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Conserved domains on  [gi|2075460303|gb|QYF64620|]
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Sodium-potassium ATPase alpha subunit, partial [Challengerosergia talismani]

Protein Classification

HAD family hydrolase( domain architecture ID 229399)

HAD (haloacid dehalogenase) family hydrolase; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

EC:  3.6.3.-
Gene Ontology:  GO:0005524|GO:0016887|GO:0005215

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
 1-187 3.99e-133

Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.


The actual alignment was detected with superfamily member cd02608:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 905  Bit Score: 394.41  E-value: 3.99e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303   1 GWKALSRIAALCNRAEFKTGMENVSILKREVNGDASEAALLKCVELAVGDCKGWRSRNKKVSEVPFNSTNKYQVSIHETE 80
Cdd:cd02608   356 TWLALSRIAGLCNRAEFKAGQENVPILKRDVNGDASESALLKCIELSCGSVMEMRERNPKVAEIPFNSTNKYQLSIHENE 435

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303  81 DKNDPRYLLVMKGAPERILERCSTIYINGEEKPLDEEMKEAFNNAYLELGGLGERVLGFCDYMLPTDKYPLGYPFDADNV 160
Cdd:cd02608   436 DPGDPRYLLVMKGAPERILDRCSTILINGKEQPLDEEMKEAFQNAYLELGGLGERVLGFCHLYLPDDKFPEGFKFDTDEV 515

                         170       180
                  ....*....|....*....|....*..
gi 2075460303 161 NFPVHGLRFVGLMSMIDPPRAAVPDAV 187
Cdd:cd02608   516 NFPTENLCFVGLMSMIDPPRAAVPDAV 542
 
Name Accession Description Interval E-value
P-type_ATPase_Na-K_like cd02608
alpha-subunit of Na(+)/K(+)-ATPases and of gastric H(+)/K(+)-ATPase, similar to the human Na(+) ...
 1-187 3.99e-133

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.


Pssm-ID: 319794 [Multi-domain]  Cd Length: 905  Bit Score: 394.41  E-value: 3.99e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303   1 GWKALSRIAALCNRAEFKTGMENVSILKREVNGDASEAALLKCVELAVGDCKGWRSRNKKVSEVPFNSTNKYQVSIHETE 80
Cdd:cd02608   356 TWLALSRIAGLCNRAEFKAGQENVPILKRDVNGDASESALLKCIELSCGSVMEMRERNPKVAEIPFNSTNKYQLSIHENE 435

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303  81 DKNDPRYLLVMKGAPERILERCSTIYINGEEKPLDEEMKEAFNNAYLELGGLGERVLGFCDYMLPTDKYPLGYPFDADNV 160
Cdd:cd02608   436 DPGDPRYLLVMKGAPERILDRCSTILINGKEQPLDEEMKEAFQNAYLELGGLGERVLGFCHLYLPDDKFPEGFKFDTDEV 515

                         170       180
                  ....*....|....*....|....*..
gi 2075460303 161 NFPVHGLRFVGLMSMIDPPRAAVPDAV 187
Cdd:cd02608   516 NFPTENLCFVGLMSMIDPPRAAVPDAV 542
ATPase-IIC_X-K TIGR01106
sodium or proton efflux -- potassium uptake antiporter, P-type ATPase, alpha subunit; This ...
 1-187 6.16e-121

