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Conserved domains on  [gi|16128468|ref|NP_415017|]
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Cu(+) exporting P-type ATPase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

copper-exporting P-type ATPase CopA( domain architecture ID 11484858)

copper-exporting P-type ATPase CopA couples the hydrolysis of ATP with the export of Cu(+) from the cytoplasm to the periplasm through the periplasmic copper chaperone CusF; P-type ATPases are distinguished from other transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
copA PRK10671
copper-exporting P-type ATPase CopA;
1-834 0e+00

copper-exporting P-type ATPase CopA;


:

Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 1687.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468    1 MSQTIDLTLDGLSCGHCVKRVKESLEQRPDVEQADVSITEAHVTGTASAEQLIETIKQAGYDASVSHPKAKPLAESSIPS 80
Cdd:PRK10671   1 MSQTIDLTLDGLSCGHCVKRVKESLEQRPDVEQADVSITEAHVTGTASAEALIETIKQAGYDASVSHPKAKPLTESSIPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   81 EALTAVSEALPAATADDDDSQQLLLSGMSCASCVTRVQNALQSVPGVTQARVNLAERTALVMGSASPQDLVQAVEKAGYG 160
Cdd:PRK10671  81 EALTAASEELPAATADDDDSQQLLLSGMSCASCVSRVQNALQSVPGVTQARVNLAERTALVMGSASPQDLVQAVEKAGYG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  161 AEAIEDDAKRRERQQETAVATMKRFRWQAIVALAVGIPVMVWGMIGDNMMVTADNRSLWLVIGLITLAVMVFAGGHFYRS 240
Cdd:PRK10671 161 AEAIEDDAKRRERQQETAQATMKRFRWQAIVALAVGIPVMVWGMIGDNMMVTADNRSLWLVIGLITLAVMVFAGGHFYRS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  241 AWKSLLNGAATMDTLVALGTGVAWLYSMSVNLWPQWFPMEARHLYYEASAMIIGLINLGHMLEARARQRSSKALEKLLDL 320
Cdd:PRK10671 241 AWKSLLNGSATMDTLVALGTGAAWLYSMSVNLWPQWFPMEARHLYYEASAMIIGLINLGHMLEARARQRSSKALEKLLDL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  321 TPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVL 400
Cdd:PRK10671 321 TPPTARVVTDEGEKSVPLADVQPGMLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  401 FRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAVFVPVVVVIALVSAAIWYFFGPAPQIVYTLVIATTVLIIACP 480
Cdd:PRK10671 401 FRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAVFVPVVVVIALVSAAIWYFFGPAPQIVYTLVIATTVLIIACP 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  481 CALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQVVAVKTFADVDEAQALRLAAALEQGS 560
Cdd:PRK10671 481 CALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTLVFDKTGTLTEGKPQVVAVKTFNGVDEAQALRLAAALEQGS 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  561 SHPLARAILDKAGDMQLPQVNGFRTLRGLGVSGEAEGHALLLGNQALLNEQQVGTKAIEAEITAQASQGATPVLLAVDGK 640
Cdd:PRK10671 561 SHPLARAILDKAGDMTLPQVNGFRTLRGLGVSGEAEGHALLLGNQALLNEQQVDTKALEAEITAQASQGATPVLLAVDGK 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  641 AVALLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVLPDGKAEAIKHLQSEGRQVAMVGD 720
Cdd:PRK10671 641 AAALLAIRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVLPDGKAEAIKRLQSQGRQVAMVGD 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  721 GINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRATLHNMKQNLLGAFIYNSIGIPVAAGILWPFT 800
Cdd:PRK10671 721 GINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRATLRNMKQNLLGAFIYNSLGIPIAAGILWPFT 800
                        810       820       830
                 ....*....|....*....|....*....|....
gi 16128468  801 GTLLNPVVAGAAMALSSITVVSNANRLLRFKPKE 834
Cdd:PRK10671 801 GTLLNPVVAGAAMALSSITVVSNANRLLRFKPKE 834
 
Name Accession Description Interval E-value
copA PRK10671
copper-exporting P-type ATPase CopA;
1-834 0e+00

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 1687.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468    1 MSQTIDLTLDGLSCGHCVKRVKESLEQRPDVEQADVSITEAHVTGTASAEQLIETIKQAGYDASVSHPKAKPLAESSIPS 80
Cdd:PRK10671   1 MSQTIDLTLDGLSCGHCVKRVKESLEQRPDVEQADVSITEAHVTGTASAEALIETIKQAGYDASVSHPKAKPLTESSIPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   81 EALTAVSEALPAATADDDDSQQLLLSGMSCASCVTRVQNALQSVPGVTQARVNLAERTALVMGSASPQDLVQAVEKAGYG 160
Cdd:PRK10671  81 EALTAASEELPAATADDDDSQQLLLSGMSCASCVSRVQNALQSVPGVTQARVNLAERTALVMGSASPQDLVQAVEKAGYG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  161 AEAIEDDAKRRERQQETAVATMKRFRWQAIVALAVGIPVMVWGMIGDNMMVTADNRSLWLVIGLITLAVMVFAGGHFYRS 240
Cdd:PRK10671 161 AEAIEDDAKRRERQQETAQATMKRFRWQAIVALAVGIPVMVWGMIGDNMMVTADNRSLWLVIGLITLAVMVFAGGHFYRS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  241 AWKSLLNGAATMDTLVALGTGVAWLYSMSVNLWPQWFPMEARHLYYEASAMIIGLINLGHMLEARARQRSSKALEKLLDL 320
Cdd:PRK10671 241 AWKSLLNGSATMDTLVALGTGAAWLYSMSVNLWPQWFPMEARHLYYEASAMIIGLINLGHMLEARARQRSSKALEKLLDL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  321 TPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVL 400
Cdd:PRK10671 321 TPPTARVVTDEGEKSVPLADVQPGMLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  401 FRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAVFVPVVVVIALVSAAIWYFFGPAPQIVYTLVIATTVLIIACP 480
Cdd:PRK10671 401 FRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAVFVPVVVVIALVSAAIWYFFGPAPQIVYTLVIATTVLIIACP 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  481 CALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQVVAVKTFADVDEAQALRLAAALEQGS 560
Cdd:PRK10671 481 CALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTLVFDKTGTLTEGKPQVVAVKTFNGVDEAQALRLAAALEQGS 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  561 SHPLARAILDKAGDMQLPQVNGFRTLRGLGVSGEAEGHALLLGNQALLNEQQVGTKAIEAEITAQASQGATPVLLAVDGK 640
Cdd:PRK10671 561 SHPLARAILDKAGDMTLPQVNGFRTLRGLGVSGEAEGHALLLGNQALLNEQQVDTKALEAEITAQASQGATPVLLAVDGK 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  641 AVALLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVLPDGKAEAIKHLQSEGRQVAMVGD 720
Cdd:PRK10671 641 AAALLAIRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVLPDGKAEAIKRLQSQGRQVAMVGD 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  721 GINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRATLHNMKQNLLGAFIYNSIGIPVAAGILWPFT 800
Cdd:PRK10671 721 GINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRATLRNMKQNLLGAFIYNSLGIPIAAGILWPFT 800
                        810       820       830
                 ....*....|....*....|....*....|....
gi 16128468  801 GTLLNPVVAGAAMALSSITVVSNANRLLRFKPKE 834
Cdd:PRK10671 801 GTLLNPVVAGAAMALSSITVVSNANRLLRFKPKE 834
P-type_ATPase_Cu-like cd02094
P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A ...
187-829 0e+00

P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A and ATP7B; The mammalian copper-transporting P-type ATPases, ATP7A and ATP7B are key molecules required for the regulation and maintenance of copper homeostasis. Menkes and Wilson diseases are caused by mutation in ATP7A and ATP7B respectively. This subfamily includes other copper-transporting ATPases such as: Bacillus subtilis CopA , Archeaoglobus fulgidus CopA, and Saccharomyces cerevisiae Ccc2p. 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.


Pssm-ID: 319783 [Multi-domain]  Cd Length: 647  Bit Score: 917.25  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 187 WQAIVALAVGIPVMVWGMIGDNMMVTA--DNRSLWLVIGLITLAVMVFAGGHFYRSAWKSLLNGAATMDTLVALGTGVAW 264
Cdd:cd02094   1 RRLILSLLLTLPLLLLMMGGMLGPPLPllLLQLNWWLQFLLATPVQFWGGRPFYRGAWKALKHGSANMDTLVALGTSAAY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 265 LYSMSVNLWPQWFPMEARHLYYEASAMIIGLINLGHMLEARARQRSSKALEKLLDLTPPTARLVTDEGEKSVPLAEVQPG 344
Cdd:cd02094  81 LYSLVALLFPALFPGGAPHVYFEAAAVIITFILLGKYLEARAKGKTSEAIKKLLGLQPKTARVIRDGKEVEVPIEEVQVG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 345 MLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQS 424
Cdd:cd02094 161 DIVRVRPGEKIPVDGVVVEGESSVDESMLTGESLPVEKKPGDKVIGGTINGNGSLLVRATRVGADTTLAQIIRLVEEAQG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 425 SKPEIGQLADKISAVFVPVVVVIALVSAAIWYFFGPAPQIVYTLVIATTVLIIACPCALGLATPMSIISGVGRAAEFGVL 504
Cdd:cd02094 241 SKAPIQRLADRVSGVFVPVVIAIAILTFLVWLLLGPEPALTFALVAAVAVLVIACPCALGLATPTAIMVGTGRAAELGIL 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 505 VRDADALQRASTLDTVVFDKTGTLTEGKPQVVAVKTFADVDEAQALRLAAALEQGSSHPLARAILDKAGDMQL--PQVNG 582
Cdd:cd02094 321 IKGGEALERAHKVDTVVFDKTGTLTEGKPEVTDVVPLPGDDEDELLRLAASLEQGSEHPLAKAIVAAAKEKGLelPEVED 400
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 583 FRTLRGLGVSGEAEGHALLLGNQALLNEQQVGTKAIEAEITAQASQGATPVLLAVDGKAVALLAVRDPLRSDSVAALQRL 662
Cdd:cd02094 401 FEAIPGKGVRGTVDGRRVLVGNRRLMEENGIDLSALEAEALALEEEGKTVVLVAVDGELAGLIAVADPLKPDAAEAIEAL 480
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 663 HKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVLPDGKAEAIKHLQSEGRQVAMVGDGINDAPALAQADVGIAMGGGSD 742
Cdd:cd02094 481 KKMGIKVVMLTGDNRRTARAIAKELGIDEVIAEVLPEDKAEKVKKLQAQGKKVAMVGDGINDAPALAQADVGIAIGSGTD 560
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 743 VAIETAAITLMRHSLMGVADALAISRATLHNMKQNLLGAFIYNSIGIPVAAGILWPFTGTLLNPVVAGAAMALSSITVVS 822
Cdd:cd02094 561 VAIESADIVLMRGDLRGVVTAIDLSRATMRNIKQNLFWAFIYNVIGIPLAAGVLYPFGGILLSPMIAGAAMALSSVSVVL 640

                ....*..
gi 16128468 823 NANRLLR 829
Cdd:cd02094 641 NSLRLRR 647
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
102-833 0e+00

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 889.88  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 102 QLLLSGMSCASCVTRVQNALQSVPGVTQARVNLAERTALVM---GSASPQDLVQAVEKAGYGAEAIEDDAKRRERQQeta 178
Cdd:COG2217   4 RLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEydpGKVSLEELIAAVEKAGYEAEPADADAAAEEARE--- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 179 vATMKRFRWQAIVALAVGIPVMVWGMIgdnmMVTADNRSLWLVIgLITLAVMVFAGGHFYRSAWKSLLNGAATMDTLVAL 258
Cdd:COG2217  81 -KELRDLLRRLAVAGVLALPVMLLSMP----EYLGGGLPGWLSL-LLATPVVFYAGWPFFRGAWRALRHRRLNMDVLVAL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 259 GTGVAWLYSMSVNLWPqwfpmeARHLYYEASAMIIGLINLGHMLEARARQRSSKALEKLLDLTPPTARLVTDEGEKSVPL 338
Cdd:COG2217 155 GTLAAFLYSLYATLFG------AGHVYFEAAAMIIFLLLLGRYLEARAKGRARAAIRALLSLQPKTARVLRDGEEVEVPV 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 339 AEVQPGMLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRM 418
Cdd:COG2217 229 EELRVGDRVLVRPGERIPVDGVVLEGESSVDESMLTGESLPVEKTPGDEVFAGTINLDGSLRVRVTKVGSDTTLARIIRL 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 419 VRQAQSSKPEIGQLADKISAVFVPVVVVIALVSAAIWYFFGPAPQivYTLVIATTVLIIACPCALGLATPMSIISGVGRA 498
Cdd:COG2217 309 VEEAQSSKAPIQRLADRIARYFVPAVLAIAALTFLVWLLFGGDFS--TALYRAVAVLVIACPCALGLATPTAIMVGTGRA 386
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 499 AEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQVVAVKTFADVDEAQALRLAAALEQGSSHPLARAILDKAGD--MQ 576
Cdd:COG2217 387 ARRGILIKGGEALERLAKVDTVVFDKTGTLTEGKPEVTDVVPLDGLDEDELLALAAALEQGSEHPLARAIVAAAKErgLE 466
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 577 LPQVNGFRTLRGLGVSGEAEGHALLLGNQALLNEQQVGTK-AIEAEITAQASQGATPVLLAVDGKAVALLAVRDPLRSDS 655
Cdd:COG2217 467 LPEVEDFEAIPGKGVEATVDGKRVLVGSPRLLEEEGIDLPeALEERAEELEAEGKTVVYVAVDGRLLGLIALADTLRPEA 546
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 656 VAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVLPDGKAEAIKHLQSEGRQVAMVGDGINDAPALAQADVGI 735
Cdd:COG2217 547 AEAIAALKALGIRVVMLTGDNERTAEAVARELGIDEVRAEVLPEDKAAAVRELQAQGKKVAMVGDGINDAPALAAADVGI 626
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 736 AMGGGSDVAIETAAITLMRHSLMGVADALAISRATLHNMKQNLLGAFIYNSIGIPVAAGIlwpftgtLLNPVVAGAAMAL 815
Cdd:COG2217 627 AMGSGTDVAIEAADIVLMRDDLRGVPDAIRLSRATMRIIRQNLFWAFGYNVIGIPLAAGG-------LLSPWIAAAAMAL 699
                       730
                ....*....|....*...
gi 16128468 816 SSITVVSNANRLLRFKPK 833
Cdd:COG2217 700 SSVSVVLNALRLRRFKPK 717
ATPase-IB1_Cu TIGR01511
copper-(or silver)-translocating P-type ATPase; This model describes the P-type ATPase ...
233-809 0e+00

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]


Pssm-ID: 273664 [Multi-domain]  Cd Length: 562  Bit Score: 734.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   233 AGGHFYRSAWKSLLNGAATMDTLVALGTGVAWLYSMSVNLWPQWFPMEARHLYYEASAMIIGLINLGHMLEARARQRSSK 312
Cdd:TIGR01511   1 AGRPFYKSAWKALRHKAPNMDTLIALGTTVAYGYSLVALLANQVLTGLHVHTFFDASAMLITFILLGRWLEMLAKGRASD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   313 ALEKLLDLTPPTARLVTDEGE-KSVPLAEVQPGMLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEPIPQQKGEGDSVHAG 391
Cdd:TIGR01511  81 ALSKLAKLQPSTATLLTKDGSiEEVPVALLQPGDIVKVLPGEKIPVDGTVIEGESEVDESLVTGESLPVPKKVGDPVIAG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   392 TVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAVFVPVVVVIALVSAAIWYFfgpapqivyTLVIA 471
Cdd:TIGR01511 161 TVNGTGSLVVRATATGEDTTLAQIVRLVRQAQQSKAPIQRLADKVAGYFVPVVIAIALITFVIWLF---------ALEFA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   472 TTVLIIACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQVVAVKTFADVDEAQALR 551
Cdd:TIGR01511 232 VTVLIIACPCALGLATPTVIAVATGLAAKNGVLIKDGDALERAANIDTVVFDKTGTLTQGKPTVTDVHVFGDRDRTELLA 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   552 LAAALEQGSSHPLARAILDKAGDMQLP--QVNGFRTLRGLGVSGEAEGHALLLGNQALLNEQQVgtkaieaEITAQASQG 629
Cdd:TIGR01511 312 LAAALEAGSEHPLAKAIVSYAKEKGITlvTVSDFKAIPGIGVEGTVEGTKIQLGNEKLLGENAI-------KIDGKAGQG 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   630 ATPVLLAVDGKAVALLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDeVIAGVLPDGKAEAIKHLQ 709
Cdd:TIGR01511 385 STVVLVAVNGELAGVFALEDQLRPEAKEVIQALKRRGIEPVMLTGDNRKTAKAVAKELGID-VRAEVLPDDKAALIKKLQ 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   710 SEGRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRATLHNMKQNLLGAFIYNSIGI 789
Cdd:TIGR01511 464 EKGPVVAMVGDGINDAPALAQADVGIAIGAGTDVAIEAADVVLLRNDLNDVATAIDLSRKTLRRIKQNLLWAFGYNVIAI 543
                         570       580
                  ....*....|....*....|
gi 16128468   790 PVAAGILWPFtGTLLNPVVA 809
Cdd:TIGR01511 544 PIAAGVLYPI-GILLSPAVA 562
E1-E2_ATPase pfam00122
E1-E2 ATPase;
319-499 3.73e-51

E1-E2 ATPase;


Pssm-ID: 425475 [Multi-domain]  Cd Length: 181  Bit Score: 176.99  E-value: 3.73e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   319 DLTPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGS 398
Cdd:pfam00122   1 SLLPPTATVLRDGTEEEVPADELVPGDIVLLKPGERVPADGRIVEGSASVDESLLTGESLPVEKKKGDMVYSGTVVVSGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   399 VLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAVFVPVVVVIALVSAAIWYFFGPAPQivYTLVIATTVLIIA 478
Cdd:pfam00122  81 AKAVVTATGEDTELGRIARLVEEAKSKKTPLQRLLDRLGKYFSPVVLLIALAVFLLWLFVGGPPL--RALLRALAVLVAA 158
                         170       180
                  ....*....|....*....|.
gi 16128468   479 CPCALGLATPMSIISGVGRAA 499
Cdd:pfam00122 159 CPCALPLATPLALAVGARRLA 179
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
7-62 2.25e-08

copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in Bacillus subtilis and related species. A number of longer protein, such as copper-translocating P-type ATPases, contain multiple CopZ-like domains, with its signature invariant CxxC motif. CopZ from other species may be more different in sequence from this family than some of those domains of longer proteins.


Pssm-ID: 411375 [Multi-domain]  Cd Length: 66  Bit Score: 51.33  E-value: 2.25e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128468    7 LTLDGLSCGHCVKRVKESLEQRPDVEQADVSITEAHVT-----GTASAEQLIETIKQAGYD 62
Cdd:NF033795   4 LNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDvefdeSKVTLDQIKEAIEDQGYD 64
 
Name Accession Description Interval E-value
copA PRK10671
copper-exporting P-type ATPase CopA;
1-834 0e+00

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 1687.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468    1 MSQTIDLTLDGLSCGHCVKRVKESLEQRPDVEQADVSITEAHVTGTASAEQLIETIKQAGYDASVSHPKAKPLAESSIPS 80
Cdd:PRK10671   1 MSQTIDLTLDGLSCGHCVKRVKESLEQRPDVEQADVSITEAHVTGTASAEALIETIKQAGYDASVSHPKAKPLTESSIPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   81 EALTAVSEALPAATADDDDSQQLLLSGMSCASCVTRVQNALQSVPGVTQARVNLAERTALVMGSASPQDLVQAVEKAGYG 160
Cdd:PRK10671  81 EALTAASEELPAATADDDDSQQLLLSGMSCASCVSRVQNALQSVPGVTQARVNLAERTALVMGSASPQDLVQAVEKAGYG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  161 AEAIEDDAKRRERQQETAVATMKRFRWQAIVALAVGIPVMVWGMIGDNMMVTADNRSLWLVIGLITLAVMVFAGGHFYRS 240
Cdd:PRK10671 161 AEAIEDDAKRRERQQETAQATMKRFRWQAIVALAVGIPVMVWGMIGDNMMVTADNRSLWLVIGLITLAVMVFAGGHFYRS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  241 AWKSLLNGAATMDTLVALGTGVAWLYSMSVNLWPQWFPMEARHLYYEASAMIIGLINLGHMLEARARQRSSKALEKLLDL 320
Cdd:PRK10671 241 AWKSLLNGSATMDTLVALGTGAAWLYSMSVNLWPQWFPMEARHLYYEASAMIIGLINLGHMLEARARQRSSKALEKLLDL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  321 TPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVL 400
Cdd:PRK10671 321 TPPTARVVTDEGEKSVPLADVQPGMLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  401 FRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAVFVPVVVVIALVSAAIWYFFGPAPQIVYTLVIATTVLIIACP 480
Cdd:PRK10671 401 FRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAVFVPVVVVIALVSAAIWYFFGPAPQIVYTLVIATTVLIIACP 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  481 CALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQVVAVKTFADVDEAQALRLAAALEQGS 560
Cdd:PRK10671 481 CALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTLVFDKTGTLTEGKPQVVAVKTFNGVDEAQALRLAAALEQGS 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  561 SHPLARAILDKAGDMQLPQVNGFRTLRGLGVSGEAEGHALLLGNQALLNEQQVGTKAIEAEITAQASQGATPVLLAVDGK 640
Cdd:PRK10671 561 SHPLARAILDKAGDMTLPQVNGFRTLRGLGVSGEAEGHALLLGNQALLNEQQVDTKALEAEITAQASQGATPVLLAVDGK 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  641 AVALLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVLPDGKAEAIKHLQSEGRQVAMVGD 720
Cdd:PRK10671 641 AAALLAIRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVLPDGKAEAIKRLQSQGRQVAMVGD 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  721 GINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRATLHNMKQNLLGAFIYNSIGIPVAAGILWPFT 800
Cdd:PRK10671 721 GINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRATLRNMKQNLLGAFIYNSLGIPIAAGILWPFT 800
                        810       820       830
                 ....*....|....*....|....*....|....
gi 16128468  801 GTLLNPVVAGAAMALSSITVVSNANRLLRFKPKE 834
Cdd:PRK10671 801 GTLLNPVVAGAAMALSSITVVSNANRLLRFKPKE 834
P-type_ATPase_Cu-like cd02094
P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A ...
187-829 0e+00

P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A and ATP7B; The mammalian copper-transporting P-type ATPases, ATP7A and ATP7B are key molecules required for the regulation and maintenance of copper homeostasis. Menkes and Wilson diseases are caused by mutation in ATP7A and ATP7B respectively. This subfamily includes other copper-transporting ATPases such as: Bacillus subtilis CopA , Archeaoglobus fulgidus CopA, and Saccharomyces cerevisiae Ccc2p. 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.


