copper-(or silver)-translocating P-type ATPase; This model describes the P-type ATPase primarily responsible for translocating copper ions accross biological membranes. These transporters are found in prokaryotes and eukaryotes. This model encompasses those species which pump copper ions out of cells or organelles (efflux pumps such as CopA of Escherichia coli) as well as those which pump the ion into cells or organelles either for the purpose of supporting life in extremely low-copper environments (for example CopA of Enterococcus hirae) or for the specific delivery of copper to a biological complex for which it is a necessary component (for example FixI of Bradyrhizobium japonicum, or CtaA and PacS of Synechocystis). The substrate specificity of these transporters may, to a varying degree, include silver ions (for example, CopA from Archaeoglobus fulgidus). Copper transporters from this family are well known as the genes which are mutated in two human disorders of copper metabolism, Wilson's and Menkes' diseases. The sequences contributing to the seed of this model are all experimentally characterized. The copper P-type ATPases have been characterized as Type IB based on a phylogenetic analysis which combines the copper-translocating ATPases with the cadmium-translocating species. This model and that describing the cadmium-ATPases (TIGR01512) are well separated, and thus we further type the copper-ATPases as IB1 (and the cadmium-ATPases as IB2). Several sequences which have not been characterized experimentally fall just below the cutoffs for both of these models (SP|Q9CCL1 from Mycobacterium leprae, GP|13816263 from Sulfolobus solfataricus, OMNI|NTL01CJ01098 from Campylobacter jejuni, OMNI|NTL01HS01687 from Halobacterium sp., GP|6899169 from Ureaplasma urealyticum and OMNI|HP1503 from Helicobacter pylori). Accession PIR|A29576 from Enterococcus faecalis scores very high against this model, but yet is annotated as an "H+/K+ exchanging ATPase". BLAST of this sequence does not hit anything else annotated in this way. This error may come from the characterization paper published in 1987. Accession GP|7415611 from Saccharomyces cerevisiae appears to be mis-annotated as a cadmium resistance protein. Accession OMNI|NTL01HS00542 from Halobacterium which scores above trusted for this model is annotated as "molybdenum-binding protein" although no evidence can be found for this classification. [Cellular processes, Detoxification, Transport and binding proteins, Cations and iron carrying compounds]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KIJ_A          6 SEALAKLISLQATEATIVTLDSDnillsEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKP 85
Cdd:TIGR01511  79 SDALSKLAKLQPSTATLLTKDGS-----IEEVPVALLQPGDIVKVLPGEKIPVDGTVIEGESEVDESLVTGESLPVPKKV 153

                          90       100       110
                  ....*....|....*....|....*....|....*....
2KIJ_A         86 GSTVIAGSINQNGSLLICATHVGADTTLSQIVKLVEEAQ 124
Cdd:TIGR01511 154 GDPVIAGTVNGTGSLVVRATATGEDTTLAQIVRLVRQAQ 192

E1-E2 ATPase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KIJ_A         33 SEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPGSTVIAGSINQNGSLLICATHVGADTT 112
Cdd:pfam00122  14 TEEEVPADELVPGDIVLLKPGERVPADGRIVEGSASVDESLLTGESLPVEKKKGDMVYSGTVVVSGSAKAVVTATGEDTE 93

