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Conserved domains on  [gi|115532280|ref|NP_001040654|]
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Serine/threonine-protein phosphatase [Caenorhabditis elegans]

Protein Classification

serine/threonine protein phosphatase( domain architecture ID 12191156)

protein phosphatase specific for serine and threonine, similar to Methanosarcina thermophila serine/threonine-protein phosphatase PP1-arch2 and Caenorhabditis elegans putative serine/threonine-protein phosphatase C23G10.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 31-339 3.47e-111

Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine phosphatases, that includes PP1, PP2A and PP2B (calcineurin) family members.


:

Pssm-ID: 197547 [Multi-domain]  Cd Length: 271  Bit Score: 326.09  E-value: 3.47e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280    31 YEKSDLLLLIGQIMELFKMEKTLATISPPVTIVGDIHGQYPDLVRILnsriskEEAKQKivtsySSNRFVFLGDYVDRGN 110
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLF------DKNGQP-----PETNYVFLGDYVDRGP 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280   111 HSIECICLVFALKvldlkfvsllvimfqIAYPTNFVLLRGNHETKAINFAYGFREELENRLGKkdgfEIWEKFNEVFSFM 190
Cdd:smart00156  70 FSIEVILLLFALK---------------ILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGE----RIYEKFNEAFSWL 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280   191 PLACLVGGRILCMHGGISEKLESLDSIDSIVRPLpEVTD--LAQDLLWSDPMDvqtlasisDTPKYAKNIvRGLAHSFND 268
Cdd:smart00156 131 PLAALINGKILCMHGGLSPDLTTLDDIRKLKRPQ-EPPDdgLLIDLLWSDPDQ--------PVNGFGPSI-RGASYIFGP 200

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115532280   269 AAVRDVCRRLNLHLVVRAHQMIPEGFKFNSDRKLLTIFSAPRYMNESDNRGATLQVDVNGQLSISVMRYTK 339
Cdd:smart00156 201 DAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPNYCDRFGNKAAVLKVDKDLKLTFEQFKPGK 271
 
Name Accession Description Interval E-value
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 31-339 3.47e-111

Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine phosphatases, that includes PP1, PP2A and PP2B (calcineurin) family members.


Pssm-ID: 197547 [Multi-domain]  Cd Length: 271  Bit Score: 326.09  E-value: 3.47e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280    31 YEKSDLLLLIGQIMELFKMEKTLATISPPVTIVGDIHGQYPDLVRILnsriskEEAKQKivtsySSNRFVFLGDYVDRGN 110
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLF------DKNGQP-----PETNYVFLGDYVDRGP 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280   111 HSIECICLVFALKvldlkfvsllvimfqIAYPTNFVLLRGNHETKAINFAYGFREELENRLGKkdgfEIWEKFNEVFSFM 190
Cdd:smart00156  70 FSIEVILLLFALK---------------ILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGE----RIYEKFNEAFSWL 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280   191 PLACLVGGRILCMHGGISEKLESLDSIDSIVRPLpEVTD--LAQDLLWSDPMDvqtlasisDTPKYAKNIvRGLAHSFND 268
Cdd:smart00156 131 PLAALINGKILCMHGGLSPDLTTLDDIRKLKRPQ-EPPDdgLLIDLLWSDPDQ--------PVNGFGPSI-RGASYIFGP 200

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115532280   269 AAVRDVCRRLNLHLVVRAHQMIPEGFKFNSDRKLLTIFSAPRYMNESDNRGATLQVDVNGQLSISVMRYTK 339
Cdd:smart00156 201 DAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPNYCDRFGNKAAVLKVDKDLKLTFEQFKPGK 271
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 61-324 1.73e-86

phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; The PPP (phosphoprotein phosphatase) family is one of two known protein phosphatase families specific for serine and threonine. This family includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277316 [Multi-domain]  Cd Length: 229  Bit Score: 261.54  E-value: 1.73e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280  61 TIVGDIHGQYPDLVRILNSRISKEEAKqkivtsyssnrFVFLGDYVDRGNHSIECICLVFALKVLdlkfvsllvimfqia 140
Cdd:cd00144    1 IVVGDIHGCFDDLLRLLEKLGFPPEDK-----------YLFLGDYVDRGPDSVEVIDLLLALKIL--------------- 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 141 YPTNFVLLRGNHETKAINFAYGFREELENRLGKKDGFEIWEKFNEVFSFMPLACLVGGRILCMHGGISEKLESLDSIDSI 220
Cdd:cd00144   55 YPDNVFLLRGNHEFMLLNFLYGFYDERTLRCLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNI 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 221 VRPLPEVTDLAQDLLWSDPmdvqtlasiSDTPKYAKNIVRGLAHSFNDAAVRDVCRRLNLHLVVRAHQMIPEGFKFNSDR 300
Cdd:cd00144  135 RPIENPDDQLVEDLLWSDP---------DESVGDFESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGG 205

                        250       260
                 ....*....|....*....|....
gi 115532280 301 KLLTIFSAPRYMNESDNRGATLQV 324
Cdd:cd00144  206 KLITIFSAPNYCGKGGNKLAALVV 229
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 10-335 1.40e-65

