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Conserved domains on  [gi|342187274|ref|NP_001230111|]
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copper-transporting ATPase 2 isoform c [Homo sapiens]

Protein Classification

copper-transporting P-type ATPase( domain architecture ID 11534132)

copper-transporting P-type ATPase couples the hydrolysis of ATP with the export of Cu(+) or Cu(2+); P-type ATPases are distinguished from other transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P-type_ATPase_Cu-like cd02094
P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A ...
541-1243 0e+00

P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A and ATP7B; The mammalian copper-transporting P-type ATPases, ATP7A and ATP7B are key molecules required for the regulation and maintenance of copper homeostasis. Menkes and Wilson diseases are caused by mutation in ATP7A and ATP7B respectively. This subfamily includes other copper-transporting ATPases such as: Bacillus subtilis CopA , Archeaoglobus fulgidus CopA, and Saccharomyces cerevisiae Ccc2p. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


:

Pssm-ID: 319783 [Multi-domain]  Cd Length: 647  Bit Score: 907.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  541 KSFLCSLVFGIPVMALMIYMlipsnephqsMVLDHNIIPGLSILNLIFFILCTFVQLLGGWYFYVQAYKSLRHRSANMDV 620
Cdd:cd02094     1 RRLILSLLLTLPLLLLMMGG----------MLGPPLPLLLLQLNWWLQFLLATPVQFWGGRPFYRGAWKALKHGSANMDT 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  621 LIVLATSIAYVYSLVILVVAVAEKAErSPVTFFDTPPMLFVFIALGRWLEHLAKSKTSEALAKLMSLQATEATVVTLGEd 700
Cdd:cd02094    71 LVALGTSAAYLYSLVALLFPALFPGG-APHVYFEAAAVIITFILLGKYLEARAKGKTSEAIKKLLGLQPKTARVIRDGK- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  701 nliirEEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMADESLITGEAMPVTKKPGSTVIAGSINAHGSVLIKATHVG 780
Cdd:cd02094   149 -----EVEVPIEEVQVGDIVRVRPGEKIPVDGVVVEGESSVDESMLTGESLPVEKKPGDKVIGGTINGNGSLLVRATRVG 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  781 NDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTLTLVVWIVIGFidfgvvqryfpnpnkhisqtEVIIRFA 860
Cdd:cd02094   224 ADTTLAQIIRLVEEAQGSKAPIQRLADRVSGVFVPVVIAIAILTFLVWLLLGP--------------------EPALTFA 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  861 FQTSITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLLGDVatl 940
Cdd:cd02094   284 LVAAVAVLVIACPCALGLATPTAIMVGTGRAAELGILIKGGEALERAHKVDTVVFDKTGTLTEGKPEVTDVVPLPGD--- 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  941 PLRKVLAVVGTAEASSEHPLGVAVTKYCKEELGteTLGYCTDFQAVPGCGIGCKVSNVEgilahserplsapashlneag 1020
Cdd:cd02094   361 DEDELLRLAASLEQGSEHPLAKAIVAAAKEKGL--ELPEVEDFEAIPGKGVRGTVDGRR--------------------- 417
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1021 slpaekdavpqtfsVLIGNREWLRRNGLTISSDVSDAMtDHEMKGQTAILVAIDGVLCGMIAIADAVKQEAALAVHTLQS 1100
Cdd:cd02094   418 --------------VLVGNRRLMEENGIDLSALEAEAL-ALEEEGKTVVLVAVDGELAGLIAVADPLKPDAAEAIEALKK 482
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1101 MGVDVVLITGDNRKTARAIATQVGINKVFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIGTGTDVA 1180
Cdd:cd02094   483 MGIKVVMLTGDNRRTARAIAKELGIDEVIAEVLPEDKAEKVKKLQAQGKKVAMVGDGINDAPALAQADVGIAIGSGTDVA 562
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187274 1181 IEAADVVLIRNDLLDVVASIHLSKRTVRRIRINLVLALIYNLVGIPIAAGVFMPI-GIVLQPWM 1243
Cdd:cd02094   563 IESADIVLMRGDLRGVVTAIDLSRATMRNIKQNLFWAFIYNVIGIPLAAGVLYPFgGILLSPMI 626
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
146-209 2.24e-18

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


:

Pssm-ID: 238219 [Multi-domain]  Cd Length: 63  Bit Score: 80.34  E-value: 2.24e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187274  146 KLRVEGMTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYlIQPEDLRDHVNDMGFEAA 209
Cdd:cd00371     1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKAR 63
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
381-443 1.89e-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 [Multi-domain]  Cd Length: 63  Bit Score: 77.65  E-value: 1.89e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 342187274  381 LQIKGMTCASCVSNIERNLQKEAGVLSVLVALMAGKAEIKYDPEViQPLEIAQFIQDLGFEAA 443
Cdd:cd00371     2 LSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPEV-SPEELLEAIEDAGYKAR 63
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
61-124 4.51e-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 [Multi-domain]  Cd Length: 63  Bit Score: 76.49  E-value: 4.51e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187274   61 TVRILGMTCQSCVKSIEDRISNLKGIISMKVSLEQGSATVKYVPSvVCLQQVCHQIGDMGFEAS 124
Cdd:cd00371     1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKAR 63
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
456-519 1.16e-16

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


:

Pssm-ID: 238219 [Multi-domain]  Cd Length: 63  Bit Score: 75.33  E-value: 1.16e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187274  456 ELTITGMTCASCVHNIESKLTRTNGITYASVALATSKALVKFDPEiIGPRDIIKIIEEIGFHAS 519
Cdd:cd00371     1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKAR 63
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
258-317 2.74e-14

Copper chaperone CopZ [Inorganic ion transport and metabolism];


:

Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 68.78  E-value: 2.74e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 342187274  258 TLQLRIDGMHCM---------ISQLEGVQQISVSLAEGTATVLYNPSVISPEELRAAIEDMGFEASVVS 317
Cdd:COG2608     3 TVTLKVEGMTCGhcvarvekaLKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYEVEKAE 71
 
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 ...
541-1243 0e+00

P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A and ATP7B; The mammalian copper-transporting P-type ATPases, ATP7A and ATP7B are key molecules required for the regulation and maintenance of copper homeostasis. Menkes and Wilson diseases are caused by mutation in ATP7A and ATP7B respectively. This subfamily includes other copper-transporting ATPases such as: Bacillus subtilis CopA , Archeaoglobus fulgidus CopA, and Saccharomyces cerevisiae Ccc2p. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319783 [Multi-domain]  Cd Length: 647  Bit Score: 907.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  541 KSFLCSLVFGIPVMALMIYMlipsnephqsMVLDHNIIPGLSILNLIFFILCTFVQLLGGWYFYVQAYKSLRHRSANMDV 620
Cdd:cd02094     1 RRLILSLLLTLPLLLLMMGG----------MLGPPLPLLLLQLNWWLQFLLATPVQFWGGRPFYRGAWKALKHGSANMDT 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  621 LIVLATSIAYVYSLVILVVAVAEKAErSPVTFFDTPPMLFVFIALGRWLEHLAKSKTSEALAKLMSLQATEATVVTLGEd 700
Cdd:cd02094    71 LVALGTSAAYLYSLVALLFPALFPGG-APHVYFEAAAVIITFILLGKYLEARAKGKTSEAIKKLLGLQPKTARVIRDGK- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  701 nliirEEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMADESLITGEAMPVTKKPGSTVIAGSINAHGSVLIKATHVG 780
Cdd:cd02094   149 -----EVEVPIEEVQVGDIVRVRPGEKIPVDGVVVEGESSVDESMLTGESLPVEKKPGDKVIGGTINGNGSLLVRATRVG 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  781 NDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTLTLVVWIVIGFidfgvvqryfpnpnkhisqtEVIIRFA 860
Cdd:cd02094   224 ADTTLAQIIRLVEEAQGSKAPIQRLADRVSGVFVPVVIAIAILTFLVWLLLGP--------------------EPALTFA 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  861 FQTSITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLLGDVatl 940
Cdd:cd02094   284 LVAAVAVLVIACPCALGLATPTAIMVGTGRAAELGILIKGGEALERAHKVDTVVFDKTGTLTEGKPEVTDVVPLPGD--- 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  941 PLRKVLAVVGTAEASSEHPLGVAVTKYCKEELGteTLGYCTDFQAVPGCGIGCKVSNVEgilahserplsapashlneag 1020
Cdd:cd02094   361 DEDELLRLAASLEQGSEHPLAKAIVAAAKEKGL--ELPEVEDFEAIPGKGVRGTVDGRR--------------------- 417
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1021 slpaekdavpqtfsVLIGNREWLRRNGLTISSDVSDAMtDHEMKGQTAILVAIDGVLCGMIAIADAVKQEAALAVHTLQS 1100
Cdd:cd02094   418 --------------VLVGNRRLMEENGIDLSALEAEAL-ALEEEGKTVVLVAVDGELAGLIAVADPLKPDAAEAIEALKK 482
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1101 MGVDVVLITGDNRKTARAIATQVGINKVFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIGTGTDVA 1180
Cdd:cd02094   483 MGIKVVMLTGDNRRTARAIAKELGIDEVIAEVLPEDKAEKVKKLQAQGKKVAMVGDGINDAPALAQADVGIAIGSGTDVA 562
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187274 1181 IEAADVVLIRNDLLDVVASIHLSKRTVRRIRINLVLALIYNLVGIPIAAGVFMPI-GIVLQPWM 1243
Cdd:cd02094   563 IESADIVLMRGDLRGVVTAIDLSRATMRNIKQNLFWAFIYNVIGIPLAAGVLYPFgGILLSPMI 626
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
455-1244 0e+00

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 848.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  455 IELTITGMTCASCVHNIESKLTRTNGITYASVALATSKALVKFDPEIIGPRDIIKIIEEIGFHASLAQRNPNAHHlDHKM 534
Cdd:COG2217     3 VRLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEKAGYEAEPADADAAAEE-AREK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  535 EIKQWKKSFLCSLVFGIPVMALMIYMLIPSNEPHqsmvldhniipglsilnLIFFILCTFVQLLGGWYFYVQAYKSLRHR 614
Cdd:COG2217    82 ELRDLLRRLAVAGVLALPVMLLSMPEYLGGGLPG-----------------WLSLLLATPVVFYAGWPFFRGAWRALRHR 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  615 SANMDVLIVLATSIAYVYSLVILVVAVAEkaerspvTFFDTPPMLFVFIALGRWLEHLAKSKTSEALAKLMSLQATEATV 694
Cdd:COG2217   145 RLNMDVLVALGTLAAFLYSLYATLFGAGH-------VYFEAAAMIIFLLLLGRYLEARAKGRARAAIRALLSLQPKTARV 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  695 VTLGEdnliirEEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMADESLITGEAMPVTKKPGSTVIAGSINAHGSVLI 774
Cdd:COG2217   218 LRDGE------EVEVPVEELRVGDRVLVRPGERIPVDGVVLEGESSVDESMLTGESLPVEKTPGDEVFAGTINLDGSLRV 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  775 KATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTLTLVVWIVIGFiDFGvvqryfpnpnkhisqte 854
Cdd:COG2217   292 RVTKVGSDTTLARIIRLVEEAQSSKAPIQRLADRIARYFVPAVLAIAALTFLVWLLFGG-DFS----------------- 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  855 viirFAFQTSITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLL 934
Cdd:COG2217   354 ----TALYRAVAVLVIACPCALGLATPTAIMVGTGRAARRGILIKGGEALERLAKVDTVVFDKTGTLTEGKPEVTDVVPL 429
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  935 GDVATlplRKVLAVVGTAEASSEHPLGVAVTKYCKEElGTETLGyCTDFQAVPGCGIGCKVSNVEgilahserplsapas 1014
Cdd:COG2217   430 DGLDE---DELLALAAALEQGSEHPLARAIVAAAKER-GLELPE-VEDFEAIPGKGVEATVDGKR--------------- 489
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1015 hlneagslpaekdavpqtfsVLIGNREWLRRNGLTISSDVSDAMTDHEMKGQTAILVAIDGVLCGMIAIADAVKQEAALA 1094
Cdd:COG2217   490 --------------------VLVGSPRLLEEEGIDLPEALEERAEELEAEGKTVVYVAVDGRLLGLIALADTLRPEAAEA 549
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1095 VHTLQSMGVDVVLITGDNRKTARAIATQVGINKVFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIG 1174
Cdd:COG2217   550 IAALKALGIRVVMLTGDNERTAEAVARELGIDEVRAEVLPEDKAAAVRELQAQGKKVAMVGDGINDAPALAAADVGIAMG 629
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1175 TGTDVAIEAADVVLIRNDLLDVVASIHLSKRTVRRIRINLVLALIYNLVGIPIAAGVFmpigivLQPWMG 1244
Cdd:COG2217   630 SGTDVAIEAADIVLMRDDLRGVPDAIRLSRATMRIIRQNLFWAFGYNVIGIPLAAGGL------LSPWIA 693
ATPase-IB1_Cu TIGR01511
copper-(or silver)-translocating P-type ATPase; This model describes the P-type ATPase ...
599-1244 0e+00

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


Pssm-ID: 273664 [Multi-domain]  Cd Length: 562  Bit Score: 739.47  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   599 GGWYFYVQAYKSLRHRSANMDVLIVLATSIAYVYSLVILVVAVAEKAErSPVTFFDTPPMLFVFIALGRWLEHLAKSKTS 678
Cdd:TIGR01511    1 AGRPFYKSAWKALRHKAPNMDTLIALGTTVAYGYSLVALLANQVLTGL-HVHTFFDASAMLITFILLGRWLEMLAKGRAS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   679 EALAKLMSLQATEATVVTLGEDnliirEEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMADESLITGEAMPVTKKPG 758
Cdd:TIGR01511   80 DALSKLAKLQPSTATLLTKDGS-----IEEVPVALLQPGDIVKVLPGEKIPVDGTVIEGESEVDESLVTGESLPVPKKVG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   759 STVIAGSINAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTLTLVVWIvigfidfgv 838
Cdd:TIGR01511  155 DPVIAGTVNGTGSLVVRATATGEDTTLAQIVRLVRQAQQSKAPIQRLADKVAGYFVPVVIAIALITFVIWL--------- 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   839 vqryfpnpnkhisqteviirFAFQTSITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAHKIKTVMFDKT 918
Cdd:TIGR01511  226 --------------------FALEFAVTVLIIACPCALGLATPTVIAVATGLAAKNGVLIKDGDALERAANIDTVVFDKT 285
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   919 GTITHGVPRVMRVLLLGDVATlplRKVLAVVGTAEASSEHPLGVAVTKYCKEELGTETLgyCTDFQAVPGCGIGCKvsnV 998
Cdd:TIGR01511  286 GTLTQGKPTVTDVHVFGDRDR---TELLALAAALEAGSEHPLAKAIVSYAKEKGITLVT--VSDFKAIPGIGVEGT---V 357
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   999 EGIlahserplsapashlneagslpaekdavpqtfSVLIGNREWLRRNGLtissdvsdAMTDHEMKGQTAILVAIDGVLC 1078
Cdd:TIGR01511  358 EGT--------------------------------KIQLGNEKLLGENAI--------KIDGKAGQGSTVVLVAVNGELA 397
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  1079 GMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGINkVFAEVLPSHKVAKVQELQNKGKKVAMVGDGV 1158
Cdd:TIGR01511  398 GVFALEDQLRPEAKEVIQALKRRGIEPVMLTGDNRKTAKAVAKELGID-VRAEVLPDDKAALIKKLQEKGPVVAMVGDGI 476
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  1159 NDSPALAQADMGVAIGTGTDVAIEAADVVLIRNDLLDVVASIHLSKRTVRRIRINLVLALIYNLVGIPIAAGVFMPIGIV 1238
Cdd:TIGR01511  477 NDAPALAQADVGIAIGAGTDVAIEAADVVLLRNDLNDVATAIDLSRKTLRRIKQNLLWAFGYNVIAIPIAAGVLYPIGIL 556

                   ....*.
gi 342187274  1239 LQPWMG 1244
Cdd:TIGR01511  557 LSPAVA 562
copA PRK10671
copper-exporting P-type ATPase CopA;
376-1241 1.38e-155

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 490.02  E-value: 1.38e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  376 PQKCFLQIKGMTCASCVSNIERNLQKEAGVLSVLV--------------ALMAGKAEIKYDPEV----IQPLEIAQfIQD 437
Cdd:PRK10671    2 SQTIDLTLDGLSCGHCVKRVKESLEQRPDVEQADVsiteahvtgtasaeALIETIKQAGYDASVshpkAKPLTESS-IPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  438 LGFEAAVME---DYAGSDGNIELTITGMTCASCVHNIESKLTRTNGITYASVALATSKALVKFDPEiigPRDIIKIIEEI 514
Cdd:PRK10671   81 EALTAASEElpaATADDDDSQQLLLSGMSCASCVSRVQNALQSVPGVTQARVNLAERTALVMGSAS---PQDLVQAVEKA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  515 GFHASL----AQRNPNAHHLDHK-MEIKQWKKSFlcSLVFGIPVMalmIYMLIPSNephqSMVLDHNIIPGLSIlnlifF 589
Cdd:PRK10671  158 GYGAEAieddAKRRERQQETAQAtMKRFRWQAIV--ALAVGIPVM---VWGMIGDN----MMVTADNRSLWLVI-----G 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  590 ILCTFVQLLGGWYFYVQAYKSLRHRSANMDVLIVLATSIAYVYSL-VILVVAVAEKAERSpvTFFDTPPMLFVFIALGRW 668
Cdd:PRK10671  224 LITLAVMVFAGGHFYRSAWKSLLNGSATMDTLVALGTGAAWLYSMsVNLWPQWFPMEARH--LYYEASAMIIGLINLGHM 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  669 LEHLAKSKTSEALAKLMSLQATEATVVTlgEDNliirEEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMADESLITG 748
Cdd:PRK10671  302 LEARARQRSSKALEKLLDLTPPTARVVT--DEG----EKSVPLADVQPGMLLRLTTGDRVPVDGEITQGEAWLDEAMLTG 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  749 EAMPVTKKPGSTVIAGSINAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTLTLVVW 828
Cdd:PRK10671  376 EPIPQQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAVFVPVVVVIALVSAAIW 455
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  829 ivigfidfgvvqrYFPNPNKHISQTEVIIrfafqtsITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAH 908
Cdd:PRK10671  456 -------------YFFGPAPQIVYTLVIA-------TTVLIIACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRAS 515
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  909 KIKTVMFDKTGTITHGVPRVMRVLLLGDVATlplRKVLAVVGTAEASSEHPLGVAVTkyckEELGTETLGYCTDFQAVPG 988
Cdd:PRK10671  516 TLDTLVFDKTGTLTEGKPQVVAVKTFNGVDE---AQALRLAAALEQGSSHPLARAIL----DKAGDMTLPQVNGFRTLRG 588
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  989 CGIGCKVSNVEgilahserplsapashlneagslpaekdavpqtfsVLIGNREWLRRNGLTiSSDVSDAMTDHEMKGQTA 1068
Cdd:PRK10671  589 LGVSGEAEGHA-----------------------------------LLLGNQALLNEQQVD-TKALEAEITAQASQGATP 632
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1069 ILVAIDGVLCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGINKVFAEVLPSHKVAKVQELQNKG 1148
Cdd:PRK10671  633 VLLAVDGKAAALLAIRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVLPDGKAEAIKRLQSQG 712
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1149 KKVAMVGDGVNDSPALAQADMGVAIGTGTDVAIEAADVVLIRNDLLDVVASIHLSKRTVRRIRINLVLALIYNLVGIPIA 1228
Cdd:PRK10671  713 RQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRATLRNMKQNLLGAFIYNSLGIPIA 792
                         890
                  ....*....|....
gi 342187274 1229 AGVFMPI-GIVLQP 1241
Cdd:PRK10671  793 AGILWPFtGTLLNP 806
E1-E2_ATPase pfam00122
E1-E2 ATPase;
686-894 4.29e-50

E1-E2 ATPase;


Pssm-ID: 425475 [Multi-domain]  Cd Length: 181  Bit Score: 175.45  E-value: 4.29e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   686 SLQATEATVVTLGEdnliirEEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMADESLITGEAMPVTKKPGSTVIAGS 765
Cdd:pfam00122    1 SLLPPTATVLRDGT------EEEVPADELVPGDIVLLKPGERVPADGRIVEGSASVDESLLTGESLPVEKKKGDMVYSGT 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   766 INAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTLTLVVWIVIGFIDFgvvqryfpn 845
Cdd:pfam00122   75 VVVSGSAKAVVTATGEDTELGRIARLVEEAKSKKTPLQRLLDRLGKYFSPVVLLIALAVFLLWLFVGGPPL--------- 145
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 342187274   846 pnkhisqteviirFAFQTSITVLCIACPCSLGLATPTAVMVGTGVAAQN 894
Cdd:pfam00122  146 -------------RALLRALAVLVAACPCALPLATPLALAVGARRLAKK 181
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
146-209 2.24e-18

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


Pssm-ID: 238219 [Multi-domain]  Cd Length: 63  Bit Score: 80.34  E-value: 2.24e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187274  146 KLRVEGMTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYlIQPEDLRDHVNDMGFEAA 209
Cdd:cd00371     1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKAR 63
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
381-443 1.89e-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 [Multi-domain]  Cd Length: 63  Bit Score: 77.65  E-value: 1.89e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 342187274  381 LQIKGMTCASCVSNIERNLQKEAGVLSVLVALMAGKAEIKYDPEViQPLEIAQFIQDLGFEAA 443
Cdd:cd00371     2 LSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPEV-SPEELLEAIEDAGYKAR 63
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
61-124 4.51e-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 [Multi-domain]  Cd Length: 63  Bit Score: 76.49  E-value: 4.51e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187274   61 TVRILGMTCQSCVKSIEDRISNLKGIISMKVSLEQGSATVKYVPSvVCLQQVCHQIGDMGFEAS 124
Cdd:cd00371     1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKAR 63
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
456-519 1.16e-16

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


Pssm-ID: 238219 [Multi-domain]  Cd Length: 63  Bit Score: 75.33  E-value: 1.16e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187274  456 ELTITGMTCASCVHNIESKLTRTNGITYASVALATSKALVKFDPEiIGPRDIIKIIEEIGFHAS 519
Cdd:cd00371     1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKAR 63
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
145-209 2.77e-16

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 74.56  E-value: 2.77e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 342187274  145 VKLRVEGMTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYLIQPEDLRDHVNDMGFEAA 209
Cdd:COG2608     4 VTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYEVE 68
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
455-522 1.72e-15

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 72.24  E-value: 1.72e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 342187274  455 IELTITGMTCASCVHNIESKLTRTNGITYASVALATSKALVKFDPEIIGPRDIIKIIEEIGFHASLAQ 522
Cdd:COG2608     4 VTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYEVEKAE 71
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
381-446 3.82e-15

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 71.47  E-value: 3.82e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 342187274  381 LQIKGMTCASCVSNIERNLQKEAGVLSVLVALMAGKAEIKYDPEVIQPLEIAQFIQDLGFEAAVME 446
Cdd:COG2608     6 LKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYEVEKAE 71
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
258-317 2.74e-14

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 68.78  E-value: 2.74e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 342187274  258 TLQLRIDGMHCM---------ISQLEGVQQISVSLAEGTATVLYNPSVISPEELRAAIEDMGFEASVVS 317
Cdd:COG2608     3 TVTLKVEGMTCGhcvarvekaLKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYEVEKAE 71
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
260-314 3.42e-14

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


Pssm-ID: 238219 [Multi-domain]  Cd Length: 63  Bit Score: 68.40  E-value: 3.42e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187274  260 QLRIDGMHC---------MISQLEGVQQISVSLAEGTATVLYNPSViSPEELRAAIEDMGFEAS 314
Cdd:cd00371     1 ELSVEGMTCagcvskiekALEKLPGVESVEVDLETGKATVEYDPEV-SPEELLEAIEDAGYKAR 63
chaper_CopZ_Eh NF033794
copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and ...
381-445 4.92e-13

copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and related species, is a small copper-binding protein with close homology to domains found, sometimes in multiple copies, in various copper-translocating copper-translocating P-type ATPases, and to distinct families of other small copper chaperones that also named CopZ.


Pssm-ID: 411374 [Multi-domain]  Cd Length: 68  Bit Score: 65.43  E-value: 4.92e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 342187274  381 LQIKGMTCASCVSNIERNLQKEAGVLSVLVALMAGKAEIKYDPEVIQPLEIAQFIQDLGFEAAVM 445
Cdd:NF033794    4 FSIKGMSCNHCVARVEKAVNELPGVKKVKVNLKKENGVVKFDETQVTAEKIAQAVNELGYQAEVV 68
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
58-127 6.15e-13

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 64.93  E-value: 6.15e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   58 ATSTVRILGMTCQSCVKSIEDRISNLKGIISMKVSLEQGSATVKYVPSVVCLQQVCHQIGDMGFEASIAE 127
Cdd:COG2608     2 KTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYEVEKAE 71
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
147-207 3.52e-11

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


Pssm-ID: 411375 [Multi-domain]  Cd Length: 66  Bit Score: 59.80  E-value: 3.52e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 342187274  147 LRVEGMTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYLIQPEDLRDHVNDMGFE 207
Cdd:NF033795    4 LNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVEFDESKVTLDQIKEAIEDQGYD 64
chaper_CopZ_Eh NF033794
copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and ...
455-521 6.01e-11

copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and related species, is a small copper-binding protein with close homology to domains found, sometimes in multiple copies, in various copper-translocating copper-translocating P-type ATPases, and to distinct families of other small copper chaperones that also named CopZ.


