magnesium transporting ATPase (MgtA), similar to Escherichia coli MgtA and Salmonella typhimurium MgtA; MgtA is a membrane protein which actively transports Mg(2+) into the cytosol with its electro-chemical gradient rather than against the gradient as other cation transporters do. It may act both as a transporter and as a sensor for Mg(2+). In Salmonella typhimurium and Escherichia coli, the two-component system PhoQ/PhoP regulates the transcription of the mgtA gene by sensing Mg(2+) concentrations in the periplasm. MgtA is activated by cardiolipin and it highly sensitive to free magnesium in vitro. It consists of a transmembrane domain and three cytosolic domains: nucleotide-binding domain, phosphorylation domain and actuator domain, and belongs to the P-type ATPase type III subfamily. The P-type ATPases, are 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 515719845  54 GLSMKEAQKRIHVYGKNELSSKR--------------------------AIFSDV----------------MMKLGEMIP 91
Cdd:cd02077    1 GLTNEEAEERLEKYGPNEISHEKfpswfklllkafinpfnivllvlalvSFFTDVllapgefdlvgaliilLMVLISGLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515719845  92 GFAkQRVHNENQCEI------VTVTVSRVEgcttvgmssdSKIMKLPVEELVPGDMVFLSAGDTVPADLRIIYAEDLLVN 165
Cdd:cd02077   81 DFI-QEIRSLKAAEKlkkmvkNTATVIRDG----------SKYMEIPIDELVPGDIVYLSAGDMIPADVRIIQSKDLFVS 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515719845 166 ESMLTGKEANVEKFEScyhlerkrfipLKRMKDYNPLQLENVCFKGTHIVNGTAKAVVVSTGKNTYSGLL 235
Cdd:cd02077  150 QSSLTGESEPVEKHAT-----------AKKTKDESILELENICFMGTNVVSGSALAVVIATGNDTYFGSI 208

magnesium-translocating P-type ATPase; This model describes the magnesium translocating P-type ATPase found in a limited number of bacterial species and best described in Salmonella typhimurium, which contains two isoforms. These transporters are active in low external Mg2+ concentrations and pump the ion into the cytoplasm. The magnesium ATPases have been classified as type IIIB by a phylogenetic analysis. [Transport and binding proteins, Cations and iron carrying compounds]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515719845   33 LIEIATRDVKSVFAYFKTTRDGLSMKEAQKRIHVYGKNELSSKRAI-------------FSDVMMKLGEM---------- 89
Cdd:TIGR01524  12 LLKESQMGKETLLRKLGVHETGLTNVEVTERLAEFGPNQTVEEKKVpnlrllirafnnpFIYILAMLMGVsyltddleat 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515719845   90 -----------IPGFAKQRVHNENQCEIVTVTVSRVEGCTTVGMSSDSKIMKLPVEELVPGDMVFLSAGDTVPADLRIIY 158
Cdd:TIGR01524  92 viialmvlasgLLGFIQESRAERAAYALKNMVKNTATVLRVINENGNGSMDEVPIDALVPGDLIELAAGDIIPADARVIS 171

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515719845  159 AEDLLVNESMLTGKEANVEKFEScyhlerkrfipLKRMKDYNPLQLENVCFKGTHIVNGTAKAVVVSTGKNTYSGLL 235
Cdd:TIGR01524 172 ARDLFINQSALTGESLPVEKFVE-----------DKRARDPEILERENLCFMGTNVLSGHAQAVVLATGSSTWFGSL 237

Cation transporter/ATPase, N-terminus; This entry represents the conserved N-terminal region found in several classes of cation-transporting P-type ATPases, including those that transport H+, Na+, Ca2+, Na+/K+, and H+/K+. In the H+/K+- and Na+/K+-exchange P-ATPases, this domain is found in the catalytic alpha chain. In gastric H+/K+-ATPases, this domain undergoes reversible sequential phosphorylation inducing conformational changes that may be important for regulating the function of these ATPases.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 515719845    38 TRDVKSVFAYFKTTRD-GLSMKEAQKRIHVYGKNELSSKR 76
Cdd:smart00831   6 ALSLEEVLERLQTDLEkGLSSEEAARRLERYGPNELPPPK 45

