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Conserved domains on  [gi|446468755|ref|WP_000546609|]
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MULTISPECIES: potassium-transporting ATPase subunit KdpB [Staphylococcus]

Protein Classification

potassium-transporting ATPase subunit KdpB( domain architecture ID 11454791)

potassium-transporting ATPase subunit KdpB is part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm, and is distinguished from other transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle

EC:  7.2.2.6
Gene Symbol:  kdpB
SCOP:  4002228
TCDB:  3.A.3

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KdpB COG2216
K+ transport ATPase, ATPase subunit KdpB [Inorganic ion transport and metabolism];
2-674 0e+00

K+ transport ATPase, ATPase subunit KdpB [Inorganic ion transport and metabolism];


:

Pssm-ID: 441818  Cd Length: 683  Bit Score: 1117.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755   2 HHVNKYFNQTMVIEALKMSFYKLNPKQLIKNPIMFVVEVGMLLTLILICFPDIFGTSyLSRGYLITIFIILLITILFANF 81
Cdd:COG2216    6 RKKRSLFDPALLRRALKDAFRKLDPRVQIRNPVMFVVEVGAILTTVLTILDLLGGGG-GPAGFNLQITLWLWFTVLFANF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  82 SEAFAEGRGKAQADSLRQAQSNLTARLIEENGAYRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGESAP 161
Cdd:COG2216   85 AEALAEGRGKAQADSLRKTRTDTVARRLVDDGTEEEVPASELRKGDVVLVEAGDIIPGDGEVIEGVASVDESAITGESAP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 162 VIKESGGDFDGVIGGTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTPNEIALFTLLTTLTIIFLVVIVTLYPIAS 241
Cdd:COG2216  165 VIRESGGDRSAVTGGTRVLSDWIVVRITANPGESFLDRMIALVEGAKRQKTPNEIALTILLAGLTLIFLLVVVTLPPFAA 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 242 YLHLILPIAMLIALTVCLIPTTIGGLLSAIGIAGMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTITYGNRIASEFLP 321
Cdd:COG2216  245 YAGAPISVTVLIALLVCLIPTTIGGLLSAIGIAGMDRLVQANVIAMSGRAVEAAGDVDTLLLDKTGTITLGNRQASEFIP 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 322 VNQQMMEKLIVAAYMSSIYDDTPEGKSIVRLAKQMYIN--ELPKDIDGTYKPFTAETRMSGI-ITNEISVFKGAPNSMIN 398
Cdd:COG2216  325 VPGVSEEELADAAQLASLADETPEGRSIVVLAKERGGLreRDLAPLGAEFVPFTAQTRMSGVdLPGGREIRKGAADAIKA 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 399 LVKQQQGNIPLNIESICMDVSSKGGTPLIVIENNVMLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAK 478
Cdd:COG2216  405 YVRELGGTVPAELDAIVEEIARSGGTPLVVAEDARVLGVIYLKDIVKPGIKERFAELRRMGIRTVMITGDNPLTAAAIAA 484
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 479 EAGVDRFVAECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAANLIDLDSNPTKLIEVVK 558
Cdd:COG2216  485 EAGVDDFLAEATPEDKLALIRREQAEGRLVAMTGDGTNDAPALAQADVGVAMNSGTQAAKEAGNMVDLDSDPTKLIEIVE 564
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 559 IGKQLLMTRGALTTFSLANDVAKYFAILPALMMSTIPEMTSLNIMHLSSPKSAIISALIFNALIIVALIPIAMKGVKVKG 638
Cdd:COG2216  565 IGKQLLMTRGALTTFSIANDVAKYFAIIPALFAAAYPQLGALNIMGLASPQSAILSAVIFNALIIPALIPLALRGVKYRP 644
                        650       660       670
                 ....*....|....*....|....*....|....*.
gi 446468755 639 YSIDRIFINNMLIYGLGGLIVPFLGIKLIDMIVQFF 674
Cdd:COG2216  645 MSAAALLRRNLLIYGLGGLIVPFIGIKLIDLLLSAL 680
 
Name Accession Description Interval E-value
KdpB COG2216
K+ transport ATPase, ATPase subunit KdpB [Inorganic ion transport and metabolism];
2-674 0e+00

K+ transport ATPase, ATPase subunit KdpB [Inorganic ion transport and metabolism];


Pssm-ID: 441818  Cd Length: 683  Bit Score: 1117.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755   2 HHVNKYFNQTMVIEALKMSFYKLNPKQLIKNPIMFVVEVGMLLTLILICFPDIFGTSyLSRGYLITIFIILLITILFANF 81
Cdd:COG2216    6 RKKRSLFDPALLRRALKDAFRKLDPRVQIRNPVMFVVEVGAILTTVLTILDLLGGGG-GPAGFNLQITLWLWFTVLFANF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  82 SEAFAEGRGKAQADSLRQAQSNLTARLIEENGAYRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGESAP 161
Cdd:COG2216   85 AEALAEGRGKAQADSLRKTRTDTVARRLVDDGTEEEVPASELRKGDVVLVEAGDIIPGDGEVIEGVASVDESAITGESAP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 162 VIKESGGDFDGVIGGTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTPNEIALFTLLTTLTIIFLVVIVTLYPIAS 241
Cdd:COG2216  165 VIRESGGDRSAVTGGTRVLSDWIVVRITANPGESFLDRMIALVEGAKRQKTPNEIALTILLAGLTLIFLLVVVTLPPFAA 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 242 YLHLILPIAMLIALTVCLIPTTIGGLLSAIGIAGMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTITYGNRIASEFLP 321
Cdd:COG2216  245 YAGAPISVTVLIALLVCLIPTTIGGLLSAIGIAGMDRLVQANVIAMSGRAVEAAGDVDTLLLDKTGTITLGNRQASEFIP 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 322 VNQQMMEKLIVAAYMSSIYDDTPEGKSIVRLAKQMYIN--ELPKDIDGTYKPFTAETRMSGI-ITNEISVFKGAPNSMIN 398
Cdd:COG2216  325 VPGVSEEELADAAQLASLADETPEGRSIVVLAKERGGLreRDLAPLGAEFVPFTAQTRMSGVdLPGGREIRKGAADAIKA 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 399 LVKQQQGNIPLNIESICMDVSSKGGTPLIVIENNVMLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAK 478
Cdd:COG2216  405 YVRELGGTVPAELDAIVEEIARSGGTPLVVAEDARVLGVIYLKDIVKPGIKERFAELRRMGIRTVMITGDNPLTAAAIAA 484
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 479 EAGVDRFVAECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAANLIDLDSNPTKLIEVVK 558
Cdd:COG2216  485 EAGVDDFLAEATPEDKLALIRREQAEGRLVAMTGDGTNDAPALAQADVGVAMNSGTQAAKEAGNMVDLDSDPTKLIEIVE 564
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 559 IGKQLLMTRGALTTFSLANDVAKYFAILPALMMSTIPEMTSLNIMHLSSPKSAIISALIFNALIIVALIPIAMKGVKVKG 638
Cdd:COG2216  565 IGKQLLMTRGALTTFSIANDVAKYFAIIPALFAAAYPQLGALNIMGLASPQSAILSAVIFNALIIPALIPLALRGVKYRP 644
                        650       660       670
                 ....*....|....*....|....*....|....*.
gi 446468755 639 YSIDRIFINNMLIYGLGGLIVPFLGIKLIDMIVQFF 674
Cdd:COG2216  645 MSAAALLRRNLLIYGLGGLIVPFIGIKLIDLLLSAL 680
P-type_ATPase_K cd02078
potassium-transporting ATPase ATP-binding subunit, KdpB, a subunit of the prokaryotic ...
9-674 0e+00

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: 988.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755   9 NQTMVIEALKMSFYKLNPKQLIKNPIMFVVEVGMLLTLiLICFPDIFGTSYLSRGYLITIFIILLITILFANFSEAFAEG 88
Cdd:cd02078    1 DKDIVKEAIKDSFKKLNPRVLAKNPVMFVVEIGSIITT-VLTFFPLLFSGGGPAGFNLAVSLWLWFTVLFANFAEAIAEG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  89 RGKAQADSLRQAQSNLTARLIEENGAYRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGESAPVIKESGG 168
Cdd:cd02078   80 RGKAQADSLRKTKTETQAKRLRNDGKIEKVPATDLKKGDIVLVEAGDIIPADGEVIEGVASVDESAITGESAPVIRESGG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 169 DFDGVIGGTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTPNEIALFTLLTTLTIIFLVVIVTLYPIASYLHLILP 248
Cdd:cd02078  160 DRSSVTGGTKVLSDRIKVRITANPGETFLDRMIALVEGASRQKTPNEIALTILLVGLTLIFLIVVATLPPFAEYSGAPVS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 249 IAMLIALTVCLIPTTIGGLLSAIGIAGMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTITYGNRIASEFLPVNQQMME 328
Cdd:cd02078  240 VTVLVALLVCLIPTTIGGLLSAIGIAGMDRLLRFNVIAKSGRAVEAAGDVDTLLLDKTGTITLGNRQATEFIPVGGVDEK 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 329 KLIVAAYMSSIYDDTPEGKSIVRLAKQMYINELPKDI-DGTYKPFTAETRMSGI-ITNEISVFKGAPNSMINLVKQQQGN 406
Cdd:cd02078  320 ELADAAQLASLADETPEGRSIVILAKQLGGTERDLDLsGAEFIPFSAETRMSGVdLPDGTEIRKGAVDAIRKYVRSLGGS 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 407 IPLNIESICMDVSSKGGTPLIVIENNVMLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEAGVDRFV 486
Cdd:cd02078  400 IPEELEAIVEEISKQGGTPLVVAEDDRVLGVIYLKDIIKPGIKERFAELRKMGIKTVMITGDNPLTAAAIAAEAGVDDFL 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 487 AECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAANLIDLDSNPTKLIEVVKIGKQLLMT 566
Cdd:cd02078  480 AEAKPEDKLELIRKEQAKGKLVAMTGDGTNDAPALAQADVGVAMNSGTQAAKEAGNMVDLDSDPTKLIEVVEIGKQLLMT 559
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 567 RGALTTFSLANDVAKYFAILPALMMSTIPEMTSLNIMHLSSPKSAIISALIFNALIIVALIPIAMKGVKVKGYSIDRIFI 646
Cdd:cd02078  560 RGALTTFSIANDVAKYFAIIPAMFAAAYPQLGALNIMHLASPYSAILSAVIFNALIIPALIPLALKGVKYRPLSASALLR 639
                        650       660
                 ....*....|....*....|....*...
gi 446468755 647 NNMLIYGLGGLIVPFLGIKLIDMIVQFF 674
Cdd:cd02078  640 RNLLIYGLGGIIVPFIGIKLIDMLITAL 667
PRK14010 PRK14010
K(+)-transporting ATPase subunit B;
1-675 0e+00

K(+)-transporting ATPase subunit B;