Pssm-ID: 319783 [Multi-domain]  Cd Length: 647  Bit Score: 917.25  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 187 WQAIVALAVGIPVMVWGMIGDNMMVTA--DNRSLWLVIGLITLAVMVFAGGHFYRSAWKSLLNGAATMDTLVALGTGVAW 264
Cdd:cd02094   1 RRLILSLLLTLPLLLLMMGGMLGPPLPllLLQLNWWLQFLLATPVQFWGGRPFYRGAWKALKHGSANMDTLVALGTSAAY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 265 LYSMSVNLWPQWFPMEARHLYYEASAMIIGLINLGHMLEARARQRSSKALEKLLDLTPPTARLVTDEGEKSVPLAEVQPG 344
Cdd:cd02094  81 LYSLVALLFPALFPGGAPHVYFEAAAVIITFILLGKYLEARAKGKTSEAIKKLLGLQPKTARVIRDGKEVEVPIEEVQVG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 345 MLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQS 424
Cdd:cd02094 161 DIVRVRPGEKIPVDGVVVEGESSVDESMLTGESLPVEKKPGDKVIGGTINGNGSLLVRATRVGADTTLAQIIRLVEEAQG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 425 SKPEIGQLADKISAVFVPVVVVIALVSAAIWYFFGPAPQIVYTLVIATTVLIIACPCALGLATPMSIISGVGRAAEFGVL 504
Cdd:cd02094 241 SKAPIQRLADRVSGVFVPVVIAIAILTFLVWLLLGPEPALTFALVAAVAVLVIACPCALGLATPTAIMVGTGRAAELGIL 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 505 VRDADALQRASTLDTVVFDKTGTLTEGKPQVVAVKTFADVDEAQALRLAAALEQGSSHPLARAILDKAGDMQL--PQVNG 582
Cdd:cd02094 321 IKGGEALERAHKVDTVVFDKTGTLTEGKPEVTDVVPLPGDDEDELLRLAASLEQGSEHPLAKAIVAAAKEKGLelPEVED 400
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 583 FRTLRGLGVSGEAEGHALLLGNQALLNEQQVGTKAIEAEITAQASQGATPVLLAVDGKAVALLAVRDPLRSDSVAALQRL 662
Cdd:cd02094 401 FEAIPGKGVRGTVDGRRVLVGNRRLMEENGIDLSALEAEALALEEEGKTVVLVAVDGELAGLIAVADPLKPDAAEAIEAL 480
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 663 HKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVLPDGKAEAIKHLQSEGRQVAMVGDGINDAPALAQADVGIAMGGGSD 742
Cdd:cd02094 481 KKMGIKVVMLTGDNRRTARAIAKELGIDEVIAEVLPEDKAEKVKKLQAQGKKVAMVGDGINDAPALAQADVGIAIGSGTD 560
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 743 VAIETAAITLMRHSLMGVADALAISRATLHNMKQNLLGAFIYNSIGIPVAAGILWPFTGTLLNPVVAGAAMALSSITVVS 822
Cdd:cd02094 561 VAIESADIVLMRGDLRGVVTAIDLSRATMRNIKQNLFWAFIYNVIGIPLAAGVLYPFGGILLSPMIAGAAMALSSVSVVL 640

                ....*..
gi 16128468 823 NANRLLR 829
Cdd:cd02094 641 NSLRLRR 647
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
102-833 0e+00

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 889.88  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 102 QLLLSGMSCASCVTRVQNALQSVPGVTQARVNLAERTALVM---GSASPQDLVQAVEKAGYGAEAIEDDAKRRERQQeta 178
Cdd:COG2217   4 RLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEydpGKVSLEELIAAVEKAGYEAEPADADAAAEEARE--- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 179 vATMKRFRWQAIVALAVGIPVMVWGMIgdnmMVTADNRSLWLVIgLITLAVMVFAGGHFYRSAWKSLLNGAATMDTLVAL 258
Cdd:COG2217  81 -KELRDLLRRLAVAGVLALPVMLLSMP----EYLGGGLPGWLSL-LLATPVVFYAGWPFFRGAWRALRHRRLNMDVLVAL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 259 GTGVAWLYSMSVNLWPqwfpmeARHLYYEASAMIIGLINLGHMLEARARQRSSKALEKLLDLTPPTARLVTDEGEKSVPL 338
Cdd:COG2217 155 GTLAAFLYSLYATLFG------AGHVYFEAAAMIIFLLLLGRYLEARAKGRARAAIRALLSLQPKTARVLRDGEEVEVPV 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 339 AEVQPGMLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRM 418
Cdd:COG2217 229 EELRVGDRVLVRPGERIPVDGVVLEGESSVDESMLTGESLPVEKTPGDEVFAGTINLDGSLRVRVTKVGSDTTLARIIRL 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 419 VRQAQSSKPEIGQLADKISAVFVPVVVVIALVSAAIWYFFGPAPQivYTLVIATTVLIIACPCALGLATPMSIISGVGRA 498
Cdd:COG2217 309 VEEAQSSKAPIQRLADRIARYFVPAVLAIAALTFLVWLLFGGDFS--TALYRAVAVLVIACPCALGLATPTAIMVGTGRA 386
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 499 AEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQVVAVKTFADVDEAQALRLAAALEQGSSHPLARAILDKAGD--MQ 576
Cdd:COG2217 387 ARRGILIKGGEALERLAKVDTVVFDKTGTLTEGKPEVTDVVPLDGLDEDELLALAAALEQGSEHPLARAIVAAAKErgLE 466
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 577 LPQVNGFRTLRGLGVSGEAEGHALLLGNQALLNEQQVGTK-AIEAEITAQASQGATPVLLAVDGKAVALLAVRDPLRSDS 655
Cdd:COG2217 467 LPEVEDFEAIPGKGVEATVDGKRVLVGSPRLLEEEGIDLPeALEERAEELEAEGKTVVYVAVDGRLLGLIALADTLRPEA 546
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 656 VAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVLPDGKAEAIKHLQSEGRQVAMVGDGINDAPALAQADVGI 735
Cdd:COG2217 547 AEAIAALKALGIRVVMLTGDNERTAEAVARELGIDEVRAEVLPEDKAAAVRELQAQGKKVAMVGDGINDAPALAAADVGI 626
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 736 AMGGGSDVAIETAAITLMRHSLMGVADALAISRATLHNMKQNLLGAFIYNSIGIPVAAGIlwpftgtLLNPVVAGAAMAL 815
Cdd:COG2217 627 AMGSGTDVAIEAADIVLMRDDLRGVPDAIRLSRATMRIIRQNLFWAFGYNVIGIPLAAGG-------LLSPWIAAAAMAL 699
                       730
                ....*....|....*...
gi 16128468 816 SSITVVSNANRLLRFKPK 833
Cdd:COG2217 700 SSVSVVLNALRLRRFKPK 717
ATPase-IB1_Cu TIGR01511
copper-(or silver)-translocating P-type ATPase; This model describes the P-type ATPase ...
233-809 0e+00

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]


Pssm-ID: 273664 [Multi-domain]  Cd Length: 562  Bit Score: 734.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   233 AGGHFYRSAWKSLLNGAATMDTLVALGTGVAWLYSMSVNLWPQWFPMEARHLYYEASAMIIGLINLGHMLEARARQRSSK 312
Cdd:TIGR01511   1 AGRPFYKSAWKALRHKAPNMDTLIALGTTVAYGYSLVALLANQVLTGLHVHTFFDASAMLITFILLGRWLEMLAKGRASD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   313 ALEKLLDLTPPTARLVTDEGE-KSVPLAEVQPGMLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEPIPQQKGEGDSVHAG 391
Cdd:TIGR01511  81 ALSKLAKLQPSTATLLTKDGSiEEVPVALLQPGDIVKVLPGEKIPVDGTVIEGESEVDESLVTGESLPVPKKVGDPVIAG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   392 TVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAVFVPVVVVIALVSAAIWYFfgpapqivyTLVIA 471
Cdd:TIGR01511 161 TVNGTGSLVVRATATGEDTTLAQIVRLVRQAQQSKAPIQRLADKVAGYFVPVVIAIALITFVIWLF---------ALEFA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   472 TTVLIIACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQVVAVKTFADVDEAQALR 551
Cdd:TIGR01511 232 VTVLIIACPCALGLATPTVIAVATGLAAKNGVLIKDGDALERAANIDTVVFDKTGTLTQGKPTVTDVHVFGDRDRTELLA 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   552 LAAALEQGSSHPLARAILDKAGDMQLP--QVNGFRTLRGLGVSGEAEGHALLLGNQALLNEQQVgtkaieaEITAQASQG 629
Cdd:TIGR01511 312 LAAALEAGSEHPLAKAIVSYAKEKGITlvTVSDFKAIPGIGVEGTVEGTKIQLGNEKLLGENAI-------KIDGKAGQG 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   630 ATPVLLAVDGKAVALLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDeVIAGVLPDGKAEAIKHLQ 709
Cdd:TIGR01511 385 STVVLVAVNGELAGVFALEDQLRPEAKEVIQALKRRGIEPVMLTGDNRKTAKAVAKELGID-VRAEVLPDDKAALIKKLQ 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   710 SEGRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRATLHNMKQNLLGAFIYNSIGI 789
Cdd:TIGR01511 464 EKGPVVAMVGDGINDAPALAQADVGIAIGAGTDVAIEAADVVLLRNDLNDVATAIDLSRKTLRRIKQNLLWAFGYNVIAI 543
                         570       580
                  ....*....|....*....|
gi 16128468   790 PVAAGILWPFtGTLLNPVVA 809
Cdd:TIGR01511 544 PIAAGVLYPI-GILLSPAVA 562
P-type_ATPase_HM cd02079
P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) ...
192-826 0e+00

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.


Pssm-ID: 319774 [Multi-domain]  Cd Length: 617  Bit Score: 621.93  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 192 ALAVGIPVMVWGMIGDNMMVTADNRSLWLVIGLITLAVMVFAGGHFYRSAWKSLLNGAATMDTLVALGTGVAWLYSMsvn 271
Cdd:cd02079   1 AALVSGALMLLAFALYLGLFGGLVQLLLWVSLLLALPALLYGGRPFLRGAWRSLRRGRLNMDVLVSLAAIGAFVASL--- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 272 lwpqWFPMEARHLYYEASAMIIGLINLGHMLEARARQRSSKALEKLLDLTPPTARLVTDEGEKSVPLAEVQPGMLLRLTT 351
Cdd:cd02079  78 ----LTPLLGGIGYFEEAAMLLFLFLLGRYLEERARSRARSALKALLSLAPETATVLEDGSTEEVPVDDLKVGDVVLVKP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 352 GDRVPVDGEITQGEAWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQ 431
Cdd:cd02079 154 GERIPVDGVVVSGESSVDESSLTGESLPVEKGAGDTVFAGTINLNGPLTIEVTKTGEDTTLAKIIRLVEEAQSSKPPLQR 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 432 LADKISAVFVPVVVVIALVSAAIWYFFGPAPQIvyTLVIATTVLIIACPCALGLATPMSIISGVGRAAEFGVLVRDADAL 511
Cdd:cd02079 234 LADRFARYFTPAVLVLAALVFLFWPLVGGPPSL--ALYRALAVLVVACPCALGLATPTAIVAGIGRAARKGILIKGGDVL 311
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 512 QRASTLDTVVFDKTGTLTEGKPQVVAVKTFADVDEAQALRLAAALEQGSSHPLARAILDKAGDMQLP--QVNGFRTLRGL 589
Cdd:cd02079 312 ETLAKVDTVAFDKTGTLTEGKPEVTEIEPLEGFSEDELLALAAALEQHSEHPLARAIVEAAEEKGLPplEVEDVEEIPGK 391
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 590 GVSGEAEGHALLLGNQALLNEQQVGTKAIEAEITAqasqGATPVLLAVDGKAVALLAVRDPLRSDSVAALQRLHKAGYRL 669
Cdd:cd02079 392 GISGEVDGREVLIGSLSFAEEEGLVEAADALSDAG----KTSAVYVGRDGKLVGLFALEDQLRPEAKEVIAELKSGGIKV 467
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 670 VMLTGDNPTTANAIAKEAGIDEVIAGVLPDGKAEAIKHLQSEGRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETAA 749
Cdd:cd02079 468 VMLTGDNEAAAQAVAKELGIDEVHAGLLPEDKLAIVKALQAEGGPVAMVGDGINDAPALAQADVGIAMGSGTDVAIETAD 547
                       570       580       590       600       610       620       630
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128468 750 ITLMRHSLMGVADALAISRATLHNMKQNLLGAFIYNSIGIPVAAGILWPftgtllnPVVAGAAMALSSITVVSNANR 826
Cdd:cd02079 548 IVLLSNDLSKLPDAIRLARRTRRIIKQNLAWALGYNAIALPLAALGLLT-------PWIAALLMEGSSLLVVLNALR 617
ATPase-IB_hvy TIGR01525
heavy metal translocating P-type ATPase; This model encompasses two equivalog models for the ...
252-827 0e+00

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.


Pssm-ID: 273669 [Multi-domain]  Cd Length: 558  Bit Score: 536.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   252 MDTLVALGTGVAWLYSmsvnlwpqwfpmearhlYYEASAMIIGLINLGHMLEARARQRSSKALEKLLDLTPPTARLVTDE 331
Cdd:TIGR01525   1 MDTLMALAAIAAYAMG-----------------LVLEGALLLFLFLLGETLEERAKSRASDALSALLALAPSTARVLQGD 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   332 G-EKSVPLAEVQPGMLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVLFRASAVGSHT 410
Cdd:TIGR01525  64 GsEEEVPVEELQVGDIVIVRPGERIPVDGVVISGESEVDESALTGESMPVEKKEGDEVFAGTINGDGSLTIRVTKLGEDS 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   411 TLSRIIRMVRQAQSSKPEIGQLADKISAVFVPVVVVIALVSAAIWYFFGPAPQIVytLVIATTVLIIACPCALGLATPMS 490
Cdd:TIGR01525 144 TLAQIVELVEEAQSSKAPIQRLADRIASYYVPAVLAIALLTFVVWLALGALWREA--LYRALTVLVVACPCALGLATPVA 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   491 IISGVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQVVAVKTFADVDEAQALRLAAALEQGSSHPLARAILD 570
Cdd:TIGR01525 222 ILVAIGAAARRGILIKGGDALEKLAKVKTVVFDKTGTLTTGKPTVVDIEPLDDASEEELLALAAALEQSSSHPLARAIVR 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   571 --KAGDMQLPQVNgFRTLRGLGVSGEAEGHA-LLLGNQALLNEQQVGTKAIEAE---ITAQASQGATPVLLAVDGKAVAL 644
Cdd:TIGR01525 302 yaKERGLELPPED-VEEVPGKGVEATVDGGReVRIGNPRFLGNRELAIEPISASpdlLNEGESQGKTVVFVAVDGELLGV 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   645 LAVRDPLRSDSVAALQRLHKAG-YRLVMLTGDNPTTANAIAKEAGI-DEVIAGVLPDGKAEAIKHLQSEGRQVAMVGDGI 722
Cdd:TIGR01525 381 IALRDQLRPEAKEAIAALKRAGgIKLVMLTGDNRSAAEAVAAELGIdDEVHAELLPEDKLAIVKKLQEEGGPVAMVGDGI 460
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   723 NDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRATLHNMKQNLLGAFIYNSIGIPVAAGIlwpftgt 802
Cdd:TIGR01525 461 NDAPALAAADVGIAMGSGSDVAIEAADIVLLNDDLRSLPTAIDLSRKTRRIIKQNLAWALGYNLVAIPLAAGG------- 533
                         570       580
                  ....*....|....*....|....*
gi 16128468   803 LLNPVVAGAAMALSSITVVSNANRL 827
Cdd:TIGR01525 534 LLPLWLAVLLHEGSTVLVVLNSLRL 558
P-type_ATPase_Cu-like cd07552
P-type heavy metal-transporting ATPase, similar to Archaeoglobus fulgidus CopB, a Cu(2+) ...
192-829 7.78e-165

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.


Pssm-ID: 319850 [Multi-domain]  Cd Length: 632  Bit Score: 492.59  E-value: 7.78e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 192 ALAVGIPVMVWG-MIGDNMMVTAD-NRSLWLVIGLITlAVMVFAGGHFYRSAWKSLLNGAATMDTLVALGTGVAWLYSMS 269
Cdd:cd07552   1 SLILTIPILLLSpMMGTLLPFQVSfPGSDWVVLILAT-ILFFYGGKPFLKGAKDELKSKKPGMMTLIALGITVAYVYSVY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 270 VNLwPQWFPMEARHLYYEASAMIIGLInLGHMLEARARQRSSKALEKLLDLTPPTARLVTDEGEKSVPLAEVQPGMLLRL 349
Cdd:cd07552  80 AFL-GNYFGEHGMDFFWELATLIVIML-LGHWIEMKAVMGAGDALKKLAELLPKTAHLVTDGSIEDVPVSELKVGDVVLV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 350 TTGDRVPVDGEITQGEAWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPEI 429
Cdd:cd07552 158 RAGEKIPADGTILEGESSVNESMVTGESKPVEKKPGDEVIGGSVNGNGTLEVKVTKTGEDSYLSQVMELVAQAQASKSRA 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 430 GQLADKISAVFVPVVVVIALVSAAIWYFFGPAPqivYTLVIATTVLIIACPCALGLATPMSIISGVGRAAEFGVLVRDAD 509
Cdd:cd07552 238 ENLADKVAGWLFYIALGVGIIAFIIWLILGDLA---FALERAVTVLVIACPHALGLAIPLVVARSTSIAAKNGLLIRNRE 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 510 ALQRASTLDTVVFDKTGTLTEGKPQVVAVKTFADVDEAQALRLAAALEQGSSHPLARAILDKAGDMQL--PQVNGFRTLR 587
Cdd:cd07552 315 ALERARDIDVVLFDKTGTLTEGKFGVTDVITFDEYDEDEILSLAAALEAGSEHPLAQAIVSAAKEKGIrpVEVENFENIP 394
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 588 GLGVSGEAEGHALLLGNQALLNEQQVGTKaiEAEITAQASQGATPVLLAVDGKAVALLAVRDPLRSDSVAALQRLHKAGY 667
Cdd:cd07552 395 GVGVEGTVNGKRYQVVSPKYLKELGLKYD--EELVKRLAQQGNTVSFLIQDGEVIGAIALGDEIKPESKEAIRALKAQGI 472
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 668 RLVMLTGDNPTTANAIAKEAGIDEVIAGVLPDGKAEAIKHLQSEGRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIET 747
Cdd:cd07552 473 TPVMLTGDNEEVAQAVAEELGIDEYFAEVLPEDKAKKVKELQAEGKKVAMVGDGVNDAPALAQADVGIAIGAGTDVAIES 552
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 748 AAITLMRHSLMGVADALAISRATLHNMKQNLLGAFIYNSIGIPVAAGILWPFtGTLLNPVVAGAAMALSSITVVSNAnRL 827
Cdd:cd07552 553 ADVVLVKSDPRDIVDFLELAKATYRKMKQNLWWGAGYNVIAIPLAAGVLAPI-GIILSPAVGAVLMSLSTVIVAINA-MT 630

                ..
gi 16128468 828 LR 829
Cdd:cd07552 631 LK 632
ATPase-IB2_Cd TIGR01512
heavy metal-(Cd/Co/Hg/Pb/Zn)-translocating P-type ATPase; This model describes the P-type ...
285-829 1.66e-139

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]