                          90
                  ....*....|..
2KIJ_A        113 LSQIVKLVEEAQ 124
Cdd:pfam00122  94 LGRIARLVEEAK 105

copper-(or silver)-translocating P-type ATPase; This model describes the P-type ATPase primarily responsible for translocating copper ions accross biological membranes. These transporters are found in prokaryotes and eukaryotes. This model encompasses those species which pump copper ions out of cells or organelles (efflux pumps such as CopA of Escherichia coli) as well as those which pump the ion into cells or organelles either for the purpose of supporting life in extremely low-copper environments (for example CopA of Enterococcus hirae) or for the specific delivery of copper to a biological complex for which it is a necessary component (for example FixI of Bradyrhizobium japonicum, or CtaA and PacS of Synechocystis). The substrate specificity of these transporters may, to a varying degree, include silver ions (for example, CopA from Archaeoglobus fulgidus). Copper transporters from this family are well known as the genes which are mutated in two human disorders of copper metabolism, Wilson's and Menkes' diseases. The sequences contributing to the seed of this model are all experimentally characterized. The copper P-type ATPases have been characterized as Type IB based on a phylogenetic analysis which combines the copper-translocating ATPases with the cadmium-translocating species. This model and that describing the cadmium-ATPases (TIGR01512) are well separated, and thus we further type the copper-ATPases as IB1 (and the cadmium-ATPases as IB2). Several sequences which have not been characterized experimentally fall just below the cutoffs for both of these models (SP|Q9CCL1 from Mycobacterium leprae, GP|13816263 from Sulfolobus solfataricus, OMNI|NTL01CJ01098 from Campylobacter jejuni, OMNI|NTL01HS01687 from Halobacterium sp., GP|6899169 from Ureaplasma urealyticum and OMNI|HP1503 from Helicobacter pylori). Accession PIR|A29576 from Enterococcus faecalis scores very high against this model, but yet is annotated as an "H+/K+ exchanging ATPase". BLAST of this sequence does not hit anything else annotated in this way. This error may come from the characterization paper published in 1987. Accession GP|7415611 from Saccharomyces cerevisiae appears to be mis-annotated as a cadmium resistance protein. Accession OMNI|NTL01HS00542 from Halobacterium which scores above trusted for this model is annotated as "molybdenum-binding protein" although no evidence can be found for this classification. [Cellular processes, Detoxification, Transport and binding proteins, Cations and iron carrying compounds]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KIJ_A          6 SEALAKLISLQATEATIVTLDSDnillsEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKP 85
Cdd:TIGR01511  79 SDALSKLAKLQPSTATLLTKDGS-----IEEVPVALLQPGDIVKVLPGEKIPVDGTVIEGESEVDESLVTGESLPVPKKV 153

                          90       100       110
                  ....*....|....*....|....*....|....*....
2KIJ_A         86 GSTVIAGSINQNGSLLICATHVGADTTLSQIVKLVEEAQ 124
Cdd:TIGR01511 154 GDPVIAGTVNGTGSLVVRATATGEDTTLAQIVRLVRQAQ 192

heavy metal translocating P-type ATPase; This model encompasses two equivalog models for the copper and cadmium-type heavy metal transporting P-type ATPases (TIGR01511 and TIGR01512) as well as those species which score ambiguously between both models. For more comments and references, see the files on TIGR01511 and 01512.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KIJ_A          6 SEALAKLISLQATEATIVTLDsdnilLSEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKP 85
Cdd:TIGR01525  43 SDALSALLALAPSTARVLQGD-----GSEEEVPVEELQVGDIVIVRPGERIPVDGVVISGESEVDESALTGESMPVEKKE 117

                          90       100       110
                  ....*....|....*....|....*....|....*....
2KIJ_A         86 GSTVIAGSINQNGSLLICATHVGADTTLSQIVKLVEEAQ 124
Cdd:TIGR01525 118 GDEVFAGTINGDGSLTIRVTKLGEDSTLAQIVELVEEAQ 156

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        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KIJ_A        6 SEALAKLISLQATEATIVTLDSdnillsEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKP 85
Cdd:cd07552 119 GDALKKLAELLPKTAHLVTDGS------IEDVPVSELKVGDVVLVRAGEKIPADGTILEGESSVNESMVTGESKPVEKKP 192

                        90       100       110
                ....*....|....*....|....*....|....*....
2KIJ_A       86 GSTVIAGSINQNGSLLICATHVGADTTLSQIVKLVEEAQ 124
Cdd:cd07552 193 GDEVIGGSVNGNGTLEVKVTKTGEDSYLSQVMELVAQAQ 231