sodium or proton efflux -- potassium uptake antiporter, P-type ATPase, alpha subunit; This model describes the P-type ATPases responsible for the exchange of either protons or sodium ions for potassium ions across the plasma membranes of eukaryotes. Unlike most other P-type ATPases, members of this subfamily require a beta subunit for activity. This model encompasses eukaryotes and consists of two functional types, a Na/K antiporter found widely distributed in eukaryotes and a H/K antiporter found only in vertebrates. The Na+ or H+/K+ antiporter P-type ATPases have been characterized as Type IIC based on a published phylogenetic analysis. Sequences from Blastocladiella emersonii (GP|6636502, GP|6636502 and PIR|T43025), C. elegans (GP|2315419, GP|6671808 and PIR|T31763) and Drosophila melanogaster (GP|7291424) score below trusted cutoff, apparently due to long branch length (excessive divergence from the last common ancestor) as evidenced by a phylogenetic tree. Experimental evidence is needed to determine whether these sequences represent ATPases with conserved function. Aside from fragments, other sequences between trusted and noise appear to be bacterial ATPases of unclear lineage, but most likely calcium pumps. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 273445 [Multi-domain]  Cd Length: 997  Bit Score: 364.88  E-value: 6.16e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303   1 GWKALSRIAALCNRAEFKTGMENVSILKREVNGDASEAALLKCVELAVGDCKGWRSRNKKVSEVPFNSTNKYQVSIHETE 80
Cdd:TIGR01106 391 TWLALSRIAGLCNRAVFKAGQENVPILKRAVAGDASESALLKCIELCLGSVMEMRERNPKVVEIPFNSTNKYQLSIHENE 470

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303  81 DKNDPRYLLVMKGAPERILERCSTIYINGEEKPLDEEMKEAFNNAYLELGGLGERVLGFCDYMLPTDKYPLGYPFDADNV 160
Cdd:TIGR01106 471 DPRDPRHLLVMKGAPERILERCSSILIHGKEQPLDEELKEAFQNAYLELGGLGERVLGFCHLYLPDEQFPEGFQFDTDDV 550

                         170       180
                  ....*....|....*....|....*..
gi 2075460303 161 NFPVHGLRFVGLMSMIDPPRAAVPDAV 187
Cdd:TIGR01106 551 NFPTDNLCFVGLISMIDPPRAAVPDAV 577
MgtA COG0474
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism];
3-187 1.21e-39

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


Pssm-ID: 440242 [Multi-domain]  Cd Length: 874  Bit Score: 142.94  E-value: 1.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303   3 KALSRIAALCNRAEfktgmenvsILKREVNGDASEAALLKCVELAVGDCKGWRSRNKKVSEVPFNSTNKYQVSIHETEDK 82
Cdd:COG0474   362 EELLRAAALCSDAQ---------LEEETGLGDPTEGALLVAAAKAGLDVEELRKEYPRVDEIPFDSERKRMSTVHEDPDG 432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303  83 ndpRYLLVMKGAPERILERCSTIYINGEEKPLDEEMKEAFNNAYLELGGLGERVLGFCdyMLPTDKYPLGYPFDADNvnf 162
Cdd:COG0474   433 ---KRLLIVKGAPEVVLALCTRVLTGGGVVPLTEEDRAEILEAVEELAAQGLRVLAVA--YKELPADPELDSEDDES--- 504

                         170       180
                  ....*....|....*....|....*
gi 2075460303 163 pvhGLRFVGLMSMIDPPRAAVPDAV 187
Cdd:COG0474   505 ---DLTFLGLVGMIDPPRPEAKEAI 526
Cation_ATPase pfam13246
Cation transport ATPase (P-type); This domain is found in cation transport ATPases, including ...
 10-105 2.71e-37

Cation transport ATPase (P-type); This domain is found in cation transport ATPases, including phospholipid-transporting ATPases, calcium-transporting ATPases, and sodium-potassium ATPases.


Pssm-ID: 463817 [Multi-domain]  Cd Length: 91  Bit Score: 124.25  E-value: 2.71e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303  10 ALCNRAEFKtgmENVSILKREVNGDASEAALLKCVELAVGDCKGWRSRNKKVSEVPFNSTNKYQVSIHETEDknDPRYLL 89
Cdd:pfam13246   1 ALCNSAAFD---ENEEKGKWEIVGDPTESALLVFAEKMGIDVEELRKDYPRVAEIPFNSDRKRMSTVHKLPD--DGKYRL 75