Pssm-ID: 411374 [Multi-domain]  Cd Length: 68  Bit Score: 59.27  E-value: 6.01e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 342187274  455 IELTITGMTCASCVHNIESKLTRTNGITYASVALATSKALVKFDPEIIGPRDIIKIIEEIGFHASLA 521
Cdd:NF033794    2 QTFSIKGMSCNHCVARVEKAVNELPGVKKVKVNLKKENGVVKFDETQVTAEKIAQAVNELGYQAEVV 68
HMA pfam00403
Heavy-metal-associated domain;
457-513 7.94e-11

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 58.78  E-value: 7.94e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 342187274   457 LTITGMTCASCVHNIESKLTRTNGITYASVALATSKALVKFDPEIIGPRDIIKIIEE 513
Cdd:pfam00403    2 FRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
145-209 7.99e-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 [Multi-domain]  Cd Length: 66  Bit Score: 56.01  E-value: 7.99e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 342187274   145 VKLRVEGMTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYLIQPEDLRDHVNDMGFEAA 209
Cdd:TIGR00003    2 QTFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEVE 66
HMA pfam00403
Heavy-metal-associated domain;
381-437 1.93e-09

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 54.55  E-value: 1.93e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 342187274   381 LQIKGMTCASCVSNIERNLQKEAGVLSVLVALMAGKAEIKYDPEVIQPLEIAQFIQD 437
Cdd:pfam00403    2 FRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
61-122 2.22e-09

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


Pssm-ID: 411375 [Multi-domain]  Cd Length: 66  Bit Score: 54.79  E-value: 2.22e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 342187274   61 TVRILGMTCQSCVKSIEDRISNLKGIISMKVSLEQGSATVKYVPSVVCLQQVCHQIGDMGFE 122
Cdd:NF033795    3 TLNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVEFDESKVTLDQIKEAIEDQGYD 64
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
258-318 7.00e-09

metal-binding (seleno)protein; Known members of this family are selenoproteins with an exceptional UXXU motif, with two selenocysteines. Known members so far derive primarily from MAGs, and have an N-terminal signal peptide N-terminal to the region represented in the seed alignment. Note that this model represents a specific clade of a more widely distributed domain that frequently appears 3 or 4 times in a single protein, so the domain-specific cutoff is critical to identification. Homologous domains, outside the scope of this model, are found in CopZ family copper chaperones and heavy metal-translocating P-type ATPases.


Pssm-ID: 469038 [Multi-domain]  Cd Length: 74  Bit Score: 53.49  E-value: 7.00e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  258 TLQLRIDGMHC---------MISQLEGVQQISVSLAEGTATVLYNPSVISPEELRAAIEDMGFEASVVSE 318
Cdd:NF041115    5 TVILAIEGMTUasupliakkALEGLEGVEKADVSYKEGRAEVAFDPDKVSAAQMVDAVNRIGFRASVIEE 74
HMA pfam00403
Heavy-metal-associated domain;
61-107 1.12e-08

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 52.62  E-value: 1.12e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 342187274    61 TVRILGMTCQSCVKSIEDRISNLKGIISMKVSLEQGSATVKYVPSVV 107
Cdd:pfam00403    1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAEST 47
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
381-443 1.50e-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 [Multi-domain]  Cd Length: 66  Bit Score: 52.54  E-value: 1.50e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 342187274   381 LQIKGMTCASCVSNIERNLQKEAGVLSVLVALMAGKAEIKYDPEVIQPLEIAQFIQDLGFEAA 443
Cdd:TIGR00003    4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEVE 66
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
61-123 4.82e-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 [Multi-domain]  Cd Length: 66  Bit Score: 51.00  E-value: 4.82e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 342187274    61 TVRILGMTCQSCVKSIEDRISNLKGIISMKVSLEQGSATVKYVPSVVCLQQVCHQIGDMGFEA 123
Cdd:TIGR00003    3 TFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEV 65
HMA pfam00403
Heavy-metal-associated domain;
147-198 5.27e-08

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 50.70  E-value: 5.27e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 342187274   147 LRVEGMTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYLIQPEDLR 198
Cdd:pfam00403    2 FRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLV 53
HMA pfam00403
Heavy-metal-associated domain;
261-308 7.36e-08

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 50.31  E-value: 7.36e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 342187274   261 LRIDGMHCM---------ISQLEGVQQISVSLAEGTATVLYNPSVISPEELRAAIED 308
Cdd:pfam00403    2 FRVSGMHCGgcaakvekaLSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
PRK13748 PRK13748
putative mercuric reductase; Provisional
455-539 1.18e-07

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 56.31  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  455 IELTITGMTCASCVHNIESKLTRTNGITYASVALATSKALVKFDPEiIGPRDIIKIIEEIGFHASLAQRNPNAHHLDHKM 534
Cdd:PRK13748    2 TTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVG-TSPDALTAAVAGLGYRATLADAPPTDNRGGLLD 80

                  ....*
gi 342187274  535 EIKQW 539
Cdd:PRK13748   81 KMRGW 85
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
457-520 1.48e-06

metal-binding (seleno)protein; Known members of this family are selenoproteins with an exceptional UXXU motif, with two selenocysteines. Known members so far derive primarily from MAGs, and have an N-terminal signal peptide N-terminal to the region represented in the seed alignment. Note that this model represents a specific clade of a more widely distributed domain that frequently appears 3 or 4 times in a single protein, so the domain-specific cutoff is critical to identification. Homologous domains, outside the scope of this model, are found in CopZ family copper chaperones and heavy metal-translocating P-type ATPases.


Pssm-ID: 469038 [Multi-domain]  Cd Length: 74  Bit Score: 46.94  E-value: 1.48e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187274  457 LTITGMTCASCVHNIESKLTRTNGITYASVALATSKALVKFDPEIIGPRDIIKIIEEIGFHASL 520
Cdd:NF041115    8 LAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDPDKVSAAQMVDAVNRIGFRASV 71
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
455-518 3.04e-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 [Multi-domain]  Cd Length: 66  Bit Score: 45.99  E-value: 3.04e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187274   455 IELTITGMTCASCVHNIESKLTRTNGITYASVALATSKALVKFDPEIIGPRDIIKIIEEIGFHA 518
Cdd:TIGR00003    2 QTFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEV 65
PRK13748 PRK13748
putative mercuric reductase; Provisional
381-444 7.94e-06

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 50.15  E-value: 7.94e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 342187274  381 LQIKGMTCASCVSNIERNLQKEAGVLSVLVALMAGKAEIKYDPEV-IQPLEIAqfIQDLGFEAAV 444
Cdd:PRK13748    4 LKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVGTsPDALTAA--VAGLGYRATL 66
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
381-446 2.41e-05

metal-binding (seleno)protein; Known members of this family are selenoproteins with an exceptional UXXU motif, with two selenocysteines. Known members so far derive primarily from MAGs, and have an N-terminal signal peptide N-terminal to the region represented in the seed alignment. Note that this model represents a specific clade of a more widely distributed domain that frequently appears 3 or 4 times in a single protein, so the domain-specific cutoff is critical to identification. Homologous domains, outside the scope of this model, are found in CopZ family copper chaperones and heavy metal-translocating P-type ATPases.


Pssm-ID: 469038 [Multi-domain]  Cd Length: 74  Bit Score: 43.47  E-value: 2.41e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 342187274  381 LQIKGMTCASCVSNIERNLQKEAGVLSVLVALMAGKAEIKYDPEVIQPLEIAQFIQDLGFEAAVME 446
Cdd:NF041115    8 LAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDPDKVSAAQMVDAVNRIGFRASVIE 73
PRK13748 PRK13748
putative mercuric reductase; Provisional
61-149 1.75e-04

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 45.91  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   61 TVRILGMTCQSCVKSIEDRISNLKGIISMKVSLEQGSATVKYVPSvVCLQQVCHQIGDMGFEASIAE-----------GK 129
Cdd:PRK13748    3 TLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVG-TSPDALTAAVAGLGYRATLADapptdnrggllDK 81
                          90       100
                  ....*....|....*....|
gi 342187274  130 AASWPSRSLPAQEAVVKLRV 149
Cdd:PRK13748   82 MRGWLGGADKHSGNERPLHV 101
PRK13748 PRK13748
putative mercuric reductase; Provisional
261-326 2.21e-04

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 45.53  E-value: 2.21e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 342187274  261 LRIDGMHC---------MISQLEGVQQISVSLAEGTATVLYNPSViSPEELRAAIEDMGFEASVVSESCSTNPLG 326
Cdd:PRK13748    4 LKITGMTCdscaahvkdALEKVPGVQSADVSYPKGSAQLAIEVGT-SPDALTAAVAGLGYRATLADAPPTDNRGG 77
PRK13748 PRK13748
putative mercuric reductase; Provisional
145-210 4.64e-04

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 44.37  E-value: 4.64e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 342187274  145 VKLRVEGMTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYlIQPEDLRDHVNDMGFEAAI 210
Cdd:PRK13748    2 TTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVG-TSPDALTAAVAGLGYRATL 66
 
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 ...
541-1243 0e+00

P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A and ATP7B; The mammalian copper-transporting P-type ATPases, ATP7A and ATP7B are key molecules required for the regulation and maintenance of copper homeostasis. Menkes and Wilson diseases are caused by mutation in ATP7A and ATP7B respectively. This subfamily includes other copper-transporting ATPases such as: Bacillus subtilis CopA , Archeaoglobus fulgidus CopA, and Saccharomyces cerevisiae Ccc2p. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319783 [Multi-domain]  Cd Length: 647  Bit Score: 907.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  541 KSFLCSLVFGIPVMALMIYMlipsnephqsMVLDHNIIPGLSILNLIFFILCTFVQLLGGWYFYVQAYKSLRHRSANMDV 620
Cdd:cd02094     1 RRLILSLLLTLPLLLLMMGG----------MLGPPLPLLLLQLNWWLQFLLATPVQFWGGRPFYRGAWKALKHGSANMDT 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  621 LIVLATSIAYVYSLVILVVAVAEKAErSPVTFFDTPPMLFVFIALGRWLEHLAKSKTSEALAKLMSLQATEATVVTLGEd 700
Cdd:cd02094    71 LVALGTSAAYLYSLVALLFPALFPGG-APHVYFEAAAVIITFILLGKYLEARAKGKTSEAIKKLLGLQPKTARVIRDGK- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  701 nliirEEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMADESLITGEAMPVTKKPGSTVIAGSINAHGSVLIKATHVG 780
Cdd:cd02094   149 -----EVEVPIEEVQVGDIVRVRPGEKIPVDGVVVEGESSVDESMLTGESLPVEKKPGDKVIGGTINGNGSLLVRATRVG 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  781 NDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTLTLVVWIVIGFidfgvvqryfpnpnkhisqtEVIIRFA 860
Cdd:cd02094   224 ADTTLAQIIRLVEEAQGSKAPIQRLADRVSGVFVPVVIAIAILTFLVWLLLGP--------------------EPALTFA 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  861 FQTSITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLLGDVatl 940
Cdd:cd02094   284 LVAAVAVLVIACPCALGLATPTAIMVGTGRAAELGILIKGGEALERAHKVDTVVFDKTGTLTEGKPEVTDVVPLPGD--- 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  941 PLRKVLAVVGTAEASSEHPLGVAVTKYCKEELGteTLGYCTDFQAVPGCGIGCKVSNVEgilahserplsapashlneag 1020
Cdd:cd02094   361 DEDELLRLAASLEQGSEHPLAKAIVAAAKEKGL--ELPEVEDFEAIPGKGVRGTVDGRR--------------------- 417
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1021 slpaekdavpqtfsVLIGNREWLRRNGLTISSDVSDAMtDHEMKGQTAILVAIDGVLCGMIAIADAVKQEAALAVHTLQS 1100
Cdd:cd02094   418 --------------VLVGNRRLMEENGIDLSALEAEAL-ALEEEGKTVVLVAVDGELAGLIAVADPLKPDAAEAIEALKK 482
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1101 MGVDVVLITGDNRKTARAIATQVGINKVFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIGTGTDVA 1180
Cdd:cd02094   483 MGIKVVMLTGDNRRTARAIAKELGIDEVIAEVLPEDKAEKVKKLQAQGKKVAMVGDGINDAPALAQADVGIAIGSGTDVA 562
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187274 1181 IEAADVVLIRNDLLDVVASIHLSKRTVRRIRINLVLALIYNLVGIPIAAGVFMPI-GIVLQPWM 1243
Cdd:cd02094   563 IESADIVLMRGDLRGVVTAIDLSRATMRNIKQNLFWAFIYNVIGIPLAAGVLYPFgGILLSPMI 626
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
455-1244 0e+00

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 848.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  455 IELTITGMTCASCVHNIESKLTRTNGITYASVALATSKALVKFDPEIIGPRDIIKIIEEIGFHASLAQRNPNAHHlDHKM 534
Cdd:COG2217     3 VRLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEKAGYEAEPADADAAAEE-AREK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  535 EIKQWKKSFLCSLVFGIPVMALMIYMLIPSNEPHqsmvldhniipglsilnLIFFILCTFVQLLGGWYFYVQAYKSLRHR 614
Cdd:COG2217    82 ELRDLLRRLAVAGVLALPVMLLSMPEYLGGGLPG-----------------WLSLLLATPVVFYAGWPFFRGAWRALRHR 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  615 SANMDVLIVLATSIAYVYSLVILVVAVAEkaerspvTFFDTPPMLFVFIALGRWLEHLAKSKTSEALAKLMSLQATEATV 694
Cdd:COG2217   145 RLNMDVLVALGTLAAFLYSLYATLFGAGH-------VYFEAAAMIIFLLLLGRYLEARAKGRARAAIRALLSLQPKTARV 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  695 VTLGEdnliirEEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMADESLITGEAMPVTKKPGSTVIAGSINAHGSVLI 774
Cdd:COG2217   218 LRDGE------EVEVPVEELRVGDRVLVRPGERIPVDGVVLEGESSVDESMLTGESLPVEKTPGDEVFAGTINLDGSLRV 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  775 KATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTLTLVVWIVIGFiDFGvvqryfpnpnkhisqte 854
Cdd:COG2217   292 RVTKVGSDTTLARIIRLVEEAQSSKAPIQRLADRIARYFVPAVLAIAALTFLVWLLFGG-DFS----------------- 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  855 viirFAFQTSITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLL 934
Cdd:COG2217   354 ----TALYRAVAVLVIACPCALGLATPTAIMVGTGRAARRGILIKGGEALERLAKVDTVVFDKTGTLTEGKPEVTDVVPL 429
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  935 GDVATlplRKVLAVVGTAEASSEHPLGVAVTKYCKEElGTETLGyCTDFQAVPGCGIGCKVSNVEgilahserplsapas 1014
Cdd:COG2217   430 DGLDE---DELLALAAALEQGSEHPLARAIVAAAKER-GLELPE-VEDFEAIPGKGVEATVDGKR--------------- 489
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1015 hlneagslpaekdavpqtfsVLIGNREWLRRNGLTISSDVSDAMTDHEMKGQTAILVAIDGVLCGMIAIADAVKQEAALA 1094
Cdd:COG2217   490 --------------------VLVGSPRLLEEEGIDLPEALEERAEELEAEGKTVVYVAVDGRLLGLIALADTLRPEAAEA 549
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1095 VHTLQSMGVDVVLITGDNRKTARAIATQVGINKVFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIG 1174
Cdd:COG2217   550 IAALKALGIRVVMLTGDNERTAEAVARELGIDEVRAEVLPEDKAAAVRELQAQGKKVAMVGDGINDAPALAAADVGIAMG 629
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1175 TGTDVAIEAADVVLIRNDLLDVVASIHLSKRTVRRIRINLVLALIYNLVGIPIAAGVFmpigivLQPWMG 1244
Cdd:COG2217   630 SGTDVAIEAADIVLMRDDLRGVPDAIRLSRATMRIIRQNLFWAFGYNVIGIPLAAGGL------LSPWIA 693
ATPase-IB1_Cu TIGR01511
copper-(or silver)-translocating P-type ATPase; This model describes the P-type ATPase ...
599-1244 0e+00

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


Pssm-ID: 273664 [Multi-domain]  Cd Length: 562  Bit Score: 739.47  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   599 GGWYFYVQAYKSLRHRSANMDVLIVLATSIAYVYSLVILVVAVAEKAErSPVTFFDTPPMLFVFIALGRWLEHLAKSKTS 678
Cdd:TIGR01511    1 AGRPFYKSAWKALRHKAPNMDTLIALGTTVAYGYSLVALLANQVLTGL-HVHTFFDASAMLITFILLGRWLEMLAKGRAS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   679 EALAKLMSLQATEATVVTLGEDnliirEEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMADESLITGEAMPVTKKPG 758
Cdd:TIGR01511   80 DALSKLAKLQPSTATLLTKDGS-----IEEVPVALLQPGDIVKVLPGEKIPVDGTVIEGESEVDESLVTGESLPVPKKVG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   759 STVIAGSINAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTLTLVVWIvigfidfgv 838
Cdd:TIGR01511  155 DPVIAGTVNGTGSLVVRATATGEDTTLAQIVRLVRQAQQSKAPIQRLADKVAGYFVPVVIAIALITFVIWL--------- 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   839 vqryfpnpnkhisqteviirFAFQTSITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAHKIKTVMFDKT 918
Cdd:TIGR01511  226 --------------------FALEFAVTVLIIACPCALGLATPTVIAVATGLAAKNGVLIKDGDALERAANIDTVVFDKT 285
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   919 GTITHGVPRVMRVLLLGDVATlplRKVLAVVGTAEASSEHPLGVAVTKYCKEELGTETLgyCTDFQAVPGCGIGCKvsnV 998
Cdd:TIGR01511  286 GTLTQGKPTVTDVHVFGDRDR---TELLALAAALEAGSEHPLAKAIVSYAKEKGITLVT--VSDFKAIPGIGVEGT---V 357
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   999 EGIlahserplsapashlneagslpaekdavpqtfSVLIGNREWLRRNGLtissdvsdAMTDHEMKGQTAILVAIDGVLC 1078
Cdd:TIGR01511  358 EGT--------------------------------KIQLGNEKLLGENAI--------KIDGKAGQGSTVVLVAVNGELA 397
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  1079 GMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGINkVFAEVLPSHKVAKVQELQNKGKKVAMVGDGV 1158
Cdd:TIGR01511  398 GVFALEDQLRPEAKEVIQALKRRGIEPVMLTGDNRKTAKAVAKELGID-VRAEVLPDDKAALIKKLQEKGPVVAMVGDGI 476
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  1159 NDSPALAQADMGVAIGTGTDVAIEAADVVLIRNDLLDVVASIHLSKRTVRRIRINLVLALIYNLVGIPIAAGVFMPIGIV 1238
Cdd:TIGR01511  477 NDAPALAQADVGIAIGAGTDVAIEAADVVLLRNDLNDVATAIDLSRKTLRRIKQNLLWAFGYNVIAIPIAAGVLYPIGIL 556

                   ....*.
gi 342187274  1239 LQPWMG 1244
Cdd:TIGR01511  557 LSPAVA 562
P-type_ATPase_HM cd02079
P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) ...
579-1244 0e+00

P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. These ATPases include mammalian copper-transporting ATPases, ATP7A and ATP7B, Bacillus subtilis CadA which transports cadmium, zinc and cobalt out of the cell, Bacillus subtilis ZosA/PfeT which transports copper, and perhaps also zinc and ferrous iron, Archaeoglobus fulgidus CopA and CopB, Staphylococcus aureus plasmid pI258 CadA, a cadmium-efflux ATPase, and Escherichia coli ZntA which is selective for Pb(2+), Zn(2+), and Cd(2+). The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This family belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319774 [Multi-domain]  Cd Length: 617  Bit Score: 616.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  579 PGLSILNLIFFILCTFVQLLGGWYFYVQAYKSLRHRSANMDVLIVLATSIAYVYSLVILVVavaekaerSPVTFFDTPPM 658
Cdd:cd02079    22 GLVQLLLWVSLLLALPALLYGGRPFLRGAWRSLRRGRLNMDVLVSLAAIGAFVASLLTPLL--------GGIGYFEEAAM 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  659 LFVFIALGRWLEHLAKSKTSEALAKLMSLQATEATVVTLGEdnliirEEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGN 738
Cdd:cd02079    94 LLFLFLLGRYLEERARSRARSALKALLSLAPETATVLEDGS------TEEVPVDDLKVGDVVLVKPGERIPVDGVVVSGE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  739 TMADESLITGEAMPVTKKPGSTVIAGSINAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFII 818
Cdd:cd02079   168 SSVDESSLTGESLPVEKGAGDTVFAGTINLNGPLTIEVTKTGEDTTLAKIIRLVEEAQSSKPPLQRLADRFARYFTPAVL 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  819 IMSTLTLVVWIVIGfidfgvvqryfpnpnkhisqteVIIRFAFQTSITVLCIACPCSLGLATPTAVMVGTGVAAQNGILI 898
Cdd:cd02079   248 VLAALVFLFWPLVG----------------------GPPSLALYRALAVLVVACPCALGLATPTAIVAGIGRAARKGILI 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  899 KGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLLGDVATlplRKVLAVVGTAEASSEHPLGVAVTKYCkEELGTETLG 978
Cdd:cd02079   306 KGGDVLETLAKVDTVAFDKTGTLTEGKPEVTEIEPLEGFSE---DELLALAAALEQHSEHPLARAIVEAA-EEKGLPPLE 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  979 YcTDFQAVPGCGIGCKVSNVEgilahserplsapashlneagslpaekdavpqtfsVLIGNREWLRRNGLtissdVSDAM 1058
Cdd:cd02079   382 V-EDVEEIPGKGISGEVDGRE-----------------------------------VLIGSLSFAEEEGL-----VEAAD 420
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1059 TDHEMKGQTAILVAIDGVLCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGINKVFAEVLPSHKV 1138
Cdd:cd02079   421 ALSDAGKTSAVYVGRDGKLVGLFALEDQLRPEAKEVIAELKSGGIKVVMLTGDNEAAAQAVAKELGIDEVHAGLLPEDKL 500
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1139 AKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIGTGTDVAIEAADVVLIRNDLLDVVASIHLSKRTVRRIRINLVLAL 1218
Cdd:cd02079   501 AIVKALQAEGGPVAMVGDGINDAPALAQADVGIAMGSGTDVAIETADIVLLSNDLSKLPDAIRLARRTRRIIKQNLAWAL 580
                         650       660
                  ....*....|....*....|....*.
gi 342187274 1219 IYNLVGIPIAAGVFMPigivlqPWMG 1244
Cdd:cd02079   581 GYNAIALPLAALGLLT------PWIA 600
ATPase-IB_hvy TIGR01525
heavy metal translocating P-type ATPase; This model encompasses two equivalog models for the ...
618-1237 0e+00

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


Pssm-ID: 273669 [Multi-domain]  Cd Length: 558  Bit Score: 607.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   618 MDVLIVLATSIAYVYSLVILVVavaekaerspvtffdtppMLFVFIALGRWLEHLAKSKTSEALAKLMSLQATEATVVTL 697
Cdd:TIGR01525    1 MDTLMALAAIAAYAMGLVLEGA------------------LLLFLFLLGETLEERAKSRASDALSALLALAPSTARVLQG 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   698 GEDnliirEEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMADESLITGEAMPVTKKPGSTVIAGSINAHGSVLIKAT 777
Cdd:TIGR01525   63 DGS-----EEEVPVEELQVGDIVIVRPGERIPVDGVVISGESEVDESALTGESMPVEKKEGDEVFAGTINGDGSLTIRVT 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   778 HVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTLTLVVWIVIGFidfgvvqryfpnpnkhisqtevII 857
Cdd:TIGR01525  138 KLGEDSTLAQIVELVEEAQSSKAPIQRLADRIASYYVPAVLAIALLTFVVWLALGA----------------------LW 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   858 RFAFQTSITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLLGDV 937
Cdd:TIGR01525  196 REALYRALTVLVVACPCALGLATPVAILVAIGAAARRGILIKGGDALEKLAKVKTVVFDKTGTLTTGKPTVVDIEPLDDA 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   938 ATlplRKVLAVVGTAEASSEHPLGVAVTKYCKEElGTETLGycTDFQAVPGCGIGCKVSNVEgilahserplsapashln 1017
Cdd:TIGR01525  276 SE---EELLALAAALEQSSSHPLARAIVRYAKER-GLELPP--EDVEEVPGKGVEATVDGGR------------------ 331
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  1018 eagslpaekdavpqtfSVLIGNREWL--RRNGLTISSDVSDAMTDHEMKGQTAILVAIDGVLCGMIAIADAVKQEAALAV 1095
Cdd:TIGR01525  332 ----------------EVRIGNPRFLgnRELAIEPISASPDLLNEGESQGKTVVFVAVDGELLGVIALRDQLRPEAKEAI 395
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  1096 HTLQSMGVD-VVLITGDNRKTARAIATQVGIN-KVFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAI 1173
Cdd:TIGR01525  396 AALKRAGGIkLVMLTGDNRSAAEAVAAELGIDdEVHAELLPEDKLAIVKKLQEEGGPVAMVGDGINDAPALAAADVGIAM 475
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187274  1174 GTGTDVAIEAADVVLIRNDLLDVVASIHLSKRTVRRIRINLVLALIYNLVGIPIAAGVFMPIGI 1237
Cdd:TIGR01525  476 GSGSDVAIEAADIVLLNDDLRSLPTAIDLSRKTRRIIKQNLAWALGYNLVAIPLAAGGLLPLWL 539
P-type_ATPase_Cu-like cd07552
P-type heavy metal-transporting ATPase, similar to Archaeoglobus fulgidus CopB, a Cu(2+) ...
546-1244 9.42e-165

