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Conserved domains on  [gi|16258817|ref|NP_434690|]
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copper-transporting ATPase 1 [Rattus norvegicus]

Protein Classification

Cu(2+)-exporting ATPase (domain architecture ID 11534155)

Cu(2+)-exporting ATPase is a P-type ATPase that forms an ATP-dependent transmembrane ion pump involved in the control of the delivery and distribution of copper

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P-type_ATPase_Cu-like cd02094
P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A ...
646-1380 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  Cd Length: 647  Bit Score: 922.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  646 FLVSLFFCIPVMGLMIYMMVMDHHLATLNHNQNMSneeminmhssMFLerqilpgLSImnllslllclPVQFCGGWYFYI 725
Cdd:cd02094    3 LILSLLLTLPLLLLMMGGMLGPPLPLLLLQLNWWL----------QFL-------LAT----------PVQFWGGRPFYR 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  726 QAYKALRHKTANMDVLIVLATTIAFAYSLVILLVAMYErAKVNPITFFDTPPMLFVFIALGRWLEHIAKGKTSEALAKLI 805
Cdd:cd02094   56 GAWKALKHGSANMDTLVALGTSAAYLYSLVALLFPALF-PGGAPHVYFEAAAVIITFILLGKYLEARAKGKTSEAIKKLL 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  806 SLQATEATIVTLNSEnlllseEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPGSTVIAGS 885
Cdd:cd02094  135 GLQPKTARVIRDGKE------VEVPIEEVQVGDIVRVRPGEKIPVDGVVVEGESSVDESMLTGESLPVEKKPGDKVIGGT 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  886 INQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFIVLVSIVTLLVWIIIGFqnfeiveayfpg 965
Cdd:cd02094  209 INGNGSLLVRATRVGADTTLAQIIRLVEEAQGSKAPIQRLADRVSGVFVPVVIAIAILTFLVWLLLGP------------ 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  966 ynrsisrtETIIRFAFQASITVLCIACPCSLGLATPTAVMVGTGVGAQNGILIKGGEPLEMAHKVKVVVFDKTGTITHGT 1045
Cdd:cd02094  277 --------EPALTFALVAAVAVLVIACPCALGLATPTAIMVGTGRAAELGILIKGGEALERAHKVDTVVFDKTGTLTEGK 348
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1046 PVVNQVKVLVESnkiSRNKILAIVGTAESNSEHPLGAAVTKYCKQELDteTLGTCTDFQVVPGCGISCKVtniegllhks 1125
Cdd:cd02094  349 PEVTDVVPLPGD---DEDELLRLAASLEQGSEHPLAKAIVAAAKEKGL--ELPEVEDFEAIPGKGVRGTV---------- 413
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1126 nlkieenniknaslvqidaineqsspsssmiidahlsnavntQQYKVLIGNREWMIRNGLVISNDVDESMiEHERRGRTA 1205
Cdd:cd02094  414 ------------------------------------------DGRRVLVGNRRLMEENGIDLSALEAEAL-ALEEEGKTV 450
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1206 VLVTIDDELCGLIAIADTVKPEAELAVHILKSMGLEVVLMTGDNSKTARSIASQVGITKVFAEVLPSHKVAKVKQLQEEG 1285
Cdd:cd02094  451 VLVAVDGELAGLIAVADPLKPDAAEAIEALKKMGIKVVMLTGDNRRTARAIAKELGIDEVIAEVLPEDKAEKVKKLQAQG 530
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1286 KRVAMVGDGINDSPALAMASVGIAIGTGTDVAIEAADVVLIRNDLLDVVASIDLSRKTVKRIRINFVFALIYNLIGIPIA 1365
Cdd:cd02094  531 KKVAMVGDGINDAPALAQADVGIAIGSGTDVAIESADIVLMRGDLRGVVTAIDLSRATMRNIKQNLFWAFIYNVIGIPLA 610
                        730
                 ....*....|....*.
gi 16258817 1366 AGVFLPI-GLVLQPWM 1380
Cdd:cd02094  611 AGVLYPFgGILLSPMI 626
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
11-73 1.18e-17

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  Cd Length: 63  Bit Score: 81.11  E-value: 1.18e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16258817   11 TITVEGMTCISCVRTIEQQIGKVNGVHHIKVSLEEKSATVIYNPKLqTPKTLQEAIDDMGFDA 73
Cdd:cd00371    1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPEV-SPEELLEAIEDAGYKA 62
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
380-442 1.72e-17

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  Cd Length: 63  Bit Score: 80.73  E-value: 1.72e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16258817  380 VININGMTCNSCVQSIEGVISKKPGVKSIHVSLTNSTGTIEYDPlLTSPEPLREAIEDMGFDA 442
Cdd:cd00371    1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEELLEAIEDAGYKA 62
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
174-236 8.62e-17

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  Cd Length: 63  Bit Score: 78.42  E-value: 8.62e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16258817  174 KMRVEGMTCHSCTSTIEGKVGKLQGVQRIKVSLDNQEATIVYQPHlITAEEIKKQIEAVGFPA 236
Cdd:cd00371    1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKA 62
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
484-545 1.16e-15

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  Cd Length: 63  Bit Score: 75.33  E-value: 1.16e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16258817  484 IQVSGMTCASCVANIERNLRREEGIYSVLVALMAGKAEVRYNPAViQPRVIAELIRELGFGA 545
Cdd:cd00371    2 LSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPEV-SPEELLEAIEDAGYKA 62
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
559-622 2.27e-15

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  Cd Length: 63  Bit Score: 74.56  E-value: 2.27e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16258817  559 ELVVRGMTCASCVHKIESTLTKHKGIFYCSVALATNKAHIKYDPEiIGPRDIIHTIGNLGFEAS 622
Cdd:cd00371    1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKAR 63
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
280-337 3.20e-15

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  Cd Length: 63  Bit Score: 74.18  E-value: 3.20e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16258817  280 TFTIDGMHCKSCVSNIESALSTLQYVSSIVVSLENRSAIVKYNASlVTPEILRKAIEA 337
Cdd:cd00371    1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIED 57
 
Name Accession Description Interval E-value
P-type_ATPase_Cu-like cd02094
P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A ...
646-1380 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  Cd Length: 647  Bit Score: 922.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  646 FLVSLFFCIPVMGLMIYMMVMDHHLATLNHNQNMSneeminmhssMFLerqilpgLSImnllslllclPVQFCGGWYFYI 725
Cdd:cd02094    3 LILSLLLTLPLLLLMMGGMLGPPLPLLLLQLNWWL----------QFL-------LAT----------PVQFWGGRPFYR 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  726 QAYKALRHKTANMDVLIVLATTIAFAYSLVILLVAMYErAKVNPITFFDTPPMLFVFIALGRWLEHIAKGKTSEALAKLI 805
Cdd:cd02094   56 GAWKALKHGSANMDTLVALGTSAAYLYSLVALLFPALF-PGGAPHVYFEAAAVIITFILLGKYLEARAKGKTSEAIKKLL 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  806 SLQATEATIVTLNSEnlllseEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPGSTVIAGS 885
Cdd:cd02094  135 GLQPKTARVIRDGKE------VEVPIEEVQVGDIVRVRPGEKIPVDGVVVEGESSVDESMLTGESLPVEKKPGDKVIGGT 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  886 INQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFIVLVSIVTLLVWIIIGFqnfeiveayfpg 965
Cdd:cd02094  209 INGNGSLLVRATRVGADTTLAQIIRLVEEAQGSKAPIQRLADRVSGVFVPVVIAIAILTFLVWLLLGP------------ 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  966 ynrsisrtETIIRFAFQASITVLCIACPCSLGLATPTAVMVGTGVGAQNGILIKGGEPLEMAHKVKVVVFDKTGTITHGT 1045
Cdd:cd02094  277 --------EPALTFALVAAVAVLVIACPCALGLATPTAIMVGTGRAAELGILIKGGEALERAHKVDTVVFDKTGTLTEGK 348
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1046 PVVNQVKVLVESnkiSRNKILAIVGTAESNSEHPLGAAVTKYCKQELDteTLGTCTDFQVVPGCGISCKVtniegllhks 1125
Cdd:cd02094  349 PEVTDVVPLPGD---DEDELLRLAASLEQGSEHPLAKAIVAAAKEKGL--ELPEVEDFEAIPGKGVRGTV---------- 413
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1126 nlkieenniknaslvqidaineqsspsssmiidahlsnavntQQYKVLIGNREWMIRNGLVISNDVDESMiEHERRGRTA 1205
Cdd:cd02094  414 ------------------------------------------DGRRVLVGNRRLMEENGIDLSALEAEAL-ALEEEGKTV 450
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1206 VLVTIDDELCGLIAIADTVKPEAELAVHILKSMGLEVVLMTGDNSKTARSIASQVGITKVFAEVLPSHKVAKVKQLQEEG 1285
Cdd:cd02094  451 VLVAVDGELAGLIAVADPLKPDAAEAIEALKKMGIKVVMLTGDNRRTARAIAKELGIDEVIAEVLPEDKAEKVKKLQAQG 530
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1286 KRVAMVGDGINDSPALAMASVGIAIGTGTDVAIEAADVVLIRNDLLDVVASIDLSRKTVKRIRINFVFALIYNLIGIPIA 1365
Cdd:cd02094  531 KKVAMVGDGINDAPALAQADVGIAIGSGTDVAIESADIVLMRGDLRGVVTAIDLSRATMRNIKQNLFWAFIYNVIGIPLA 610
                        730
                 ....*....|....*.
gi 16258817 1366 AGVFLPI-GLVLQPWM 1380
Cdd:cd02094  611 AGVLYPFgGILLSPMI 626
ATPase-IB1_Cu TIGR01511
copper-(or silver)-translocating P-type ATPase; This model describes the P-type ATPase ...
719-1381 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  Cd Length: 562  Bit Score: 786.85  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    719 GGWYFYIQAYKALRHKTANMDVLIVLATTIAFAYSLVILLVAMYERaKVNPITFFDTPPMLFVFIALGRWLEHIAKGKTS 798
Cdd:TIGR01511    1 AGRPFYKSAWKALRHKAPNMDTLIALGTTVAYGYSLVALLANQVLT-GLHVHTFFDASAMLITFILLGRWLEMLAKGRAS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    799 EALAKLISLQATEATIVTLNSEnlllsEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPG 878
Cdd:TIGR01511   80 DALSKLAKLQPSTATLLTKDGS-----IEEVPVALLQPGDIVKVLPGEKIPVDGTVIEGESEVDESLVTGESLPVPKKVG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    879 STVIAGSINQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFIVLVSIVTLLVWIiigfqnfei 958
Cdd:TIGR01511  155 DPVIAGTVNGTGSLVVRATATGEDTTLAQIVRLVRQAQQSKAPIQRLADKVAGYFVPVVIAIALITFVIWL--------- 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    959 veayfpgynrsisrtetiirFAFQASITVLCIACPCSLGLATPTAVMVGTGVGAQNGILIKGGEPLEMAHKVKVVVFDKT 1038
Cdd:TIGR01511  226 --------------------FALEFAVTVLIIACPCALGLATPTVIAVATGLAAKNGVLIKDGDALERAANIDTVVFDKT 285
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1039 GTITHGTPVVNQVKVLVESnkiSRNKILAIVGTAESNSEHPLGAAVTKYCKQELdtETLGTCTDFQVVPGCGISCKVTNi 1118
Cdd:TIGR01511  286 GTLTQGKPTVTDVHVFGDR---DRTELLALAAALEAGSEHPLAKAIVSYAKEKG--ITLVTVSDFKAIPGIGVEGTVEG- 359
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1119 egllhksnlkieenniknaslvqidaineqsspsssmiidahlsnavntqqYKVLIGNREWMIRNGLVISndvdesmiEH 1198
Cdd:TIGR01511  360 ---------------------------------------------------TKIQLGNEKLLGENAIKID--------GK 380
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1199 ERRGRTAVLVTIDDELCGLIAIADTVKPEAELAVHILKSMGLEVVLMTGDNSKTARSIASQVGITkVFAEVLPSHKVAKV 1278
Cdd:TIGR01511  381 AGQGSTVVLVAVNGELAGVFALEDQLRPEAKEVIQALKRRGIEPVMLTGDNRKTAKAVAKELGID-VRAEVLPDDKAALI 459
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1279 KQLQEEGKRVAMVGDGINDSPALAMASVGIAIGTGTDVAIEAADVVLIRNDLLDVVASIDLSRKTVKRIRINFVFALIYN 1358
Cdd:TIGR01511  460 KKLQEKGPVVAMVGDGINDAPALAQADVGIAIGAGTDVAIEAADVVLLRNDLNDVATAIDLSRKTLRRIKQNLLWAFGYN 539
                          650       660
                   ....*....|....*....|...
gi 16258817   1359 LIGIPIAAGVFLPIGLVLQPWMG 1381
Cdd:TIGR01511  540 VIAIPIAAGVLYPIGILLSPAVA 562
ZntA COG2217
Cation transport ATPase [Inorganic ion transport and metabolism];
558-1381 0e+00

Cation transport ATPase [Inorganic ion transport and metabolism];


Pssm-ID: 225127  Cd Length: 713  Bit Score: 769.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  558 LELVVRGMTCASCVHKIEStLTKHKGIFYCSVALATNKAHIKYDPEIIGPR-DIIHTIGNLGFEASLVKKDRSANHLDHK 636
Cdd:COG2217    4 TSLSVEGMTCAACASRIEA-LNKLPGVEEARVNLATERATVVYDPEEVDLPaDIVAAVEKAGYSARLTAALADPAEAEAR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  637 REIKQWRgSFLVSLFFCIPVMGLMIYMMvmdhhlatlnhnqnmsneeminmhssmflerqilPGLSIMNLLSLLLCLPVQ 716
Cdd:COG2217   83 LLRELLR-RLIIAGLLTLPLLLLSLGLL----------------------------------LGAFLLPWVSFLLATPVL 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  717 FCGGWYFYIQAYKALRHKTANMDVLIVLATTIAFAYSLVILLVAMYerakvnpitfFDTPPMLFVFIALGRWLEHIAKGK 796
Cdd:COG2217  128 FYGGWPFYRGAWRALRRGRLNMDTLVALATIGAYAYSLYATLFPVY----------FEEAAMLIFLFLLGRYLEARAKGR 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  797 TSEALAKLISLQATEATIVTLNSEnlllsEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKK 876
Cdd:COG2217  198 ARRAIRALLDLAPKTATVVRGDGE-----EEEVPVEEVQVGDIVLVRPGERIPVDGVVVSGSSSVDESMLTGESLPVEKK 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  877 PGSTVIAGSINQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFIVLVSIVTLLVWIIIGFQNF 956
Cdd:COG2217  273 PGDEVFAGTVNLDGSLTIRVTRVGADTTLARIIRLVEEAQSSKAPIQRLADRVASYFVPVVLVIAALTFALWPLFGGGDW 352
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  957 EiveayfpgynrsisrtetiirFAFQASITVLCIACPCSLGLATPTAVMVGTGVGAQNGILIKGGEPLEMAHKVKVVVFD 1036
Cdd:COG2217  353 E---------------------TALYRALAVLVIACPCALGLATPTAILVGIGRAARRGILIKGGEALERLAKVDTVVFD 411
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1037 KTGTITHGTPVVNQVKVLvesnKISRNKILAIVGTAESNSEHPLGAAVTKYCKQELDTETlgtcTDFQVVPGCGISCKVT 1116
Cdd:COG2217  412 KTGTLTEGKPEVTDVVAL----DGDEDELLALAAALEQHSEHPLAKAIVKAAAERGLPDV----EDFEEIPGRGVEAEVD 483
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1117 NIEgllhksnlkieenniknaslvqidaineqsspsssmiidahlsnavntqqykVLIGNREWMIRNGLVISNdVDESMI 1196
Cdd:COG2217  484 GER----------------------------------------------------VLVGNARLLGEEGIDLPL-LSERIE 510
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1197 EHERRGRTAVLVTIDDELCGLIAIADTVKPEAELAVHILKSMGLEVVLMTGDNSKTARSIASQVGITKVFAEVLPSHKVA 1276
Cdd:COG2217  511 ALESEGKTVVFVAVDGKLVGVIALADELRPDAKEAIAALKALGIKVVMLTGDNRRTAEAIAKELGIDEVRAELLPEDKAE 590
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1277 KVKQLQEEGKRVAMVGDGINDSPALAMASVGIAIGTGTDVAIEAADVVLIRNDLLDVVASIDLSRKTVKRIRINFVFALI 1356
Cdd:COG2217  591 IVRELQAEGRKVAMVGDGINDAPALAAADVGIAMGSGTDVAIEAADVVLMRDDLSAVPEAIDLSRATRRIIKQNLFWAFG 670
                        810       820
                 ....*....|....*....|....*
gi 16258817 1357 YNLIGIPIAAGVFLPiglvlqPWMG 1381
Cdd:COG2217  671 YNAIAIPLAAGGLLT------PWIA 689
copA PRK10671
copper exporting ATPase; Provisional
375-1378 2.39e-136