                          90
                  ....*....|....*.
gi 2075460303  90 VMKGAPERILERCSTI 105
Cdd:pfam13246  76 FVKGAPEIILDRCTTI 91
PRK10517 PRK10517
magnesium-transporting P-type ATPase MgtA;
39-180 1.31e-09

magnesium-transporting P-type ATPase MgtA;


Pssm-ID: 236705 [Multi-domain]  Cd Length: 902  Bit Score: 56.62  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303  39 ALLKCVELAVGDCKGwrSRNKKVSEVPFNSTNK-YQVSIHETEDKndprYLLVMKGAPERILERCSTIYINGEEKPLDEE 117
Cdd:PRK10517  424 AVLEGVDEESARSLA--SRWQKIDEIPFDFERRrMSVVVAENTEH----HQLICKGALEEILNVCSQVRHNGEIVPLDDI 497

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2075460303 118 MKEAFNNAYLELGGLGERVLGFCDYMLPTDKYPLGYPFDADnvnfpvhgLRFVGLMSMIDPPR 180
Cdd:PRK10517  498 MLRRIKRVTDTLNRQGLRVVAVATKYLPAREGDYQRADESD--------LILEGYIAFLDPPK 552
 
Name Accession Description Interval E-value
P-type_ATPase_Na-K_like cd02608
alpha-subunit of Na(+)/K(+)-ATPases and of gastric H(+)/K(+)-ATPase, similar to the human Na(+) ...
 1-187 3.99e-133

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.


Pssm-ID: 319794 [Multi-domain]  Cd Length: 905  Bit Score: 394.41  E-value: 3.99e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303   1 GWKALSRIAALCNRAEFKTGMENVSILKREVNGDASEAALLKCVELAVGDCKGWRSRNKKVSEVPFNSTNKYQVSIHETE 80
Cdd:cd02608   356 TWLALSRIAGLCNRAEFKAGQENVPILKRDVNGDASESALLKCIELSCGSVMEMRERNPKVAEIPFNSTNKYQLSIHENE 435

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303  81 DKNDPRYLLVMKGAPERILERCSTIYINGEEKPLDEEMKEAFNNAYLELGGLGERVLGFCDYMLPTDKYPLGYPFDADNV 160
Cdd:cd02608   436 DPGDPRYLLVMKGAPERILDRCSTILINGKEQPLDEEMKEAFQNAYLELGGLGERVLGFCHLYLPDDKFPEGFKFDTDEV 515

                         170       180
                  ....*....|....*....|....*..
gi 2075460303 161 NFPVHGLRFVGLMSMIDPPRAAVPDAV 187
Cdd:cd02608   516 NFPTENLCFVGLMSMIDPPRAAVPDAV 542
ATPase-IIC_X-K TIGR01106
sodium or proton efflux -- potassium uptake antiporter, P-type ATPase, alpha subunit; This ...
 1-187 6.16e-121

sodium or proton efflux -- potassium uptake antiporter, P-type ATPase, alpha subunit; This model describes the P-type ATPases responsible for the exchange of either protons or sodium ions for potassium ions across the plasma membranes of eukaryotes. Unlike most other P-type ATPases, members of this subfamily require a beta subunit for activity. This model encompasses eukaryotes and consists of two functional types, a Na/K antiporter found widely distributed in eukaryotes and a H/K antiporter found only in vertebrates. The Na+ or H+/K+ antiporter P-type ATPases have been characterized as Type IIC based on a published phylogenetic analysis. Sequences from Blastocladiella emersonii (GP|6636502, GP|6636502 and PIR|T43025), C. elegans (GP|2315419, GP|6671808 and PIR|T31763) and Drosophila melanogaster (GP|7291424) score below trusted cutoff, apparently due to long branch length (excessive divergence from the last common ancestor) as evidenced by a phylogenetic tree. Experimental evidence is needed to determine whether these sequences represent ATPases with conserved function. Aside from fragments, other sequences between trusted and noise appear to be bacterial ATPases of unclear lineage, but most likely calcium pumps. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 273445 [Multi-domain]  Cd Length: 997  Bit Score: 364.88  E-value: 6.16e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303   1 GWKALSRIAALCNRAEFKTGMENVSILKREVNGDASEAALLKCVELAVGDCKGWRSRNKKVSEVPFNSTNKYQVSIHETE 80
Cdd:TIGR01106 391 TWLALSRIAGLCNRAVFKAGQENVPILKRAVAGDASESALLKCIELCLGSVMEMRERNPKVVEIPFNSTNKYQLSIHENE 470