Pssm-ID: 273665 [Multi-domain]  Cd Length: 550  Bit Score: 424.43  E-value: 1.66e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   285 YYEASAMIIGLINLGHMLEARARQRSSKALEKLLDLTPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPVDGEITQG 364
Cdd:TIGR01512  17 EYLEGALLLLLFSIGETLEEYASGRARRALKALMELAPDTARRLQGDSLEEVAVEELKVGDVVVVKPGERVPVDGEVLSG 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   365 EAWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAVFVPVV 444
Cdd:TIGR01512  97 TSSVDESALTGESVPVEKAPGDEVFAGAINLDGVLTIEVTKLPADSTIAKIVNLVEEAQSRKAPTQRFIDRFARYYTPAV 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   445 VVIALVSAAIWYFFGPAPQIVYtLVIATTVLIIACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFDK 524
Cdd:TIGR01512 177 LAIALAAALVPPLLGAGPFLEW-IYRALVLLVVASPCALVISAPAAYLSAISAAARHGILIKGGAALEALAKIKTVAFDK 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   525 TGTLTEGKPQVVAVKTFADVDEAQALRLAAALEQGSSHPLARAILDKAGDMQL-PQVNGFRTLRGLGVSGEAEGHALLLG 603
Cdd:TIGR01512 256 TGTLTTGKPKVTDVHPADGHSESEVLRLAAAAEQGSTHPLARAIVDYARARELaPPVEDVEEVPGEGVRAVVDGGEVRIG 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   604 NQALLNEqqvgtkAIEAEITAQASQGATPVLLAVDGKAVALLAVRDPLRSDSVAALQRLHKAGY-RLVMLTGDNPTTANA 682
Cdd:TIGR01512 336 NPRSLSE------AVGASIAVPESAGKTIVLVARDGTLLGYIALSDELRPDAAEAIAELKALGIkRLVMLTGDRRAVAEA 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   683 IAKEAGIDEVIAGVLPDGKAEAIKHLQSEGRQVAMVGDGINDAPALAQADVGIAMGG-GSDVAIETAAITLMRHSLMGVA 761
Cdd:TIGR01512 410 VARELGIDEVHAELLPEDKLEIVKELREKAGPVAMVGDGINDAPALAAADVGIAMGAsGSDVALETADVVLLNDDLSRLP 489
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128468   762 DALAISRATLHNMKQNLLGAfiynsIGIpVAAGILWPFTGtLLNPVVAGAAMALSSITVVSNANRLLR 829
Cdd:TIGR01512 490 QAIRLARRTRRIIKQNVVIA-----LGI-ILVLILLALFG-VLPLWLAVLGHEGSTVLVILNALRLLR 550
P-type_ATPase_HM_ZosA_PfeT-like cd07551
P-type heavy metal-transporting ATPase, similar to Bacillus subtilis ZosA/PfeT which ...
285-828 8.67e-134

P-type heavy metal-transporting ATPase, similar to Bacillus subtilis ZosA/PfeT which transports copper, and perhaps zinc under oxidative stress, and perhaps ferrous iron; Bacillus subtilis ZosA/PfeT (previously known as YkvW) transports copper, it may also transport zinc under oxidative stress and may also be involved in ferrous iron efflux. ZosA/PfeT is expressed under the regulation of the peroxide-sensing repressor PerR. It is involved in competence development. Disruption of the zosA/pfeT gene results in low transformability. 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: 319849 [Multi-domain]  Cd Length: 611  Bit Score: 411.64  E-value: 8.67e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 285 YYEASAMIIGLINLGHMLEARARQRSSKALEKLLDLTPPTARLVTDEG-EKSVPLAEVQPGMLLRLTTGDRVPVDGEITQ 363
Cdd:cd07551  74 YWAEGALLIFIFSLSHALEDYAMGRSKRAITALMQLAPETARRIQRDGeIEEVPVEELQIGDRVQVRPGERVPADGVILS 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 364 GEAWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAVFVPV 443
Cdd:cd07551 154 GSSSIDEASITGESIPVEKTPGDEVFAGTINGSGALTVRVTKLSSDTVFAKIVQLVEEAQSEKSPTQSFIERFERIYVKG 233
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 444 VVVIALVSAAIWYFFGPAPQIVyTLVIATTVLIIACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFD 523
Cdd:cd07551 234 VLLAVLLLLLLPPFLLGWTWAD-SFYRAMVFLVVASPCALVASTPPATLSAIANAARQGVLFKGGVHLENLGSVKAIAFD 312
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 524 KTGTLTEGKPQVVAVKTFADVDEAQALRLAAALEQGSSHPLARAILDKAGDMQ--LPQVNGFRTLRGLGVSGEAEGHALL 601
Cdd:cd07551 313 KTGTLTEGKPRVTDVIPAEGVDEEELLQVAAAAESQSEHPLAQAIVRYAEERGipRLPAIEVEAVTGKGVTATVDGQTYR 392
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 602 LGNQALLneQQVGTKAIEAEITAQA-SQGATPVLLAVDGKAVALLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTA 680
Cdd:cd07551 393 IGKPGFF--GEVGIPSEAAALAAELeSEGKTVVYVARDDQVVGLIALMDTPRPEAKEAIAALRLGGIKTIMLTGDNERTA 470
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 681 NAIAKEAGIDEVIAGVLPDGKAEAIKHLQSEGRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGV 760
Cdd:cd07551 471 EAVAKELGIDEVVANLLPEDKVAIIRELQQEYGTVAMVGDGINDAPALANADVGIAMGAGTDVALETADVVLMKDDLSKL 550
                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128468 761 ADALAISRATLHNMKQNllgafIYNSIGIpVAAGILWPFTGTL-LNPVVAGAAMalSSITVVSNANRLL 828
Cdd:cd07551 551 PYAIRLSRKMRRIIKQN-----LIFALAV-IALLIVANLFGLLnLPLGVVGHEG--STLLVILNGLRLL 611
P-type_ATPase_Cd-like cd07545
P-type heavy metal-transporting ATPase, similar to Staphylococcus aureus plasmid pI258 CadA, a ...
220-829 5.04e-133

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.


Pssm-ID: 319845 [Multi-domain]  Cd Length: 599  Bit Score: 409.50  E-value: 5.04e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 220 LVIGLITLAVMVFAGGHFYRSAWKSLLNGAATMDTLVAlgtgVAWLYSMSVNLWPQwfpmearhlyyeaSAMIIGLINLG 299
Cdd:cd07545  10 LVVIALFLASIVLGGYGLFKKGWRNLIRRNFDMKTLMT----IAVIGAALIGEWPE-------------AAMVVFLFAIS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 300 HMLEARARQRSSKALEKLLDLTPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEPIP 379
Cdd:cd07545  73 EALEAYSMDRARRSIRSLMDIAPKTALVRRDGQEREVPVAEVAVGDRMIVRPGERIAMDGIIVRGESSVNQAAITGESLP 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 380 QQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAVFVPVVVVIALVSAAI--WYF 457
Cdd:cd07545 153 VEKGVGDEVFAGTLNGEGALEVRVTKPAEDSTIARIIHLVEEAQAERAPTQAFVDRFARYYTPVVMAIAALVAIVppLFF 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 458 FGPAPQIVYTlviATTVLIIACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQVVA 537
Cdd:cd07545 233 GGAWFTWIYR---GLALLVVACPCALVISTPVSIVSAIGNAARKGVLIKGGVYLEELGRLKTVAFDKTGTLTKGKPVVTD 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 538 VKTFADVDEAQALRLAAALEQGSSHPLARAILDKAGDMQL--PQVNGFRTLRGLGVSGEAEGHALLLGNQALLNEQQV-G 614
Cdd:cd07545 310 VVVLGGQTEKELLAIAAALEYRSEHPLASAIVKKAEQRGLtlSAVEEFTALTGRGVRGVVNGTTYYIGSPRLFEELNLsE 389
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 615 TKAIEAEITAQASQGATPVLLAVDGKAVALLAVRDPLRSDSVAALQRLHKAG-YRLVMLTGDNPTTANAIAKEAGIDEVI 693
Cdd:cd07545 390 SPALEAKLDALQNQGKTVMILGDGERILGVIAVADQVRPSSRNAIAALHQLGiKQTVMLTGDNPQTAQAIAAQVGVSDIR 469
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 694 AGVLPDGKAEAIKHLQSEGRQVAMVGDGINDAPALAQADVGIAMGG-GSDVAIETAAITLMRHSLMGVADALAISRATLH 772
Cdd:cd07545 470 AELLPQDKLDAIEALQAEGGRVAMVGDGVNDAPALAAADVGIAMGAaGTDTALETADIALMGDDLRKLPFAVRLSRKTLA 549
                       570       580       590       600       610       620
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 773 NMKQNllgafIYNSIGIP-VAAGILWPFTGTLLNPVVA--GAamalsSITVVSNANRLLR 829
Cdd:cd07545 550 IIKQN-----IAFALGIKlIALLLVIPGWLTLWMAVFAdmGA-----SLLVTLNSLRLLR 599
P-type_ATPase_HM cd07550
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
225-826 3.44e-128

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 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: 319848 [Multi-domain]  Cd Length: 592  Bit Score: 396.65  E-value: 3.44e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 225 ITLAVMVFAGGHFYRSAWKSLLNGAATMDTLVALGTGVAWLysmsvnlwpqwfpmearHLYYEASAMIIGLINLGHMLEA 304
Cdd:cd07550  19 VRAAVTLAAAFPVLRRALESLKERRLNVDVLDSLAVLLSLL-----------------TGDYLAANTIAFLLELGELLED 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 305 RARQRSSKALEKLLDLTPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEPIPQQKGE 384
Cdd:cd07550  82 YTARKSEKALLDLLSPQERTVWVERDGVEVEVPADEVQPGDTVVVGAGDVIPVDGTVLSGEALIDQASLTGESLPVEKRE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 385 GDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAVFVPVVVviaLVSAAIWYFFGPAPQi 464
Cdd:cd07550 162 GDLVFASTVVEEGQLVIRAERVGRETRAARIAELIEQSPSLKARIQNYAERLADRLVPPTL---GLAGLVYALTGDISR- 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 465 vytlviATTVLIIACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQVVAVKTFAD- 543
Cdd:cd07550 238 ------AAAVLLVDFSCGIRLSTPVAVLSALNHAARHGILVKGGRALELLAKVDTVVFDKTGTLTEGEPEVTAIITFDGr 311
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 544 VDEAQALRLAAALEQGSSHPLARAILDKAGD--MQLPQVNGFRTLRGLGVSGEAEGHALLLGNQALLNEQQVG-TKAIEA 620
Cdd:cd07550 312 LSEEDLLYLAASAEEHFPHPVARAIVREAEErgIEHPEHEEVEYIVGHGIASTVDGKRIRVGSRHFMEEEEIIlIPEVDE 391
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 621 EITAQASQGATPVLLAVDGKAVALLAVRDPLRSDSVAALQRLHKAGY-RLVMLTGDNPTTANAIAKEAGIDEVIAGVLPD 699
Cdd:cd07550 392 LIEDLHAEGKSLLYVAIDGRLIGVIGLSDPLRPEAAEVIARLRALGGkRIIMLTGDHEQRARALAEQLGIDRYHAEALPE 471
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 700 GKAEAIKHLQSEGRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRATLHNMKQNll 779
Cdd:cd07550 472 DKAEIVEKLQAEGRTVAFVGDGINDSPALSYADVGISMRGGTDIARETADVVLLEDDLRGLAEAIELARETMALIKRN-- 549
                       570       580       590       600
                ....*....|....*....|....*....|....*....|....*..
gi 16128468 780 gafiYNSIGIPVAAGILWPFTGtLLNPVVAGAAMALSSITVVSNANR 826
Cdd:cd07550 550 ----IALVVGPNTAVLAGGVFG-LLSPILAAVLHNGTTLLALLNSLR 591
P-type_ATPase_FixI-like cd02092
Rhizobium meliloti FixI and related proteins; belongs to P-type heavy metal-transporting ...
224-827 4.68e-127

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.


Pssm-ID: 319782 [Multi-domain]  Cd Length: 605  Bit Score: 394.03  E-value: 4.68e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 224 LITLAVMVFAGGHFYRSAWKSLLNGAATMDTLVALGTGVAWLYSMSVNLwpqwfpMEARHLYYEASAMIIGLINLGHMLE 303
Cdd:cd02092  33 LIALPAVAYAGRPFFRSAWAALRHGRTNMDVPISIGVLLATGMSLFETL------HGGEHAYFDAAVMLLFFLLIGRYLD 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 304 ARARQRSSKALEKLLDLTPPTARLVTDEGEKS-VPLAEVQPGMLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEPIPQQK 382
Cdd:cd02092 107 HRMRGRARSAAEELAALEARGAQRLQADGSREyVPVAEIRPGDRVLVAAGERIPVDGTVVSGTSELDRSLLTGESAPVTV 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 383 GEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAVFVPVVVVIALVSAAIWYFFGPAP 462
Cdd:cd02092 187 APGDLVQAGAMNLSGPLRLRATAAGDDTLLAEIARLMEAAEQGRSRYVRLADRAARLYAPVVHLLALLTFVGWVAAGGDW 266
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 463 QivYTLVIATTVLIIACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQVVAvktfA 542
Cdd:cd02092 267 R--HALLIAVAVLIITCPCALGLAVPAVQVVASGRLFRRGVLVKDGTALERLAEVDTVVFDKTGTLTLGSPRLVG----A 340
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 543 DVDEAQALRLAAALEQGSSHPLARAILDKAGDMQlPQVNGFRTLRGLGVSGEAEGHALLLGNQALL-NEQQVGTkaieae 621
Cdd:cd02092 341 HAISADLLALAAALAQASRHPLSRALAAAAGARP-VELDDAREVPGRGVEGRIDGARVRLGRPAWLgASAGVST------ 413
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 622 itaqasqgATPVLLAVDGKAVALLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVLPDGK 701
Cdd:cd02092 414 --------ASELALSKGGEEAARFPFEDRPRPDAREAISALRALGLSVEILSGDREPAVRALARALGIEDWRAGLTPAEK 485
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 702 AEAIKHLQSEGRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRATLHNMKQNLLGA 781
Cdd:cd02092 486 VARIEELKAQGRRVLMVGDGLNDAPALAAAHVSMAPASAVDASRSAADIVFLGDSLAPVPEAIEIARRARRLIRQNFALA 565
                       570       580       590       600
                ....*....|....*....|....*....|....*....|....*..
gi 16128468 782 FIYNSIGIPVA-AGilwpftgtLLNPVVAGAAMALSSITVVSNANRL 827
Cdd:cd02092 566 IGYNVIAVPLAiAG--------YVTPLIAALAMSTSSIVVVLNALRL 604
zntA PRK11033
zinc/cadmium/mercury/lead-transporting ATPase; Provisional
87-832 6.58e-118

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


Pssm-ID: 236827 [Multi-domain]  Cd Length: 741  Bit Score: 374.33  E-value: 6.58e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   87 SEALPAATADDDDSQQL--LLSGMSCASCVTRVQNALQSVPGVTQARVNLAERTALVMGSASPQDLV-QAVEKAGYgaea 163
Cdd:PRK11033  39 SSPTLSEDTPLVSGTRYswKVSGMDCPSCARKVENAVRQLAGVNQVQVLFATEKLVVDADNDIRAQVeSAVQKAGF---- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  164 ieddakRRERQQETAVATMKRFRWQ--AIVALAVGIpVMVWGMIGDNMMVTADNRSLWLVIGLITLAvmvfagghfyRSA 241
Cdd:PRK11033 115 ------SLRDEQAAAAAPESRLKSEnlPLITLAVMM-AISWGLEQFNHPFGQLAFIATTLVGLYPIA----------RKA 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  242 WKSLLNGAA----TMDTLVALGTgvawlysmsvnlwpqwfpmearhLYYEAS---AMIIGLINLGHMLEARARQRSSKAL 314
Cdd:PRK11033 178 LRLIRSGSPfaieTLMSVAAIGA-----------------------LFIGATaeaAMVLLLFLIGERLEGYAASRARRGV 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  315 EKLLDLTPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEPIPQQKGEGDSVHAGTVV 394
Cdd:PRK11033 235 SALMALVPETATRLRDGEREEVAIADLRPGDVIEVAAGGRLPADGKLLSPFASFDESALTGESIPVERATGEKVPAGATS 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  395 QDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAVFVPVVVVIALVSAAI--WYFFGPAPQIVYTlviAT 472
Cdd:PRK11033 315 VDRLVTLEVLSEPGASAIDRILHLIEEAEERRAPIERFIDRFSRIYTPAIMLVALLVILVppLLFAAPWQEWIYR---GL 391
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  473 TVLIIACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQVVAVKTFADVDEAQALRL 552
Cdd:PRK11033 392 TLLLIGCPCALVISTPAAITSGLAAAARRGALIKGGAALEQLGRVTTVAFDKTGTLTEGKPQVTDIHPATGISESELLAL 471
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  553 AAALEQGSSHPLARAILDKAGDMQL--PQVNGFRTLRGLGVSGEAEGHALLLGNQALLNEQqvgTKAIEAEITAQASQGA 630
Cdd:PRK11033 472 AAAVEQGSTHPLAQAIVREAQVRGLaiPEAESQRALAGSGIEGQVNGERVLICAPGKLPPL---ADAFAGQINELESAGK 548
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  631 TPVLLAVDGKAVALLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDeVIAGVLPDGKAEAIKHLQS 710
Cdd:PRK11033 549 TVVLVLRNDDVLGLIALQDTLRADARQAISELKALGIKGVMLTGDNPRAAAAIAGELGID-FRAGLLPEDKVKAVTELNQ 627
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  711 EgRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRATLHNMKQN------LLGAFIY 784
Cdd:PRK11033 628 H-APLAMVGDGINDAPAMKAASIGIAMGSGTDVALETADAALTHNRLRGLAQMIELSRATHANIRQNitialgLKAIFLV 706
                        730       740       750       760
                 ....*....|....*....|....*....|....*....|....*....
gi 16128468  785 NSI-GIpvaagilwpfTGTLLNPVVAGAAMALssitVVSNANRLLRFKP 832
Cdd:PRK11033 707 TTLlGI----------TGLWLAVLADSGATAL----VTANALRLLRKRS 741
ATPase_P-type TIGR01494
ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large ...
291-813 3.43e-117

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: 366.26  E-value: 3.43e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   291 MIIGLINLGHMLEARARQRSSKALEKLLD-LTPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPVDGEITQGEAWLD 369
Cdd:TIGR01494   1 FILFLVLLFVLLEVKQKLKAEDALRSLKDsLVNTATVLVLRNGWKEISSKDLVPGDVVLVKSGDTVPADGVLLSGSAFVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   370 EAMLTGEPIPQQK---GEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAVFVPVVVV 446
Cdd:TIGR01494  81 ESSLTGESLPVLKtalPDGDAVFAGTINFGGTLIVKVTATGILTTVGKIAVVVYTGFSTKTPLQSKADKFENFIFILFLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   447 IALVSAAI--WYFFGPAPQIVYTLVIATTVLIIACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFDK 524
Cdd:TIGR01494 161 LLALAVFLllPIGGWDGNSIYKAILRALAVLVIAIPCALPLAVSVALAVGDARMAKKGILVKNLNALEELGKVDVICFDK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   525 TGTLTEGKPQVVAVKTFADVDEAQALRLAAALEQ--GSSHPLARAILDKAGDMQLPQVNGFRT-----------LRGLGV 591
Cdd:TIGR01494 241 TGTLTTNKMTLQKVIIIGGVEEASLALALLAASLeyLSGHPLERAIVKSAEGVIKSDEINVEYkildvfpfssvLKRMGV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   592 ---SGEAEGHALLLGNQALLNEQQVGTKAIEAEITAQASQGATPVLLAVDG-----KAVALLAVRDPLRSDSVAALQRLH 663
Cdd:TIGR01494 321 iveGANGSDLLFVKGAPEFVLERCNNENDYDEKVDEYARQGLRVLAFASKKlpddlEFLGLLTFEDPLRPDAKETIEALR 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   664 KAGYRLVMLTGDNPTTANAIAKEAGIDeVIAGVLPDGKAEAIKHLQSEGRQVAMVGDGINDAPALAQADVGIAMGGGsDV 743
Cdd:TIGR01494 401 KAGIKVVMLTGDNVLTAKAIAKELGID-VFARVKPEEKAAIVEALQEKGRTVAMTGDGVNDAPALKKADVGIAMGSG-DV 478
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   744 AIETAAITLMRHSLMGVADALAISRATLHNMKQNLLGAFIYNSIGIPVAAGiLWPFtgTLLNPVVAGAAM 813
Cdd:TIGR01494 479 AKAAADIVLLDDDLSTIVEAVKEGRKTFSNIKKNIFWAIAYNLILIPLALL-LIVI--ILLPPLLAALAL 545
P-type_ATPase_Pb_Zn_Cd2-like cd07546
P-type heavy metal-transporting ATPase, similar to Escherichia coli ZntA which is selective ...
287-831 3.03e-116

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.


Pssm-ID: 319846 [Multi-domain]  Cd Length: 597  Bit Score: 365.57  E-value: 3.03e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 287 EASAMIIGLINLGHMLEARARQRSSKALEKLLDLTPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPVDGEITQGEA 366
Cdd:cd07546  63 AEAAMVLLLFLVGELLEGYAASRARSGVKALMALVPETALREENGERREVPADSLRPGDVIEVAPGGRLPADGELLSGFA 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 367 WLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAVFVPVVVV 446
Cdd:cd07546 143 SFDESALTGESIPVEKAAGDKVFAGSINVDGVLRIRVTSAPGDNAIDRILHLIEEAEERRAPIERFIDRFSRWYTPAIMA 222
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 447 IALVSAAI--WYFFGPAPQIVYTlviATTVLIIACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFDK 524
Cdd:cd07546 223 VALLVIVVppLLFGADWQTWIYR---GLALLLIGCPCALVISTPAAITSGLAAAARRGALIKGGAALEQLGRVTTVAFDK 299
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 525 TGTLTEGKPQVVAVKTFADVDEAQALRLAAALEQGSSHPLARAILDKAGDMQL--PQVNGFRTLRGLGVSGEAEGHALLL 602
Cdd:cd07546 300 TGTLTRGKPVVTDVVPLTGISEAELLALAAAVEMGSSHPLAQAIVARAQAAGLtiPPAEEARALVGRGIEGQVDGERVLI 379
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 603 GNQALLNEQqvGTKAIEAEITAQASQGATPVLLAVDGKAVALLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANA 682
Cdd:cd07546 380 GAPKFAADR--GTLEVQGRIAALEQAGKTVVVVLANGRVLGLIALRDELRPDAAEAVAELNALGIKALMLTGDNPRAAAA 457
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 683 IAKEAGIDeVIAGVLPDGKAEAIKHLQSEGRqVAMVGDGINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVAD 762
Cdd:cd07546 458 IAAELGLD-FRAGLLPEDKVKAVRELAQHGP-VAMVGDGINDAPAMKAASIGIAMGSGTDVALETADAALTHNRLGGVAA 535
                       490       500       510       520       530       540       550
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128468 763 ALAISRATLHNMKQN------LLGAFIYNSIgipvaAGI--LWPftgtllnpvvagAAMALSSIT--VVSNANRLLRFK 831
Cdd:cd07546 536 MIELSRATLANIRQNitialgLKAVFLVTTL-----LGItgLWL------------AVLADTGATvlVTANALRLLRFR 597
P-type_ATPase_HM cd07544
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
286-808 1.94e-109

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.