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 210.15  E-value: 1.40e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280  10 IHQFIKSHLFVKNWINYRQHVYEKSDLLLLIGQIMELFKMEKTLATISPPVTIVGDIHGQYPDLVRILnsriskeeakQK 89
Cdd:PTZ00244   4 VQTLIEKMLTVKGNRTQRQILIREEDIRAVLTEVREIFMSQPMLLEIRPPVRVCGDTHGQYYDLLRIF----------EK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280  90 IVTSYSSNrFVFLGDYVDRGNHSIECICLVFAlkvldlkfvsllvimFQIAYPTNFVLLRGNHETKAINFAYGFREELEN 169
Cdd:PTZ00244  74 CGFPPYSN-YLFLGDYVDRGKHSVETITLQFC---------------YKIVYPENFFLLRGNHECASINKMYGFFDDVKR 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 170 RLGKKdgfeIWEKFNEVFSFMPLACLVGGRILCMHGGISEKLESLDSIDSIVRPLpEVTD--LAQDLLWSDPMD-VQTLA 246
Cdd:PTZ00244 138 RYNIK----LFKAFTDVFNTMPVCCVISEKIICMHGGLSPDLTSLASVNEIERPC-DVPDrgILCDLLWADPEDeVRGFL 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 247 SiSDtpkyaknivRGLAHSFNDAAVRDVCRRLNLHLVVRAHQMIPEGFKFNSDRKLLTIFSAPRYMNESDNRGATLQVDV 326
Cdd:PTZ00244 213 E-SD---------RGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLVTVFSAPNYCGEFDNDAAVMNIDD 282


                 ....*....
gi 115532280 327 NGQLSISVM 335
Cdd:PTZ00244 283 KLQCSFLII 291
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 59-198 2.58e-12

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: 63.00  E-value: 2.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280   59 PVTIVGDIH--GQYPDLVRILNSRISKEEAKQkivtsyssnrFVFLGDYVDRGNHSIECICLVFALKVLDlkfvsllvim 136
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEEGKPDL----------VLHAGDLVDRGPPSEEVLELLERLIKYV---------- 61

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115532280  137 fqiayptNFVLLRGNHEtkainfaYGFREELENRLGKKDGFEIWEKFNEVFSFMPLACLVGG 198
Cdd:pfam00149  62 -------PVYLVRGNHD-------FDYGECLRLYPYLGLLARPWKRFLEVFNFLPLAGILSG 109
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
62-226 3.16e-04

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 41.05  E-value: 3.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280  62 IVGDIHGQYPDLVRILnsriskEEAKQKIVtsyssNRFVFLGDYVDRGNHSIECICLVFALKVldlkfvsllvimfqiay 141
Cdd:COG0622    4 VISDTHGNLPALEAVL------EDLEREGV-----DLIVHLGDLVGYGPDPPEVLDLLRELPI----------------- 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 142 ptnfVLLRGNHETKAINF--AYGFREELEnrlgkkdgfeiwekfnevfsfmplacLVGGRILCMHGGISEKLESLDSIDS 219
Cdd:COG0622   56 ----VAVRGNHDGAVLRGlrSLPETLRLE--------------------------LEGVRILLVHGSPNEYLLPDTPAER 105


                 ....*..
gi 115532280 220 IVRPLPE 226
Cdd:COG0622  106 LRALAAE 112
 
Name Accession Description Interval E-value
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 31-339 3.47e-111

Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine phosphatases, that includes PP1, PP2A and PP2B (calcineurin) family members.


Pssm-ID: 197547 [Multi-domain]  Cd Length: 271  Bit Score: 326.09  E-value: 3.47e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280    31 YEKSDLLLLIGQIMELFKMEKTLATISPPVTIVGDIHGQYPDLVRILnsriskEEAKQKivtsySSNRFVFLGDYVDRGN 110
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLF------DKNGQP-----PETNYVFLGDYVDRGP 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280   111 HSIECICLVFALKvldlkfvsllvimfqIAYPTNFVLLRGNHETKAINFAYGFREELENRLGKkdgfEIWEKFNEVFSFM 190
Cdd:smart00156  70 FSIEVILLLFALK---------------ILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGE----RIYEKFNEAFSWL 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280   191 PLACLVGGRILCMHGGISEKLESLDSIDSIVRPLpEVTD--LAQDLLWSDPMDvqtlasisDTPKYAKNIvRGLAHSFND 268
Cdd:smart00156 131 PLAALINGKILCMHGGLSPDLTTLDDIRKLKRPQ-EPPDdgLLIDLLWSDPDQ--------PVNGFGPSI-RGASYIFGP 200