copper exporting ATPase; Provisional


Pssm-ID: 182635  Cd Length: 834  Bit Score: 444.57  E-value: 2.39e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   375 LTQEVVININGMTCNSCVQSIEGVISKKPGVKSIHVSLTNS--TGTieydpllTSPEPLREAIEDMGFDAVLpadmkepl 452
Cdd:PRK10671    1 MSQTIDLTLDGLSCGHCVKRVKESLEQRPDVEQADVSITEAhvTGT-------ASAEALIETIKQAGYDASV-------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   453 vviAQPSLEtPLLPSTTEPEnvmtpvqnkcyiqvsgmtcascvaniernlrreegiysvlvALMAGKAEVrynPAviqpr 532
Cdd:PRK10671   66 ---SHPKAK-PLTESSIPSE-----------------------------------------ALTAASEEL---PA----- 92
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   533 viaelirelgfgavvmENAGEGNGIlELVVRGMTCASCVHKIESTLTKHKGIFYCSVALATNKAHIKYDPEiigPRDIIH 612
Cdd:PRK10671   93 ----------------ATADDDDSQ-QLLLSGMSCASCVSRVQNALQSVPGVTQARVNLAERTALVMGSAS---PQDLVQ 152
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   613 TIGNLGFEASLVKKD---RSANHLDHKREIKQWRGSFLVSLFFCIPVmglMIYMMVMDHHLATlNHNQnmsneeminmhs 689
Cdd:PRK10671  153 AVEKAGYGAEAIEDDakrRERQQETAQATMKRFRWQAIVALAVGIPV---MVWGMIGDNMMVT-ADNR------------ 216
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   690 SMFLERQILPgLSIMnllslllclpvQFCGGwYFYIQAYKALRHKTANMDVLIVLATTIAFAYSLVILL----VAMYERA 765
Cdd:PRK10671  217 SLWLVIGLIT-LAVM-----------VFAGG-HFYRSAWKSLLNGSATMDTLVALGTGAAWLYSMSVNLwpqwFPMEARH 283
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   766 kvnpiTFFDTPPMLFVFIALGRWLEHIAKGKTSEALAKLISLQATEATIVTLNSENLL-LSEeqvdvelVQRGDIIKVVP 844
Cdd:PRK10671  284 -----LYYEASAMIIGLINLGHMLEARARQRSSKALEKLLDLTPPTARVVTDEGEKSVpLAD-------VQPGMLLRLTT 351
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   845 GGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPGSTVIAGSINQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQ 924
Cdd:PRK10671  352 GDRVPVDGEITQGEAWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQ 431
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   925 FADKLSGYFVPFIVLVSIVTLLVWiiigfqnfeiveaYFPGYNRSISRTETIIrfafqasITVLCIACPCSLGLATPTAV 1004
Cdd:PRK10671  432 LADKISAVFVPVVVVIALVSAAIW-------------YFFGPAPQIVYTLVIA-------TTVLIIACPCALGLATPMSI 491
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  1005 MVGTGVGAQNGILIKGGEPLEMAHKVKVVVFDKTGTITHGTPVVNQVKVLvesNKISRNKILAIVGTAESNSEHPLGAAV 1084
Cdd:PRK10671  492 ISGVGRAAEFGVLVRDADALQRASTLDTLVFDKTGTLTEGKPQVVAVKTF---NGVDEAQALRLAAALEQGSSHPLARAI 568
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  1085 TkyckQELDTETLGTCTDFQVVPGCGISCKVTNIEgllhksnlkieenniknaslvqidaineqsspsssmiidahlsna 1164
Cdd:PRK10671  569 L----DKAGDMTLPQVNGFRTLRGLGVSGEAEGHA--------------------------------------------- 599
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  1165 vntqqykVLIGNREWMIRNGlVISNDVDESMIEHERRGRTAVLVTIDDELCGLIAIADTVKPEAELAVHILKSMGLEVVL 1244
Cdd:PRK10671  600 -------LLLGNQALLNEQQ-VDTKALEAEITAQASQGATPVLLAVDGKAAALLAIRDPLRSDSVAALQRLHKAGYRLVM 671
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  1245 MTGDNSKTARSIASQVGITKVFAEVLPSHKVAKVKQLQEEGKRVAMVGDGINDSPALAMASVGIAIGTGTDVAIEAADVV 1324
Cdd:PRK10671  672 LTGDNPTTANAIAKEAGIDEVIAGVLPDGKAEAIKRLQSQGRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETAAIT 751
                         970       980       990      1000      1010
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16258817  1325 LIRNDLLDVVASIDLSRKTVKRIRINFVFALIYNLIGIPIAAGVFLPI-GLVLQP 1378
Cdd:PRK10671  752 LMRHSLMGVADALAISRATLRNMKQNLLGAFIYNSLGIPIAAGILWPFtGTLLNP 806
E1-E2_ATPase pfam00122
E1-E2 ATPase;
778-1025 5.24e-60

E1-E2 ATPase;


Pssm-ID: 306602  Cd Length: 221  Bit Score: 208.18  E-value: 5.24e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    778 MLFVFIALGRWLEHIAKGKTSEALAKLISLQATEATIVTLNSEnlllseEQVDVELVQRGDIIKVVPGGKFPVDGRVIEG 857
Cdd:pfam00122    2 IILLLVLLNALLEFYQEARARKALKALKSLLPPTATVLRDGGE------VEVPADELVPGDIVLLKPGERIPADGRIVEG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    858 HSMVDESLITGEAMPVAKKPGSTVIAGSINQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFI 937
Cdd:pfam00122   76 SLSVDESALTGESLPVEKKKGDMVFSGTVVVSGSAKAVVTATGEDTTLGKIARLVEEAKSKKTPLQRLLDKLAKYFTPVV 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    938 VLVSIVTLLVWIIIGFQnfeiveayfpgynrsisrtetiIRFAFQASITVLCIACPCSLGLATPTAVMVGTGVGAQNGIL 1017
Cdd:pfam00122  156 LLLALAVFLLTLLLGGD----------------------LAEALLRALAVLVAACPCALPLATPLALAVGARRLAKKGIL 213

                   ....*...
gi 16258817   1018 IKGGEPLE 1025
Cdd:pfam00122  214 VKRLSALE 221
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
11-73 1.18e-17

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  Cd Length: 63  Bit Score: 81.11  E-value: 1.18e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16258817   11 TITVEGMTCISCVRTIEQQIGKVNGVHHIKVSLEEKSATVIYNPKLqTPKTLQEAIDDMGFDA 73
Cdd:cd00371    1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPEV-SPEELLEAIEDAGYKA 62
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
380-442 1.72e-17

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  Cd Length: 63  Bit Score: 80.73  E-value: 1.72e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16258817  380 VININGMTCNSCVQSIEGVISKKPGVKSIHVSLTNSTGTIEYDPlLTSPEPLREAIEDMGFDA 442
Cdd:cd00371    1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEELLEAIEDAGYKA 62
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
174-236 8.62e-17

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  Cd Length: 63  Bit Score: 78.42  E-value: 8.62e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16258817  174 KMRVEGMTCHSCTSTIEGKVGKLQGVQRIKVSLDNQEATIVYQPHlITAEEIKKQIEAVGFPA 236
Cdd:cd00371    1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKA 62
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
484-545 1.16e-15

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  Cd Length: 63  Bit Score: 75.33  E-value: 1.16e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16258817  484 IQVSGMTCASCVANIERNLRREEGIYSVLVALMAGKAEVRYNPAViQPRVIAELIRELGFGA 545
Cdd:cd00371    2 LSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPEV-SPEELLEAIEDAGYKA 62
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
559-622 2.27e-15

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  Cd Length: 63  Bit Score: 74.56  E-value: 2.27e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16258817  559 ELVVRGMTCASCVHKIESTLTKHKGIFYCSVALATNKAHIKYDPEiIGPRDIIHTIGNLGFEAS 622
Cdd:cd00371    1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKAR 63
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
280-337 3.20e-15

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  Cd Length: 63  Bit Score: 74.18  E-value: 3.20e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16258817  280 TFTIDGMHCKSCVSNIESALSTLQYVSSIVVSLENRSAIVKYNASlVTPEILRKAIEA 337
Cdd:cd00371    1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIED 57
HMA pfam00403
Heavy-metal-associated domain;
280-337 1.01e-12

Heavy-metal-associated domain;


Pssm-ID: 306833  Cd Length: 58  Bit Score: 66.48  E-value: 1.01e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 16258817    280 TFTIDGMHCKSCVSNIESALSTLQYVSSIVVSLENRSAIVKYNASLVTPEILRKAIEA 337
Cdd:pfam00403    1 TFRVEGMHCGSCAKKVEKALSKLPGVSSVSVDLATKTVTVTGDAESTKLRKLVEAIEK 58
HMA pfam00403
Heavy-metal-associated domain;
380-437 8.54e-12

Heavy-metal-associated domain;


Pssm-ID: 306833  Cd Length: 58  Bit Score: 63.79  E-value: 8.54e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 16258817    380 VININGMTCNSCVQSIEGVISKKPGVKSIHVSLTNSTGTIEYDPLLTSPEPLREAIED 437
Cdd:pfam00403    1 TFRVEGMHCGSCAKKVEKALSKLPGVSSVSVDLATKTVTVTGDAESTKLRKLVEAIEK 58
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
377-443 1.67e-11

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 225328  Cd Length: 71  Bit Score: 63.55  E-value: 1.67e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16258817  377 QEVVININGMTCNSCVQSIEGVISKKPGVKSIHVSLTNSTGTIEYDPLLTSPEPLREAIEDMGFDAV 443
Cdd:COG2608    2 MKTTLKVEGMTCGHCVKTVEKALEEVDGVASVDVDLEKGTATVTFDSNKVDIEAIIEAIEDAGYKVE 68
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
173-236 4.28e-11

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 225328  Cd Length: 71  Bit Score: 62.40  E-value: 4.28e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16258817  173 LKMRVEGMTCHSCTSTIEGKVGKLQGVQRIKVSLDNQEATIVYQPHLITAEEIKKQIEAVGFPA 236
Cdd:COG2608    4 TTLKVEGMTCGHCVKTVEKALEEVDGVASVDVDLEKGTATVTFDSNKVDIEAIIEAIEDAGYKV 67
HMA pfam00403
Heavy-metal-associated domain;
11-68 4.84e-11

Heavy-metal-associated domain;


Pssm-ID: 306833  Cd Length: 58  Bit Score: 61.86  E-value: 4.84e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 16258817     11 TITVEGMTCISCVRTIEQQIGKVNGVHHIKVSLEEKSATVIYNPKLQTPKTLQEAIDD 68
Cdd:pfam00403    1 TFRVEGMHCGSCAKKVEKALSKLPGVSSVSVDLATKTVTVTGDAESTKLRKLVEAIEK 58
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
10-73 1.19e-10

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 225328  Cd Length: 71  Bit Score: 60.86  E-value: 1.19e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16258817   10 ITITVEGMTCISCVRTIEQQIGKVNGVHHIKVSLEEKSATVIYNPKLQTPKTLQEAIDDMGFDA 73
Cdd:COG2608    4 TTLKVEGMTCGHCVKTVEKALEEVDGVASVDVDLEKGTATVTFDSNKVDIEAIIEAIEDAGYKV 67
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
10-73 3.85e-10

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  Cd Length: 66  Bit Score: 59.48  E-value: 3.85e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16258817     10 ITITVEGMTCISCVRTIEQQIGKVNGVHHIKVSLEEKSATVIYNPKLQTPKTLQEAIDDMGFDA 73
Cdd:TIGR00003    2 QTFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEV 65
HMA pfam00403
Heavy-metal-associated domain;
176-231 2.66e-09

Heavy-metal-associated domain;


Pssm-ID: 306833  Cd Length: 58  Bit Score: 56.85  E-value: 2.66e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 16258817    176 RVEGMTCHSCTSTIEGKVGKLQGVQRIKVSLDNQEATIVYQPHLITAEEIKKQIEA 231
Cdd:pfam00403    3 RVEGMHCGSCAKKVEKALSKLPGVSSVSVDLATKTVTVTGDAESTKLRKLVEAIEK 58
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
279-336 2.68e-09

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 225328  Cd Length: 71  Bit Score: 57.01  E-value: 2.68e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16258817  279 ITFTIDGMHCKSCVSNIESALSTLQYVSSIVVSLENRSAIVKYNASLVTPEILRKAIE 336
Cdd:COG2608    4 TTLKVEGMTCGHCVKTVEKALEEVDGVASVDVDLEKGTATVTFDSNKVDIEAIIEAIE 61
HMA pfam00403
Heavy-metal-associated domain;
484-540 3.74e-09

Heavy-metal-associated domain;


Pssm-ID: 306833  Cd Length: 58  Bit Score: 56.08  E-value: 3.74e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 16258817    484 IQVSGMTCASCVANIERNLRREEGIYSVLVALMAGKAEVRYNPAVIQPRVIAELIRE 540
Cdd:pfam00403    2 FRVEGMHCGSCAKKVEKALSKLPGVSSVSVDLATKTVTVTGDAESTKLRKLVEAIEK 58
HMA pfam00403
Heavy-metal-associated domain;
562-614 1.03e-08

Heavy-metal-associated domain;


Pssm-ID: 306833  Cd Length: 58  Bit Score: 54.93  E-value: 1.03e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 16258817    562 VRGMTCASCVHKIESTLTKHKGIFYCSVALATNKAHIKYDPEIIGPRDIIHTI 614
Cdd:pfam00403    4 VEGMHCGSCAKKVEKALSKLPGVSSVSVDLATKTVTVTGDAESTKLRKLVEAI 56
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
378-443 6.69e-08

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  Cd Length: 66  Bit Score: 52.93  E-value: 6.69e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16258817    378 EVVININGMTCNSCVQSIEGVISKKPGVKSIHVSLTNSTGTIEYDPLLTSPEPLREAIEDMGFDAV 443
Cdd:TIGR00003    1 KQTFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEVE 66
PRK13748 PRK13748
putative mercuric reductase; Provisional
381-444 8.85e-08

putative mercuric reductase; Provisional


Pssm-ID: 184298  Cd Length: 561  Bit Score: 56.31  E-value: 8.85e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16258817   381 ININGMTCNSCVQSIEGVISKKPGVKSIHVSLTNSTGTIEYDPlLTSPEPLREAIEDMGFDAVL 444
Cdd:PRK13748    4 LKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEV-GTSPDALTAAVAGLGYRATL 66
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
177-236 9.38e-08

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  Cd Length: 66  Bit Score: 52.16  E-value: 9.38e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    177 VEGMTCHSCTSTIEGKVGKLQGVQRIKVSLDNQEATIVYQPHLITAEEIKKQIEAVGFPA 236
Cdd:TIGR00003    6 VKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEV 65
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
483-547 4.08e-07

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 225328  Cd Length: 71  Bit Score: 50.46  E-value: 4.08e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16258817  483 YIQVSGMTCASCVANIERNLRREEGIYSVLVALMAGKAEVRYNPAVIQPRVIAELIRELGFGAVV 547
Cdd:COG2608    5 TLKVEGMTCGHCVKTVEKALEEVDGVASVDVDLEKGTATVTFDSNKVDIEAIIEAIEDAGYKVEE 69
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
484-546 9.41e-07