Pssm-ID: 319844 [Multi-domain]  Cd Length: 596  Bit Score: 347.77  E-value: 1.94e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 286 YEASAMIIGLINLGHMLEARARQRSSKALEKLLDLTPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPVDGEITQGE 365
Cdd:cd07544  73 YWASLIILLMLTGGEALEDYAQRRASRELTALLDRAPRIAHRLVGGQLEEVPVEEVTVGDRLLVRPGEVVPVDGEVVSGT 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 366 AWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAvfvpVVV 445
Cdd:cd07544 153 ATLDESSLTGESKPVSKRPGDRVMSGAVNGDSALTMVATKLAADSQYAGIVRLVKEAQANPAPFVRLADRYAV----PFT 228
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 446 VIALVSAAIWYFFGPAPqivytlVIATTVLIIACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFDKT 525
Cdd:cd07544 229 LLALAIAGVAWAVSGDP------VRFAAVLVVATPCPLILAAPVAIVSGMSRSSRRGILVKDGGVLEKLARAKTVAFDKT 302
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 526 GTLTEGKPQVVAVKTFADVDEAQALRLAAALEQGSSHPLARAILD--KAGDMQLPQVNGFRTLRGLGVSGEAEGHALLLG 603
Cdd:cd07544 303 GTLTYGQPKVVDVVPAPGVDADEVLRLAASVEQYSSHVLARAIVAaaRERELQLSAVTELTEVPGAGVTGTVDGHEVKVG 382
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 604 NQALlneqqVGTKAIEAEITAQASQGATPVLLAVDGKAVALLAVRDPLRSDSVAALQRLHKAGY-RLVMLTGDNPTTANA 682
Cdd:cd07544 383 KLKF-----VLARGAWAPDIRNRPLGGTAVYVSVDGKYAGAITLRDEVRPEAKETLAHLRKAGVeRLVMLTGDRRSVAEY 457
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 683 IAKEAGIDEVIAGVLPDGKAEAIKHlQSEGRQVAMVGDGINDAPALAQADVGIAMG-GGSDVAIETAAITLMRHSLMGVA 761
Cdd:cd07544 458 IASEVGIDEVRAELLPEDKLAAVKE-APKAGPTIMVGDGVNDAPALAAADVGIAMGaRGSTAASEAADVVILVDDLDRVV 536
                       490       500       510       520
                ....*....|....*....|....*....|....*....|....*...
gi 16128468 762 DALAISRATLHNMKQNLLGAFIYNSIGIPVAA-GILWPFTGTLLNPVV 808
Cdd:cd07544 537 DAVAIARRTRRIALQSVLIGMALSIIGMLIAAfGLIPPVAGALLQEVI 584
P-type_ATPase-Cd_Zn_Co_like cd07548
P-type heavy metal-transporting ATPase, similar to Bacillus subtilis CadA which appears to ...
227-782 6.94e-107

P-type heavy metal-transporting ATPase, similar to Bacillus subtilis CadA which appears to transport cadmium, zinc and cobalt but not copper out of the cell; Bacillus subtilis CadA/YvgW appears to transport cadmium, zinc and cobalt but not copper, out of the cell. Functions in metal ion resistance and cellular metal ion homeostasis. CadA/YvgW is also important for sporulation in B. subtilis, the significant specific expression of the cadA/yvgW gene during the late stage of sporulation, is controlled by forespore-specific sigma factor, sigma G, and mother cell-specific sigma factor, sigma E. This subfamily also includes Helicobacter pylori CadA an essential resistance pump with ion specificity towards Cd(2+), Zn(2+) and Co(2+), and Zn-transporting ATPase, ZiaA(N) in Synechocystis PCC 6803. Transcription of ziaA is induced by Zn under the control of the Zn responsive repressor ZiaR. 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.


Pssm-ID: 319847 [Multi-domain]  Cd Length: 604  Bit Score: 341.14  E-value: 6.94e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 227 LAVMVFAGGHFYRSAWKSLLNGAA-------TMDTLVALGTGVawlYSMSVnlwpqwfpmeARHLYYEAsamiiglinlG 299
Cdd:cd07548  29 LIAYLLIGGDVILKAVRNILKGQFfdenflmSIATLGAFAIGE---YPEAV----------AVMLFYEV----------G 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 300 HMLEARARQRSSKALEKLLDLTPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEPIP 379
Cdd:cd07548  86 ELFQDLAVERSRKSIKALLDIRPDYANLKRNNELKDVKPEEVQIGDIIVVKPGEKIPLDGVVLKGESFLDTSALTGESVP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 380 QQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAVFVPVVVVIALVSAAIWYFFG 459
Cdd:cd07548 166 VEVKEGSSVLAGFINLNGVLEIKVTKPFKDSAVAKILELVENASARKAPTEKFITKFARYYTPIVVFLALLLAVIPPLFS 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 460 PAPQIVYTLVIATTVLIIACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQVVAVK 539
Cdd:cd07548 246 PDGSFSDWIYRALVFLVISCPCALVISIPLGYFGGIGAASRKGILIKGSNYLEALSQVKTVVFDKTGTLTKGVFKVTEIV 325
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 540 TFADVDEAQALRLAAALEQGSSHPLARAILDKAGDM-QLPQVNGFRTLRGLGVSGEAEGHALLLGNQALLNEQQvgtkaI 618
Cdd:cd07548 326 PAPGFSKEELLKLAALAESNSNHPIARSIQKAYGKMiDPSEIEDYEEIAGHGIRAVVDGKEILVGNEKLMEKFN-----I 400
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 619 EAEITAQASqgaTPVLLAVDGKAVALLAVRDPLRSDSVAALQRLHKAGY-RLVMLTGDNPTTANAIAKEAGIDEVIAGVL 697
Cdd:cd07548 401 EHDEDEIEG---TIVHVALDGKYVGYIVISDEIKEDAKEAIKGLKELGIkNLVMLTGDRKSVAEKVAKKLGIDEVYAELL 477
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 698 PDGKAEAIKHLQSEGR-QVAMVGDGINDAPALAQADVGIAMGG-GSDVAIETAAITLMRHSLMGVADALAISRATLHNMK 775
Cdd:cd07548 478 PEDKVEKVEELKAESKgKVAFVGDGINDAPVLARADVGIAMGGlGSDAAIEAADVVLMNDEPSKVAEAIKIARKTRRIVW 557

                ....*..
gi 16128468 776 QNLLGAF 782
Cdd:cd07548 558 QNIILAL 564
P-type_ATPase_HM cd07553
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
219-833 1.18e-102

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.


Pssm-ID: 319851 [Multi-domain]  Cd Length: 610  Bit Score: 330.25  E-value: 1.18e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 219 WLVIGLiTLAVMVFAGGHFYRSAWKSLLNGAATMDTLVALGTGVAWLYSMsVNLWpqwfpMEARHLYYEASAMIIGLINL 298
Cdd:cd07553  31 WLSSAF-ALPSMLYCGSYFYGKAWKSAKQGIPHIDLPIALGIVIGFVVSW-YGLI-----KGDGLVYFDSLSVLVFLMLV 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 299 GHMLEARARQRSSKALEKLlDLTPPTARLVTDEGEKSVPLAE-VQPGMLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEP 377
Cdd:cd07553 104 GRWLQVVTQERNRNRLADS-RLEAPITEIETGSGSRIKTRADqIKSGDVYLVASGQRVPVDGKLLSEQASIDMSWLTGES 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 378 IPQQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAVFVPVVVVIALVSAAIWYF 457
Cdd:cd07553 183 LPRIVERGDKVPAGTSLENQAFEIRVEHSLAESWSGSILQKVEAQEARKTPRDLLADKIIHYFTVIALLIAVAGFGVWLA 262
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 458 FGpapqIVYTLVIATTVLIIACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQVVA 537
Cdd:cd07553 263 ID----LSIALKVFTSVLIVACPCALALATPFTDEIALARLKKKGVLIKNASSLERLSRVRTIVFDKTGTLTRGKSSFVM 338
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 538 VKtfADVDEAQALRLAAALEQGSSHPLARAI---LDKAGDMQLPqVNGFRTLRGLGVSGEAEGHALLLGnqallneqqvg 614
Cdd:cd07553 339 VN--PEGIDRLALRAISAIEAHSRHPISRAIrehLMAKGLIKAG-ASELVEIVGKGVSGNSSGSLWKLG----------- 404
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 615 tKAIEAeitaqASQGATPVLLAVDGKAVALLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGID--EV 692
Cdd:cd07553 405 -SAPDA-----CGIQESGVVIARDGRQLLDLSFNDLLRPDSNREIEELKKGGLSIAILSGDNEEKVRLVGDSLGLDprQL 478
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 693 IAGVLPDGKAEAIKHLQSEgrQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRATLH 772
Cdd:cd07553 479 FGNLSPEEKLAWIESHSPE--NTLMVGDGANDALALASAFVGIAVAGEVGVSLEAADIYYAGNGIGGIRDLLTLSKQTIK 556
                       570       580       590       600       610       620
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128468 773 NMKQNLLGAFIYNSIGIpVAAGILWpftgtlLNPVVAGAAMALSSITVVSNANRLLRFKPK 833
Cdd:cd07553 557 AIKGLFAFSLLYNLVAI-GLALSGW------ISPLVAAILMPLSSITILGIVWAALGFRSK 610
MgtA COG0474
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism];
286-775 4.66e-56

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


Pssm-ID: 440242 [Multi-domain]  Cd Length: 874  Bit Score: 208.04  E-value: 4.66e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 286 YEASAMIIG--LIN--LGHMLEARArqrsSKALEKLLDLTPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPVDGEI 361
Cdd:COG0474  81 WVDAIVILAvvLLNaiIGFVQEYRA----EKALEALKKLLAPTARVLRDGKWVEIPAEELVPGDIVLLEAGDRVPADLRL 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 362 TQGEA-WLDEAMLTGEPIPQQKGE------------GDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKP- 427
Cdd:COG0474 157 LEAKDlQVDESALTGESVPVEKSAdplpedaplgdrGNMVFMGTLVTSGRGTAVVVATGMNTEFGKIAKLLQEAEEEKTp 236
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 428 ---EIGQLADKISAVFVPvvvvIALVSAAIWYFFGPAPQIVYTLVIATTVLIIacPCALglatPMsIIS-----GVGRAA 499
Cdd:COG0474 237 lqkQLDRLGKLLAIIALV----LAALVFLIGLLRGGPLLEALLFAVALAVAAI--PEGL----PA-VVTitlalGAQRMA 305
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 500 EFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQVVAVKTFA---DVDEAQALRL-------------AAALEQGSSHP 563
Cdd:COG0474 306 KRNAIVRRLPAVETLGSVTVICTDKTGTLTQNKMTVERVYTGGgtyEVTGEFDPALeellraaalcsdaQLEEETGLGDP 385
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 564 LARAILDKAGDMQLPQVNGFRTLRGLG-------------VSGEAEGHALLL------------------GNQALLNEQQ 612
Cdd:COG0474 386 TEGALLVAAAKAGLDVEELRKEYPRVDeipfdserkrmstVHEDPDGKRLLIvkgapevvlalctrvltgGGVVPLTEED 465
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 613 VgtKAIEAEITAQASQG------------ATPVLLAVDGKA----VALLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDN 676
Cdd:COG0474 466 R--AEILEAVEELAAQGlrvlavaykelpADPELDSEDDESdltfLGLVGMIDPPRPEAKEAIAECRRAGIRVKMITGDH 543
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 677 PTTANAIAKEAGIDE---------------------------VIAGVLPDGKAEAIKHLQSEGRQVAMVGDGINDAPALA 729
Cdd:COG0474 544 PATARAIARQLGLGDdgdrvltgaeldamsdeelaeavedvdVFARVSPEHKLRIVKALQANGHVVAMTGDGVNDAPALK 623
                       570       580       590       600
                ....*....|....*....|....*....|....*....|....*..
gi 16128468 730 QADVGIAMG-GGSDVAIETAAITLMRHSLMGVADALAISRATLHNMK 775
Cdd:COG0474 624 AADIGIAMGiTGTDVAKEAADIVLLDDNFATIVAAVEEGRRIYDNIR 670
P-type_ATPase cd02609
uncharacterized subfamily of P-type ATPase transporter, similar to uncharacterized ...
291-774 3.28e-51

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.


Pssm-ID: 319795 [Multi-domain]  Cd Length: 661  Bit Score: 190.57  E-value: 3.28e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 291 MIIGLINlghmlEARARqrssKALEKLLDLTPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPVDGEITQG-EAWLD 369
Cdd:cd02609  69 TVIGIVQ-----EIRAK----RQLDKLSILNAPKVTVIRDGQEVKIPPEELVLDDILILKPGEQIPADGEVVEGgGLEVD 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 370 EAMLTGEPIPQQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAVFVPVVVVIAL 449
Cdd:cd02609 140 ESLLTGESDLIPKKAGDKLLSGSFVVSGAAYARVTAVGAESYAAKLTLEAKKHKLINSELLNSINKILKFTSFIIIPLGL 219
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 450 VSAAIWYFFGPAPQivYTLVIAT-TVLIIACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTL 528
Cdd:cd02609 220 LLFVEALFRRGGGW--RQAVVSTvAALLGMIPEGLVLLTSVALAVGAIRLAKKKVLVQELYSIETLARVDVLCLDKTGTI 297
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 529 TEGKPQVVAVKTF--ADVDEAQALRLAAALEQGSSHPLARAILDK-AGDMQLPQVN--GFRTLRGLGVSGEAEGHALLLG 603
Cdd:cd02609 298 TEGKMKVERVEPLdeANEAEAAAALAAFVAASEDNNATMQAIRAAfFGNNRFEVTSiiPFSSARKWSAVEFRDGGTWVLG 377
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 604 N-QALLNEQQvgtKAIEAEITAQASQGATPVLLA------------VDGKAVALLAVRDPLRSDSVAALQRLHKAGYRLV 670
Cdd:cd02609 378 ApEVLLGDLP---SEVLSRVNELAAQGYRVLLLArsagaltheqlpVGLEPLALILLTDPIRPEAKETLAYFAEQGVAVK 454
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 671 MLTGDNPTTANAIAKEAGID------------------------EVIAGVLPDGKAEAIKHLQSEGRQVAMVGDGINDAP 726
Cdd:cd02609 455 VISGDNPVTVSAIAKRAGLEgaesyidastlttdeelaeavenyTVFGRVTPEQKRQLVQALQALGHTVAMTGDGVNDVL 534
                       490       500       510       520
                ....*....|....*....|....*....|....*....|....*...
gi 16128468 727 ALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRATLHNM 774
Cdd:cd02609 535 ALKEADCSIAMASGSDATRQVAQVVLLDSDFSALPDVVFEGRRVVNNI 582
E1-E2_ATPase pfam00122
E1-E2 ATPase;
319-499 3.73e-51

E1-E2 ATPase;


Pssm-ID: 425475 [Multi-domain]  Cd Length: 181  Bit Score: 176.99  E-value: 3.73e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   319 DLTPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGS 398
Cdd:pfam00122   1 SLLPPTATVLRDGTEEEVPADELVPGDIVLLKPGERVPADGRIVEGSASVDESLLTGESLPVEKKKGDMVYSGTVVVSGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   399 VLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAVFVPVVVVIALVSAAIWYFFGPAPQivYTLVIATTVLIIA 478
Cdd:pfam00122  81 AKAVVTATGEDTELGRIARLVEEAKSKKTPLQRLLDRLGKYFSPVVLLIALAVFLLWLFVGGPPL--RALLRALAVLVAA 158
                         170       180
                  ....*....|....*....|.
gi 16128468   479 CPCALGLATPMSIISGVGRAA 499
Cdd:pfam00122 159 CPCALPLATPLALAVGARRLA 179
kdpB TIGR01497
K+-transporting ATPase, B subunit; This model describes the P-type ATPase subunit of the ...
246-748 1.69e-50

K+-transporting ATPase, B subunit; This model describes the P-type ATPase subunit of the complex responsible for translocating potassium ions across biological membranes in microbes. In E. coli and other species, this complex consists of the proteins KdpA, KdpB, KdpC and KdpF. KdpB is the ATPase subunit, while KdpA is the potassium-ion translocating subunit. The function of KdpC is unclear, although cit has been suggested to couple the ATPase subunit to the ion-translocating subunit, while KdpF serves to stabilize the complex. The potassium P-type ATPases have been characterized as Type IA based on a phylogenetic analysis which places this clade closest to the heavy-metal translocating ATPases (Type IB). Others place this clade closer to the Na+/K+ antiporter type (Type IIC) based on physical characteristics. This model is very clear-cut, with a strong break between trusted hits and noise. All members of the seed alignment, from Clostridium, Anabaena and E. coli are in the characterized table. One sequence above trusted, OMNI|NTL01TA01282, is apparently mis-annotated in the primary literature, but properly annotated by TIGR. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 130561 [Multi-domain]  Cd Length: 675  Bit Score: 188.94  E-value: 1.69e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   246 LNGAATMDTLVALGTGVAWLYSMSVNLWPQWFPMEARHL-YYEASAMIIGLINL--GHMLEARARQRSSKALEKLLDLTP 322
Cdd:TIGR01497  24 LNPKAQWRNPVMFIVWVGSLLTTCITIAPASFGMPGNNLaLFNAIITGILFITVlfANFAEAVAEGRGKAQADSLKGTKK 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   323 PT-ARLVTDEGE-KSVPLAEVQPGMLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEPIPQQKGEGD---SVHAGTVVQDG 397
Cdd:TIGR01497 104 TTfAKLLRDDGAiDKVPADQLKKGDIVLVEAGDVIPCDGEVIEGVASVDESAITGESAPVIKESGGdfaSVTGGTRILSD 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   398 SVLFRASAVGSHTTLSRIIRMVRQAQSSKP--EIGqladkISAVFVPVVVVIALVSAAIWYF--FGPAPQIVYTLVIATT 473
Cdd:TIGR01497 184 WLVVECTANPGETFLDRMIALVEGAQRRKTpnEIA-----LTILLIALTLVFLLVTATLWPFaaYGGNAISVTVLVALLV 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   474 VLIiacPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQVVAVKTFADVDEAQALRLA 553
Cdd:TIGR01497 259 CLI---PTTIGGLLSAIGIAGMDRVLGFNVIATSGRAVEACGDVDTLLLDKTGTITLGNRLASEFIPAQGVDEKTLADAA 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   554 AALEQGSSHPLARAILDKAGDMQLP-QVNGFRTLRGLGVSGEAEGHALLLGNQALLNEQQVG-------------TKAIE 619
Cdd:TIGR01497 336 QLASLADDTPEGKSIVILAKQLGIReDDVQSLHATFVEFTAQTRMSGINLDNGRMIRKGAVDaikrhveangghiPTDLD 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   620 AEITAQASQGATPVLLAVDGKAVALLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVLPD 699
Cdd:TIGR01497 416 QAVDQVARQGGTPLVVCEDNRIYGVIYLKDIVKGGIKERFAQLRKMGIKTIMITGDNRLTAAAIAAEAGVDDFIAEATPE 495
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 16128468   700 GKAEAIKHLQSEGRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETA 748
Cdd:TIGR01497 496 DKIALIRQEQAEGKLVAMTGDGTNDAPALAQADVGVAMNSGTQAAKEAA 544
P-type_ATPase_K cd02078
potassium-transporting ATPase ATP-binding subunit, KdpB, a subunit of the prokaryotic ...
326-748 1.32e-49

potassium-transporting ATPase ATP-binding subunit, KdpB, a subunit of the prokaryotic high-affinity potassium uptake system KdpFABC; similar to Escherichia coli KdpB; KdpFABC is a prokaryotic high-affinity potassium uptake system. It is expressed under K(+) limiting conditions when the other potassium transport systems are not able to provide a sufficient flow of K(+) into the bacteria. The KdpB subunit represents the catalytic subunit performing ATP hydrolysis. KdpB is comprised of four domains: the transmembrane domain, the nucleotide-binding domain, the phosphorylation domain, and the actuator domain. 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: 319773 [Multi-domain]  Cd Length: 667  Bit Score: 186.31  E-value: 1.32e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 326 RLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEPIPQQKGEGD---SVHAGTVVQDGSVLFR 402
Cdd:cd02078  99 RLRNDGKIEKVPATDLKKGDIVLVEAGDIIPADGEVIEGVASVDESAITGESAPVIRESGGdrsSVTGGTKVLSDRIKVR 178
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 403 ASAVGSHTTLSRIIRMVRQAQSSKP--EIGqladkISAVFVPVVVVIALVSAAIWYF--FGPAPQIVYTLVIATTVLIia 478
Cdd:cd02078 179 ITANPGETFLDRMIALVEGASRQKTpnEIA-----LTILLVGLTLIFLIVVATLPPFaeYSGAPVSVTVLVALLVCLI-- 251
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 479 cPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQVVAVKTFADVDEAQALRLAAALEQ 558
Cdd:cd02078 252 -PTTIGGLLSAIGIAGMDRLLRFNVIAKSGRAVEAAGDVDTLLLDKTGTITLGNRQATEFIPVGGVDEKELADAAQLASL 330
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 559 GSSHPLARAILD---------KAGDMQLPQVNGF--------------RTLRGlGVSGEAEGHALLLGNQAllneqqvgT 615
Cdd:cd02078 331 ADETPEGRSIVIlakqlggteRDLDLSGAEFIPFsaetrmsgvdlpdgTEIRK-GAVDAIRKYVRSLGGSI--------P 401
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 616 KAIEAEITAQASQGATPVLLAVDGKAVALLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAG 695
Cdd:cd02078 402 EELEAIVEEISKQGGTPLVVAEDDRVLGVIYLKDIIKPGIKERFAELRKMGIKTVMITGDNPLTAAAIAAEAGVDDFLAE 481
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|...
gi 16128468 696 VLPDGKAEAIKHLQSEGRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETA 748
Cdd:cd02078 482 AKPEDKLELIRKEQAKGKLVAMTGDGTNDAPALAQADVGVAMNSGTQAAKEAG 534
P-type_ATPase cd07539
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ...
289-775 2.78e-49