P-type heavy metal-transporting ATPase, similar to Archaeoglobus fulgidus CopB, a Cu(2+)-ATPase; Archaeoglobus fulgidus CopB transports Cu(2+) from the cytoplasm to the exterior of the cell using ATP as energy source, it transports preferentially Cu(2+) over Cu(+), it is activated by Cu(2+) with high affinity and partially by Cu(+) and Ag(+). This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319850 [Multi-domain]  Cd Length: 632  Bit Score: 507.23  E-value: 9.42e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  546 SLVFGIPVMAL--MIYMLIPsnephqsmvldhnIIPGLSILNLIFFILCTFVQLLGGWYFYVQAYKSLRHRSANMDVLIV 623
Cdd:cd07552     1 SLILTIPILLLspMMGTLLP-------------FQVSFPGSDWVVLILATILFFYGGKPFLKGAKDELKSKKPGMMTLIA 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  624 LATSIAYVYSlvilVVAVAEKAERSPVT-FFDTPPMLFVFIALGRWLEHLAKSKTSEALAKLMSLQATEATVVTLGEdnl 702
Cdd:cd07552    68 LGITVAYVYS----VYAFLGNYFGEHGMdFFWELATLIVIMLLGHWIEMKAVMGAGDALKKLAELLPKTAHLVTDGS--- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  703 iirEEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMADESLITGEAMPVTKKPGSTVIAGSINAHGSVLIKATHVGND 782
Cdd:cd07552   141 ---IEDVPVSELKVGDVVLVRAGEKIPADGTILEGESSVNESMVTGESKPVEKKPGDEVIGGSVNGNGTLEVKVTKTGED 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  783 TTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTLTLVVWIVIGfiDFGvvqryfpnpnkhisqteviirFAFQ 862
Cdd:cd07552   218 SYLSQVMELVAQAQASKSRAENLADKVAGWLFYIALGVGIIAFIIWLILG--DLA---------------------FALE 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  863 TSITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLLGDVATlpl 942
Cdd:cd07552   275 RAVTVLVIACPHALGLAIPLVVARSTSIAAKNGLLIRNREALERARDIDVVLFDKTGTLTEGKFGVTDVITFDEYDE--- 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  943 RKVLAVVGTAEASSEHPLGVAVTKYCKEELgtETLGYCTDFQAVPGCGIGCKVSNVEgilahserplsapashlneagsl 1022
Cdd:cd07552   352 DEILSLAAALEAGSEHPLAQAIVSAAKEKG--IRPVEVENFENIPGVGVEGTVNGKR----------------------- 406
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1023 paekdavpqtfsVLIGNREWLRRNGLTISSDVSDAMTDHemkGQTAILVAIDGVLCGMIAIADAVKQEAALAVHTLQSMG 1102
Cdd:cd07552   407 ------------YQVVSPKYLKELGLKYDEELVKRLAQQ---GNTVSFLIQDGEVIGAIALGDEIKPESKEAIRALKAQG 471
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1103 VDVVLITGDNRKTARAIATQVGINKVFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIGTGTDVAIE 1182
Cdd:cd07552   472 ITPVMLTGDNEEVAQAVAEELGIDEYFAEVLPEDKAKKVKELQAEGKKVAMVGDGVNDAPALAQADVGIAIGAGTDVAIE 551
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 342187274 1183 AADVVLIRNDLLDVVASIHLSKRTVRRIRINLVLALIYNLVGIPIAAGVFMPIGIVLQPWMG 1244
Cdd:cd07552   552 SADVVLVKSDPRDIVDFLELAKATYRKMKQNLWWGAGYNVIAIPLAAGVLAPIGIILSPAVG 613
copA PRK10671
copper-exporting P-type ATPase CopA;
376-1241 1.38e-155

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 490.02  E-value: 1.38e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  376 PQKCFLQIKGMTCASCVSNIERNLQKEAGVLSVLV--------------ALMAGKAEIKYDPEV----IQPLEIAQfIQD 437
Cdd:PRK10671    2 SQTIDLTLDGLSCGHCVKRVKESLEQRPDVEQADVsiteahvtgtasaeALIETIKQAGYDASVshpkAKPLTESS-IPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  438 LGFEAAVME---DYAGSDGNIELTITGMTCASCVHNIESKLTRTNGITYASVALATSKALVKFDPEiigPRDIIKIIEEI 514
Cdd:PRK10671   81 EALTAASEElpaATADDDDSQQLLLSGMSCASCVSRVQNALQSVPGVTQARVNLAERTALVMGSAS---PQDLVQAVEKA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  515 GFHASL----AQRNPNAHHLDHK-MEIKQWKKSFlcSLVFGIPVMalmIYMLIPSNephqSMVLDHNIIPGLSIlnlifF 589
Cdd:PRK10671  158 GYGAEAieddAKRRERQQETAQAtMKRFRWQAIV--ALAVGIPVM---VWGMIGDN----MMVTADNRSLWLVI-----G 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  590 ILCTFVQLLGGWYFYVQAYKSLRHRSANMDVLIVLATSIAYVYSL-VILVVAVAEKAERSpvTFFDTPPMLFVFIALGRW 668
Cdd:PRK10671  224 LITLAVMVFAGGHFYRSAWKSLLNGSATMDTLVALGTGAAWLYSMsVNLWPQWFPMEARH--LYYEASAMIIGLINLGHM 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  669 LEHLAKSKTSEALAKLMSLQATEATVVTlgEDNliirEEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMADESLITG 748
Cdd:PRK10671  302 LEARARQRSSKALEKLLDLTPPTARVVT--DEG----EKSVPLADVQPGMLLRLTTGDRVPVDGEITQGEAWLDEAMLTG 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  749 EAMPVTKKPGSTVIAGSINAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTLTLVVW 828
Cdd:PRK10671  376 EPIPQQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAVFVPVVVVIALVSAAIW 455
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  829 ivigfidfgvvqrYFPNPNKHISQTEVIIrfafqtsITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAH 908
Cdd:PRK10671  456 -------------YFFGPAPQIVYTLVIA-------TTVLIIACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRAS 515
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  909 KIKTVMFDKTGTITHGVPRVMRVLLLGDVATlplRKVLAVVGTAEASSEHPLGVAVTkyckEELGTETLGYCTDFQAVPG 988
Cdd:PRK10671  516 TLDTLVFDKTGTLTEGKPQVVAVKTFNGVDE---AQALRLAAALEQGSSHPLARAIL----DKAGDMTLPQVNGFRTLRG 588
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  989 CGIGCKVSNVEgilahserplsapashlneagslpaekdavpqtfsVLIGNREWLRRNGLTiSSDVSDAMTDHEMKGQTA 1068
Cdd:PRK10671  589 LGVSGEAEGHA-----------------------------------LLLGNQALLNEQQVD-TKALEAEITAQASQGATP 632
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1069 ILVAIDGVLCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGINKVFAEVLPSHKVAKVQELQNKG 1148
Cdd:PRK10671  633 VLLAVDGKAAALLAIRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVLPDGKAEAIKRLQSQG 712
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1149 KKVAMVGDGVNDSPALAQADMGVAIGTGTDVAIEAADVVLIRNDLLDVVASIHLSKRTVRRIRINLVLALIYNLVGIPIA 1228
Cdd:PRK10671  713 RQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRATLRNMKQNLLGAFIYNSLGIPIA 792
                         890
                  ....*....|....
gi 342187274 1229 AGVFMPI-GIVLQP 1241
Cdd:PRK10671  793 AGILWPFtGTLLNP 806
ATPase-IB2_Cd TIGR01512
heavy metal-(Cd/Co/Hg/Pb/Zn)-translocating P-type ATPase; This model describes the P-type ...
658-1235 1.23e-143

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


Pssm-ID: 273665 [Multi-domain]  Cd Length: 550  Bit Score: 448.70  E-value: 1.23e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   658 MLFVFIALGRWLEHLAKSKTSEALAKLMSLQATEATVVTLGEdnliirEEQVPMELVQRGDIVKVVPGGKFPVDGKVLEG 737
Cdd:TIGR01512   23 LLLLLFSIGETLEEYASGRARRALKALMELAPDTARRLQGDS------LEEVAVEELKVGDVVVVKPGERVPVDGEVLSG 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   738 NTMADESLITGEAMPVTKKPGSTVIAGSINAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFI 817
Cdd:TIGR01512   97 TSSVDESALTGESVPVEKAPGDEVFAGAINLDGVLTIEVTKLPADSTIAKIVNLVEEAQSRKAPTQRFIDRFARYYTPAV 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   818 IImstLTLVVWIVIGFIdfgvvqryFPNPNKHisqteviirfAFQTSITVLCIACPCSLGLATPTAVMVGTGVAAQNGIL 897
Cdd:TIGR01512  177 LA---IALAAALVPPLL--------GAGPFLE----------WIYRALVLLVVASPCALVISAPAAYLSAISAAARHGIL 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   898 IKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLLGDVAtlpLRKVLAVVGTAEASSEHPLGVAVTKYCKEelgTETL 977
Cdd:TIGR01512  236 IKGGAALEALAKIKTVAFDKTGTLTTGKPKVTDVHPADGHS---ESEVLRLAAAAEQGSTHPLARAIVDYARA---RELA 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   978 GYCTDFQAVPGCGIGCKVSNVEgilahserplsapashlneagslpaekdavpqtfsVLIGNREWLRRngltissDVSDA 1057
Cdd:TIGR01512  310 PPVEDVEEVPGEGVRAVVDGGE-----------------------------------VRIGNPRSLSE-------AVGAS 347
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  1058 MTDHEMKGQTAILVAIDGVLCGMIAIADAVKQEAALAVHTLQSMGVD-VVLITGDNRKTARAIATQVGINKVFAEVLPSH 1136
Cdd:TIGR01512  348 IAVPESAGKTIVLVARDGTLLGYIALSDELRPDAAEAIAELKALGIKrLVMLTGDRRAVAEAVARELGIDEVHAELLPED 427
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  1137 KVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIGT-GTDVAIEAADVVLIRNDLLDVVASIHLSKRTVRRIRINLV 1215
Cdd:TIGR01512  428 KLEIVKELREKAGPVAMVGDGINDAPALAAADVGIAMGAsGSDVALETADVVLLNDDLSRLPQAIRLARRTRRIIKQNVV 507
                          570       580
                   ....*....|....*....|
gi 342187274  1216 LALIYNLVGIPIAAGVFMPI 1235
Cdd:TIGR01512  508 IALGIILVLILLALFGVLPL 527
P-type_ATPase_HM_ZosA_PfeT-like cd07551
P-type heavy metal-transporting ATPase, similar to Bacillus subtilis ZosA/PfeT which ...
584-1231 6.43e-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 [Multi-domain]  Cd Length: 611  Bit Score: 432.83  E-value: 6.43e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  584 LNLIFFILCTfvqLLGGWYFYVQAYKS-LRHRSANMDVLIVLATSIAyvyslvILVVAVAEKAerspvtffdtppMLFVF 662
Cdd:cd07551    26 VPWALFLLAY---LIGGYASAKEGIEAtLRKKTLNVDLLMILAAIGA------AAIGYWAEGA------------LLIFI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  663 IALGRWLEHLAKSKTSEALAKLMSLQATEATVVTLGEDnliirEEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMAD 742
Cdd:cd07551    85 FSLSHALEDYAMGRSKRAITALMQLAPETARRIQRDGE-----IEEVPVEELQIGDRVQVRPGERVPADGVILSGSSSID 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  743 ESLITGEAMPVTKKPGSTVIAGSINAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMST 822
Cdd:cd07551   160 EASITGESIPVEKTPGDEVFAGTINGSGALTVRVTKLSSDTVFAKIVQLVEEAQSEKSPTQSFIERFERIYVKGVLLAVL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  823 LTLVVWIVIGFIDFgvvqryfpnpnkhisqTEVIIRfafqtSITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGK 902
Cdd:cd07551   240 LLLLLPPFLLGWTW----------------ADSFYR-----AMVFLVVASPCALVASTPPATLSAIANAARQGVLFKGGV 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  903 PLEMAHKIKTVMFDKTGTITHGVPRVMRVLLLGDVATlplRKVLAVVGTAEASSEHPLGVAVTKYCkEELGTETLGYcTD 982
Cdd:cd07551   299 HLENLGSVKAIAFDKTGTLTEGKPRVTDVIPAEGVDE---EELLQVAAAAESQSEHPLAQAIVRYA-EERGIPRLPA-IE 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  983 FQAVPGCGIgckVSNVEGIlahserplsapashlneagslpaekdavpqtfSVLIGNREWLRRNGltISSDVSDAMTDHE 1062
Cdd:cd07551   374 VEAVTGKGV---TATVDGQ--------------------------------TYRIGKPGFFGEVG--IPSEAAALAAELE 416
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1063 MKGQTAILVAIDGVLCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGINKVFAEVLPSHKVAKVQ 1142
Cdd:cd07551   417 SEGKTVVYVARDDQVVGLIALMDTPRPEAKEAIAALRLGGIKTIMLTGDNERTAEAVAKELGIDEVVANLLPEDKVAIIR 496
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1143 ELQNKGKKVAMVGDGVNDSPALAQADMGVAIGTGTDVAIEAADVVLIRNDLLDVVASIHLSKRTVRRIRINLVLAL---- 1218
Cdd:cd07551   497 ELQQEYGTVAMVGDGINDAPALANADVGIAMGAGTDVALETADVVLMKDDLSKLPYAIRLSRKMRRIIKQNLIFALavia 576
                         650
                  ....*....|....*..
gi 342187274 1219 ---IYNLVG-IPIAAGV 1231
Cdd:cd07551   577 lliVANLFGlLNLPLGV 593
P-type_ATPase_Cd-like cd07545
P-type heavy metal-transporting ATPase, similar to Staphylococcus aureus plasmid pI258 CadA, a ...
597-1228 1.13e-123

P-type heavy metal-transporting ATPase, similar to Staphylococcus aureus plasmid pI258 CadA, a cadmium-efflux ATPase; CadA from gram-positive Staphylococcus aureus plasmid pI258 is required for full Cd(2+) and Zn(2+) resistance. This subfamily also includes CadA, from the gram-negative bacilli, Stenotrophomonas maltophilia D457R, which is a cadmium efflux pump acquired as part of a cluster of antibiotic and heavy metal resistance genes from gram-positive bacteria. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319845 [Multi-domain]  Cd Length: 599  Bit Score: 396.79  E-value: 1.13e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  597 LLGGWYFYVQAYKSLRHRSANMDVLIVLAtsiayvyslVILVVAVAEKAERSPVTFfdtppmLFvfiALGRWLEHLAKSK 676
Cdd:cd07545    21 VLGGYGLFKKGWRNLIRRNFDMKTLMTIA---------VIGAALIGEWPEAAMVVF------LF---AISEALEAYSMDR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  677 TSEALAKLMSLQATEATVVTLGednliiREEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMADESLITGEAMPVTKK 756
Cdd:cd07545    83 ARRSIRSLMDIAPKTALVRRDG------QEREVPVAEVAVGDRMIVRPGERIAMDGIIVRGESSVNQAAITGESLPVEKG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  757 PGSTVIAGSINAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTLTLVVW-IVIGFID 835
Cdd:cd07545   157 VGDEVFAGTLNGEGALEVRVTKPAEDSTIARIIHLVEEAQAERAPTQAFVDRFARYYTPVVMAIAALVAIVPpLFFGGAW 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  836 FGVVQRyfpnpnkhisqteviirfafqtSITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAHKIKTVMF 915
Cdd:cd07545   237 FTWIYR----------------------GLALLVVACPCALVISTPVSIVSAIGNAARKGVLIKGGVYLEELGRLKTVAF 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  916 DKTGTITHGVPRVMRVLLLGDVATlplRKVLAVVGTAEASSEHPLGVAVTKYCKEElgTETLGYCTDFQAVPGCGigckv 995
Cdd:cd07545   295 DKTGTLTKGKPVVTDVVVLGGQTE---KELLAIAAALEYRSEHPLASAIVKKAEQR--GLTLSAVEEFTALTGRG----- 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  996 snVEGILAHSErplsapashlneagslpaekdavpqtfsVLIGNREWLRRNGLTISSDVSDAMTDHEMKGQTAILVAIDG 1075
Cdd:cd07545   365 --VRGVVNGTT----------------------------YYIGSPRLFEELNLSESPALEAKLDALQNQGKTVMILGDGE 414
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1076 VLCGMIAIADAVKQEAALAVHTL-QSMGVDVVLITGDNRKTARAIATQVGINKVFAEVLPSHKVAKVQELQNKGKKVAMV 1154
Cdd:cd07545   415 RILGVIAVADQVRPSSRNAIAALhQLGIKQTVMLTGDNPQTAQAIAAQVGVSDIRAELLPQDKLDAIEALQAEGGRVAMV 494
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 342187274 1155 GDGVNDSPALAQADMGVAIG-TGTDVAIEAADVVLIRNDLLDVVASIHLSKRTVRRIRINLVLALIYNLVGIPIA 1228
Cdd:cd07545   495 GDGVNDAPALAAADVGIAMGaAGTDTALETADIALMGDDLRKLPFAVRLSRKTLAIIKQNIAFALGIKLIALLLV 569
P-type_ATPase_HM cd07550
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
606-1232 6.43e-117

P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily of the heavy metal-transporting ATPases (Type IB ATPases) which transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319848 [Multi-domain]  Cd Length: 592  Bit Score: 378.54  E-value: 6.43e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  606 QAYKSLRHRSANMDVLIVLATSIAYvyslvilvvavAEKAERSPVTffdtppMLFVfIALGRWLEHLAKSKTSEALAKLM 685
Cdd:cd07550    34 RALESLKERRLNVDVLDSLAVLLSL-----------LTGDYLAANT------IAFL-LELGELLEDYTARKSEKALLDLL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  686 SLQATEATVVTLGednliiREEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMADESLITGEAMPVTKKPGSTVIAGS 765
Cdd:cd07550    96 SPQERTVWVERDG------VEVEVPADEVQPGDTVVVGAGDVIPVDGTVLSGEALIDQASLTGESLPVEKREGDLVFAST 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  766 INAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTLtlvVWIVIGfidfgvvqryfpN 845
Cdd:cd07550   170 VVEEGQLVIRAERVGRETRAARIAELIEQSPSLKARIQNYAERLADRLVPPTLGLAGL---VYALTG------------D 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  846 PNKHISqteviirfafqtsitVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAHKIKTVMFDKTGTITHGV 925
Cdd:cd07550   235 ISRAAA---------------VLLVDFSCGIRLSTPVAVLSALNHAARHGILVKGGRALELLAKVDTVVFDKTGTLTEGE 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  926 PRVMRVLLLGDvaTLPLRKVLAVVGTAEASSEHPLGVAVTKYCKEElGTEtLGYCTDFQAVPGCGIgckvsnvegilahs 1005
Cdd:cd07550   300 PEVTAIITFDG--RLSEEDLLYLAASAEEHFPHPVARAIVREAEER-GIE-HPEHEEVEYIVGHGI-------------- 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1006 erplsapASHLNEAgslpaekdavpqtfSVLIGNREWLRRNGLTISSDVSDAMTDHEMKGQTAILVAIDGVLCGMIAIAD 1085
Cdd:cd07550   362 -------ASTVDGK--------------RIRVGSRHFMEEEEIILIPEVDELIEDLHAEGKSLLYVAIDGRLIGVIGLSD 420
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1086 AVKQEAALAVHTL-QSMGVDVVLITGDNRKTARAIATQVGINKVFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPAL 1164
Cdd:cd07550   421 PLRPEAAEVIARLrALGGKRIIMLTGDHEQRARALAEQLGIDRYHAEALPEDKAEIVEKLQAEGRTVAFVGDGINDSPAL 500
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 342187274 1165 AQADMGVAIGTGTDVAIEAADVVLIRNDLLDVVASIHLSKRTVRRIRINLVLALIYNLvgIPIAAGVF 1232
Cdd:cd07550   501 SYADVGISMRGGTDIARETADVVLLEDDLRGLAEAIELARETMALIKRNIALVVGPNT--AVLAGGVF 566
P-type_ATPase_Pb_Zn_Cd2-like cd07546
P-type heavy metal-transporting ATPase, similar to Escherichia coli ZntA which is selective ...
587-1218 3.28e-109

P-type heavy metal-transporting ATPase, similar to Escherichia coli ZntA which is selective for Pb(2+), Zn(2+), and Cd(2+); Escherichia coli ZntA mediates resistance to toxic levels of selected divalent metal ions. ZntA has the highest selectivity for Pb(2+), followed by Zn(2+) and Cd(2+); it also shows low levels of activity with Cu(2+), Ni(2+), and Co(2+). It is upregulated by the transcription factor ZntR at high zinc concentrations. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319846 [Multi-domain]  Cd Length: 597  Bit Score: 357.48  E-value: 3.28e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  587 IFFILCTfvqLLGGWYFYVQAYKSLRHRSA-NMDVLIVLATsiayvyslvILVVAVAEKAERSPVTFfdtppmLFvfiAL 665
Cdd:cd07546    16 WAFIAAT---LVGLFPIARKAFRLARSGSPfSIETLMTVAA---------IGALFIGATAEAAMVLL------LF---LV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  666 GRWLEHLAKSKTSEALAKLMSLQATEATVVTLGEdnliirEEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMADESL 745
Cdd:cd07546    75 GELLEGYAASRARSGVKALMALVPETALREENGE------RREVPADSLRPGDVIEVAPGGRLPADGELLSGFASFDESA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  746 ITGEAMPVTKKPGSTVIAGSINAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTLTL 825
Cdd:cd07546   149 LTGESIPVEKAAGDKVFAGSINVDGVLRIRVTSAPGDNAIDRILHLIEEAEERRAPIERFIDRFSRWYTPAIMAVALLVI 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  826 VV-----------WIVIGfidfgvvqryfpnpnkhisqteviirfafqtsITVLCIACPCSLGLATPTAVMVGTGVAAQN 894
Cdd:cd07546   229 VVppllfgadwqtWIYRG--------------------------------LALLLIGCPCALVISTPAAITSGLAAAARR 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  895 GILIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLLGDVATlplRKVLAVVGTAEASSEHPLGVAVTKYCKEELGT 974
Cdd:cd07546   277 GALIKGGAALEQLGRVTTVAFDKTGTLTRGKPVVTDVVPLTGISE---AELLALAAAVEMGSSHPLAQAIVARAQAAGLT 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  975 ETLGycTDFQAVPGCGIGckvSNVEGilahsERPLSAPASHLNEAGSLpaekdAVPQTFSVLignrewlrrngltissdv 1054
Cdd:cd07546   354 IPPA--EEARALVGRGIE---GQVDG-----ERVLIGAPKFAADRGTL-----EVQGRIAAL------------------ 400
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1055 sdamtdhEMKGQTAILVAIDGVLCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGINkVFAEVLP 1134
Cdd:cd07546   401 -------EQAGKTVVVVLANGRVLGLIALRDELRPDAAEAVAELNALGIKALMLTGDNPRAAAAIAAELGLD-FRAGLLP 472
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1135 SHKVAKVQELQNKGKkVAMVGDGVNDSPALAQADMGVAIGTGTDVAIEAADVVLIRNDLLDVVASIHLSKRTVRRIRINL 1214
Cdd:cd07546   473 EDKVKAVRELAQHGP-VAMVGDGINDAPAMKAASIGIAMGSGTDVALETADAALTHNRLGGVAAMIELSRATLANIRQNI 551

                  ....
gi 342187274 1215 VLAL 1218
Cdd:cd07546   552 TIAL 555
P-type_ATPase_FixI-like cd02092
Rhizobium meliloti FixI and related proteins; belongs to P-type heavy metal-transporting ...
600-1235 2.17e-105