heavy metal-(Cd/Co/Hg/Pb/Zn)-translocating P-type ATPase; This model describes the P-type ATPase primarily responsible for translocating cadmium ions (and other closely-related divalent heavy metals such as cobalt, mercury, lead and zinc) across biological membranes. These transporters are found in prokaryotes and plants. Experimentally characterized members of the seed alignment include: SP|P37617 from E. coli, SP|Q10866 from Mycobacterium tuberculosis and SP|Q59998 from Synechocystis PCC6803. The cadmium P-type ATPases have been characterized as Type IB based on a phylogenetic analysis which combines the copper-translocating ATPases with the cadmium-translocating species. This model and that describing the copper-ATPases (TIGR01511) are well separated, and thus we further type the copper-ATPases as IB1 and the cadmium-ATPases as IB2. Several sequences which have not been characterized experimentally fall just below trusted cutoff for both of these models (SP|Q9CCL1 from Mycobacterium leprae, GP|13816263 from Sulfolobus solfataricus, OMNI|NTL01CJ01098 from Campylobacter jejuni, OMNI|NTL01HS01687 from Halobacterium sp., GP|6899169 from Ureaplasma urealyticum and OMNI|HP1503 from Helicobacter pylori). [Transport and binding proteins, Cations and iron carrying compounds]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KIJ_A          6 SEALAKLISLQATEATIVTLDSdnillsEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKP 85
Cdd:TIGR01512  43 RRALKALMELAPDTARRLQGDS------LEEVAVEELKVGDVVVVKPGERVPVDGEVLSGTSSVDESALTGESVPVEKAP 116

                          90       100       110
                  ....*....|....*....|....*....|....*....
2KIJ_A         86 GSTVIAGSINQNGSLLICATHVGADTTLSQIVKLVEEAQ 124
Cdd:TIGR01512 117 GDEVFAGAINLDGVLTIEVTKLPADSTIAKIVNLVEEAQ 155

P-type heavy metal-transporting ATPase, similar to Staphylococcus aureus plasmid pI258 CadA, a cadmium-efflux ATPase; CadA from gram-positive Staphylococcus aureus plasmid pI258 is required for full Cd(2+) and Zn(2+) resistance. This subfamily also includes CadA, from the gram-negative bacilli, Stenotrophomonas maltophilia D457R, which is a cadmium efflux pump acquired as part of a cluster of antibiotic and heavy metal resistance genes from gram-positive bacteria. 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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KIJ_A       34 EEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPGSTVIAGSINQNGSLLICATHVGADTTL 113
Cdd:cd07545 106 EREVPVAEVAVGDRMIVRPGERIAMDGIIVRGESSVNQAAITGESLPVEKGVGDEVFAGTLNGEGALEVRVTKPAEDSTI 185

                        90
                ....*....|.
2KIJ_A      114 SQIVKLVEEAQ 124
Cdd:cd07545 186 ARIIHLVEEAQ 196

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        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KIJ_A        8 ALAKLISLQATEATIVTLDSdnillSEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPGS 87
Cdd:cd02092 116 AAEELAALEARGAQRLQADG-----SREYVPVAEIRPGDRVLVAAGERIPVDGTVVSGTSELDRSLLTGESAPVTVAPGD 190

                        90       100       110
                ....*....|....*....|....*....|....*.
2KIJ_A       88 TVIAGSINQNGSLLICATHVGADTTLSQIVKLVEEA 123
Cdd:cd02092 191 LVQAGAMNLSGPLRLRATAAGDDTLLAEIARLMEAA 226

P-type heavy metal-transporting ATPase, similar to Escherichia coli ZntA which is selective for Pb(2+), Zn(2+), and Cd(2+); Escherichia coli ZntA mediates resistance to toxic levels of selected divalent metal ions. ZntA has the highest selectivity for Pb(2+), followed by Zn(2+) and Cd(2+); it also shows low levels of activity with Cu(2+), Ni(2+), and Co(2+). It is upregulated by the transcription factor ZntR at high zinc concentrations. 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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KIJ_A       35 EQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPGSTVIAGSINQNGSLLICATHVGADTTLS 114
Cdd:cd07546 110 REVPADSLRPGDVIEVAPGGRLPADGELLSGFASFDESALTGESIPVEKAAGDKVFAGSINVDGVLRIRVTSAPGDNAID 189

                        90
                ....*....|
2KIJ_A      115 QIVKLVEEAQ 124
Cdd:cd07546 190 RILHLIEEAE 199

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KIJ_A       35 EQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPGSTVIAGSINQNGSLLICATHVGADTTLS 114
Cdd:cd07544 121 EEVPVEEVTVGDRLLVRPGEVVPVDGEVVSGTATLDESSLTGESKPVSKRPGDRVMSGAVNGDSALTMVATKLAADSQYA 200