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303  81 DKNDPRYLLVMKGAPERILERCSTIYINGEEKPLDEEMKEAFNNAYLELGGLGERVLGFCDYMLPTDKYPLGYPFDADNV 160
Cdd:TIGR01106 471 DPRDPRHLLVMKGAPERILERCSSILIHGKEQPLDEELKEAFQNAYLELGGLGERVLGFCHLYLPDEQFPEGFQFDTDDV 550

                         170       180
                  ....*....|....*....|....*..
gi 2075460303 161 NFPVHGLRFVGLMSMIDPPRAAVPDAV 187
Cdd:TIGR01106 551 NFPTDNLCFVGLISMIDPPRAAVPDAV 577
MgtA COG0474
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism];
3-187 1.21e-39

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


Pssm-ID: 440242 [Multi-domain]  Cd Length: 874  Bit Score: 142.94  E-value: 1.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303   3 KALSRIAALCNRAEfktgmenvsILKREVNGDASEAALLKCVELAVGDCKGWRSRNKKVSEVPFNSTNKYQVSIHETEDK 82
Cdd:COG0474   362 EELLRAAALCSDAQ---------LEEETGLGDPTEGALLVAAAKAGLDVEELRKEYPRVDEIPFDSERKRMSTVHEDPDG 432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303  83 ndpRYLLVMKGAPERILERCSTIYINGEEKPLDEEMKEAFNNAYLELGGLGERVLGFCdyMLPTDKYPLGYPFDADNvnf 162
Cdd:COG0474   433 ---KRLLIVKGAPEVVLALCTRVLTGGGVVPLTEEDRAEILEAVEELAAQGLRVLAVA--YKELPADPELDSEDDES--- 504

                         170       180
                  ....*....|....*....|....*
gi 2075460303 163 pvhGLRFVGLMSMIDPPRAAVPDAV 187
Cdd:COG0474   505 ---DLTFLGLVGMIDPPRPEAKEAI 526
Cation_ATPase pfam13246
Cation transport ATPase (P-type); This domain is found in cation transport ATPases, including ...
 10-105 2.71e-37

Cation transport ATPase (P-type); This domain is found in cation transport ATPases, including phospholipid-transporting ATPases, calcium-transporting ATPases, and sodium-potassium ATPases.


Pssm-ID: 463817 [Multi-domain]  Cd Length: 91  Bit Score: 124.25  E-value: 2.71e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303  10 ALCNRAEFKtgmENVSILKREVNGDASEAALLKCVELAVGDCKGWRSRNKKVSEVPFNSTNKYQVSIHETEDknDPRYLL 89
Cdd:pfam13246   1 ALCNSAAFD---ENEEKGKWEIVGDPTESALLVFAEKMGIDVEELRKDYPRVAEIPFNSDRKRMSTVHKLPD--DGKYRL 75

                          90
                  ....*....|....*.
gi 2075460303  90 VMKGAPERILERCSTI 105
Cdd:pfam13246  76 FVKGAPEIILDRCTTI 91
P-type_ATPase_Ca_prok cd02089
prokaryotic P-type Ca(2+)-ATPase similar to Synechococcus elongatus sp. strain PCC 7942 PacL ...
 33-187 1.53e-28

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.