Rhizobium meliloti FixI and related proteins; belongs to P-type heavy metal-transporting ATPase subfamily; FixI may be a pump of a specific cation involved in symbiotic nitrogen fixation. The Rhizobium fixI gene is part of an operon conserved among rhizobia, fixGHIS. FixG, FixH, FixI, and FixS may participate in a membrane-bound complex coupling the FixI cation pump with a redox process catalyzed by FixG, an iron-sulfur protein. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319782 [Multi-domain]  Cd Length: 605  Bit Score: 347.42  E-value: 2.17e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  600 GWYFYVQAYKSLRHRSANMDVLIVLATSIAYVYSLViLVVAVAEKAerspvtFFDTPPMLFVFIALGRWLEHLAKSKTSE 679
Cdd:cd02092    43 GRPFFRSAWAALRHGRTNMDVPISIGVLLATGMSLF-ETLHGGEHA------YFDAAVMLLFFLLIGRYLDHRMRGRARS 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  680 ALAKLMSLQATEATVVTLGEdnliiREEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMADESLITGEAMPVTKKPGS 759
Cdd:cd02092   116 AAEELAALEARGAQRLQADG-----SREYVPVAEIRPGDRVLVAAGERIPVDGTVVSGTSELDRSLLTGESAPVTVAPGD 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  760 TVIAGSINAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTLTLVVWIVIGfIDfgvv 839
Cdd:cd02092   191 LVQAGAMNLSGPLRLRATAAGDDTLLAEIARLMEAAEQGRSRYVRLADRAARLYAPVVHLLALLTFVGWVAAG-GD---- 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  840 qryfpnpnkhisqteviIRFAFQTSITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAHKIKTVMFDKTG 919
Cdd:cd02092   266 -----------------WRHALLIAVAVLIITCPCALGLAVPAVQVVASGRLFRRGVLVKDGTALERLAEVDTVVFDKTG 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  920 TITHGVPRVMRvlllgdvATLPLRKVLAVVGTAEASSEHPLGVAVTKyckeELGTETLGYcTDFQAVPGCGIgckVSNVE 999
Cdd:cd02092   329 TLTLGSPRLVG-------AHAISADLLALAAALAQASRHPLSRALAA----AAGARPVEL-DDAREVPGRGV---EGRID 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1000 GILAHSERPLSAPAShlneagslpaekdAVPQTFSVLignreWLRRNgltissdvsdamtdhemkGQTAILVAIDgvlcg 1079
Cdd:cd02092   394 GARVRLGRPAWLGAS-------------AGVSTASEL-----ALSKG------------------GEEAARFPFE----- 432
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1080 miaiaDAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGINKVFAEVLPSHKVAKVQELQNKGKKVAMVGDGVN 1159
Cdd:cd02092   433 -----DRPRPDAREAISALRALGLSVEILSGDREPAVRALARALGIEDWRAGLTPAEKVARIEELKAQGRRVLMVGDGLN 507
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 342187274 1160 DSPALAQADMGVAIGTGTDVAIEAADVVLIRNDLLDVVASIHLSKRTVRRIRINLVLALIYNLVGIPIA-AGVFMPI 1235
Cdd:cd02092   508 DAPALAAAHVSMAPASAVDASRSAADIVFLGDSLAPVPEAIEIARRARRLIRQNFALAIGYNVIAVPLAiAGYVTPL 584
P-type_ATPase-Cd_Zn_Co_like cd07548
P-type heavy metal-transporting ATPase, similar to Bacillus subtilis CadA which appears to ...
658-1218 8.62e-104

P-type heavy metal-transporting ATPase, similar to Bacillus subtilis CadA which appears to transport cadmium, zinc and cobalt but not copper out of the cell; Bacillus subtilis CadA/YvgW appears to transport cadmium, zinc and cobalt but not copper, out of the cell. Functions in metal ion resistance and cellular metal ion homeostasis. CadA/YvgW is also important for sporulation in B. subtilis, the significant specific expression of the cadA/yvgW gene during the late stage of sporulation, is controlled by forespore-specific sigma factor, sigma G, and mother cell-specific sigma factor, sigma E. This subfamily also includes Helicobacter pylori CadA an essential resistance pump with ion specificity towards Cd(2+), Zn(2+) and Co(2+), and Zn-transporting ATPase, ZiaA(N) in Synechocystis PCC 6803. Transcription of ziaA is induced by Zn under the control of the Zn responsive repressor ZiaR. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319847 [Multi-domain]  Cd Length: 604  Bit Score: 343.06  E-value: 8.62e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  658 MLFVfiALGRWLEHLAKSKTSEALAKLMSLQATEATVVTLGEdnliirEEQVPMELVQRGDIVKVVPGGKFPVDGKVLEG 737
Cdd:cd07548    79 MLFY--EVGELFQDLAVERSRKSIKALLDIRPDYANLKRNNE------LKDVKPEEVQIGDIIVVKPGEKIPLDGVVLKG 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  738 NTMADESLITGEAMPVTKKPGSTVIAGSINAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFI 817
Cdd:cd07548   151 ESFLDTSALTGESVPVEVKEGSSVLAGFINLNGVLEIKVTKPFKDSAVAKILELVENASARKAPTEKFITKFARYYTPIV 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  818 IIMSTL-TLVVWIVIGFIDFGV-VQRyfpnpnkhisqteviirfafqtSITVLCIACPCSLGLATPTAVMVGTGVAAQNG 895
Cdd:cd07548   231 VFLALLlAVIPPLFSPDGSFSDwIYR----------------------ALVFLVISCPCALVISIPLGYFGGIGAASRKG 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  896 ILIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLLGDVATlplRKVLAVVGTAEASSEHPLGVAVTKYCKEELGTE 975
Cdd:cd07548   289 ILIKGSNYLEALSQVKTVVFDKTGTLTKGVFKVTEIVPAPGFSK---EELLKLAALAESNSNHPIARSIQKAYGKMIDPS 365
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  976 TLgycTDFQAVPGCGIgckvsnvegilahserplsapashlneagslpaekDAVPQTFSVLIGNREWLRRNGltISSDVS 1055
Cdd:cd07548   366 EI---EDYEEIAGHGI-----------------------------------RAVVDGKEILVGNEKLMEKFN--IEHDED 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1056 DamTDHemkgqTAILVAIDGVLCGMIAIADAVKQEAALAVHTLQSMGVD-VVLITGDNRKTARAIATQVGINKVFAEVLP 1134
Cdd:cd07548   406 E--IEG-----TIVHVALDGKYVGYIVISDEIKEDAKEAIKGLKELGIKnLVMLTGDRKSVAEKVAKKLGIDEVYAELLP 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1135 SHKVAKVQELQNKGK-KVAMVGDGVNDSPALAQADMGVAIGT-GTDVAIEAADVVLIRNDLLDVVASIHLSKRTVRRIRI 1212
Cdd:cd07548   479 EDKVEKVEELKAESKgKVAFVGDGINDAPVLARADVGIAMGGlGSDAAIEAADVVLMNDEPSKVAEAIKIARKTRRIVWQ 558

                  ....*.
gi 342187274 1213 NLVLAL 1218
Cdd:cd07548   559 NIILAL 564
ATPase_P-type TIGR01494
ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large ...
658-1232 8.69e-104

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


Pssm-ID: 273656 [Multi-domain]  Cd Length: 545  Bit Score: 340.83  E-value: 8.69e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   658 MLFVFIALgrwlEHLAKSKTSEALAKLMSLQATEATVVtlgednlIIRE--EQVPMELVQRGDIVKVVPGGKFPVDGKVL 735
Cdd:TIGR01494    5 LVLLFVLL----EVKQKLKAEDALRSLKDSLVNTATVL-------VLRNgwKEISSKDLVPGDVVLVKSGDTVPADGVLL 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   736 EGNTMADESLITGEAMPVTKKPGST---VIAGSINAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSG- 811
Cdd:TIGR01494   74 SGSAFVDESSLTGESLPVLKTALPDgdaVFAGTINFGGTLIVKVTATGILTTVGKIAVVVYTGFSTKTPLQSKADKFENf 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   812 YFVPFIIIMSTLTLVVWIVIGfidfgvvqryfpnpnkhisQTEVIIRFAFQTSITVLCIACPCSLGLATPTAVMVGTGVA 891
Cdd:TIGR01494  154 IFILFLLLLALAVFLLLPIGG-------------------WDGNSIYKAILRALAVLVIAIPCALPLAVSVALAVGDARM 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   892 AQNGILIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLLGDVATlPLRKVLAVVGTAEASSEHPLGVAVTKYckee 971
Cdd:TIGR01494  215 AKKGILVKNLNALEELGKVDVICFDKTGTLTTNKMTLQKVIIIGGVEE-ASLALALLAASLEYLSGHPLERAIVKS---- 289
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   972 lgTETLGYCTdfqavpgcGIGCKVSNVEGILAHSERPLSAPASHLNEAGSLPAEKDAvPQTFSVLIGNREWLRRNGLTIS 1051
Cdd:TIGR01494  290 --AEGVIKSD--------EINVEYKILDVFPFSSVLKRMGVIVEGANGSDLLFVKGA-PEFVLERCNNENDYDEKVDEYA 358
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  1052 SDvsdamtdhemkGQTAILVAIDGV-----LCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGIn 1126
Cdd:TIGR01494  359 RQ-----------GLRVLAFASKKLpddleFLGLLTFEDPLRPDAKETIEALRKAGIKVVMLTGDNVLTAKAIAKELGI- 426
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  1127 KVFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIGtGTDVAIEAADVVLIRNDLLDVVASIHLSKRT 1206
Cdd:TIGR01494  427 DVFARVKPEEKAAIVEALQEKGRTVAMTGDGVNDAPALKKADVGIAMG-SGDVAKAAADIVLLDDDLSTIVEAVKEGRKT 505
                          570       580
                   ....*....|....*....|....*.
gi 342187274  1207 VRRIRINLVLALIYNLVGIPIAAGVF 1232
Cdd:TIGR01494  506 FSNIKKNIFWAIAYNLILIPLALLLI 531
P-type_ATPase_HM cd07544
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
577-1240 1.05e-103

P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily of the heavy metal-transporting ATPases (Type IB ATPases) which transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319844 [Multi-domain]  Cd Length: 596  Bit Score: 342.38  E-value: 1.05e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  577 IIPGLSILNLIFFILCTFVQLLGGWYFYVQAY----KSLRHRSANMDVLIVLA--TSIA---YVYSLVILVvavaekaer 647
Cdd:cd07544    11 VIALILCFGLHQPLLAAWIVLIGGVVIALSLLwemiKTLRRGRYGVDLLAILAivATLLvgeYWASLIILL--------- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  648 spvtffdtppMLfvfiALGRWLEHLAKSKTSEALAKLMSLQATEATVVTLGEdnliirEEQVPMELVQRGDIVKVVPGGK 727
Cdd:cd07544    82 ----------ML----TGGEALEDYAQRRASRELTALLDRAPRIAHRLVGGQ------LEEVPVEEVTVGDRLLVRPGEV 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  728 FPVDGKVLEGNTMADESLITGEAMPVTKKPGSTVIAGSINAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQLAD 807
Cdd:cd07544   142 VPVDGEVVSGTATLDESSLTGESKPVSKRPGDRVMSGAVNGDSALTMVATKLAADSQYAGIVRLVKEAQANPAPFVRLAD 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  808 RfsgYFVPFIIIMSTLTLVVWIVIGfidfgvvqryfpnpnkhisqteVIIRFAfqtsiTVLCIACPCSLGLATPTAVMVG 887
Cdd:cd07544   222 R---YAVPFTLLALAIAGVAWAVSG----------------------DPVRFA-----AVLVVATPCPLILAAPVAIVSG 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  888 TGVAAQNGILIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLLGDVATLplrKVLAVVGTAEASSEHPLGVAVTKY 967
Cdd:cd07544   272 MSRSSRRGILVKDGGVLEKLARAKTVAFDKTGTLTYGQPKVVDVVPAPGVDAD---EVLRLAASVEQYSSHVLARAIVAA 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  968 CKEELgtETLGYCTDFQAVPGCGigckvsnVEGILAHSErplsapashlneagslpaekdavpqtfsVLIGNREWLRRNG 1047
Cdd:cd07544   349 ARERE--LQLSAVTELTEVPGAG-------VTGTVDGHE----------------------------VKVGKLKFVLARG 391
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1048 LtiSSDVSDAMTDhemkGQTAILVAIDGVLCGMIAIADAVKQEAALAVHTLQSMGVD-VVLITGDNRKTARAIATQVGIN 1126
Cdd:cd07544   392 A--WAPDIRNRPL----GGTAVYVSVDGKYAGAITLRDEVRPEAKETLAHLRKAGVErLVMLTGDRRSVAEYIASEVGID 465
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1127 KVFAEVLPSHKVAKVQElQNKGKKVAMVGDGVNDSPALAQADMGVAIGT-GTDVAIEAADVVLIRNDLLDVVASIHLSKR 1205
Cdd:cd07544   466 EVRAELLPEDKLAAVKE-APKAGPTIMVGDGVNDAPALAAADVGIAMGArGSTAASEAADVVILVDDLDRVVDAVAIARR 544
                         650       660       670
                  ....*....|....*....|....*....|....*..
gi 342187274 1206 TVRRIRINLVLALIYNLVGIPIAAGVFMP--IGIVLQ 1240
Cdd:cd07544   545 TRRIALQSVLIGMALSIIGMLIAAFGLIPpvAGALLQ 581
zntA PRK11033
zinc/cadmium/mercury/lead-transporting ATPase; Provisional
459-1218 2.15e-102

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


Pssm-ID: 236827 [Multi-domain]  Cd Length: 741  Bit Score: 343.51  E-value: 2.15e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  459 ITGMTCASCVHNIESKLTRTNGITYASVALATSKALVKFDPEIIGPrdIIKIIEEIGFH----ASLAQRNPNAHHLDHkm 534
Cdd:PRK11033   59 VSGMDCPSCARKVENAVRQLAGVNQVQVLFATEKLVVDADNDIRAQ--VESAVQKAGFSlrdeQAAAAAPESRLKSEN-- 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  535 eikqwkksflcslvfgIPVMALMIYMLIPSnephqsmvldhniipGLSILN----LIFFILCTfvqLLGGWYFYVQAYKS 610
Cdd:PRK11033  135 ----------------LPLITLAVMMAISW---------------GLEQFNhpfgQLAFIATT---LVGLYPIARKALRL 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  611 LRHRSAnmdVLIVLATSIAYVYSLVIlvVAVAEKAerspvtffdtppMLFVFIALGRWLEHLAKSKTSEALAKLMSLQAT 690
Cdd:PRK11033  181 IRSGSP---FAIETLMSVAAIGALFI--GATAEAA------------MVLLLFLIGERLEGYAASRARRGVSALMALVPE 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  691 EATVVTLGEdnliiREEqVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMADESLITGEAMPVTKKPGSTVIAGSINAHG 770
Cdd:PRK11033  244 TATRLRDGE-----REE-VAIADLRPGDVIEVAAGGRLPADGKLLSPFASFDESALTGESIPVERATGEKVPAGATSVDR 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  771 SVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTLTLVV-----------WIVIGfidfgvv 839
Cdd:PRK11033  318 LVTLEVLSEPGASAIDRILHLIEEAEERRAPIERFIDRFSRIYTPAIMLVALLVILVppllfaapwqeWIYRG------- 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  840 qryfpnpnkhisqteviirfafqtsITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAHKIKTVMFDKTG 919
Cdd:PRK11033  391 -------------------------LTLLLIGCPCALVISTPAAITSGLAAAARRGALIKGGAALEQLGRVTTVAFDKTG 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  920 TITHGVPRVMRVLLLGDVatlPLRKVLAVVGTAEASSEHPLGVAVTKYCKEElgTETLGYCTDFQAVPGCGIgckvsnvE 999
Cdd:PRK11033  446 TLTEGKPQVTDIHPATGI---SESELLALAAAVEQGSTHPLAQAIVREAQVR--GLAIPEAESQRALAGSGI-------E 513
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1000 GILAHSERPLSAPashlneaGSLPAEKDAVPQTFSVLignrewlrrngltissdvsdamtdhEMKGQTAILVAIDGVLCG 1079
Cdd:PRK11033  514 GQVNGERVLICAP-------GKLPPLADAFAGQINEL-------------------------ESAGKTVVLVLRNDDVLG 561
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1080 MIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGINkVFAEVLPSHKVAKVQELqNKGKKVAMVGDGVN 1159
Cdd:PRK11033  562 LIALQDTLRADARQAISELKALGIKGVMLTGDNPRAAAAIAGELGID-FRAGLLPEDKVKAVTEL-NQHAPLAMVGDGIN 639
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 342187274 1160 DSPALAQADMGVAIGTGTDVAIEAADVVLIRNDLLDVVASIHLSKRTVRRIRINLVLAL 1218
Cdd:PRK11033  640 DAPAMKAASIGIAMGSGTDVALETADAALTHNRLRGLAQMIELSRATHANIRQNITIAL 698
P-type_ATPase_HM cd07553
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
584-1235 1.41e-82

P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily of the heavy metal-transporting ATPases (Type IB ATPases) which transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319851 [Multi-domain]  Cd Length: 610  Bit Score: 283.64  E-value: 1.41e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  584 LNLIFFILctfVQLLGGWYFYVQAYKSLRHRSANMDVLIVLATSIAYVYSLVILVVAVAEkaerspvTFFDTPPMLFVFI 663
Cdd:cd07553    32 LSSAFALP---SMLYCGSYFYGKAWKSAKQGIPHIDLPIALGIVIGFVVSWYGLIKGDGL-------VYFDSLSVLVFLM 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  664 ALGRWLEHLAKSKTSEALAKlMSLQATEATVVTLGEDNLIIREEQVpmelvQRGDIVKVVPGGKFPVDGKVLEGNTMADE 743
Cdd:cd07553   102 LVGRWLQVVTQERNRNRLAD-SRLEAPITEIETGSGSRIKTRADQI-----KSGDVYLVASGQRVPVDGKLLSEQASIDM 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  744 SLITGEAMPVTKKPGSTVIAGSINAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTL 823
Cdd:cd07553   176 SWLTGESLPRIVERGDKVPAGTSLENQAFEIRVEHSLAESWSGSILQKVEAQEARKTPRDLLADKIIHYFTVIALLIAVA 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  824 TLVVWIvigFIDFGVvqryfpnpnkhisqteviirfAFQTSITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKP 903
Cdd:cd07553   256 GFGVWL---AIDLSI---------------------ALKVFTSVLIVACPCALALATPFTDEIALARLKKKGVLIKNASS 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  904 LEMAHKIKTVMFDKTGTITHGvprvMRVLLLGDVATLPLRKVLAVVGTaEASSEHPLGVAVTKYCkEELGTETLGYCtDF 983
Cdd:cd07553   312 LERLSRVRTIVFDKTGTLTRG----KSSFVMVNPEGIDRLALRAISAI-EAHSRHPISRAIREHL-MAKGLIKAGAS-EL 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  984 QAVPGCGIGckvSNVEGilahserplsapasHLNEAGSLPaekdavpqtfsvlignrewlrrngltissdvsdamtDHEM 1063
Cdd:cd07553   385 VEIVGKGVS---GNSSG--------------SLWKLGSAP------------------------------------DACG 411
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1064 KGQTAILVAIDGVLCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGIN--KVFAEVLPSHKVAKV 1141
Cdd:cd07553   412 IQESGVVIARDGRQLLDLSFNDLLRPDSNREIEELKKGGLSIAILSGDNEEKVRLVGDSLGLDprQLFGNLSPEEKLAWI 491
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1142 QELQNKGkkVAMVGDGVNDSPALAQADMGVAIGTGTDVAIEAADVVLIRNDLLDVVASIHLSKRTVRRIRINLVLALIYN 1221
Cdd:cd07553   492 ESHSPEN--TLMVGDGANDALALASAFVGIAVAGEVGVSLEAADIYYAGNGIGGIRDLLTLSKQTIKAIKGLFAFSLLYN 569
                         650       660
                  ....*....|....*....|...
gi 342187274 1222 LVGI---------PIAAGVFMPI 1235
Cdd:cd07553   570 LVAIglalsgwisPLVAAILMPL 592
MgtA COG0474
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism];
658-1241 2.23e-57

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


Pssm-ID: 440242 [Multi-domain]  Cd Length: 874  Bit Score: 215.36  E-value: 2.23e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  658 MLFVFIALGRWLEHlaksKTSEALAKLMSLQATEATVvtlgednliIR---EEQVPM-ELVqRGDIVKVVPGGKFPVDGK 733
Cdd:COG0474    90 VVLLNAIIGFVQEY----RAEKALEALKKLLAPTARV---------LRdgkWVEIPAeELV-PGDIVLLEAGDRVPADLR 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  734 VLEGNTM-ADESLITGEAMPVTKKP------------------GSTVIAGSinAHGSVlikaTHVGNDTTLAQIVKLVEE 794
Cdd:COG0474   156 LLEAKDLqVDESALTGESVPVEKSAdplpedaplgdrgnmvfmGTLVTSGR--GTAVV----VATGMNTEFGKIAKLLQE 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  795 AQMSKAPIQQLADRFSGYFVPFIIIMStltLVVWIVIGFIDFGVVQryfpnpnkhisqteviirfAFQTSITVLcIAcpc 874
Cdd:COG0474   230 AEEEKTPLQKQLDRLGKLLAIIALVLA---ALVFLIGLLRGGPLLE-------------------ALLFAVALA-VA--- 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  875 slglATP-------TAVM-VGTGVAAQNGILIKggkplemahKIKTV-----M----FDKTGTITHGVPRVMRVLLLGdv 937
Cdd:COG0474   284 ----AIPeglpavvTITLaLGAQRMAKRNAIVR---------RLPAVetlgsVtvicTDKTGTLTQNKMTVERVYTGG-- 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  938 atlplrKVLAVVGTAEASSEHPLGVAVtkyckeelgtetlgYCTDFQAVPGCGIGckvSNVEG-ILAHSERpLSAPASHL 1016
Cdd:COG0474   349 ------GTYEVTGEFDPALEELLRAAA--------------LCSDAQLEEETGLG---DPTEGaLLVAAAK-AGLDVEEL 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1017 NEAGSLPAEK--DAVPQTFSVLIGNRE-------------------WLRRNG----LT--ISSDVSDAMTDHEMKGQTAI 1069
Cdd:COG0474   405 RKEYPRVDEIpfDSERKRMSTVHEDPDgkrllivkgapevvlalctRVLTGGgvvpLTeeDRAEILEAVEELAAQGLRVL 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1070 LVA---IDG-------------VLCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGINK------ 1127
Cdd:COG0474   485 AVAykeLPAdpeldseddesdlTFLGLVGMIDPPRPEAKEAIAECRRAGIRVKMITGDHPATARAIARQLGLGDdgdrvl 564
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1128 ---------------------VFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIG-TGTDVAIEAAD 1185
Cdd:COG0474   565 tgaeldamsdeelaeavedvdVFARVSPEHKLRIVKALQANGHVVAMTGDGVNDAPALKAADIGIAMGiTGTDVAKEAAD 644
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 342187274 1186 VVLIRNDLLDVVASIHLSkrtvRRIRINLVLALIYNL---VGI--PIAAGVFMPIGIVLQP 1241
Cdd:COG0474   645 IVLLDDNFATIVAAVEEG----RRIYDNIRKFIKYLLssnFGEvlSVLLASLLGLPLPLTP 701
P-type_ATPase_K cd02078
potassium-transporting ATPase ATP-binding subunit, KdpB, a subunit of the prokaryotic ...
678-1197 6.52e-55

potassium-transporting ATPase ATP-binding subunit, KdpB, a subunit of the prokaryotic high-affinity potassium uptake system KdpFABC; similar to Escherichia coli KdpB; KdpFABC is a prokaryotic high-affinity potassium uptake system. It is expressed under K(+) limiting conditions when the other potassium transport systems are not able to provide a sufficient flow of K(+) into the bacteria. The KdpB subunit represents the catalytic subunit performing ATP hydrolysis. KdpB is comprised of four domains: the transmembrane domain, the nucleotide-binding domain, the phosphorylation domain, and the actuator domain. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319773 [Multi-domain]  Cd Length: 667  Bit Score: 204.03  E-value: 6.52e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  678 SEALAKLM------SLQAT--EATVVTLGEDNliiREEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMADESLITGE 749
Cdd:cd02078    73 AEAIAEGRgkaqadSLRKTktETQAKRLRNDG---KIEKVPATDLKKGDIVLVEAGDIIPADGEVIEGVASVDESAITGE 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  750 AMPVTKKPG---STVIAGSINAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQqladrfsgyfVPFIIIMSTLTLV 826
Cdd:cd02078   150 SAPVIRESGgdrSSVTGGTKVLSDRIKVRITANPGETFLDRMIALVEGASRQKTPNE----------IALTILLVGLTLI 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  827 VWIVI----GFIDFGVVQryfpnpnkhisqteviirfafqTSITVLcIACPCSLGLATPTAVMVGTGVAA-----QNGIL 897
Cdd:cd02078   220 FLIVVatlpPFAEYSGAP----------------------VSVTVL-VALLVCLIPTTIGGLLSAIGIAGmdrllRFNVI 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  898 IKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLLGDVAtlplrkVLAVVGTAEASS---EHPLGVAVTKYCKEELGT 974
Cdd:cd02078   277 AKSGRAVEAAGDVDTLLLDKTGTITLGNRQATEFIPVGGVD------EKELADAAQLASladETPEGRSIVILAKQLGGT 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  975 ETlgyctdfqavpgcgigckvsnvEGILAHSER-PLSAPA--SHLNEAGSLPAEKDAVPQTfsvlignREWLRRNGLTIS 1051
Cdd:cd02078   351 ER----------------------DLDLSGAEFiPFSAETrmSGVDLPDGTEIRKGAVDAI-------RKYVRSLGGSIP 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1052 SDVSDAMTDHEMKGQTAILVAIDGVLCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGINKVFAE 1131
Cdd:cd02078   402 EELEAIVEEISKQGGTPLVVAEDDRVLGVIYLKDIIKPGIKERFAELRKMGIKTVMITGDNPLTAAAIAAEAGVDDFLAE 481
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 342187274 1132 VLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIGTGTDVAIEAADVVLIRND---LLDVV 1197
Cdd:cd02078   482 AKPEDKLELIRKEQAKGKLVAMTGDGTNDAPALAQADVGVAMNSGTQAAKEAGNMVDLDSDptkLIEVV 550
E1-E2_ATPase pfam00122
E1-E2 ATPase;
686-894 4.29e-50