Pssm-ID: 184448 [Multi-domain]  Cd Length: 673  Bit Score: 873.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755   1 MHHVNKYFNQTMVIEALKMSFYKLNPKQLIKNPIMFVVEVGMLLTLILICFPDIFGTSYLSRGYLITIFIILLITILFAN 80
Cdd:PRK14010   1 MAETTKIFESHLVKQALKDSVLKLYPVYMIKNPIMFVVEVGMLLALGLTIYPDLFHQESVSRLYVFSIFIILLLTLVFAN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  81 FSEAFAEGRGKAQADSLRQAQSNLTARLIEENGAYRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGESA 160
Cdd:PRK14010  81 FSEALAEGRGKAQANALRQTQTEMKARRIKQDGSYEMIDASDLKKGHIVRVATGEQIPNDGKVIKGLATVDESAITGESA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 161 PVIKESGGDFDGVIGGTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTPNEIALFTLLTTLTIIFLVVIVTLYPIA 240
Cdd:PRK14010 161 PVIKESGGDFDNVIGGTSVASDWLEVEITSEPGHSFLDKMIGLVEGATRKKTPNEIALFTLLMTLTIIFLVVILTMYPLA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 241 SYLHLILPIAMLIALTVCLIPTTIGGLLSAIGIAGMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTITYGNRIASEFL 320
Cdd:PRK14010 241 KFLNFNLSIAMLIALAVCLIPTTIGGLLSAIGIAGMDRVTQFNILAKSGRSVETCGDVNVLILDKTGTITYGNRMADAFI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 321 PVNQQMMEKLIVAAYMSSIYDDTPEGKSIVRLAKQMYInELPKDiDGTYKPFTAETRMSGIITNEISVFKGAPNSMINLV 400
Cdd:PRK14010 321 PVKSSSFERLVKAAYESSIADDTPEGRSIVKLAYKQHI-DLPQE-VGEYIPFTAETRMSGVKFTTREVYKGAPNSMVKRV 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 401 KQQQGNIPLNIESICMDVSSKGGTPLIVIENNVMLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEA 480
Cdd:PRK14010 399 KEAGGHIPVDLDALVKGVSKKGGTPLVVLEDNEILGVIYLKDVIKDGLVERFRELREMGIETVMCTGDNELTAATIAKEA 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 481 GVDRFVAECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAANLIDLDSNPTKLIEVVKIG 560
Cdd:PRK14010 479 GVDRFVAECKPEDKINVIREEQAKGHIVAMTGDGTNDAPALAEANVGLAMNSGTMSAKEAANLIDLDSNPTKLMEVVLIG 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 561 KQLLMTRGALTTFSLANDVAKYFAILPALMMSTIPEMTSLNIMHLSSPKSAIISALIFNALIIVALIPIAMKGVKVKGYS 640
Cdd:PRK14010 559 KQLLMTRGSLTTFSIANDIAKYFAILPAMFMAAMPAMNHLNIMHLHSPESAVLSALIFNALIIVLLIPIAMKGVKFKGAS 638
                        650       660       670
                 ....*....|....*....|....*....|....*
gi 446468755 641 IDRIFINNMLIYGLGGLIVPFLGIKLIDMIVQFFV 675
Cdd:PRK14010 639 TQTILMKNMLVYGLGGMIVPFIGIKLIDLIIQLFV 673
kdpB TIGR01497
K+-transporting ATPase, B subunit; This model describes the P-type ATPase subunit of the ...
6-671 0e+00

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


Pssm-ID: 130561 [Multi-domain]  Cd Length: 675  Bit Score: 837.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755    6 KYFNQTMVIEALKMSFYKLNPKQLIKNPIMFVVEVGMLLTLILICFPDIFGTS-YLSRGYLITIFIILLITILFANFSEA 84
Cdd:TIGR01497   6 KLFTKTIVVQAIKEAFKKLNPKAQWRNPVMFIVWVGSLLTTCITIAPASFGMPgNNLALFNAIITGILFITVLFANFAEA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755   85 FAEGRGKAQADSLRQAQSNLTARLIEENGAYRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGESAPVIK 164
Cdd:TIGR01497  86 VAEGRGKAQADSLKGTKKTTFAKLLRDDGAIDKVPADQLKKGDIVLVEAGDVIPCDGEVIEGVASVDESAITGESAPVIK 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  165 ESGGDFDGVIGGTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTPNEIALFTLLTTLTIIFLVVIVTLYPIASYLH 244
Cdd:TIGR01497 166 ESGGDFASVTGGTRILSDWLVVECTANPGETFLDRMIALVEGAQRRKTPNEIALTILLIALTLVFLLVTATLWPFAAYGG 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  245 LILPIAMLIALTVCLIPTTIGGLLSAIGIAGMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTITYGNRIASEFLPVNQ 324
Cdd:TIGR01497 246 NAISVTVLVALLVCLIPTTIGGLLSAIGIAGMDRVLGFNVIATSGRAVEACGDVDTLLLDKTGTITLGNRLASEFIPAQG 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  325 QMMEKLIVAAYMSSIYDDTPEGKSIVRLAKQMYINE-LPKDIDGTYKPFTAETRMSGI-ITNEISVFKGAPNSMINLVKQ 402
Cdd:TIGR01497 326 VDEKTLADAAQLASLADDTPEGKSIVILAKQLGIREdDVQSLHATFVEFTAQTRMSGInLDNGRMIRKGAVDAIKRHVEA 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  403 QQGNIPLNIESICMDVSSKGGTPLIVIENNVMLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEAGV 482
Cdd:TIGR01497 406 NGGHIPTDLDQAVDQVARQGGTPLVVCEDNRIYGVIYLKDIVKGGIKERFAQLRKMGIKTIMITGDNRLTAAAIAAEAGV 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  483 DRFVAECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAANLIDLDSNPTKLIEVVKIGKQ 562
Cdd:TIGR01497 486 DDFIAEATPEDKIALIRQEQAEGKLVAMTGDGTNDAPALAQADVGVAMNSGTQAAKEAANMVDLDSDPTKLIEVVHIGKQ 565
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  563 LLMTRGALTTFSLANDVAKYFAILPALMMSTIPEMTSLNIMHLSSPKSAIISALIFNALIIVALIPIAMKGVKVKGYSID 642
Cdd:TIGR01497 566 LLITRGALTTFSIANDVAKYFAIIPAIFAAAYPQLQALNIMCLHSPDSAILSALIFNALIIPALIPLALKGVSYRPLTAS 645
                         650       660
                  ....*....|....*....|....*....
gi 446468755  643 RIFINNMLIYGLGGLIVPFLGIKLIDMIV 671
Cdd:TIGR01497 646 ALLRRNLWIYGLGGLIVPFIGIKVIDLLI 674
E1-E2_ATPase pfam00122
E1-E2 ATPase;
105-278 4.14e-24

E1-E2 ATPase;


Pssm-ID: 425475 [Multi-domain]  Cd Length: 181  Bit Score: 99.95  E-value: 4.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  105 TARLIEeNGAYRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGESAPVIKESGgdfDGVIGGTLVTSDWL 184
Cdd:pfam00122   6 TATVLR-DGTEEEVPADELVPGDIVLLKPGERVPADGRIVEGSASVDESLLTGESLPVEKKKG---DMVYSGTVVVSGSA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  185 EIRVESEAGTSFLDKMIALVEGAERNKTPNEIALFTLLTTLTIIFLVVIVTLYPIASYLHLILPIAMLIALTVCL--IPT 262
Cdd:pfam00122  82 KAVVTATGEDTELGRIARLVEEAKSKKTPLQRLLDRLGKYFSPVVLLIALAVFLLWLFVGGPPLRALLRALAVLVaaCPC 161
                         170
                  ....*....|....*.
gi 446468755  263 TIGGLLSAIGIAGMDR 278
Cdd:pfam00122 162 ALPLATPLALAVGARR 177
 
Name Accession Description Interval E-value
KdpB COG2216
K+ transport ATPase, ATPase subunit KdpB [Inorganic ion transport and metabolism];
2-674 0e+00

K+ transport ATPase, ATPase subunit KdpB [Inorganic ion transport and metabolism];


Pssm-ID: 441818  Cd Length: 683  Bit Score: 1117.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755   2 HHVNKYFNQTMVIEALKMSFYKLNPKQLIKNPIMFVVEVGMLLTLILICFPDIFGTSyLSRGYLITIFIILLITILFANF 81
Cdd:COG2216    6 RKKRSLFDPALLRRALKDAFRKLDPRVQIRNPVMFVVEVGAILTTVLTILDLLGGGG-GPAGFNLQITLWLWFTVLFANF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  82 SEAFAEGRGKAQADSLRQAQSNLTARLIEENGAYRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGESAP 161
Cdd:COG2216   85 AEALAEGRGKAQADSLRKTRTDTVARRLVDDGTEEEVPASELRKGDVVLVEAGDIIPGDGEVIEGVASVDESAITGESAP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 162 VIKESGGDFDGVIGGTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTPNEIALFTLLTTLTIIFLVVIVTLYPIAS 241
Cdd:COG2216  165 VIRESGGDRSAVTGGTRVLSDWIVVRITANPGESFLDRMIALVEGAKRQKTPNEIALTILLAGLTLIFLLVVVTLPPFAA 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 242 YLHLILPIAMLIALTVCLIPTTIGGLLSAIGIAGMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTITYGNRIASEFLP 321
Cdd:COG2216  245 YAGAPISVTVLIALLVCLIPTTIGGLLSAIGIAGMDRLVQANVIAMSGRAVEAAGDVDTLLLDKTGTITLGNRQASEFIP 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 322 VNQQMMEKLIVAAYMSSIYDDTPEGKSIVRLAKQMYIN--ELPKDIDGTYKPFTAETRMSGI-ITNEISVFKGAPNSMIN 398
Cdd:COG2216  325 VPGVSEEELADAAQLASLADETPEGRSIVVLAKERGGLreRDLAPLGAEFVPFTAQTRMSGVdLPGGREIRKGAADAIKA 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 399 LVKQQQGNIPLNIESICMDVSSKGGTPLIVIENNVMLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAK 478
Cdd:COG2216  405 YVRELGGTVPAELDAIVEEIARSGGTPLVVAEDARVLGVIYLKDIVKPGIKERFAELRRMGIRTVMITGDNPLTAAAIAA 484
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 479 EAGVDRFVAECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAANLIDLDSNPTKLIEVVK 558
Cdd:COG2216  485 EAGVDDFLAEATPEDKLALIRREQAEGRLVAMTGDGTNDAPALAQADVGVAMNSGTQAAKEAGNMVDLDSDPTKLIEIVE 564
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 559 IGKQLLMTRGALTTFSLANDVAKYFAILPALMMSTIPEMTSLNIMHLSSPKSAIISALIFNALIIVALIPIAMKGVKVKG 638
Cdd:COG2216  565 IGKQLLMTRGALTTFSIANDVAKYFAIIPALFAAAYPQLGALNIMGLASPQSAILSAVIFNALIIPALIPLALRGVKYRP 644
                        650       660       670
                 ....*....|....*....|....*....|....*.
gi 446468755 639 YSIDRIFINNMLIYGLGGLIVPFLGIKLIDMIVQFF 674
Cdd:COG2216  645 MSAAALLRRNLLIYGLGGLIVPFIGIKLIDLLLSAL 680
P-type_ATPase_K cd02078
potassium-transporting ATPase ATP-binding subunit, KdpB, a subunit of the prokaryotic ...
9-674 0e+00