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  Cd Length: 66  Bit Score: 49.46  E-value: 9.41e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16258817    484 IQVSGMTCASCVANIERNLRREEGIYSVLVALMAGKAEVRYNPAVIQPRVIAELIRELGFGAV 546
Cdd:TIGR00003    4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEVE 66
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
279-336 1.17e-06

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  Cd Length: 66  Bit Score: 49.08  E-value: 1.17e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 16258817    279 ITFTIDGMHCKSCVSNIESALSTLQYVSSIVVSLENRSAIVKYNASLVTPEILRKAIE 336
Cdd:TIGR00003    2 QTFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAIL 59
PRK13748 PRK13748
putative mercuric reductase; Provisional
10-82 1.25e-06

putative mercuric reductase; Provisional


Pssm-ID: 184298  Cd Length: 561  Bit Score: 52.85  E-value: 1.25e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16258817    10 ITITVEGMTCISCVRTIEQQIGKVNGVHHIKVSLEEKSATVIYNPKLqTPKTLQEAIDDMGFDALLHNANPLP 82
Cdd:PRK13748    2 TTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVGT-SPDALTAAVAGLGYRATLADAPPTD 73
PRK13748 PRK13748
putative mercuric reductase; Provisional
559-645 1.18e-05

putative mercuric reductase; Provisional


Pssm-ID: 184298  Cd Length: 561  Bit Score: 49.76  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   559 ELVVRGMTCASCVHKIESTLTKHKGIFYCSVALATNKAHIKYDPEiIGPRDIIHTIGNLGFEASLVKKDRSANHLDHKRE 638
Cdd:PRK13748    3 TLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVG-TSPDALTAAVAGLGYRATLADAPPTDNRGGLLDK 81

                  ....*..
gi 16258817   639 IKQWRGS 645
Cdd:PRK13748   82 MRGWLGG 88
PRK13748 PRK13748
putative mercuric reductase; Provisional
278-350 5.14e-05

putative mercuric reductase; Provisional


Pssm-ID: 184298  Cd Length: 561  Bit Score: 47.45  E-value: 5.14e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16258817   278 AITFTIDGMHCKSCVSNIESALSTLQYVSSIVVSLENRSAIVKYNASlVTPEILRKAIEAVSpgqYRVSISSE 350
Cdd:PRK13748    1 MTTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVG-TSPDALTAAVAGLG---YRATLADA 69
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
558-625 6.58e-05

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 225328  Cd Length: 71  Bit Score: 43.91  E-value: 6.58e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16258817  558 LELVVRGMTCASCVHKIESTLTKHKGIFYCSVALATNKAHIKYDPEIIGPRDIIHTIGNLGFEASLVK 625
Cdd:COG2608    4 TTLKVEGMTCGHCVKTVEKALEEVDGVASVDVDLEKGTATVTFDSNKVDIEAIIEAIEDAGYKVEEIK 71
PRK13748 PRK13748
putative mercuric reductase; Provisional
484-547 8.15e-05

putative mercuric reductase; Provisional


Pssm-ID: 184298  Cd Length: 561  Bit Score: 47.07  E-value: 8.15e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16258817   484 IQVSGMTCASCVANIERNLRREEGIYSVLVALMAGKAEVRYNPAVIQPRVIAElIRELGFGAVV 547
Cdd:PRK13748    4 LKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVGTSPDALTAA-VAGLGYRATL 66
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
559-621 3.38e-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  Cd Length: 66  Bit Score: 41.76  E-value: 3.38e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16258817    559 ELVVRGMTCASCVHKIESTLTKHKGIFYCSVALATNKAHIKYDPEIIGPRDIIHTIGNLGFEA 621
Cdd:TIGR00003    3 TFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEV 65
 
Name Accession Description Interval E-value
P-type_ATPase_Cu-like cd02094
P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A ...
646-1380 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  Cd Length: 647  Bit Score: 922.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  646 FLVSLFFCIPVMGLMIYMMVMDHHLATLNHNQNMSneeminmhssMFLerqilpgLSImnllslllclPVQFCGGWYFYI 725
Cdd:cd02094    3 LILSLLLTLPLLLLMMGGMLGPPLPLLLLQLNWWL----------QFL-------LAT----------PVQFWGGRPFYR 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  726 QAYKALRHKTANMDVLIVLATTIAFAYSLVILLVAMYErAKVNPITFFDTPPMLFVFIALGRWLEHIAKGKTSEALAKLI 805
Cdd:cd02094   56 GAWKALKHGSANMDTLVALGTSAAYLYSLVALLFPALF-PGGAPHVYFEAAAVIITFILLGKYLEARAKGKTSEAIKKLL 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  806 SLQATEATIVTLNSEnlllseEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPGSTVIAGS 885
Cdd:cd02094  135 GLQPKTARVIRDGKE------VEVPIEEVQVGDIVRVRPGEKIPVDGVVVEGESSVDESMLTGESLPVEKKPGDKVIGGT 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  886 INQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFIVLVSIVTLLVWIIIGFqnfeiveayfpg 965
Cdd:cd02094  209 INGNGSLLVRATRVGADTTLAQIIRLVEEAQGSKAPIQRLADRVSGVFVPVVIAIAILTFLVWLLLGP------------ 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  966 ynrsisrtETIIRFAFQASITVLCIACPCSLGLATPTAVMVGTGVGAQNGILIKGGEPLEMAHKVKVVVFDKTGTITHGT 1045
Cdd:cd02094  277 --------EPALTFALVAAVAVLVIACPCALGLATPTAIMVGTGRAAELGILIKGGEALERAHKVDTVVFDKTGTLTEGK 348
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1046 PVVNQVKVLVESnkiSRNKILAIVGTAESNSEHPLGAAVTKYCKQELDteTLGTCTDFQVVPGCGISCKVtniegllhks 1125
Cdd:cd02094  349 PEVTDVVPLPGD---DEDELLRLAASLEQGSEHPLAKAIVAAAKEKGL--ELPEVEDFEAIPGKGVRGTV---------- 413
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1126 nlkieenniknaslvqidaineqsspsssmiidahlsnavntQQYKVLIGNREWMIRNGLVISNDVDESMiEHERRGRTA 1205
Cdd:cd02094  414 ------------------------------------------DGRRVLVGNRRLMEENGIDLSALEAEAL-ALEEEGKTV 450
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1206 VLVTIDDELCGLIAIADTVKPEAELAVHILKSMGLEVVLMTGDNSKTARSIASQVGITKVFAEVLPSHKVAKVKQLQEEG 1285
Cdd:cd02094  451 VLVAVDGELAGLIAVADPLKPDAAEAIEALKKMGIKVVMLTGDNRRTARAIAKELGIDEVIAEVLPEDKAEKVKKLQAQG 530
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1286 KRVAMVGDGINDSPALAMASVGIAIGTGTDVAIEAADVVLIRNDLLDVVASIDLSRKTVKRIRINFVFALIYNLIGIPIA 1365
Cdd:cd02094  531 KKVAMVGDGINDAPALAQADVGIAIGSGTDVAIESADIVLMRGDLRGVVTAIDLSRATMRNIKQNLFWAFIYNVIGIPLA 610
                        730
                 ....*....|....*.
gi 16258817 1366 AGVFLPI-GLVLQPWM 1380
Cdd:cd02094  611 AGVLYPFgGILLSPMI 626
ATPase-IB1_Cu TIGR01511
copper-(or silver)-translocating P-type ATPase; This model describes the P-type ATPase ...
719-1381 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  Cd Length: 562  Bit Score: 786.85  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    719 GGWYFYIQAYKALRHKTANMDVLIVLATTIAFAYSLVILLVAMYERaKVNPITFFDTPPMLFVFIALGRWLEHIAKGKTS 798
Cdd:TIGR01511    1 AGRPFYKSAWKALRHKAPNMDTLIALGTTVAYGYSLVALLANQVLT-GLHVHTFFDASAMLITFILLGRWLEMLAKGRAS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    799 EALAKLISLQATEATIVTLNSEnlllsEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPG 878
Cdd:TIGR01511   80 DALSKLAKLQPSTATLLTKDGS-----IEEVPVALLQPGDIVKVLPGEKIPVDGTVIEGESEVDESLVTGESLPVPKKVG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    879 STVIAGSINQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFIVLVSIVTLLVWIiigfqnfei 958
Cdd:TIGR01511  155 DPVIAGTVNGTGSLVVRATATGEDTTLAQIVRLVRQAQQSKAPIQRLADKVAGYFVPVVIAIALITFVIWL--------- 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    959 veayfpgynrsisrtetiirFAFQASITVLCIACPCSLGLATPTAVMVGTGVGAQNGILIKGGEPLEMAHKVKVVVFDKT 1038
Cdd:TIGR01511  226 --------------------FALEFAVTVLIIACPCALGLATPTVIAVATGLAAKNGVLIKDGDALERAANIDTVVFDKT 285
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1039 GTITHGTPVVNQVKVLVESnkiSRNKILAIVGTAESNSEHPLGAAVTKYCKQELdtETLGTCTDFQVVPGCGISCKVTNi 1118
Cdd:TIGR01511  286 GTLTQGKPTVTDVHVFGDR---DRTELLALAAALEAGSEHPLAKAIVSYAKEKG--ITLVTVSDFKAIPGIGVEGTVEG- 359
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1119 egllhksnlkieenniknaslvqidaineqsspsssmiidahlsnavntqqYKVLIGNREWMIRNGLVISndvdesmiEH 1198
Cdd:TIGR01511  360 ---------------------------------------------------TKIQLGNEKLLGENAIKID--------GK 380
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1199 ERRGRTAVLVTIDDELCGLIAIADTVKPEAELAVHILKSMGLEVVLMTGDNSKTARSIASQVGITkVFAEVLPSHKVAKV 1278
Cdd:TIGR01511  381 AGQGSTVVLVAVNGELAGVFALEDQLRPEAKEVIQALKRRGIEPVMLTGDNRKTAKAVAKELGID-VRAEVLPDDKAALI 459
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1279 KQLQEEGKRVAMVGDGINDSPALAMASVGIAIGTGTDVAIEAADVVLIRNDLLDVVASIDLSRKTVKRIRINFVFALIYN 1358
Cdd:TIGR01511  460 KKLQEKGPVVAMVGDGINDAPALAQADVGIAIGAGTDVAIEAADVVLLRNDLNDVATAIDLSRKTLRRIKQNLLWAFGYN 539
                          650       660
                   ....*....|....*....|...
gi 16258817   1359 LIGIPIAAGVFLPIGLVLQPWMG 1381
Cdd:TIGR01511  540 VIAIPIAAGVLYPIGILLSPAVA 562
ZntA COG2217
Cation transport ATPase [Inorganic ion transport and metabolism];
558-1381 0e+00

Cation transport ATPase [Inorganic ion transport and metabolism];


Pssm-ID: 225127  Cd Length: 713  Bit Score: 769.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  558 LELVVRGMTCASCVHKIEStLTKHKGIFYCSVALATNKAHIKYDPEIIGPR-DIIHTIGNLGFEASLVKKDRSANHLDHK 636
Cdd:COG2217    4 TSLSVEGMTCAACASRIEA-LNKLPGVEEARVNLATERATVVYDPEEVDLPaDIVAAVEKAGYSARLTAALADPAEAEAR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  637 REIKQWRgSFLVSLFFCIPVMGLMIYMMvmdhhlatlnhnqnmsneeminmhssmflerqilPGLSIMNLLSLLLCLPVQ 716
Cdd:COG2217   83 LLRELLR-RLIIAGLLTLPLLLLSLGLL----------------------------------LGAFLLPWVSFLLATPVL 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  717 FCGGWYFYIQAYKALRHKTANMDVLIVLATTIAFAYSLVILLVAMYerakvnpitfFDTPPMLFVFIALGRWLEHIAKGK 796
Cdd:COG2217  128 FYGGWPFYRGAWRALRRGRLNMDTLVALATIGAYAYSLYATLFPVY----------FEEAAMLIFLFLLGRYLEARAKGR 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  797 TSEALAKLISLQATEATIVTLNSEnlllsEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKK 876
Cdd:COG2217  198 ARRAIRALLDLAPKTATVVRGDGE-----EEEVPVEEVQVGDIVLVRPGERIPVDGVVVSGSSSVDESMLTGESLPVEKK 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  877 PGSTVIAGSINQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFIVLVSIVTLLVWIIIGFQNF 956
Cdd:COG2217  273 PGDEVFAGTVNLDGSLTIRVTRVGADTTLARIIRLVEEAQSSKAPIQRLADRVASYFVPVVLVIAALTFALWPLFGGGDW 352
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  957 EiveayfpgynrsisrtetiirFAFQASITVLCIACPCSLGLATPTAVMVGTGVGAQNGILIKGGEPLEMAHKVKVVVFD 1036
Cdd:COG2217  353 E---------------------TALYRALAVLVIACPCALGLATPTAILVGIGRAARRGILIKGGEALERLAKVDTVVFD 411
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1037 KTGTITHGTPVVNQVKVLvesnKISRNKILAIVGTAESNSEHPLGAAVTKYCKQELDTETlgtcTDFQVVPGCGISCKVT 1116
Cdd:COG2217  412 KTGTLTEGKPEVTDVVAL----DGDEDELLALAAALEQHSEHPLAKAIVKAAAERGLPDV----EDFEEIPGRGVEAEVD 483
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1117 NIEgllhksnlkieenniknaslvqidaineqsspsssmiidahlsnavntqqykVLIGNREWMIRNGLVISNdVDESMI 1196
Cdd:COG2217  484 GER----------------------------------------------------VLVGNARLLGEEGIDLPL-LSERIE 510
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1197 EHERRGRTAVLVTIDDELCGLIAIADTVKPEAELAVHILKSMGLEVVLMTGDNSKTARSIASQVGITKVFAEVLPSHKVA 1276
Cdd:COG2217  511 ALESEGKTVVFVAVDGKLVGVIALADELRPDAKEAIAALKALGIKVVMLTGDNRRTAEAIAKELGIDEVRAELLPEDKAE 590
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1277 KVKQLQEEGKRVAMVGDGINDSPALAMASVGIAIGTGTDVAIEAADVVLIRNDLLDVVASIDLSRKTVKRIRINFVFALI 1356
Cdd:COG2217  591 IVRELQAEGRKVAMVGDGINDAPALAAADVGIAMGSGTDVAIEAADVVLMRDDLSAVPEAIDLSRATRRIIKQNLFWAFG 670
                        810       820
                 ....*....|....*....|....*
gi 16258817 1357 YNLIGIPIAAGVFLPiglvlqPWMG 1381
Cdd:COG2217  671 YNAIAIPLAAGGLLT------PWIA 689
ATPase-IB_hvy TIGR01525
heavy metal translocating P-type ATPase; This model encompasses two equivalog models for the ...
738-1374 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  Cd Length: 558  Bit Score: 629.66  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    738 MDVLIVLATTIAFAYSLVILLVamyerakvnpitffdtppMLFVFIALGRWLEHIAKGKTSEALAKLISLQATEATIVTL 817
Cdd:TIGR01525    1 MDTLMALAAIAAYAMGLVLEGA------------------LLLFLFLLGETLEERAKSRASDALSALLALAPSTARVLQG 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    818 NsenllLSEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPGSTVIAGSINQNGSLLIRAT 897
Cdd:TIGR01525   63 D-----GSEEEVPVEELQVGDIVIVRPGERIPVDGVVISGESEVDESALTGESMPVEKKEGDEVFAGTINGDGSLTIRVT 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    898 HVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFIVLVSIVTLLVWIIIGFQNfeiveayfpgynrsisrtetii 977
Cdd:TIGR01525  138 KLGEDSTLAQIVELVEEAQSSKAPIQRLADRIASYYVPAVLAIALLTFVVWLALGALW---------------------- 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    978 RFAFQASITVLCIACPCSLGLATPTAVMVGTGVGAQNGILIKGGEPLEMAHKVKVVVFDKTGTITHGTPVVNQVKVLves 1057
Cdd:TIGR01525  196 REALYRALTVLVVACPCALGLATPVAILVAIGAAARRGILIKGGDALEKLAKVKTVVFDKTGTLTTGKPTVVDIEPL--- 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1058 NKISRNKILAIVGTAESNSEHPLGAAVTKYCKqELDTETLGtcTDFQVVPGCGISckvtniegllhksnlkieennikna 1137
Cdd:TIGR01525  273 DDASEEELLALAAALEQSSSHPLARAIVRYAK-ERGLELPP--EDVEEVPGKGVE------------------------- 324
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1138 slVQIDAineqsspsssmiidahlsnavntqQYKVLIGNREWMI--RNGLVISNDVDESMIEHERRGRTAVLVTIDDELC 1215
Cdd:TIGR01525  325 --ATVDG------------------------GREVRIGNPRFLGnrELAIEPISASPDLLNEGESQGKTVVFVAVDGELL 378
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1216 GLIAIADTVKPEAELAVHILKSMG-LEVVLMTGDNSKTARSIASQVGIT-KVFAEVLPSHKVAKVKQLQEEGKRVAMVGD 1293
Cdd:TIGR01525  379 GVIALRDQLRPEAKEAIAALKRAGgIKLVMLTGDNRSAAEAVAAELGIDdEVHAELLPEDKLAIVKKLQEEGGPVAMVGD 458
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1294 GINDSPALAMASVGIAIGTGTDVAIEAADVVLIRNDLLDVVASIDLSRKTVKRIRINFVFALIYNLIGIPIAAGVFLPIG 1373
Cdd:TIGR01525  459 GINDAPALAAADVGIAMGSGSDVAIEAADIVLLNDDLRSLPTAIDLSRKTRRIIKQNLAWALGYNLVAIPLAAGGLLPLW 538

