phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human PSP, EC 3.1.3.3, catalyzes the third and final of the L-serine biosynthesis pathway, the Mg2+-dependent hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, L-serine is a precursor for the biosynthesis of glycine. HPSP regulates the levels of glycine and D-serine (converted from L-serine), the putative co-agonists for the glycine site of the NMDA receptor in the brain. Plant 3-PSP catalyzes the conversion of 3-phosphoserine to serine in the last step of the plastidic pathway of serine biosynthesis. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661601  62 QIVCFDVDSTVICEEGIDELAEYCGKGSEVARVTKEAMGGAMTFQDALKIRLNIIRPTQQQVRDFIQERPSTLSKNVKRF 141
Cdd:cd04309   1 DAVCFDVDSTVIQEEGIDELAKFCGVGDEVAELTRRAMGGSIPFRDALRKRLAIINPTKEQVDEFLEEHPPRLTPGVEEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661601 142 VSHLKAEGKQVYLISGGFDCLIAPVANELGIPLKNVYANKMLFDYLGEYDSFDINQPTSRSGGKAEAIALIRKENsDDSL 221
Cdd:cd04309  81 VSRLKARGVEVYLISGGFRELIEPVASQLGIPLENVFANRLLFDFNGEYAGFDETQPTSRSGGKAKVIEQLKEKH-HYKR 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 24661601 222 ITMIGDGATDLEAVPPANYFIGFGGNVVRPEVYRRAQYYVTDF 264
Cdd:cd04309 160 VIMIGDGATDLEACPPADAFIGFGGNVIREKVKARADWYVTDF 202

phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human PSP, EC 3.1.3.3, catalyzes the third and final of the L-serine biosynthesis pathway, the Mg2+-dependent hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, L-serine is a precursor for the biosynthesis of glycine. HPSP regulates the levels of glycine and D-serine (converted from L-serine), the putative co-agonists for the glycine site of the NMDA receptor in the brain. Plant 3-PSP catalyzes the conversion of 3-phosphoserine to serine in the last step of the plastidic pathway of serine biosynthesis. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661601  62 QIVCFDVDSTVICEEGIDELAEYCGKGSEVARVTKEAMGGAMTFQDALKIRLNIIRPTQQQVRDFIQERPSTLSKNVKRF 141
Cdd:cd04309   1 DAVCFDVDSTVIQEEGIDELAKFCGVGDEVAELTRRAMGGSIPFRDALRKRLAIINPTKEQVDEFLEEHPPRLTPGVEEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661601 142 VSHLKAEGKQVYLISGGFDCLIAPVANELGIPLKNVYANKMLFDYLGEYDSFDINQPTSRSGGKAEAIALIRKENsDDSL 221
Cdd:cd04309  81 VSRLKARGVEVYLISGGFRELIEPVASQLGIPLENVFANRLLFDFNGEYAGFDETQPTSRSGGKAKVIEQLKEKH-HYKR 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 24661601 222 ITMIGDGATDLEAVPPANYFIGFGGNVVRPEVYRRAQYYVTDF 264
Cdd:cd04309 160 VIMIGDGATDLEACPPADAFIGFGGNVIREKVKARADWYVTDF 202

phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction 3-phospho-serine + H2O = L-serine + phosphate. It catalyzes the last of three steps in the biosynthesis of serine from D-3-phosphoglycerate. Note that this enzyme acts on free phosphoserine, not on phosphoserine residues of phosphoproteins. [Amino acid biosynthesis, Serine family]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661601    56 KVIQQSQIVCFDVDSTVICEEGIDELAEYCGKGSEVARVTKEAMGGAMTFQDALKIRLNIIRPTQQQVRDFIQERPsTLS 135
Cdd:TIGR00338   9 PLLRSKKLVVFDMDSTLINAETIDEIAKIAGVEEEVSEITERAMRGELDFKASLRERVALLKGLPVELLKEVRENL-PLT 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661601   136 KNVKRFVSHLKAEGKQVYLISGGFDCLIAPVANELGIPLknVYANKMLFdYLGEYDSFDINQPTSRSGGKAEAIALIRKE 215
Cdd:TIGR00338  88 EGAEELVKTLKEKGYKVAVISGGFDLFAEHVKDKLGLDA--AFANRLEV-EDGKLTGLVEGPIVDASYKGKTLLILLRKE 164

