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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424758     45 LPVNVFDSLVLTAHKILHKERNCVHIDdldsvSNVVVVGDIHGQLHDLLFLLKDTGFPCQNRcYVFNGDYVDRGAWGLET 124
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVS-----APVTVCGDIHGQFDDLLRLFDKNGQPPETN-YVFLGDYVDRGPFSIEV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424758    125 FLVLLSWKVLMPDRVYLLRGNHESKYCTSMYGFEKEVLTKYgdkGKHVYRKCLGCFEGLPLASIISGRVYTAHGGLfrsp 204
Cdd:smart00156  75 ILLLFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKY---GERIYEKFNEAFSWLPLAALINGKILCMHGGL---- 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424758    205 vlpkrttrgkknrrvvllepepsSMKLGTLDELMQARRSVLDPPWEgsnlIPGDVLWSDPSMT-PGLSPNeQRGIGLLWG 283
Cdd:smart00156 148 -----------------------SPDLTTLDDIRKLKRPQEPPDDG----LLIDLLWSDPDQPvNGFGPS-IRGASYIFG 199

                          250
                   ....*....|....
gi 18424758    284 PDCTEDFLKKYELK 297
Cdd:smart00156 200 PDAVDEFLKKNNLK 213

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424758    79 VVVVGDIH--GQLHDLLFLLKDTGFPCQNRCYVFNGDYVDRGAWGLETFLVLLSWKVLMPdrVYLLRGNHESKYCtsmyg 156
Cdd:pfam00149   3 ILVIGDLHlpGQLDDLLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLELLERLIKYVP--VYLVRGNHDFDYG----- 75

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 18424758   157 fEKEVLTKYGDKGKHVYRKCLGCFEGLPLASIISG 191
Cdd:pfam00149  76 -ECLRLYPYLGLLARPWKRFLEVFNFLPLAGILSG 109

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424758  80 VVVGDIHGQLHDLLFLLKDTGFPCqNRCYVFNGDYVDRGAWGLETFLVLLSWKVLMPDRVYLLRGNHESKYCTSMYGFEK 159
Cdd:cd00144   1 IVVGDIHGCFDDLLRLLEKLGFPP-EDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424758 160 EVLTKYGDK-GKHVYRKCLGCFEGLPLASIISGRVYTAHGGLFRSpvlpkrttrgkknrrvvllepepssmkLGTLDELM 238
Cdd:cd00144  80 ERTLRCLRKgGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPD---------------------------LTLLDQIR 132

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18424758 239 QARrsvldPPWEGSNLIPGDVLWSDPSMTPGLSPNEQRGIGLLWGPDCTEDFLKKYELK 297
Cdd:cd00144 133 NIR-----PIENPDDQLVEDLLWSDPDESVGDFESSSRGGGYLFGEDAVDEFLKKNGLK 186

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424758     45 LPVNVFDSLVLTAHKILHKERNCVHIDdldsvSNVVVVGDIHGQLHDLLFLLKDTGFPCQNRcYVFNGDYVDRGAWGLET 124
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVS-----APVTVCGDIHGQFDDLLRLFDKNGQPPETN-YVFLGDYVDRGPFSIEV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424758    125 FLVLLSWKVLMPDRVYLLRGNHESKYCTSMYGFEKEVLTKYgdkGKHVYRKCLGCFEGLPLASIISGRVYTAHGGLfrsp 204
Cdd:smart00156  75 ILLLFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKY---GERIYEKFNEAFSWLPLAALINGKILCMHGGL---- 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424758    205 vlpkrttrgkknrrvvllepepsSMKLGTLDELMQARRSVLDPPWEgsnlIPGDVLWSDPSMT-PGLSPNeQRGIGLLWG 283
Cdd:smart00156 148 -----------------------SPDLTTLDDIRKLKRPQEPPDDG----LLIDLLWSDPDQPvNGFGPS-IRGASYIFG 199

                          250
                   ....*....|....
gi 18424758    284 PDCTEDFLKKYELK 297
Cdd:smart00156 200 PDAVDEFLKKNNLK 213

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424758  57 AHKILHKERNCVHIDDldSVSN-VVVVGDIHGQLHDLLFLLKDTGFPCQNRCYVFNGDYVDRGAWGLETFLVLLSWKVLM 135
Cdd:cd07420  32 ARKSLKQLPNISRVST--SYSKeVTICGDLHGKLDDLLLIFYKNGLPSPENPYVFNGDFVDRGKRSIEILMILFAFVLVY 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424758 136 PDRVYLLRGNHESKYCTSMYGFEKEVLTKYGDKGKHVYRKCLGCFEGLPLASIISGRVYTAHGGLFRSPVLP--KRTTRG 213
Cdd:cd07420 110 PNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKDHGKKILRLLEDVFSWLPLATIIDNKVLVVHGGISDSTDLDllDKIDRH 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424758 214 KknrrvvllepepssMKlGTLDELMQarrsVLdppwegsnlipgDVLWSDPSMTPGLSPNEQRGIGLLWGPDCTEDFLKK 293
Cdd:cd07420 190 K--------------YV-STKTEWQQ----VV------------DILWSDPKATKGCKPNTFRGGGCYFGPDVTSQFLQK 238