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: 184.54  E-value: 2.78e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 289 SAMIIGLINLGHMLEARARQRSSKALEKLLDLTPPTARLVTDEG--EKSVPLAEVQPGMLLRLTTGDRVPVDGEITQGEA 366
Cdd:cd07539  60 AVLIVGVLTVNAVIGGVQRLRAERALAALLAQQQQPARVVRAPAgrTQTVPAESLVPGDVIELRAGEVVPADARLLEADD 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 367 W-LDEAMLTGEPIPQQK----------GE-GDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLAD 434
Cdd:cd07539 140 LeVDESALTGESLPVDKqvaptpgaplADrACMLYEGTTVVSGQGRAVVVATGPHTEAGRAQSLVAPVETATGVQAQLRE 219
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 435 KISAVFVPVVVVIALVSAAIWYFFGPAPQivyTLVIATTVLIIACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRA 514
Cdd:cd07539 220 LTSQLLPLSLGGGAAVTGLGLLRGAPLRQ---AVADGVSLAVAAVPEGLPLVATLAQLAAARRLSRRGVLVRSPRTVEAL 296
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 515 STLDTVVFDKTGTLTEGKPQVVAVKTFADVDEAQALRLAAALEQGSSHPLARAILDKAGDMQLPQVNGFRTLRGLGVSGE 594
Cdd:cd07539 297 GRVDTICFDKTGTLTENRLRVVQVRPPLAELPFESSRGYAAAIGRTGGGIPLLAVKGAPEVVLPRCDRRMTGGQVVPLTE 376
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 595 AEGHALLLGNQALLNEqqvGTKAIE-AEITAQASQGATPVLLAVDGKAVALLAVRDPLRSDSVAALQRLHKAGYRLVMLT 673
Cdd:cd07539 377 ADRQAIEEVNELLAGQ---GLRVLAvAYRTLDAGTTHAVEAVVDDLELLGLLGLADTARPGAAALIAALHDAGIDVVMIT 453
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 674 GDNPTTANAIAKEAGIDE--------------------------VIAGVLPDGKAEAIKHLQSEGRQVAMVGDGINDAPA 727
Cdd:cd07539 454 GDHPITARAIAKELGLPRdaevvtgaeldaldeealtglvadidVFARVSPEQKLQIVQALQAAGRVVAMTGDGANDAAA 533
                       490       500       510       520
                ....*....|....*....|....*....|....*....|....*....
gi 16128468 728 LAQADVGIAMG-GGSDVAIETAAITLMRHSLMGVADALAISRATLHNMK 775
Cdd:cd07539 534 IRAADVGIGVGaRGSDAAREAADLVLTDDDLETLLDAVVEGRTMWQNVR 582
P-type_ATPases cd01431
ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, ...
519-827 1.55e-48

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: 174.56  E-value: 1.55e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 519 TVVFDKTGTLTEGKPQVV----AVKTFADVDEAQALRLAAAleqgsshPLARAILDKAGDMQLPQVNGFRTLrglgvsge 594
Cdd:cd01431   1 VICSDKTGTLTKNGMTVTklfiEEIPFNSTRKRMSVVVRLP-------GRYRAIVKGAPETILSRCSHALTE-------- 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 595 aEGHALLLGNQALLNEQQVGTKAIEAEITAQASQGATPVLlavDGKAVALLAVRDPLRSDSVAALQRLHKAGYRLVMLTG 674
Cdd:cd01431  66 -EDRNKIEKAQEESAREGLRVLALAYREFDPETSKEAVEL---NLVFLGLIGLQDPPRPEVKEAIAKCRTAGIKVVMITG 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 675 DNPTTANAIAKEAGID---------------------------EVIAGVLPDGKAEAIKHLQSEGRQVAMVGDGINDAPA 727
Cdd:cd01431 142 DNPLTAIAIAREIGIDtkasgvilgeeademseeelldliakvAVFARVTPEQKLRIVKALQARGEVVAMTGDGVNDAPA 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 728 LAQADVGIAMGG-GSDVAIETAAITLMRHSLMGVADALAISRATLHNMKQNLLGAFIYNSIGIPVAAGILwpFTGTLLnP 806
Cdd:cd01431 222 LKQADVGIAMGStGTDVAKEAADIVLLDDNFATIVEAVEEGRAIYDNIKKNITYLLANNVAEVFAIALAL--FLGGPL-P 298
                       330       340
                ....*....|....*....|.
gi 16128468 807 VVAGAAMALSSITVVSNANRL 827
Cdd:cd01431 299 LLAFQILWINLVTDLIPALAL 319
P-type_ATPase cd07538
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ...
287-821 1.71e-47

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: 179.95  E-value: 1.71e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 287 EASAMIIGLInLGHMLEARARQRSSKALEKLLDLTPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPVDGEITQGEA 366
Cdd:cd07538  58 EGLILLIFVV-VIIAIEVVQEWRTERALEALKNLSSPRATVIRDGRERRIPSRELVPGDLLILGEGERIPADGRLLENDD 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 367 W-LDEAMLTGEPIPQQKGEGDS------------VHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLA 433
Cdd:cd07538 137 LgVDESTLTGESVPVWKRIDGKamsapggwdknfCYAGTLVVRGRGVAKVEATGSRTELGKIGKSLAEMDDEPTPLQKQT 216
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 434 DKISAVFVPVVVVI-ALVSAAIWYFFGPAPQ-IVYTLVIATTVLIIACPCALGLATPMsiisGVGRAAEFGVLVRDADAL 511
Cdd:cd07538 217 GRLVKLCALAALVFcALIVAVYGVTRGDWIQaILAGITLAMAMIPEEFPVILTVFMAM----GAWRLAKKNVLVRRAAAV 292
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 512 QRASTLDTVVFDKTGTLTEGKPQVVAVKTFAdvdeaqalrlaaaleqgSSHPLaRAILDKAGDMQLPQVNGFRTLRGlgv 591
Cdd:cd07538 293 ETLGSITVLCVDKTGTLTKNQMEVVELTSLV-----------------REYPL-RPELRMMGQVWKRPEGAFAAAKG--- 351
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 592 SGEAeghallLGNQALLNEQQVgtKAIEAEITAQASQGATpvLLAVDGKA-----------------VALLAVRDPLRSD 654
Cdd:cd07538 352 SPEA------IIRLCRLNPDEK--AAIEDAVSEMAGEGLR--VLAVAACRidesflpddledavfifVGLIGLADPLRED 421
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 655 SVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDE--------------------------VIAGVLPDGKAEAIKHL 708
Cdd:cd07538 422 VPEAVRICCEAGIRVVMITGDNPATAKAIAKQIGLDNtdnvitgqeldamsdeelaekvrdvnIFARVVPEQKLRIVQAF 501
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 709 QSEGRQVAMVGDGINDAPALAQADVGIAMGG-GSDVAIETAAITLMRHSLMGVADALAISRATLHNMKQNLlgAFIYnSI 787
Cdd:cd07538 502 KANGEIVAMTGDGVNDAPALKAAHIGIAMGKrGTDVAREASDIVLLDDNFSSIVSTIRLGRRIYDNLKKAI--TYVF-AI 578
                       570       580       590
                ....*....|....*....|....*....|....
gi 16128468 788 GIPVAagilwpftGTLLNPVVAGAAMALSSITVV 821
Cdd:cd07538 579 HVPIA--------GLALLPPLLGLPPLLFPVHVV 604
P-type_ATPase_H cd02076
plant and fungal plasma membrane H(+)-ATPases, and related bacterial and archaeal putative H(+) ...
289-816 6.85e-45

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: 173.57  E-value: 6.85e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 289 SAMIIGLINL----GHMLEARARqrssKALEKLLDLTPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPVDGEITQG 364
Cdd:cd02076  58 FAIILLLLLInagiGFIEERQAG----NAVAALKKSLAPKARVLRDGQWQEIDAKELVPGDIVSLKIGDIVPADARLLTG 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 365 EAW-LDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSsKPEIGQLADKISavFVPV 443
Cdd:cd02076 134 DALqVDQSALTGESLPVTKHPGDEAYSGSIVKQGEMLAVVTATGSNTFFGKTAALVASAEE-QGHLQKVLNKIG--NFLI 210
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 444 VVVIALVSAAIWYFFGPAPQIVYTLVIATTVLIIACPCALG--LATPMSIisGVGRAAEFGVLVRDADALQRASTLDTVV 521
Cdd:cd02076 211 LLALILVLIIVIVALYRHDPFLEILQFVLVLLIASIPVAMPavLTVTMAV--GALELAKKKAIVSRLSAIEELAGVDILC 288
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 522 FDKTGTLTE-----GKPQVVAVKTFADVdeaqALRLAAALEQGSSHPLARAILdKAGDMQLPQVNGFRTL---------- 586
Cdd:cd02076 289 SDKTGTLTLnklslDEPYSLEGDGKDEL----LLLAALASDTENPDAIDTAIL-NALDDYKPDLAGYKQLkftpfdpvdk 363
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 587 --RGLGVSGEAEGHALLLGNQ----ALLNEQQVGTKAIEAEITAQASQG--ATPVLLAVDGKA---VALLAVRDPLRSDS 655
Cdd:cd02076 364 rtEATVEDPDGERFKVTKGAPqvilELVGNDEAIRQAVEEKIDELASRGyrSLGVARKEDGGRwelLGLLPLFDPPRPDS 443
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 656 VAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVI------------------------------AGVLPDGKAEAI 705
Cdd:cd02076 444 KATIARAKELGVRVKMITGDQLAIAKETARQLGMGTNIlsaerlklggggggmpgseliefiedadgfAEVFPEHKYRIV 523
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 706 KHLQSEGRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRATLHNMKQNL------- 778
Cdd:cd02076 524 EALQQRGHLVGMTGDGVNDAPALKKADVGIAVSGATDAARAAADIVLTAPGLSVIIDAIKTSRQIFQRMKSYViyriaet 603
                       570       580       590       600
                ....*....|....*....|....*....|....*....|....*.
gi 16128468 779 --------LGAFIYNSIGIPVAAGILWpftgTLLNpvvAGAAMALS 816
Cdd:cd02076 604 lrilvfftLGILILNFYPLPLIMIVLI----AILN---DGATLTIA 642
P-type_ATPase_Ca_prok cd02089
prokaryotic P-type Ca(2+)-ATPase similar to Synechococcus elongatus sp. strain PCC 7942 PacL ...
288-752 1.53e-42

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: 165.48  E-value: 1.53e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 288 ASAMIIGLI---N--LGHMLEARARqrssKALEKLLDLTPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPVDGEIT 362
Cdd:cd02089  57 VDAIVIIAIvilNavLGFVQEYKAE----KALAALKKMSAPTAKVLRDGKKQEIPARELVPGDIVLLEAGDYVPADGRLI 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 363 QGEAW-LDEAMLTGEPIPQQK----------GEGDS---VHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPE 428
Cdd:cd02089 133 ESASLrVEESSLTGESEPVEKdadtlleedvPLGDRknmVFSGTLVTYGRGRAVVTATGMNTEMGKIATLLEETEEEKTP 212
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 429 IGQLADKISAVFVPVVVVIALVSAAIWYFFGPAPQIVYTLVIATTVLIIacPCALGLATPMSIISGVGRAAEFGVLVRDA 508
Cdd:cd02089 213 LQKRLDQLGKRLAIAALIICALVFALGLLRGEDLLDMLLTAVSLAVAAI--PEGLPAIVTIVLALGVQRMAKRNAIIRKL 290
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 509 DALQRASTLDTVVFDKTGTLTEGKPQVVAVKTFADvdeaqaLRLAAALEQGSSHPLARAILDKAGDMQ--LP-------- 578
Cdd:cd02089 291 PAVETLGSVSVICSDKTGTLTQNKMTVEKIYTIGD------PTETALIRAARKAGLDKEELEKKYPRIaeIPfdserklm 364
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 579 -QVNGFRTLRGLGVSGEAE------GHALLLGNQALLNEQQVgtKAIEAEITAQASQG------------ATPVLLAVDG 639
Cdd:cd02089 365 tTVHKDAGKYIVFTKGAPDvllprcTYIYINGQVRPLTEEDR--AKILAVNEEFSEEAlrvlavaykpldEDPTESSEDL 442
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 640 KA----VALLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGI----DEVIAG---------------- 695
Cdd:cd02089 443 ENdlifLGLVGMIDPPRPEVKDAVAECKKAGIKTVMITGDHKLTARAIAKELGIledgDKALTGeeldkmsdeelekkve 522
                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128468 696 -------VLPDGKAEAIKHLQSEGRQVAMVGDGINDAPALAQADVGIAMG-GGSDVAIETAAITL 752
Cdd:cd02089 523 qisvyarVSPEHKLRIVKALQRKGKIVAMTGDGVNDAPALKAADIGVAMGiTGTDVAKEAADMIL 587
P-type_ATPase_Mg cd02077
magnesium transporting ATPase (MgtA), similar to Escherichia coli MgtA and Salmonella ...
291-774 3.17e-39

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.


Pssm-ID: 319772 [Multi-domain]  Cd Length: 768  Bit Score: 156.25  E-value: 3.17e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 291 MIIGLINLGHMLEARarqrSSKALEKLLDLTPPTARLVTDE-GEKSVPLAEVQPGMLLRLTTGDRVPVDGEITQGEA-WL 368
Cdd:cd02077  73 MVLISGLLDFIQEIR----SLKAAEKLKKMVKNTATVIRDGsKYMEIPIDELVPGDIVYLSAGDMIPADVRIIQSKDlFV 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 369 DEAMLTGEPIPQQKGEGDSVHA-------------GTVVQDGSVLFRASAVGSHTTLSRI-IRMVRQAQSSKPEIGqlad 434
Cdd:cd02077 149 SQSSLTGESEPVEKHATAKKTKdesilelenicfmGTNVVSGSALAVVIATGNDTYFGSIaKSITEKRPETSFDKG---- 224
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 435 kisavfvpvvvvIALVSaaiWYFfgpapqIVYTLVIATTVLII--------------ACPCALGL---ATPMsIIS---- 493
Cdd:cd02077 225 ------------INKVS---KLL------IRFMLVMVPVVFLIngltkgdwleallfALAVAVGLtpeMLPM-IVTsnla 282
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 494 -GVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKpqvVAVKTFADVDEAQALRLAAALEQGSSH------PLAR 566
Cdd:cd02077 283 kGAVRMSKRKVIVKNLNAIQNFGAMDILCTDKTGTLTQDK---IVLERHLDVNGKESERVLRLAYLNSYFqtglknLLDK 359
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 567 AILDKAGDMQLPQ-----------------------VNGFRTLRGLGVSGEAEG------HALLLGNQALLNEQQvgTKA 617
Cdd:cd02077 360 AIIDHAEEANANGliqdytkideipfdferrrmsvvVKDNDGKHLLITKGAVEEilnvctHVEVNGEVVPLTDTL--REK 437
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 618 IEAEITAQASQGATPVLLAV-------------DGKAVAL---LAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTAN 681
Cdd:cd02077 438 ILAQVEELNREGLRVLAIAYkklpapegeysvkDEKELILigfLAFLDPPKESAAQAIKALKKNGVNVKILTGDNEIVTK 517
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 682 AIAKEAGID--EVIAG-----------------------VLPDGKAEAIKHLQSEGRQVAMVGDGINDAPALAQADVGIA 736
Cdd:cd02077 518 AICKQVGLDinRVLTGseiealsdeelakiveetnifakLSPLQKARIIQALKKNGHVVGFMGDGINDAPALRQADVGIS 597
                       570       580       590
                ....*....|....*....|....*....|....*...
gi 16128468 737 MGGGSDVAIETAAITLMRHSLMGVADALAISRATLHNM 774
Cdd:cd02077 598 VDSAVDIAKEAADIILLEKDLMVLEEGVIEGRKTFGNI 635
P-type_ATPase_cation cd02080
P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, ...
289-753 1.50e-38

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: 154.34  E-value: 1.50e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 289 SAMIIG--LIN--LGHMLEARArqrsSKALEKLLDLTPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPVDGE-ITQ 363
Cdd:cd02080  59 AIVIFGvvLINaiIGYIQEGKA----EKALAAIKNMLSPEATVLRDGKKLTIDAEELVPGDIVLLEAGDKVPADLRlIEA 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 364 GEAWLDEAMLTGEPIPQQKGEG----DSVHA--------GTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSK-Peig 430
Cdd:cd02080 135 RNLQIDESALTGESVPVEKQEGpleeDTPLGdrknmaysGTLVTAGSATGVVVATGADTEIGRINQLLAEVEQLAtP--- 211
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 431 qLADKISAVFVPVVVVIaLVSAAIWYFFG------PAPQIvYTLVIATTVLIIAcpcaLGLATPMSII--SGVGRAAEFG 502
Cdd:cd02080 212 -LTRQIAKFSKALLIVI-LVLAALTFVFGllrgdySLVEL-FMAVVALAVAAIP----EGLPAVITITlaIGVQRMAKRN 284
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 503 VLVRDADALQRASTLDTVVFDKTGTLTEGKPQVVAVKTFADvDEAQALRLAAALEQGSshPLARAILDKAGDMQLPQVNG 582
Cdd:cd02080 285 AIIRRLPAVETLGSVTVICSDKTGTLTRNEMTVQAIVTLCN-DAQLHQEDGHWKITGD--PTEGALLVLAAKAGLDPDRL 361
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 583 FRTLRGLG------------------------VSGEAEgHALLLGNQALLNEQQVG--TKAIEAEITAQASQGATpvLLA 636
Cdd:cd02080 362 ASSYPRVDkipfdsayrymatlhrddgqrviyVKGAPE-RLLDMCDQELLDGGVSPldRAYWEAEAEDLAKQGLR--VLA 438
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 637 VDGKAVA-------------------LLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGI-------- 689
Cdd:cd02080 439 FAYREVDseveeidhadleggltflgLQGMIDPPRPEAIAAVAECQSAGIRVKMITGDHAETARAIGAQLGLgdgkkvlt 518
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 690 --------DE----------VIAGVLPDGKAEAIKHLQSEGRQVAMVGDGINDAPALAQADVGIAMG-GGSDVAIETAAI 750
Cdd:cd02080 519 gaeldaldDEelaeavdevdVFARTSPEHKLRLVRALQARGEVVAMTGDGVNDAPALKQADIGIAMGiKGTEVAKEAADM 598

                ...
gi 16128468 751 TLM 753
Cdd:cd02080 599 VLA 601
PRK14010 PRK14010
K(+)-transporting ATPase subunit B;
262-771 1.25e-36

K(+)-transporting ATPase subunit B;