Pssm-ID: 319781 [Multi-domain]  Cd Length: 674  Bit Score: 111.17  E-value: 1.53e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303  33 GDASEAALLKCVELAVGDCKGWRSRNKKVSEVPFNSTNKYQVSIHETEDKndprYLLVMKGAPERILERCSTIYINGEEK 112
Cdd:cd02089   324 GDPTETALIRAARKAGLDKEELEKKYPRIAEIPFDSERKLMTTVHKDAGK----YIVFTKGAPDVLLPRCTYIYINGQVR 399

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2075460303 113 PLDEEMKEAFNNAYLELGGLGERVLGFCDYMLPTDKYPlgypfDADNVNfpvHGLRFVGLMSMIDPPRAAVPDAV 187
Cdd:cd02089   400 PLTEEDRAKILAVNEEFSEEALRVLAVAYKPLDEDPTE-----SSEDLE---NDLIFLGLVGMIDPPRPEVKDAV 466
P-type_ATPase_cation cd02080
P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, ...
 7-187 3.41e-23

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.


Pssm-ID: 319775 [Multi-domain]  Cd Length: 819  Bit Score: 95.79  E-value: 3.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303   7 RIAALCNRAEfktgmenvsiLKRE-----VNGDASEAALLKCVELAVGDCKGWRSRNKKVSEVPFNSTNKYQVSIHETED 81
Cdd:cd02080   319 AIVTLCNDAQ----------LHQEdghwkITGDPTEGALLVLAAKAGLDPDRLASSYPRVDKIPFDSAYRYMATLHRDDG 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303  82 KNdpryLLVMKGAPERILERCSTIYINGEEKPLDeemKEAFNNAYLELGGLGERVLGFCDYMLPTDKYPLgypfDADNVn 161
Cdd:cd02080   389 QR----VIYVKGAPERLLDMCDQELLDGGVSPLD---RAYWEAEAEDLAKQGLRVLAFAYREVDSEVEEI----DHADL- 456

                         170       180
                  ....*....|....*....|....*.
gi 2075460303 162 fpVHGLRFVGLMSMIDPPRAAVPDAV 187
Cdd:cd02080   457 --EGGLTFLGLQGMIDPPRPEAIAAV 480
P-type_ATPases cd01431
ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, ...
 61-187 5.39e-21

ATP-dependent membrane-bound cation and aminophospholipid transporters; 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.


Pssm-ID: 319764 [Multi-domain]  Cd Length: 319  Bit Score: 87.89  E-value: 5.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303  61 VSEVPFNSTNKYQVSIHEtedkNDPRYLLVMKGAPERILERCStiyingeeKPLDEEMKEAFNNAYLELGGLGERVLGFC 140
Cdd:cd01431    22 IEEIPFNSTRKRMSVVVR----LPGRYRAIVKGAPETILSRCS--------HALTEEDRNKIEKAQEESAREGLRVLALA 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2075460303 141 dymlptdKYPLGYPFDADNVnfpVHGLRFVGLMSMIDPPRAAVPDAV 187
Cdd:cd01431    90 -------YREFDPETSKEAV---ELNLVFLGLIGLQDPPRPEVKEAI 126
ATPase_P-type TIGR01494
ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large ...
 16-187 5.18e-17

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.


Pssm-ID: 273656 [Multi-domain]  Cd Length: 545  Bit Score: 77.74  E-value: 5.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303  16 EFKTGMENVSILKREVNGDASEAALLKCVELaVGDCKGWRSRNKKVSEVPFNSTNKYQVSIHETEDKNDpryLLVMKGAP 95
Cdd:TIGR01494 262 EASLALALLAASLEYLSGHPLERAIVKSAEG-VIKSDEINVEYKILDVFPFSSVLKRMGVIVEGANGSD---LLFVKGAP 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303  96 ERILERCstiyingeekpldeEMKEAFNNAYLELGGLGERVLGFCDYMLPTDkyplgypfdadnvnfpvhgLRFVGLMSM 175
Cdd:TIGR01494 338 EFVLERC--------------NNENDYDEKVDEYARQGLRVLAFASKKLPDD-------------------LEFLGLLTF 384

                         170
                  ....*....|..
gi 2075460303 176 IDPPRAAVPDAV 187
Cdd:TIGR01494 385 EDPLRPDAKETI 396
P-type_ATPase_SERCA cd02083
sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; ...
 5-187 1.04e-16

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.