                        90
                ....*....|
2KIJ_A      115 QIVKLVEEAQ 124
Cdd:cd07544 201 GIVRLVKEAQ 210

Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KIJ_A        7 EALAKLISLQAT---EATIVTLDSDnillseeqvdvELVqRGDIIKVVPGGKFPVDGRVIEGHSM-VDESLITGEAMPVA 82
Cdd:COG0474 110 EALKKLLAPTARvlrDGKWVEIPAE-----------ELV-PGDIVLLEAGDRVPADLRLLEAKDLqVDESALTGESVPVE 177

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
2KIJ_A       83 KKP------------------GSTVIAGSinqnGSLLICAThvGADTTLSQIVKLVEEAQ 124
Cdd:COG0474 178 KSAdplpedaplgdrgnmvfmGTLVTSGR----GTAVVVAT--GMNTEFGKIAKLLQEAE 231

zinc/cadmium/mercury/lead-transporting ATPase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KIJ_A        35 EQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPGSTVIAGSINQNGSLLICATHVGADTTLS 114
Cdd:PRK11033 254 EEVAIADLRPGDVIEVAAGGRLPADGKLLSPFASFDESALTGESIPVERATGEKVPAGATSVDRLVTLEVLSEPGASAID 333

                         90
                 ....*....|
2KIJ_A       115 QIVKLVEEAQ 124
Cdd:PRK11033 334 RILHLIEEAE 343

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KIJ_A       19 EATIVTLDSDNIllSEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPGSTVIAGSINQNG 98
Cdd:cd07553 125 EAPITEIETGSG--SRIKTRADQIKSGDVYLVASGQRVPVDGKLLSEQASIDMSWLTGESLPRIVERGDKVPAGTSLENQ 202

                        90       100
                ....*....|....*....|....*
2KIJ_A       99 SLLICATHVGADTTLSQIVKLVEEA 123
Cdd:cd07553 203 AFEIRVEHSLAESWSGSILQKVEAQ 227

plant and fungal plasma membrane H(+)-ATPases, and related bacterial and archaeal putative H(+)-ATPases; This subfamily includes eukaryotic plasma membrane H(+)-ATPase which transports H(+) from the cytosol to the extracellular space, thus energizing the plasma membrane for the uptake of ions and nutrients, and is expressed in plants and fungi. This H(+)-ATPase consists of four domains: 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. This subfamily also includes the putative P-type H(+)-ATPase, MJ1226p of the anaerobic hyperthermophilic archaea Methanococcus jannaschii. 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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KIJ_A       36 QVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSM-VDESLITGEAMPVAKKPGSTVIAGSINQNGSLLICATHVGADTTLS 114
Cdd:cd02076 104 EIDAKELVPGDIVSLKIGDIVPADARLLTGDALqVDQSALTGESLPVTKHPGDEAYSGSIVKQGEMLAVVTATGSNTFFG 183

                        90
                ....*....|
2KIJ_A      115 QIVKLVEEAQ 124
Cdd:cd02076 184 KTAALVASAE 193

plasma-membrane calcium-translocating P-type ATPase; This model describes the P-type ATPase responsible for translocating calcium ions across the plasma membrane of eukaryotes, out of the cell. In some organisms, this type of pump may also be found in vacuolar membranes. In humans and mice, at least, there are multiple isoforms of the PMCA pump with overlapping but not redundant functions. Accordingly, there are no human diseases linked to PMCA defects, although alterations of PMCA function do elicit physiological effects. The calcium P-type ATPases have been characterized as Type IIB based on a phylogenetic analysis which distinguishes this group from the Type IIA SERCA calcium pump. A separate analysis divides Type IIA into sub-types (SERCA and PMR1) which are represented by two corresponding models (TIGR01116 and TIGR01522). This model is well separated from those.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KIJ_A         33 SEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMV-DESLITGEAMPVAKKP--GSTVIAGSINQNGSLLICATHVGA 109
Cdd:TIGR01517 178 QEQQISIHDIVVGDIVSLSTGDVVPADGVFISGLSLEiDESSITGESDPIKKGPvqDPFLLSGTVVNEGSGRMLVTAVGV 257