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: 988.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755   9 NQTMVIEALKMSFYKLNPKQLIKNPIMFVVEVGMLLTLiLICFPDIFGTSYLSRGYLITIFIILLITILFANFSEAFAEG 88
Cdd:cd02078    1 DKDIVKEAIKDSFKKLNPRVLAKNPVMFVVEIGSIITT-VLTFFPLLFSGGGPAGFNLAVSLWLWFTVLFANFAEAIAEG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  89 RGKAQADSLRQAQSNLTARLIEENGAYRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGESAPVIKESGG 168
Cdd:cd02078   80 RGKAQADSLRKTKTETQAKRLRNDGKIEKVPATDLKKGDIVLVEAGDIIPADGEVIEGVASVDESAITGESAPVIRESGG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 169 DFDGVIGGTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTPNEIALFTLLTTLTIIFLVVIVTLYPIASYLHLILP 248
Cdd:cd02078  160 DRSSVTGGTKVLSDRIKVRITANPGETFLDRMIALVEGASRQKTPNEIALTILLVGLTLIFLIVVATLPPFAEYSGAPVS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 249 IAMLIALTVCLIPTTIGGLLSAIGIAGMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTITYGNRIASEFLPVNQQMME 328
Cdd:cd02078  240 VTVLVALLVCLIPTTIGGLLSAIGIAGMDRLLRFNVIAKSGRAVEAAGDVDTLLLDKTGTITLGNRQATEFIPVGGVDEK 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 329 KLIVAAYMSSIYDDTPEGKSIVRLAKQMYINELPKDI-DGTYKPFTAETRMSGI-ITNEISVFKGAPNSMINLVKQQQGN 406
Cdd:cd02078  320 ELADAAQLASLADETPEGRSIVILAKQLGGTERDLDLsGAEFIPFSAETRMSGVdLPDGTEIRKGAVDAIRKYVRSLGGS 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 407 IPLNIESICMDVSSKGGTPLIVIENNVMLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEAGVDRFV 486
Cdd:cd02078  400 IPEELEAIVEEISKQGGTPLVVAEDDRVLGVIYLKDIIKPGIKERFAELRKMGIKTVMITGDNPLTAAAIAAEAGVDDFL 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 487 AECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAANLIDLDSNPTKLIEVVKIGKQLLMT 566
Cdd:cd02078  480 AEAKPEDKLELIRKEQAKGKLVAMTGDGTNDAPALAQADVGVAMNSGTQAAKEAGNMVDLDSDPTKLIEVVEIGKQLLMT 559
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 567 RGALTTFSLANDVAKYFAILPALMMSTIPEMTSLNIMHLSSPKSAIISALIFNALIIVALIPIAMKGVKVKGYSIDRIFI 646
Cdd:cd02078  560 RGALTTFSIANDVAKYFAIIPAMFAAAYPQLGALNIMHLASPYSAILSAVIFNALIIPALIPLALKGVKYRPLSASALLR 639
                        650       660
                 ....*....|....*....|....*...
gi 446468755 647 NNMLIYGLGGLIVPFLGIKLIDMIVQFF 674
Cdd:cd02078  640 RNLLIYGLGGIIVPFIGIKLIDMLITAL 667
PRK14010 PRK14010
K(+)-transporting ATPase subunit B;
1-675 0e+00

K(+)-transporting ATPase subunit B;


Pssm-ID: 184448 [Multi-domain]  Cd Length: 673  Bit Score: 873.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755   1 MHHVNKYFNQTMVIEALKMSFYKLNPKQLIKNPIMFVVEVGMLLTLILICFPDIFGTSYLSRGYLITIFIILLITILFAN 80
Cdd:PRK14010   1 MAETTKIFESHLVKQALKDSVLKLYPVYMIKNPIMFVVEVGMLLALGLTIYPDLFHQESVSRLYVFSIFIILLLTLVFAN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  81 FSEAFAEGRGKAQADSLRQAQSNLTARLIEENGAYRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGESA 160
Cdd:PRK14010  81 FSEALAEGRGKAQANALRQTQTEMKARRIKQDGSYEMIDASDLKKGHIVRVATGEQIPNDGKVIKGLATVDESAITGESA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 161 PVIKESGGDFDGVIGGTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTPNEIALFTLLTTLTIIFLVVIVTLYPIA 240
Cdd:PRK14010 161 PVIKESGGDFDNVIGGTSVASDWLEVEITSEPGHSFLDKMIGLVEGATRKKTPNEIALFTLLMTLTIIFLVVILTMYPLA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 241 SYLHLILPIAMLIALTVCLIPTTIGGLLSAIGIAGMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTITYGNRIASEFL 320
Cdd:PRK14010 241 KFLNFNLSIAMLIALAVCLIPTTIGGLLSAIGIAGMDRVTQFNILAKSGRSVETCGDVNVLILDKTGTITYGNRMADAFI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 321 PVNQQMMEKLIVAAYMSSIYDDTPEGKSIVRLAKQMYInELPKDiDGTYKPFTAETRMSGIITNEISVFKGAPNSMINLV 400
Cdd:PRK14010 321 PVKSSSFERLVKAAYESSIADDTPEGRSIVKLAYKQHI-DLPQE-VGEYIPFTAETRMSGVKFTTREVYKGAPNSMVKRV 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 401 KQQQGNIPLNIESICMDVSSKGGTPLIVIENNVMLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEA 480
Cdd:PRK14010 399 KEAGGHIPVDLDALVKGVSKKGGTPLVVLEDNEILGVIYLKDVIKDGLVERFRELREMGIETVMCTGDNELTAATIAKEA 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 481 GVDRFVAECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAANLIDLDSNPTKLIEVVKIG 560
Cdd:PRK14010 479 GVDRFVAECKPEDKINVIREEQAKGHIVAMTGDGTNDAPALAEANVGLAMNSGTMSAKEAANLIDLDSNPTKLMEVVLIG 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 561 KQLLMTRGALTTFSLANDVAKYFAILPALMMSTIPEMTSLNIMHLSSPKSAIISALIFNALIIVALIPIAMKGVKVKGYS 640
Cdd:PRK14010 559 KQLLMTRGSLTTFSIANDIAKYFAILPAMFMAAMPAMNHLNIMHLHSPESAVLSALIFNALIIVLLIPIAMKGVKFKGAS 638
                        650       660       670
                 ....*....|....*....|....*....|....*
gi 446468755 641 IDRIFINNMLIYGLGGLIVPFLGIKLIDMIVQFFV 675
Cdd:PRK14010 639 TQTILMKNMLVYGLGGMIVPFIGIKLIDLIIQLFV 673
kdpB TIGR01497
K+-transporting ATPase, B subunit; This model describes the P-type ATPase subunit of the ...
6-671 0e+00

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


Pssm-ID: 130561 [Multi-domain]  Cd Length: 675  Bit Score: 837.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755    6 KYFNQTMVIEALKMSFYKLNPKQLIKNPIMFVVEVGMLLTLILICFPDIFGTS-YLSRGYLITIFIILLITILFANFSEA 84
Cdd:TIGR01497   6 KLFTKTIVVQAIKEAFKKLNPKAQWRNPVMFIVWVGSLLTTCITIAPASFGMPgNNLALFNAIITGILFITVLFANFAEA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755   85 FAEGRGKAQADSLRQAQSNLTARLIEENGAYRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGESAPVIK 164
Cdd:TIGR01497  86 VAEGRGKAQADSLKGTKKTTFAKLLRDDGAIDKVPADQLKKGDIVLVEAGDVIPCDGEVIEGVASVDESAITGESAPVIK 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  165 ESGGDFDGVIGGTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTPNEIALFTLLTTLTIIFLVVIVTLYPIASYLH 244
Cdd:TIGR01497 166 ESGGDFASVTGGTRILSDWLVVECTANPGETFLDRMIALVEGAQRRKTPNEIALTILLIALTLVFLLVTATLWPFAAYGG 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  245 LILPIAMLIALTVCLIPTTIGGLLSAIGIAGMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTITYGNRIASEFLPVNQ 324
Cdd:TIGR01497 246 NAISVTVLVALLVCLIPTTIGGLLSAIGIAGMDRVLGFNVIATSGRAVEACGDVDTLLLDKTGTITLGNRLASEFIPAQG 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  325 QMMEKLIVAAYMSSIYDDTPEGKSIVRLAKQMYINE-LPKDIDGTYKPFTAETRMSGI-ITNEISVFKGAPNSMINLVKQ 402
Cdd:TIGR01497 326 VDEKTLADAAQLASLADDTPEGKSIVILAKQLGIREdDVQSLHATFVEFTAQTRMSGInLDNGRMIRKGAVDAIKRHVEA 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  403 QQGNIPLNIESICMDVSSKGGTPLIVIENNVMLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEAGV 482
Cdd:TIGR01497 406 NGGHIPTDLDQAVDQVARQGGTPLVVCEDNRIYGVIYLKDIVKGGIKERFAQLRKMGIKTIMITGDNRLTAAAIAAEAGV 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  483 DRFVAECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAANLIDLDSNPTKLIEVVKIGKQ 562
Cdd:TIGR01497 486 DDFIAEATPEDKIALIRQEQAEGKLVAMTGDGTNDAPALAQADVGVAMNSGTQAAKEAANMVDLDSDPTKLIEVVHIGKQ 565
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  563 LLMTRGALTTFSLANDVAKYFAILPALMMSTIPEMTSLNIMHLSSPKSAIISALIFNALIIVALIPIAMKGVKVKGYSID 642
Cdd:TIGR01497 566 LLITRGALTTFSIANDVAKYFAIIPAIFAAAYPQLQALNIMCLHSPDSAILSALIFNALIIPALIPLALKGVSYRPLTAS 645
                         650       660
                  ....*....|....*....|....*....
gi 446468755  643 RIFINNMLIYGLGGLIVPFLGIKLIDMIV 671
Cdd:TIGR01497 646 ALLRRNLWIYGLGGLIVPFIGIKVIDLLI 674
ATPase_P-type TIGR01494
ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large ...
79-603 8.93e-97