                   .
gi 16258817   1374 L 1374
Cdd:TIGR01525  539 L 539
P-type_ATPase_HM cd02079
P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) ...
714-1381 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  Cd Length: 617  Bit Score: 627.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  714 PVQFCGGWYFYIQAYKALRHKTANMDVLIVLATTIAFAYSLVILLVamyerakvNPITFFDTPPMLFVFIALGRWLEHIA 793
Cdd:cd02079   37 PALLYGGRPFLRGAWRSLRRGRLNMDVLVSLAAIGAFVASLLTPLL--------GGIGYFEEAAMLLFLFLLGRYLEERA 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  794 KGKTSEALAKLISLQATEATIVTLNSEnlllseEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPV 873
Cdd:cd02079  109 RSRARSALKALLSLAPETATVLEDGST------EEVPVDDLKVGDVVLVKPGERIPVDGVVVSGESSVDESSLTGESLPV 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  874 AKKPGSTVIAGSINQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFIVLVSIVTLLVWIIIGf 953
Cdd:cd02079  183 EKGAGDTVFAGTINLNGPLTIEVTKTGEDTTLAKIIRLVEEAQSSKPPLQRLADRFARYFTPAVLVLAALVFLFWPLVG- 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  954 qnfeiveayfpgynrsisrteTIIRFAFQASITVLCIACPCSLGLATPTAVMVGTGVGAQNGILIKGGEPLEMAHKVKVV 1033
Cdd:cd02079  262 ---------------------GPPSLALYRALAVLVVACPCALGLATPTAIVAGIGRAARKGILIKGGDVLETLAKVDTV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1034 VFDKTGTITHGTPVVNQVKVLvesNKISRNKILAIVGTAESNSEHPLGAAVTKYCKQelDTETLGTCTDFQVVPGCGISC 1113
Cdd:cd02079  321 AFDKTGTLTEGKPEVTEIEPL---EGFSEDELLALAAALEQHSEHPLARAIVEAAEE--KGLPPLEVEDVEEIPGKGISG 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1114 KVtniegllhksnlkieenniknaslvqidaineqsspsssmiiDAHlsnavntqqyKVLIGNREWMIRNGLVisndvdE 1193
Cdd:cd02079  396 EV------------------------------------------DGR----------EVLIGSLSFAEEEGLV------E 417
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1194 SMIEHERRGRT-AVLVTIDDELCGLIAIADTVKPEAELAVHILKSMGLEVVLMTGDNSKTARSIASQVGITKVFAEVLPS 1272
Cdd:cd02079  418 AADALSDAGKTsAVYVGRDGKLVGLFALEDQLRPEAKEVIAELKSGGIKVVMLTGDNEAAAQAVAKELGIDEVHAGLLPE 497
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1273 HKVAKVKQLQEEGKRVAMVGDGINDSPALAMASVGIAIGTGTDVAIEAADVVLIRNDLLDVVASIDLSRKTVKRIRINFV 1352
Cdd:cd02079  498 DKLAIVKALQAEGGPVAMVGDGINDAPALAQADVGIAMGSGTDVAIETADIVLLSNDLSKLPDAIRLARRTRRIIKQNLA 577
                        650       660
                 ....*....|....*....|....*....
gi 16258817 1353 FALIYNLIGIPIAAGVFLPiglvlqPWMG 1381
Cdd:cd02079  578 WALGYNAIALPLAALGLLT------PWIA 600
P-type_ATPase_Cu-like cd07552
P-type heavy metal-transporting ATPase, similar to Archaeoglobus fulgidus CopB, a Cu(2+) ...
717-1381 1.30e-164

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  Cd Length: 632  Bit Score: 513.78  E-value: 1.30e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  717 FCGGWYFYIQAYKALRHKTANMDVLIVLATTIAFAYSLVILLvAMYERAKVNPitFFDTPPMLFVFIALGRWLEHIAKGK 796
Cdd:cd07552   41 FYGGKPFLKGAKDELKSKKPGMMTLIALGITVAYVYSVYAFL-GNYFGEHGMD--FFWELATLIVIMLLGHWIEMKAVMG 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  797 TSEALAKLISLQATEATIVTLNSEnlllseEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKK 876
Cdd:cd07552  118 AGDALKKLAELLPKTAHLVTDGSI------EDVPVSELKVGDVVLVRAGEKIPADGTILEGESSVNESMVTGESKPVEKK 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  877 PGSTVIAGSINQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFIVLVSIVTLLVWIIIGfqNF 956
Cdd:cd07552  192 PGDEVIGGSVNGNGTLEVKVTKTGEDSYLSQVMELVAQAQASKSRAENLADKVAGWLFYIALGVGIIAFIIWLILG--DL 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  957 EiveayfpgynrsisrtetiirFAFQASITVLCIACPCSLGLATPTAVMVGTGVGAQNGILIKGGEPLEMAHKVKVVVFD 1036
Cdd:cd07552  270 A---------------------FALERAVTVLVIACPHALGLAIPLVVARSTSIAAKNGLLIRNREALERARDIDVVLFD 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1037 KTGTITHGTPVVNQVkvlVESNKISRNKILAIVGTAESNSEHPLGAAVTKYCKQELdtETLGTCTDFQVVPGCGISCKVt 1116
Cdd:cd07552  329 KTGTLTEGKFGVTDV---ITFDEYDEDEILSLAAALEAGSEHPLAQAIVSAAKEKG--IRPVEVENFENIPGVGVEGTV- 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1117 niegllhksnlkieenniknaslvqidaineqsspsssmiidahlsnavntQQYKVLIGNREWMIRNGLVISNDVDESMI 1196
Cdd:cd07552  403 ---------------------------------------------------NGKRYQVVSPKYLKELGLKYDEELVKRLA 431
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1197 EHerrGRTAVLVTIDDELCGLIAIADTVKPEAELAVHILKSMGLEVVLMTGDNSKTARSIASQVGITKVFAEVLPSHKVA 1276
Cdd:cd07552  432 QQ---GNTVSFLIQDGEVIGAIALGDEIKPESKEAIRALKAQGITPVMLTGDNEEVAQAVAEELGIDEYFAEVLPEDKAK 508
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1277 KVKQLQEEGKRVAMVGDGINDSPALAMASVGIAIGTGTDVAIEAADVVLIRNDLLDVVASIDLSRKTVKRIRINFVFALI 1356
Cdd:cd07552  509 KVKELQAEGKKVAMVGDGVNDAPALAQADVGIAIGAGTDVAIESADVVLVKSDPRDIVDFLELAKATYRKMKQNLWWGAG 588
                        650       660
                 ....*....|....*....|....*
gi 16258817 1357 YNLIGIPIAAGVFLPIGLVLQPWMG 1381
Cdd:cd07552  589 YNVIAIPLAAGVLAPIGIILSPAVG 613
P-type_ATPase_HM_ZosA_PfeT-like cd07551
P-type heavy metal-transporting ATPase, similar to Bacillus subtilis ZosA/PfeT which ...
719-1368 1.12e-137

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  Cd Length: 611  Bit Score: 440.92  E-value: 1.12e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  719 GGWYFYIQAYKA-LRHKTANMDVLIVLATTIAfayslvillVAMYErakvnpitFFDTPPMLFVFiALGRWLEHIAKGKT 797
Cdd:cd07551   38 GGYASAKEGIEAtLRKKTLNVDLLMILAAIGA---------AAIGY--------WAEGALLIFIF-SLSHALEDYAMGRS 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  798 SEALAKLISLQATEATIVTLNSEnlllsEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKP 877
Cdd:cd07551  100 KRAITALMQLAPETARRIQRDGE-----IEEVPVEELQIGDRVQVRPGERVPADGVILSGSSSIDEASITGESIPVEKTP 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  878 GSTVIAGSINQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFIVLVSIVTLLVWIIIGFQNFe 957
Cdd:cd07551  175 GDEVFAGTINGSGALTVRVTKLSSDTVFAKIVQLVEEAQSEKSPTQSFIERFERIYVKGVLLAVLLLLLLPPFLLGWTW- 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  958 iveayfpgyNRSISRtetiirfafqaSITVLCIACPCSLGLATPTAVMVGTGVGAQNGILIKGGEPLEMAHKVKVVVFDK 1037
Cdd:cd07551  254 ---------ADSFYR-----------AMVFLVVASPCALVASTPPATLSAIANAARQGVLFKGGVHLENLGSVKAIAFDK 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1038 TGTITHGTPVVNQVKVLvesNKISRNKILAIVGTAESNSEHPLGAAVTKYCKQELdtETLGTCTDFQVVPGCGIsckVTN 1117
Cdd:cd07551  314 TGTLTEGKPRVTDVIPA---EGVDEEELLQVAAAAESQSEHPLAQAIVRYAEERG--IPRLPAIEVEAVTGKGV---TAT 385
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1118 IEGLLHKsnlkieennIKNASLVQIDAINEQSSPsssmiidahLSNavntqqykvlignrewmirnglvisndvdesmiE 1197
Cdd:cd07551  386 VDGQTYR---------IGKPGFFGEVGIPSEAAA---------LAA---------------------------------E 414
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1198 HERRGRTAVLVTIDDELCGLIAIADTVKPEAELAVHILKSMGLEVVLMTGDNSKTARSIASQVGITKVFAEVLPSHKVAK 1277
Cdd:cd07551  415 LESEGKTVVYVARDDQVVGLIALMDTPRPEAKEAIAALRLGGIKTIMLTGDNERTAEAVAKELGIDEVVANLLPEDKVAI 494
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1278 VKQLQEEGKRVAMVGDGINDSPALAMASVGIAIGTGTDVAIEAADVVLIRNDLLDVVASIDLSRKTVKRIRINFVFAL-- 1355
Cdd:cd07551  495 IRELQQEYGTVAMVGDGINDAPALANADVGIAMGAGTDVALETADVVLMKDDLSKLPYAIRLSRKMRRIIKQNLIFALav 574
                        650
                 ....*....|....*....
gi 16258817 1356 -----IYNLIG-IPIAAGV 1368
Cdd:cd07551  575 ialliVANLFGlLNLPLGV 593
ATPase-IB2_Cd TIGR01512
heavy metal-(Cd/Co/Hg/Pb/Zn)-translocating P-type ATPase; This model describes the P-type ...
778-1377 6.27e-137

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  Cd Length: 550  Bit Score: 436.75  E-value: 6.27e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    778 MLFVFIALGRWLEHIAKGKTSEALAKLISLQATEATIVTLNSEnlllseEQVDVELVQRGDIIKVVPGGKFPVDGRVIEG 857
Cdd:TIGR01512   23 LLLLLFSIGETLEEYASGRARRALKALMELAPDTARRLQGDSL------EEVAVEELKVGDVVVVKPGERVPVDGEVLSG 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    858 HSMVDESLITGEAMPVAKKPGSTVIAGSINQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFI 937
Cdd:TIGR01512   97 TSSVDESALTGESVPVEKAPGDEVFAGAINLDGVLTIEVTKLPADSTIAKIVNLVEEAQSRKAPTQRFIDRFARYYTPAV 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    938 VLVSivtLLVWIIigfqnfeiveayfPGYNRSISRTETIIRFAfqasiTVLCIACPCSLGLATPTAVMVGTGVGAQNGIL 1017
Cdd:TIGR01512  177 LAIA---LAAALV-------------PPLLGAGPFLEWIYRAL-----VLLVVASPCALVISAPAAYLSAISAAARHGIL 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1018 IKGGEPLEMAHKVKVVVFDKTGTITHGTPVVNQVKVLvesNKISRNKILAIVGTAESNSEHPLGAAVTKYCKQeldTETL 1097
Cdd:TIGR01512  236 IKGGAALEALAKIKTVAFDKTGTLTTGKPKVTDVHPA---DGHSESEVLRLAAAAEQGSTHPLARAIVDYARA---RELA 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1098 GTCTDFQVVPGCGISCKVTNIEgllhksnlkieenniknaslvqidaineqsspsssmiidahlsnavntqqykVLIGNR 1177
Cdd:TIGR01512  310 PPVEDVEEVPGEGVRAVVDGGE----------------------------------------------------VRIGNP 337
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1178 EWmirnglvISNDVDESMIEHERRGRTAVLVTIDDELCGLIAIADTVKPEAELAVHILKSMGLEVVLM-TGDNSKTARSI 1256
Cdd:TIGR01512  338 RS-------LSEAVGASIAVPESAGKTIVLVARDGTLLGYIALSDELRPDAAEAIAELKALGIKRLVMlTGDRRAVAEAV 410
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1257 ASQVGITKVFAEVLPSHKVAKVKQLQEEGKRVAMVGDGINDSPALAMASVGIAIGT-GTDVAIEAADVVLIRNDLLDVVA 1335
Cdd:TIGR01512  411 ARELGIDEVHAELLPEDKLEIVKELREKAGPVAMVGDGINDAPALAAADVGIAMGAsGSDVALETADVVLLNDDLSRLPQ 490
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*.
gi 16258817   1336 SIDLSRKTVKRIRINFVFALIynLIGIPIAAGVF----LPIGLVLQ 1377
Cdd:TIGR01512  491 AIRLARRTRRIIKQNVVIALG--IILVLILLALFgvlpLWLAVLGH 534
copA PRK10671
copper exporting ATPase; Provisional
375-1378 2.39e-136