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115532280   269 AAVRDVCRRLNLHLVVRAHQMIPEGFKFNSDRKLLTIFSAPRYMNESDNRGATLQVDVNGQLSISVMRYTK 339
Cdd:smart00156 201 DAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPNYCDRFGNKAAVLKVDKDLKLTFEQFKPGK 271
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 61-324 1.73e-86

phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; The PPP (phosphoprotein phosphatase) family is one of two known protein phosphatase families specific for serine and threonine. This family includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277316 [Multi-domain]  Cd Length: 229  Bit Score: 261.54  E-value: 1.73e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280  61 TIVGDIHGQYPDLVRILNSRISKEEAKqkivtsyssnrFVFLGDYVDRGNHSIECICLVFALKVLdlkfvsllvimfqia 140
Cdd:cd00144    1 IVVGDIHGCFDDLLRLLEKLGFPPEDK-----------YLFLGDYVDRGPDSVEVIDLLLALKIL--------------- 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 141 YPTNFVLLRGNHETKAINFAYGFREELENRLGKKDGFEIWEKFNEVFSFMPLACLVGGRILCMHGGISEKLESLDSIDSI 220
Cdd:cd00144   55 YPDNVFLLRGNHEFMLLNFLYGFYDERTLRCLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNI 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 221 VRPLPEVTDLAQDLLWSDPmdvqtlasiSDTPKYAKNIVRGLAHSFNDAAVRDVCRRLNLHLVVRAHQMIPEGFKFNSDR 300
Cdd:cd00144  135 RPIENPDDQLVEDLLWSDP---------DESVGDFESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGG 205

                        250       260
                 ....*....|....*....|....
gi 115532280 301 KLLTIFSAPRYMNESDNRGATLQV 324
Cdd:cd00144  206 KLITIFSAPNYCGKGGNKLAALVV 229
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 9-327 4.90e-77

PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 (protein phosphatase type 1) is a serine/threonine phosphatase that regulates many cellular processes including: cell-cycle progression, protein synthesis, muscle contraction, carbohydrate metabolism, transcription and neuronal signaling, through its interaction with at least 180 known targeting proteins. PP1 occurs in all tissues and regulates many pathways, ranging from cell-cycle progression to carbohydrate metabolism. Also included here are the PPKL (PP1 and kelch-like) enzymes including the PPQ, PPZ1, and PPZ2 fungal phosphatases. These PPKLs have a large N-terminal kelch repeat in addition to a C-terminal phosphoesterase domain. The PPP (phosphoprotein phosphatase) family, to which PP1 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277359 [Multi-domain]  Cd Length: 291  Bit Score: 239.55  E-value: 4.90e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280   9 DIHQFIKSHLFVKNWINYRQHVYEKSDLLLLIGQIMELFKMEKTLATISPPVTIVGDIHGQYPDLVRILNSRISKEEAKq 88
Cdd:cd07414    1 DIDSIIERLLEVRGSRPGKNVQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESN- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280  89 kivtsyssnrFVFLGDYVDRGNHSIECICLVFALKvldlkfvsllvimfqIAYPTNFVLLRGNHETKAINFAYGFREELE 168
Cdd:cd07414   80 ----------YLFLGDYVDRGKQSLETICLLLAYK---------------IKYPENFFLLRGNHECASINRIYGFYDECK 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 169 NRLGKKdgfeIWEKFNEVFSFMPLACLVGGRILCMHGGISEKLESLDSIDSIVRP--LPEvTDLAQDLLWSDPMDvqtla 246
Cdd:cd07414  135 RRYNIK----LWKTFTDCFNCLPVAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPtdVPD-QGLLCDLLWSDPDK----- 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 247 sisDTPKYAKNiVRGLAHSFNDAAVRDVCRRLNLHLVVRAHQMIPEGFKFNSDRKLLTIFSAPRYMNESDNRGATLQVDV 326
Cdd:cd07414  205 ---DVQGWGEN-DRGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDE 280


                 .
gi 115532280 327 N 327
Cdd:cd07414  281 T 281
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 34-329 1.09e-69

PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of phosphoprotein phosphatases (PPP's) including PP4 and PP6. PP2A (Protein phosphatase 2A) is a critical regulator of many cellular activities. PP2A comprises about 1% of total cellular proteins. PP2A, together with protein phosphatase 1 (PP1), accounts for more than 90% of all serine/threonine phosphatase activities in most cells and tissues. The PP2A subunit in addition to having a catalytic domain homologous to PP1, has a unique C-terminal tail, containing a motif that is conserved in the catalytic subunits of all PP2A-like phosphatases including PP4 and PP6, and has an important role in PP2A regulation. The PP2A-like family of phosphatases all share a similar heterotrimeric architecture, that includes: a 65kDa scaffolding subunit (A), a 36kDa catalytic subunit (C), and one of 18 regulatory subunits (B). The PPP (phosphoprotein phosphatase) family, to which PP2A belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277360 [Multi-domain]  Cd Length: 285  Bit Score: 220.54  E-value: 1.09e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280  34 SDLLLLIGQIMELFKMEKTLATISPPVTIVGDIHGQYPDLVRILnsriskeeakqKIVTSYSSNRFVFLGDYVDRGNHSI 113
Cdd:cd07415   18 SEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELF-----------RIGGDVPDTNYLFLGDYVDRGYYSV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 114 ECICLVFALKVLdlkfvsllvimfqiaYPTNFVLLRGNHETKAINFAYGFREELENRLGKKDgfeIWEKFNEVFSFMPLA 193
Cdd:cd07415   87 ETFLLLLALKVR---------------YPDRITLLRGNHESRQITQVYGFYDECLRKYGNAN---VWKYFTDLFDYLPLA 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 194 CLVGGRILCMHGGISEKLESLDSIDSIVR--PLPEVTDLAqDLLWSDPMDVQTLaSISDtpkyaknivRGLAHSFNDAAV 271
Cdd:cd07415  149 ALIDGQIFCVHGGLSPSIQTLDQIRALDRfqEVPHEGPMC-DLLWSDPDDREGW-GISP---------RGAGYLFGQDVV 217