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: 308.48  E-value: 8.93e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755   79 ANFSEAFAEGRGKAQADSLRQAQSNLTARLIEENGAYRIvNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGE 158
Cdd:TIGR01494   9 FVLLEVKQKLKAEDALRSLKDSLVNTATVLVLRNGWKEI-SSKDLVPGDVVLVKSGDTVPADGVLLSGSAFVDESSLTGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  159 SAPVIKESGGDFDGVIGGTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTPNEIALFTLLTTLTIIFLVVIVTLYP 238
Cdd:TIGR01494  88 SLPVLKTALPDGDAVFAGTINFGGTLIVKVTATGILTTVGKIAVVVYTGFSTKTPLQSKADKFENFIFILFLLLLALAVF 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  239 IASYLHLILPIAML------IALTVCLIPTTIGGLLSAIGIAGMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTITYG 312
Cdd:TIGR01494 168 LLLPIGGWDGNSIYkailraLAVLVIAIPCALPLAVSVALAVGDARMAKKGILVKNLNALEELGKVDVICFDKTGTLTTN 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  313 NRIASEFLPVNQQMMEKLIVAAYMSSIYDDT--PEGKSIVRLAKQMYINELPKDIDGTYK--PFTAETRMSGII-----T 383
Cdd:TIGR01494 248 KMTLQKVIIIGGVEEASLALALLAASLEYLSghPLERAIVKSAEGVIKSDEINVEYKILDvfPFSSVLKRMGVIveganG 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  384 NEISVFKGAPNSMINLVKQQqgnipLNIESICMDVSSKGGTPLIVIENNV-----MLGVIYLKDVIKDGLVERFAELRKM 458
Cdd:TIGR01494 328 SDLLFVKGAPEFVLERCNNE-----NDYDEKVDEYARQGLRVLAFASKKLpddleFLGLLTFEDPLRPDAKETIEALRKA 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  459 GIETVMCTGDNALTAATIAKEAGVDrFVAECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTIsAK 538
Cdd:TIGR01494 403 GIKVVMLTGDNVLTAKAIAKELGID-VFARVKPEEKAAIVEALQEKGRTVAMTGDGVNDAPALKKADVGIAMGSGDV-AK 480
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446468755  539 EAANLIDLDSNPTKLIEVVKIGKQLLMTRGALTTFSLANDVAKYFAILPALMMSTIPEMTSLNIM 603
Cdd:TIGR01494 481 AAADIVLLDDDLSTIVEAVKEGRKTFSNIKKNIFWAIAYNLILIPLALLLIVIILLPPLLAALAL 545
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
83-562 8.50e-96

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 310.92  E-value: 8.50e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  83 EAFAEGRGKAQADSLRQAQSNlTARLIEeNGAYRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGESAPV 162
Cdd:COG2217  193 EARAKGRARAAIRALLSLQPK-TARVLR-DGEEVEVPVEELRVGDRVLVRPGERIPVDGVVLEGESSVDESMLTGESLPV 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 163 IKESGgdfDGVIGGTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTPneialftllttltiiflvvIVTLY-PIAS 241
Cdd:COG2217  271 EKTPG---DEVFAGTINLDGSLRVRVTKVGSDTTLARIIRLVEEAQSSKAP-------------------IQRLAdRIAR 328
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 242 YLhliLPIAMLIALTVCLIPTTIGGLLS----------------AIGIA-------GMDRVTQFNVLAKSGRAVEVCGDV 298
Cdd:COG2217  329 YF---VPAVLAIAALTFLVWLLFGGDFStalyravavlviacpcALGLAtptaimvGTGRAARRGILIKGGEALERLAKV 405
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 299 DVMILDKTGTITYGNRIASEFLPVNQQMMEKLI-VAAYMSSiYDDTPEGKSIVRLAKQMYINELPkdIDGtykpFTAETR 377
Cdd:COG2217  406 DTVVFDKTGTLTEGKPEVTDVVPLDGLDEDELLaLAAALEQ-GSEHPLARAIVAAAKERGLELPE--VED----FEAIPG 478
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 378 --MSGIITNEiSVFKGAPNsminLVKQQQGNIPLNIESICMDVSSKGGTPLIVIENNVMLGVIYLKDVIKDGLVERFAEL 455
Cdd:COG2217  479 kgVEATVDGK-RVLVGSPR----LLEEEGIDLPEALEERAEELEAEGKTVVYVAVDGRLLGLIALADTLRPEAAEAIAAL 553
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 456 RKMGIETVMCTGDNALTAATIAKEAGVDRFVAECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTI 535
Cdd:COG2217  554 KALGIRVVMLTGDNERTAEAVARELGIDEVRAEVLPEDKAAAVRELQAQGKKVAMVGDGINDAPALAAADVGIAMGSGTD 633
                        490       500
                 ....*....|....*....|....*..
gi 446468755 536 SAKEAANLIDLDSNPTKLIEVVKIGKQ 562
Cdd:COG2217  634 VAIEAADIVLMRDDLRGVPDAIRLSRA 660
P-type_ATPase_Cu-like cd02094
P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A ...
105-561 8.48e-85

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: 279.75  E-value: 8.48e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 105 TARLIEENGAyRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGESAPVIKESGgdfDGVIGGTLVTSDWL 184
Cdd:cd02094  140 TARVIRDGKE-VEVPIEEVQVGDIVRVRPGEKIPVDGVVVEGESSVDESMLTGESLPVEKKPG---DKVIGGTINGNGSL 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 185 EIRVESEAGTSFLDKMIALVEGAERNKTP-----NEIALFTllttltiiflVVIVTLYPIASYL--HLILP-----IAML 252
Cdd:cd02094  216 LVRATRVGADTTLAQIIRLVEEAQGSKAPiqrlaDRVSGVF----------VPVVIAIAILTFLvwLLLGPepaltFALV 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 253 IALTVCLI----------PTTIggllsaigIAGMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTITYGNRIASEFLPV 322
Cdd:cd02094  286 AAVAVLVIacpcalglatPTAI--------MVGTGRAAELGILIKGGEALERAHKVDTVVFDKTGTLTEGKPEVTDVVPL 357
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 323 NQQMMEKLIVAAYMSSIYDDTPEGKSIVRLAKQMYINELPKDIdgtykpFTAETR--MSGIItNEISVFKGAPNSMinlv 400
Cdd:cd02094  358 PGDDEDELLRLAASLEQGSEHPLAKAIVAAAKEKGLELPEVED------FEAIPGkgVRGTV-DGRRVLVGNRRLM---- 426
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 401 kQQQGNIPLNIESICMDVSSKGGTPLIVIENNVMLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEA 480
Cdd:cd02094  427 -EENGIDLSALEAEALALEEEGKTVVLVAVDGELAGLIAVADPLKPDAAEAIEALKKMGIKVVMLTGDNRRTARAIAKEL 505
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 481 GVDRFVAECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAANLIDLDSNPTKLIEVVKIG 560
Cdd:cd02094  506 GIDEVIAEVLPEDKAEKVKKLQAQGKKVAMVGDGINDAPALAQADVGIAIGSGTDVAIESADIVLMRGDLRGVVTAIDLS 585

                 .
gi 446468755 561 K 561
Cdd:cd02094  586 R 586
ATPase-IB_hvy TIGR01525
heavy metal translocating P-type ATPase; This model encompasses two equivalog models for the ...
79-616 9.74e-83

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: 271.81  E-value: 9.74e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755   79 ANFSEAFAEGRGKAQADSLRQAQSNlTARLIEENGAYRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGE 158
Cdd:TIGR01525  31 GETLEERAKSRASDALSALLALAPS-TARVLQGDGSEEEVPVEELQVGDIVIVRPGERIPVDGVVISGESEVDESALTGE 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  159 SAPVIKESGgdfDGVIGGTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTP-----NEIALFTLLTTLTIIFLVVI 233
Cdd:TIGR01525 110 SMPVEKKEG---DEVFAGTINGDGSLTIRVTKLGEDSTLAQIVELVEEAQSSKAPiqrlaDRIASYYVPAVLAIALLTFV 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  234 VTLYPIASYLH-LILPIAMLIALTVCLI----PTTIgglLSAIGIAgmdrvTQFNVLAKSGRAVEVCGDVDVMILDKTGT 308
Cdd:TIGR01525 187 VWLALGALWREaLYRALTVLVVACPCALglatPVAI---LVAIGAA-----ARRGILIKGGDALEKLAKVKTVVFDKTGT 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  309 ITYGNRIASEFLPVNQQMMEKLI-VAAYMSSiYDDTPEGKSIVRLAKQMYINELPKDIdgTYKPftaETRMSGIITNEIS 387
Cdd:TIGR01525 259 LTTGKPTVVDIEPLDDASEEELLaLAAALEQ-SSSHPLARAIVRYAKERGLELPPEDV--EEVP---GKGVEATVDGGRE 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  388 VFKGAPNSMINLVKQQQGNIPLNIESICMdvSSKGGTPLIVIENNVMLGVIYLKDVIKDGLVERFAELRKMG-IETVMCT 466
Cdd:TIGR01525 333 VRIGNPRFLGNRELAIEPISASPDLLNEG--ESQGKTVVFVAVDGELLGVIALRDQLRPEAKEAIAALKRAGgIKLVMLT 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  467 GDNALTAATIAKEAGVDR-FVAECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAANLID 545
Cdd:TIGR01525 411 GDNRSAAEAVAAELGIDDeVHAELLPEDKLAIVKKLQEEGGPVAMVGDGINDAPALAAADVGIAMGSGSDVAIEAADIVL 490
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446468755  546 LDSNPTKLIEVVKIGKQllMTRGALTTFSLANdVAKYFAILPALMMSTIPEMTSLniMHLSSPKSAIISAL 616
Cdd:TIGR01525 491 LNDDLRSLPTAIDLSRK--TRRIIKQNLAWAL-GYNLVAIPLAAGGLLPLWLAVL--LHEGSTVLVVLNSL 556
P-type_ATPase_HM cd02079
P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) ...
85-562 3.41e-79

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: 264.08  E-value: 3.41e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  85 FAEGRGKAQAdslRQAQSNLTA-----RLIEENGAYRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGES 159
Cdd:cd02079  103 YLEERARSRA---RSALKALLSlapetATVLEDGSTEEVPVDDLKVGDVVLVKPGERIPVDGVVVSGESSVDESSLTGES 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 160 APVIKESGgdfDGVIGGTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTP-----NEIALFTLLTTLTIIFLVVIV 234
Cdd:cd02079  180 LPVEKGAG---DTVFAGTINLNGPLTIEVTKTGEDTTLAKIIRLVEEAQSSKPPlqrlaDRFARYFTPAVLVLAALVFLF 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 235 TLYPIASYLHlilpiAMLIALTVCLI----------PTTIgglLSAIGIAGmdrvtQFNVLAKSGRAVEVCGDVDVMILD 304
Cdd:cd02079  257 WPLVGGPPSL-----ALYRALAVLVVacpcalglatPTAI---VAGIGRAA-----RKGILIKGGDVLETLAKVDTVAFD 323
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 305 KTGTITYGNRIASEFLPVNQQMMEKLIVAAYMSSIYDDTPEGKSIVRLAKQMyinELPKDIDGTYKPFTAETRMSGIITN 384
Cdd:cd02079  324 KTGTLTEGKPEVTEIEPLEGFSEDELLALAAALEQHSEHPLARAIVEAAEEK---GLPPLEVEDVEEIPGKGISGEVDGR 400
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 385 EISVfkGAPNSMINLVKQQQgniplniesICMDVSSKGGTPLIVIENNVMLGVIYLKDVIKDGLVERFAELRKMGIETVM 464
Cdd:cd02079  401 EVLI--GSLSFAEEEGLVEA---------ADALSDAGKTSAVYVGRDGKLVGLFALEDQLRPEAKEVIAELKSGGIKVVM 469
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 465 CTGDNALTAATIAKEAGVDRFVAECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAANLI 544
Cdd:cd02079  470 LTGDNEAAAQAVAKELGIDEVHAGLLPEDKLAIVKALQAEGGPVAMVGDGINDAPALAQADVGIAMGSGTDVAIETADIV 549
                        490
                 ....*....|....*...
gi 446468755 545 DLDSNPTKLIEVVKIGKQ 562
Cdd:cd02079  550 LLSNDLSKLPDAIRLARR 567
ATPase-IB2_Cd TIGR01512
heavy metal-(Cd/Co/Hg/Pb/Zn)-translocating P-type ATPase; This model describes the P-type ...
79-590 2.86e-76