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 24661601   216 NSDDSLITMIGDGATDLEAVPPANYFIGFGGNVVRPEV 253
Cdd:TIGR00338 165 GISPENTVAVGDGANDLSMIKAAGLGIAFNAKPKLQQK 202

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661601    63 IVCFDVDSTVI-----CEEGIDELA-----------EYCGKGSEVARVTKEAMGGAMTFQDALKIRLNIIRPTQQQ---- 122
Cdd:pfam00702   3 AVVFDLDGTLTdgepvVTEAIAELAsehplakaivaAAEDLPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEgltv 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661601   123 -----VRDFIQERPSTLSKNVKRFVSHLKAEGKQVYLISGGFDCLIAPVANELGIPLknvyankmLFDYLGEYDSFDINQ 197
Cdd:pfam00702  83 vlvelLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDD--------YFDVVISGDDVGVGK 154

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 24661601   198 PTSRsgGKAEAIALIRKENSDdslITMIGDGATDLEA 234
Cdd:pfam00702 155 PKPE--IYLAALERLGVKPEE---VLMVGDGVNDIPA 186

phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human PSP, EC 3.1.3.3, catalyzes the third and final of the L-serine biosynthesis pathway, the Mg2+-dependent hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, L-serine is a precursor for the biosynthesis of glycine. HPSP regulates the levels of glycine and D-serine (converted from L-serine), the putative co-agonists for the glycine site of the NMDA receptor in the brain. Plant 3-PSP catalyzes the conversion of 3-phosphoserine to serine in the last step of the plastidic pathway of serine biosynthesis. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661601  62 QIVCFDVDSTVICEEGIDELAEYCGKGSEVARVTKEAMGGAMTFQDALKIRLNIIRPTQQQVRDFIQERPSTLSKNVKRF 141
Cdd:cd04309   1 DAVCFDVDSTVIQEEGIDELAKFCGVGDEVAELTRRAMGGSIPFRDALRKRLAIINPTKEQVDEFLEEHPPRLTPGVEEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661601 142 VSHLKAEGKQVYLISGGFDCLIAPVANELGIPLKNVYANKMLFDYLGEYDSFDINQPTSRSGGKAEAIALIRKENsDDSL 221
Cdd:cd04309  81 VSRLKARGVEVYLISGGFRELIEPVASQLGIPLENVFANRLLFDFNGEYAGFDETQPTSRSGGKAKVIEQLKEKH-HYKR 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 24661601 222 ITMIGDGATDLEAVPPANYFIGFGGNVVRPEVYRRAQYYVTDF 264
Cdd:cd04309 160 VIMIGDGATDLEACPPADAFIGFGGNVIREKVKARADWYVTDF 202

phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction 3-phospho-serine + H2O = L-serine + phosphate. It catalyzes the last of three steps in the biosynthesis of serine from D-3-phosphoglycerate. Note that this enzyme acts on free phosphoserine, not on phosphoserine residues of phosphoproteins. [Amino acid biosynthesis, Serine family]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661601    56 KVIQQSQIVCFDVDSTVICEEGIDELAEYCGKGSEVARVTKEAMGGAMTFQDALKIRLNIIRPTQQQVRDFIQERPsTLS 135
Cdd:TIGR00338   9 PLLRSKKLVVFDMDSTLINAETIDEIAKIAGVEEEVSEITERAMRGELDFKASLRERVALLKGLPVELLKEVRENL-PLT 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661601   136 KNVKRFVSHLKAEGKQVYLISGGFDCLIAPVANELGIPLknVYANKMLFdYLGEYDSFDINQPTSRSGGKAEAIALIRKE 215
Cdd:TIGR00338  88 EGAEELVKTLKEKGYKVAVISGGFDLFAEHVKDKLGLDA--AFANRLEV-EDGKLTGLVEGPIVDASYKGKTLLILLRKE 164

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 24661601   216 NSDDSLITMIGDGATDLEAVPPANYFIGFGGNVVRPEV 253
Cdd:TIGR00338 165 GISPENTVAVGDGANDLSMIKAAGLGIAFNAKPKLQQK 202

Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model represents a subfamily of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. Subfamily IA, B, C and D are distinguished from the rest of the superfamily by the presence of a variable domain between the first and second conserved catalytic motifs. In subfamilies IA and IB, this domain consists of an alpha-helical bundle. It was necessary to model these two subfamilies separately, breaking them at a an apparent phylogenetic bifurcation, so that the resulting model(s) are not so broadly defined that members of subfamily III (which lack the variable domain) are included. Subfamily IA includes the enzyme phosphoserine phosphatase (TIGR00338) as well as three hypothetical equivalogs. Many members of these hypothetical equivalogs have been annotated as PSPase-like or PSPase-family proteins. In particular, the hypothetical equivalog which appears to be most closely related to PSPase contains only Archaea (while TIGR00338 contains only eukaryotes and bacteria) of which some are annotated as PSPases. Although this is a reasonable conjecture, none of these sequences has sufficient evidence for this assignment. If such should be found, this model should be retired while the PSPase model should be broadened to include these sequences. [Unknown function, Enzymes of unknown specificity]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661601    63 IVCFDVDSTVICEEG-IDELAEYCGKGSEVARVTKEAMGGAMTFQDALKIRLNIIR--PTQQQVRDFIQERPsTLSKNVK 139
Cdd:TIGR01488   1 LAIFDFDGTLTRQDSlIDLLAKLLGTNDEVIELTRLAPSGRISFEDALGRRLALLHrsRSEEVAKEFLARQV-ALRPGAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661601   140 RFVSHLKAEGKQVYLISGGFDCLIAPVANELGIPlkNVYANKMLFDYLGEYDSFDINQPTSRSGGKAEAIALIRKENSDD 219
Cdd:TIGR01488  80 ELISWLKERGIDTVIVSGGFDFFVEPVAEKLGID--DVFANRLEFDDNGLLTGPIEGQVNPEGECKGKVLKELLEESKIT 157

                         170       180
                  ....*....|....*....|
gi 24661601   220 -SLITMIGDGATDLEAVPPA 238
Cdd:TIGR01488 158 lKKIIAVGDSVNDLPMLKLA 177

phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like superfamily; Bacillus subtilis recycles two toxic byproducts of polyamine metabolism, methylthioadenosine and methylthioribose, into methionine by a salvage pathway. The sixth reaction in this pathway is catalyzed by B. subtilis MtnX: the dephosphorylation of 2- hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HKMTP- 1-P) into 1,2-dihydroxy-3-keto-5-methylthiopentene. The hydrolysis of HK-MTP-1-P is a two-step mechanism involving the formation of a transiently phosphorylated aspartyl intermediate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661601  62 QIVCfDVDSTVICEEGIDELAEYCGKGSEVAR-VTKEAMGGAMTFQDALKIRLNIIRPTQQQ-VRDFIQERPsTLSKNVK 139
Cdd:cd07524   1 IVFC-DFDGTITENDNIIYLMDEFAPPLEEWEaLKEGVLSQTLSFREGVGQMFELLPSSLKDeIIEFLEKTA-KIRPGFK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661601 140 RFVSHLKAEGKQVYLISGGFDCLIAPVANELGIPLKNVYANKMlfDYLGEYDSFDINQPTSRSGGKAEAIAL-IRKENSD 218
Cdd:cd07524  79 EFVAFCQEHGIPFIIVSGGMDFFIEPLLEGLVIEKIAIYCNGS--DFSGEQIHIDWPHECDCTNGCGCCKSSiIRKYSKP 156

                       170       180
                ....*....|....*....|..
gi 24661601 219 DSLITMIGDGATDLEAVPPANY 240
Cdd:cd07524 157 RPFIIVIGDSVTDLEAAKEADL 178

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661601    63 IVCFDVDSTVI-----CEEGIDELA-----------EYCGKGSEVARVTKEAMGGAMTFQDALKIRLNIIRPTQQQ---- 122
Cdd:pfam00702   3 AVVFDLDGTLTdgepvVTEAIAELAsehplakaivaAAEDLPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEgltv 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661601   123 -----VRDFIQERPSTLSKNVKRFVSHLKAEGKQVYLISGGFDCLIAPVANELGIPLknvyankmLFDYLGEYDSFDINQ 197
Cdd:pfam00702  83 vlvelLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDD--------YFDVVISGDDVGVGK 154