magnesium transporting ATPase (MgtA), similar to Escherichia coli MgtA and Salmonella typhimurium MgtA; MgtA is a membrane protein which actively transports Mg(2+) into the cytosol with its electro-chemical gradient rather than against the gradient as other cation transporters do. It may act both as a transporter and as a sensor for Mg(2+). In Salmonella typhimurium and Escherichia coli, the two-component system PhoQ/PhoP regulates the transcription of the mgtA gene by sensing Mg(2+) concentrations in the periplasm. MgtA is activated by cardiolipin and it highly sensitive to free magnesium in vitro. It consists of a transmembrane domain and three cytosolic domains: nucleotide-binding domain, phosphorylation domain and actuator domain, and belongs to the P-type ATPase type III subfamily. The P-type ATPases, are 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 515719845  54 GLSMKEAQKRIHVYGKNELSSKR--------------------------AIFSDV----------------MMKLGEMIP 91
Cdd:cd02077    1 GLTNEEAEERLEKYGPNEISHEKfpswfklllkafinpfnivllvlalvSFFTDVllapgefdlvgaliilLMVLISGLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515719845  92 GFAkQRVHNENQCEI------VTVTVSRVEgcttvgmssdSKIMKLPVEELVPGDMVFLSAGDTVPADLRIIYAEDLLVN 165
Cdd:cd02077   81 DFI-QEIRSLKAAEKlkkmvkNTATVIRDG----------SKYMEIPIDELVPGDIVYLSAGDMIPADVRIIQSKDLFVS 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515719845 166 ESMLTGKEANVEKFEScyhlerkrfipLKRMKDYNPLQLENVCFKGTHIVNGTAKAVVVSTGKNTYSGLL 235
Cdd:cd02077  150 QSSLTGESEPVEKHAT-----------AKKTKDESILELENICFMGTNVVSGSALAVVIATGNDTYFGSI 208

magnesium-transporting P-type ATPase MgtA;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515719845 108 TVTVSRVEGCTtvgmsSDSKIMKLPVEELVPGDMVFLSAGDTVPADLRIIYAEDLLVNESMLTGKEANVEKFESCYHLER 187
Cdd:PRK10517 160 TATVLRVINDK-----GENGWLEIPIDQLVPGDIIKLAAGDMIPADLRILQARDLFVAQASLTGESLPVEKFATTRQPEH 234

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515719845 188 KrfiplkrmkdyNPLQLENVCFKGTHIVNGTAKAVVVSTGKNTYSGLLHTCCSQT 242
Cdd:PRK10517 235 S-----------NPLECDTLCFMGTNVVSGTAQAVVIATGANTWFGQLAGRVSEQ 278

prokaryotic P-type Ca(2+)-ATPase similar to Synechococcus elongatus sp. strain PCC 7942 PacL and Listeria monocytogenes LMCA1; Ca(2+) transport ATPase is a plasma membrane protein which pumps Ca(2+) ion out of the cytoplasm. This prokaryotic subfamily includes the Ca(2+)-ATPase Synechococcus elongatus PacL, Listeria monocytogenes Ca(2+)-ATPase 1 (LMCA1) which has a low Ca(2+) affinity and a high pH optimum (pH about 9) and may remove Ca(2+) from the microorganism in environmental conditions when e.g. stressed by high Ca(2+) and alkaline pH, and the Bacillus subtilis putative P-type Ca(2+)-transport ATPase encoded by the yloB gene, which is expressed during sporulation. 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 515719845  54 GLSMKEAQKRIHVYGKNELSSKRAI---------FSDVM-----------MKLGE--------------MIPGFAkQRVH 99
Cdd:cd02089    1 GLSEEEAERRLAKYGPNELVEKKKRspwkkfleqFKDFMvivllaaavisGVLGEyvdaiviiaivilnAVLGFV-QEYK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515719845 100 NENQCE------IVTVTVSRvegcttvgmssDSKIMKLPVEELVPGDMVFLSAGDTVPADLRIIYAEDLLVNESMLTGKE 173
Cdd:cd02089   80 AEKALAalkkmsAPTAKVLR-----------DGKKQEIPARELVPGDIVLLEAGDYVPADGRLIESASLRVEESSLTGES 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515719845 174 ANVEKFescyhlerkrfiPLKRMKDYNPL--QLeNVCFKGTHIVNGTAKAVVVSTGKNT 230
Cdd:cd02089  149 EPVEKD------------ADTLLEEDVPLgdRK-NMVFSGTLVTYGRGRAVVTATGMNT 194

sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; SERCA is a transmembrane (Ca2+)-ATPase and a major regulator of Ca(2+) homeostasis and contractility in cardiac and skeletal muscle. It re-sequesters cytoplasmic Ca(2+) to the sarco/endoplasmic reticulum store, thereby also terminating Ca(2+)-induced signaling such as in muscle contraction. Three genes (ATP2A1-3/SERCA1-3) encode SERCA pumps in mammals, further isoforms exist due to alternative splicing of transcripts. The activity of SERCA is regulated by two small membrane proteins called phospholamban and sarcolipin. 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 515719845  38 TRDVKSVFAYFKTTRD-GLSMKEAQKRIHVYGKNELSSKR---------AIFSDVMMK--LGEMIPGFAKQRVhnENQCE 105
Cdd:cd02083    2 SKTVEEVLAYFGVDPTrGLSDEQVKRRREKYGPNELPAEEgkslwelvlEQFDDLLVRilLLAAIISFVLALF--EEGEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515719845 106 IVTvtvSRVEGC---------TTVGMS------------------------SDSKIMKLPVEELVPGDMVFLSAGDTVPA 152
Cdd:cd02083   80 GVT---AFVEPFvillilianAVVGVWqernaekaiealkeyepemakvlrNGKGVQRIRARELVPGDIVEVAVGDKVPA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515719845 153 DLRI--IYAEDLLVNESMLTGKEANVEKFESCYHLERkrfiPLKRMKdynplqlENVCFKGTHIVNGTAKAVVVSTGKNT 230
Cdd:cd02083  157 DIRIieIKSTTLRVDQSILTGESVSVIKHTDVVPDPR----AVNQDK-------KNMLFSGTNVAAGKARGVVVGTGLNT 225

                        250
                 ....*....|...
gi 515719845 231 YSGLLHTCCSQTS 243
Cdd:cd02083  226 EIGKIRDEMAETE 238

E1-E2 ATPase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515719845  125 DSKIMKLPVEELVPGDMVFLSAGDTVPADLRIIYAEDlLVNESMLTGKEANVEKFEscyhlerkrfiplkrmkdynplql 204
Cdd:pfam00122  12 DGTEEEVPADELVPGDIVLLKPGERVPADGRIVEGSA-SVDESLLTGESLPVEKKK------------------------ 66

                          90       100
                  ....*....|....*....|....*..
gi 515719845  205 ENVCFKGTHIVNGTAKAVVVSTGKNTY 231
Cdd:pfam00122  67 GDMVYSGTVVVSGSAKAVVTATGEDTE 93

alpha-subunit of Na(+)/K(+)-ATPases and of gastric H(+)/K(+)-ATPase, similar to the human Na(+)/K(+)-ATPase alpha subunits 1-4; This subfamily includes the alpha subunit of Na(+)/K(+)-ATPase a heteromeric transmembrane protein composed of an alpha- and beta-subunit and an optional third subunit belonging to the FXYD proteins which are more tissue specific regulatory subunits of the enzyme. The alpha-subunit is the catalytic subunit responsible for transport activities of the enzyme. This subfamily includes all four isotopes of the human alpha subunit: (alpha1-alpha4, encoded by the ATP1A1- ATP1A4 genes). Na(+)/K(+)-ATPase functions chiefly as an ion pump, hydrolyzing one molecule of ATP to pump three Na(+) out of the cell in exchange for two K(+)entering the cell per pump cycle. In addition Na(+)/K(+)-ATPase acts as a signal transducer. This subfamily also includes Oreochromis mossambicus (tilapia) Na(+)/K(+)-ATPase alpha 1 and alpha 3 subunits, and gastric H(+)/K(+)-ATPase which exchanges hydronium ion with potassium and is responsible for gastric acid secretion. Gastric H(+)/K(+)-ATPase is an alpha,beta-heterodimeric enzyme. 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 515719845 125 DSKIMKLPVEELVPGDMVFLSAGDTVPADLRIIYAEDLLVNESMLTGkeanvekfEScyhlErkrfiPLKRMKDY---NP 201
Cdd:cd02608  113 DGEKMQINAEELVVGDLVEVKGGDRIPADIRIISAHGCKVDNSSLTG--------ES----E-----PQTRSPEFtheNP 175