Pssm-ID: 184448 [Multi-domain]  Cd Length: 673  Bit Score: 147.54  E-value: 1.25e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  262 VAWLYSMSVNLWPQWFPMEARHLYYEASAMIIGLINL--GHMLEARARQRSsKALEKLLDLTPP--TARLVTDEGE-KSV 336
Cdd:PRK14010  40 VGMLLALGLTIYPDLFHQESVSRLYVFSIFIILLLTLvfANFSEALAEGRG-KAQANALRQTQTemKARRIKQDGSyEMI 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  337 PLAEVQPGMLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEPIP---QQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLS 413
Cdd:PRK14010 119 DASDLKKGHIVRVATGEQIPNDGKVIKGLATVDESAITGESAPvikESGGDFDNVIGGTSVASDWLEVEITSEPGHSFLD 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  414 RIIRMVRQAQSSKPeigqlADKISAVFVPVVVVIALVsAAIWYFFGPAPQIVYTLVIATTVLIIAC--PCALGLATPMSI 491
Cdd:PRK14010 199 KMIGLVEGATRKKT-----PNEIALFTLLMTLTIIFL-VVILTMYPLAKFLNFNLSIAMLIALAVCliPTTIGGLLSAIG 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  492 ISGVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQVVAVKTFADVDEAQALRLAAALEQGSSHPLARAI--L 569
Cdd:PRK14010 273 IAGMDRVTQFNILAKSGRSVETCGDVNVLILDKTGTITYGNRMADAFIPVKSSSFERLVKAAYESSIADDTPEGRSIvkL 352
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  570 DKAGDMQLPQVNG-----FRTLRGLGVSGEAEGHALLLGNQALLNEQQVG---TKAIEAEITAQASQGATPVLLAVDGKA 641
Cdd:PRK14010 353 AYKQHIDLPQEVGeyipfTAETRMSGVKFTTREVYKGAPNSMVKRVKEAGghiPVDLDALVKGVSKKGGTPLVVLEDNEI 432
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  642 VALLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVLPDGKAEAIKHLQSEGRQVAMVGDG 721
Cdd:PRK14010 433 LGVIYLKDVIKDGLVERFRELREMGIETVMCTGDNELTAATIAKEAGVDRFVAECKPEDKINVIREEQAKGHIVAMTGDG 512
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 16128468  722 INDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRATL 771
Cdd:PRK14010 513 TNDAPALAEANVGLAMNSGTMSAKEAANLIDLDSNPTKLMEVVLIGKQLL 562
P-type_ATPase_Ca_PMCA-like cd02081
animal plasma membrane Ca2(+)-ATPases (PMCA), similar to human ATP2B1-4/PMCA1-4, and related ...
332-753 2.83e-36

animal plasma membrane Ca2(+)-ATPases (PMCA), similar to human ATP2B1-4/PMCA1-4, and related Ca2(+)-ATPases including Saccharomyces cerevisiae vacuolar PMC1; Animal PMCAs function to export Ca(2+) from cells and play a role in regulating Ca(2+) signals following stimulus induction and in preventing calcium toxicity. Many PMCA pump variants exist due to alternative splicing of transcripts. PMCAs are regulated by the binding of calmodulin or by kinase-mediated phosphorylation. Saccharomyces cerevisiae vacuolar transporter Pmc1p facilitates the accumulation of Ca2+ into vacuoles. Pmc1p is not regulated by direct calmodulin binding but responds to the calmodulin/calcineurin-signaling pathway and is controlled by the transcription factor complex Tcn1p/Crz1p. Similarly, the expression of the gene for Dictyostelium discoideum Ca(2+)-ATPase PAT1, patA, is under the control of a calcineurin-dependent transcription factor. Plant vacuolar Ca(2+)-ATPases, are regulated by direct-calmodulin binding. Plant Ca(2+)-ATPases are present at various cellular locations including the plasma membrane, endoplasmic reticulum, chloroplast and vacuole. 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: 319776 [Multi-domain]  Cd Length: 721  Bit Score: 146.58  E-value: 2.83e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 332 GEK-SVPLAEVQPGMLLRLTTGDRVPVDGEITQGEAW-LDEAMLTGEPIPQQKGEGDSVH-----AGTVVQDGSVLFRAS 404
Cdd:cd02081 108 GEViQISVFDIVVGDIVQLKYGDLIPADGLLIEGNDLkIDESSLTGESDPIKKTPDNQIPdpfllSGTKVLEGSGKMLVT 187
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 405 AVGSHTTLSRIIRMVRQAQSSKP----EIGQLADKISAVFVPVVVVIALVSAAIW---YFFGPAP--------QIVYTLV 469
Cdd:cd02081 188 AVGVNSQTGKIMTLLRAENEEKTplqeKLTKLAVQIGKVGLIVAALTFIVLIIRFiidGFVNDGKsfsaedlqEFVNFFI 267
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 470 IATTVLIIACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQVVAV----KT----- 540
Cdd:cd02081 268 IAVTIIVVAVPEGLPLAVTLSLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTQNRMTVVQGyignKTecall 347
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 541 -FADvdeaqalrlaaalEQGSSHPLARAILDKAGDMQLP--------------QVNGFRtlrgLGVSGEAEghaLLL--- 602
Cdd:cd02081 348 gFVL-------------ELGGDYRYREKRPEEKVLKVYPfnsarkrmstvvrlKDGGYR----LYVKGASE---IVLkkc 407
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 603 -------GNQALLNEQQvgTKAIEAEITAQASQGATPVLLA----VDGKA-------------------VALLAVRDPLR 652
Cdd:cd02081 408 syilnsdGEVVFLTSEK--KEEIKRVIEPMASDSLRTIGLAyrdfSPDEEptaerdwddeediesdltfIGIVGIKDPLR 485
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 653 SDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGI------DEVIAG---------------------------VL-- 697
Cdd:cd02081 486 PEVPEAVAKCQRAGITVRMVTGDNINTARAIARECGIltegedGLVLEGkefrelideevgevcqekfdkiwpklrVLar 565
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16128468 698 --PDGKAEAIKHLQSEGRQVAMVGDGINDAPALAQADVGIAMG-GGSDVAIETAAITLM 753
Cdd:cd02081 566 ssPEDKYTLVKGLKDSGEVVAVTGDGTNDAPALKKADVGFAMGiAGTEVAKEASDIILL 624
ATPase-IIIA_H TIGR01647
plasma-membrane proton-efflux P-type ATPase; This model describes the plasma membrane proton ...
313-775 7.71e-36

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.


Pssm-ID: 273731 [Multi-domain]  Cd Length: 754  Bit Score: 145.55  E-value: 7.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   313 ALEKLLDLTPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPVDGEITQGEAW-LDEAMLTGEPIPQQKGEGDSVHAG 391
Cdd:TIGR01647  82 AVEALKQSLAPKARVLRDGKWQEIPASELVPGDVVRLKIGDIVPADCRLFEGDYIqVDQAALTGESLPVTKKTGDIAYSG 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   392 TVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAV-FVPVVVVIALVSAAIWYFFGPA--PQIVYTL 468
Cdd:TIGR01647 162 STVKQGEAEAVVTATGMNTFFGKAAALVQSTETGSGHLQKILSKIGLFlIVLIGVLVLIELVVLFFGRGESfrEGLQFAL 241
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   469 VIATTVLIIACPCALglATPMSIisGVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGK---PQVVAVKTFADVD 545
Cdd:TIGR01647 242 VLLVGGIPIAMPAVL--SVTMAV--GAAELAKKKAIVTRLTAIEELAGMDILCSDKTGTLTLNKlsiDEILPFFNGFDKD 317
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   546 EAQALRLAAALEQGSShPLARAILDKAGDMQLpQVNGFRTLRGLG-----------VSGEAEGHALLLGNQA------LL 608
Cdd:TIGR01647 318 DVLLYAALASREEDQD-AIDTAVLGSAKDLKE-ARDGYKVLEFVPfdpvdkrteatVEDPETGKRFKVTKGApqvildLC 395
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   609 NEQQVGTKAIEAEITAQASQGATPVLLAVDGKA-----VALLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDnpttANAI 683
Cdd:TIGR01647 396 DNKKEIEEKVEEKVDELASRGYRALGVARTDEEgrwhfLGLLPLFDPPRHDTKETIERARHLGVEVKMVTGD----HLAI 471
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   684 AKE---------------------------AGIDEVI------AGVLPDGKAEAIKHLQSEGRQVAMVGDGINDAPALAQ 730
Cdd:TIGR01647 472 AKEtarrlglgtniytadvllkgdnrddlpSGLGEMVedadgfAEVFPEHKYEIVEILQKRGHLVGMTGDGVNDAPALKK 551
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 16128468   731 ADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRATLHNMK 775
Cdd:TIGR01647 552 ADVGIAVAGATDAARSAADIVLTEPGLSVIVDAILESRKIFQRMK 596
P-type_ATPase_Na_ENA cd02086
fungal-type Na(+)-ATPase, similar to the plasma membrane sodium transporters Saccharomyces ...
290-785 2.41e-31

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: 132.19  E-value: 2.41e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 290 AMIIGL-INLGHMLEARArqrsSKALEKLLDLTPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPVDGE-ITQGEAW 367
Cdd:cd02086  63 AAVIALnVIVGFIQEYKA----EKTMDSLRNLSSPNAHVIRSGKTETISSKDVVPGDIVLLKVGDTVPADLRlIETKNFE 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 368 LDEAMLTGEPIPQQK------------GEGDS---VHAGTVVQDGsvlfRASAVGSHTTLSRIIRMVRQAQSSKPEIGQL 432
Cdd:cd02086 139 TDEALLTGESLPVIKdaelvfgkeedvSVGDRlnlAYSSSTVTKG----RAKGIVVATGMNTEIGKIAKALRGKGGLISR 214
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 433 ADKISAVFVPVVVVIALVSAAIWYFFGPAPQIVYTlVIATTVLIIACPCAL-----------------GLATPMSIIS-- 493
Cdd:cd02086 215 DRVKSWLYGTLIVTWDAVGRFLGTNVGTPLQRKLS-KLAYLLFFIAVILAIivfavnkfdvdneviiyAIALAISMIPes 293
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 494 -----------GVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQVVAVKTFADVDEAQALRLAAALEQGSSH 562
Cdd:cd02086 294 lvavltitmavGAKRMVKRNVIVRKLDALEALGAVTDICSDKTGTLTQGKMVVRQVWIPAALCNIATVFKDEETDCWKAH 373
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 563 ---------------PLARAILDKAGDMQLPQVNGF---RTLRGLGV---SGEAEGH-----------------ALLLGN 604
Cdd:cd02086 374 gdpteialqvfatkfDMGKNALTKGGSAQFQHVAEFpfdSTVKRMSVvyyNNQAGDYyaymkgavervleccssMYGKDG 453
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 605 QALLNEQQVgtKAIEAEITAQASQGATPVLLA---VDGKA----------------------VALLAVRDPLRSDSVAAL 659
Cdd:cd02086 454 IIPLDDEFR--KTIIKNVESLASQGLRVLAFAsrsFTKAQfnddqlknitlsradaesdltfLGLVGIYDPPRNESAGAV 531
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 660 QRLHKAGYRLVMLTGDNPTTANAIAKEAGI----------------------------DE---------VIAGVLPDGKA 702
Cdd:cd02086 532 EKCHQAGITVHMLTGDHPGTAKAIAREVGIlppnsyhysqeimdsmvmtasqfdglsdEEvdalpvlplVIARCSPQTKV 611
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 703 EAIKHLQSEGRQVAMVGDGINDAPALAQADVGIAMG-GGSDVAIETAAITLMRHSLMGVADALAISRATLHNMKQNLLGA 781
Cdd:cd02086 612 RMIEALHRRKKFCAMTGDGVNDSPSLKMADVGIAMGlNGSDVAKDASDIVLTDDNFASIVNAIEEGRRMFDNIQKFVLHL 691

                ....
gi 16128468 782 FIYN 785
Cdd:cd02086 692 LAEN 695
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
517-732 2.69e-30

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


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 118.46  E-value: 2.69e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   517 LDTVVFDKTGTLTEGKPQVVAVktfadvdeaqalrlaaALEQGSSHPLARAILDKAGDMQLPqvngfrtlrglgvsGEAE 596
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEA----------------IAELASEHPLAKAIVAAAEDLPIP--------------VEDF 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   597 GHALLLGNQALLNEQQvgtkAIEAEITAQASQGATPVLLAVDGkaVALLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDN 676
Cdd:pfam00702  51 TARLLLGKRDWLEELD----ILRGLVETLEAEGLTVVLVELLG--VIALADELKLYPGAAEALKALKERGIKVAILTGDN 124
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128468   677 PTTANAIAKEAGI-----------DEVIAGVLPDGKAEAIKHLQSEGRQVAMVGDGINDAPALAQAD 732
Cdd:pfam00702 125 PEAAEALLRLLGLddyfdvvisgdDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
P-type_ATPase_SPCA cd02085
golgi-associated secretory pathway Ca(2+) transport ATPases, similar to human ATPase secretory ...
309-775 2.77e-30

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: 128.29  E-value: 2.77e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 309 RSSKALEKLLDLTPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPVDGEITQG-EAWLDEAMLTGEPIPQQK----- 382
Cdd:cd02085  70 RSEKSLEALNKLVPPECHCLRDGKLEHFLARELVPGDLVCLSIGDRIPADLRLFEAtDLSIDESSLTGETEPCSKttevi 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 383 --GEGDSVHA-------GTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAVFVPVVVVIALVSAA 453
Cdd:cd02085 150 pkASNGDLTTrsniafmGTLVRCGHGKGIVIGTGENSEFGEVFKMMQAEEAPKTPLQKSMDKLGKQLSLYSFIIIGVIML 229
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 454 IWYFFGPapQIVYTLVIATTVLIIACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKP 533
Cdd:cd02085 230 IGWLQGK--NLLEMFTIGVSLAVAAIPEGLPIVVTVTLALGVMRMAKRRAIVKKLPIVETLGCVNVICSDKTGTLTKNEM 307
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 534 QVVAVKTFADVDEAQALRLAAAleqgsSHPLARAILDKAGDMQLPQV-NGFRTLRGLGVSGEAEGHAL------------ 600
Cdd:cd02085 308 TVTKIVTGCVCNNAVIRNNTLM-----GQPTEGALIALAMKMGLSDIrETYIRKQEIPFSSEQKWMAVkcipkynsdnee 382
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 601 ------------------LLGNQALLNEQQVGTKAIEAEITAQASQGATPVLLAVDGKA-----VALLAVRDPLRSDSVA 657
Cdd:cd02085 383 iyfmkgaleqvldycttyNSSDGSALPLTQQQRSEINEEEKEMGSKGLRVLALASGPELgdltfLGLVGINDPPRPGVRE 462
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 658 ALQRLHKAGYRLVMLTGDNPTTANAIAKEAGID---------------------------EVIAGVLPDGKAEAIKHLQS 710
Cdd:cd02085 463 AIQILLESGVRVKMITGDAQETAIAIGSSLGLYspslqalsgeevdqmsdsqlasvvrkvTVFYRASPRHKLKIVKALQK 542
                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128468 711 EGRQVAMVGDGINDAPALAQADVGIAMG-GGSDVAIETAAITLMRHSLMGVADALAISRATLHNMK 775
Cdd:cd02085 543 SGAVVAMTGDGVNDAVALKSADIGIAMGrTGTDVCKEAADMILVDDDFSTILAAIEEGKGIFYNIK 608
ATPase-IIB_Ca TIGR01517
plasma-membrane calcium-translocating P-type ATPase; This model describes the P-type ATPase ...
333-797 1.67e-29

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.


Pssm-ID: 273668 [Multi-domain]  Cd Length: 956  Bit Score: 126.05  E-value: 1.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   333 EKSVPLAEVQPGMLLRLTTGDRVPVDGEITQGEAW-LDEAMLTGEPIPQQKGEGDS--VHAGTVVQDGSVLFRASAVGSH 409
Cdd:TIGR01517 179 EQQISIHDIVVGDIVSLSTGDVVPADGVFISGLSLeIDESSITGESDPIKKGPVQDpfLLSGTVVNEGSGRMLVTAVGVN 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   410 TTLSRIIRMVRQA-QSSKP---EIGQLADKISaVFVPVVVVIALVSAAIWYFFGPAPQ-------------IVYTLVIAT 472
Cdd:TIGR01517 259 SFGGKLMMELRQAgEEETPlqeKLSELAGLIG-KFGMGSAVLLFLVLSLRYVFRIIRGdgrfedteedaqtFLDHFIIAV 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   473 TVLIIACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQVVAV---KTFADVDEAQA 549
Cdd:TIGR01517 338 TIVVVAVPEGLPLAVTIALAYSMKKMMKDNNLVRHLAACETMGSATAICSDKTGTLTQNVMSVVQGyigEQRFNVRDEIV 417
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   550 LRLAAALEQGSS------------------------HPLARAILDKAGDMQLPQVNGFRTLRGLGV-------SGEAEGH 598
Cdd:TIGR01517 418 LRNLPAAVRNILvegislnssseevvdrggkrafigSKTECALLDFGLLLLLQSRDVQEVRAEEKVvkiypfnSERKFMS 497
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   599 ALLLGNQALLNEQQVGTKAI--------------------------EAEITAQASQGATPVLLA---VDGKA-------- 641
Cdd:TIGR01517 498 VVVKHSGGKYREFRKGASEIvlkpcrkrldsngeatpiseddkdrcADVIEPLASDALRTICLAyrdFAPEEfprkdypn 577
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   642 -----VALLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGID-------------------------- 690
Cdd:TIGR01517 578 kgltlIGVVGIKDPLRPGVREAVQECQRAGITVRMVTGDNIDTAKAIARNCGILtfgglamegkefrslvyeemdpilpk 657
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   691 -EVIAGVLPDGKAEAIKHLQSEGRQVAMVGDGINDAPALAQADVGIAMG-GGSDVAIETAAITLMRHSLMGVADALAISR 768
Cdd:TIGR01517 658 lRVLARSSPLDKQLLVLMLKDMGEVVAVTGDGTNDAPALKLADVGFSMGiSGTEVAKEASDIILLDDNFASIVRAVKWGR 737
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*
gi 16128468   769 ATLHNMKQ---------------NLLGAFIYNSIGIPVAA-GILW 797
Cdd:TIGR01517 738 NVYDNIRKflqfqltvnvvavilTFVGSCISSSHTSPLTAvQLLW 782
ATPase-IIIB_Mg TIGR01524
magnesium-translocating P-type ATPase; This model describes the magnesium translocating P-type ...
298-774 3.79e-28

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]


Pssm-ID: 130587 [Multi-domain]  Cd Length: 867  Bit Score: 121.51  E-value: 3.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   298 LGHMLEARArQRSSKALEKLLDLTPPTARLVTDEGEKS---VPLAEVQPGMLLRLTTGDRVPVDGEITQG-EAWLDEAML 373
Cdd:TIGR01524 104 LGFIQESRA-ERAAYALKNMVKNTATVLRVINENGNGSmdeVPIDALVPGDLIELAAGDIIPADARVISArDLFINQSAL 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   374 TGEPIPQQKGEGDS-VHAGTVVQDGSVLFRASAVGSHTTlsriiRMVRQAQSSKPEIGQLADKISAVFVPVV--VVIALV 450
Cdd:TIGR01524 183 TGESLPVEKFVEDKrARDPEILERENLCFMGTNVLSGHA-----QAVVLATGSSTWFGSLAIAATERRGQTAfdKGVKSV 257
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   451 SAAIWYFFgpapqivytLVIATTVLII--------------ACPCALGLAT---PMSIISGVGRAA----EFGVLVRDAD 509
Cdd:TIGR01524 258 SKLLIRFM---------LVMVPVVLMInglmkgdwleaflfALAVAVGLTPemlPMIVSSNLAKGAinmsKKKVIVKELS 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   510 ALQRASTLDTVVFDKTGTLTEGKpqvVAVKTFADVDEAQALRLAAALEQGSSHP------LARAILDKAGDMQLPQVNG- 582
Cdd:TIGR01524 329 AIQNFGAMDILCTDKTGTLTQDK---IELEKHIDSSGETSERVLKMAWLNSYFQtgwknvLDHAVLAKLDESAARQTASr 405
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   583 -----------FRTLRGLGVSGEAEGHAL--------------------------------LLGNQALLNEQQVGTKAIe 619
Cdd:TIGR01524 406 wkkvdeipfdfDRRRLSVVVENRAEVTRLickgaveemltvcthkrfggavvtlsesekseLQDMTAEMNRQGIRVIAV- 484
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   620 AEITAQASQGATPVLLAVDGKAVALLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGID--------- 690
Cdd:TIGR01524 485 ATKTLKVGEADFTKTDEEQLIIEGFLGFLDPPKESTKEAIAALFKNGINVKVLTGDNEIVTARICQEVGIDandfllgad 564
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   691 ----------------EVIAGVLPDGKAEAIKHLQSEGRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETAAITLMR 754
Cdd:TIGR01524 565 ieelsdeelarelrkyHIFARLTPMQKSRIIGLLKKAGHTVGFLGDGINDAPALRKADVGISVDTAADIAKEASDIILLE 644
                         570       580
                  ....*....|....*....|
gi 16128468   755 HSLMGVADALAISRATLHNM 774
Cdd:TIGR01524 645 KSLMVLEEGVIEGRNTFGNI 664
PRK10517 PRK10517
magnesium-transporting P-type ATPase MgtA;
290-774 2.44e-27

magnesium-transporting P-type ATPase MgtA;


Pssm-ID: 236705 [Multi-domain]  Cd Length: 902  Bit Score: 119.02  E-value: 2.44e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  290 AMIIGL-INLGHMLEARARQRSSKALEKLLDLTPPTA---RLVTDEGEKS---VPLAEVQPGMLLRLTTGDRVPVDGEIT 362
Cdd:PRK10517 125 AGVIALmVAISTLLNFIQEARSTKAADALKAMVSNTAtvlRVINDKGENGwleIPIDQLVPGDIIKLAAGDMIPADLRIL 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  363 QG-EAWLDEAMLTGEPIPQQK--GEGDSVHAGTVVQDgSVLFRASAVGSHTTLSRIIrmvrqAQSSKPEIGQLADKISAV 439
Cdd:PRK10517 205 QArDLFVAQASLTGESLPVEKfaTTRQPEHSNPLECD-TLCFMGTNVVSGTAQAVVI-----ATGANTWFGQLAGRVSEQ 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  440 FVPVVVVIALVSAAIWYFfgpapqIVYTLVIATTVLII--------------ACPCALGLAT---PMSIISGVGRAAEF- 501
Cdd:PRK10517 279 DSEPNAFQQGISRVSWLL------IRFMLVMAPVVLLIngytkgdwweaalfALSVAVGLTPemlPMIVTSTLARGAVKl 352
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  502 ---GVLVRDADALQRASTLDTVVFDKTGTLTEGKpqvVAVKTFADV------DEAQALRLAAALEQGSSHPLARAILDKA 572
Cdd:PRK10517 353 skqKVIVKRLDAIQNFGAMDILCTDKTGTLTQDK---IVLENHTDIsgktseRVLHSAWLNSHYQTGLKNLLDTAVLEGV 429
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  573 GDMQLPQVNG-----------FRTLRGLGVSGEAEGHALLLGNQAL-----------LNEQQVG-TKAIEAEITA----Q 625
Cdd:PRK10517 430 DEESARSLASrwqkideipfdFERRRMSVVVAENTEHHQLICKGALeeilnvcsqvrHNGEIVPlDDIMLRRIKRvtdtL 509
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  626 ASQGATPVLLA-------------VDGKAVAL---LAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGI 689
Cdd:PRK10517 510 NRQGLRVVAVAtkylparegdyqrADESDLILegyIAFLDPPKETTAPALKALKASGVTVKILTGDSELVAAKVCHEVGL 589
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  690 D-------------------------EVIAGVLPDGKAEAIKHLQSEGRQVAMVGDGINDAPALAQADVGIAMGGGSDVA 744
Cdd:PRK10517 590 DagevligsdietlsddelanlaertTLFARLTPMHKERIVTLLKREGHVVGFMGDGINDAPALRAADIGISVDGAVDIA 669
                        570       580       590
                 ....*....|....*....|....*....|
gi 16128468  745 IETAAITLMRHSLMGVADALAISRATLHNM 774
Cdd:PRK10517 670 REAADIILLEKSLMVLEEGVIEGRRTFANM 699
ATPase-IIA1_Ca TIGR01116
sarco/endoplasmic reticulum calcium-translocating P-type ATPase; This model describes the ...
309-776 8.35e-26