                ....
gi 18424758 294 YELK 297
Cdd:cd07420 239 HGLS 242

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424758  81 VVGDIHGQLHDLLFLLKDTGFPCQNRcYVFNGDYVDRGAWGLETFLVLLSWKVLMPDRVYLLRGNHESKYCTSMYGFEKE 160
Cdd:cd07414  54 ICGDIHGQYYDLLRLFEYGGFPPESN-YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDE 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424758 161 VLTKYGDKgkhVYRKCLGCFEGLPLASIISGRVYTAHGGLfrSPVLpkrttrgkknrrvvllepepSSMKlgtldelmQA 240
Cdd:cd07414 133 CKRRYNIK---LWKTFTDCFNCLPVAAIVDEKIFCCHGGL--SPDL--------------------QSME--------QI 179

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18424758 241 RRSV--LDPPWEGsnlIPGDVLWSDPSM-TPGLSPNEqRGIGLLWGPDCTEDFLKKYEL 296
Cdd:cd07414 180 RRIMrpTDVPDQG---LLCDLLWSDPDKdVQGWGEND-RGVSFTFGADVVAKFLHKHDL 234

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424758  81 VVGDIHGQLHDLLFLLKDTGFPCQNRC-------YVFNGDYVDRGAWGLETFLVLLSWKVLMPDRVYLLRGNHESKYCTS 153
Cdd:cd07419  52 IFGDIHGQFGDLMRLFDEYGSPVTEEAgdieyidYLFLGDYVDRGSHSLETICLLLALKVKYPNQIHLIRGNHEAADINA 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424758 154 MYGFEKEVLTKYGDK---GKHVYRKCLGCFEGLPLASIISGRVYTAHGGLFRSpvlpkrttrgkknrrvvllepepssmk 230
Cdd:cd07419 132 LFGFREECIERLGEDirdGDSVWQRINRLFNWLPLAALIEDKIICVHGGIGRS--------------------------- 184

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18424758 231 LGTLDELMQARRSVLDPPwegSNLIPGDVLWSDPSMT---PGLSPN--EQRGIGLL--WGPDCTEDFLKKYELKV 298
Cdd:cd07419 185 INHIHQIENLKRPITMEA---GSPVVMDLLWSDPTENdsvLGLRPNaiDPRGTGLIvkFGPDRVMEFLEENDLQM 256

serine/threonine-protein phosphatase PP1; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424758   79 VVVVGDIHGQLHDLLFLLKDTGFPCQNRcYVFNGDYVDRGAWGLETFLVLLSWKVLMPDRVYLLRGNHESKYCTSMYGFE 158
Cdd:PTZ00244  54 VRVCGDTHGQYYDLLRIFEKCGFPPYSN-YLFLGDYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGFF 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424758  159 KEVLTKYGDKgkhVYRKCLGCFEGLPLASIISGRVYTAHGGLfrspvlpkrttrgkknrrvvllepEPSSMKLGTLDELM 238
Cdd:PTZ00244 133 DDVKRRYNIK---LFKAFTDVFNTMPVCCVISEKIICMHGGL------------------------SPDLTSLASVNEIE 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 18424758  239 QArrsvLDPPWEGsnlIPGDVLWSDPSMTPGLSPNEQRGIGLLWGPDCTEDFL 291
Cdd:PTZ00244 186 RP----CDVPDRG---ILCDLLWADPEDEVRGFLESDRGVSYLFGEDIVNDFL 231

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424758  81 VVGDIHGQLHDLLFLLKDTGF----------PcQNRCYVFNGDYVDRGAWGLETflVLLSWKVLMPDRVYLLRGNHESKY 150
Cdd:cd07423   2 IIGDVHGCYDELVELLEKLGYqkkeeglyvhP-EGRKLVFLGDLVDRGPDSIDV--LRLVMNMVKAGKALYVPGNHCNKL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424758 151 C--------TSMYGFEKEV--LTKYG-DKGKHVYRKCLGCFEGLPLASIIS-GRVYTAHGGLfrspvlpKRTTRGKKNRR 218
Cdd:cd07423  79 YrylkgrnvQLAHGLETTVeeLEALSkEERPEFRERFAEFLESLPSHLVLDgGRLVVAHAGI-------KEEMIGRGSKR 151

                .
gi 18424758 219 V 219
Cdd:cd07423 152 V 152

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.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18424758  80 VVVGDIHGQLHDLLFLLKD-TGFPCQNRCYVFNGDYVDRGAWGLETFLVLLSWKvLMPDRVYLLRGNHE 147
Cdd:cd00838   1 LVISDIHGNLEALEAVLEAaLAKAEKPDLVICLGDLVDYGPDPEEVELKALRLL-LAGIPVYVVPGNHD 68

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424758  80 VVVGDIHGQLHDLLFLLKDTGFPCQNRCYVFN-------GDYVDRGAWGLETFLVLLSWKVLMPD---RVYLLRGNHES- 148
Cdd:cd07425   1 VAIGDLHGDLDRLRTILKLAGVIDSNDRWIGGdtvvvqtGDILDRGDDEIEILKLLEKLKRQARKaggKVILLLGNHELm 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18424758 149 ------KYCTS----MYGFEKEVLTKYGDKGKHVYRKclgcFEGLPLASIISGRVYtAHGGLfrSPVL 206
Cdd:cd07425  81 nlcgdfRYVHPrglnEFGGVAKRRYALLSDGGYIGRY----LRTHPVVLVVNDILF-VHGGL--GPLW 141