E1-E2 ATPase;


Pssm-ID: 425475 [Multi-domain]  Cd Length: 181  Bit Score: 175.45  E-value: 4.29e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   686 SLQATEATVVTLGEdnliirEEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMADESLITGEAMPVTKKPGSTVIAGS 765
Cdd:pfam00122    1 SLLPPTATVLRDGT------EEEVPADELVPGDIVLLKPGERVPADGRIVEGSASVDESLLTGESLPVEKKKGDMVYSGT 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   766 INAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTLTLVVWIVIGFIDFgvvqryfpn 845
Cdd:pfam00122   75 VVVSGSAKAVVTATGEDTELGRIARLVEEAKSKKTPLQRLLDRLGKYFSPVVLLIALAVFLLWLFVGGPPL--------- 145
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 342187274   846 pnkhisqteviirFAFQTSITVLCIACPCSLGLATPTAVMVGTGVAAQN 894
Cdd:pfam00122  146 -------------RALLRALAVLVAACPCALPLATPLALAVGARRLAKK 181
P-type_ATPase_H cd02076
plant and fungal plasma membrane H(+)-ATPases, and related bacterial and archaeal putative H(+) ...
658-1235 6.68e-47

plant and fungal plasma membrane H(+)-ATPases, and related bacterial and archaeal putative H(+)-ATPases; This subfamily includes eukaryotic plasma membrane H(+)-ATPase which transports H(+) from the cytosol to the extracellular space, thus energizing the plasma membrane for the uptake of ions and nutrients, and is expressed in plants and fungi. This H(+)-ATPase consists of four domains: a transmembrane domain and three cytosolic domains: nucleotide-binding domain, phosphorylation domain and actuator domain, and belongs to the P-type ATPase type III subfamily. This subfamily also includes the putative P-type H(+)-ATPase, MJ1226p of the anaerobic hyperthermophilic archaea Methanococcus jannaschii. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319771 [Multi-domain]  Cd Length: 781  Bit Score: 181.66  E-value: 6.68e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  658 MLFVFIALGRWLEHLAKSktseALAKLMSLQATEATVVTLGEDNLIIREEQVPmelvqrGDIVKVVPGGKFPVDGKVLEG 737
Cdd:cd02076    64 LLLINAGIGFIEERQAGN----AVAALKKSLAPKARVLRDGQWQEIDAKELVP------GDIVSLKIGDIVPADARLLTG 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  738 NTMA-DESLITGEAMPVTKKPGSTVIAGSINAHGSVLIKATHVGNDTTLAQIVKLVEEAQmSKAPIQQLADRFSGYFVPF 816
Cdd:cd02076   134 DALQvDQSALTGESLPVTKHPGDEAYSGSIVKQGEMLAVVTATGSNTFFGKTAALVASAE-EQGHLQKVLNKIGNFLILL 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  817 IIIMsTLTLVVWIVIGFIDFGVvqryfpnpnkhisqtevIIRFAFQTSITVLCIACPCSLglatpTAVM-VGTGVAAQNG 895
Cdd:cd02076   213 ALIL-VLIIVIVALYRHDPFLE-----------------ILQFVLVLLIASIPVAMPAVL-----TVTMaVGALELAKKK 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  896 ILIKGGKPLEMAHKIKTVMFDKTGTITH-----GVPRVMRVLLLGDVatlplrkVLAVVGTAEASSEHPLGVAVTKYCKE 970
Cdd:cd02076   270 AIVSRLSAIEELAGVDILCSDKTGTLTLnklslDEPYSLEGDGKDEL-------LLLAALASDTENPDAIDTAILNALDD 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  971 EL----GTETLGYcTDFQAVPGCgigckvsnvegILAHSERPlsapashlnEAGSLPAEKDAvPQTFSVLIGNREWLRRN 1046
Cdd:cd02076   343 YKpdlaGYKQLKF-TPFDPVDKR-----------TEATVEDP---------DGERFKVTKGA-PQVILELVGNDEAIRQA 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1047 gltissdVSDAMTDHEMKGQTAILVAIDGV-----LCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIAT 1121
Cdd:cd02076   401 -------VEEKIDELASRGYRSLGVARKEDggrweLLGLLPLFDPPRPDSKATIARAKELGVRVKMITGDQLAIAKETAR 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1122 QVGINK------------------------------VFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGV 1171
Cdd:cd02076   474 QLGMGTnilsaerlklggggggmpgseliefiedadGFAEVFPEHKYRIVEALQQRGHLVGMTGDGVNDAPALKKADVGI 553
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 342187274 1172 AIGTGTDVAIEAADVVLIRNDLLDVVASIHLSKRTVRR------------IRINLVLALIY---NLVGIPIAAGVFMPI 1235
Cdd:cd02076   554 AVSGATDAARAAADIVLTAPGLSVIIDAIKTSRQIFQRmksyviyriaetLRILVFFTLGIlilNFYPLPLIMIVLIAI 632
P-type_ATPase cd07539
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ...
674-1231 4.79e-45

uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase transporters of unknown function. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids. They are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd2+, and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine.


Pssm-ID: 319840 [Multi-domain]  Cd Length: 634  Bit Score: 173.76  E-value: 4.79e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  674 KSKTSEALAKLMSLQATEATVVTLGEDnliiREEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMA-DESLITGEAMP 752
Cdd:cd07539    78 RLRAERALAALLAQQQQPARVVRAPAG----RTQTVPAESLVPGDVIELRAGEVVPADARLLEADDLEvDESALTGESLP 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  753 VTKK-----------------PGSTVIAGsinaHGSVLIKAThvGNDTTLAQIVKLVEEAQmSKAPIQQLADRFSGYFVP 815
Cdd:cd07539   154 VDKQvaptpgapladracmlyEGTTVVSG----QGRAVVVAT--GPHTEAGRAQSLVAPVE-TATGVQAQLRELTSQLLP 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  816 fiIIMSTLTLVVWIvigfidfGVVQRYfpnpnkhisqtevIIRFAFQTSITVLCIACPCSLGLATPTAVMVGTGVAAQNG 895
Cdd:cd07539   227 --LSLGGGAAVTGL-------GLLRGA-------------PLRQAVADGVSLAVAAVPEGLPLVATLAQLAAARRLSRRG 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  896 ILIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLllGDVATLPLRkvlavvgtaeasSEHPLGVAVTKYCKEELgte 975
Cdd:cd07539   285 VLVRSPRTVEALGRVDTICFDKTGTLTENRLRVVQVR--PPLAELPFE------------SSRGYAAAIGRTGGGIP--- 347
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  976 tlgyctdFQAVPGcgigckvsNVEGILAHSERplsapashLNEAGSLPAEKDAVPQTFSVligNREWLRRNGLTISSDVS 1055
Cdd:cd07539   348 -------LLAVKG--------APEVVLPRCDR--------RMTGGQVVPLTEADRQAIEE---VNELLAGQGLRVLAVAY 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1056 DAMTDHEmkGQTAILVAIDGVLCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGINK-------- 1127
Cdd:cd07539   402 RTLDAGT--THAVEAVVDDLELLGLLGLADTARPGAAALIAALHDAGIDVVMITGDHPITARAIAKELGLPRdaevvtga 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1128 ------------------VFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIGT-GTDVAIEAADVVL 1188
Cdd:cd07539   480 eldaldeealtglvadidVFARVSPEQKLQIVQALQAAGRVVAMTGDGANDAAAIRAADVGIGVGArGSDAAREAADLVL 559
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|...
gi 342187274 1189 IRNDLLDVVASIHLSKRTVRRIRINLVLALIYNLVGIPIAAGV 1231
Cdd:cd07539   560 TDDDLETLLDAVVEGRTMWQNVRDAVHVLLGGNLGEVMFTLIG 602
P-type_ATPase_cation cd02080
P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, ...
675-1235 2.28e-44

P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, and Synechocystis sp. PCC 6803 PMA1, a putative Ca(2+)-ATPase; This subfamily includes the P-type Na(+)-ATPase of an alkaliphilic bacterium Exiguobacterium aurantiacum Mna and cyanobacterium Synechocystis sp. PCC 6803 PMA1, a cation-transporting ATPase which may translocate calcium. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319775 [Multi-domain]  Cd Length: 819  Bit Score: 174.37  E-value: 2.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  675 SKTSEALAKLMSLQATEATVVTLGEDNLIIREEQVPmelvqrGDIVKVVPGGKFPVDGKVLEG-NTMADESLITGEAMPV 753
Cdd:cd02080    78 GKAEKALAAIKNMLSPEATVLRDGKKLTIDAEELVP------GDIVLLEAGDKVPADLRLIEArNLQIDESALTGESVPV 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  754 TKK------------------PGSTVIAGSinAHGSVLikAThvGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVP 815
Cdd:cd02080   152 EKQegpleedtplgdrknmaySGTLVTAGS--ATGVVV--AT--GADTEIGRINQLLAEVEQLATPLTRQIAKFSKALLI 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  816 FIIIMSTLTLVVWIVIGfidfgvvqryfpnpnkHISQTEviirfAFQTSITVLCIACPcsLGLATPTAVMVGTGV---AA 892
Cdd:cd02080   226 VILVLAALTFVFGLLRG----------------DYSLVE-----LFMAVVALAVAAIP--EGLPAVITITLAIGVqrmAK 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  893 QNGIlIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLLGDVATL------------PLRKVLAVVGTAEASSEHPL 960
Cdd:cd02080   283 RNAI-IRRLPAVETLGSVTVICSDKTGTLTRNEMTVQAIVTLCNDAQLhqedghwkitgdPTEGALLVLAAKAGLDPDRL 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  961 GVAVTKyckeelgTETLGYCTDFQ--AVPGCGIGCKVSNVEGilaHSERPLSAPASHLNEAGSLPAEKDAVPQtfsvlig 1038
Cdd:cd02080   362 ASSYPR-------VDKIPFDSAYRymATLHRDDGQRVIYVKG---APERLLDMCDQELLDGGVSPLDRAYWEA------- 424
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1039 NREWLRRNGLTI------SSDVSDAMTDHEmkgqtailVAIDG-VLCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGD 1111
Cdd:cd02080   425 EAEDLAKQGLRVlafayrEVDSEVEEIDHA--------DLEGGlTFLGLQGMIDPPRPEAIAAVAECQSAGIRVKMITGD 496
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1112 NRKTARAIATQVGI--------------------------NKVFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALA 1165
Cdd:cd02080   497 HAETARAIGAQLGLgdgkkvltgaeldalddeelaeavdeVDVFARTSPEHKLRLVRALQARGEVVAMTGDGVNDAPALK 576
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1166 QADMGVAIG-TGTDVAIEAADVVLIRNDLLDVVASIhlskRTVRRIRINLVLALIYNL---------VGIPIAAGVFMPI 1235
Cdd:cd02080   577 QADIGIAMGiKGTEVAKEAADMVLADDNFATIAAAV----EEGRRVYDNLKKFILFTLptnlgeglvIIVAILFGVTLPL 652
P-type_ATPase cd02609
uncharacterized subfamily of P-type ATPase transporter, similar to uncharacterized ...
681-1239 2.83e-44

uncharacterized subfamily of P-type ATPase transporter, similar to uncharacterized Streptococcus pneumoniae exported protein 7, Exp7; This subfamily contains P-type ATPase transporters of unknown function, similar to Streptococcus pneumoniae Exp7. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids. They are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd(2+), and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine.


Pssm-ID: 319795 [Multi-domain]  Cd Length: 661  Bit Score: 172.08  E-value: 2.83e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  681 LAKLMSLQATEATVVTLGEdnliirEEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTM-ADESLITGEAMPVTKKPGS 759
Cdd:cd02609    83 LDKLSILNAPKVTVIRDGQ------EVKIPPEELVLDDILILKPGEQIPADGEVVEGGGLeVDESLLTGESDLIPKKAGD 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  760 TVIAGSINAHGSVLIKATHVGNDTTlaqIVKLVEEAQMSK---APIQQLADRFSGyFVPFIIIMstltlvvwivIGFIDF 836
Cdd:cd02609   157 KLLSGSFVVSGAAYARVTAVGAESY---AAKLTLEAKKHKlinSELLNSINKILK-FTSFIIIP----------LGLLLF 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  837 gvVQRYFPNpnkHISQTEVIIRfafqtSITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAHKIKTVMFD 916
Cdd:cd02609   223 --VEALFRR---GGGWRQAVVS-----TVAALLGMIPEGLVLLTSVALAVGAIRLAKKKVLVQELYSIETLARVDVLCLD 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  917 KTGTITHGvprvmrvlllgdvaTLPLRKVLAVVGTAEASSEHPLGVAVtkyCKEELGTETLGYCTDFQAVPGcgigcKVS 996
Cdd:cd02609   293 KTGTITEG--------------KMKVERVEPLDEANEAEAAAALAAFV---AASEDNNATMQAIRAAFFGNN-----RFE 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  997 NVEGILAHSERPLSAPASHLNEAGSLPAEKDAVPQTFSVLIGNREWLRRNGL-TISSDVSDAMTDHEMKGQTAILVAIdg 1075
Cdd:cd02609   351 VTSIIPFSSARKWSAVEFRDGGTWVLGAPEVLLGDLPSEVLSRVNELAAQGYrVLLLARSAGALTHEQLPVGLEPLAL-- 428
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1076 vlcgmIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGIN------------------------KVFAE 1131
Cdd:cd02609   429 -----ILLTDPIRPEAKETLAYFAEQGVAVKVISGDNPVTVSAIAKRAGLEgaesyidastlttdeelaeavenyTVFGR 503
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1132 VLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIGTGTDVAIEAADVVLIRND---LLDV------------ 1196
Cdd:cd02609   504 VTPEQKRQLVQALQALGHTVAMTGDGVNDVLALKEADCSIAMASGSDATRQVAQVVLLDSDfsaLPDVvfegrrvvnnie 583
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....
gi 342187274 1197 -VASIHLSKrTVRRIrinlVLALIYNLVGIPIAagvFMPIGIVL 1239
Cdd:cd02609   584 rVASLFLVK-TIYSV----LLALICVITALPFP---FLPIQITL 619
P-type_ATPase cd07538
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ...
658-1241 4.38e-44

uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase transporters of unknown function. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids. They are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd2+, and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine.


Pssm-ID: 319839 [Multi-domain]  Cd Length: 653  Bit Score: 171.47  E-value: 4.38e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  658 MLFVFIALGRWLEHLAKSKTSEALAKLMSLQATEATVVTLGEDNLIIREEQVPmelvqrGDIVKVVPGGKFPVDGKVLEG 737
Cdd:cd07538    61 ILLIFVVVIIAIEVVQEWRTERALEALKNLSSPRATVIRDGRERRIPSRELVP------GDLLILGEGERIPADGRLLEN 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  738 NTMA-DESLITGEAMPVTKKPGST------------VIAGSINAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQ 804
Cdd:cd07538   135 DDLGvDESTLTGESVPVWKRIDGKamsapggwdknfCYAGTLVVRGRGVAKVEATGSRTELGKIGKSLAEMDDEPTPLQK 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  805 LADRFSGYFVPFIIIMSTLTLVVwivigfidFGVVQryfpnpnKHISQteviirfAFQTSITVLCIACPCSLGLATPTAV 884
Cdd:cd07538   215 QTGRLVKLCALAALVFCALIVAV--------YGVTR-------GDWIQ-------AILAGITLAMAMIPEEFPVILTVFM 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  885 MVGTGVAAQNGILIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLLgdVATLPLRKVLAVVGTAEASSEhplgvav 964
Cdd:cd07538   273 AMGAWRLAKKNVLVRRAAAVETLGSITVLCVDKTGTLTKNQMEVVELTSL--VREYPLRPELRMMGQVWKRPE------- 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  965 tkyckeelgtetlGYctdFQAVPGcgigckvsnvegilahserplsAPASHLNEAGSLPAEKDAVPQTFSVLigNREWLR 1044
Cdd:cd07538   344 -------------GA---FAAAKG----------------------SPEAIIRLCRLNPDEKAAIEDAVSEM--AGEGLR 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1045 RNGLTISSDVSDAMTDHEMkgqtailvaiDGVLC--GMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQ 1122
Cdd:cd07538   384 VLAVAACRIDESFLPDDLE----------DAVFIfvGLIGLADPLREDVPEAVRICCEAGIRVVMITGDNPATAKAIAKQ 453
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1123 VGIN--------------------------KVFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIGT- 1175
Cdd:cd07538   454 IGLDntdnvitgqeldamsdeelaekvrdvNIFARVVPEQKLRIVQAFKANGEIVAMTGDGVNDAPALKAAHIGIAMGKr 533
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 342187274 1176 GTDVAIEAADVVLIRNDLLDVVASIHLSkrtvRRIRINLVLALIYNL-VGIPIAAGVFMPIGIVLQP 1241
Cdd:cd07538   534 GTDVAREASDIVLLDDNFSSIVSTIRLG----RRIYDNLKKAITYVFaIHVPIAGLALLPPLLGLPP 596
P-type_ATPases cd01431
ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, ...
1063-1236 5.17e-44

ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids. They are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd(2+), and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine.


Pssm-ID: 319764 [Multi-domain]  Cd Length: 319  Bit Score: 163.01  E-value: 5.17e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1063 MKGQTAILVAIDGVLCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGI----------------- 1125
Cdd:cd01431    94 DPETSKEAVELNLVFLGLIGLQDPPRPEVKEAIAKCRTAGIKVVMITGDNPLTAIAIAREIGIdtkasgvilgeeadems 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1126 ----------NKVFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIG-TGTDVAIEAADVVLIRNDLL 1194
Cdd:cd01431   174 eeelldliakVAVFARVTPEQKLRIVKALQARGEVVAMTGDGVNDAPALKQADVGIAMGsTGTDVAKEAADIVLLDDNFA 253
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 342187274 1195 DVVASIHLSKRTVRRIRINLVLALIYNLVGIPIAAGVFMPIG 1236
Cdd:cd01431   254 TIVEAVEEGRAIYDNIKKNITYLLANNVAEVFAIALALFLGG 295
P-type_ATPase_Ca_prok cd02089
prokaryotic P-type Ca(2+)-ATPase similar to Synechococcus elongatus sp. strain PCC 7942 PacL ...
675-1224 5.69e-41

prokaryotic P-type Ca(2+)-ATPase similar to Synechococcus elongatus sp. strain PCC 7942 PacL and Listeria monocytogenes LMCA1; Ca(2+) transport ATPase is a plasma membrane protein which pumps Ca(2+) ion out of the cytoplasm. This prokaryotic subfamily includes the Ca(2+)-ATPase Synechococcus elongatus PacL, Listeria monocytogenes Ca(2+)-ATPase 1 (LMCA1) which has a low Ca(2+) affinity and a high pH optimum (pH about 9) and may remove Ca(2+) from the microorganism in environmental conditions when e.g. stressed by high Ca(2+) and alkaline pH, and the Bacillus subtilis putative P-type Ca(2+)-transport ATPase encoded by the yloB gene, which is expressed during sporulation. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319781 [Multi-domain]  Cd Length: 674  Bit Score: 162.01  E-value: 5.69e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  675 SKTSEALAKLMSLQATEATVVTLGEDNLIIREEQVPmelvqrGDIVKVVPGGKFPVDGKVLEG-NTMADESLITGEAMPV 753
Cdd:cd02089    78 YKAEKALAALKKMSAPTAKVLRDGKKQEIPARELVP------GDIVLLEAGDYVPADGRLIESaSLRVEESSLTGESEPV 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  754 TKKPG-------------STVIAGSINAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSgyfvpfiiim 820
Cdd:cd02089   152 EKDADtlleedvplgdrkNMVFSGTLVTYGRGRAVVTATGMNTEMGKIATLLEETEEEKTPLQKRLDQLG---------- 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  821 STLTLVVwIVIGFIDFGVVqryfpnpnkHISQTEVIIRFAFQTSITVLCIacPCSLGlATPTAVM-VGTGVAAQNGILIK 899
Cdd:cd02089   222 KRLAIAA-LIICALVFALG---------LLRGEDLLDMLLTAVSLAVAAI--PEGLP-AIVTIVLaLGVQRMAKRNAIIR 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  900 GGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLLGD---VATLP-----------LRKVLAVVGTAEASSE-------H 958
Cdd:cd02089   289 KLPAVETLGSVSVICSDKTGTLTQNKMTVEKIYTIGDpteTALIRaarkagldkeeLEKKYPRIAEIPFDSErklmttvH 368
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  959 PLG---VAVTKYCKEELgtetLGYCTDFQavpgcGIGCKVSNVEGILAHserplsapASHLNEAGSlpaekdavpqtfsv 1035
Cdd:cd02089   369 KDAgkyIVFTKGAPDVL----LPRCTYIY-----INGQVRPLTEEDRAK--------ILAVNEEFS-------------- 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1036 lignREWLRRNGL---TISSDVSDAMTDHEMkgqtailvaiDGVLCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDN 1112
Cdd:cd02089   418 ----EEALRVLAVaykPLDEDPTESSEDLEN----------DLIFLGLVGMIDPPRPEVKDAVAECKKAGIKTVMITGDH 483
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1113 RKTARAIATQVGINK---------------------------VFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALA 1165
Cdd:cd02089   484 KLTARAIAKELGILEdgdkaltgeeldkmsdeelekkveqisVYARVSPEHKLRIVKALQRKGKIVAMTGDGVNDAPALK 563
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1166 QADMGVAIG-TGTDVAIEAADVVLIRNDLLDVVASIhlskRTVRRIRINLVLALIYNLVG 1224
Cdd:cd02089   564 AADIGVAMGiTGTDVAKEAADMILTDDNFATIVAAV----EEGRTIYDNIRKFIRYLLSG 619
PRK14010 PRK14010
K(+)-transporting ATPase subunit B;
622-1187 2.50e-39

K(+)-transporting ATPase subunit B;


Pssm-ID: 184448 [Multi-domain]  Cd Length: 673  Bit Score: 157.17  E-value: 2.50e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  622 IVLATSIAYVYSLVILVVAVAEKAERSPVTF-FDTPPMLFVFIALGRWLEHLAKSKtSEALAKLMSLQATEATVVTLGED 700
Cdd:PRK14010   34 IMFVVEVGMLLALGLTIYPDLFHQESVSRLYvFSIFIILLLTLVFANFSEALAEGR-GKAQANALRQTQTEMKARRIKQD 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  701 NliiREEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMADESLITGEAMPVTKKPG---STVIAGSINAHGSVLIKAT 777
Cdd:PRK14010  113 G---SYEMIDASDLKKGHIVRVATGEQIPNDGKVIKGLATVDESAITGESAPVIKESGgdfDNVIGGTSVASDWLEVEIT 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  778 HVGNDTTLAQIVKLVEEAQMSKAPIQqladrfsgyfVPFIIIMSTLTLVVwivigfidFGVVQRYFPnpnkhisqTEVII 857
Cdd:PRK14010  190 SEPGHSFLDKMIGLVEGATRKKTPNE----------IALFTLLMTLTIIF--------LVVILTMYP--------LAKFL 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  858 RFAFQTSITVLCIAC--PCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLllg 935
Cdd:PRK14010  244 NFNLSIAMLIALAVCliPTTIGGLLSAIGIAGMDRVTQFNILAKSGRSVETCGDVNVLILDKTGTITYGNRMADAFI--- 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  936 DVATLPLRKVLAVVGTAEASSEHPLGVAVTKYCKEElgteTLGYCTDFQAVPGCGIGCKVSNVEgiLAHSERPLSAPASH 1015
Cdd:PRK14010  321 PVKSSSFERLVKAAYESSIADDTPEGRSIVKLAYKQ----HIDLPQEVGEYIPFTAETRMSGVK--FTTREVYKGAPNSM 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1016 LNEagslpaekdavpqtfsvlignrewLRRNGLTISSDVSDAMTDHEMKGQTAILVAIDGVLCGMIAIADAVKQEAALAV 1095
Cdd:PRK14010  395 VKR------------------------VKEAGGHIPVDLDALVKGVSKKGGTPLVVLEDNEILGVIYLKDVIKDGLVERF 450
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1096 HTLQSMGVDVVLITGDNRKTARAIATQVGINKVFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIGT 1175
Cdd:PRK14010  451 RELREMGIETVMCTGDNELTAATIAKEAGVDRFVAECKPEDKINVIREEQAKGHIVAMTGDGTNDAPALAEANVGLAMNS 530
                         570
                  ....*....|..
gi 342187274 1176 GTDVAIEAADVV 1187
Cdd:PRK14010  531 GTMSAKEAANLI 542
ATPase-IIIA_H TIGR01647
plasma-membrane proton-efflux P-type ATPase; This model describes the plasma membrane proton ...
658-1211 2.78e-33