Pssm-ID: 319778 [Multi-domain]  Cd Length: 979  Bit Score: 76.95  E-value: 1.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303   5 LSRIAALCNRA-----EFKTGMENVsilkrevnGDASEAALLKCVE----------------LAVGDCKGWRSRNKKVSE 63
Cdd:cd02083   407 LATICALCNDSsldynESKGVYEKV--------GEATETALTVLVEkmnvfntdksglskreRANACNDVIEQLWKKEFT 478

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303  64 VPFnSTNKYQVSIHETEDKNDPRYLLVMKGAPERILERCSTIYINGEEK-PLDEEMKEAFNNAYLELGGLGERVLGFC-- 140
Cdd:cd02083   479 LEF-SRDRKSMSVYCSPTKASGGNKLFVKGAPEGVLERCTHVRVGGGKVvPLTAAIKILILKKVWGYGTDTLRCLALAtk 557

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2075460303 141 DYMLPTDKYPLGypfdaDNVNFpVH---GLRFVGLMSMIDPPRAAVPDAV 187
Cdd:cd02083   558 DTPPKPEDMDLE-----DSTKF-YKyetDLTFVGVVGMLDPPRPEVRDSI 601
P-type_ATPase_SPCA cd02085
golgi-associated secretory pathway Ca(2+) transport ATPases, similar to human ATPase secretory ...
 9-187 1.80e-15

golgi-associated secretory pathway Ca(2+) transport ATPases, similar to human ATPase secretory pathway Ca(2+) transporting 1/hSPCA1 and Saccharomyces cerevisiae Ca(2+)/Mn(2+)-transporting P-type ATPase, Pmr1p; SPCAs are Ca(2+) pumps important for the golgi-associated secretion pathway, in addition some function as Mn(2+) pumps in Mn(2+) detoxification. Saccharomyces cerevisiae Pmr1p is a high affinity Ca(2+)/Mn(2+) ATPase which transports Ca(2+) and Mn(2+) from the cytoplasm into the Golgi. Pmr1p also contributes to Cd(2+) detoxification. This subfamily includes human SPCA1 and SPCA2, encoded by the ATP2C1 and ATP2C2 genes; autosomal dominant Hailey-Hailey disease is caused by mutations in the human ATP2C1 gene. It also includes Strongylocentrotus purpuratus testis secretory pathway calcium transporting ATPase SPCA which plays an important role in fertilization. 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.


Pssm-ID: 319779 [Multi-domain]  Cd Length: 804  Bit Score: 73.59  E-value: 1.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303   9 AALCNraefktgmeNVSILKREVNGDASEAALLKCVELAvgDCKGWRSRNKKVSEVPFNSTNKYQV--SIHETEDKNDPR 86
Cdd:cd02085   315 GCVCN---------NAVIRNNTLMGQPTEGALIALAMKM--GLSDIRETYIRKQEIPFSSEQKWMAvkCIPKYNSDNEEI 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303  87 YLlvMKGAPERILERCSTIYI-NGEEKPLDEEMKEAFNNAYLELGGLGERVLGFCDYMLPTDkyplgypfdadnvnfpvh 165
Cdd:cd02085   384 YF--MKGALEQVLDYCTTYNSsDGSALPLTQQQRSEINEEEKEMGSKGLRVLALASGPELGD------------------ 443