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: 254.56  E-value: 2.86e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755   79 ANFSEAFAEGRGKAQADSLRqAQSNLTARLIEeNGAYRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGE 158
Cdd:TIGR01512  31 GETLEEYASGRARRALKALM-ELAPDTARRLQ-GDSLEEVAVEELKVGDVVVVKPGERVPVDGEVLSGTSSVDESALTGE 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  159 SAPVIKESGgdfDGVIGGTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTPNE-----IALFTLLTTLTIIFLVVI 233
Cdd:TIGR01512 109 SVPVEKAPG---DEVFAGAINLDGVLTIEVTKLPADSTIAKIVNLVEEAQSRKAPTQrfidrFARYYTPAVLAIALAAAL 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  234 VTLYPIASYLHLILPIAM--LIALTVC-LIPTTIGGLLSAIGIAGmdrvtQFNVLAKSGRAVEVCGDVDVMILDKTGTIT 310
Cdd:TIGR01512 186 VPPLLGAGPFLEWIYRALvlLVVASPCaLVISAPAAYLSAISAAA-----RHGILIKGGAALEALAKIKTVAFDKTGTLT 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  311 YGNRIASEFLPVNQQMMEKLI-VAAYMSSiYDDTPEGKSIVRLAKQMyinelpkDIDGTYKPFTAETRMsGII--TNEIS 387
Cdd:TIGR01512 261 TGKPKVTDVHPADGHSESEVLrLAAAAEQ-GSTHPLARAIVDYARAR-------ELAPPVEDVEEVPGE-GVRavVDGGE 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  388 VFKGAPNSminlvkqqqgnIPLNIESICMDVSSKGGTPLIVIENNVMLGVIYLKDVIKDGLVERFAELRKMGIE-TVMCT 466
Cdd:TIGR01512 332 VRIGNPRS-----------LSEAVGASIAVPESAGKTIVLVARDGTLLGYIALSDELRPDAAEAIAELKALGIKrLVMLT 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  467 GDNALTAATIAKEAGVDRFVAECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAM-NSGTISAKEAANLID 545
Cdd:TIGR01512 401 GDRRAVAEAVARELGIDEVHAELLPEDKLEIVKELREKAGPVAMVGDGINDAPALAAADVGIAMgASGSDVALETADVVL 480
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 446468755  546 LDSNPTKLIEVVKIGKQllMTRGAL--TTFSLAndvAKYFAILPALM 590
Cdd:TIGR01512 481 LNDDLSRLPQAIRLARR--TRRIIKqnVVIALG---IILVLILLALF 522
P-type_ATPase_HM_ZosA_PfeT-like cd07551
P-type heavy metal-transporting ATPase, similar to Bacillus subtilis ZosA/PfeT which ...
79-563 4.51e-76

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: 255.64  E-value: 4.51e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  79 ANFSEAFAEGRGKAQADSLRQAQSNlTARLIEENGAYRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGE 158
Cdd:cd07551   88 SHALEDYAMGRSKRAITALMQLAPE-TARRIQRDGEIEEVPVEELQIGDRVQVRPGERVPADGVILSGSSSIDEASITGE 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 159 SAPVIKESGgdfDGVIGGTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTPneIALFTLLTTLTIIFLVVIVTLYP 238
Cdd:cd07551  167 SIPVEKTPG---DEVFAGTINGSGALTVRVTKLSSDTVFAKIVQLVEEAQSEKSP--TQSFIERFERIYVKGVLLAVLLL 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 239 IASYlHLILP----------IAMLIALTVC-LIPTTIGGLLSAIGIAGmdrvtQFNVLAKSGRAVEVCGDVDVMILDKTG 307
Cdd:cd07551  242 LLLP-PFLLGwtwadsfyraMVFLVVASPCaLVASTPPATLSAIANAA-----RQGVLFKGGVHLENLGSVKAIAFDKTG 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 308 TITYGNRIASEFLPVNQQMMEKLIVAAYMSSIYDDTPEGKSIVRLAKQMYINELP----KDIDGtyKPFTAETRMSGIIT 383
Cdd:cd07551  316 TLTEGKPRVTDVIPAEGVDEEELLQVAAAAESQSEHPLAQAIVRYAEERGIPRLPaievEAVTG--KGVTATVDGQTYRI 393
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 384 NEISVFKGAPnsminlvkqqqgnIPLNIESICMDVSSKGGTPLIVIENNVMLGVIYLKDVIKDGLVERFAELRKMGIETV 463
Cdd:cd07551  394 GKPGFFGEVG-------------IPSEAAALAAELESEGKTVVYVARDDQVVGLIALMDTPRPEAKEAIAALRLGGIKTI 460
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 464 MCTGDNALTAATIAKEAGVDRFVAECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAANL 543
Cdd:cd07551  461 MLTGDNERTAEAVAKELGIDEVVANLLPEDKVAIIRELQQEYGTVAMVGDGINDAPALANADVGIAMGAGTDVALETADV 540
                        490       500
                 ....*....|....*....|
gi 446468755 544 IDLDSNPTKLIEVVKIGKQL 563
Cdd:cd07551  541 VLMKDDLSKLPYAIRLSRKM 560
ATPase-IB1_Cu TIGR01511
copper-(or silver)-translocating P-type ATPase; This model describes the P-type ATPase ...
89-550 4.02e-70

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: 238.33  E-value: 4.02e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755   89 RGKAQAdslrqAQSNL------TARLIEENGAYRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGESAPV 162
Cdd:TIGR01511  75 KGRASD-----ALSKLaklqpsTATLLTKDGSIEEVPVALLQPGDIVKVLPGEKIPVDGTVIEGESEVDESLVTGESLPV 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  163 IKESGgdfDGVIGGTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTPNE-IALFTLLTTLTIIFLVVIVTLypias 241
Cdd:TIGR01511 150 PKKVG---DPVIAGTVNGTGSLVVRATATGEDTTLAQIVRLVRQAQQSKAPIQrLADKVAGYFVPVVIAIALITF----- 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  242 ylhLILPIAMLIALTVCLI--PTTIG-----GLLSAIGIAgmdrvTQFNVLAKSGRAVEVCGDVDVMILDKTGTITYGNR 314
Cdd:TIGR01511 222 ---VIWLFALEFAVTVLIIacPCALGlatptVIAVATGLA-----AKNGVLIKDGDALERAANIDTVVFDKTGTLTQGKP 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  315 IASEFLPVNQqmMEKLIVAAYMSSI--YDDTPEGKSIVRLAKQMYInelpkdidgtykpftAETRMSGIITNEISVFKGA 392
Cdd:TIGR01511 294 TVTDVHVFGD--RDRTELLALAAALeaGSEHPLAKAIVSYAKEKGI---------------TLVTVSDFKAIPGIGVEGT 356
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  393 PNS-MINLVKQ---QQGNIPLNIEsicmdvSSKGGTPLIVIENNVMLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGD 468
Cdd:TIGR01511 357 VEGtKIQLGNEkllGENAIKIDGK------AGQGSTVVLVAVNGELAGVFALEDQLRPEAKEVIQALKRRGIEPVMLTGD 430
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  469 NALTAATIAKEAGVDrFVAECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAANLIDLDS 548
Cdd:TIGR01511 431 NRKTAKAVAKELGID-VRAEVLPDDKAALIKKLQEKGPVVAMVGDGINDAPALAQADVGIAIGAGTDVAIEAADVVLLRN 509

                  ..
gi 446468755  549 NP 550
Cdd:TIGR01511 510 DL 511
P-type_ATPase_Cd-like cd07545
P-type heavy metal-transporting ATPase, similar to Staphylococcus aureus plasmid pI258 CadA, a ...
108-597 2.74e-65

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: 226.15  E-value: 2.74e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 108 LIEENGAYRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGESAPVIKESGgdfDGVIGGTLVTSDWLEIR 187
Cdd:cd07545   99 LVRRDGQEREVPVAEVAVGDRMIVRPGERIAMDGIIVRGESSVNQAAITGESLPVEKGVG---DEVFAGTLNGEGALEVR 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 188 VESEAGTSFLDKMIALVEGAERNKTPNE-----IALFTLLTTLTIIFLVVIVT-LYPIASYLHLILP-IAMLIALTVC-L 259
Cdd:cd07545  176 VTKPAEDSTIARIIHLVEEAQAERAPTQafvdrFARYYTPVVMAIAALVAIVPpLFFGGAWFTWIYRgLALLVVACPCaL 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 260 IPTTIGGLLSAIGIAGmdrvtQFNVLAKSGRAVEVCGDVDVMILDKTGTITYGNRIASEFLPVNQQMMEKLIVAAYMSSI 339
Cdd:cd07545  256 VISTPVSIVSAIGNAA-----RKGVLIKGGVYLEELGRLKTVAFDKTGTLTKGKPVVTDVVVLGGQTEKELLAIAAALEY 330
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 340 YDDTPEGKSIVRLAKQMYINELPkdidgtYKPFTAETR--MSGIITNEiSVFKGAPNsminLVKQQQGNIPLNIESICMD 417
Cdd:cd07545  331 RSEHPLASAIVKKAEQRGLTLSA------VEEFTALTGrgVRGVVNGT-TYYIGSPR----LFEELNLSESPALEAKLDA 399
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 418 VSSKGGTPLIVIENNVMLGVIYLKDVIKDGLVERFAELRKMGI-ETVMCTGDNALTAATIAKEAGVDRFVAECKPEDKIK 496
Cdd:cd07545  400 LQNQGKTVMILGDGERILGVIAVADQVRPSSRNAIAALHQLGIkQTVMLTGDNPQTAQAIAAQVGVSDIRAELLPQDKLD 479
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 497 VIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAM-NSGTISAKEAANLIDLDSNPTKLIEVVKIGKQLLMTRGALTTFSL 575
Cdd:cd07545  480 AIEALQAEGGRVAMVGDGVNDAPALAAADVGIAMgAAGTDTALETADIALMGDDLRKLPFAVRLSRKTLAIIKQNIAFAL 559
                        490       500
                 ....*....|....*....|....*
gi 446468755 576 ANDVAKYFAILP---ALMMSTIPEM 597
Cdd:cd07545  560 GIKLIALLLVIPgwlTLWMAVFADM 584
P-type_ATPase_Pb_Zn_Cd2-like cd07546
P-type heavy metal-transporting ATPase, similar to Escherichia coli ZntA which is selective ...
83-564 1.63e-61