copper exporting ATPase; Provisional


Pssm-ID: 182635  Cd Length: 834  Bit Score: 444.57  E-value: 2.39e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   375 LTQEVVININGMTCNSCVQSIEGVISKKPGVKSIHVSLTNS--TGTieydpllTSPEPLREAIEDMGFDAVLpadmkepl 452
Cdd:PRK10671    1 MSQTIDLTLDGLSCGHCVKRVKESLEQRPDVEQADVSITEAhvTGT-------ASAEALIETIKQAGYDASV-------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   453 vviAQPSLEtPLLPSTTEPEnvmtpvqnkcyiqvsgmtcascvaniernlrreegiysvlvALMAGKAEVrynPAviqpr 532
Cdd:PRK10671   66 ---SHPKAK-PLTESSIPSE-----------------------------------------ALTAASEEL---PA----- 92
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   533 viaelirelgfgavvmENAGEGNGIlELVVRGMTCASCVHKIESTLTKHKGIFYCSVALATNKAHIKYDPEiigPRDIIH 612
Cdd:PRK10671   93 ----------------ATADDDDSQ-QLLLSGMSCASCVSRVQNALQSVPGVTQARVNLAERTALVMGSAS---PQDLVQ 152
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   613 TIGNLGFEASLVKKD---RSANHLDHKREIKQWRGSFLVSLFFCIPVmglMIYMMVMDHHLATlNHNQnmsneeminmhs 689
Cdd:PRK10671  153 AVEKAGYGAEAIEDDakrRERQQETAQATMKRFRWQAIVALAVGIPV---MVWGMIGDNMMVT-ADNR------------ 216
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   690 SMFLERQILPgLSIMnllslllclpvQFCGGwYFYIQAYKALRHKTANMDVLIVLATTIAFAYSLVILL----VAMYERA 765
Cdd:PRK10671  217 SLWLVIGLIT-LAVM-----------VFAGG-HFYRSAWKSLLNGSATMDTLVALGTGAAWLYSMSVNLwpqwFPMEARH 283
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   766 kvnpiTFFDTPPMLFVFIALGRWLEHIAKGKTSEALAKLISLQATEATIVTLNSENLL-LSEeqvdvelVQRGDIIKVVP 844
Cdd:PRK10671  284 -----LYYEASAMIIGLINLGHMLEARARQRSSKALEKLLDLTPPTARVVTDEGEKSVpLAD-------VQPGMLLRLTT 351
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   845 GGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPGSTVIAGSINQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQ 924
Cdd:PRK10671  352 GDRVPVDGEITQGEAWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQ 431
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   925 FADKLSGYFVPFIVLVSIVTLLVWiiigfqnfeiveaYFPGYNRSISRTETIIrfafqasITVLCIACPCSLGLATPTAV 1004
Cdd:PRK10671  432 LADKISAVFVPVVVVIALVSAAIW-------------YFFGPAPQIVYTLVIA-------TTVLIIACPCALGLATPMSI 491
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  1005 MVGTGVGAQNGILIKGGEPLEMAHKVKVVVFDKTGTITHGTPVVNQVKVLvesNKISRNKILAIVGTAESNSEHPLGAAV 1084
Cdd:PRK10671  492 ISGVGRAAEFGVLVRDADALQRASTLDTLVFDKTGTLTEGKPQVVAVKTF---NGVDEAQALRLAAALEQGSSHPLARAI 568
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  1085 TkyckQELDTETLGTCTDFQVVPGCGISCKVTNIEgllhksnlkieenniknaslvqidaineqsspsssmiidahlsna 1164
Cdd:PRK10671  569 L----DKAGDMTLPQVNGFRTLRGLGVSGEAEGHA--------------------------------------------- 599
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  1165 vntqqykVLIGNREWMIRNGlVISNDVDESMIEHERRGRTAVLVTIDDELCGLIAIADTVKPEAELAVHILKSMGLEVVL 1244
Cdd:PRK10671  600 -------LLLGNQALLNEQQ-VDTKALEAEITAQASQGATPVLLAVDGKAAALLAIRDPLRSDSVAALQRLHKAGYRLVM 671
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  1245 MTGDNSKTARSIASQVGITKVFAEVLPSHKVAKVKQLQEEGKRVAMVGDGINDSPALAMASVGIAIGTGTDVAIEAADVV 1324
Cdd:PRK10671  672 LTGDNPTTANAIAKEAGIDEVIAGVLPDGKAEAIKRLQSQGRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETAAIT 751
                         970       980       990      1000      1010
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16258817  1325 LIRNDLLDVVASIDLSRKTVKRIRINFVFALIYNLIGIPIAAGVFLPI-GLVLQP 1378
Cdd:PRK10671  752 LMRHSLMGVADALAISRATLRNMKQNLLGAFIYNSLGIPIAAGILWPFtGTLLNP 806
P-type_ATPase_Cd-like cd07545
P-type heavy metal-transporting ATPase, similar to Staphylococcus aureus plasmid pI258 CadA, a ...
719-1380 8.10e-124

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  Cd Length: 599  Bit Score: 402.57  E-value: 8.10e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  719 GGWYFYIQAYKALRHKTANMDVLIVLATTIAfayslviLLVAMYERAKVnpitffdtppMLFVFiALGRWLEHIAKGKTS 798
Cdd:cd07545   23 GGYGLFKKGWRNLIRRNFDMKTLMTIAVIGA-------ALIGEWPEAAM----------VVFLF-AISEALEAYSMDRAR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  799 EALAKLISLQATEATIVTlNSEnlllsEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPG 878
Cdd:cd07545   85 RSIRSLMDIAPKTALVRR-DGQ-----EREVPVAEVAVGDRMIVRPGERIAMDGIIVRGESSVNQAAITGESLPVEKGVG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  879 STVIAGSINQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFI----VLVSIVTLLVwiiigfq 954
Cdd:cd07545  159 DEVFAGTLNGEGALEVRVTKPAEDSTIARIIHLVEEAQAERAPTQAFVDRFARYYTPVVmaiaALVAIVPPLF------- 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  955 nfeIVEAYFPGYNRSIsrtetiirfafqasiTVLCIACPCSLGLATPTAVMVGTGVGAQNGILIKGGEPLEMAHKVKVVV 1034
Cdd:cd07545  232 ---FGGAWFTWIYRGL---------------ALLVVACPCALVISTPVSIVSAIGNAARKGVLIKGGVYLEELGRLKTVA 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1035 FDKTGTITHGTPVVNQVKVLvesNKISRNKILAIVGTAESNSEHPLGAAVTKYCKQelDTETLGTCTDFQVVPGCGIsck 1114
Cdd:cd07545  294 FDKTGTLTKGKPVVTDVVVL---GGQTEKELLAIAAALEYRSEHPLASAIVKKAEQ--RGLTLSAVEEFTALTGRGV--- 365
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1115 VTNIEGLLhksnlkieenniknaslvqidaineqsspsssmiidahlsnavntqqykVLIGNREWMIRNGLVISNDVDES 1194
Cdd:cd07545  366 RGVVNGTT-------------------------------------------------YYIGSPRLFEELNLSESPALEAK 396
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1195 MIEHERRGRTAVLVTIDDELCGLIAIADTVKPEAELAVHILK-SMGLEVVLMTGDNSKTARSIASQVGITKVFAEVLPSH 1273
Cdd:cd07545  397 LDALQNQGKTVMILGDGERILGVIAVADQVRPSSRNAIAALHqLGIKQTVMLTGDNPQTAQAIAAQVGVSDIRAELLPQD 476
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1274 KVAKVKQLQEEGKRVAMVGDGINDSPALAMASVGIAIG-TGTDVAIEAADVVLIRNDLLDVVASIDLSRKTVKRIRINFV 1352
Cdd:cd07545  477 KLDAIEALQAEGGRVAMVGDGVNDAPALAAADVGIAMGaAGTDTALETADIALMGDDLRKLPFAVRLSRKTLAIIKQNIA 556
                        650       660
                 ....*....|....*....|....*...
gi 16258817 1353 FALiynliGIPIAAgvflpIGLVLQPWM 1380
Cdd:cd07545  557 FAL-----GIKLIA-----LLLVIPGWL 574
P-type_ATPase_HM cd07550
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
726-1376 4.35e-115

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  Cd Length: 592  Bit Score: 377.77  E-value: 4.35e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  726 QAYKALRHKTANMDVLIVLAttiafayslVILLVAMYERAKVNPITFFdtppmlfvfIALGRWLEHIAKGKTSEALAKLI 805
Cdd:cd07550   34 RALESLKERRLNVDVLDSLA---------VLLSLLTGDYLAANTIAFL---------LELGELLEDYTARKSEKALLDLL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  806 SLQATEATIVTLNSEnlllseEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPGSTVIAGS 885
Cdd:cd07550   96 SPQERTVWVERDGVE------VEVPADEVQPGDTVVVGAGDVIPVDGTVLSGEALIDQASLTGESLPVEKREGDLVFAST 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  886 INQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFIVLVSIvtlLVWIIIgfqnfeiveayfpg 965
Cdd:cd07550  170 VVEEGQLVIRAERVGRETRAARIAELIEQSPSLKARIQNYAERLADRLVPPTLGLAG---LVYALT-------------- 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  966 ynRSISRtetiirfafqaSITVLCIACPCSLGLATPTAVMVGTGVGAQNGILIKGGEPLEMAHKVKVVVFDKTGTITHGT 1045
Cdd:cd07550  233 --GDISR-----------AAAVLLVDFSCGIRLSTPVAVLSALNHAARHGILVKGGRALELLAKVDTVVFDKTGTLTEGE 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1046 PVVNQVKVLveSNKISRNKILAIVGTAESNSEHPLGAAVTKYCKQE-LDtetLGTCTDFQVVPGCGISCKvtniegllhk 1124
Cdd:cd07550  300 PEVTAIITF--DGRLSEEDLLYLAASAEEHFPHPVARAIVREAEERgIE---HPEHEEVEYIVGHGIAST---------- 364
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1125 snlkieenniknaslvqidaineqsspsssmiIDAHlsnavntqqyKVLIGNREWMIRNGLVISNDVDESMIEHERRGRT 1204
Cdd:cd07550  365 --------------------------------VDGK----------RIRVGSRHFMEEEEIILIPEVDELIEDLHAEGKS 402
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1205 AVLVTIDDELCGLIAIADTVKPEAELAVHILK-SMGLEVVLMTGDNSKTARSIASQVGITKVFAEVLPSHKVAKVKQLQE 1283
Cdd:cd07550  403 LLYVAIDGRLIGVIGLSDPLRPEAAEVIARLRaLGGKRIIMLTGDHEQRARALAEQLGIDRYHAEALPEDKAEIVEKLQA 482
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1284 EGKRVAMVGDGINDSPALAMASVGIAIGTGTDVAIEAADVVLIRNDLLDVVASIDLSRKTVKRIRINFVFALIYNLIGip 1363
Cdd:cd07550  483 EGRTVAFVGDGINDSPALSYADVGISMRGGTDIARETADVVLLEDDLRGLAEAIELARETMALIKRNIALVVGPNTAV-- 560
                        650
                 ....*....|....*.
gi 16258817 1364 IAAGVFL---PIGLVL 1376
Cdd:cd07550  561 LAGGVFGllsPILAAV 576
P-type_ATPase_FixI-like cd02092
Rhizobium meliloti FixI and related proteins; belongs to P-type heavy metal-transporting ...
715-1372 2.55e-112

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  Cd Length: 605  Bit Score: 370.53  E-value: 2.55e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  715 VQFCGGWYFYiQAYKALRHKTANMDVLIVLATTIAFAYSLvillvamYERAKVNPITFFDTPPMLFVFIALGRWLEHIAK 794
Cdd:cd02092   39 VAYAGRPFFR-SAWAALRHGRTNMDVPISIGVLLATGMSL-------FETLHGGEHAYFDAAVMLLFFLLIGRYLDHRMR 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  795 GKTSEALAKLISLQATEATIVTLNSenlllSEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVA 874
Cdd:cd02092  111 GRARSAAEELAALEARGAQRLQADG-----SREYVPVAEIRPGDRVLVAAGERIPVDGTVVSGTSELDRSLLTGESAPVT 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  875 KKPGSTVIAGSINQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFIVLVSIVTLLVWIIIGFQ 954
Cdd:cd02092  186 VAPGDLVQAGAMNLSGPLRLRATAAGDDTLLAEIARLMEAAEQGRSRYVRLADRAARLYAPVVHLLALLTFVGWVAAGGD 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  955 nfeiveayfpgynrsisrtetiIRFAFQASITVLCIACPCSLGLATPTAVMVGTGVGAQNGILIKGGEPLEMAHKVKVVV 1034
Cdd:cd02092  266 ----------------------WRHALLIAVAVLIITCPCALGLAVPAVQVVASGRLFRRGVLVKDGTALERLAEVDTVV 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1035 FDKTGTITHGTPvvnqvkVLVESNKISRNkILAIVGTAESNSEHPLGAAVTkyckQELDTETLGTcTDFQVVPGCGisck 1114
Cdd:cd02092  324 FDKTGTLTLGSP------RLVGAHAISAD-LLALAAALAQASRHPLSRALA----AAAGARPVEL-DDAREVPGRG---- 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1115 vtnIEGllhksnlkieenniknaslvQIDAineqsspsssmiidahlsnavntQQYKVliGNREWmirngLVISNDVDES 1194
Cdd:cd02092  388 ---VEG--------------------RIDG-----------------------ARVRL--GRPAW-----LGASAGVSTA 414
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1195 mieherrgrTAVLVTIDDELCGLIAIADTVKPEAELAVHILKSMGLEVVLMTGDNSKTARSIASQVGITKVFAEVLPSHK 1274
Cdd:cd02092  415 ---------SELALSKGGEEAARFPFEDRPRPDAREAISALRALGLSVEILSGDREPAVRALARALGIEDWRAGLTPAEK 485
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1275 VAKVKQLQEEGKRVAMVGDGINDSPALAMASVGIAIGTGTDVAIEAADVVLIRNDLLDVVASIDLSRKTVKRIRINFVFA 1354
Cdd:cd02092  486 VARIEELKAQGRRVLMVGDGLNDAPALAAAHVSMAPASAVDASRSAADIVFLGDSLAPVPEAIEIARRARRLIRQNFALA 565
                        650
                 ....*....|....*....
gi 16258817 1355 LIYNLIGIPIA-AGVFLPI 1372
Cdd:cd02092  566 IGYNVIAVPLAiAGYVTPL 584
P-type_ATPase_Pb_Zn_Cd2-like cd07546
P-type heavy metal-transporting ATPase, similar to Escherichia coli ZntA which is selective ...
779-1355 5.92e-111

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  Cd Length: 597  Bit Score: 366.34  E-value: 5.92e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  779 LFVFiALGRWLEHIAKGKTSEALAKLISLQATEATIVTLNSEnlllseEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGH 858
Cdd:cd07546   69 LLLF-LVGELLEGYAASRARSGVKALMALVPETALREENGER------REVPADSLRPGDVIEVAPGGRLPADGELLSGF 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  859 SMVDESLITGEAMPVAKKPGSTVIAGSINQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFIV 938
Cdd:cd07546  142 ASFDESALTGESIPVEKAAGDKVFAGSINVDGVLRIRVTSAPGDNAIDRILHLIEEAEERRAPIERFIDRFSRWYTPAIM 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  939 LVSIVTLLVWIIIGFQNFEiveayfpgynrsisrtETIIRfafqaSITVLCIACPCSLGLATPTAVMVGTGVGAQNGILI 1018
Cdd:cd07546  222 AVALLVIVVPPLLFGADWQ----------------TWIYR-----GLALLLIGCPCALVISTPAAITSGLAAAARRGALI 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1019 KGGEPLEMAHKVKVVVFDKTGTITHGTPVVNQVKVLvesNKISRNKILAIVGTAESNSEHPLGAAVTKycKQELDTETLG 1098
Cdd:cd07546  281 KGGAALEQLGRVTTVAFDKTGTLTRGKPVVTDVVPL---TGISEAELLALAAAVEMGSSHPLAQAIVA--RAQAAGLTIP 355
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1099 TCTDFQVVPGCGISCKVtniegllhksnlkieennikNASLVQIdaineqSSPsssmiidahlsNAVNTQqykvlignre 1178
Cdd:cd07546  356 PAEEARALVGRGIEGQV--------------------DGERVLI------GAP-----------KFAADR---------- 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1179 wmirnglvISNDVDESMIEHERRGRTAVLVTIDDELCGLIAIADTVKPEAELAVHILKSMGLEVVLMTGDNSKTARSIAS 1258
Cdd:cd07546  389 --------GTLEVQGRIAALEQAGKTVVVVLANGRVLGLIALRDELRPDAAEAVAELNALGIKALMLTGDNPRAAAAIAA 460
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1259 QVGItKVFAEVLPSHKVAKVKQLQEEGkRVAMVGDGINDSPALAMASVGIAIGTGTDVAIEAADVVLIRNDLLDVVASID 1338
Cdd:cd07546  461 ELGL-DFRAGLLPEDKVKAVRELAQHG-PVAMVGDGINDAPAMKAASIGIAMGSGTDVALETADAALTHNRLGGVAAMIE 538
                        570
                 ....*....|....*..
gi 16258817 1339 LSRKTVKRIRINFVFAL 1355
Cdd:cd07546  539 LSRATLANIRQNITIAL 555
P-type_ATPase-Cd_Zn_Co_like cd07548
P-type heavy metal-transporting ATPase, similar to Bacillus subtilis CadA which appears to ...
778-1355 1.65e-105