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 115532280 272 RDVCRRLNLHLVVRAHQMIPEGFKFNSDRKLLTIFSAPRYMNESDNRGATLQVDVNGQ 329
Cdd:cd07415  218 EEFNHNNGLTLICRAHQLVMEGYQWMFNNKLVTVWSAPNYCYRCGNVASILELDEHLN 275
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 11-327 7.63e-68

PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein phosphatase in its regulation by a second messenger (calcium and calmodulin). PP2B is involved in many biological processes including immune responses, the second messenger cAMP pathway, sodium/potassium ion transport in the nephron, cell cycle progression in lower eukaryotes, cardiac hypertrophy, and memory formation. PP2B is highly conserved from yeast to humans, but is absent from plants. PP2B is a heterodimer consisting of a catalytic subunit (CnA) and a regulatory subunit (CnB); CnB contains four Ca2+ binding motifs referred to as EF hands. The PPP (phosphoprotein phosphatase) family, to which PP2B belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277361 [Multi-domain]  Cd Length: 305  Bit Score: 216.40  E-value: 7.63e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280  11 HQFIKSHLFvknwinyRQHVYEKSDLLLLIGQIMELFKMEKTLATISPPVTIVGDIHGQYPDLVRILnsriskeeakqKI 90
Cdd:cd07416    3 VDILKAHFM-------REGRLSEEDALRIITEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLF-----------EV 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280  91 VTSYSSNRFVFLGDYVDRGNHSIECICLVFALKVLdlkfvsllvimfqiaYPTNFVLLRGNHETKAINFAYGFREELENr 170
Cdd:cd07416   65 GGSPANTRYLFLGDYVDRGYFSIECVLYLWALKIL---------------YPKTLFLLRGNHECRHLTEYFTFKQECKI- 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 171 lgkKDGFEIWEKFNEVFSFMPLACLVGGRILCMHGGISEKLESLDSIDSIVR-PLPEVTDLAQDLLWSDPM-DVQTLASi 248
Cdd:cd07416  129 ---KYSERVYDACMEAFDCLPLAALMNQQFLCVHGGLSPELKTLDDIRKLDRfREPPSYGPMCDLLWSDPLeDFGNEKT- 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 249 sdTPKYAKNIVRGLAHSFNDAAVRDVCRRLNLHLVVRAHQMIPEGFKFNsdRK--------LLTIFSAPRYMNESDNRGA 320
Cdd:cd07416  205 --QEHFVHNTVRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDAGYRMY--RKsqttgfpsLITIFSAPNYLDVYNNKAA 280


                 ....*..
gi 115532280 321 TLQVDVN 327
Cdd:cd07416  281 VLKYENN 287
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 10-335 1.40e-65

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 210.15  E-value: 1.40e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280  10 IHQFIKSHLFVKNWINYRQHVYEKSDLLLLIGQIMELFKMEKTLATISPPVTIVGDIHGQYPDLVRILnsriskeeakQK 89
Cdd:PTZ00244   4 VQTLIEKMLTVKGNRTQRQILIREEDIRAVLTEVREIFMSQPMLLEIRPPVRVCGDTHGQYYDLLRIF----------EK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280  90 IVTSYSSNrFVFLGDYVDRGNHSIECICLVFAlkvldlkfvsllvimFQIAYPTNFVLLRGNHETKAINFAYGFREELEN 169
Cdd:PTZ00244  74 CGFPPYSN-YLFLGDYVDRGKHSVETITLQFC---------------YKIVYPENFFLLRGNHECASINKMYGFFDDVKR 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 170 RLGKKdgfeIWEKFNEVFSFMPLACLVGGRILCMHGGISEKLESLDSIDSIVRPLpEVTD--LAQDLLWSDPMD-VQTLA 246
Cdd:PTZ00244 138 RYNIK----LFKAFTDVFNTMPVCCVISEKIICMHGGLSPDLTSLASVNEIERPC-DVPDrgILCDLLWADPEDeVRGFL 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 247 SiSDtpkyaknivRGLAHSFNDAAVRDVCRRLNLHLVVRAHQMIPEGFKFNSDRKLLTIFSAPRYMNESDNRGATLQVDV 326
Cdd:PTZ00244 213 E-SD---------RGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLVTVFSAPNYCGEFDNDAAVMNIDD 282


                 ....*....
gi 115532280 327 NGQLSISVM 335
Cdd:PTZ00244 283 KLQCSFLII 291
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 27-322 6.85e-65

Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase domain; Bsu1 encodes a nuclear serine-threonine protein phosphatase found in plants and protozoans. Bsu1 has a C-terminal phosphatase domain and an N-terminal Kelch-repeat domain. Bsu1 is preferentially expressed in elongating plant cells. It modulates the phosphorylation state of Bes1, a transcriptional regulator phosphorylated by the glycogen synthase kinase Bin2, as part of a steroid hormone signal transduction pathway. The PPP (phosphoprotein phosphatase) family, to which Bsu1 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277363 [Multi-domain]  Cd Length: 311  Bit Score: 209.22  E-value: 6.85e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280  27 RQHVYEKSDLLLLIGQIMELFKMEKTLATISPPVTIVGDIHGQYPDLVRIL-NSRISKEEAKQKIvtsySSNRFVFLGDY 105
Cdd:cd07419   17 RRFFFDCQEIAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFdEYGSPVTEEAGDI----EYIDYLFLGDY 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 106 VDRGNHSIECICLVFALKvldlkfvsllvimfqIAYPTNFVLLRGNHETKAINFAYGFREELENRLGK--KDGFEIWEKF 183
Cdd:cd07419   93 VDRGSHSLETICLLLALK---------------VKYPNQIHLIRGNHEAADINALFGFREECIERLGEdiRDGDSVWQRI 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 184 NEVFSFMPLACLVGGRILCMHGGISEKLESLDSIDSIVRPLPEVTD--LAQDLLWSDPMDVQTLASISDTPKYAKNivRG 261
Cdd:cd07419  158 NRLFNWLPLAALIEDKIICVHGGIGRSINHIHQIENLKRPITMEAGspVVMDLLWSDPTENDSVLGLRPNAIDPRG--TG 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115532280 262 LAHSFNDAAVRDVCRRLNLHLVVRAHQMIPEGFKFNSDRKLLTIFSAPRYMNESDNRGATL 322
Cdd:cd07419  236 LIVKFGPDRVMEFLEENDLQMIIRAHECVMDGFERFAQGHLITLFSATNYCGTAGNAGAIL 296
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 3-336 1.98e-59

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 195.26  E-value: 1.98e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280   3 DDNITLDIHQFIKSHLFVKNWINYRQHVYEKSDLLLLIGQIMELFKMEKTLATISPPVTIVGDIHGQYPDLVRILNSRIS 82
Cdd:PTZ00480   4 DKKGEIDVDNIIERLLSVRGSKPGKNVNLTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGGY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280  83 KEEAKqkivtsyssnrFVFLGDYVDRGNHSIECICLVFAlkvldlkfvsllvimFQIAYPTNFVLLRGNHETKAINFAYG 162
Cdd:PTZ00480  84 PPESN-----------YLFLGDYVDRGKQSLETICLLLA---------------YKIKYPENFFLLRGNHECASINRIYG 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 163 FREELENRLGKKdgfeIWEKFNEVFSFMPLACLVGGRILCMHGGISEKLESLDSIDSIVRP--LPEvTDLAQDLLWSDP- 239
Cdd:PTZ00480 138 FYDECKRRYTIK----LWKTFTDCFNCLPVAALIDEKILCMHGGLSPELSNLEQIRRIMRPtdVPD-TGLLCDLLWSDPd 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 240 MDVQTLASISdtpkyaknivRGLAHSFNDAAVRDVCRRLNLHLVVRAHQMIPEGFKFNSDRKLLTIFSAPRYMNESDNRG 319
Cdd:PTZ00480 213 KDVQGWADNE----------RGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAG 282

                        330
                 ....*....|....*..
gi 115532280 320 ATLQVDVNGQLSISVMR 336
Cdd:PTZ00480 283 SMMTIDESLMCSFQILK 299
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 1-320 9.36e-57

PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a member of the PPP gene family of protein phosphatases that is highly conserved among eukaryotes and widely expressed in mammalian tissues. PP5 has a C-terminal phosphatase domain and an extended N-terminal TPR (tetratricopeptide repeat) domain containing three TPR motifs. The PPP (phosphoprotein phosphatase) family, to which PP5 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277362 [Multi-domain]  Cd Length: 316  Bit Score: 188.23  E-value: 9.36e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280   1 MADDNITLDihqfikshlFVKNWINY--RQHVYEKSDLLLLIGQIMELFKMEKTLATISPP----VTIVGDIHGQYPDLV 74
Cdd:cd07417    6 LEDGKVTLE---------FVKEMMEWfkDQKKLHKKYAYQILLQVKEILKKLPSLVEITIPegekITVCGDTHGQFYDLL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280  75 RI--LNSRISKEeakqkivtsyssNRFVFLGDYVDRGNHSIECICLVFALKVLdlkfvsllvimfqiaYPTNFVLLRGNH 152
Cdd:cd07417   77 NIfeLNGLPSET------------NPYLFNGDFVDRGSFSVEVILTLFAFKLL---------------YPNHFHLNRGNH 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 153 ETKAINFAYGFREELENRLGKKdgfeIWEKFNEVFSFMPLACLVGGRILCMHGGI-SEKLESLDSIDSIVR-PLPEVTDL 230
Cdd:cd07417  130 ETDNMNKIYGFEGEVKAKYNEQ----MFNLFSEVFNWLPLAHLINGKVLVVHGGLfSDDGVTLDDIRKIDRfRQPPDSGL 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 231 AQDLLWSDPMDvQTLASISDtpkyaknivRGLAHSFNDAAVRDVCRRLNLHLVVRAHQMIPEGFKFNSDRKLLTIFSAPR 310
Cdd:cd07417  206 MCELLWSDPQP-QPGRGPSK---------RGVGCQFGPDVTKRFLEENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPN 275

                        330
                 ....*....|
gi 115532280 311 YMNESDNRGA 320
Cdd:cd07417  276 YCDQMGNKGA 285
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 35-329 4.46e-52