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: 215.73  E-value: 1.63e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  83 EAFAEGRGKAQADSLrQAQSNLTARLiEENGAYRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGESAPV 162
Cdd:cd07546   79 EGYAASRARSGVKAL-MALVPETALR-EENGERREVPADSLRPGDVIEVAPGGRLPADGELLSGFASFDESALTGESIPV 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 163 IKESGgdfDGVIGGTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTPNEIAlftllttltiiflvvivtlypIASY 242
Cdd:cd07546  157 EKAAG---DKVFAGSINVDGVLRIRVTSAPGDNAIDRILHLIEEAEERRAPIERF---------------------IDRF 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 243 LHLILPIAMLIALTVCLIPTTIGG-------------LL------------SAIGiAGMDRVTQFNVLAKSGRAVEVCGD 297
Cdd:cd07546  213 SRWYTPAIMAVALLVIVVPPLLFGadwqtwiyrglalLLigcpcalvistpAAIT-SGLAAAARRGALIKGGAALEQLGR 291
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 298 VDVMILDKTGTITYGNRIASEFLPVNQQMMEKLIVAAYMSSIYDDTPEGKSIVRLAKQMYINELPKDIDGTykpfTAETR 377
Cdd:cd07546  292 VTTVAFDKTGTLTRGKPVVTDVVPLTGISEAELLALAAAVEMGSSHPLAQAIVARAQAAGLTIPPAEEARA----LVGRG 367
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 378 MSGIItNEISVFKGAPnsminlvKQQQGNIPLNIESICMDVSSKGGTPLIVIENNVMLGVIYLKDVIKDGLVERFAELRK 457
Cdd:cd07546  368 IEGQV-DGERVLIGAP-------KFAADRGTLEVQGRIAALEQAGKTVVVVLANGRVLGLIALRDELRPDAAEAVAELNA 439
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 458 MGIETVMCTGDNALTAATIAKEAGVDrFVAECKPEDKIKVIKDEQAKGHiVAMTGDGTNDAPALAQANIGLAMNSGTISA 537
Cdd:cd07546  440 LGIKALMLTGDNPRAAAAIAAELGLD-FRAGLLPEDKVKAVRELAQHGP-VAMVGDGINDAPAMKAASIGIAMGSGTDVA 517
                        490       500
                 ....*....|....*....|....*..
gi 446468755 538 KEAANLIDLDSNPTKLIEVVKIGKQLL 564
Cdd:cd07546  518 LETADAALTHNRLGGVAAMIELSRATL 544
P-type_ATPase_Cu-like cd07552
P-type heavy metal-transporting ATPase, similar to Archaeoglobus fulgidus CopB, a Cu(2+) ...
105-562 1.73e-61

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: 216.79  E-value: 1.73e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 105 TARLIEENGAyRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGESAPVIKESGgdfDGVIGGTLVTSDWL 184
Cdd:cd07552  132 TAHLVTDGSI-EDVPVSELKVGDVVLVRAGEKIPADGTILEGESSVNESMVTGESKPVEKKPG---DEVIGGSVNGNGTL 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 185 EIRVESEAGTSFLDKMIALVEGAERNKTPNE-IALFTLLTTLTIIFLVVIVTLypIASYLHLILPIAMLIALTVCLI--P 261
Cdd:cd07552  208 EVKVTKTGEDSYLSQVMELVAQAQASKSRAEnLADKVAGWLFYIALGVGIIAF--IIWLILGDLAFALERAVTVLVIacP 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 262 TTIG---GLLSAI--GIAGmdrvtQFNVLAKSGRAVEVCGDVDVMILDKTGTITYGNRIASEfLPVNQQMMEKLIVAaYM 336
Cdd:cd07552  286 HALGlaiPLVVARstSIAA-----KNGLLIRNREALERARDIDVVLFDKTGTLTEGKFGVTD-VITFDEYDEDEILS-LA 358
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 337 SSIYDDT--PEGKSIVRLAKQMYInelpkdidgTYKPFTAETRMSGI-ITNEIsvfkGAPNSMI---NLVKQQQGNIPln 410
Cdd:cd07552  359 AALEAGSehPLAQAIVSAAKEKGI---------RPVEVENFENIPGVgVEGTV----NGKRYQVvspKYLKELGLKYD-- 423
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 411 iESICMDVSSKGGTPLIVIENNVMLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEAGVDRFVAECK 490
Cdd:cd07552  424 -EELVKRLAQQGNTVSFLIQDGEVIGAIALGDEIKPESKEAIRALKAQGITPVMLTGDNEEVAQAVAEELGIDEYFAEVL 502
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446468755 491 PEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAANLIDLDSNPTKLIEVVKIGKQ 562
Cdd:cd07552  503 PEDKAKKVKELQAEGKKVAMVGDGVNDAPALAQADVGIAIGAGTDVAIESADVVLVKSDPRDIVDFLELAKA 574
P-type_ATPases cd01431
ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, ...
300-617 4.31e-61

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: 206.92  E-value: 4.31e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 300 VMILDKTGTITYGN----RIASEFLPVNQqmmekliVAAYMSSIYDDTPEGKSIVRLAkqmyinelpkdidgtykPFTAE 375
Cdd:cd01431    1 VICSDKTGTLTKNGmtvtKLFIEEIPFNS-------TRKRMSVVVRLPGRYRAIVKGA-----------------PETIL 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 376 TRMSGIITNEISvfkgapnSMINLVKQQQGNIPLNIESICMDVSSKGGTPLIVIENNVMLGVIYLKDVIKDGLVERFAEL 455
Cdd:cd01431   57 SRCSHALTEEDR-------NKIEKAQEESAREGLRVLALAYREFDPETSKEAVELNLVFLGLIGLQDPPRPEVKEAIAKC 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 456 RKMGIETVMCTGDNALTAATIAKEAGVD---------------------------RFVAECKPEDKIKVIKDEQAKGHIV 508
Cdd:cd01431  130 RTAGIKVVMITGDNPLTAIAIAREIGIDtkasgvilgeeademseeelldliakvAVFARVTPEQKLRIVKALQARGEVV 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 509 AMTGDGTNDAPALAQANIGLAMNS-GTISAKEAANLIDLDSNPTKLIEVVKIGKQLLMTRGALTTFSLANDVAKYFAILP 587
Cdd:cd01431  210 AMTGDGVNDAPALKQADVGIAMGStGTDVAKEAADIVLLDDNFATIVEAVEEGRAIYDNIKKNITYLLANNVAEVFAIAL 289
                        330       340       350
                 ....*....|....*....|....*....|
gi 446468755 588 ALMMSTIPEMTSLNIMHLSSPKSAIISALI 617
Cdd:cd01431  290 ALFLGGPLPLLAFQILWINLVTDLIPALAL 319
P-type_ATPase_HM cd07550
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
109-564 1.78e-55

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: 199.04  E-value: 1.78e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 109 IEENGAYRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGESAPVIKESGgdfDGVIGGTLVTSDWLEIRV 188
Cdd:cd07550  104 VERDGVEVEVPADEVQPGDTVVVGAGDVIPVDGTVLSGEALIDQASLTGESLPVEKREG---DLVFASTVVEEGQLVIRA 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 189 ESEAGTSFLDKMIALVEGAERNKT-----PNEIALFTLLTTLTIIFLVVIVTLYP--IASYLHLILPIAMLIALTVCLip 261
Cdd:cd07550  181 ERVGRETRAARIAELIEQSPSLKAriqnyAERLADRLVPPTLGLAGLVYALTGDIsrAAAVLLVDFSCGIRLSTPVAV-- 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 262 ttigglLSAIGIAGmdrvtQFNVLAKSGRAVEVCGDVDVMILDKTGTITYGNRIASEFLPVNQQMMEK---LIVAAYMSS 338
Cdd:cd07550  259 ------LSALNHAA-----RHGILVKGGRALELLAKVDTVVFDKTGTLTEGEPEVTAIITFDGRLSEEdllYLAASAEEH 327
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 339 IYDdtPEGKSIVRLAKQMYInELPKDIDGTYKP-FTAETRMSGiitNEISVfkGAPNsminLVKQQQGNIPLNIESICMD 417
Cdd:cd07550  328 FPH--PVARAIVREAEERGI-EHPEHEEVEYIVgHGIASTVDG---KRIRV--GSRH----FMEEEEIILIPEVDELIED 395
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 418 VSSKGGTPLIVIENNVMLGVIYLKDVIKDGLVERFAELRK-MGIETVMCTGDNALTAATIAKEAGVDRFVAECKPEDKIK 496
Cdd:cd07550  396 LHAEGKSLLYVAIDGRLIGVIGLSDPLRPEAAEVIARLRAlGGKRIIMLTGDHEQRARALAEQLGIDRYHAEALPEDKAE 475
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446468755 497 VIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAANLIDLDSNPTKLIEVVKIGKQLL 564
Cdd:cd07550  476 IVEKLQAEGRTVAFVGDGINDSPALSYADVGISMRGGTDIARETADVVLLEDDLRGLAEAIELARETM 543
P-type_ATPase_HM cd07544
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
98-590 1.11e-51

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: 188.68  E-value: 1.11e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  98 RQAQSNLTARL--------IEENGAYRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGESAPVIKESGgd 169
Cdd:cd07544   95 RRASRELTALLdrapriahRLVGGQLEEVPVEEVTVGDRLLVRPGEVVPVDGEVVSGTATLDESSLTGESKPVSKRPG-- 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 170 fDGVIGGTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTP-----NEIALFTLLTTLTIIFLVVIVTLYP--IASY 242
Cdd:cd07544  173 -DRVMSGAVNGDSALTMVATKLAADSQYAGIVRLVKEAQANPAPfvrlaDRYAVPFTLLALAIAGVAWAVSGDPvrFAAV 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 243 LHLILPIAMLIALTVCLIpttiggllsaigiAGMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTITYGNRIASEFLPV 322
Cdd:cd07544  252 LVVATPCPLILAAPVAIV-------------SGMSRSSRRGILVKDGGVLEKLARAKTVAFDKTGTLTYGQPKVVDVVPA 318
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 323 NQQMMEKLIVAAYMSSIYDDTPEGKSIVRLAKQMYInELPKDIDgtykpfTAETRMSGIITN----EISVFKGAPNSMIN 398
Cdd:cd07544  319 PGVDADEVLRLAASVEQYSSHVLARAIVAAAREREL-QLSAVTE------LTEVPGAGVTGTvdghEVKVGKLKFVLARG 391
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 399 LVKQQQGNIPLniesicmdvsskGGTPLIVIENNVMLGVIYLKDVIKDGLVERFAELRKMGIE-TVMCTGDNALTAATIA 477
Cdd:cd07544  392 AWAPDIRNRPL------------GGTAVYVSVDGKYAGAITLRDEVRPEAKETLAHLRKAGVErLVMLTGDRRSVAEYIA 459
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 478 KEAGVDRFVAECKPEDKIKVIKdEQAKGHIVAMTGDGTNDAPALAQANIGLAMNS-GTISAKEAANLIDLDSNPTKLIEV 556
Cdd:cd07544  460 SEVGIDEVRAELLPEDKLAAVK-EAPKAGPTIMVGDGVNDAPALAAADVGIAMGArGSTAASEAADVVILVDDLDRVVDA 538
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 446468755 557 VKIGKQllMTRGALT------TFSLANDVAKYFAILPALM 590
Cdd:cd07544  539 VAIARR--TRRIALQsvligmALSIIGMLIAAFGLIPPVA 576
zntA PRK11033
zinc/cadmium/mercury/lead-transporting ATPase; Provisional
83-541 7.77e-51