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


Pssm-ID: 273731 [Multi-domain]  Cd Length: 754  Bit Score: 139.00  E-value: 2.78e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   658 MLFVFIALGRWLEHLAKSktseALAKLMSLQATEATVVTLGEDNLIIREEQVPmelvqrGDIVKVVPGGKFPVDGKVLEG 737
Cdd:TIGR01647   64 LLLLNATIGFIEENKAGN----AVEALKQSLAPKARVLRDGKWQEIPASELVP------GDVVRLKIGDIVPADCRLFEG 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   738 NTM-ADESLITGEAMPVTKKPGSTVIAGSINAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPF 816
Cdd:TIGR01647  134 DYIqVDQAALTGESLPVTKKTGDIAYSGSTVKQGEAEAVVTATGMNTFFGKAAALVQSTETGSGHLQKILSKIGLFLIVL 213
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   817 IIImstLTLVVWIVIGFIdfgvvqryfpnpnKHISQTEvIIRFAFQTSITVLCIACPCSLglatpTAVM-VGTGVAAQNG 895
Cdd:TIGR01647  214 IGV---LVLIELVVLFFG-------------RGESFRE-GLQFALVLLVGGIPIAMPAVL-----SVTMaVGAAELAKKK 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   896 ILIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLLGDvaTLPLRKVLavVGTAEASSEHPLG------VAVTKYCK 969
Cdd:TIGR01647  272 AIVTRLTAIEELAGMDILCSDKTGTLTLNKLSIDEILPFFN--GFDKDDVL--LYAALASREEDQDaidtavLGSAKDLK 347
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   970 EELGTETLGYCTDFQAVpgcgigckvsnvegiLAHSERPLSAPAshlnEAGSLPAEKDAvPQTFSVLIGNREwlrrnglT 1049
Cdd:TIGR01647  348 EARDGYKVLEFVPFDPV---------------DKRTEATVEDPE----TGKRFKVTKGA-PQVILDLCDNKK-------E 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  1050 ISSDVSDAMTDHEMKGQTAILVAIDGV-----LCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVG 1124
Cdd:TIGR01647  401 IEEKVEEKVDELASRGYRALGVARTDEegrwhFLGLLPLFDPPRHDTKETIERARHLGVEVKMVTGDHLAIAKETARRLG 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  1125 INKV-----------------------------FAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIGT 1175
Cdd:TIGR01647  481 LGTNiytadvllkgdnrddlpsglgemvedadgFAEVFPEHKYEIVEILQKRGHLVGMTGDGVNDAPALKKADVGIAVAG 560
                          570       580       590
                   ....*....|....*....|....*....|....*.
gi 342187274  1176 GTDVAIEAADVVLIRNDLLDVVASIHLSKRTVRRIR 1211
Cdd:TIGR01647  561 ATDAARSAADIVLTEPGLSVIVDAILESRKIFQRMK 596
ATPase-IIB_Ca TIGR01517
plasma-membrane calcium-translocating P-type ATPase; This model describes the P-type ATPase ...
705-1228 4.18e-33

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


Pssm-ID: 273668 [Multi-domain]  Cd Length: 956  Bit Score: 139.14  E-value: 4.18e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   705 REEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTM-ADESLITGEAMPVTKKP--GSTVIAGSINAHGSVLIKATHVGN 781
Cdd:TIGR01517  178 QEQQISIHDIVVGDIVSLSTGDVVPADGVFISGLSLeIDESSITGESDPIKKGPvqDPFLLSGTVVNEGSGRMLVTAVGV 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   782 DTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTLTLVVWIVIGFIDFGVVQRYFPNPNKHISQtevIIRFaF 861
Cdd:TIGR01517  258 NSFGGKLMMELRQAGEEETPLQEKLSELAGLIGKFGMGSAVLLFLVLSLRYVFRIIRGDGRFEDTEEDAQT---FLDH-F 333
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   862 QTSITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLLGDVATL- 940
Cdd:TIGR01517  334 IIAVTIVVVAVPEGLPLAVTIALAYSMKKMMKDNNLVRHLAACETMGSATAICSDKTGTLTQNVMSVVQGYIGEQRFNVr 413
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   941 ---PLRKVLAVVG---TAEASSEHPLGVAVTKYCKEE-LGTETLGYCTDFQAVPGcGIGCKVSNVEGILAHSE-RPLSap 1012
Cdd:TIGR01517  414 deiVLRNLPAAVRnilVEGISLNSSSEEVVDRGGKRAfIGSKTECALLDFGLLLL-LQSRDVQEVRAEEKVVKiYPFN-- 490
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  1013 aSHLNEAGSLPAEKDAVPQTFSVliGNREWLRRN---------GLTISSDVSDAMTDHEMKG------QTAILVAIDG-- 1075
Cdd:TIGR01517  491 -SERKFMSVVVKHSGGKYREFRK--GASEIVLKPcrkrldsngEATPISEDDKDRCADVIEPlasdalRTICLAYRDFap 567
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  1076 -------------VLCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGIN---------------- 1126
Cdd:TIGR01517  568 eefprkdypnkglTLIGVVGIKDPLRPGVREAVQECQRAGITVRMVTGDNIDTAKAIARNCGILtfgglamegkefrslv 647
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  1127 -----------KVFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIG-TGTDVAIEAADVVLIRNDLL 1194
Cdd:TIGR01517  648 yeemdpilpklRVLARSSPLDKQLLVLMLKDMGEVVAVTGDGTNDAPALKLADVGFSMGiSGTEVAKEASDIILLDDNFA 727
                          570       580       590
                   ....*....|....*....|....*....|....
gi 342187274  1195 DVVASIHLSKRTVRRIRINLVLALIYNLVGIPIA 1228
Cdd:TIGR01517  728 SIVRAVKWGRNVYDNIRKFLQFQLTVNVVAVILT 761
ATPase-IIA1_Ca TIGR01116
sarco/endoplasmic reticulum calcium-translocating P-type ATPase; This model describes the ...
635-1201 1.74e-31

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


Pssm-ID: 273452 [Multi-domain]  Cd Length: 917  Bit Score: 134.14  E-value: 1.74e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   635 VILVVAVAEKAERSPVTFFDtpPMLFVFI-----ALGRWLEHLAKsktsEALAKLMSLQATEATVVTLGEDNLIIREEQV 709
Cdd:TIGR01116   19 VSFVLAWFEEGEETVTAFVE--PFVILLIlvanaIVGVWQERNAE----KAIEALKEYESEHAKVLRDGRWSVIKAKDLV 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   710 PmelvqrGDIVKVVPGGKFPVDGKVLEGNTM-ADESLITGEAMPVTKKPGST-------------VIAGSINAHGSVLIK 775
Cdd:TIGR01116   93 P------GDIVELAVGDKVPADIRVLSLKTLrVDQSILTGESVSVNKHTESVpderavnqdkknmLFSGTLVVAGKARGV 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   776 ATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIiimSTLTLVVWIV-IG-FIDFGVVQRYFpnpnkhisQT 853
Cdd:TIGR01116  167 VVRTGMSTEIGKIRDEMRAAEQEDTPLQKKLDEFGELLSKVI---GLICILVWVInIGhFNDPALGGGWI--------QG 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   854 EViirFAFQTSITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLL 933
Cdd:TIGR01116  236 AI---YYFKIAVALAVAAIPEGLPAVITTCLALGTRKMAKKNAIVRKLPSVETLGCTTVICSDKTGTLTTNQMSVCKVVA 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   934 LGDV---------------------------------ATLPLRKVLAVV-----------GTAEASSE----------HP 959
Cdd:TIGR01116  313 LDPSssslnefcvtgttyapeggvikddgpvaggqdaGLEELATIAALCndssldfnerkGVYEKVGEateaalkvlvEK 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   960 LGVAVTKYCKEELGTETLGYCTDFQAVPG-------------CGIGCKVSN---------VEGILAHSERPLsapashLN 1017
Cdd:TIGR01116  393 MGLPATKNGVSSKRRPALGCNSVWNDKFKklatlefsrdrksMSVLCKPSTgnklfvkgaPEGVLERCTHIL------NG 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  1018 EAGSLPAEKDAVPQTFSVL--IGNREWLRRNGLTISSDVSDAMTDHEMKGQTAILVAIDGVLCGMIAIADAVKQEAALAV 1095
Cdd:TIGR01116  467 DGRAVPLTDKMKNTILSVIkeMGTTKALRCLALAFKDIPDPREEDLLSDPANFEAIESDLTFIGVVGMLDPPRPEVADAI 546
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  1096 HTLQSMGVDVVLITGDNRKTARAIATQVGI-------------------------------NKVFAEVLPSHKVAKVQEL 1144
Cdd:TIGR01116  547 EKCRTAGIRVIMITGDNKETAEAICRRIGIfspdedvtfksftgrefdemgpakqraacrsAVLFSRVEPSHKSELVELL 626
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 342187274  1145 QNKGKKVAMVGDGVNDSPALAQADMGVAIGTGTDVAIEAADVVLIRNDLLDVVASIH 1201
Cdd:TIGR01116  627 QEQGEIVAMTGDGVNDAPALKKADIGIAMGSGTEVAKEASDMVLADDNFATIVAAVE 683
P-type_ATPase_Ca_PMCA-like cd02081
animal plasma membrane Ca2(+)-ATPases (PMCA), similar to human ATP2B1-4/PMCA1-4, and related ...
708-1224 4.12e-31

animal plasma membrane Ca2(+)-ATPases (PMCA), similar to human ATP2B1-4/PMCA1-4, and related Ca2(+)-ATPases including Saccharomyces cerevisiae vacuolar PMC1; Animal PMCAs function to export Ca(2+) from cells and play a role in regulating Ca(2+) signals following stimulus induction and in preventing calcium toxicity. Many PMCA pump variants exist due to alternative splicing of transcripts. PMCAs are regulated by the binding of calmodulin or by kinase-mediated phosphorylation. Saccharomyces cerevisiae vacuolar transporter Pmc1p facilitates the accumulation of Ca2+ into vacuoles. Pmc1p is not regulated by direct calmodulin binding but responds to the calmodulin/calcineurin-signaling pathway and is controlled by the transcription factor complex Tcn1p/Crz1p. Similarly, the expression of the gene for Dictyostelium discoideum Ca(2+)-ATPase PAT1, patA, is under the control of a calcineurin-dependent transcription factor. Plant vacuolar Ca(2+)-ATPases, are regulated by direct-calmodulin binding. Plant Ca(2+)-ATPases are present at various cellular locations including the plasma membrane, endoplasmic reticulum, chloroplast and vacuole. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319776 [Multi-domain]  Cd Length: 721  Bit Score: 131.94  E-value: 4.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  708 QVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTM-ADESLITGEAMPVTKKP-----------GSTVIAGSinahGSVLIK 775
Cdd:cd02081   112 QISVFDIVVGDIVQLKYGDLIPADGLLIEGNDLkIDESSLTGESDPIKKTPdnqipdpfllsGTKVLEGS----GKMLVT 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  776 AthVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTLTLVVwIVIGFIDFGVVQRYFPNPNKHISQtev 855
Cdd:cd02081   188 A--VGVNSQTGKIMTLLRAENEEKTPLQEKLTKLAVQIGKVGLIVAALTFIV-LIIRFIIDGFVNDGKSFSAEDLQE--- 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  856 IIRFaFQTSITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMR----- 930
Cdd:cd02081   262 FVNF-FIIAVTIIVVAVPEGLPLAVTLSLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTQNRMTVVQgyign 340
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  931 ----------VLLLGDVATLPLRKVLAVVGTAEASSE---------HPLGVaVTKYCKeelgtetlgyctdfqavpgcgi 991
Cdd:cd02081   341 ktecallgfvLELGGDYRYREKRPEEKVLKVYPFNSArkrmstvvrLKDGG-YRLYVK---------------------- 397
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  992 gckvsnvegilAHSERPLSAPASHLNEAGSLPAEKDAVPQTFSVLIgnrEWLRRNGL-TI--------SSDVSDAMTDHE 1062
Cdd:cd02081   398 -----------GASEIVLKKCSYILNSDGEVVFLTSEKKEEIKRVI---EPMASDSLrTIglayrdfsPDEEPTAERDWD 463
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1063 M-----KGQTAIlvaidgvlcGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGI-----------N 1126
Cdd:cd02081   464 DeedieSDLTFI---------GIVGIKDPLRPEVPEAVAKCQRAGITVRMVTGDNINTARAIARECGIltegedglvleG 534
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1127 KVFAE----------------------VL----PSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIG-TGTDV 1179
Cdd:cd02081   535 KEFRElideevgevcqekfdkiwpklrVLarssPEDKYTLVKGLKDSGEVVAVTGDGTNDAPALKKADVGFAMGiAGTEV 614
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 342187274 1180 AIEAADVVLIRNDLLDVVASIHLSkRTV-RRIR--------INLVlALIYNLVG 1224
Cdd:cd02081   615 AKEASDIILLDDNFSSIVKAVMWG-RNVyDSIRkflqfqltVNVV-AVILAFIG 666
P-type_ATPase_Mg cd02077
magnesium transporting ATPase (MgtA), similar to Escherichia coli MgtA and Salmonella ...
620-1194 1.29e-29

magnesium transporting ATPase (MgtA), similar to Escherichia coli MgtA and Salmonella typhimurium MgtA; MgtA is a membrane protein which actively transports Mg(2+) into the cytosol with its electro-chemical gradient rather than against the gradient as other cation transporters do. It may act both as a transporter and as a sensor for Mg(2+). In Salmonella typhimurium and Escherichia coli, the two-component system PhoQ/PhoP regulates the transcription of the mgtA gene by sensing Mg(2+) concentrations in the periplasm. MgtA is activated by cardiolipin and it highly sensitive to free magnesium in vitro. It consists of a transmembrane domain and three cytosolic domains: nucleotide-binding domain, phosphorylation domain and actuator domain, and belongs to the P-type ATPase type III subfamily. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319772 [Multi-domain]  Cd Length: 768  Bit Score: 127.36  E-value: 1.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  620 VLIVLAtsiayVYSLVILVVAVAEkaERSPVTFFDTPPMLFVFIALGRWLEHlaksKTSEALAKLMSLQATEATVVtlge 699
Cdd:cd02077    42 VLLVLA-----LVSFFTDVLLAPG--EFDLVGALIILLMVLISGLLDFIQEI----RSLKAAEKLKKMVKNTATVI---- 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  700 dNLIIREEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTM-ADESLITGEAMPVTKKP-------------------GS 759
Cdd:cd02077   107 -RDGSKYMEIPIDELVPGDIVYLSAGDMIPADVRIIQSKDLfVSQSSLTGESEPVEKHAtakktkdesilelenicfmGT 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  760 TVIAGSINAhgsVLIKathVGNDTTLAQIVKLVEEAQmSKAPIQQLADRFSGYFVPFIIIMstlTLVVWIVIGFIDFGVV 839
Cdd:cd02077   186 NVVSGSALA---VVIA---TGNDTYFGSIAKSITEKR-PETSFDKGINKVSKLLIRFMLVM---VPVVFLINGLTKGDWL 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  840 QRYFpnpnkhisqteviirfaFQTSITVlciacpcslGLaTPTAV-MVGTgvaaQNgiLIKGGKplEMAhKIKTVM---- 914
Cdd:cd02077   256 EALL-----------------FALAVAV---------GL-TPEMLpMIVT----SN--LAKGAV--RMS-KRKVIVknln 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  915 ------------FDKTGTITHGVPRVMRVLLLGDVATLPLRKVLAVVGTAEASSEHPLGVAVTKYCKEELGTETLGYCT- 981
Cdd:cd02077   300 aiqnfgamdilcTDKTGTLTQDKIVLERHLDVNGKESERVLRLAYLNSYFQTGLKNLLDKAIIDHAEEANANGLIQDYTk 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  982 ------DFQ----------AVPGCGIGCKVSnVEGILAHSerplsapaSHLNEAGSL----PAEKDAVPQTFSVLigNRE 1041
Cdd:cd02077   380 ideipfDFErrrmsvvvkdNDGKHLLITKGA-VEEILNVC--------THVEVNGEVvpltDTLREKILAQVEEL--NRE 448
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1042 WLRRNGL---TISSDVSDAMTDHEMkgqtailvaiDGVLCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARA 1118
Cdd:cd02077   449 GLRVLAIaykKLPAPEGEYSVKDEK----------ELILIGFLAFLDPPKESAAQAIKALKKNGVNVKILTGDNEIVTKA 518
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1119 IATQVGIN-------------------------KVFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAI 1173
Cdd:cd02077   519 ICKQVGLDinrvltgseiealsdeelakiveetNIFAKLSPLQKARIIQALKKNGHVVGFMGDGINDAPALRQADVGISV 598
                         650       660
                  ....*....|....*....|.
gi 342187274 1174 GTGTDVAIEAADVVLIRNDLL 1194
Cdd:cd02077   599 DSAVDIAKEAADIILLEKDLM 619
P-type_ATPase_Na_ENA cd02086
fungal-type Na(+)-ATPase, similar to the plasma membrane sodium transporters Saccharomyces ...
605-1222 5.83e-29

fungal-type Na(+)-ATPase, similar to the plasma membrane sodium transporters Saccharomyces cerevisiae Ena1p, Ena2p and Ustilago maydis Ena1, and the endoplasmic reticulum sodium transporter Ustilago maydis Ena2; Fungal-type Na(+)-ATPase (also called ENA ATPases). This subfamily includes the Saccharomyces cerevisiae plasma membrane transporters: Na(+)/Li(+)-exporting ATPase Ena1p which may also extrudes K(+), and Na(+)-exporting P-type ATPase Ena2p. It also includes Ustilago maydis plasma membrane Ena1, an K(+)/Na(+)-ATPase whose chief role is to pump Na(+) and K(+) out of the cytoplasm, especially at high pH values, and endoplasmic reticulum Ena2 ATPase which mediates Na(+) or K(+) fluxes in the ER or in other endomembranes. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319780 [Multi-domain]  Cd Length: 920  Bit Score: 125.65  E-value: 5.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  605 VQAYKSLRHRSAN-MDVLIVLATSIAYvyslvilvvAVAEKAERSPVTFfdtppMLFVFIALGRWLEHLAKsKTSEALAK 683
Cdd:cd02086    25 VSAWKILLRQVANaMTLVLIIAMALSF---------AVKDWIEGGVIAA-----VIALNVIVGFIQEYKAE-KTMDSLRN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  684 LMSlqaTEATVVTLGEDNLIIREEQVPmelvqrGDIVKVVPGGKFPVDGKVLEG-NTMADESLITGEAMPVTKK------ 756
Cdd:cd02086    90 LSS---PNAHVIRSGKTETISSKDVVP------GDIVLLKVGDTVPADLRLIETkNFETDEALLTGESLPVIKDaelvfg 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  757 ---------------PGSTVIAGsiNAHGSVLIKA--THVG-------NDTTLAQIVKLVEEAQMSKAPIQQLADRFSGY 812
Cdd:cd02086   161 keedvsvgdrlnlaySSSTVTKG--RAKGIVVATGmnTEIGkiakalrGKGGLISRDRVKSWLYGTLIVTWDAVGRFLGT 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  813 FV--PFIIIMSTLTLVV-WIVIGF--IDFGVvqryfpnpNKHISQTEVIIrFAFQTSITVLciacPCSLgLATPTAVM-V 886
Cdd:cd02086   239 NVgtPLQRKLSKLAYLLfFIAVILaiIVFAV--------NKFDVDNEVII-YAIALAISMI----PESL-VAVLTITMaV 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  887 GTGVAAQNGILIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLLGDVATLplrkvlAVVGTAEAS---------SE 957
Cdd:cd02086   305 GAKRMVKRNVIVRKLDALEALGAVTDICSDKTGTLTQGKMVVRQVWIPAALCNI------ATVFKDEETdcwkahgdpTE 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  958 HPLGVAVTK--YCKEELGTETLGYCTDFQAVPgCGIGCK------VSNVEGIL-AHS----ERPLSAPASHLNEAGSLPA 1024
Cdd:cd02086   379 IALQVFATKfdMGKNALTKGGSAQFQHVAEFP-FDSTVKrmsvvyYNNQAGDYyAYMkgavERVLECCSSMYGKDGIIPL 457
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1025 EKDAVPQtfsvLIGNREWLRRNGLTISSDVSDAMTDHEMKGQTAI-------LVAIDGVLCGMIAIADAVKQEAALAVHT 1097
Cdd:cd02086   458 DDEFRKT----IIKNVESLASQGLRVLAFASRSFTKAQFNDDQLKnitlsraDAESDLTFLGLVGIYDPPRNESAGAVEK 533
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1098 LQSMGVDVVLITGDNRKTARAIATQVGINK-------------------------------------VFAEVLPSHKVAK 1140
Cdd:cd02086   534 CHQAGITVHMLTGDHPGTAKAIAREVGILPpnsyhysqeimdsmvmtasqfdglsdeevdalpvlplVIARCSPQTKVRM 613
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1141 VQELQNKGKKVAMVGDGVNDSPALAQADMGVAIGT-GTDVAIEAADVVLIRNDLLDVVASIHLSKRTVRRIRINLVLALI 1219
Cdd:cd02086   614 IEALHRRKKFCAMTGDGVNDSPSLKMADVGIAMGLnGSDVAKDASDIVLTDDNFASIVNAIEEGRRMFDNIQKFVLHLLA 693