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 175.77  E-value: 4.46e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280  35 DLLLLIGQIMELFKMEKTLATISPPVTIVGDIHGQYPDLVRILNSRiskeeakqkivTSYSSNRFVFLGDYVDRGNHSIE 114
Cdd:PTZ00239  20 DLKLICERAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEG-----------GDIPNANYIFIGDFVDRGYNSVE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 115 CICLVFALKVldlkfvsllvimfqiAYPTNFVLLRGNHETKAINFAYGFREELENRLGKKDGfeiWEKFNEVFSFMPLAC 194
Cdd:PTZ00239  89 TMEYLLCLKV---------------KYPGNITLLRGNHESRQCTQVYGFYEEILRKYGNSNP---WRLFMDVFDCLPLAA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 195 LVGGRILCMHGGISEKLESLDSIDSIVRP--LPEVTDLAqDLLWSDPMDVQTLASISdtpkyaknivRGLAHSFNDAAVR 272
Cdd:PTZ00239 151 LIEGQILCVHGGLSPDMRTIDQIRTIDRKieIPHEGPFC-DLMWSDPEEVEYWAVNS----------RGAGYLFGAKVTK 219

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 115532280 273 DVCRRLNLHLVVRAHQMIPEGFKF-NSDRKLLTIFSAPRYMNESDNRGATLQVDVNGQ 329
Cdd:PTZ00239 220 EFCRLNDLTLICRAHQLVMEGYKYwFPDQNLVTVWSAPNYCYRCGNIASILCLDENLQ 277
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 56-320 1.34e-50

Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal degeneration C) is a vertebrate serine-threonine protein phosphatase that is required to prevent light-induced retinal degeneration. In addition to its catalytic domain, RdgC has two C-terminal EF hands. Homologs of RdgC include the human phosphatases protein phosphatase with EF hands 1 and -2 (PPEF-1 and -2). PPEF-1 transcripts are present at low levels in the retina, PPEF-2 transcripts and PPEF-2 protein are present at high levels in photoreceptors. The PPP (phosphoprotein phosphatase) family, to which RdgC belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277364 [Multi-domain]  Cd Length: 297  Bit Score: 171.44  E-value: 1.34e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280  56 ISPPVTIVGDIHGQYPDLVRIL--NSRISKEeakqkivtsyssNRFVFLGDYVDRGNHSIECICLVFAlkvldlkfvsll 133
Cdd:cd07420   49 YSKEVTICGDLHGKLDDLLLIFykNGLPSPE------------NPYVFNGDFVDRGKRSIEILMILFA------------ 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 134 vimFQIAYPTNFVLLRGNHETKAINFAYGFREELENRLgKKDGFEIWEKFNEVFSFMPLACLVGGRILCMHGGISEKLEs 213
Cdd:cd07420  105 ---FVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKY-KDHGKKILRLLEDVFSWLPLATIIDNKVLVVHGGISDSTD- 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 214 LDSIDSIVRP--LPEVTDLAQ--DLLWSDPMDvqtlasisdTPKYAKNIVRGLAHSFNDAAVRDVCRRLNLHLVVRAHQM 289
Cdd:cd07420  180 LDLLDKIDRHkyVSTKTEWQQvvDILWSDPKA---------TKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHEC 250

                        250       260       270
                 ....*....|....*....|....*....|.
gi 115532280 290 IPEGFKFNSDRKLLTIFSAPRYMNESDNRGA 320
Cdd:cd07420  251 KPEGYEFCHNNKVITIFSASNYYEEGSNRGA 281
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 46-320 1.14e-36

PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly expressed in a subset of stomata and thought to play an important role in sensory signaling. PP7 acts as a positive regulator of signaling downstream of cryptochrome blue light photoreceptors. PP7 also controls amplification of phytochrome signaling, and interacts with nucleotidediphosphate kinase 2 (NDPK2), a positive regulator of phytochrome signalling. In addition, PP7 interacts with heat shock transcription factor HSF and up-regulates protective heat shock proteins. PP7 may also play a role in salicylic acid-dependent defense signaling. The PPP (phosphoprotein phosphatase) family, to which PP7 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP2A, PP2B (calcineurin), PP4, PP5, PP6, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 163661 [Multi-domain]  Cd Length: 377  Bit Score: 136.85  E-value: 1.14e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280  46 LFKMEKTLATI----SPPVTIVGDIHGQYPDLVRILnsriskeeakqKIVTSYSSNR-FVFLGDYVDRGNHSIECICLVF 120
Cdd:cd07418   50 ILHREPNCVRIdvedVCEVVVVGDVHGQLHDVLFLL-----------EDAGFPDQNRfYVFNGDYVDRGAWGLETFLLLL 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 121 ALKVLdlkfvsllvimfqiaYPTNFVLLRGNHETKAINFAYGFREELENRLGKKdGFEIWEKFNEVFSFMPLACLVGGRI 200
Cdd:cd07418  119 SWKVL---------------LPDRVYLLRGNHESKFCTSMYGFEQEVLTKYGDK-GKHVYRKCLGCFEGLPLASIIAGRV 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 201 LCMHGGI---------------------------SEKLESLDSIDSIVR----PLPEVTDL-AQDLLWSDPmdvqtlasi 248
Cdd:cd07418  183 YTAHGGLfrspslpkrkkqkgknrrvlllepeseSLKLGTLDDLMKARRsvldPPGEGSNLiPGDVLWSDP--------- 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 249 SDTPKYAKNIVRGLAHSFNDAAVRDVCRRLNLHLVVRAHQ------------MIPEGFKFNSD---RKLLTIFSAPRYMN 313
Cdd:cd07418  254 SLTPGLSPNKQRGIGLLWGPDCTEEFLEKNNLKLIIRSHEgpdarekrpglaGMNKGYTVDHDvesGKLITLFSAPDYPQ 333