                         170       180
                  ....*....|....*....|..
gi 2075460303 166 gLRFVGLMSMIDPPRAAVPDAV 187
Cdd:cd02085   444 -LTFLGLVGINDPPRPGVREAI 464
P-type_ATPase_Na_ENA cd02086
fungal-type Na(+)-ATPase, similar to the plasma membrane sodium transporters Saccharomyces ...
 9-187 6.97e-15

fungal-type Na(+)-ATPase, similar to the plasma membrane sodium transporters Saccharomyces cerevisiae Ena1p, Ena2p and Ustilago maydis Ena1, and the endoplasmic reticulum sodium transporter Ustilago maydis Ena2; Fungal-type Na(+)-ATPase (also called ENA ATPases). This subfamily includes the Saccharomyces cerevisiae plasma membrane transporters: Na(+)/Li(+)-exporting ATPase Ena1p which may also extrudes K(+), and Na(+)-exporting P-type ATPase Ena2p. It also includes Ustilago maydis plasma membrane Ena1, an K(+)/Na(+)-ATPase whose chief role is to pump Na(+) and K(+) out of the cytoplasm, especially at high pH values, and endoplasmic reticulum Ena2 ATPase which mediates Na(+) or K(+) fluxes in the ER or in other endomembranes. 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.


Pssm-ID: 319780 [Multi-domain]  Cd Length: 920  Bit Score: 71.72  E-value: 6.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303   9 AALCNRAEfktgmenvsILKRE------VNGDASEAAL-LKCVELAVGD---CKGWRSRNKKVSEVPFNSTNKYQVSIHE 78
Cdd:cd02086   353 AALCNIAT---------VFKDEetdcwkAHGDPTEIALqVFATKFDMGKnalTKGGSAQFQHVAEFPFDSTVKRMSVVYY 423

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303  79 TEDKNDprYLLVMKGAPERILERCSTIYINGEEKPLDEE-MKEAFNNAYlELGGLGERVLGFCDYMLPTDKyplgypFDA 157
Cdd:cd02086   424 NNQAGD--YYAYMKGAVERVLECCSSMYGKDGIIPLDDEfRKTIIKNVE-SLASQGLRVLAFASRSFTKAQ------FND 494

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2075460303 158 DNVNFPV-------HGLRFVGLMSMIDPPRAAVPDAV 187
Cdd:cd02086   495 DQLKNITlsradaeSDLTFLGLVGIYDPPRNESAGAV 531
P-type_ATPase cd07539
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ...
 63-187 5.66e-12

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.


Pssm-ID: 319840 [Multi-domain]  Cd Length: 634  Bit Score: 63.20  E-value: 5.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303  63 EVPFNSTNKYQVSIHETEDKndpRYLLVMKGAPERILERCSTIYINGEEKPLDEEMKEAFNNAYLELGGLGERVLGFCdY 142
Cdd:cd07539   326 ELPFESSRGYAAAIGRTGGG---IPLLAVKGAPEVVLPRCDRRMTGGQVVPLTEADRQAIEEVNELLAGQGLRVLAVA-Y 401

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2075460303 143 MLPTDKYPLGYPFDADNvnfpvhgLRFVGLMSMIDPPRAAVPDAV 187
Cdd:cd07539   402 RTLDAGTTHAVEAVVDD-------LELLGLLGLADTARPGAAALI 439
ATPase-IID_K-Na TIGR01523
potassium and/or sodium efflux P-type ATPase, fungal-type; Initially described as a calcium ...
 61-187 5.29e-11

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.


Pssm-ID: 130586 [Multi-domain]  Cd Length: 1053  Bit Score: 60.80  E-value: 5.29e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303   61 VSEVPFNSTNKYQVSIHEteDKNDPRYLLVMKGAPERILERCSTIYINGEEK--PLDEEMKEAFNNAYLELGGLGERVLG 138
Cdd:TIGR01523  528 IAEFPFDSEIKRMASIYE--DNHGETYNIYAKGAFERIIECCSSSNGKDGVKisPLEDCDRELIIANMESLAAEGLRVLA 605

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2075460303  139 FCDYMLPTDK-YPLGYPFDADNVNFPVHGLRFVGLMSMIDPPRAAVPDAV 187
Cdd:TIGR01523  606 FASKSFDKADnNDDQLKNETLNRATAESDLEFLGLIGIYDPPRNESAGAV 655
PRK10517 PRK10517
magnesium-transporting P-type ATPase MgtA;
39-180 1.31e-09

magnesium-transporting P-type ATPase MgtA;