                         90       100       110
                 ....*....|....*....|....*....|..
gi 515719845 202 LQLENVCFKGTHIVNGTAKAVVVSTGKNTYSG 233
Cdd:cd02608  176 LETKNIAFFSTNCVEGTARGIVINTGDRTVMG 207

sarco/endoplasmic reticulum calcium-translocating P-type ATPase; This model describes the P-type ATPase responsible for translocating calcium ions across the endoplasmic reticulum membrane of eukaryotes, and is of particular importance in the sarcoplasmic reticulum of skeletal and cardiac muscle in vertebrates. These pumps transfer Ca2+ from the cytoplasm to the lumen of the endoplasmic reticulum. In humans and mice, at least, there are multiple isoforms of the SERCA pump with overlapping but not redundant functions. Defects in SERCA isoforms are associated with diseases in humans. The calcium P-type ATPases have been characterized as Type IIA based on a phylogenetic analysis which distinguishes this group from the Type IIB PMCA calcium pump modelled by TIGR01517. A separate analysis divides Type IIA into sub-types, SERCA and PMR1, the latter of which is modelled by TIGR01522. [Transport and binding proteins, Cations and iron carrying compounds]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515719845  131 LPVEELVPGDMVFLSAGDTVPADLRIIYAEDLLVNESMLTGKEANVEKFESCYHLERKRFiPLKrmkdynplqlENVCFK 210
Cdd:TIGR01116  86 IKAKDLVPGDIVELAVGDKVPADIRVLSLKTLRVDQSILTGESVSVNKHTESVPDERAVN-QDK----------KNMLFS 154

                          90       100
                  ....*....|....*....|....*.
gi 515719845  211 GTHIVNGTAKAVVVSTGKNTYSGLLH 236
Cdd:TIGR01116 155 GTLVVAGKARGVVVRTGMSTEIGKIR 180

uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase transporters of unknown function. The P-type ATPases, are 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. They 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. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd2+, and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515719845  54 GLSMKEAQKRIHVYGKNEL--SSKRAIFSDVMMKLGE------MIPGFAKQRVHNENQCEIVTVTVSRVEGCTTV----- 120
Cdd:cd07538    1 GLTEAEARRRLESGGKNELpqPKKRTLLASILDVLREpmflllLAAALIYFVLGDPREGLILLIFVVVIIAIEVVqewrt 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515719845 121 --------GMSS-------DSKIMKLPVEELVPGDMVFLSAGDTVPADLRIIYAEDLLVNESMLTGKEANVekfescyhl 185
Cdd:cd07538   81 eralealkNLSSpratvirDGRERRIPSRELVPGDLLILGEGERIPADGRLLENDDLGVDESTLTGESVPV--------- 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 515719845 186 eRKRfIPLKRMKDYNPLQLeNVCFKGTHIVNGTAKAVVVSTGKNTYSG 233
Cdd:cd07538  152 -WKR-IDGKAMSAPGGWDK-NFCYAGTLVVRGRGVAKVEATGSRTELG 196

plasma-membrane proton-efflux P-type ATPase; This model describes the plasma membrane proton efflux P-type ATPase found in plants, fungi, protozoa, slime molds and archaea. The best studied representative is from yeast.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515719845   54 GLSMKEAQKRIHVYGKNELSSKRA----IFSDVM-------MKLGEMIPGFAKQRVHNENQCEI--VTVTVSRVEGCTT- 119
Cdd:TIGR01647   1 GLTSAEAKKRLAKYGPNELPEKKVspllKFLGFFwnplswvMEAAAIIAIALENWVDFVIILGLllLNATIGFIEENKAg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515719845  120 -------VGMSSDSKIMK------LPVEELVPGDMVFLSAGDTVPADLRIIYAEDLLVNESMLTGKEANVEKfescyhle 186
Cdd:TIGR01647  81 navealkQSLAPKARVLRdgkwqeIPASELVPGDVVRLKIGDIVPADCRLFEGDYIQVDQAALTGESLPVTK-------- 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 515719845  187 rkrfiplkrmkdynplQLENVCFKGTHIVNGTAKAVVVSTGKNTYSG 233
Cdd:TIGR01647 153 ----------------KTGDIAYSGSTVKQGEAEAVVTATGMNTFFG 183

ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large family of trans-membrane transporters acting on charged substances. The distinguishing feature of the family is the formation of a phosphorylated intermediate (aspartyl-phosphate) during the course of the reaction. Another common name for these enzymes is the E1-E2 ATPases based on the two isolable conformations: E1 (unphosphorylated) and E2 (phosphorylated). Generally, P-type ATPases consist of only a single subunit encompassing the ATPase and ion translocation pathway, however, in the case of the potassium (TIGR01497) and sodium/potassium (TIGR01106) varieties, these functions are split between two subunits. Additional small regulatory or stabilizing subunits may also exist in some forms. P-type ATPases are nearly ubiquitous in life and are found in numerous copies in higher organisms (at least 45 in Arabidopsis thaliana, for instance). Phylogenetic analyses have revealed that the P-type ATPase subfamily is divided up into groups based on substrate specificities and this is represented in the various subfamily and equivalog models that have been made: IA (K+) TIGR01497, IB (heavy metals) TIGR01525, IIA1 (SERCA-type Ca++) TIGR01116, IIA2 (PMR1-type Ca++) TIGR01522, IIB (PMCA-type Ca++) TIGR01517, IIC (Na+/K+, H+/K+ antiporters) TIGR01106, IID (fungal-type Na+ and K+) TIGR01523, IIIA (H+) TIGR01647, IIIB (Mg++) TIGR01524, IV (phospholipid, flippase) TIGR01652 and V (unknown specificity) TIGR01657. The crystal structure of one calcium-pumping ATPase and an analysis of the fold of the catalytic domain of the P-type ATPases have been published. These reveal that the catalytic core of these enzymes is a haloacid dehalogenase(HAD)-type aspartate-nucleophile hydrolase. The location of the ATP-binding loop in between the first and second HAD conserved catalytic motifs defines these enzymes as members of subfamily I of the HAD superfamily (see also TIGR01493, TIGR01509, TIGR01549, TIGR01544 and TIGR01545). Based on these classifications, the P-type ATPase _superfamily_ corresponds to the IC subfamily of the HAD superfamily.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515719845  131 LPVEELVPGDMVFLSAGDTVPADLrIIYAEDLLVNESMLTGkEAN-VEKFescyhlerkrfiplkrmkdynPLQLENVCF 209
Cdd:TIGR01494  47 ISSKDLVPGDVVLVKSGDTVPADG-VLLSGSAFVDESSLTG-ESLpVLKT---------------------ALPDGDAVF 103

                          90       100
                  ....*....|....*....|.
gi 515719845  210 KGTHIVNGTAKAVVVSTGKNT 230
Cdd:TIGR01494 104 AGTINFGGTLIVKVTATGILT 124

uncharacterized subfamily of P-type ATPase transporter, similar to uncharacterized Streptococcus pneumoniae exported protein 7, Exp7; This subfamily contains P-type ATPase transporters of unknown function, similar to Streptococcus pneumoniae Exp7. The P-type ATPases, are 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. They 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. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd(2+), and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515719845 125 DSKIMKLPVEELVPGDMVFLSAGDTVPADLRIIYAEDLLVNESMLTGKEANVEKfescyhlerkrfiplkrmkdynplQL 204
Cdd:cd02609   99 DGQEVKIPPEELVLDDILILKPGEQIPADGEVVEGGGLEVDESLLTGESDLIPK------------------------KA 154

                         90       100
                 ....*....|....*....|....*..
gi 515719845 205 ENVCFKGTHIVNGTAKAVVVSTGKNTY 231
Cdd:cd02609  155 GDKLLSGSFVVSGAAYARVTAVGAESY 181