                        330
                 ....*....|...
gi 115532280 314 ESD------NRGA 320
Cdd:cd07418  334 FQAteerynNKGA 346
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 59-198 2.58e-12

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: 63.00  E-value: 2.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280   59 PVTIVGDIH--GQYPDLVRILNSRISKEEAKQkivtsyssnrFVFLGDYVDRGNHSIECICLVFALKVLDlkfvsllvim 136
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEEGKPDL----------VLHAGDLVDRGPPSEEVLELLERLIKYV---------- 61

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115532280  137 fqiayptNFVLLRGNHEtkainfaYGFREELENRLGKKDGFEIWEKFNEVFSFMPLACLVGG 198
Cdd:pfam00149  62 -------PVYLVRGNHD-------FDYGECLRLYPYLGLLARPWKRFLEVFNFLPLAGILSG 109
PHA02239 PHA02239
putative protein phosphatase
 60-133 7.67e-08

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 52.69  E-value: 7.67e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115532280  60 VTIVGDIHGQYPDLVRILNSRISKEEAKQKIVtsyssnrfvFLGDYVDRGNHSIECICLVFALKVLDLKFVSLL 133
Cdd:PHA02239   3 IYVVPDIHGEYQKLLTIMDKINNERKPEETIV---------FLGDYVDRGKRSKDVVNYIFDLMSNDDNVVTLL 67
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 62-211 8.39e-08

Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein phosphatase E) is a bacterial member of the PPP (phosphoprotein phosphatase) family of serine/threonine phosphatases and a key signal transduction pathway component controlling the expression of spore germination receptors GerA and GerK in Bacillus subtilis. PrpE is closely related to ApaH (also known symmetrical Ap(4)A hydrolase and bis(5'nucleosyl)-tetraphosphatase). PrpE has specificity for phosphotyrosine only, unlike the serine/threonine phosphatases to which it is related. The Bacilli members of this family are single domain proteins while the other members have N- and C-terminal domains in addition to this phosphatase domain. Pnkp is the end-healing and end-sealing component of an RNA repair system present in bacteria. It is composed of three catalytic modules: an N-terminal polynucleotide 5' kinase, a central 2',3' phosphatase, and a C-terminal ligase. Pnkp is a Mn(2+)-dependent phosphodiesterase-monoesterase that dephosphorylates 2',3'-cyclic phosphate RNA ends. An RNA binding site is suggested by a continuous tract of positive surface potential flanking the active site. The PPP (phosphoprotein phosphatase) family, to which PrpE belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277366 [Multi-domain]  Cd Length: 235  Bit Score: 52.52  E-value: 8.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280  62 IVGDIHGQYPDLVRILnSRISKEEAKQKIVTSYSSNRFVFLGDYVDRGNHSIECICLVF-------ALKVLdlkfvsllv 134
Cdd:cd07423    2 IIGDVHGCYDELVELL-EKLGYQKKEEGLYVHPEGRKLVFLGDLVDRGPDSIDVLRLVMnmvkagkALYVP--------- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 135 imfqiayptnfvllrGNHETK--------AINFAYGFREELE--NRLGKKDGFEIWEKFNEVFSFMPL-ACLVGGRILCM 203
Cdd:cd07423   72 ---------------GNHCNKlyrylkgrNVQLAHGLETTVEelEALSKEERPEFRERFAEFLESLPShLVLDGGRLVVA 136


                 ....*...
gi 115532280 204 HGGISEKL 211
Cdd:cd07423  137 HAGIKEEM 144
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 62-153 1.70e-04

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: 41.10  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280  62 IVGDIHGQYPDLVRILNSRISKEEAkqkivtsysSNRFVFLGDYVDRGNHSIECICLVFALKvldlkfvsllvimfqiAY 141
Cdd:cd00838    2 VISDIHGNLEALEAVLEAALAKAEK---------PDLVICLGDLVDYGPDPEEVELKALRLL----------------LA 56

                         90
                 ....*....|..
gi 115532280 142 PTNFVLLRGNHE 153
Cdd:cd00838   57 GIPVYVVPGNHD 68
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
62-226 3.16e-04

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 41.05  E-value: 3.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280  62 IVGDIHGQYPDLVRILnsriskEEAKQKIVtsyssNRFVFLGDYVDRGNHSIECICLVFALKVldlkfvsllvimfqiay 141
Cdd:COG0622    4 VISDTHGNLPALEAVL------EDLEREGV-----DLIVHLGDLVGYGPDPPEVLDLLRELPI----------------- 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 142 ptnfVLLRGNHETKAINF--AYGFREELEnrlgkkdgfeiwekfnevfsfmplacLVGGRILCMHGGISEKLESLDSIDS 219
Cdd:COG0622   56 ----VAVRGNHDGAVLRGlrSLPETLRLE--------------------------LEGVRILLVHGSPNEYLLPDTPAER 105