Pssm-ID: 236705 [Multi-domain]  Cd Length: 902  Bit Score: 56.62  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303  39 ALLKCVELAVGDCKGwrSRNKKVSEVPFNSTNK-YQVSIHETEDKndprYLLVMKGAPERILERCSTIYINGEEKPLDEE 117
Cdd:PRK10517  424 AVLEGVDEESARSLA--SRWQKIDEIPFDFERRrMSVVVAENTEH----HQLICKGALEEILNVCSQVRHNGEIVPLDDI 497

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2075460303 118 MKEAFNNAYLELGGLGERVLGFCDYMLPTDKYPLGYPFDADnvnfpvhgLRFVGLMSMIDPPR 180
Cdd:PRK10517  498 MLRRIKRVTDTLNRQGLRVVAVATKYLPAREGDYQRADESD--------LILEGYIAFLDPPK 552
P-type_ATPase_H cd02076
plant and fungal plasma membrane H(+)-ATPases, and related bacterial and archaeal putative H(+) ...
 29-187 4.06e-07

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.


Pssm-ID: 319771 [Multi-domain]  Cd Length: 781  Bit Score: 49.15  E-value: 4.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303  29 REVNGDASEAALLKcvelAVGDCKGWRSRNKKVSEVPFNSTNKYQVSIHETedkNDPRYLLVMKGAPERILERCStiyin 108
Cdd:cd02076   325 DTENPDAIDTAILN----ALDDYKPDLAGYKQLKFTPFDPVDKRTEATVED---PDGERFKVTKGAPQVILELVG----- 392

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2075460303 109 geekpLDEEMKEAFNNAYLELGGLGERVLGFCdymlptdkyplgypfdadnVNFPVHGLRFVGLMSMIDPPRAAVPDAV 187
Cdd:cd02076   393 -----NDEAIRQAVEEKIDELASRGYRSLGVA-------------------RKEDGGRWELLGLLPLFDPPRPDSKATI 447
P-type_ATPase cd07538
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ...
 61-187 7.82e-07

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.


Pssm-ID: 319839 [Multi-domain]  Cd Length: 653  Bit Score: 48.21  E-value: 7.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303  61 VSEVPFNSTNKYQVSIHETEDKndprYLLVMKGAPERILERCStiyingeekpLDEEMKEAFNNAYLELGGLGERVLGFC 140
Cdd:cd07538   323 VREYPLRPELRMMGQVWKRPEG----AFAAAKGSPEAIIRLCR----------LNPDEKAAIEDAVSEMAGEGLRVLAVA 388

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2075460303 141 DYMLPTDKYPLgypfDADNVNFpvhglRFVGLMSMIDPPRAAVPDAV 187
Cdd:cd07538   389 ACRIDESFLPD----DLEDAVF-----IFVGLIGLADPLREDVPEAV 426
PRK15122 PRK15122
magnesium-transporting ATPase; Provisional
 39-187 1.80e-05

magnesium-transporting ATPase; Provisional


Pssm-ID: 237914 [Multi-domain]  Cd Length: 903  Bit Score: 44.25  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075460303  39 ALLKCVELAVGDCKGWRSRnkKVSEVPFNSTNKyQVSIhETEDKNDpRYLLVMKGAPERILERCSTIYINGEEKPLDEEM 118
Cdd:PRK15122  422 AVVAFAEGNPEIVKPAGYR--KVDELPFDFVRR-RLSV-VVEDAQG-QHLLICKGAVEEMLAVATHVRDGDTVRPLDEAR 496

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2075460303 119 KEAFNNAYLELGGLGERVLgfcdyMLPTDKYPlgypfdADNVNFPV-----HGLRFVGLMSMIDPPRAAVPDAV 187
Cdd:PRK15122  497 RERLLALAEAYNADGFRVL-----LVATREIP------GGESRAQYstadeRDLVIRGFLTFLDPPKESAAPAI 559
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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