                  ...
gi 342187274 1220 YNL 1222
Cdd:cd02086   694 ENV 696
P-type_ATPase_SPCA cd02085
golgi-associated secretory pathway Ca(2+) transport ATPases, similar to human ATPase secretory ...
676-1200 9.35e-29

golgi-associated secretory pathway Ca(2+) transport ATPases, similar to human ATPase secretory pathway Ca(2+) transporting 1/hSPCA1 and Saccharomyces cerevisiae Ca(2+)/Mn(2+)-transporting P-type ATPase, Pmr1p; SPCAs are Ca(2+) pumps important for the golgi-associated secretion pathway, in addition some function as Mn(2+) pumps in Mn(2+) detoxification. Saccharomyces cerevisiae Pmr1p is a high affinity Ca(2+)/Mn(2+) ATPase which transports Ca(2+) and Mn(2+) from the cytoplasm into the Golgi. Pmr1p also contributes to Cd(2+) detoxification. This subfamily includes human SPCA1 and SPCA2, encoded by the ATP2C1 and ATP2C2 genes; autosomal dominant Hailey-Hailey disease is caused by mutations in the human ATP2C1 gene. It also includes Strongylocentrotus purpuratus testis secretory pathway calcium transporting ATPase SPCA which plays an important role in fertilization. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319779 [Multi-domain]  Cd Length: 804  Bit Score: 124.82  E-value: 9.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  676 KTSEALAKLMSlqaTEATVVTLGEDNLIIREEQVPmelvqrGDIVKVVPGGKFPVDGKVLEGNTMA-DESLITGEAMPVt 754
Cdd:cd02085    73 KSLEALNKLVP---PECHCLRDGKLEHFLARELVP------GDLVCLSIGDRIPADLRLFEATDLSiDESSLTGETEPC- 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  755 KKPGSTVIAGSINAHGS--------VLIKATH-------VGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSgyfvpfiii 819
Cdd:cd02085   143 SKTTEVIPKASNGDLTTrsniafmgTLVRCGHgkgivigTGENSEFGEVFKMMQAEEAPKTPLQKSMDKLG--------- 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  820 mSTLTLVVWIVIGFIDF-GVVQryfpnpNKHISQTeviirfaFQTSITVLCIACPcsLGLATPTAVMVGTGV---AAQNG 895
Cdd:cd02085   214 -KQLSLYSFIIIGVIMLiGWLQ------GKNLLEM-------FTIGVSLAVAAIP--EGLPIVVTVTLALGVmrmAKRRA 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  896 IlIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVL--------------LLG---DVATLPLRKVLAVVGTAEA---S 955
Cdd:cd02085   278 I-VKKLPIVETLGCVNVICSDKTGTLTKNEMTVTKIVtgcvcnnavirnntLMGqptEGALIALAMKMGLSDIRETyirK 356
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  956 SEHPLGvAVTKY--CKEELGTETLGYCTDFqavpgcgigckvsnVEGILahsERPLSAPASHLNEAGS-LPAEkdavPQT 1032
Cdd:cd02085   357 QEIPFS-SEQKWmaVKCIPKYNSDNEEIYF--------------MKGAL---EQVLDYCTTYNSSDGSaLPLT----QQQ 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1033 FSVLIGNREWLRRNGLTISSDVSDAMTDhemkgqtailvaiDGVLCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDN 1112
Cdd:cd02085   415 RSEINEEEKEMGSKGLRVLALASGPELG-------------DLTFLGLVGINDPPRPGVREAIQILLESGVRVKMITGDA 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1113 RKTARAIATQVG-------------------------INKV--FAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALA 1165
Cdd:cd02085   482 QETAIAIGSSLGlyspslqalsgeevdqmsdsqlasvVRKVtvFYRASPRHKLKIVKALQKSGAVVAMTGDGVNDAVALK 561
                         570       580       590
                  ....*....|....*....|....*....|....*.
gi 342187274 1166 QADMGVAIG-TGTDVAIEAADVVLIRNDLLDVVASI 1200
Cdd:cd02085   562 SADIGIAMGrTGTDVCKEAADMILVDDDFSTILAAI 597
P-type_ATPase_SERCA cd02083
sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; ...
620-1188 1.99e-26

sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; SERCA is a transmembrane (Ca2+)-ATPase and a major regulator of Ca(2+) homeostasis and contractility in cardiac and skeletal muscle. It re-sequesters cytoplasmic Ca(2+) to the sarco/endoplasmic reticulum store, thereby also terminating Ca(2+)-induced signaling such as in muscle contraction. Three genes (ATP2A1-3/SERCA1-3) encode SERCA pumps in mammals, further isoforms exist due to alternative splicing of transcripts. The activity of SERCA is regulated by two small membrane proteins called phospholamban and sarcolipin. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319778 [Multi-domain]  Cd Length: 979  Bit Score: 117.78  E-value: 1.99e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  620 VLIVLATSIayvyslVILVVAVAEKAERSPVTFFDTPPMLFVFIA---LGRWLEHLAKSktseALAKLMSLQATEATVVT 696
Cdd:cd02083    58 VRILLLAAI------ISFVLALFEEGEEGVTAFVEPFVILLILIAnavVGVWQERNAEK----AIEALKEYEPEMAKVLR 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  697 LGEDNLIIR-EEQVPmelvqrGDIVKVVPGGKFPVDGKVLE--GNTM-ADESLITGEAMPVTK------KP--------- 757
Cdd:cd02083   128 NGKGVQRIRaRELVP------GDIVEVAVGDKVPADIRIIEikSTTLrVDQSILTGESVSVIKhtdvvpDPravnqdkkn 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  758 ----GSTVIAGSinAHGSVlikaTHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFsGYFVPFIIimSTLTLVVWIV-IG 832
Cdd:cd02083   202 mlfsGTNVAAGK--ARGVV----VGTGLNTEIGKIRDEMAETEEEKTPLQQKLDEF-GEQLSKVI--SVICVAVWAInIG 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  833 fidfgvvqrYFPNPNKHISQTEVIIRFaFQTSITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAHKIKT 912
Cdd:cd02083   273 ---------HFNDPAHGGSWIKGAIYY-FKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSV 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  913 VMFDKTGTITHGVPRVMRVLLLGDVATLPLRKVLAVVGTAEA-------------SSEHPLGVAVTKYCK---------- 969
Cdd:cd02083   343 ICSDKTGTLTTNQMSVSRMFILDKVEDDSSLNEFEVTGSTYApegevfkngkkvkAGQYDGLVELATICAlcndssldyn 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  970 ------EELG--TET--------LG-YCTDFQAVP--GCGIGC---------KVSNVE--------GILAHSERPLS--- 1010
Cdd:cd02083   423 eskgvyEKVGeaTETaltvlvekMNvFNTDKSGLSkrERANACndvieqlwkKEFTLEfsrdrksmSVYCSPTKASGgnk 502
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1011 -----APASHLNEAGS-LPAEKDAVPQTFSV--LIGNREW------LRRNGLTIssdVSDAMTDHEMK-GQTAILVAI-- 1073
Cdd:cd02083   503 lfvkgAPEGVLERCTHvRVGGGKVVPLTAAIkiLILKKVWgygtdtLRCLALAT---KDTPPKPEDMDlEDSTKFYKYet 579
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1074 DGVLCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGI---------------------------- 1125
Cdd:cd02083   580 DLTFVGVVGMLDPPRPEVRDSIEKCRDAGIRVIVITGDNKGTAEAICRRIGIfgededttgksytgrefddlspeeqrea 659
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 342187274 1126 ---NKVFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIGTGTDVAIEAADVVL 1188
Cdd:cd02083   660 crrARLFSRVEPSHKSKIVELLQSQGEITAMTGDGVNDAPALKKAEIGIAMGSGTAVAKSASDMVL 725
P-type_ATPase_Na-K_like cd02608
alpha-subunit of Na(+)/K(+)-ATPases and of gastric H(+)/K(+)-ATPase, similar to the human Na(+) ...
1077-1238 1.60e-25

alpha-subunit of Na(+)/K(+)-ATPases and of gastric H(+)/K(+)-ATPase, similar to the human Na(+)/K(+)-ATPase alpha subunits 1-4; This subfamily includes the alpha subunit of Na(+)/K(+)-ATPase a heteromeric transmembrane protein composed of an alpha- and beta-subunit and an optional third subunit belonging to the FXYD proteins which are more tissue specific regulatory subunits of the enzyme. The alpha-subunit is the catalytic subunit responsible for transport activities of the enzyme. This subfamily includes all four isotopes of the human alpha subunit: (alpha1-alpha4, encoded by the ATP1A1- ATP1A4 genes). Na(+)/K(+)-ATPase functions chiefly as an ion pump, hydrolyzing one molecule of ATP to pump three Na(+) out of the cell in exchange for two K(+)entering the cell per pump cycle. In addition Na(+)/K(+)-ATPase acts as a signal transducer. This subfamily also includes Oreochromis mossambicus (tilapia) Na(+)/K(+)-ATPase alpha 1 and alpha 3 subunits, and gastric H(+)/K(+)-ATPase which exchanges hydronium ion with potassium and is responsible for gastric acid secretion. Gastric H(+)/K(+)-ATPase is an alpha,beta-heterodimeric enzyme. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319794 [Multi-domain]  Cd Length: 905  Bit Score: 114.75  E-value: 1.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1077 LC--GMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGInKVFAEVLPSHKVAKVQELQNKGKKVAMV 1154
Cdd:cd02608   522 LCfvGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGI-IVFARTSPQQKLIIVEGCQRQGAIVAVT 600
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1155 GDGVNDSPALAQADMGVAIG-TGTDVAIEAADVVLirndLLDVVASIHLSKRTVRRIRINLVLALIYNLV-GIP------ 1226
Cdd:cd02608   601 GDGVNDSPALKKADIGVAMGiAGSDVSKQAADMIL----LDDNFASIVTGVEEGRLIFDNLKKSIAYTLTsNIPeitpfl 676
                         170
                  ....*....|....
gi 342187274 1227 --IAAGVFMPIGIV 1238
Cdd:cd02608   677 ifIIANIPLPLGTI 690
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
910-1168 7.77e-25

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


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 103.43  E-value: 7.77e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   910 IKTVMFDKTGTITHGVPRVMRVLllgdvatlplrkvlavvgtAEASSEHPLGVAVTKYCKEELGTETlgyctDFQAVpgc 989
Cdd:pfam00702    1 IKAVVFDLDGTLTDGEPVVTEAI-------------------AELASEHPLAKAIVAAAEDLPIPVE-----DFTAR--- 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   990 gigckvsnvegilahserplsapashlneagslpaekdavpqtfsVLIGNREWLRRNGltissDVSDAMTDHEMKGQTAI 1069
Cdd:pfam00702   54 ---------------------------------------------LLLGKRDWLEELD-----ILRGLVETLEAEGLTVV 83
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  1070 LVAIDGVLcgMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGINKVF-----------AEVLPSHKV 1138
Cdd:pfam00702   84 LVELLGVI--ALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFdvvisgddvgvGKPKPEIYL 161
                          250       260       270
                   ....*....|....*....|....*....|
gi 342187274  1139 AKVQELQNKGKKVAMVGDGVNDSPALAQAD 1168
Cdd:pfam00702  162 AALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
PRK10517 PRK10517
magnesium-transporting P-type ATPase MgtA;
659-1194 5.66e-22

magnesium-transporting P-type ATPase MgtA;


Pssm-ID: 236705 [Multi-domain]  Cd Length: 902  Bit Score: 103.23  E-value: 5.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  659 LFVFIALGRWLEHLAKSKTSEALAKLMSLQATEATVVTLGEDNLIIREEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGN 738
Cdd:PRK10517  128 IALMVAISTLLNFIQEARSTKAADALKAMVSNTATVLRVINDKGENGWLEIPIDQLVPGDIIKLAAGDMIPADLRILQAR 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  739 TM-ADESLITGEAMPVTKKP-------------------GSTVIAGSINAhgsvLIKAThvGNDTTLAQIVKLVEEAQMS 798
Cdd:PRK10517  208 DLfVAQASLTGESLPVEKFAttrqpehsnplecdtlcfmGTNVVSGTAQA----VVIAT--GANTWFGQLAGRVSEQDSE 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  799 KAPIQQLADRFSGYFVPFIIIMstlTLVVWIVIGFI--DFgvvqryfpnpnkhisqTEViirFAFQTSITVlciacpcsl 876
Cdd:PRK10517  282 PNAFQQGISRVSWLLIRFMLVM---APVVLLINGYTkgDW----------------WEA---ALFALSVAV--------- 330
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  877 GLaTPTAV-MVGTGVAAQNGILIKGGK-------PLEMAHKIKTVMFDKTGTIT------------HGVP--RVMRVLLL 934
Cdd:PRK10517  331 GL-TPEMLpMIVTSTLARGAVKLSKQKvivkrldAIQNFGAMDILCTDKTGTLTqdkivlenhtdiSGKTseRVLHSAWL 409
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  935 GDVATLPLRKVL--AVVGTAEASSEHPLGVAVTKYckEELGTetlgyctDFQ--------AVPGCG--IGCKvSNVEGIL 1002
Cdd:PRK10517  410 NSHYQTGLKNLLdtAVLEGVDEESARSLASRWQKI--DEIPF-------DFErrrmsvvvAENTEHhqLICK-GALEEIL 479
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1003 AHSerplsapaSHLNEAGslpaekDAVPQTFSVLIGNR---EWLRRNGLTISSDVSDAMTDHEmkGQTAILVAIDGVLCG 1079
Cdd:PRK10517  480 NVC--------SQVRHNG------EIVPLDDIMLRRIKrvtDTLNRQGLRVVAVATKYLPARE--GDYQRADESDLILEG 543
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1080 MIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGIN-------------------------KVFAEVLP 1134
Cdd:PRK10517  544 YIAFLDPPKETTAPALKALKASGVTVKILTGDSELVAAKVCHEVGLDagevligsdietlsddelanlaertTLFARLTP 623
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1135 SHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIGTGTDVAIEAADVVLIRNDLL 1194
Cdd:PRK10517  624 MHKERIVTLLKREGHVVGFMGDGINDAPALRAADIGISVDGAVDIAREAADIILLEKSLM 683
PRK15122 PRK15122
magnesium-transporting ATPase; Provisional
1076-1194 5.06e-19

magnesium-transporting ATPase; Provisional


Pssm-ID: 237914 [Multi-domain]  Cd Length: 903  Bit Score: 93.55  E-value: 5.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1076 VLCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGIN-------------------------KVFA 1130
Cdd:PRK15122  540 VIRGFLTFLDPPKESAAPAIAALRENGVAVKVLTGDNPIVTAKICREVGLEpgepllgteieamddaalareveerTVFA 619
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187274 1131 EVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIGTGTDVAIEAADVVLIRNDLL 1194
Cdd:PRK15122  620 KLTPLQKSRVLKALQANGHTVGFLGDGINDAPALRDADVGISVDSGADIAKESADIILLEKSLM 683
ATPase-IID_K-Na TIGR01523
potassium and/or sodium efflux P-type ATPase, fungal-type; Initially described as a calcium ...
1041-1240 5.26e-19

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


Pssm-ID: 130586 [Multi-domain]  Cd Length: 1053  Bit Score: 93.54  E-value: 5.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  1041 EWLRRNGLTISSDVSDAMTDHEMKGQTA--ILVAIDGVLCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARA 1118
Cdd:TIGR01523  599 EGLRVLAFASKSFDKADNNDDQLKNETLnrATAESDLEFLGLIGIYDPPRNESAGAVEKCHQAGINVHMLTGDFPETAKA 678
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  1119 IATQVGINK-------------------------------------VFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDS 1161
Cdd:TIGR01523  679 IAQEVGIIPpnfihdrdeimdsmvmtgsqfdalsdeevddlkalclVIARCAPQTKVKMIEALHRRKAFCAMTGDGVNDS 758
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  1162 PALAQADMGVAIG-TGTDVAIEAADVVLIRNDLLDVVASIHLSKRTVRRIRiNLVLALIYNLVGipiaAGVFMPIGIVLQ 1240
Cdd:TIGR01523  759 PSLKMANVGIAMGiNGSDVAKDASDIVLSDDNFASILNAIEEGRRMFDNIM-KFVLHLLAENVA----EAILLIIGLAFR 833
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
146-209 2.24e-18

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


Pssm-ID: 238219 [Multi-domain]  Cd Length: 63  Bit Score: 80.34  E-value: 2.24e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187274  146 KLRVEGMTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYlIQPEDLRDHVNDMGFEAA 209
Cdd:cd00371     1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKAR 63
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
381-443 1.89e-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 [Multi-domain]  Cd Length: 63  Bit Score: 77.65  E-value: 1.89e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 342187274  381 LQIKGMTCASCVSNIERNLQKEAGVLSVLVALMAGKAEIKYDPEViQPLEIAQFIQDLGFEAA 443
Cdd:cd00371     2 LSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPEV-SPEELLEAIEDAGYKAR 63
ATPase-IIC_X-K TIGR01106
sodium or proton efflux -- potassium uptake antiporter, P-type ATPase, alpha subunit; This ...
1077-1238 2.17e-17

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


Pssm-ID: 273445 [Multi-domain]  Cd Length: 997  Bit Score: 88.31  E-value: 2.17e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  1077 LC--GMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGI----------------------NK----- 1127
Cdd:TIGR01106  557 LCfvGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIisegnetvediaarlnipvsqvNPrdaka 636
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  1128 --------------------------VFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIG-TGTDVA 1180
Cdd:TIGR01106  637 cvvhgsdlkdmtseqldeilkyhteiVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGiAGSDVS 716
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 342187274  1181 IEAADVVLirndLLDVVASIHLSKRTVRRIRINLVLALIYNLV-GIP--------IAAGVFMPIGIV 1238
Cdd:TIGR01106  717 KQAADMIL----LDDNFASIVTGVEEGRLIFDNLKKSIAYTLTsNIPeitpflifIIANIPLPLGTI 779
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
61-124 4.51e-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 [Multi-domain]  Cd Length: 63  Bit Score: 76.49  E-value: 4.51e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187274   61 TVRILGMTCQSCVKSIEDRISNLKGIISMKVSLEQGSATVKYVPSvVCLQQVCHQIGDMGFEAS 124
Cdd:cd00371     1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKAR 63
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
456-519 1.16e-16

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


Pssm-ID: 238219 [Multi-domain]  Cd Length: 63  Bit Score: 75.33  E-value: 1.16e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187274  456 ELTITGMTCASCVHNIESKLTRTNGITYASVALATSKALVKFDPEiIGPRDIIKIIEEIGFHAS 519
Cdd:cd00371     1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKAR 63
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
145-209 2.77e-16

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 74.56  E-value: 2.77e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 342187274  145 VKLRVEGMTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYLIQPEDLRDHVNDMGFEAA 209
Cdd:COG2608     4 VTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYEVE 68
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
455-522 1.72e-15

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 72.24  E-value: 1.72e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 342187274  455 IELTITGMTCASCVHNIESKLTRTNGITYASVALATSKALVKFDPEIIGPRDIIKIIEEIGFHASLAQ 522
Cdd:COG2608     4 VTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYEVEKAE 71
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
381-446 3.82e-15

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 71.47  E-value: 3.82e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 342187274  381 LQIKGMTCASCVSNIERNLQKEAGVLSVLVALMAGKAEIKYDPEVIQPLEIAQFIQDLGFEAAVME 446
Cdd:COG2608     6 LKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYEVEKAE 71
P-type_ATPase_cation cd07542
P-type cation-transporting ATPases, similar to human ATPase type 13A2 (ATP13A2) protein and ...
661-1171 1.12e-14

P-type cation-transporting ATPases, similar to human ATPase type 13A2 (ATP13A2) protein and Saccharomyces cerevisiae Ypk9p; Saccharomyces cerevisiae Yph9p localizes to the yeast vacuole and may play a role in sequestering heavy metal ions, its deletion confers sensitivity for growth for cadmium, manganese, nickel or selenium. Human ATP13A2 (PARK9/CLN12) is a lysosomal transporter with zinc as the possible substrate. Mutation in the ATP13A2 gene has been linked to Parkinson's disease and Kufor-Rakeb syndrome, and to neuronal ceroid lipofuscinoses. ATP13A3/AFURS1 is a candidate gene for oculo auriculo vertebral spectrum (OAVS), being one of nine genes included in a 3q29 microduplication in a patient with OAVS. Mutation in the human ATP13A4 may be involved in a speech-language disorder. This subfamily also includes zebrafish ATP13A2 a lysosome-specific transmembrane ATPase protein of unknown function which plays a crucial role during embryonic development, its deletion is lethal. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319842 [Multi-domain]  Cd Length: 760  Bit Score: 79.21  E-value: 1.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  661 VFIALGRWLEHLAKSKTSEALAKLMSLQATEATVVTLGEDNLIIREEQVPmelvqrGDIVKVVPGGK-FPVDGKVLEGNT 739
Cdd:cd07542    58 VIISVISIFLSLYETRKQSKRLREMVHFTCPVRVIRDGEWQTISSSELVP------GDILVIPDNGTlLPCDAILLSGSC 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  740 MADESLITGEAMPVTKKP-------------------------GSTVIAGSINAHGSVLIKATHVGNDTTLAQIVKLVEE 794
Cdd:cd07542   132 IVNESMLTGESVPVTKTPlpdesndslwsiysiedhskhtlfcGTKVIQTRAYEGKPVLAVVVRTGFNTTKGQLVRSILY 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  795 AQmsKAPIQQLADRFSgyfvpFIIIMSTLTLvvwivIGFIdFGVVQRYFPNPNKHisqtEVIIRfafqtSITVLCIACPC 874
Cdd:cd07542   212 PK--PVDFKFYRDSMK-----FILFLAIIAL-----IGFI-YTLIILILNGESLG----EIIIR-----ALDIITIVVPP 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  875 SLglatPTAVMVGTgVAAQN-----GILIKGGKPLEMAHKIKTVMFDKTGTIT------HGVPRVMRVlLLGDVATLPLR 943
Cdd:cd07542   270 AL----PAALTVGI-IYAQSrlkkkGIFCISPQRINICGKINLVCFDKTGTLTedgldlWGVRPVSGN-NFGDLEVFSLD 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  944 KVLavvgTAEASSEHPLGVAVTKYCKEELGTETLGYCTD---FQAVpgCGIGCKVSNVEgiLAHSERPLSAPASHLNE-- 1018
Cdd:cd07542   344 LDL----DSSLPNGPLLRAMATCHSLTLIDGELVGDPLDlkmFEFT--GWSLEILRQFP--FSSALQRMSVIVKTPGDds 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1019 -------AGSLPAE---KDAVPQTFSVLIgnrEWLRRNGLTISSDVSDAMtdhEMKGQTAILVAIDGV-----LCGMIAI 1083
Cdd:cd07542   416 mmaftkgAPEMIASlckPETVPSNFQEVL---NEYTKQGFRVIALAYKAL---ESKTWLLQKLSREEVesdleFLGLIVM 489
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1084 ADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGI------------------------------NKVFAEVL 1133
Cdd:cd07542   490 ENRLKPETAPVINELNRANIRTVMVTGDNLLTAISVARECGMispskkvilieavkpedddsasltwtlllkGTVFARMS 569
                         570       580       590
                  ....*....|....*....|....*....|....*...
gi 342187274 1134 PSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGV 1171
Cdd:cd07542   570 PDQKSELVEELQKLDYTVGMCGDGANDCGALKAADVGI 607
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
258-317 2.74e-14

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 68.78  E-value: 2.74e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 342187274  258 TLQLRIDGMHCM---------ISQLEGVQQISVSLAEGTATVLYNPSVISPEELRAAIEDMGFEASVVS 317
Cdd:COG2608     3 TVTLKVEGMTCGhcvarvekaLKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYEVEKAE 71
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
260-314 3.42e-14

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


Pssm-ID: 238219 [Multi-domain]  Cd Length: 63  Bit Score: 68.40  E-value: 3.42e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187274  260 QLRIDGMHC---------MISQLEGVQQISVSLAEGTATVLYNPSViSPEELRAAIEDMGFEAS 314
Cdd:cd00371     1 ELSVEGMTCagcvskiekALEKLPGVESVEVDLETGKATVEYDPEV-SPEELLEAIEDAGYKAR 63
chaper_CopZ_Eh NF033794
copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and ...
381-445 4.92e-13

copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and related species, is a small copper-binding protein with close homology to domains found, sometimes in multiple copies, in various copper-translocating copper-translocating P-type ATPases, and to distinct families of other small copper chaperones that also named CopZ.