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


Pssm-ID: 236827 [Multi-domain]  Cd Length: 741  Bit Score: 188.66  E-value: 7.77e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  83 EAFAEGRGkaqadslRQAQSNLTARLIEE-----NGAYRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITG 157
Cdd:PRK11033 223 EGYAASRA-------RRGVSALMALVPETatrlrDGEREEVAIADLRPGDVIEVAAGGRLPADGKLLSPFASFDESALTG 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 158 ESAPVIKESGgdfDGVIGGTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTPNEIAlftllttltiiflvvivtly 237
Cdd:PRK11033 296 ESIPVERATG---EKVPAGATSVDRLVTLEVLSEPGASAIDRILHLIEEAEERRAPIERF-------------------- 352
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 238 pIASYLHLILPIAMLIALTVCLIPTTIGG-------------LL------------SAIgIAGMDRVTQFNVLAKSGRAV 292
Cdd:PRK11033 353 -IDRFSRIYTPAIMLVALLVILVPPLLFAapwqewiyrgltlLLigcpcalvistpAAI-TSGLAAAARRGALIKGGAAL 430
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 293 EVCGDVDVMILDKTGTITYGNRIASEFLPVNQQMMEKLIVAAYMSSIYDDTPEGKSIVRLAKQMYINeLPkdidgtykpf 372
Cdd:PRK11033 431 EQLGRVTTVAFDKTGTLTEGKPQVTDIHPATGISESELLALAAAVEQGSTHPLAQAIVREAQVRGLA-IP---------- 499
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 373 TAETRM----SGI--ITNEISVFKGAPNSMINLVKQQQGNIplniesicMDVSSKGGTPLIVIENNVMLGVIYLKDVIKD 446
Cdd:PRK11033 500 EAESQRalagSGIegQVNGERVLICAPGKLPPLADAFAGQI--------NELESAGKTVVLVLRNDDVLGLIALQDTLRA 571
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 447 GLVERFAELRKMGIETVMCTGDNALTAATIAKEAGVDrFVAECKPEDKIKVIKDEQAKgHIVAMTGDGTNDAPALAQANI 526
Cdd:PRK11033 572 DARQAISELKALGIKGVMLTGDNPRAAAAIAGELGID-FRAGLLPEDKVKAVTELNQH-APLAMVGDGINDAPAMKAASI 649
                        490
                 ....*....|....*
gi 446468755 527 GLAMNSGTISAKEAA 541
Cdd:PRK11033 650 GIAMGSGTDVALETA 664
MgtA COG0474
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism];
87-560 2.53e-50

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


Pssm-ID: 440242 [Multi-domain]  Cd Length: 874  Bit Score: 188.39  E-value: 2.53e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  87 EGRGKAQADSLRQaQSNLTARLIEeNGAYRIVNATELKAGQNIRVENGETIPADGVVI--NGLaTVDESAITGESAPVIK 164
Cdd:COG0474  102 EYRAEKALEALKK-LLAPTARVLR-DGKWVEIPAEELVPGDIVLLEAGDRVPADLRLLeaKDL-QVDESALTGESVPVEK 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 165 ESG-GDFDGVIG--------GTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTP-----NEIALFTLLTTltiifl 230
Cdd:COG0474  179 SADpLPEDAPLGdrgnmvfmGTLVTSGRGTAVVVATGMNTEFGKIAKLLQEAEEEKTPlqkqlDRLGKLLAIIA------ 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 231 VVIVTLYPIASYLHLILPIAML---IALTVCLIPTtigGLLSAIGIA---GMDRVTQFNVLAKSGRAVEVCGDVDVMILD 304
Cdd:COG0474  253 LVLAALVFLIGLLRGGPLLEALlfaVALAVAAIPE---GLPAVVTITlalGAQRMAKRNAIVRRLPAVETLGSVTVICTD 329
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 305 KTGTITYgNRI-------ASEFLPVNQQ---MMEKLIVAAYMSS---IYDDTPEG----KSIVRLAKQMYINelPKDIDG 367
Cdd:COG0474  330 KTGTLTQ-NKMtvervytGGGTYEVTGEfdpALEELLRAAALCSdaqLEEETGLGdpteGALLVAAAKAGLD--VEELRK 406
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 368 TYK-----PFTAET-RMSGIITNE----ISVFKGAPNSMINLVKQQQGN---IPLN------IESICMDVSSKG------ 422
Cdd:COG0474  407 EYPrvdeiPFDSERkRMSTVHEDPdgkrLLIVKGAPEVVLALCTRVLTGggvVPLTeedraeILEAVEELAAQGlrvlav 486
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 423 ---------GTPLIVIENN-VMLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEAGVDRF------- 485
Cdd:COG0474  487 aykelpadpELDSEDDESDlTFLGLVGMIDPPRPEAKEAIAECRRAGIRVKMITGDHPATARAIARQLGLGDDgdrvltg 566
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 486 --------------------VAECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAM-NSGTISAKEAANLI 544
Cdd:COG0474  567 aeldamsdeelaeavedvdvFARVSPEHKLRIVKALQANGHVVAMTGDGVNDAPALKAADIGIAMgITGTDVAKEAADIV 646
                        570
                 ....*....|....*.
gi 446468755 545 DLDSNPTKLIEVVKIG 560
Cdd:COG0474  647 LLDDNFATIVAAVEEG 662
P-type_ATPase-Cd_Zn_Co_like cd07548
P-type heavy metal-transporting ATPase, similar to Bacillus subtilis CadA which appears to ...
106-562 3.00e-50

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: 184.75  E-value: 3.00e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 106 ARLIEENGAyRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGESAPVIKESGgdfDGVIGGTLVTSDWLE 185
Cdd:cd07548  111 ANLKRNNEL-KDVKPEEVQIGDIIVVKPGEKIPLDGVVLKGESFLDTSALTGESVPVEVKEG---SSVLAGFINLNGVLE 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 186 IRVESEAGTSFLDKMIALVEGAERNKTPNEIAlftllttltiiflvvivtlypIASYLHLILPIAMLIALTVCLIPTTIG 265
Cdd:cd07548  187 IKVTKPFKDSAVAKILELVENASARKAPTEKF---------------------ITKFARYYTPIVVFLALLLAVIPPLFS 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 266 GLLS--------------------AIGI-----AGMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTITYGNRIASEFL 320
Cdd:cd07548  246 PDGSfsdwiyralvflviscpcalVISIplgyfGGIGAASRKGILIKGSNYLEALSQVKTVVFDKTGTLTKGVFKVTEIV 325
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 321 PVNQQMMEKLIVAAYMSSIYDDTPEGKSIVRLAKQMYINELPKDidgtYKPFTAETRMSGIITNEISVFKgapNSMInlv 400
Cdd:cd07548  326 PAPGFSKEELLKLAALAESNSNHPIARSIQKAYGKMIDPSEIED----YEEIAGHGIRAVVDGKEILVGN---EKLM--- 395
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 401 kqQQGNIPLNIESIcmdvsskGGTPLIVIENNVMLGVIYLKDVIKDGLVERFAELRKMGIE-TVMCTGDNALTAATIAKE 479
Cdd:cd07548  396 --EKFNIEHDEDEI-------EGTIVHVALDGKYVGYIVISDEIKEDAKEAIKGLKELGIKnLVMLTGDRKSVAEKVAKK 466
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 480 AGVDRFVAECKPEDKIKVIKDEQAK-GHIVAMTGDGTNDAPALAQANIGLAMNS-GTISAKEAANLIDLDSNPTKLIEVV 557
Cdd:cd07548  467 LGIDEVYAELLPEDKVEKVEELKAEsKGKVAFVGDGINDAPVLARADVGIAMGGlGSDAAIEAADVVLMNDEPSKVAEAI 546

                 ....*
gi 446468755 558 KIGKQ 562
Cdd:cd07548  547 KIARK 551
copA PRK10671
copper-exporting P-type ATPase CopA;
105-541 1.04e-44

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 171.46  E-value: 1.04e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 105 TARLIEENGAyRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGESAPVIKESGgdfDGVIGGTLVTSDWL 184
Cdd:PRK10671 324 TARVVTDEGE-KSVPLADVQPGMLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEPIPQQKGEG---DSVHAGTVVQDGSV 399
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 185 EIRVESEAGTSFLDKMIALVEGAERNKTpnEIALFTLLTTLTIIFLVVIVTLYPIASYlHLILP-----IAMLIALTVCL 259
Cdd:PRK10671 400 LFRASAVGSHTTLSRIIRMVRQAQSSKP--EIGQLADKISAVFVPVVVVIALVSAAIW-YFFGPapqivYTLVIATTVLI 476
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 260 I--PTTIGGLLSAIGIAGMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTITYGNRIASEFLPVNQQMMEKLIVAAYMS 337
Cdd:PRK10671 477 IacPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTLVFDKTGTLTEGKPQVVAVKTFNGVDEAQALRLAAAL 556
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 338 SIYDDTPEGKSIVRLAKQMyinELPkdidgTYKPFT--AETRMSGIItNEISVFKGAPNsminLVKQQQGNIPlNIESIC 415
Cdd:PRK10671 557 EQGSSHPLARAILDKAGDM---TLP-----QVNGFRtlRGLGVSGEA-EGHALLLGNQA----LLNEQQVDTK-ALEAEI 622
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 416 MDVSSKGGTPLIVIENNVMLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEAGVDRFVAECKPEDKI 495
Cdd:PRK10671 623 TAQASQGATPVLLAVDGKAAALLAIRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVLPDGKA 702
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 446468755 496 KVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAA 541
Cdd:PRK10671 703 EAIKRLQSQGRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETA 748
P-type_ATPase_H cd02076
plant and fungal plasma membrane H(+)-ATPases, and related bacterial and archaeal putative H(+) ...
112-606 8.63e-44