                 ....*..
gi 115532280 220 IVRPLPE 226
Cdd:COG0622  106 LRALAAE 112
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 62-158 3.34e-04

PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine and tyrosine phosphatases thought to modulate the expression of proteins that protect the cell upon accumulation of misfolded proteins in the periplasm. The PPP (phosphoprotein phosphatase) family, to which PrpA and PrpB belong, is one of two known protein phosphatase families specific for serine and threonine. This family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277367 [Multi-domain]  Cd Length: 201  Bit Score: 41.53  E-value: 3.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280  62 IVGDIHGQYPDLVRILNSrISKEEAKqkivtsyssNRFVFLGDYVDRGNHSIECiclvfaLKVLDLKFvsllvimfqiay 141
Cdd:cd07424    5 VVGDIHGHFQRLQRALDA-VGFDPAR---------DRLISVGDLVDRGPESLEV------LELLKQPW------------ 56

                         90
                 ....*....|....*..
gi 115532280 142 ptnFVLLRGNHETKAIN 158
Cdd:cd07424   57 ---FHAVQGNHEQMAID 70
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
 62-210 4.76e-04

bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 41.23  E-value: 4.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280  62 IVGDIHGQYPDLVRIlnsrISK--EEAKQKIVTSYSSNRFVFLGDYVDRGNHSIECIclvfalkvldlKFVSLLVIMFQI 139
Cdd:PRK13625   5 IIGDIHGCYQEFQAL----TEKlgYNWSSGLPVHPDQRKLAFVGDLTDRGPHSLRMI-----------EIVWELVEKKAA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 140 AYptnfvlLRGNHETKAINF--------AYGFR---EELENrLGKKDGFEIWEKFNEVFSFMPL-ACLVGGRILCMHGGI 207
Cdd:PRK13625  70 YY------VPGNHCNKLYRFflgrnvtiAHGLEttvAEYEA-LPSHKQNMIKEKFITLYEQAPLyHILDEGRLVVAHAGI 142


                 ...
gi 115532280 208 SEK 210
Cdd:PRK13625 143 RQD 145
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 63-208 4.78e-04

Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, eukaryotic, and archeal proteins orthologous to the Shewanella cold-active protein-tyrosine phosphatase, CAPTPase. CAPTPase is an uncharacterized protein that belongs to the Shelph (Shewanella-like phosphatase) family of PPP (phosphoprotein phosphatases). The PPP family is one of two known protein phosphatase families specific for serine and threonine. In addition to Shelps, the PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277368 [Multi-domain]  Cd Length: 209  Bit Score: 41.13  E-value: 4.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280  63 VGDIHGQYPDLVRILnsRISKeeakqkiVTSYSSNR------FVFLGDYVDRGNHsieciclvfalkvlDLKFVSLLVIM 136
Cdd:cd07425    3 IGDLHGDLDRLRTIL--KLAG-------VIDSNDRWiggdtvVVQTGDILDRGDD--------------EIEILKLLEKL 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 137 FQIAYPTN--FVLLRGNHETKAI--NFAY---------GFREELENRLGKKDGFeiwekfneVFSF---MPLACLVGGrI 200
Cdd:cd07425   60 KRQARKAGgkVILLLGNHELMNLcgDFRYvhprglnefGGVAKRRYALLSDGGY--------IGRYlrtHPVVLVVND-I 130


                 ....*...
gi 115532280 201 LCMHGGIS 208
Cdd:cd07425  131 LFVHGGLG 138
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
62-208 1.50e-03

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 40.15  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280  62 IVGDIHGQYPDLVRILnsriskeeakQKIVTSYSSNRFVFLGDYVDRGNHSIECiclvfalkvldLKFVsllvimfqIAY 141
Cdd:PRK00166   5 AIGDIQGCYDELQRLL----------EKIDFDPAKDTLWLVGDLVNRGPDSLEV-----------LRFV--------KSL 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280 142 PTNFVLLRGNHETKAINFAYGFReelenRLGKKDgfeiweKFNEVFS------------FMPLACLVGGRILCM-HGGIS 208
Cdd:PRK00166  56 GDSAVTVLGNHDLHLLAVAAGIK-----RNKKKD------TLDPILEapdrdelldwlrHQPLLHVDEELGLVMvHAGIP 124
MPP_PA3087 cd07413
Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an ...
 62-159 9.83e-03

Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an uncharacterized protein from Pseudomonas aeruginosa with a metallophosphatase domain that belongs to the phosphoprotein phosphatase (PPP) family. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277358 [Multi-domain]  Cd Length: 222  Bit Score: 37.14  E-value: 9.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532280  62 IVGDIHGQYPDLVRILNSRiskEEAKQKIVTSYSSNRFVFLGDYVDRGNHSIECICLVFALkvldLKFVSLLVIMfqiay 141
Cdd:cd07413    3 LIGDVHGCAHTLDRLLDLL---GYRLQGGVWRHPRRQALFVGDLIDRGPRIREVLHRVHAM----VDAGEALCVM----- 70

                         90
                 ....*....|....*...
gi 115532280 142 ptnfvllrGNHETKAINF 159
Cdd:cd07413   71 --------GNHEFNALAW 80
 
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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