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]


Pssm-ID: 273452 [Multi-domain]  Cd Length: 917  Bit Score: 114.11  E-value: 8.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   309 RSSKALEKLLDLTPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPVDGEITQGEAW-LDEAMLTGEPIPQQKgEGDS 387
Cdd:TIGR01116  59 NAEKAIEALKEYESEHAKVLRDGRWSVIKAKDLVPGDIVELAVGDKVPADIRVLSLKTLrVDQSILTGESVSVNK-HTES 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   388 VH--------------AGTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAVFVPVvvvIALVSAA 453
Cdd:TIGR01116 138 VPderavnqdkknmlfSGTLVVAGKARGVVVRTGMSTEIGKIRDEMRAAEQEDTPLQKKLDEFGELLSKV---IGLICIL 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   454 IW-----YFFGPAPQI------VYTLVIATTVLIIACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVF 522
Cdd:TIGR01116 215 VWvinigHFNDPALGGgwiqgaIYYFKIAVALAVAAIPEGLPAVITTCLALGTRKMAKKNAIVRKLPSVETLGCTTVICS 294
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   523 DKTGTLTEGKPQVVAVKTFADVDEAQ------------ALRLAAALEQGSSHPLA----------------------RAI 568
Cdd:TIGR01116 295 DKTGTLTTNQMSVCKVVALDPSSSSLnefcvtgttyapEGGVIKDDGPVAGGQDAgleelatiaalcndssldfnerKGV 374
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   569 LDKAGD-------MQLPQVNGFRTLRGLGVSGE----------------------------------AEGHALLLGN--Q 605
Cdd:TIGR01116 375 YEKVGEateaalkVLVEKMGLPATKNGVSSKRRpalgcnsvwndkfkklatlefsrdrksmsvlckpSTGNKLFVKGapE 454
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   606 ALL---NEQQVGT-----------KAIEAEITAQASQGA----------TPVLLAVDGKA--------------VALLAV 647
Cdd:TIGR01116 455 GVLercTHILNGDgravpltdkmkNTILSVIKEMGTTKAlrclalafkdIPDPREEDLLSdpanfeaiesdltfIGVVGM 534
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   648 RDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGI---DEVIAG----------------------------V 696
Cdd:TIGR01116 535 LDPPRPEVADAIEKCRTAGIRVIMITGDNKETAEAICRRIGIfspDEDVTFksftgrefdemgpakqraacrsavlfsrV 614
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   697 LPDGKAEAIKHLQSEGRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRATLHNMKQ 776
Cdd:TIGR01116 615 EPSHKSELVELLQEQGEIVAMTGDGVNDAPALKKADIGIAMGSGTEVAKEASDMVLADDNFATIVAAVEEGRAIYNNMKQ 694
P-type_ATPase_SERCA cd02083
sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; ...
642-776 1.81e-24

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: 110.07  E-value: 1.81e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 642 VALLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGI---DEVIAG----------------------- 695
Cdd:cd02083 584 VGVVGMLDPPRPEVRDSIEKCRDAGIRVIVITGDNKGTAEAICRRIGIfgeDEDTTGksytgrefddlspeeqreacrra 663
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 696 -----VLPDGKAEAIKHLQSEGRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRAT 770
Cdd:cd02083 664 rlfsrVEPSHKSKIVELLQSQGEITAMTGDGVNDAPALKKAEIGIAMGSGTAVAKSASDMVLADDNFATIVAAVEEGRAI 743

                ....*.
gi 16128468 771 LHNMKQ 776
Cdd:cd02083 744 YNNMKQ 749
PRK15122 PRK15122
magnesium-transporting ATPase; Provisional
309-758 2.45e-22

magnesium-transporting ATPase; Provisional


Pssm-ID: 237914 [Multi-domain]  Cd Length: 903  Bit Score: 103.18  E-value: 2.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  309 RSSKALEKLLDLTPPTA---RLVTDEGE---KSVPLAEVQPGMLLRLTTGDRVPVDGE-ITQGEAWLDEAMLTGEPIPQQ 381
Cdd:PRK15122 134 RSNKAAEALKAMVRTTAtvlRRGHAGAEpvrREIPMRELVPGDIVHLSAGDMIPADVRlIESRDLFISQAVLTGEALPVE 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  382 KGE------GDSVHAGTVVQDG-----SVLFRASAVGSHTTlsriiRMVRQAQSSKPEIGQLADKI--SAVFVPVVVVIA 448
Cdd:PRK15122 214 KYDtlgavaGKSADALADDEGSlldlpNICFMGTNVVSGTA-----TAVVVATGSRTYFGSLAKSIvgTRAQTAFDRGVN 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  449 LVSaaiWYFfgpapqIVYTLVIATTVLII--------------ACPCALGLAT---PMSIISGVGRAA----EFGVLVRD 507
Cdd:PRK15122 289 SVS---WLL------IRFMLVMVPVVLLIngftkgdwleallfALAVAVGLTPemlPMIVSSNLAKGAiamaRRKVVVKR 359
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  508 ADALQRASTLDTVVFDKTGTLTEGK---PQVVAVKTFADVDEAQALRLAAALEQGSSHPLARAIL---DKAGDMQLPQvn 581
Cdd:PRK15122 360 LNAIQNFGAMDVLCTDKTGTLTQDRiilEHHLDVSGRKDERVLQLAWLNSFHQSGMKNLMDQAVVafaEGNPEIVKPA-- 437
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  582 GFRTL---------RGLGVSGEAEGHALLL----------------------------GNQALL------NEQQ-----V 613
Cdd:PRK15122 438 GYRKVdelpfdfvrRRLSVVVEDAQGQHLLickgaveemlavathvrdgdtvrpldeaRRERLLalaeayNADGfrvllV 517
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  614 GTKAIEAEITAQASQGATPVLLAVDGkavaLLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGID--- 690
Cdd:PRK15122 518 ATREIPGGESRAQYSTADERDLVIRG----FLTFLDPPKESAAPAIAALRENGVAVKVLTGDNPIVTAKICREVGLEpge 593
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468  691 ----------------------EVIAGVLPDGKAEAIKHLQSEGRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETA 748
Cdd:PRK15122 594 pllgteieamddaalareveerTVFAKLTPLQKSRVLKALQANGHTVGFLGDGINDAPALRDADVGISVDSGADIAKESA 673
                        570
                 ....*....|
gi 16128468  749 AITLMRHSLM 758
Cdd:PRK15122 674 DIILLEKSLM 683
ATPase-IID_K-Na TIGR01523
potassium and/or sodium efflux P-type ATPase, fungal-type; Initially described as a calcium ...
642-785 1.87e-21

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: 100.47  E-value: 1.87e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468    642 VALLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGI---------------------------DE--- 691
Cdd:TIGR01523  638 LGLIGIYDPPRNESAGAVEKCHQAGINVHMLTGDFPETAKAIAQEVGIippnfihdrdeimdsmvmtgsqfdalsDEevd 717
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468    692 -------VIAGVLPDGKAEAIKHLQSEGRQVAMVGDGINDAPALAQADVGIAMG-GGSDVAIETAAITLMRHSLMGVADA 763
Cdd:TIGR01523  718 dlkalclVIARCAPQTKVKMIEALHRRKAFCAMTGDGVNDSPSLKMANVGIAMGiNGSDVAKDASDIVLSDDNFASILNA 797
                          170       180
                   ....*....|....*....|..
gi 16128468    764 LAISRATLHNMKQNLLGAFIYN 785
Cdd:TIGR01523  798 IEEGRRMFDNIMKFVLHLLAEN 819
P-type_ATPase_cation cd02082
P-type cation-transporting ATPases, similar to human ATPase type 13A1-A4 (ATP13A1-A4) proteins ...
283-773 4.52e-21

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.


Pssm-ID: 319777 [Multi-domain]  Cd Length: 786  Bit Score: 98.82  E-value: 4.52e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 283 HLYYEASAMIIGLINLGHMLEARARQRSskaleKLLDLTPPTARL-VTDEGEKSVPLA--EVQPG--MLLRLTtGDRVPV 357
Cdd:cd02082  49 YVYYAITVVFMTTINSLSCIYIRGVMQK-----ELKDACLNNTSViVQRHGYQEITIAsnMIVPGdiVLIKRR-EVTLPC 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 358 DGEITQGEAWLDEAMLTGEPIPQQKG--EGDSVHAGTVVQDGS---VLFRASAV------------------GSHTTLSR 414
Cdd:cd02082 123 DCVLLEGSCIVTEAMLTGESVPIGKCqiPTDSHDDVLFKYESSkshTLFQGTQVmqiippeddilkaivvrtGFGTSKGQ 202
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 415 IIRMVRQAQSSKPEIGQLADKISaVFVPVVVVIALVSAAIWYFFGPAPqiVYTLVIATT-VLIIACPCALGLATPMSIIS 493
Cdd:cd02082 203 LIRAILYPKPFNKKFQQQAVKFT-LLLATLALIGFLYTLIRLLDIELP--PLFIAFEFLdILTYSVPPGLPMLIAITNFV 279
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 494 GVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQVVAV------KTFADVDEAQALRLAAALEQGSS-HPLAR 566
Cdd:cd02082 280 GLKRLKKNQILCQDPNRISQAGRIQTLCFDKTGTLTEDKLDLIGYqlkgqnQTFDPIQCQDPNNISIEHKLFAIcHSLTK 359
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 567 A-------------------ILDKAGDM-QLP-----------QVNGFRT-LRGLGVSGEAEG--------HALLLGN-- 604
Cdd:cd02082 360 IngkllgdpldvkmaeastwDLDYDHEAkQHYsksgtkrfyiiQVFQFHSaLQRMSVVAKEVDmitkdfkhYAFIKGApe 439
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 605 --QALLNEQQVGTKAIEAEITAQ------------------ASQGATPVLLAVDGKAVALLAVRDPLRSDSVAALQRLHK 664
Cdd:cd02082 440 kiQSLFSHVPSDEKAQLSTLINEgyrvlalgykelpqseidAFLDLSREAQEANVQFLGFIIYKNNLKPDTQAVIKEFKE 519
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 665 AGYRLVMLTGDNPTTANAIAKEAGIDE------------------------------VIAGVLPDGKAEAIKHLQSEGRQ 714
Cdd:cd02082 520 ACYRIVMITGDNPLTALKVAQELEIINrknptiiihllipeiqkdnstqwiliihtnVFARTAPEQKQTIIRLLKESDYI 599
                       570       580       590       600       610
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16128468 715 VAMVGDGINDAPALAQADVGIAMGGGsDVAIeTAAITLMRHSLMGVADALAISRATLHN 773
Cdd:cd02082 600 VCMCGDGANDCGALKEADVGISLAEA-DASF-ASPFTSKSTSISCVKRVILEGRVNLST 656
P-type_ATPase_Na-K_like cd02608
alpha-subunit of Na(+)/K(+)-ATPases and of gastric H(+)/K(+)-ATPase, similar to the human Na(+) ...
642-753 1.41e-20

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: 97.42  E-value: 1.41e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 642 VALLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIdEVIAGVLPDGKAEAIKHLQSEGRQVAMVGDG 721
Cdd:cd02608 525 VGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGI-IVFARTSPQQKLIIVEGCQRQGAIVAVTGDG 603
                        90       100       110
                ....*....|....*....|....*....|...
gi 16128468 722 INDAPALAQADVGIAMG-GGSDVAIETAAITLM 753
Cdd:cd02608 604 VNDSPALKKADIGVAMGiAGSDVSKQAADMILL 636
P-ATPase-V TIGR01657
P-type ATPase of unknown pump specificity (type V); These P-type ATPases form a distinct clade ...
269-737 2.30e-19

P-type ATPase of unknown pump specificity (type V); These P-type ATPases form a distinct clade but the substrate of their pumping activity has yet to be determined. This clade has been designated type V in.


Pssm-ID: 273738 [Multi-domain]  Cd Length: 1054  Bit Score: 93.58  E-value: 2.30e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468    269 SVNLWpqwfpmEARHLYYEASAMIIGLInlghMLEARARQRSSKALEKLLD--LTPPTARLVTDEGEKSVPLAEVQPG-- 344
Cdd:TIGR01657  183 SVILW------LLDEYYYYSLCIVFMSS----TSISLSVYQIRKQMQRLRDmvHKPQSVIVIRNGKWVTIASDELVPGdi 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468    345 MLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEPIPQQK----GEGDS--------------VHAGT-VVQ------DGSV 399
Cdd:TIGR01657  253 VSIPRPEEKTMPCDSVLLSGSCIVNESMLTGESVPVLKfpipDNGDDdedlflyetskkhvLFGGTkILQirpypgDTGC 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468    400 LFRASAVGSHTTLSRIIRMVRQaqsSKPEIGQLaDKISAVFVPVVVVIALVSAA-IWYFFGPAPQIVYTLVI-ATTVLII 477
Cdd:TIGR01657  333 LAIVVRTGFSTSKGQLVRSILY---PKPRVFKF-YKDSFKFILFLAVLALIGFIyTIIELIKDGRPLGKIILrSLDIITI 408
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468    478 ACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQVVAV------KTF--ADVDEAQA 549
Cdd:TIGR01657  409 VVPPALPAELSIGINNSLARLKKKGIFCTSPFRINFAGKIDVCCFDKTGTLTEDGLDLRGVqglsgnQEFlkIVTEDSSL 488
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468    550 LRLAAALEQGSSHPLARA-------------------ILDKAGDMQLP-------------------QVNGFRT-LRGLG 590
Cdd:TIGR01657  489 KPSITHKALATCHSLTKLegklvgdpldkkmfeatgwTLEEDDESAEPtsilavvrtddppqelsiiRRFQFSSaLQRMS 568
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468    591 V----SGEAEGHALLLGN----QALLNEQQVGT--KAIEAEITAQASQgatpvLLAVDGKA------------------- 641
Cdd:TIGR01657  569 VivstNDERSPDAFVKGApetiQSLCSPETVPSdyQEVLKSYTREGYR-----VLALAYKElpkltlqkaqdlsrdaves 643
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468    642 ----VALLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGI---------------------------- 689
Cdd:TIGR01657  644 nltfLGFIVFENPLKPDTKEVIKELKRASIRTVMITGDNPLTAVHVARECGIvnpsntlilaeaeppesgkpnqikfevi 723
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468    690 DE-------------------------------------------------------VIAGVLPDGKAEAIKHLQSEGRQ 714
Cdd:TIGR01657  724 DSipfastqveipyplgqdsvedllasryhlamsgkafavlqahspelllrllshttVFARMAPDQKETLVELLQKLDYT 803
                          650       660
                   ....*....|....*....|...
gi 16128468    715 VAMVGDGINDAPALAQADVGIAM 737
Cdd:TIGR01657  804 VGMCGDGANDCGALKQADVGISL 826
P-type_ATPase_cation cd07543
P-type cation-transporting ATPases, similar to human cation-transporting ATPase type 13A1 ...
650-776 5.75e-17

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.


Pssm-ID: 319843 [Multi-domain]  Cd Length: 804  Bit Score: 85.51  E-value: 5.75e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 650 PLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDE------------------------VIAGVLPDGKAEAI 705
Cdd:cd07543 509 PLKPDSKETIKELNNSSHRVVMITGDNPLTACHVAKELGIVDkpvlililseegksnewkliphvkVFARVAPKQKEFII 588
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128468 706 KHLQSEGRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIeTAAITLMRHSLMGVADALAISRATLHNMKQ 776
Cdd:cd07543 589 TTLKELGYVTLMCGDGTNDVGALKHAHVGVALLKLGDASI-AAPFTSKLSSVSCVCHIIKQGRCTLVTTLQ 658
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
102-165 7.24e-17

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 75.71  E-value: 7.24e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128468 102 QLLLSGMSCASCVTRVQNALQSVPGVTQARVNLAERTALVMGS---ASPQDLVQAVEKAGYGAEAIE 165
Cdd:COG2608   5 TLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDpekVSLEDIKAAIEEAGYEVEKAE 71
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
102-162 1.05e-16

Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid residues found in a number of proteins that transport or detoxify heavy metals, for example, the CPx-type heavy metal ATPases and copper chaperones. HMA domain contains two cysteine residues that are important in binding and transfer of metal ions, such as copper, cadmium, cobalt and zinc. In the case of copper, stoichiometry of binding is one Cu+ ion per binding domain. Repeats of the HMA domain in copper chaperone has been associated with Menkes/Wilson disease due to binding of multiple copper ions.


Pssm-ID: 238219 [Multi-domain]  Cd Length: 63  Bit Score: 74.95  E-value: 1.05e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128468 102 QLLLSGMSCASCVTRVQNALQSVPGVTQARVNLAERTALVMGSA--SPQDLVQAVEKAGYGAE 162
Cdd:cd00371   1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPevSPEELLEAIEDAGYKAR 63
ATPase-IIC_X-K TIGR01106
sodium or proton efflux -- potassium uptake antiporter, P-type ATPase, alpha subunit; This ...
642-811 9.80e-15

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: 78.68  E-value: 9.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   642 VALLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGI-------------------------------- 689
Cdd:TIGR01106 560 VGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIisegnetvediaarlnipvsqvnprdakacvv 639
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   690 -------------DE--------VIAGVLPDGKAEAIKHLQSEGRQVAMVGDGINDAPALAQADVGIAMG-GGSDVAIET 747
Cdd:TIGR01106 640 hgsdlkdmtseqlDEilkyhteiVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGiAGSDVSKQA 719
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128468   748 AAITLMRHSLMGVADALAISRATLHNMKQNL----------LGAF-IYNSIGIPVAAG---ILWPFTGTLLNPVVAGA 811
Cdd:TIGR01106 720 ADMILLDDNFASIVTGVEEGRLIFDNLKKSIaytltsnipeITPFlIFIIANIPLPLGtitILCIDLGTDMVPAISLA 797
P-type_ATPase_cation cd07542
P-type cation-transporting ATPases, similar to human ATPase type 13A2 (ATP13A2) protein and ...
285-735 3.26e-14

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.


Pssm-ID: 319842 [Multi-domain]  Cd Length: 760  Bit Score: 76.90  E-value: 3.26e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 285 YYEASAMIIgLINLGH-MLEARARQRSSKALEKLLDLTPPtARLVTDEGEKSVPLAEVQPGMLLRLTT-GDRVPVDGEIT 362
Cdd:cd07542  50 YYYYAACIV-IISVISiFLSLYETRKQSKRLREMVHFTCP-VRVIRDGEWQTISSSELVPGDILVIPDnGTLLPCDAILL 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 363 QGEAWLDEAMLTGEPIPQQK-----GEGDSVHAGTVVQDGS--VLF------RASAVGSHTTLSRIIR---------MVR 420
Cdd:cd07542 128 SGSCIVNESMLTGESVPVTKtplpdESNDSLWSIYSIEDHSkhTLFcgtkviQTRAYEGKPVLAVVVRtgfnttkgqLVR 207
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 421 QAQSSKPEIGQLAdKISAVFVPVVVVIALVSaaiwyffgpapqIVYTLVI--------------ATTVLIIACPCALGLA 486
Cdd:cd07542 208 SILYPKPVDFKFY-RDSMKFILFLAIIALIG------------FIYTLIIlilngeslgeiiirALDIITIVVPPALPAA 274
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 487 TPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQVVAVKTfadvdeaqalrlAAALEQGSSHPLar 566
Cdd:cd07542 275 LTVGIIYAQSRLKKKGIFCISPQRINICGKINLVCFDKTGTLTEDGLDLWGVRP------------VSGNNFGDLEVF-- 340
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 567 aILDKAGDMQLPQVNGFRTLrglgvsgeAEGHAL-LLGNQAL---------------------------LNEQQVGTK-- 616
Cdd:cd07542 341 -SLDLDLDSSLPNGPLLRAM--------ATCHSLtLIDGELVgdpldlkmfeftgwsleilrqfpfssaLQRMSVIVKtp 411
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 617 -----------AIE--AEITAQ--------------ASQGATpvLLAVDGKAVA----------------------LLAV 647
Cdd:cd07542 412 gddsmmaftkgAPEmiASLCKPetvpsnfqevlneyTKQGFR--VIALAYKALEsktwllqklsreevesdleflgLIVM 489
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 648 RDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGI----DEVI--------------------------AGVL 697
Cdd:cd07542 490 ENRLKPETAPVINELNRANIRTVMVTGDNLLTAISVARECGMispsKKVIlieavkpedddsasltwtlllkgtvfARMS 569
                       570       580       590
                ....*....|....*....|....*....|....*...
gi 16128468 698 PDGKAEAIKHLQSEGRQVAMVGDGINDAPALAQADVGI 735
Cdd:cd07542 570 PDQKSELVEELQKLDYTVGMCGDGANDCGALKAADVGI 607
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
2-65 8.19e-14

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 66.85  E-value: 8.19e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128468   2 SQTIDLTLDGLSCGHCVKRVKESLEQRPDVEQADVSITEAHVT-----GTASAEQLIETIKQAGYDASV 65
Cdd:COG2608   1 MKTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATvtydpEKVSLEDIKAAIEEAGYEVEK 69
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
6-64 1.20e-11

Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid residues found in a number of proteins that transport or detoxify heavy metals, for example, the CPx-type heavy metal ATPases and copper chaperones. HMA domain contains two cysteine residues that are important in binding and transfer of metal ions, such as copper, cadmium, cobalt and zinc. In the case of copper, stoichiometry of binding is one Cu+ ion per binding domain. Repeats of the HMA domain in copper chaperone has been associated with Menkes/Wilson disease due to binding of multiple copper ions.