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  Cd Length: 604  Bit Score: 351.15  E-value: 1.65e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  778 MLFVfiALGRWLEHIAKGKTSEALAKLISLQATEATIVTlNSEnlllsEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEG 857
Cdd:cd07548   79 MLFY--EVGELFQDLAVERSRKSIKALLDIRPDYANLKR-NNE-----LKDVKPEEVQIGDIIVVKPGEKIPLDGVVLKG 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  858 HSMVDESLITGEAMPVAKKPGSTVIAGSINQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFI 937
Cdd:cd07548  151 ESFLDTSALTGESVPVEVKEGSSVLAGFINLNGVLEIKVTKPFKDSAVAKILELVENASARKAPTEKFITKFARYYTPIV 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  938 VLVSI-VTLLVWIIIGFQNFEIveayfpgynrsisrtetiirFAFQAsITVLCIACPCSLGLATPTAVMVGTGVGAQNGI 1016
Cdd:cd07548  231 VFLALlLAVIPPLFSPDGSFSD--------------------WIYRA-LVFLVISCPCALVISIPLGYFGGIGAASRKGI 289
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1017 LIKGGEPLEMAHKVKVVVFDKTGTITHGTPVVNQVKVlveSNKISRNKILAIVGTAESNSEHPLGAAVTKYCKQELDTET 1096
Cdd:cd07548  290 LIKGSNYLEALSQVKTVVFDKTGTLTKGVFKVTEIVP---APGFSKEELLKLAALAESNSNHPIARSIQKAYGKMIDPSE 366
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1097 LgtcTDFQVVPGCGISCKVtniegllhksnlkieenniknaslvqidaineqsspsssmiidahlsnavntQQYKVLIGN 1176
Cdd:cd07548  367 I---EDYEEIAGHGIRAVV----------------------------------------------------DGKEILVGN 391
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1177 REWMIRNGlvISNDVDEsmIEHerrgrTAVLVTIDDELCGLIAIADTVKPEAELAVHILKSMGLE-VVLMTGDNSKTARS 1255
Cdd:cd07548  392 EKLMEKFN--IEHDEDE--IEG-----TIVHVALDGKYVGYIVISDEIKEDAKEAIKGLKELGIKnLVMLTGDRKSVAEK 462
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1256 IASQVGITKVFAEVLPSHKVAKVKQLQEEGK-RVAMVGDGINDSPALAMASVGIAIGT-GTDVAIEAADVVLIRNDLLDV 1333
Cdd:cd07548  463 VAKKLGIDEVYAELLPEDKVEKVEELKAESKgKVAFVGDGINDAPVLARADVGIAMGGlGSDAAIEAADVVLMNDEPSKV 542
                        570       580
                 ....*....|....*....|..
gi 16258817 1334 VASIDLSRKTVKRIRINFVFAL 1355
Cdd:cd07548  543 AEAIKIARKTRRIVWQNIILAL 564
P-type_ATPase_HM cd07544
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
729-1377 5.17e-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: 319844  Cd Length: 596  Bit Score: 340.84  E-value: 5.17e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  729 KALRHKTANMDVLIVLA--TTIA---FAYSLVILLvamyerakvnpitffdtppMLfvfiALGRWLEHIAKGKTSEALAK 803
Cdd:cd07544   47 KTLRRGRYGVDLLAILAivATLLvgeYWASLIILL-------------------ML----TGGEALEDYAQRRASRELTA 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  804 LisLQATEATIVTLNSENLllseEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPGSTVIA 883
Cdd:cd07544  104 L--LDRAPRIAHRLVGGQL----EEVPVEEVTVGDRLLVRPGEVVPVDGEVVSGTATLDESSLTGESKPVSKRPGDRVMS 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  884 GSINQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKlsgYFVPFIVLVSIVTLLVWIIIGfqnfeiveayf 963
Cdd:cd07544  178 GAVNGDSALTMVATKLAADSQYAGIVRLVKEAQANPAPFVRLADR---YAVPFTLLALAIAGVAWAVSG----------- 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  964 pgynrsisrteTIIRFAfqasiTVLCIACPCSLGLATPTAVMVGTGVGAQNGILIKGGEPLEMAHKVKVVVFDKTGTITH 1043
Cdd:cd07544  244 -----------DPVRFA-----AVLVVATPCPLILAAPVAIVSGMSRSSRRGILVKDGGVLEKLARAKTVAFDKTGTLTY 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1044 GTPVVNQVKVLvesNKISRNKILAIVGTAESNSEHPLGAAVTKYCKQeldtetlgtctdfqvvpgcgisckvtniegllh 1123
Cdd:cd07544  308 GQPKVVDVVPA---PGVDADEVLRLAASVEQYSSHVLARAIVAAARE--------------------------------- 351
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1124 ksnlkieenniKNASLVQIDAINEQSSPSSSMIIDAHlsnavntqqyKVLIGNREWmirnglVISNDVDESMIEHERRGR 1203
Cdd:cd07544  352 -----------RELQLSAVTELTEVPGAGVTGTVDGH----------EVKVGKLKF------VLARGAWAPDIRNRPLGG 404
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1204 TAVLVTIDDELCGLIAIADTVKPEAELAVHILKSMGLE-VVLMTGDNSKTARSIASQVGITKVFAEVLPSHKVAKVKQLQ 1282
Cdd:cd07544  405 TAVYVSVDGKYAGAITLRDEVRPEAKETLAHLRKAGVErLVMLTGDRRSVAEYIASEVGIDEVRAELLPEDKLAAVKEAP 484
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1283 EEGKrVAMVGDGINDSPALAMASVGIAIGT-GTDVAIEAADVVLIRNDLLDVVASIDLSRKTVKRIRINFVFALIYNLIG 1361
Cdd:cd07544  485 KAGP-TIMVGDGVNDAPALAAADVGIAMGArGSTAASEAADVVILVDDLDRVVDAVAIARRTRRIALQSVLIGMALSIIG 563
                        650
                 ....*....|....*...
gi 16258817 1362 IPIAAGVFLP--IGLVLQ 1377
Cdd:cd07544  564 MLIAAFGLIPpvAGALLQ 581
ATPase_P-type TIGR01494
ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large ...
778-1377 5.27e-101

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  Cd Length: 545  Bit Score: 336.21  E-value: 5.27e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    778 MLFVFIALgrwlEHIAKGKTSEALAKLISLQATEATIVTLNSenlllSEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEG 857
Cdd:TIGR01494    5 LVLLFVLL----EVKQKLKAEDALRSLKDSLVNTATVLVLRN-----GWKEISSKDLVPGDVVLVKSGDTVPADGVLLSG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    858 HSMVDESLITGEAMPVAKKPGST---VIAGSINQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSG-YF 933
Cdd:TIGR01494   76 SAFVDESSLTGESLPVLKTALPDgdaVFAGTINFGGTLIVKVTATGILTTVGKIAVVVYTGFSTKTPLQSKADKFENfIF 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    934 VPFIVLVSIVTLLVWIIIGFQNFEIVeayfpgynrsisrtetiirFAFQASITVLCIACPCSLGLATPTAVMVGTGVGAQ 1013
Cdd:TIGR01494  156 ILFLLLLALAVFLLLPIGGWDGNSIY-------------------KAILRALAVLVIAIPCALPLAVSVALAVGDARMAK 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1014 NGILIKGGEPLEMAHKVKVVVFDKTGTITHGTPVVnqVKVLVESNKISRNKILA-IVGTAESNSEHPLGAAVTKYCKQ-E 1091
Cdd:TIGR01494  217 KGILVKNLNALEELGKVDVICFDKTGTLTTNKMTL--QKVIIIGGVEEASLALAlLAASLEYLSGHPLERAIVKSAEGvI 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1092 LDTETLGTCTDFQVVPgcgisckvtniegllHKSNLKieenniknaslvqidaineqsspSSSMIIdahlsNAVNTQQYK 1171
Cdd:TIGR01494  295 KSDEINVEYKILDVFP---------------FSSVLK-----------------------RMGVIV-----EGANGSDLL 331
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1172 VLIGNREWMIRNGLVIsNDVDESMIEHERRGRTAVLV-----TIDDELCGLIAIADTVKPEAELAVHILKSMGLEVVLMT 1246
Cdd:TIGR01494  332 FVKGAPEFVLERCNNE-NDYDEKVDEYARQGLRVLAFaskklPDDLEFLGLLTFEDPLRPDAKETIEALRKAGIKVVMLT 410
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1247 GDNSKTARSIASQVGItKVFAEVLPSHKVAKVKQLQEEGKRVAMVGDGINDSPALAMASVGIAIGtGTDVAIEAADVVLI 1326
Cdd:TIGR01494  411 GDNVLTAKAIAKELGI-DVFARVKPEEKAAIVEALQEKGRTVAMTGDGVNDAPALKKADVGIAMG-SGDVAKAAADIVLL 488
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|.
gi 16258817   1327 RNDLLDVVASIDLSRKTVKRIRINFVFALIYNLIGIPIAAGVFLpIGLVLQ 1377
Cdd:TIGR01494  489 DDDLSTIVEAVKEGRKTFSNIKKNIFWAIAYNLILIPLALLLIV-IILLPP 538
zntA PRK11033
zinc/cadmium/mercury/lead-transporting ATPase; Provisional
561-1355 3.79e-92

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


Pssm-ID: 236827  Cd Length: 741  Bit Score: 316.93  E-value: 3.79e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   561 VVRGMTCASCVHKIESTLTKHKGIFYCSVALATNKAHIKYDPEIIGPrdIIHTIGNLGFeaSLVKKDRSANhldhKREIK 640
Cdd:PRK11033   58 KVSGMDCPSCARKVENAVRQLAGVNQVQVLFATEKLVVDADNDIRAQ--VESAVQKAGF--SLRDEQAAAA----APESR 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   641 QWRGSflvslffcIPVMGLMIyMMVMDHHLATLNHNqnmsneeminMHSSMFlerqILPGLsimnllslllclpvqfCGG 720
Cdd:PRK11033  130 LKSEN--------LPLITLAV-MMAISWGLEQFNHP----------FGQLAF----IATTL----------------VGL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   721 WYFYIQAYKALRHKTA-NMDVLIVLATTIAfayslvILLVAMYERAKVnpitffdtppmLFVFIaLGRWLEHIAKGKTSE 799
Cdd:PRK11033  171 YPIARKALRLIRSGSPfAIETLMSVAAIGA------LFIGATAEAAMV-----------LLLFL-IGERLEGYAASRARR 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   800 ALAKLISLQATEATIVTlNSEnlllsEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPGS 879
Cdd:PRK11033  233 GVSALMALVPETATRLR-DGE-----REEVAIADLRPGDVIEVAAGGRLPADGKLLSPFASFDESALTGESIPVERATGE 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   880 TVIAGSINQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFIVLVSIVTLLVWIIIGFQNFEiv 959
Cdd:PRK11033  307 KVPAGATSVDRLVTLEVLSEPGASAIDRILHLIEEAEERRAPIERFIDRFSRIYTPAIMLVALLVILVPPLLFAAPWQ-- 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   960 eayfpgynrsisrtETIIRfafqaSITVLCIACPCSLGLATPTAVMVGTGVGAQNGILIKGGEPLEMAHKVKVVVFDKTG 1039
Cdd:PRK11033  385 --------------EWIYR-----GLTLLLIGCPCALVISTPAAITSGLAAAARRGALIKGGAALEQLGRVTTVAFDKTG 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  1040 TITHGTPVVNQVKVLVEsnkISRNKILAIVGTAESNSEHPLGAAVTKYCKQEldTETLGTCTDFQVVPGCGISCKVtnie 1119
Cdd:PRK11033  446 TLTEGKPQVTDIHPATG---ISESELLALAAAVEQGSTHPLAQAIVREAQVR--GLAIPEAESQRALAGSGIEGQV---- 516
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  1120 gllhksnlkieennikNASLVQIdaineqSSPSSSmiidAHLSNAVNTQqykvlignrewmirnglvisndvdesMIEHE 1199
Cdd:PRK11033  517 ----------------NGERVLI------CAPGKL----PPLADAFAGQ--------------------------INELE 544
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  1200 RRGRTAVLVTIDDELCGLIAIADTVKPEAELAVHILKSMGLEVVLMTGDNSKTARSIASQVGITkvF-AEVLPSHKVAKV 1278
Cdd:PRK11033  545 SAGKTVVLVLRNDDVLGLIALQDTLRADARQAISELKALGIKGVMLTGDNPRAAAAIAGELGID--FrAGLLPEDKVKAV 622
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16258817  1279 KQLQEEgKRVAMVGDGINDSPALAMASVGIAIGTGTDVAIEAADVVLIRNDLLDVVASIDLSRKTVKRIRINFVFAL 1355
Cdd:PRK11033  623 TELNQH-APLAMVGDGINDAPAMKAASIGIAMGSGTDVALETADAALTHNRLRGLAQMIELSRATHANIRQNITIAL 698
P-type_ATPase_HM cd07553
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
714-1372 2.02e-85

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  Cd Length: 610  Bit Score: 294.04  E-value: 2.02e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  714 PVQFCGGWYFYIQAYKALRHKTANMDVLIVLATTIAFAYSlVILLVAMYERAkvnpitFFDTPPMLFVFIALGRWLEHia 793
Cdd:cd07553   39 PSMLYCGSYFYGKAWKSAKQGIPHIDLPIALGIVIGFVVS-WYGLIKGDGLV------YFDSLSVLVFLMLVGRWLQV-- 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  794 kgKTSEALAKLISLQATEATIVTLNSENLllSEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPV 873
Cdd:cd07553  110 --VTQERNRNRLADSRLEAPITEIETGSG--SRIKTRADQIKSGDVYLVASGQRVPVDGKLLSEQASIDMSWLTGESLPR 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  874 AKKPGSTVIAGSINQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFIVLVSIVTLLVWIIIGF 953
Cdd:cd07553  186 IVERGDKVPAGTSLENQAFEIRVEHSLAESWSGSILQKVEAQEARKTPRDLLADKIIHYFTVIALLIAVAGFGVWLAIDL 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  954 QNfeiveayfpgynrsisrtetiirfAFQASITVLCIACPCSLGLATPTAVMVGTGVGAQNGILIKGGEPLEMAHKVKVV 1033
Cdd:cd07553  266 SI------------------------ALKVFTSVLIVACPCALALATPFTDEIALARLKKKGVLIKNASSLERLSRVRTI 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1034 VFDKTGTITHGTPVVnqvkVLVESNKISRNKILAIVGTaESNSEHPLGAAVTKYCkQELDTETLGTCtDFQVVPGCGISC 1113
Cdd:cd07553  322 VFDKTGTLTRGKSSF----VMVNPEGIDRLALRAISAI-EAHSRHPISRAIREHL-MAKGLIKAGAS-ELVEIVGKGVSG 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1114 KVtniegllhksnlkieenniknaslvqidaineqsspsssmiiDAHLsnavntqqykVLIGNREWMIRNglvisndvde 1193
Cdd:cd07553  395 NS------------------------------------------SGSL----------WKLGSAPDACGI---------- 412
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1194 smieherrGRTAVLVTIDDELCGLIAIADTVKPEAELAVHILKSMGLEVVLMTGDNSKTARSIASQVGI--TKVFAEVLP 1271
Cdd:cd07553  413 --------QESGVVIARDGRQLLDLSFNDLLRPDSNREIEELKKGGLSIAILSGDNEEKVRLVGDSLGLdpRQLFGNLSP 484
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1272 SHKVAKVKQLQEEGkrVAMVGDGINDSPALAMASVGIAIGTGTDVAIEAADVVLIRNDLLDVVASIDLSRKTVKRIRINF 1351
Cdd:cd07553  485 EEKLAWIESHSPEN--TLMVGDGANDALALASAFVGIAVAGEVGVSLEAADIYYAGNGIGGIRDLLTLSKQTIKAIKGLF 562
                        650       660       670
                 ....*....|....*....|....*....|
gi 16258817 1352 VFALIYNLIGI---------PIAAGVFLPI 1372
Cdd:cd07553  563 AFSLLYNLVAIglalsgwisPLVAAILMPL 592
MgtA COG0474
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism];
777-1377 3.40e-60