P-type cation-transporting ATPases, similar to human ATPase type 13A2 (ATP13A2) protein and Saccharomyces cerevisiae Ypk9p; Saccharomyces cerevisiae Yph9p localizes to the yeast vacuole and may play a role in sequestering heavy metal ions, its deletion confers sensitivity for growth for cadmium, manganese, nickel or selenium. Human ATP13A2 (PARK9/CLN12) is a lysosomal transporter with zinc as the possible substrate. Mutation in the ATP13A2 gene has been linked to Parkinson's disease and Kufor-Rakeb syndrome, and to neuronal ceroid lipofuscinoses. ATP13A3/AFURS1 is a candidate gene for oculo auriculo vertebral spectrum (OAVS), being one of nine genes included in a 3q29 microduplication in a patient with OAVS. Mutation in the human ATP13A4 may be involved in a speech-language disorder. This subfamily also includes zebrafish ATP13A2 a lysosome-specific transmembrane ATPase protein of unknown function which plays a crucial role during embryonic development, its deletion is lethal. 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 515719845  96 QRVHNENQCEIVTVTVSRVEGCTTVGMSsdskimklpveELVPGDMVFLSA-GDTVPADlRIIYAEDLLVNESMLTGKEA 174
Cdd:cd07542   76 SKRLREMVHFTCPVRVIRDGEWQTISSS-----------ELVPGDILVIPDnGTLLPCD-AILLSGSCIVNESMLTGESV 143

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515719845 175 NVEKFescyhlerkrfiPLKRMKDYNPLQLEN-------VCFKGTHIV------NGTAKAVVVSTGKNTYSGLL 235
Cdd:cd07542  144 PVTKT------------PLPDESNDSLWSIYSiedhskhTLFCGTKVIqtrayeGKPVLAVVVRTGFNTTKGQL 205

P-type heavy metal-transporting ATPase, similar to Archaeoglobus fulgidus CopB, a Cu(2+)-ATPase; Archaeoglobus fulgidus CopB transports Cu(2+) from the cytoplasm to the exterior of the cell using ATP as energy source, it transports preferentially Cu(2+) over Cu(+), it is activated by Cu(2+) with high affinity and partially by Cu(+) and Ag(+). 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
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515719845 125 DSKIMKLPVEELVPGDMVFLSAGDTVPADLRIIYAEDlLVNESMLTGKEANVEK 178
Cdd:cd07552  138 DGSIEDVPVSELKVGDVVLVRAGEKIPADGTILEGES-SVNESMVTGESKPVEK 190

Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515719845 125 DSKIMKLPVEELVPGDMVFLSAGDTVPADLRIIyAEDLLVNESMLTGkeanvekfEScyhlerkrfIPLKRMKDynplql 204
Cdd:COG2217  220 DGEEVEVPVEELRVGDRVLVRPGERIPVDGVVL-EGESSVDESMLTG--------ES---------LPVEKTPG------ 275

                         90       100
                 ....*....|....*....|....*..
gi 515719845 205 ENVcFKGTHIVNGTAKAVVVSTGKNTY 231
Cdd:COG2217  276 DEV-FAGTINLDGSLRVRVTKVGSDTT 301

P-type cation-transporting ATPases, similar to human cation-transporting ATPase type 13A1 (ATP13A1) and Saccharomyces manganese-transporting ATPase 1 Spf1p; Saccharomyces Spf1p may mediate manganese transport into the endoplasmic reticulum (ER); one consequence of deletion of SPF1 is severe ER stress. This subfamily also includes Arabidopsis thaliana MIA (Male Gametogenesis Impaired Anthers) protein which is highly abundant in the endoplasmic reticulum and small vesicles of developing pollen grains and tapetum cells. The MIA gene functionally complements a mutant in the SPF1 from Saccharomyces cerevisiae. The expression of ATP13A1 has been followed during mouse development, ATP13A1 transcript expression showed an increase as development progressed, with the highest expression at the peak of neurogenesis. 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 515719845 125 DSKIMKLPVEELVPGDMVFLSAG---DTVPADLRIIYAEdLLVNESMLTGkeanvekfESCYHLERkrfiPLKRMKDYNP 201
Cdd:cd07543   93 DGKWVPISSDELLPGDLVSIGRSaedNLVPCDLLLLRGS-CIVNEAMLTG--------ESVPLMKE----PIEDRDPEDV 159