Pssm-ID: 411374 [Multi-domain]  Cd Length: 68  Bit Score: 65.43  E-value: 4.92e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 342187274  381 LQIKGMTCASCVSNIERNLQKEAGVLSVLVALMAGKAEIKYDPEVIQPLEIAQFIQDLGFEAAVM 445
Cdd:NF033794    4 FSIKGMSCNHCVARVEKAVNELPGVKKVKVNLKKENGVVKFDETQVTAEKIAQAVNELGYQAEVV 68
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
58-127 6.15e-13

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 64.93  E-value: 6.15e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   58 ATSTVRILGMTCQSCVKSIEDRISNLKGIISMKVSLEQGSATVKYVPSVVCLQQVCHQIGDMGFEASIAE 127
Cdd:COG2608     2 KTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYEVEKAE 71
P-ATPase-V TIGR01657
P-type ATPase of unknown pump specificity (type V); These P-type ATPases form a distinct clade ...
630-1172 6.90e-13

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


Pssm-ID: 273738 [Multi-domain]  Cd Length: 1054  Bit Score: 73.55  E-value: 6.90e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   630 YVYSLVILVvavaekaerspvtffdtppMLFVFIALGrwlehLAKSKTSEALAKLMSLQATEATVVTLGEDNLIIREEQV 709
Cdd:TIGR01657  193 YYYSLCIVF-------------------MSSTSISLS-----VYQIRKQMQRLRDMVHKPQSVIVIRNGKWVTIASDELV 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   710 PMELVqrgdIVKVVPGGKFPVDGKVLEGNTMADESLITGEAMPVTKKP------------------------GSTVIAGS 765
Cdd:TIGR01657  249 PGDIV----SIPRPEEKTMPCDSVLLSGSCIVNESMLTGESVPVLKFPipdngdddedlflyetskkhvlfgGTKILQIR 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   766 INAH-GSVLIKATHVGNDTTLAQIVKlveeAQMSKAPIQQladRFSGYFVPFIIIMSTLTLV--VWIVIGFIDFGVvqry 842
Cdd:TIGR01657  325 PYPGdTGCLAIVVRTGFSTSKGQLVR----SILYPKPRVF---KFYKDSFKFILFLAVLALIgfIYTIIELIKDGR---- 393
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   843 fpnpnkhiSQTEVIIRfafqtSITVLCIACPCSLglatPTAVMVGTGVA----AQNGILIKGGKPLEMAHKIKTVMFDKT 918
Cdd:TIGR01657  394 --------PLGKIILR-----SLDIITIVVPPAL----PAELSIGINNSlarlKKKGIFCTSPFRINFAGKIDVCCFDKT 456
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   919 GTIT------HGVPRVM--RVLL--LGDVATLPLRKVLAVVGTAEASSE-------HPLGVAVTK-----YCKE-ELGTE 975
Cdd:TIGR01657  457 GTLTedgldlRGVQGLSgnQEFLkiVTEDSSLKPSITHKALATCHSLTKlegklvgDPLDKKMFEatgwtLEEDdESAEP 536
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   976 TLGYCTDFQAVPGCGIGCkvsnVEGILAHSE-RPLSAPASHLNEAGSLPAEKDAvPQTFSVLIgnrewlrrNGLTISSDV 1054
Cdd:TIGR01657  537 TSILAVVRTDDPPQELSI----IRRFQFSSAlQRMSVIVSTNDERSPDAFVKGA-PETIQSLC--------SPETVPSDY 603
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  1055 SDAMTDHEMKG----------------QTAILVAIDGVLC-----GMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNR 1113
Cdd:TIGR01657  604 QEVLKSYTREGyrvlalaykelpkltlQKAQDLSRDAVESnltflGFIVFENPLKPDTKEVIKELKRASIRTVMITGDNP 683
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  1114 KTARAIATQVGI-------------------------------------------------------------------- 1125
Cdd:TIGR01657  684 LTAVHVARECGIvnpsntlilaeaeppesgkpnqikfevidsipfastqveipyplgqdsvedllasryhlamsgkafav 763
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 342187274  1126 ---------------NKVFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVA 1172
Cdd:TIGR01657  764 lqahspelllrllshTTVFARMAPDQKETLVELLQKLDYTVGMCGDGANDCGALKQADVGIS 825
P-type_ATPase_cation cd02082
P-type cation-transporting ATPases, similar to human ATPase type 13A1-A4 (ATP13A1-A4) proteins ...
705-1231 1.12e-12

P-type cation-transporting ATPases, similar to human ATPase type 13A1-A4 (ATP13A1-A4) proteins and Saccharomyces cerevisiae Ypk9p and Spf1p; Saccharomyces cerevisiae Yph9p localizes to the yeast vacuole and may play a role in sequestering heavy metal ions, its deletion confers sensitivity for growth for cadmium, manganese, nickel or selenium. Saccharomyces 1 Spf1p may mediate manganese transport into the endoplasmic reticulum. Human ATP13A2 (PARK9/CLN12) is a lysosomal transporter with zinc as the possible substrate. Mutation in the ATP13A2 gene has been linked to Parkinson's disease and Kufor-Rakeb syndrome, and to neuronal ceroid lipofuscinoses. ATP13A3/AFURS1 is a candidate gene for oculo auriculo vertebral spectrum (OAVS), being one of nine genes included in a 3q29 microduplication in a patient with OAVS. Mutation in the human ATP13A4 may be involved in a speech-language disorder. The expression of ATP13A1 has been followed during mouse development, ATP13A1 transcript expression showed an increase as development progressed, with the highest expression at the peak of neurogenesis. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319777 [Multi-domain]  Cd Length: 786  Bit Score: 72.62  E-value: 1.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  705 REEQVPMELVQRGDIVKV-VPGGKFPVDGKVLEGNTMADESLITGEAMPVTKKP-----------------------GST 760
Cdd:cd02082    96 QEITIASNMIVPGDIVLIkRREVTLPCDCVLLEGSCIVTEAMLTGESVPIGKCQiptdshddvlfkyesskshtlfqGTQ 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  761 VIAGSINAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTLTLVVWIVIGfidfgvVQ 840
Cdd:cd02082   176 VMQIIPPEDDILKAIVVRTGFGTSKGQLIRAILYPKPFNKKFQQQAVKFTLLLATLALIGFLYTLIRLLDIE------LP 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  841 RYFpnpnkhisqteVIIRFafqtsITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAHKIKTVMFDKTGT 920
Cdd:cd02082   250 PLF-----------IAFEF-----LDILTYSVPPGLPMLIAITNFVGLKRLKKNQILCQDPNRISQAGRIQTLCFDKTGT 313
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  921 ITHGVPRVMRVLLLGDVATL-------PLRKVLAVVGTAEASS---------EHPLGVA--------VTKYCKEE----- 971
Cdd:cd02082   314 LTEDKLDLIGYQLKGQNQTFdpiqcqdPNNISIEHKLFAICHSltkingkllGDPLDVKmaeastwdLDYDHEAKqhysk 393
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  972 LGTETLGYCTDFQ---AVPGCGIGCKVSNVEGI-LAHSERPLSAPASHLNEAGSLPAEKDAVPQTFSvlignREWLRRNG 1047
Cdd:cd02082   394 SGTKRFYIIQVFQfhsALQRMSVVAKEVDMITKdFKHYAFIKGAPEKIQSLFSHVPSDEKAQLSTLI-----NEGYRVLA 468
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1048 LTiSSDVSDAMTDHEMK-GQTAILVAIDGVlcGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGI- 1125
Cdd:cd02082   469 LG-YKELPQSEIDAFLDlSREAQEANVQFL--GFIIYKNNLKPDTQAVIKEFKEACYRIVMITGDNPLTALKVAQELEIi 545
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1126 -----------------------------NKVFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIGTG 1176
Cdd:cd02082   546 nrknptiiihllipeiqkdnstqwiliihTNVFARTAPEQKQTIIRLLKESDYIVCMCGDGANDCGALKEADVGISLAEA 625
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 342187274 1177 tDVAIEAADVVLIrndlldvvASIHLSKRTVRRIRINLVLAL----IYNLVGIPIAAGV 1231
Cdd:cd02082   626 -DASFASPFTSKS--------TSISCVKRVILEGRVNLSTSVeifkGYALVALIRYLSF 675
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
145-212 1.57e-12

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 72.10  E-value: 1.57e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 342187274  145 VKLRVEGMTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYLIQPEDLRDHVNDMGFEAAIKS 212
Cdd:COG2217     3 VRLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEKAGYEAEPAD 70
P-type_ATPase_cation cd07543
P-type cation-transporting ATPases, similar to human cation-transporting ATPase type 13A1 ...
1079-1173 2.28e-11

P-type cation-transporting ATPases, similar to human cation-transporting ATPase type 13A1 (ATP13A1) and Saccharomyces manganese-transporting ATPase 1 Spf1p; Saccharomyces Spf1p may mediate manganese transport into the endoplasmic reticulum (ER); one consequence of deletion of SPF1 is severe ER stress. This subfamily also includes Arabidopsis thaliana MIA (Male Gametogenesis Impaired Anthers) protein which is highly abundant in the endoplasmic reticulum and small vesicles of developing pollen grains and tapetum cells. The MIA gene functionally complements a mutant in the SPF1 from Saccharomyces cerevisiae. The expression of ATP13A1 has been followed during mouse development, ATP13A1 transcript expression showed an increase as development progressed, with the highest expression at the peak of neurogenesis. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319843 [Multi-domain]  Cd Length: 804  Bit Score: 68.56  E-value: 2.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1079 GMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGIN------------------------KVFAEVLP 1134
Cdd:cd07543   502 GFIVFSCPLKPDSKETIKELNNSSHRVVMITGDNPLTACHVAKELGIVdkpvlililseegksnewkliphvKVFARVAP 581
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 342187274 1135 SHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAI 1173
Cdd:cd07543   582 KQKEFIITTLKELGYVTLMCGDGTNDVGALKHAHVGVAL 620
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
147-207 3.52e-11

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


Pssm-ID: 411375 [Multi-domain]  Cd Length: 66  Bit Score: 59.80  E-value: 3.52e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 342187274  147 LRVEGMTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYLIQPEDLRDHVNDMGFE 207
Cdd:NF033795    4 LNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVEFDESKVTLDQIKEAIEDQGYD 64
chaper_CopZ_Eh NF033794
copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and ...
455-521 6.01e-11

copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and related species, is a small copper-binding protein with close homology to domains found, sometimes in multiple copies, in various copper-translocating copper-translocating P-type ATPases, and to distinct families of other small copper chaperones that also named CopZ.


Pssm-ID: 411374 [Multi-domain]  Cd Length: 68  Bit Score: 59.27  E-value: 6.01e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 342187274  455 IELTITGMTCASCVHNIESKLTRTNGITYASVALATSKALVKFDPEIIGPRDIIKIIEEIGFHASLA 521
Cdd:NF033794    2 QTFSIKGMSCNHCVARVEKAVNELPGVKKVKVNLKKENGVVKFDETQVTAEKIAQAVNELGYQAEVV 68
HMA pfam00403
Heavy-metal-associated domain;
457-513 7.94e-11

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 58.78  E-value: 7.94e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 342187274   457 LTITGMTCASCVHNIESKLTRTNGITYASVALATSKALVKFDPEIIGPRDIIKIIEE 513
Cdd:pfam00403    2 FRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
1068-1188 1.70e-10

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


Pssm-ID: 319816 [Multi-domain]  Cd Length: 139  Bit Score: 60.30  E-value: 1.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1068 AILVAIDGVLC---GMIAIadavkqEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGINK-VFAE---VLPSHKVAK 1140
Cdd:cd07514     1 LIAVDIDGTLTdrrRSIDL------RAIEAIRKLEKAGIPVVLVTGNSLPVARALAKYLGLSGpVVAEnggVDKGTGLEK 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 342187274 1141 VQELQN-KGKKVAMVGDGVNDSPALAQADMGVAIGTGTDVAIEAADVVL 1188
Cdd:cd07514    75 LAERLGiDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVT 123
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
145-209 7.99e-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 [Multi-domain]  Cd Length: 66  Bit Score: 56.01  E-value: 7.99e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 342187274   145 VKLRVEGMTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYLIQPEDLRDHVNDMGFEAA 209
Cdd:TIGR00003    2 QTFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEVE 66
HMA pfam00403
Heavy-metal-associated domain;
381-437 1.93e-09

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 54.55  E-value: 1.93e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 342187274   381 LQIKGMTCASCVSNIERNLQKEAGVLSVLVALMAGKAEIKYDPEVIQPLEIAQFIQD 437
Cdd:pfam00403    2 FRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
61-122 2.22e-09

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


Pssm-ID: 411375 [Multi-domain]  Cd Length: 66  Bit Score: 54.79  E-value: 2.22e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 342187274   61 TVRILGMTCQSCVKSIEDRISNLKGIISMKVSLEQGSATVKYVPSVVCLQQVCHQIGDMGFE 122
Cdd:NF033795    3 TLNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVEFDESKVTLDQIKEAIEDQGYD 64
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
258-318 7.00e-09

metal-binding (seleno)protein; Known members of this family are selenoproteins with an exceptional UXXU motif, with two selenocysteines. Known members so far derive primarily from MAGs, and have an N-terminal signal peptide N-terminal to the region represented in the seed alignment. Note that this model represents a specific clade of a more widely distributed domain that frequently appears 3 or 4 times in a single protein, so the domain-specific cutoff is critical to identification. Homologous domains, outside the scope of this model, are found in CopZ family copper chaperones and heavy metal-translocating P-type ATPases.


Pssm-ID: 469038 [Multi-domain]  Cd Length: 74  Bit Score: 53.49  E-value: 7.00e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  258 TLQLRIDGMHC---------MISQLEGVQQISVSLAEGTATVLYNPSVISPEELRAAIEDMGFEASVVSE 318
Cdd:NF041115    5 TVILAIEGMTUasupliakkALEGLEGVEKADVSYKEGRAEVAFDPDKVSAAQMVDAVNRIGFRASVIEE 74
HMA pfam00403
Heavy-metal-associated domain;
61-107 1.12e-08

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 52.62  E-value: 1.12e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 342187274    61 TVRILGMTCQSCVKSIEDRISNLKGIISMKVSLEQGSATVKYVPSVV 107
Cdd:pfam00403    1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAEST 47
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
58-132 1.22e-08

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 59.39  E-value: 1.22e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 342187274   58 ATSTVRILGMTCQSCVKSIEDRISNLKGIISMKVSLEQGSATVKYVPSVVCLQQVCHQIGDMGFEASIAEGKAAS 132
Cdd:COG2217     1 ERVRLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEKAGYEAEPADADAAA 75
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
381-443 1.50e-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 [Multi-domain]  Cd Length: 66  Bit Score: 52.54  E-value: 1.50e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 342187274   381 LQIKGMTCASCVSNIERNLQKEAGVLSVLVALMAGKAEIKYDPEVIQPLEIAQFIQDLGFEAA 443
Cdd:TIGR00003    4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEVE 66
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
61-123 4.82e-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 [Multi-domain]  Cd Length: 66  Bit Score: 51.00  E-value: 4.82e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 342187274    61 TVRILGMTCQSCVKSIEDRISNLKGIISMKVSLEQGSATVKYVPSVVCLQQVCHQIGDMGFEA 123
Cdd:TIGR00003    3 TFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEV 65
HMA pfam00403
Heavy-metal-associated domain;
147-198 5.27e-08

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 50.70  E-value: 5.27e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 342187274   147 LRVEGMTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYLIQPEDLR 198
Cdd:pfam00403    2 FRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLV 53
HMA pfam00403
Heavy-metal-associated domain;
261-308 7.36e-08

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 50.31  E-value: 7.36e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 342187274   261 LRIDGMHCM---------ISQLEGVQQISVSLAEGTATVLYNPSVISPEELRAAIED 308
Cdd:pfam00403    2 FRVSGMHCGgcaakvekaLSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
1068-1173 1.15e-07

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


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 51.24  E-value: 1.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1068 AILVAIDGVLCgmiaiadavkqeAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGINKVFAEVL---------PSHKV 1138
Cdd:cd01427     1 AVLFDLDGTLL------------AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIgsdgggtpkPKPKP 68
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 342187274 1139 AKV--QELQNKGKKVAMVGDGVNDSPALAQADM-GVAI 1173
Cdd:cd01427    69 LLLllLKLGVDPEEVLFVGDSENDIEAARAAGGrTVAV 106
PRK13748 PRK13748
putative mercuric reductase; Provisional
455-539 1.18e-07

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 56.31  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  455 IELTITGMTCASCVHNIESKLTRTNGITYASVALATSKALVKFDPEiIGPRDIIKIIEEIGFHASLAQRNPNAHHLDHKM 534
Cdd:PRK13748    2 TTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVG-TSPDALTAAVAGLGYRATLADAPPTDNRGGLLD 80

                  ....*
gi 342187274  535 EIKQW 539
Cdd:PRK13748   81 KMRGW 85
copA PRK10671
copper-exporting P-type ATPase CopA;
66-210 1.45e-07

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 56.29  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   66 GMTCQSCVKSIEDRISNLKGIismkvslEQGSATVKY--VPSVVCLQQVCHQIGDMGFEASIAEGKA-----ASWPSRSL 138
Cdd:PRK10671   11 GLSCGHCVKRVKESLEQRPDV-------EQADVSITEahVTGTASAEALIETIKQAGYDASVSHPKAkplteSSIPSEAL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  139 PA-----------QEAVVKLRVEGMTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPyliQPEDLRDHVNDMGFE 207
Cdd:PRK10671   84 TAaseelpaatadDDDSQQLLLSGMSCASCVSRVQNALQSVPGVTQARVNLAERTALVMGSA---SPQDLVQAVEKAGYG 160

                  ...
gi 342187274  208 AAI 210
Cdd:PRK10671  161 AEA 163
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
1080-1185 6.64e-07

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


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 51.76  E-value: 6.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1080 MIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGINKVFA------------EVL-----PSHKVAKVQ 1142
Cdd:COG0560    82 LFEEVPRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIAnelevedgrltgEVVgpivdGEGKAEALR 161
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 342187274 1143 ELQNKG----KKVAMVGDGVNDSPALAQADMGVAIgTGTDVAIEAAD 1185
Cdd:COG0560   162 ELAAELgidlEQSYAYGDSANDLPMLEAAGLPVAV-NPDPALREAAD 207
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
457-520 1.48e-06

metal-binding (seleno)protein; Known members of this family are selenoproteins with an exceptional UXXU motif, with two selenocysteines. Known members so far derive primarily from MAGs, and have an N-terminal signal peptide N-terminal to the region represented in the seed alignment. Note that this model represents a specific clade of a more widely distributed domain that frequently appears 3 or 4 times in a single protein, so the domain-specific cutoff is critical to identification. Homologous domains, outside the scope of this model, are found in CopZ family copper chaperones and heavy metal-translocating P-type ATPases.


Pssm-ID: 469038 [Multi-domain]  Cd Length: 74  Bit Score: 46.94  E-value: 1.48e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187274  457 LTITGMTCASCVHNIESKLTRTNGITYASVALATSKALVKFDPEIIGPRDIIKIIEEIGFHASL 520
Cdd:NF041115    8 LAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDPDKVSAAQMVDAVNRIGFRASV 71
COG4087 COG4087
Soluble P-type ATPase [General function prediction only];
1071-1187 1.58e-06

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


Pssm-ID: 443263 [Multi-domain]  Cd Length: 156  Bit Score: 49.39  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1071 VAIDGVLcgmiaiADAVKQeaalAVHTLQSMgVDVVLITGDNRKTARAIATQVGINkvfAEVLPS-----HKVAKVQELq 1145
Cdd:COG4087    25 LAVDGKL------IPGVKE----RLEELAEK-LEIHVLTADTFGTVAKELAGLPVE---LHILPSgdqaeEKLEFVEKL- 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 342187274 1146 nKGKKVAMVGDGVNDSPALAQADMGVAI----GTGTDvAIEAADVV 1187
Cdd:COG4087    90 -GAETTVAIGNGRNDVLMLKEAALGIAVigpeGASVK-ALLAADIV 133
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
455-518 3.04e-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 [Multi-domain]  Cd Length: 66  Bit Score: 45.99  E-value: 3.04e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187274   455 IELTITGMTCASCVHNIESKLTRTNGITYASVALATSKALVKFDPEIIGPRDIIKIIEEIGFHA 518
Cdd:TIGR00003    2 QTFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEV 65
PRK13748 PRK13748
putative mercuric reductase; Provisional
381-444 7.94e-06

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 50.15  E-value: 7.94e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 342187274  381 LQIKGMTCASCVSNIERNLQKEAGVLSVLVALMAGKAEIKYDPEV-IQPLEIAqfIQDLGFEAAV 444
Cdd:PRK13748    4 LKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVGTsPDALTAA--VAGLGYRATL 66
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
381-446 2.41e-05

metal-binding (seleno)protein; Known members of this family are selenoproteins with an exceptional UXXU motif, with two selenocysteines. Known members so far derive primarily from MAGs, and have an N-terminal signal peptide N-terminal to the region represented in the seed alignment. Note that this model represents a specific clade of a more widely distributed domain that frequently appears 3 or 4 times in a single protein, so the domain-specific cutoff is critical to identification. Homologous domains, outside the scope of this model, are found in CopZ family copper chaperones and heavy metal-translocating P-type ATPases.


Pssm-ID: 469038 [Multi-domain]  Cd Length: 74  Bit Score: 43.47  E-value: 2.41e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 342187274  381 LQIKGMTCASCVSNIERNLQKEAGVLSVLVALMAGKAEIKYDPEVIQPLEIAQFIQDLGFEAAVME 446
Cdd:NF041115    8 LAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDPDKVSAAQMVDAVNRIGFRASVIE 73
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
1094-1200 2.93e-05

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 46.85  E-value: 2.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1094 AVHTLQSMGVDVVLITGDNRKTARAIATQVGINKVFAEV-----LPSHK-----VAKV-QELQNKGKKVAMVGDGVNDsp 1162
Cdd:COG0546    92 LLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIvggddVPPAKpkpepLLEAlERLGLDPEEVLMVGDSPHD-- 169
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 342187274 1163 ALA--QADM---GVAIGTGTDVAIEA--ADVVLirNDLLDVVASI 1200
Cdd:COG0546   170 IEAarAAGVpfiGVTWGYGSAEELEAagADYVI--DSLAELLALL 212
PRK13748 PRK13748
putative mercuric reductase; Provisional
61-149 1.75e-04

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 45.91  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274   61 TVRILGMTCQSCVKSIEDRISNLKGIISMKVSLEQGSATVKYVPSvVCLQQVCHQIGDMGFEASIAE-----------GK 129
Cdd:PRK13748    3 TLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVG-TSPDALTAAVAGLGYRATLADapptdnrggllDK 81
                          90       100
                  ....*....|....*....|
gi 342187274  130 AASWPSRSLPAQEAVVKLRV 149
Cdd:PRK13748   82 MRGWLGGADKHSGNERPLHV 101
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
1095-1172 1.92e-04

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


Pssm-ID: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 43.69  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1095 VHTLQSMGVDVVLITGDNRKTARAIATQVGINKVFAEVL-----------------PSHKVAKVQELQNKGK----KVAM 1153
Cdd:cd07500    79 IQTLKAKGYKTAVVSGGFTYFTDRLAEELGLDYAFANELeikdgkltgkvlgpivdAQRKAETLQELAARLGipleQTVA 158
                          90
                  ....*....|....*....
gi 342187274 1154 VGDGVNDSPALAQADMGVA 1172
Cdd:cd07500   159 VGDGANDLPMLKAAGLGIA 177
PRK13748 PRK13748
putative mercuric reductase; Provisional
261-326 2.21e-04

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 45.53  E-value: 2.21e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 342187274  261 LRIDGMHC---------MISQLEGVQQISVSLAEGTATVLYNPSViSPEELRAAIEDMGFEASVVSESCSTNPLG 326
Cdd:PRK13748    4 LKITGMTCdscaahvkdALEKVPGVQSADVSYPKGSAQLAIEVGT-SPDALTAAVAGLGYRATLADAPPTDNRGG 77
PRK13748 PRK13748
putative mercuric reductase; Provisional
145-210 4.64e-04

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 44.37  E-value: 4.64e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 342187274  145 VKLRVEGMTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYlIQPEDLRDHVNDMGFEAAI 210
Cdd:PRK13748    2 TTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVG-TSPDALTAAVAGLGYRATL 66
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
1124-1187 5.12e-04

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 43.04  E-value: 5.12e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 342187274 1124 GINKVFAevlpshkVAKVQELQN-KGKKVAMVGDGVNDSPALAQADMGVAIGTGTDVAIEAADVV 1187
Cdd:PRK01158  155 GVNKGTG-------LKKLAELMGiDPEEVAAIGDSENDLEMFEVAGFGVAVANADEELKEAADYV 212
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
1121-1187 9.40e-04

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


Pssm-ID: 272905 [Multi-domain]  Cd Length: 256  Bit Score: 42.64  E-value: 9.40e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 342187274  1121 TQVGINKVFAevlpshkvakVQELQNKG----KKVAMVGDGVNDSPALAQADMGVAIGTGTDVAIEAADVV 1187
Cdd:TIGR00099  183 TAKGVSKGSA----------LQSLAEALgislEDVIAFGDGMNDIEMLEAAGYGVAMGNADEELKALADYV 243
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
1098-1188 1.86e-03

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


Pssm-ID: 319769 [Multi-domain]  Cd Length: 146  Bit Score: 40.20  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1098 LQSMGVDVVLITGDNRKTARAIATQVGINKVFAEVlpSHKVAKVQELQNKGK----KVAMVGDGVNDSPALAQADMGVAI 1173
Cdd:cd01630    40 LQKSGIEVAIITGRQSEAVRRRAKELGIEDLFQGV--KDKLEALEELLEKLGlsdeEVAYMGDDLPDLPVMKRVGLSVAP 117
                          90
                  ....*....|....*
gi 342187274 1174 GTGTDVAIEAADVVL 1188
Cdd:cd01630   118 ADAHPEVREAADYVT 132
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
1083-1174 1.92e-03

phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319796 [Multi-domain]  Cd Length: 195  Bit Score: 41.14  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1083 IADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGINKVFAEVL--------------PSHKVAKVQELQNKG 1148
Cdd:cd02612    81 ILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIDNVLGTQLetedgrytgriigpPCYGEGKVKRLREWL 160
                          90       100       110
                  ....*....|....*....|....*....|...
gi 342187274 1149 -------KKVAMVGDGVNDSPALAQADMGVAIG 1174
Cdd:cd02612   161 aeegidlKDSYAYSDSINDLPMLEAVGHPVAVN 193
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
1094-1167 3.15e-03

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


Pssm-ID: 273653 [Multi-domain]  Cd Length: 177  Bit Score: 40.03  E-value: 3.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274  1094 AVHTLQSMGVDVVLITGDNRKTARAIATQVGINKVFA-----------------EVLPS--HKVAKVQELQNKGK----K 1150
Cdd:TIGR01488   81 LISWLKERGIDTVIVSGGFDFFVEPVAEKLGIDDVFAnrlefddnglltgpiegQVNPEgeCKGKVLKELLEESKitlkK 160
                           90
                   ....*....|....*..
gi 342187274  1151 VAMVGDGVNDSPALAQA 1167
Cdd:TIGR01488  161 IIAVGDSVNDLPMLKLA 177
PLN02957 PLN02957
copper, zinc superoxide dismutase
152-208 4.90e-03

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 40.12  E-value: 4.90e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 342187274  152 MTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEA-VITYQPYliqpEDLRDHVNDMGFEA 208
Cdd:PLN02957   14 MKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVrVLGSSPV----KAMTAALEQTGRKA 67
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
1131-1192 6.88e-03

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 39.91  E-value: 6.88e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 342187274  1131 EVLP--SHKVAKVQELQN----KGKKVAMVGDGVNDSPALAQADMGVAIGTGTDVAIEAADVVLIRND 1192
Cdd:pfam08282  180 EIMPkgVSKGTALKALAKhlniSLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVKAAADYVTDSNN 247
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
1088-1192 8.83e-03

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


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 38.96  E-value: 8.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187274 1088 KQEAALAVHTLQSMGVDVVLITGDNRKTARAIAtqVGINKVFAevlpshkVAKVQELQN-KGKKVAMVGDGVNDSPALAQ 1166
Cdd:COG0561    85 PEDVREILELLREHGLHLQVVVRSGPGFLEILP--KGVSKGSA-------LKKLAERLGiPPEEVIAFGDSGNDLEMLEA 155
                          90       100
                  ....*....|....*....|....*.
gi 342187274 1167 ADMGVAIGTGTDVAIEAADVVLIRND 1192
Cdd:COG0561   156 AGLGVAMGNAPPEVKAAADYVTGSND 181
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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