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


Pssm-ID: 223550  Cd Length: 917  Bit Score: 224.91  E-value: 3.40e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  777 PMLFVFIALGRWLEHIAKgKTSEALAKLISLQAT---EATIVTLNSENLLLseeqvdvelvqrGDIIKVVPGGKFPVDGR 853
Cdd:COG0474  111 LVVVINALLGFVQEYRAE-KALEALKKMSSPKAKvlrDGKFVEIPASELVP------------GDIVLLEAGDVVPADLR 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  854 VIEGHSM-VDESLITGEAMPVAKKP--------------GSTVIAGSINQNGSLLIRATHVGADTTLSQIVKLVEEAQTS 918
Cdd:COG0474  178 LLESSDLeVDESALTGESLPVEKQAlpltksdaplgldrDNMLFSGTTVVSGRAKGIVVATGFETEFGKIARLLPTKKEV 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  919 KAPIQQFADKLSGYFVPFIVLVSIVTLLVWIIIGFQNFEIveayfpgynrsisrtetiirfAFQASITVLCIACPCSLGL 998
Cdd:COG0474  258 KTPLQRKLNKLGKFLLVLALVLGALVFVVGLFRGGNGLLE---------------------SFLTALALAVAAVPEGLPA 316
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  999 ATPTAVMVGTGVGAQNGILIKGGEPLEMAHKVKVVVFDKTGTITHgtpvvnqvkvlvesNKISRNKILAIVGTAESNSEH 1078
Cdd:COG0474  317 VVTIALALGAQRMAKDNAIVRSLNAIETLGSVDVICSDKTGTLTQ--------------NKMTVKKIYINGGGKDIDDKD 382
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1079 PLGAAVTKYCKQeldteTLGTCTDFQVVPGCG----------ISCKVTNIEGLLHKSNLKIEENNIKN----------AS 1138
Cdd:COG0474  383 LKDSPALLRFLL-----AAALCNSVTPEKNGWyqagdptegaLVEFAEKLGFSLDLSGLEVEYPILAEipfdserkrmSV 457
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1139 LVQIDAIN---------EQSSPSSSMIIDAHLSNAVNTQQYKvlIGNREwMIRNGL-VI-----SNDVDESMIEHErrgr 1203
Cdd:COG0474  458 IVKTDEGKyilfvkgapEVILERCKSIGELEPLTEEGLRTLE--EAVKE-LASEGLrVLavaykKLDRAEKDDEVD---- 530
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1204 tavLVTIDDELCGLIAIADTVKPEAELAVHILKSMGLEVVLMTGDNSKTARSIASQVGI--------------------- 1262
Cdd:COG0474  531 ---EIESDLVFLGLTGIEDPPREDVKEAIEELREAGIKVWMITGDHVETAIAIAKECGIeaeaesalvidgaeldalsde 607
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1263 --------TKVFAEVLPSHKVAKVKQLQEEGKRVAMVGDGINDSPALAMASVGIAIG-TGTDVAIEAADVVLIRNDLLDV 1333
Cdd:COG0474  608 elaelveeLSVFARVSPEQKARIVEALQKSGHVVAMTGDGVNDAPALKAADVGIAMGgEGTDAAKEAADIVLLDDNFATI 687
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16258817 1334 VASIDLSRKTVKRIR-----------INFVFALIYNLIGIPIAagVFLPIGLVLQ 1377
Cdd:COG0474  688 VLAVVEGRRVYVNIKkfilyllsknvGEVLTLLIYSLFNLFFL--PLTPLQLLWI 740
E1-E2_ATPase pfam00122
E1-E2 ATPase;
778-1025 5.24e-60

E1-E2 ATPase;


Pssm-ID: 306602  Cd Length: 221  Bit Score: 208.18  E-value: 5.24e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    778 MLFVFIALGRWLEHIAKGKTSEALAKLISLQATEATIVTLNSEnlllseEQVDVELVQRGDIIKVVPGGKFPVDGRVIEG 857
Cdd:pfam00122    2 IILLLVLLNALLEFYQEARARKALKALKSLLPPTATVLRDGGE------VEVPADELVPGDIVLLKPGERIPADGRIVEG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    858 HSMVDESLITGEAMPVAKKPGSTVIAGSINQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFI 937
Cdd:pfam00122   76 SLSVDESALTGESLPVEKKKGDMVFSGTVVVSGSAKAVVTATGEDTTLGKIARLVEEAKSKKTPLQRLLDKLAKYFTPVV 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    938 VLVSIVTLLVWIIIGFQnfeiveayfpgynrsisrtetiIRFAFQASITVLCIACPCSLGLATPTAVMVGTGVGAQNGIL 1017
Cdd:pfam00122  156 LLLALAVFLLTLLLGGD----------------------LAEALLRALAVLVAACPCALPLATPLALAVGARRLAKKGIL 213

                   ....*...
gi 16258817   1018 IKGGEPLE 1025
Cdd:pfam00122  214 VKRLSALE 221
P-type_ATPase_K cd02078
potassium-transporting ATPase ATP-binding subunit, KdpB, a subunit of the prokaryotic ...
767-1334 3.78e-50

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  Cd Length: 667  Bit Score: 191.32  E-value: 3.78e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  767 VNPITFFDTPPMLF-VFIALGRWL--------EHIAKGKtSEALAKliSLQATEATIVTlnseNLLL---SEEQVDVELV 834
Cdd:cd02078   42 FFPLLFSGGGPAGFnLAVSLWLWFtvlfanfaEAIAEGR-GKAQAD--SLRKTKTETQA----KRLRndgKIEKVPATDL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  835 QRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPG---STVIAGSINQNGSLLIRATHVGADTTLSQIVKL 911
Cdd:cd02078  115 KKGDIVLVEAGDIIPADGEVIEGVASVDESAITGESAPVIRESGgdrSSVTGGTKVLSDRIKVRITANPGETFLDRMIAL 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  912 VEEAQTSKAPIQqfadklsgyfVPFIVLVSIVTLLvwiiigfqnFEIVEAYFPGYNRSISRTetiirfafqASITVLcIA 991
Cdd:cd02078  195 VEGASRQKTPNE----------IALTILLVGLTLI---------FLIVVATLPPFAEYSGAP---------VSVTVL-VA 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  992 CPCSLGLATPTAVMVGTGVGA-----QNGILIKGGEPLEMAHKVKVVVFDKTGTITHGtpvvNQVKVLVESNKISRNKIL 1066
Cdd:cd02078  246 LLVCLIPTTIGGLLSAIGIAGmdrllRFNVIAKSGRAVEAAGDVDTLLLDKTGTITLG----NRQATEFIPVGGVDEKEL 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1067 AIVGTAESNS-EHPLGAAVTKYCKQELDTETLGTCTDFQVVPgcgISCKvTNIEGLlhksNLKIEENNIKNASlvqiDAI 1145
Cdd:cd02078  322 ADAAQLASLAdETPEGRSIVILAKQLGGTERDLDLSGAEFIP---FSAE-TRMSGV----DLPDGTEIRKGAV----DAI 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1146 neqsspsssmiidahlsnavntqqykvlignREWMIRNGLVISNDVDESMIEHERRGRTAVLVTIDDELCGLIAIADTVK 1225
Cdd:cd02078  390 -------------------------------RKYVRSLGGSIPEELEAIVEEISKQGGTPLVVAEDDRVLGVIYLKDIIK 438
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1226 PEAELAVHILKSMGLEVVLMTGDNSKTARSIASQVGITKVFAEVLPSHKVAKVKQLQEEGKRVAMVGDGINDSPALAMAS 1305
Cdd:cd02078  439 PGIKERFAELRKMGIKTVMITGDNPLTAAAIAAEAGVDDFLAEAKPEDKLELIRKEQAKGKLVAMTGDGTNDAPALAQAD 518
                        570       580       590
                 ....*....|....*....|....*....|..
gi 16258817 1306 VGIAIGTGTDVAIEAADVVLIRND---LLDVV 1334
Cdd:cd02078  519 VGVAMNSGTQAAKEAGNMVDLDSDptkLIEVV 550
P-type_ATPase_H cd02076
plant and fungal plasma membrane H(+)-ATPases, and related bacterial and archaeal putative H(+) ...
828-1372 2.66e-48

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  Cd Length: 781  Bit Score: 186.28  E-value: 2.66e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  828 QVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSM-VDESLITGEAMPVAKKPGSTVIAGSINQNGSLLIRATHVGADTTLS 906
Cdd:cd02076  104 EIDAKELVPGDIVSLKIGDIVPADARLLTGDALqVDQSALTGESLPVTKHPGDEAYSGSIVKQGEMLAVVTATGSNTFFG 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  907 QIVKLVEEAQtSKAPIQQFADKLSGYFvpfIVLVSIVTLLVWIIIgfqnfeiveayFPGYNRSIsrteTIIRFAFqasit 986
Cdd:cd02076  184 KTAALVASAE-EQGHLQKVLNKIGNFL---ILLALILVLIIVIVA-----------LYRHDPFL----EILQFVL----- 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  987 VLCIAcpcSLGLATPTAVMVGTGVGAQN----GILIKGGEPLEMAHKVKVVVFDKTGTITHGTPVVNQVKVLVESnkiSR 1062
Cdd:cd02076  240 VLLIA---SIPVAMPAVLTVTMAVGALElakkKAIVSRLSAIEELAGVDILCSDKTGTLTLNKLSLDEPYSLEGD---GK 313
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1063 NKILAIVGTAeSNSEH--PLGAAVTKYCKqeldtETLGTCTDFQVVpgcgiscKVTNIEGLLHKSNLKIEENN------I 1134
Cdd:cd02076  314 DELLLLAALA-SDTENpdAIDTAILNALD-----DYKPDLAGYKQL-------KFTPFDPVDKRTEATVEDPDgerfkvT 380
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1135 KNASLVQIDAineqsspsssmiidAHLSNAVNTQqykvlignrewmirnglvISNDVDESMiehERRGRT-AVLVTID-- 1211
Cdd:cd02076  381 KGAPQVILEL--------------VGNDEAIRQA------------------VEEKIDELA---SRGYRSlGVARKEDgg 425
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1212 -DELCGLIAIADTVKPEAELAVHILKSMGLEVVLMTGDNSKTARSIASQVGI-TKV------------------------ 1265
Cdd:cd02076  426 rWELLGLLPLFDPPRPDSKATIARAKELGVRVKMITGDQLAIAKETARQLGMgTNIlsaerlklggggggmpgseliefi 505
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1266 -----FAEVLPSHKVAKVKQLQEEGKRVAMVGDGINDSPALAMASVGIAIGTGTDVAIEAADVVLIRNDLLDVVASIDLS 1340
Cdd:cd02076  506 edadgFAEVFPEHKYRIVEALQQRGHLVGMTGDGVNDAPALKKADVGIAVSGATDAARAAADIVLTAPGLSVIIDAIKTS 585
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*..
gi 16258817 1341 RKTVKR------------IRINFVFALIY---NLIGIPIAAGVFLPI 1372
Cdd:cd02076  586 RQIFQRmksyviyriaetLRILVFFTLGIlilNFYPLPLIMIVLIAI 632
KdpB COG2216
High-affinity K+ transport system, ATPase chain B [Inorganic ion transport and metabolism];
794-1334 5.26e-48

High-affinity K+ transport system, ATPase chain B [Inorganic ion transport and metabolism];


Pssm-ID: 225126  Cd Length: 681  Bit Score: 184.78  E-value: 5.26e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  794 KGKTSEALAKLISlqaTEATIVTLNSENLllseEQVDVELVQRGDIIkvvpggkfPVDGRVIEGHSMVDESLITGEAMPV 873
Cdd:COG2216   98 RKTKTETIARLLR---ADGSIEMVPATEL----KKGDIVLVEAGEII--------PSDGEVIEGVASVDESAITGESAPV 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  874 AKKPG---STVIAGSINQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQqfadklsgyfVPFIVLVSIVTLLvwii 950
Cdd:COG2216  163 IRESGgdfSSVTGGTRVLSDWLKIRITANPGETFLDRMIALVEGAERQKTPNE----------IALTILLSGLTLI---- 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  951 igfqnFEIVEAYFPGYNRSISRTetiirfafQASITVLcIACPCSLGLATPTAVMVGTGVGA-----QNGILIKGGEPLE 1025
Cdd:COG2216  229 -----FLLAVATLYPFAIYSGGG--------AASVTVL-VALLVCLIPTTIGGLLSAIGIAGmdrvtQFNVIATSGRAVE 294
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1026 MAHKVKVVVFDKTGTITHGTpvvNQVKVLVESNKISRNKILAIVGTAESNSEHPLGAAVTKYCKQ---ELDTETLGTCTD 1102
Cdd:COG2216  295 AAGDVDTLLLDKTGTITLGN---RQASEFIPVPGVSEEELADAAQLASLADETPEGRSIVELAKKlgiELREDDLQSHAE 371
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1103 FqvVPgcgISCKvTNIEGLLHKSNLKIeennIKNAslvqIDAIneqsspsssmiidahlsnavntqqykvlignREWMIR 1182
Cdd:COG2216  372 F--VP---FTAQ-TRMSGVDLPGGREI----RKGA----VDAI-------------------------------RRYVRE 406
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1183 NGLVISNDVDESMIEHERRGRTAVLVTIDDELCGLIAIADTVKPEAELAVHILKSMGLEVVLMTGDNSKTARSIASQVGI 1262
Cdd:COG2216  407 RGGHIPEDLDAAVDEVSRLGGTPLVVVENGRILGVIYLKDIVKPGIKERFAELRKMGIKTVMITGDNPLTAAAIAAEAGV 486
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16258817 1263 TKVFAEVLPSHKVAKVKQLQEEGKRVAMVGDGINDSPALAMASVGIAIGTGTDVAIEAADVVLIRND---LLDVV 1334
Cdd:COG2216  487 DDFIAEATPEDKLALIRQEQAEGRLVAMTGDGTNDAPALAQADVGVAMNSGTQAAKEAANMVDLDSNptkLIEVV 561
kdpB TIGR01497
K+-transporting ATPase, B subunit; This model describes the P-type ATPase subunit of the ...
794-1334 1.14e-47

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  Cd Length: 675  Bit Score: 183.54  E-value: 1.14e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    794 KGKTSEALAKLISlqaTEATIVTLNSENLllseEQVDVELVQRGDIIkvvpggkfPVDGRVIEGHSMVDESLITGEAMPV 873
Cdd:TIGR01497   99 KGTKKTTFAKLLR---DDGAIDKVPADQL----KKGDIVLVEAGDVI--------PCDGEVIEGVASVDESAITGESAPV 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    874 AKKPGS---TVIAGSINQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQqfadklsgyfVPFIVLVSIVTLLvwii 950
Cdd:TIGR01497  164 IKESGGdfaSVTGGTRILSDWLVVECTANPGETFLDRMIALVEGAQRRKTPNE----------IALTILLIALTLV---- 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    951 igfqnFEIVEAYFPGYNrsisrTETIIRFAFQASITVLCIACPCSLGLATPTAVMVGTGVGAQNGILIKGGEPLEMAHKV 1030
Cdd:TIGR01497  230 -----FLLVTATLWPFA-----AYGGNAISVTVLVALLVCLIPTTIGGLLSAIGIAGMDRVLGFNVIATSGRAVEACGDV 299
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1031 KVVVFDKTGTITHGTpvvNQVKVLVESNKISRNKILAIVGTAESNSEHPLGAAVTKYCKQeldtetLGTCTDFQvvpgcg 1110
Cdd:TIGR01497  300 DTLLLDKTGTITLGN---RLASEFIPAQGVDEKTLADAAQLASLADDTPEGKSIVILAKQ------LGIREDDV------ 364
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1111 iscKVTNIEGLLHKSNLKIEENNIKNASLVQ---IDAIneqsspsssmiidahlsnavntqqykvlignREWMIRNGLVI 1187
Cdd:TIGR01497  365 ---QSLHATFVEFTAQTRMSGINLDNGRMIRkgaVDAI-------------------------------KRHVEANGGHI 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1188 SNDVDESMIEHERRGRTAVLVTIDDELCGLIAIADTVKPEAELAVHILKSMGLEVVLMTGDNSKTARSIASQVGITKVFA 1267
Cdd:TIGR01497  411 PTDLDQAVDQVARQGGTPLVVCEDNRIYGVIYLKDIVKGGIKERFAQLRKMGIKTIMITGDNRLTAAAIAAEAGVDDFIA 490
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1268 EVLPSHKVAKVKQLQEEGKRVAMVGDGINDSPALAMASVGIAIGTGTDVAIEAADVVLIRND---LLDVV 1334
Cdd:TIGR01497  491 EATPEDKIALIRQEQAEGKLVAMTGDGTNDAPALAQADVGVAMNSGTQAAKEAANMVDLDSDptkLIEVV 560
ATPase-IIIA_H TIGR01647
plasma-membrane proton-efflux P-type ATPase; This model describes the plasma membrane proton ...
778-1372 1.50e-44