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 24661601   198 PTSRsgGKAEAIALIRKENSDdslITMIGDGATDLEA 234
Cdd:pfam00702 155 PKPE--IYLAALERLGVKPEE---VLMVGDGVNDIPA 186

phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661601  66 FDVDSTVIC---------EEGIDELAEYCGKGSEVARVTKEAMGGAMTFQ--DALKIRLNIIRPT-QQQVRDFIQE-RPS 132
Cdd:cd02612   4 FDLDGTLIAgdsffaflrFKGIAERRAPLEELLLLRLMALYALGRLDGAGmeALLGFATAGLAGElAALVEEFVEEyILR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661601 133 TLSKNVKRFVSHLKAEGKQVYLISGGFDCLIAPVANELGIPlkNVYANKMLFD---YLGEydsfdINQPTSRSGGKAEAI 209
Cdd:cd02612  84 VLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGID--NVLGTQLETEdgrYTGR-----IIGPPCYGEGKVKRL 156

                       170       180
                ....*....|....*....|....*
gi 24661601 210 -ALIRKENSDDSLITMIGDGATDLE 233
Cdd:cd02612 157 rEWLAEEGIDLKDSYAYSDSINDLP 181

HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The sequences modelled here are all bacterial. The IB subfamily includes the enzyme phosphoserine phosphatase (TIGR00338). Due to this relationship, several of these sequences have been annotated as "phosphoserine phosphatase related proteins," or "Phosphoserine phosphatase-family enzymes." There is presently no evidence that any of the enzymes in this model possess PSPase activity. OMNI|NTL01ML1250 is annotated as a "possible transferase," however this is due to the C-terminal domain found on this sequence which is homologous to a group of glycerol-phosphate acyltransferases (between trusted and noise to TIGR00530). A subset of these sequences including OMNI|CC1962, the Caulobacter crescentus CicA protein cluster together and may represent a separate equivalog. [Unknown function, Enzymes of unknown specificity]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661601    66 FDVDSTVICEEGIDE-LAEYCGKG--SEVARVtKEAMGGAMTFQ-----DALKIRLNIIRPT----QQQVRDFIQE---- 129
Cdd:TIGR01490   4 FDFDGTLTAKDTLFIfLKFLASKNilFEELRL-PKVLARFEFFLnrgldYMAYYRAFALDALagllEEDVRAIVEEfvnq 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661601   130 -RPSTLSKNVKRFVSHLKAEGKQVYLISGGFDCLIAPVANELGIplKNVYANKMLFD----YLGEydsfdINQPTSRSGG 204
Cdd:TIGR01490  83 kIESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGI--DNAIGTRLEESedgiYTGN-----IDGNNCKGEG 155

                         170       180       190
                  ....*....|....*....|....*....|
gi 24661601   205 KAEAIA-LIRKENSDDSLITMIGDGATDLE 233
Cdd:TIGR01490 156 KVHALAeLLAEEQIDLKDSYAYGDSISDLP 185

P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily of the heavy metal-transporting ATPases (Type IB ATPases) which transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661601  77 GIDELAEYCGKGSEVARVTKEAMGGAMTFQDALKIRLNIIRPTQQQVRDFIQERPstLSKNVKRFVSHLKAEGKQVYLIS 156
Cdd:cd07553 380 GASELVEIVGKGVSGNSSGSLWKLGSAPDACGIQESGVVIARDGRQLLDLSFNDL--LRPDSNREIEELKKGGLSIAILS 457

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661601 157 GGFDCLIAPVANELGIPLKNVYANKMlfdylgeydsfdinqptsrsggKAEAIALIRKENSDDSLitMIGDGATDLEAVP 236
Cdd:cd07553 458 GDNEEKVRLVGDSLGLDPRQLFGNLS----------------------PEEKLAWIESHSPENTL--MVGDGANDALALA 513

                       170
                ....*....|..
gi 24661601 237 PANYFIGFGGNV 248
Cdd:cd07553 514 SAFVGIAVAGEV 525