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515719845 202 LQLEN-----VCFKGTHIVNGTAK-------------AVVVSTGKNTYSG-LLHT 237
Cdd:cd07543  160 LDDDGddklhVLFGGTKVVQHTPPgkgglkppdggclAYVLRTGFETSQGkLLRT 214

P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. These ATPases include mammalian copper-transporting ATPases, ATP7A and ATP7B, Bacillus subtilis CadA which transports cadmium, zinc and cobalt out of the cell, Bacillus subtilis ZosA/PfeT which transports copper, and perhaps also zinc and ferrous iron, Archaeoglobus fulgidus CopA and CopB, Staphylococcus aureus plasmid pI258 CadA, a cadmium-efflux ATPase, and Escherichia coli ZntA which is selective for Pb(2+), Zn(2+), and Cd(2+). The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This family 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 515719845 130 KLPVEELVPGDMVFLSAGDTVPADlRIIYAEDLLVNESMLTGkeanvekfEScyhlerkrfIPLKRMKDynplqlENVcF 209
Cdd:cd02079  137 EVPVDDLKVGDVVLVKPGERIPVD-GVVVSGESSVDESSLTG--------ES---------LPVEKGAG------DTV-F 191

                         90       100
                 ....*....|....*....|.
gi 515719845 210 KGTHIVNGTAKAVVVSTGKNT 230
Cdd:cd02079  192 AGTINLNGPLTIEVTKTGEDT 212

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
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515719845 125 DSKIMKLPVEELVPGDMVFLSAGDTVPADLRIIYAEDLLvNESMLTGKEANVEKF 179
Cdd:cd07544  117 GGQLEEVPVEEVTVGDRLLVRPGEVVPVDGEVVSGTATL-DESSLTGESKPVSKR 170

Rhizobium meliloti FixI and related proteins; belongs to P-type heavy metal-transporting ATPase subfamily; FixI may be a pump of a specific cation involved in symbiotic nitrogen fixation. The Rhizobium fixI gene is part of an operon conserved among rhizobia, fixGHIS. FixG, FixH, FixI, and FixS may participate in a membrane-bound complex coupling the FixI cation pump with a redox process catalyzed by FixG, an iron-sulfur protein. 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
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515719845 125 DSKIMKLPVEELVPGDMVFLSAGDTVPADLRIIYAEDLLvNESMLTGKEANVE 177
Cdd:cd02092  134 DGSREYVPVAEIRPGDRVLVAAGERIPVDGTVVSGTSEL-DRSLLTGESAPVT 185

P-type cation-transporting ATPases, similar to human ATPase type 13A1-A4 (ATP13A1-A4) proteins and Saccharomyces cerevisiae Ypk9p and Spf1p; Saccharomyces cerevisiae Yph9p localizes to the yeast vacuole and may play a role in sequestering heavy metal ions, its deletion confers sensitivity for growth for cadmium, manganese, nickel or selenium. Saccharomyces 1 Spf1p may mediate manganese transport into the endoplasmic reticulum. Human ATP13A2 (PARK9/CLN12) is a lysosomal transporter with zinc as the possible substrate. Mutation in the ATP13A2 gene has been linked to Parkinson's disease and Kufor-Rakeb syndrome, and to neuronal ceroid lipofuscinoses. ATP13A3/AFURS1 is a candidate gene for oculo auriculo vertebral spectrum (OAVS), being one of nine genes included in a 3q29 microduplication in a patient with OAVS. Mutation in the human ATP13A4 may be involved in a speech-language disorder. The expression of ATP13A1 has been followed during mouse development, ATP13A1 transcript expression showed an increase as development progressed, with the highest expression at the peak of neurogenesis. 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 515719845 124 SDSKIMKLPVEELVPGD-MVFLSAGDTVPADLRIIYAEdLLVNESMLTGKEANVEKFE-SCYHLERKRFIPLKRMKdynp 201
Cdd:cd02082   93 HGYQEITIASNMIVPGDiVLIKRREVTLPCDCVLLEGS-CIVTEAMLTGESVPIGKCQiPTDSHDDVLFKYESSKS---- 167

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 515719845 202 lqleNVCFKGTHIV------NGTAKAVVVSTGKNTYSGLL 235
Cdd:cd02082  168 ----HTLFQGTQVMqiippeDDILKAIVVRTGFGTSKGQL 203