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  Cd Length: 754  Bit Score: 174.44  E-value: 1.50e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    778 MLFVFIALGRWLEHIAkGKTSEALAKLISLQAT---EATIVTLNSenlllseeqvdVELVQrGDIIKVVPGGKFPVDGRV 854
Cdd:TIGR01647   64 LLLLNATIGFIEENKA-GNAVEALKQSLAPKARvlrDGKWQEIPA-----------SELVP-GDVVRLKIGDIVPADCRL 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    855 IEGHSM-VDESLITGEAMPVAKKPGSTVIAGSINQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYF 933
Cdd:TIGR01647  131 FEGDYIqVDQAALTGESLPVTKKTGDIAYSGSTVKQGEAEAVVTATGMNTFFGKAAALVQSTETGSGHLQKILSKIGLFL 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817    934 vpfIVLVSIVTLLVWIIIgfqnfeiveayFPGYNRSISRTetiIRFAFqasitVLCIAcpcSLGLATPTAVMVGTGVGAQ 1013
Cdd:TIGR01647  211 ---IVLIGVLVLIELVVL-----------FFGRGESFREG---LQFAL-----VLLVG---GIPIAMPAVLSVTMAVGAA 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1014 N----GILIKGGEPLEMAHKVKVVVFDKTGTIThgtpvvnqvkvlveSNKISRNKILAIVGTAESNSEHPLGAAVTKYCK 1089
Cdd:TIGR01647  266 ElakkKAIVTRLTAIEELAGMDILCSDKTGTLT--------------LNKLSIDEILPFFNGFDKDDVLLYAALASREED 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1090 QE-LDTETLGTCTDfqvvpgcgisckvtniegllhksnLKIEENNIKNASLVQIDaineqsspSSSMIIDAHLSNAVNTQ 1168
Cdd:TIGR01647  332 QDaIDTAVLGSAKD------------------------LKEARDGYKVLEFVPFD--------PVDKRTEATVEDPETGK 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1169 QYKVLIGNREWMIR---NGLVISNDVDESMIEHERRGRTAVLVTIDDE-----LCGLIAIADTVKPEAELAVHILKSMGL 1240
Cdd:TIGR01647  380 RFKVTKGAPQVILDlcdNKKEIEEKVEEKVDELASRGYRALGVARTDEegrwhFLGLLPLFDPPRHDTKETIERARHLGV 459
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1241 EVVLMTGDNSKTARSIASQVGI-TKV----------------------------FAEVLPSHKVAKVKQLQEEGKRVAMV 1291
Cdd:TIGR01647  460 EVKMVTGDHLAIAKETARRLGLgTNIytadvllkgdnrddlpsglgemvedadgFAEVFPEHKYEIVEILQKRGHLVGMT 539
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   1292 GDGINDSPALAMASVGIAIGTGTDVAIEAADVVLIRNDLLDVVASIDLSRKTVKR------------IRINFVFAL---I 1356
Cdd:TIGR01647  540 GDGVNDAPALKKADVGIAVAGATDAARSAADIVLTEPGLSVIVDAILESRKIFQRmksyviyriaetIRIVFFFGLlilI 619
                          650
                   ....*....|....*.
gi 16258817   1357 YNlIGIPIAAGVFLPI 1372
Cdd:TIGR01647  620 LN-FYFPPIMVVIIAI 634
P-type_ATPase cd07538
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ...
778-1378 1.02e-43

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  Cd Length: 653  Bit Score: 170.70  E-value: 1.02e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  778 MLFVFIALGRWLEHIAKGKTSEALAKLISLQATEATIVTLNSENLLLSEEQVdvelvqRGDIIKVVPGGKFPVDGRVIEG 857
Cdd:cd07538   61 ILLIFVVVIIAIEVVQEWRTERALEALKNLSSPRATVIRDGRERRIPSRELV------PGDLLILGEGERIPADGRLLEN 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  858 HSM-VDESLITGEAMPVAKKPGST------------VIAGSINQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQ 924
Cdd:cd07538  135 DDLgVDESTLTGESVPVWKRIDGKamsapggwdknfCYAGTLVVRGRGVAKVEATGSRTELGKIGKSLAEMDDEPTPLQK 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  925 FADKLSGYFVPFIVLVSIVTLLVWiiigfqnfeiveayfpGYNRSiSRTETIIrfafqASITVLCIACPCSLGLATPTAV 1004
Cdd:cd07538  215 QTGRLVKLCALAALVFCALIVAVY----------------GVTRG-DWIQAIL-----AGITLAMAMIPEEFPVILTVFM 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1005 MVGTGVGAQNGILIKGGEPLEMAHKVKVVVFDKTGTIT-------------HGTPVVNQVKVLVESNKISRNKILAIVGT 1071
Cdd:cd07538  273 AMGAWRLAKKNVLVRRAAAVETLGSITVLCVDKTGTLTknqmevveltslvREYPLRPELRMMGQVWKRPEGAFAAAKGS 352
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1072 AEsnsehplgaAVTKYCkqeldtetlgtctdfqvvpgcgisckvtniegllhksNLKIEEnniKNASLVQIDAINEQSsp 1151
Cdd:cd07538  353 PE---------AIIRLC-------------------------------------RLNPDE---KAAIEDAVSEMAGEG-- 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1152 sssmiidahlsnavntqqYKVLignrewmirnGLVISNDVDESMIEHerrgrtavlvtIDD---ELCGLIAIADTVKPEA 1228
Cdd:cd07538  382 ------------------LRVL----------AVAACRIDESFLPDD-----------LEDavfIFVGLIGLADPLREDV 422
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1229 ELAVHILKSMGLEVVLMTGDNSKTARSIASQVGI--------------------------TKVFAEVLPSHKVAKVKQLQ 1282
Cdd:cd07538  423 PEAVRICCEAGIRVVMITGDNPATAKAIAKQIGLdntdnvitgqeldamsdeelaekvrdVNIFARVVPEQKLRIVQAFK 502
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1283 EEGKRVAMVGDGINDSPALAMASVGIAIGT-GTDVAIEAADVVLIRNDLLDVVASIDLSRKTVKRIR--INFVFAliynl 1359
Cdd:cd07538  503 ANGEIVAMTGDGVNDAPALKAAHIGIAMGKrGTDVAREASDIVLLDDNFSSIVSTIRLGRRIYDNLKkaITYVFA----- 577
                        650
                 ....*....|....*....
gi 16258817 1360 IGIPIAAGVFLPIGLVLQP 1378
Cdd:cd07538  578 IHVPIAGLALLPPLLGLPP 596
P-type_ATPase_cation cd02080
P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, ...
792-1372 2.84e-42

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  Cd Length: 819  Bit Score: 167.82  E-value: 2.84e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  792 IAKGKTSEALAKLISLQATEATiVTLNSENLLLSEEqvdvELVQrGDIIKVVPGGKFPVDGRVIEGHSM-VDESLITGEA 870
Cdd:cd02080   75 IQEGKAEKALAAIKNMLSPEAT-VLRDGKKLTIDAE----ELVP-GDIVLLEAGDKVPADLRLIEARNLqIDESALTGES 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  871 MPVAKK------------------PGSTVIAGSinqnGSLLIRAThvGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGY 932
Cdd:cd02080  149 VPVEKQegpleedtplgdrknmaySGTLVTAGS----ATGVVVAT--GADTEIGRINQLLAEVEQLATPLTRQIAKFSKA 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  933 FVPFIVLVSIVTLLVWIIIGfqNFEIVEAyfpgynrsisrtetiirfaFQASITVLCIACPcsLGLATPTAVMVGTGVG- 1011
Cdd:cd02080  223 LLIVILVLAALTFVFGLLRG--DYSLVEL-------------------FMAVVALAVAAIP--EGLPAVITITLAIGVQr 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1012 -AQNGILIKGGEPLEMAHKVKVVVFDKTGTITHGTPVVNQVKVLV-ESNKISRNKILAIVGTAESnsehplGAAVTKYCK 1089
Cdd:cd02080  280 mAKRNAIIRRLPAVETLGSVTVICSDKTGTLTRNEMTVQAIVTLCnDAQLHQEDGHWKITGDPTE------GALLVLAAK 353
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1090 QELDTETLGTctdfqvvpgcgiscKVTNIEGLLHKSNLKIEenniknASLVQIDA---INEQSSPSS--SMIIDAHLSNA 1164
Cdd:cd02080  354 AGLDPDRLAS--------------SYPRVDKIPFDSAYRYM------ATLHRDDGqrvIYVKGAPERllDMCDQELLDGG 413
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1165 VNTQQYKVLIGNREWMIRNGL-VI-----SNDVDESMIEHErrgrtavlvTIDDEL--CGLIAIADTVKPEAELAVHILK 1236
Cdd:cd02080  414 VSPLDRAYWEAEAEDLAKQGLrVLafayrEVDSEVEEIDHA---------DLEGGLtfLGLQGMIDPPRPEAIAAVAECQ 484
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1237 SMGLEVVLMTGDNSKTARSIASQVGI--------------------------TKVFAEVLPSHKVAKVKQLQEEGKRVAM 1290
Cdd:cd02080  485 SAGIRVKMITGDHAETARAIGAQLGLgdgkkvltgaeldalddeelaeavdeVDVFARTSPEHKLRLVRALQARGEVVAM 564
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1291 VGDGINDSPALAMASVGIAIG-TGTDVAIEAADVVLIRNDLLDVVASIDLSRKTVKRIRINFVFALIYNL-----IGIPI 1364
Cdd:cd02080  565 TGDGVNDAPALKQADIGIAMGiKGTEVAKEAADMVLADDNFATIAAAVEEGRRVYDNLKKFILFTLPTNLgeglvIIVAI 644

                 ....*...
gi 16258817 1365 AAGVFLPI 1372
Cdd:cd02080  645 LFGVTLPL 652
PRK01122 PRK01122
potassium-transporting ATPase subunit B; Provisional
767-1334 2.76e-41

potassium-transporting ATPase subunit B; Provisional


Pssm-ID: 234905  Cd Length: 679  Bit Score: 163.44  E-value: 2.76e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   767 VNPITFFDTPPMLFVF-IALGRWL--------EHIAKGKtSEALAKliSLQATEATIVT--LNSENlllSEEQVDVELVQ 835
Cdd:PRK01122   51 IAPLLFQSGGPAGFNLaITLWLWFtvlfanfaEALAEGR-GKAQAD--SLRGAKKDTFArkLREPG---AAEEVPATELR 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   836 RGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPG---STVIAGSINQNGSLLIRATHVGADTTLSQIVKLV 912
Cdd:PRK01122  125 KGDIVLVEAGEIIPADGEVIEGVASVDESAITGESAPVIRESGgdfSSVTGGTRVLSDWIVIRITANPGESFLDRMIALV 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   913 EEAQTSKAPiQQFAdkLSgyfvpfiVLVSIVTLLvwiiigfqnFEIVEAyfpgynrsisrteTIIRFA----FQASITVL 988
Cdd:PRK01122  205 EGAKRQKTP-NEIA--LT-------ILLAGLTII---------FLLVVA-------------TLPPFAaysgGALSITVL 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817   989 cIA---C--PCSLGlatptAVMVGTGVG-----AQNGILIKGGEPLEMAHKVKVVVFDKTGTITHGTpvvNQVKVLVESN 1058
Cdd:PRK01122  253 -VAllvCliPTTIG-----GLLSAIGIAgmdrvLQANVIATSGRAVEAAGDVDTLLLDKTGTITLGN---RQASEFLPVP 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  1059 KISRNKILAIVGTAESNSEHPLGAAVTKYCKQELdtetlgtctdfqvvpgcgisckvtniegllhksNLKIEENNIKNAS 1138
Cdd:PRK01122  324 GVTEEELADAAQLSSLADETPEGRSIVVLAKQRF---------------------------------NLRERDLQSLHAT 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  1139 LVQIDAINEQSspsssmiidahlsnAVNTQQYKVLIGN----REWMIRNGLVISNDVDESMIEHERRGRTAVLVTIDDEL 1214
Cdd:PRK01122  371 FVPFSAQTRMS--------------GVDLDGREIRKGAvdaiRRYVESNGGHFPAELDAAVDEVARKGGTPLVVAEDNRV 436
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  1215 CGLIAIADTVKP---E--AELavhilKSMGLEVVLMTGDNSKTARSIASQVGITKVFAEVLPSHKVAKVKQLQEEGKRVA 1289
Cdd:PRK01122  437 LGVIYLKDIVKPgikErfAEL-----RKMGIKTVMITGDNPLTAAAIAAEAGVDDFLAEATPEDKLALIRQEQAEGRLVA 511
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*...
gi 16258817  1290 MVGDGINDSPALAMASVGIAIGTGTDVAIEAADVVLIRND---LLDVV 1334
Cdd:PRK01122  512 MTGDGTNDAPALAQADVGVAMNSGTQAAKEAGNMVDLDSNptkLIEVV 559
P-type_ATPase cd07539
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ...
826-1369 6.60e-41

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  Cd Length: 634  Bit Score: 161.82  E-value: 6.60e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  826 EEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSM-VDESLITGEAMPVAK-------KP----------GSTVIAGSin 887
Cdd:cd07539  106 TQTVPAESLVPGDVIELRAGEVVPADARLLEADDLeVDESALTGESLPVDKqvaptpgAPladracmlyeGTTVVSGQ-- 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  888 qnGSLLIRAThvGADTTLSQIVKLVEEAqTSKAPIQQFADKLSGYFVPF-IVLVSIVTLLvwiiigfqnfeiveayfpGY 966
Cdd:cd07539  184 --GRAVVVAT--GPHTEAGRAQSLVAPV-ETATGVQAQLRELTSQLLPLsLGGGAAVTGL------------------GL 240
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817  967 NRSISrtetiIRFAFQASITVLCIACPCSLGLATPTAVMVGTGVGAQNGILIKGGEPLEMAHKVKVVVFDKTGTITHGTP 1046
Cdd:cd07539  241 LRGAP-----LRQAVADGVSLAVAAVPEGLPLVATLAQLAAARRLSRRGVLVRSPRTVEALGRVDTICFDKTGTLTENRL 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1047 VVNQVK-VLVESN-KISRNKILAIVGTaesNSEHPL----GAAVTkyckqeldtetlgtctdfqVVPGCGISCKVTNIEG 1120
Cdd:cd07539  316 RVVQVRpPLAELPfESSRGYAAAIGRT---GGGIPLlavkGAPEV-------------------VLPRCDRRMTGGQVVP 373
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1121 LLHKSNLKIEENNIKNASlvqidaineqsspsssmiidahlsnavntQQYKVL-IGNREWMIRNGLVISNDVDESmiehe 1199
Cdd:cd07539  374 LTEADRQAIEEVNELLAG-----------------------------QGLRVLaVAYRTLDAGTTHAVEAVVDDL----- 419
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16258817 1200 rrgrtavlvtiddELCGLIAIADTVKPEAELAVHILKSMGLEVVLMTGDNSKTARSIASQVGI----------------- 1262
Cdd:cd07539  420 -------------ELLGLLGLADTARPGAAALIAALHDAGIDVVMITGDHPITARAIAKELGLprdaevvtgaeldalde 486
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|