                          90
                  ....*....|....
2KIJ_A        110 DTTLSQIVKLVEEA 123
Cdd:TIGR01517 258 NSFGGKLMMELRQA 271

P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, and Synechocystis sp. PCC 6803 PMA1, a putative Ca(2+)-ATPase; This subfamily includes the P-type Na(+)-ATPase of an alkaliphilic bacterium Exiguobacterium aurantiacum Mna and cyanobacterium Synechocystis sp. PCC 6803 PMA1, a cation-transporting ATPase which may translocate calcium. 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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KIJ_A        7 EALAKLISLQATEATiVTLDSDNILLSEEqvdvELVQrGDIIKVVPGGKFPVDGRVIEGHSM-VDESLITGEAMPVAKK- 84
Cdd:cd02080  82 KALAAIKNMLSPEAT-VLRDGKKLTIDAE----ELVP-GDIVLLEAGDKVPADLRLIEARNLqIDESALTGESVPVEKQe 155

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
2KIJ_A       85 -----------------PGSTVIAGSinqnGSLLICAThvGADTTLSQIVKLVEEAQ 124
Cdd:cd02080 156 gpleedtplgdrknmaySGTLVTAGS----ATGVVVAT--GADTEIGRINQLLAEVE 206

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KIJ_A        2 SFTMSEALAKLISLQATeatiVTLDSDNillsEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSM-VDESLITGEAMP 80
Cdd:cd02077  88 SLKAAEKLKKMVKNTAT----VIRDGSK----YMEIPIDELVPGDIVYLSAGDMIPADVRIIQSKDLfVSQSSLTGESEP 159

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
2KIJ_A       81 VAKKP-------------------GSTVIAGSinqnGSLLICAThvGADTTLSQIVKLVEE 122
Cdd:cd02077 160 VEKHAtakktkdesilelenicfmGTNVVSGS----ALAVVIAT--GNDTYFGSIAKSITE 214

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
2KIJ_A        8 ALAKLISLQATEATIVTLDSDNILLSEEqvdvELVQrGDIIKVVPGGKFPVDGRVIEGHSM---VDESLITGEAMPVAK 83
Cdd:cd02083 111 AIEALKEYEPEMAKVLRNGKGVQRIRAR----ELVP-GDIVEVAVGDKVPADIRIIEIKSTtlrVDQSILTGESVSVIK 184

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KIJ_A        7 EALAKLISLQATeatiVTLDSDNIllseeQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSM-VDESLITGEAMPVAKKP 85
Cdd:cd02608  98 DSFKNMVPQQAL----VIRDGEKM-----QINAEELVVGDLVEVKGGDRIPADIRIISAHGCkVDNSSLTGESEPQTRSP 168

                ...
2KIJ_A       86 GST 88
Cdd:cd02608 169 EFT 171

potassium and/or sodium efflux P-type ATPase, fungal-type; Initially described as a calcium efflux ATPase, more recent work has shown that the S. pombe CTA3 gene is in fact a potassium ion efflux pump. This model describes the clade of fungal P-type ATPases responsible for potassium and sodium efflux. The degree to which these pumps show preference for sodium or potassium varies. This group of ATPases has been classified by phylogentic analysis as type IID. The Leishmania sequence (GP|3192903), which falls between trusted and noise in this model, may very well turn out to be an active potassium pump.

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                   ....*....|....*....|....*....|....*....|....*....|
2KIJ_A          35 EQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSM-VDESLITGEAMPVAK 83
Cdd:TIGR01523  129 DAIDSHDLVPGDICLLKTGDTIPADLRLIETKNFdTDEALLTGESLPVIK 178

magnesium-transporting P-type ATPase MgtA;

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KIJ_A         6 SEALAKLISLQATeativTLDSDNILLSEEQVDV---ELVQrGDIIKVVPGGKFPVDGRVIEGHSM-VDESLITGEAMPV 81
Cdd:PRK10517 150 ADALKAMVSNTAT-----VLRVINDKGENGWLEIpidQLVP-GDIIKLAAGDMIPADLRILQARDLfVAQASLTGESLPV 223

                 ....*.
2KIJ_A        82 AKKPGS 87
Cdd:PRK10517 224 EKFATT 229