Pssm-ID: 238219 [Multi-domain]  Cd Length: 63  Bit Score: 60.70  E-value: 1.20e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128468   6 DLTLDGLSCGHCVKRVKESLEQRPDVEQADVSIT--EAHVTG--TASAEQLIETIKQAGYDAS 64
Cdd:cd00371   1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLEtgKATVEYdpEVSPEELLEAIEDAGYKAR 63
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
644-736 4.35e-11

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 63.32  E-value: 4.35e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 644 LLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIA-------GVL----------PDGKAEAIK 706
Cdd:COG0560  82 LFEEVPRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIAnelevedGRLtgevvgpivdGEGKAEALR 161
                        90       100       110
                ....*....|....*....|....*....|....
gi 16128468 707 -HLQSEG---RQVAMVGDGINDAPALAQADVGIA 736
Cdd:COG0560 162 eLAAELGidlEQSYAYGDSANDLPMLEAAGLPVA 195
HMA pfam00403
Heavy-metal-associated domain;
103-156 2.19e-10

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 56.86  E-value: 2.19e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 16128468   103 LLLSGMSCASCVTRVQNALQSVPGVTQARVNLAERTALVMGSASPQDLVQAVEK 156
Cdd:pfam00403   2 FRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEA 55
PRK13748 PRK13748
putative mercuric reductase; Provisional
103-169 5.53e-10

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 62.86  E-value: 5.53e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128468  103 LLLSGMSCASCVTRVQNALQSVPGVTQARVNLAERTALVM--GSASPQDLVQAVEKAGYGAEAIEDDAK 169
Cdd:PRK13748   4 LKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAieVGTSPDALTAAVAGLGYRATLADAPPT 72
PLN02957 PLN02957
copper, zinc superoxide dismutase
108-164 7.84e-09

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 57.07  E-value: 7.84e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16128468  108 MSCASCVTRVQNALQSVPGVTQARVNLAERTALVMGSASPQDLVQAVEKAGYGAEAI 164
Cdd:PLN02957  14 MKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLGSSPVKAMTAALEQTGRKARLI 70
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
7-62 2.25e-08

copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in Bacillus subtilis and related species. A number of longer protein, such as copper-translocating P-type ATPases, contain multiple CopZ-like domains, with its signature invariant CxxC motif. CopZ from other species may be more different in sequence from this family than some of those domains of longer proteins.


Pssm-ID: 411375 [Multi-domain]  Cd Length: 66  Bit Score: 51.33  E-value: 2.25e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128468    7 LTLDGLSCGHCVKRVKESLEQRPDVEQADVSITEAHVT-----GTASAEQLIETIKQAGYD 62
Cdd:NF033795   4 LNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDvefdeSKVTLDQIKEAIEDQGYD 64
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
656-737 3.59e-08

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 52.01  E-value: 3.59e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 656 VAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVL---------PDGKAEAI--KHLQSEGRQVAMVGDGIND 724
Cdd:cd01427  13 VELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIgsdgggtpkPKPKPLLLllLKLGVDPEEVLFVGDSEND 92
                        90
                ....*....|....
gi 16128468 725 APALAQADV-GIAM 737
Cdd:cd01427  93 IEAARAAGGrTVAV 106
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
659-736 3.90e-07

phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p; This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 51.01  E-value: 3.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 659 LQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVL-----------------PDGKAEAIKHLQSE----GRQVAM 717
Cdd:cd07500  79 IQTLKAKGYKTAVVSGGFTYFTDRLAEELGLDYAFANELeikdgkltgkvlgpivdAQRKAETLQELAARlgipLEQTVA 158
                        90
                ....*....|....*....
gi 16128468 718 VGDGINDAPALAQADVGIA 736
Cdd:cd07500 159 VGDGANDLPMLKAAGLGIA 177
PRK13748 PRK13748
putative mercuric reductase; Provisional
5-137 1.45e-06

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 51.69  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468    5 IDLTLDGLSCGHCVKRVKESLEQRPDVEQADVSITEAHVTGTA----SAEQLIETIKQAGYDASVShpkakPLAESSIPS 80
Cdd:PRK13748   2 TTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIevgtSPDALTAAVAGLGYRATLA-----DAPPTDNRG 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128468   81 EALTAVSEALPAATADDDDSQQLLL----SGMSCASCvtrvqnALQSVPGvtQARVNLAER 137
Cdd:PRK13748  77 GLLDKMRGWLGGADKHSGNERPLHVavigSGGAAMAA------ALKAVEQ--GARVTLIER 129
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
654-764 2.06e-06

phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), and Pyrococcus horikoshii PH1421, a magnesium-dependent phosphatase; belongs to the haloacid dehalogenase-like superfamily; Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PGPase) catalyzes the magnesium-dependent dephosphorylation of phosphoglycolate. This family also includes Pyrococcus horikoshii OT3 PH1421, a magnesium-dependent phosphatase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319816 [Multi-domain]  Cd Length: 139  Bit Score: 47.97  E-value: 2.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 654 DSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDE-VIA---GVlpdGKAEAIKHLQS----EGRQVAMVGDGINDA 725
Cdd:cd07514  20 RAIEAIRKLEKAGIPVVLVTGNSLPVARALAKYLGLSGpVVAengGV---DKGTGLEKLAErlgiDPEEVLAIGDSENDI 96
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 16128468 726 PALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADAL 764
Cdd:cd07514  97 EMFKVAGFKVAVANADEELKEAADYVTDASYGDGVLEAI 135
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
656-724 2.70e-06

Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 49.16  E-value: 2.70e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 656 VAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVL-----------PDGKAEAIKHLQSEGRQVAMVGDGIND 724
Cdd:COG0546  90 RELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVggddvppakpkPEPLLEALERLGLDPEEVLMVGDSPHD 169
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
658-736 2.70e-06

3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily phosphatases [Cell wall/membrane/envelope biogenesis, General function prediction only];


Pssm-ID: 441384 [Multi-domain]  Cd Length: 170  Bit Score: 48.12  E-value: 2.70e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 658 ALQRLHKAGYRLVMLTG-DNPTTANAiAKEAGIDEVIAGVlpDGKAEAIKHLQSEGR----QVAMVGDGINDAPALAQAD 732
Cdd:COG1778  43 GIKLLRKAGIKVAIITGrDSPAVRRR-AEELGITHVYQGV--KDKLEALEELLAKLGlspeEVAYIGDDLPDLPVMRRVG 119

                ....
gi 16128468 733 VGIA 736
Cdd:COG1778 120 LSVA 123
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
650-720 3.81e-06

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 48.87  E-value: 3.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 650 PLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVL---------PDGKA--EAIKHLQSEGRQVAMV 718
Cdd:COG1011  93 EPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVsseevgvrkPDPEIfeLALERLGVPPEEALFV 172

                ..
gi 16128468 719 GD 720
Cdd:COG1011 173 GD 174
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
620-752 5.37e-06

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


Pssm-ID: 273022 [Multi-domain]  Cd Length: 219  Bit Score: 48.12  E-value: 5.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   620 AEITAQASQGATP--------VLLAVDGKAVALLAVRD--PLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGI 689
Cdd:TIGR00338  45 SEITERAMRGELDfkaslrerVALLKGLPVELLKEVREnlPLTEGAEELVKTLKEKGYKVAVISGGFDLFAEHVKDKLGL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   690 DEVIAGVL--PDG---------------KAEAIKHLQSE----GRQVAMVGDGINDAPALAQADVGIAMGGG------SD 742
Cdd:TIGR00338 125 DAAFANRLevEDGkltglvegpivdasyKGKTLLILLRKegisPENTVAVGDGANDLSMIKAAGLGIAFNAKpklqqkAD 204
                         170
                  ....*....|
gi 16128468   743 VAIETAAITL 752
Cdd:TIGR00338 205 ICINKKDLTD 214
HMA pfam00403
Heavy-metal-associated domain;
7-58 5.83e-06

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 44.15  E-value: 5.83e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 16128468     7 LTLDGLSCGHCVKRVKESLEQRPDVEQADVSITE--AHVTGTASA---EQLIETIKQ 58
Cdd:pfam00403   2 FRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATktVTVTGDAEStklEKLVEAIEK 58
MerP TIGR02052
mercuric transport protein periplasmic component; This model represents the periplasmic ...
82-159 6.27e-06

mercuric transport protein periplasmic component; This model represents the periplasmic mercury (II) binding protein of the bacterial mercury detoxification system which passes mercuric ion to the MerT transporter for subsequent reduction to Hg(0) by the mercuric reductase MerA. MerP contains a distinctive GMTCXXC motif associated with metal binding. MerP is related to a larger family of metal binding proteins (pfam00403). [Cellular processes, Detoxification]


Pssm-ID: 131107 [Multi-domain]  Cd Length: 92  Bit Score: 45.41  E-value: 6.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468    82 ALTAVSEALPAATADDDDSQQLLLSGMSCASCVTRVQNALQSVPGVTQARVNLAERTALVM---GSASPQDLVQAVEKAG 158
Cdd:TIGR02052   6 TLLALFVLTSLPAWAATQTVTLEVPGMTCVACPITVETALQKVDGVSKAEVTFKTKLAVVTfddEKTNVKALTEATTDAG 85

                  .
gi 16128468   159 Y 159
Cdd:TIGR02052  86 Y 86
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
659-772 7.29e-06

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; 5'-nucleotidases dephosphorylate nucleoside 5'-monophosphates to nucleosides and inorganic phosphate. Purified Pseudomonas aeruginosa PA0065 displayed high activity toward 5'-UMP and 5'-IMP, significant activity against 5'-XMP and 5'-TMP, and low activity against 5'-CMP. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319798 [Multi-domain]  Cd Length: 209  Bit Score: 47.59  E-value: 7.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 659 LQRLHKAGYRLVMLTGDNPTTANAIAKEAGID---EVIAGVLPDG----KAEAIKH----LQSEGRQVAMVGDGIND--- 724
Cdd:cd04302  90 LEKLKAAGYRLYVATSKPEVFARRILEHFGLDeyfDGIAGASLDGsrvhKADVIRYaldtLGIAPEQAVMIGDRKHDiig 169
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 16128468 725 APALAQADVGIAMGGGSDVAIETAAitlmrhslmgvADALAISRATLH 772
Cdd:cd04302 170 ARANGIDSIGVLYGYGSEDELEEAG-----------ATYIVETPAELL 206
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
656-764 1.10e-05

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 47.05  E-value: 1.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 656 VAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAG---------------------------------------- 695
Cdd:COG0561  25 KEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITsngaliydpdgevlyerpldpedvreilellrehglhlqv 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 696 ----------VLPDG--KAEAIKHLQSE----GRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMG 759
Cdd:COG0561 105 vvrsgpgfleILPKGvsKGSALKKLAERlgipPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVKAAADYVTGSNDEDG 184

                ....*
gi 16128468 760 VADAL 764
Cdd:COG0561 185 VAEAL 189
COG4087 COG4087
Soluble P-type ATPase [General function prediction only];
635-736 3.39e-05

Soluble P-type ATPase [General function prediction only];


Pssm-ID: 443263 [Multi-domain]  Cd Length: 156  Bit Score: 44.77  E-value: 3.39e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 635 LAVDGKAVallavrdplrsDSVAA-LQRLHKAgYRLVMLTGDNPTTANAIAKEAGIdEVIagVLPDG-----KAEAIKHL 708
Cdd:COG4087  25 LAVDGKLI-----------PGVKErLEELAEK-LEIHVLTADTFGTVAKELAGLPV-ELH--ILPSGdqaeeKLEFVEKL 89
                        90       100
                ....*....|....*....|....*...
gi 16128468 709 QSEGrqVAMVGDGINDAPALAQADVGIA 736
Cdd:COG4087  90 GAET--TVAIGNGRNDVLMLKEAALGIA 115
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
696-748 5.44e-05

Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272905 [Multi-domain]  Cd Length: 256  Bit Score: 45.72  E-value: 5.44e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 16128468   696 VLPDG--KAEAI----KHLQSEGRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETA 748
Cdd:TIGR00099 182 ITAKGvsKGSALqslaEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEELKALA 240
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
5-63 1.15e-04

copper ion binding protein; This model describes an apparently copper-specific subfamily of the metal-binding domain HMA (pfam00403). Closely related sequences outside this model include mercury resistance proteins and repeated domains of eukaryotic eukaryotic copper transport proteins. Members of this family are strictly prokaryotic. The model identifies both small proteins consisting of just this domain and N-terminal regions of cation (probably copper) transporting ATPases. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 188014 [Multi-domain]  Cd Length: 66  Bit Score: 40.99  E-value: 1.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128468     5 IDLTLDGLSCGHCVKRVKESLEQRPDVEQADVSITEAHV-----TGTASAEQLIETIKQAGYDA 63
Cdd:TIGR00003   2 QTFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVvvefdAPNVSATEICEAILDAGYEV 65
HAD pfam12710
haloacid dehalogenase-like hydrolase;
656-728 2.71e-04

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 42.91  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   656 VAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVL-------------------PDGKAEAIK-HLQSEGRQV 715
Cdd:pfam12710  90 LELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLATELevddgrftgelrligppcaGEGKVRRLRaWLAARGLGL 169
                          90
                  ....*....|....*...
gi 16128468   716 AM-----VGDGINDAPAL 728
Cdd:pfam12710 170 DLadsvaYGDSPSDLPML 187
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
101-162 3.44e-04

copper ion binding protein; This model describes an apparently copper-specific subfamily of the metal-binding domain HMA (pfam00403). Closely related sequences outside this model include mercury resistance proteins and repeated domains of eukaryotic eukaryotic copper transport proteins. Members of this family are strictly prokaryotic. The model identifies both small proteins consisting of just this domain and N-terminal regions of cation (probably copper) transporting ATPases. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 188014 [Multi-domain]  Cd Length: 66  Bit Score: 39.45  E-value: 3.44e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128468   101 QQLLLSGMSCASCVTRVQNALQSVPGVTQARVNLAERTALV---MGSASPQDLVQAVEKAGYGAE 162
Cdd:TIGR00003   2 QTFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVefdAPNVSATEICEAILDAGYEVE 66
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
657-752 5.14e-04

haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) phosphatase KdsC, and rainbow trout N-acylneuraminate cytidylyltransferase; KDO 8-P phosphatase catalyzes the hydrolysis of KDO 8-P to KDO (3-deoxy-D-manno-octulosonate) and inorganic phosphate and is the last enzyme in the KDO biosynthetic pathway. KDO is an 8-carbon sugar that links the lipid A and polysaccharide moieties of the lipopolysaccharide region in Gram-negative bacteria. An interruption in KDO biosynthesis leads to the accumulation of lipid A precursors and subsequent arrest in cell growth. The KDO biosynthesis pathway involves five sequential enzymatic reactions. This family also includes rainbow trout CMP-sialic acid synthetase which effectively converts both deaminoneuraminic acid (KDN, 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid) and N-acetylneuraminic acid (Neu5Ac) to CMP-KDN and CMP-Neu5Ac, respectively. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319769 [Multi-domain]  Cd Length: 146  Bit Score: 40.97  E-value: 5.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 657 AALQRLHKAGYRLVMLTG-DNPTTANAiAKEAGIDEVIAGVlpDGKAEAIKHLQSEG----RQVAMVGDGINDAPALAQA 731
Cdd:cd01630  35 LGIKLLQKSGIEVAIITGrQSEAVRRR-AKELGIEDLFQGV--KDKLEALEELLEKLglsdEEVAYMGDDLPDLPVMKRV 111
                        90       100
                ....*....|....*....|.
gi 16128468 732 DVGIAMGGGSDVAIETAAITL 752
Cdd:cd01630 112 GLSVAPADAHPEVREAADYVT 132
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
658-736 5.17e-04

pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 42.27  E-value: 5.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 658 ALQRLHKAGYRLVMLTGDNPTTANAIAKEAGID---EVIAGV--------LPDGKAEAIKHLQSEGRQVAMVGDGINDAP 726
Cdd:cd02616  88 TLARLKSQGIKLGVVTTKLRETALKGLKLLGLDkyfDVIVGGddvthhkpDPEPVLKALELLGAEPEEALMVGDSPHDIL 167
                        90
                ....*....|
gi 16128468 727 ALAQADVGIA 736
Cdd:cd02616 168 AGKNAGVKTV 177
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
654-697 9.03e-04

L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 41.48  E-value: 9.03e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 16128468 654 DSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVL 697
Cdd:cd02588  95 DVVAGLRRLREAGYRLAILSNGSPDLIEDVVANAGLRDLFDAVL 138
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
650-731 9.45e-04

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


Pssm-ID: 273653 [Multi-domain]  Cd Length: 177  Bit Score: 40.80  E-value: 9.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468   650 PLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIA--------GVL-----------PDGKAEAIKHLQS 710
Cdd:TIGR01488  73 ALRPGARELISWLKERGIDTVIVSGGFDFFVEPVAEKLGIDDVFAnrlefddnGLLtgpiegqvnpeGECKGKVLKELLE 152
                          90       100
                  ....*....|....*....|....*
gi 16128468   711 EG----RQVAMVGDGINDAPALAQA 731
Cdd:TIGR01488 153 ESkitlKKIIAVGDSVNDLPMLKLA 177
P-type_ATPase_APLT_Neo1-like cd07541
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Neo1p and human ...
635-739 9.95e-04

Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Neo1p and human putative APLT, ATP9B; Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as a flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. The yeast Neo1 gene is an essential gene; Neo1p localizes to the endoplasmic reticulum and the Golgi complex and plays a role in membrane trafficking within the endomembrane system. Also included in this sub family is human putative ATPase phospholipid transporting 9B, ATP9B, which localizes to the trans-golgi network in a CDC50 protein-independent manner. Levels of ATP9B, along with levels of other ATPase genes, may contribute to expressivity of and atypical presentations of Hailey-Hailey disease (HHD), and the ATP9B gene has recently been identified as a putative Alzheimer's disease loci. 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: 319841 [Multi-domain]  Cd Length: 792  Bit Score: 42.78  E-value: 9.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 635 LAVDGKAVALLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAG---------------IDE-------- 691
Cdd:cd07541 464 LERELELLCLTGVEDKLQEDVKPTLELLRNAGIKIWMLTGDKLETATCIAKSSKlvsrgqyihvfrkvtTREeahlelnn 543
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 692 ---------VIAG----------------------------VLPDGKAEAIKHLQSE-GRQVAMVGDGINDAPALAQADV 733
Cdd:cd07541 544 lrrkhdcalVIDGeslevclkyyehefielacqlpavvccrCSPTQKAQIVRLIQKHtGKRTCAIGDGGNDVSMIQAADV 623

                ....*.
gi 16128468 734 GIAMGG 739
Cdd:cd07541 624 GVGIEG 629
HAD_PSP_eu cd04309
phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human ...
687-739 1.05e-03

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


Pssm-ID: 319801 [Multi-domain]  Cd Length: 202  Bit Score: 41.11  E-value: 1.05e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16128468 687 AGIDEVIAGVLPDGKAEAIKHLQSE--GRQVAMVGDGINDAPALAQADVGIAMGG 739
Cdd:cd04309 130 AGFDETQPTSRSGGKAKVIEQLKEKhhYKRVIMIGDGATDLEACPPADAFIGFGG 184
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
701-764 1.43e-03

haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like hydrolase enzymes.


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 41.45  E-value: 1.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128468   701 KAEAI----KHLQSEGRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETA-AITLMRHSlMGVADAL 764
Cdd:pfam08282 188 KGTALkalaKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVKAAAdYVTDSNNE-DGVAKAL 255
PLN02957 PLN02957
copper, zinc superoxide dismutase
12-63 4.58e-03

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 39.73  E-value: 4.58e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16128468   12 LSCGHCVKRVKESLEQRPDVEQADVSITEAHVT--GTASAEQLIETIKQAGYDA 63
Cdd:PLN02957  14 MKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRvlGSSPVKAMTAALEQTGRKA 67
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
657-739 8.14e-03

phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase PGP/CbbZ; Phosphoglycolate phosphatase catalyzes the dephosphorylation of phosphoglycolate; its activity requires divalent cations, especially Mg++. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319799 [Multi-domain]  Cd Length: 201  Bit Score: 38.49  E-value: 8.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128468 657 AALQRLHKAGYRLVMLTGDNPTTANAIAKEAGID---EVIAGVLPDGKAEAIKHL----QSEGRQVAMVGDGINDAPAlA 729
Cdd:cd04303  86 DMLRALHARGVRLAVVSSNSEENIRRVLGPEELIslfAVIEGSSLFGKAKKIRRVlrrtKITAAQVIYVGDETRDIEA-A 164
                        90
                ....*....|
gi 16128468 730 QAdVGIAMGG 739
Cdd:cd04303 165 RK-VGLAFAA 173
 
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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