipwGDVASLALLQRQFDVDILISGHTHKFEAFEHENKFYINPGSATG 147
Cdd:cd00841    77 LEIGGLRILLTHGHL----FGVLEALYLAKEGGADVVVFGHTHVPVIERVGGTLLLNPGSVSG 135
PRK09453 PRK09453
phosphodiesterase; Provisional
 13-146 1.27e-09

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 54.87  E-value: 1.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069507063  13 VLVLGDLHiphrcNSLPA--KFKKLLVPGKIQHILCTGNLCTK-------ESYD------YLKTLAGDVHVVRGDFDEN- 76
Cdd:PRK09453    3 LMFASDTH-----GSLPAteKALELFAQSGADWLVHLGDVLYHgprnplpEGYApkkvaeLLNAYADKIIAVRGNCDSEv 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2069507063  77 ----LNYPEQK---VVTVGQFKIGLIHGHQVIPwGDVASLAllqrqfDVDILISGHTHKFEAFEHENKFYINPGSAT 146
Cdd:PRK09453   78 dqmlLHFPIMApyqQVLLEGKRLFLTHGHLYGP-ENLPALH------DGDVLVYGHTHIPVAEKQGGIILFNPGSVS 147
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 13-129 1.53e-06

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: 45.28  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069507063  13 VLVLGDLHIPHRCNSLPAKFKKLLVPGKIQHILCTGNL--CTKESYDYLKTLA-----GDVHVVRGDFDENLNYPEQKVV 85
Cdd:pfam00149   3 ILVIGDLHLPGQLDDLLELLKKLLEEGKPDLVLHAGDLvdRGPPSEEVLELLErlikyVPVYLVRGNHDFDYGECLRLYP 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2069507063  86 TVGQFKIGLIHGHQVIPWgdvaslallqrqFDVDILISGHTHKF 129
Cdd:pfam00149  83 YLGLLARPWKRFLEVFNF------------LPLAGILSGHTHVP 114
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 14-143 1.54e-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: 42.64  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069507063  14 LVLGDLHIPHRCNSLPAKfKKLLVPGKIQHILCTGNLCTK--------ESYDYLKTLAGDVHVVRGDFDenlnypeqkvv 85
Cdd:cd00838     1 LVISDIHGNLEALEAVLE-AALAKAEKPDLVICLGDLVDYgpdpeeveLKALRLLLAGIPVYVVPGNHD----------- 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069507063  86 tvgqfkIGLIHGHQVIP--------WGDVASLALLQRQFDVDILISGHTHKFEAFEHE--NKFYINPG 143
Cdd:cd00838    69 ------ILVTHGPPYDPldegspgeDPGSEALLELLDKYGPDLVLSGHTHVPGRREVDkgGTLVVNPG 130
MPP_YbbF-LpxH cd07398
Escherichia coli YbbF/LpxH and related proteins, metallophosphatase domain; YbbF/LpxH is an ...
 109-144 7.78e-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: 38.88  E-value: 7.78e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2069507063 109 LALLQRQFDVDILISGHTHKFEAFEHENKFYINPGS 144
Cdd:cd07398   181 VARLARHRGVDGVICGHTHRPAIHRLDGILYINLGD 216
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
89-177 3.42e-03

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 36.98  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069507063  89 QFKIGLIHgHQVIPWG---------DVASLALLQRQFDVDILISGHTHKFEAFEHENKFYINPGSaTGAYSALENniisS 159
Cdd:COG1409   140 KPVIVFLH-HPPYSTGsgsdriglrNAEELLALLARYGVDLVLSGHVHRYERTRRDGVPYIVAGS-TGGQVRLPP----G 213

                          90
                  ....*....|....*...
gi 2069507063 160 FVLMDIQASTVVTYVYQL 177
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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