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: 168.56  E-value: 8.63e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 112 NGAYRIVNATELKAGQNIRVENGETIPADGVVINGLA-TVDESAITGESAPVIKESGgdfDGVIGGTLVTSDWLEIRVES 190
Cdd:cd02076   99 DGQWQEIDAKELVPGDIVSLKIGDIVPADARLLTGDAlQVDQSALTGESLPVTKHPG---DEAYSGSIVKQGEMLAVVTA 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 191 EAGTSFLDKMIALVEGAER----NKTPNEIALFTLLTTLTIIFLVVIVTLYPIASYLHLILPIAMLialTVCLIPTTIGG 266
Cdd:cd02076  176 TGSNTFFGKTAALVASAEEqghlQKVLNKIGNFLILLALILVLIIVIVALYRHDPFLEILQFVLVL---LIASIPVAMPA 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 267 LLSAIGIAGMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTITYgNRIA-SEFLPVNQQMMEKLIVAAYMSSiyddTPE 345
Cdd:cd02076  253 VLTVTMAVGALELAKKKAIVSRLSAIEELAGVDILCSDKTGTLTL-NKLSlDEPYSLEGDGKDELLLLAALAS----DTE 327
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 346 GKSIVRLAKQMYINELPKDIDG----TYKPFTAETRMSGIITNE-----ISVFKGAPNSMINLVKQQQGnIPLNIESICM 416
Cdd:cd02076  328 NPDAIDTAILNALDDYKPDLAGykqlKFTPFDPVDKRTEATVEDpdgerFKVTKGAPQVILELVGNDEA-IRQAVEEKID 406
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 417 DVSSKGGTPLIV-----IENNVMLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEAG---------- 481
Cdd:cd02076  407 ELASRGYRSLGVarkedGGRWELLGLLPLFDPPRPDSKATIARAKELGVRVKMITGDQLAIAKETARQLGmgtnilsaer 486
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 482 --------------VDRFV------AECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAA 541
Cdd:cd02076  487 lklggggggmpgseLIEFIedadgfAEVFPEHKYRIVEALQQRGHLVGMTGDGVNDAPALKKADVGIAVSGATDAARAAA 566
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446468755 542 NLIDLDSNPTKLIEVVKIGKQLL-------MTRGALT-----TFSLANDVAKYFAIlPALMMSTIPEMTSLNIMHLS 606
Cdd:cd02076  567 DIVLTAPGLSVIIDAIKTSRQIFqrmksyvIYRIAETlrilvFFTLGILILNFYPL-PLIMIVLIAILNDGATLTIA 642
P-type_ATPase cd07538
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ...
83-563 2.23e-43

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


Pssm-ID: 319839 [Multi-domain]  Cd Length: 653  Bit Score: 166.08  E-value: 2.23e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  83 EAFAEGRGKAQADSLRQAqSNLTARLIEeNGAYRIVNATELKAGQNIRVENGETIPADGVVI-NGLATVDESAITGESAP 161
Cdd:cd07538   73 EVVQEWRTERALEALKNL-SSPRATVIR-DGRERRIPSRELVPGDLLILGEGERIPADGRLLeNDDLGVDESTLTGESVP 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 162 VIKESGGDFDGVIG---------GTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTP--NEIALFTLLTTLTIIFL 230
Cdd:cd07538  151 VWKRIDGKAMSAPGgwdknfcyaGTLVVRGRGVAKVEATGSRTELGKIGKSLAEMDDEPTPlqKQTGRLVKLCALAALVF 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 231 VVIVTLYPIASYLHLILPIAMLIALTVCLIPTTIGGLLSAIGIAGMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTIT 310
Cdd:cd07538  231 CALIVAVYGVTRGDWIQAILAGITLAMAMIPEEFPVILTVFMAMGAWRLAKKNVLVRRAAAVETLGSITVLCVDKTGTLT 310
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 311 YgnriaseflpvNQQMMEKLIvaaymssiyddtpegkSIVRlakqmyinelpkdidgTYkPFTAETRMSG----IITNEI 386
Cdd:cd07538  311 K-----------NQMEVVELT----------------SLVR----------------EY-PLRPELRMMGqvwkRPEGAF 346
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 387 SVFKGAPNSMINLVKQQQGNIPlNIESICMDVSSKGGTPLIV----IENNVM-----------LGVIYLKDVIKDGLVER 451
Cdd:cd07538  347 AAAKGSPEAIIRLCRLNPDEKA-AIEDAVSEMAGEGLRVLAVaacrIDESFLpddledavfifVGLIGLADPLREDVPEA 425
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 452 FAELRKMGIETVMCTGDNALTAATIAKEAGVD--------------------------RFVAECKPEDKIKVIKDEQAKG 505
Cdd:cd07538  426 VRICCEAGIRVVMITGDNPATAKAIAKQIGLDntdnvitgqeldamsdeelaekvrdvNIFARVVPEQKLRIVQAFKANG 505
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446468755 506 HIVAMTGDGTNDAPALAQANIGLAMNS-GTISAKEAANLIDLDSNPTKLIEVVKIGKQL 563
Cdd:cd07538  506 EIVAMTGDGVNDAPALKAAHIGIAMGKrGTDVAREASDIVLLDDNFSSIVSTIRLGRRI 564
P-type_ATPase_Ca_prok cd02089
prokaryotic P-type Ca(2+)-ATPase similar to Synechococcus elongatus sp. strain PCC 7942 PacL ...
87-561 9.28e-42

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


Pssm-ID: 319781 [Multi-domain]  Cd Length: 674  Bit Score: 161.63  E-value: 9.28e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  87 EGRGKAQADSLRQAQSNLTARLieENGAYRIVNATELKAGQNIRVENGETIPADGVVI-NGLATVDESAITGESAPVIK- 164
Cdd:cd02089   77 EYKAEKALAALKKMSAPTAKVL--RDGKKQEIPARELVPGDIVLLEAGDYVPADGRLIeSASLRVEESSLTGESEPVEKd 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 165 -ESGGDFDGVIG--------GTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTP--NEIALFTLLTTLTIIFLVVI 233
Cdd:cd02089  155 aDTLLEEDVPLGdrknmvfsGTLVTYGRGRAVVTATGMNTEMGKIATLLEETEEEKTPlqKRLDQLGKRLAIAALIICAL 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 234 VTLYPIASYLHLILPIAMLIALTVCLIPTTIGGLLSAIGIAGMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTITygn 313
Cdd:cd02089  235 VFALGLLRGEDLLDMLLTAVSLAVAAIPEGLPAIVTIVLALGVQRMAKRNAIIRKLPAVETLGSVSVICSDKTGTLT--- 311
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 314 riaseflpvnqqmMEKLIVAAYMSsIYDDTpEGkSIVRLAKQMYINElpKDIDGTYK-----PFTAET-RMSGII---TN 384
Cdd:cd02089  312 -------------QNKMTVEKIYT-IGDPT-ET-ALIRAARKAGLDK--EELEKKYPriaeiPFDSERkLMTTVHkdaGK 373
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 385 EISVFKGAPNSMINLVKQQQGN---IPLN------IESICMDVSSKG---------------GTPLIVIENN-VMLGVIY 439
Cdd:cd02089  374 YIVFTKGAPDVLLPRCTYIYINgqvRPLTeedrakILAVNEEFSEEAlrvlavaykpldedpTESSEDLENDlIFLGLVG 453
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 440 LKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEAG-------------------------VD--RFVAECKPE 492
Cdd:cd02089  454 MIDPPRPEVKDAVAECKKAGIKTVMITGDHKLTARAIAKELGiledgdkaltgeeldkmsdeelekkVEqiSVYARVSPE 533
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 493 DKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMN-SGTISAKEAANLIDLDSNPTKLIEVVKIGK 561
Cdd:cd02089  534 HKLRIVKALQRKGKIVAMTGDGVNDAPALKAADIGVAMGiTGTDVAKEAADMILTDDNFATIVAAVEEGR 603
P-type_ATPase cd07539
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ...
84-563 2.65e-41

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


Pssm-ID: 319840 [Multi-domain]  Cd Length: 634  Bit Score: 159.50  E-value: 2.65e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  84 AFAEGRGKAQADSLRQAQSNLTARLIEENGAYRIVNATELKAGQNIRVENGETIPADGVVI--NGLaTVDESAITGESAP 161
Cdd:cd07539   75 GVQRLRAERALAALLAQQQQPARVVRAPAGRTQTVPAESLVPGDVIELRAGEVVPADARLLeaDDL-EVDESALTGESLP 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 162 VIKE---SGGDFDG-----VIGGTLVTS-DWLEIRVESEAGTSfLDKMIALVEGAErNKTP-----NEIALFTLLTTLTI 227
Cdd:cd07539  154 VDKQvapTPGAPLAdracmLYEGTTVVSgQGRAVVVATGPHTE-AGRAQSLVAPVE-TATGvqaqlRELTSQLLPLSLGG 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 228 IFLVVIVTL---YPiasylhLILPIAMLIALTVCLIPTTIGGLLSAIGIAGMDRVTQFNVLAKSGRAVEVCGDVDVMILD 304
Cdd:cd07539  232 GAAVTGLGLlrgAP------LRQAVADGVSLAVAAVPEGLPLVATLAQLAAARRLSRRGVLVRSPRTVEALGRVDTICFD 305
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 305 KTGTITYGNRIASEFLPVNQQMMEKlIVAAYMSSIYDDTPEGKSIVrlakqmyinelpkdIDGTykPFTAETRMSGIITN 384
Cdd:cd07539  306 KTGTLTENRLRVVQVRPPLAELPFE-SSRGYAAAIGRTGGGIPLLA--------------VKGA--PEVVLPRCDRRMTG 368
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 385 EISV-FKGAPNSMINLVKQQQGNIPLNIESIC---MDVSSKGGTPLIViENNVMLGVIYLKDVIKDGLVERFAELRKMGI 460
Cdd:cd07539  369 GQVVpLTEADRQAIEEVNELLAGQGLRVLAVAyrtLDAGTTHAVEAVV-DDLELLGLLGLADTARPGAAALIAALHDAGI 447
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 461 ETVMCTGDNALTAATIAKEAGVDR--------------------------FVAECKPEDKIKVIKDEQAKGHIVAMTGDG 514
Cdd:cd07539  448 DVVMITGDHPITARAIAKELGLPRdaevvtgaeldaldeealtglvadidVFARVSPEQKLQIVQALQAAGRVVAMTGDG 527
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 446468755 515 TNDAPALAQANIGLAM-NSGTISAKEAANLIDLDSNPTKLIEVVKIGKQL 563
Cdd:cd07539  528 ANDAAAIRAADVGIGVgARGSDAAREAADLVLTDDDLETLLDAVVEGRTM 577
P-type_ATPase_FixI-like cd02092
Rhizobium meliloti FixI and related proteins; belongs to P-type heavy metal-transporting ...
89-605 1.62e-40

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: 157.13  E-value: 1.62e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  89 RGKAqadslRQAQSNL------TARLIEENGAYRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGESAPV 162
Cdd:cd02092  110 RGRA-----RSAAEELaalearGAQRLQADGSREYVPVAEIRPGDRVLVAAGERIPVDGTVVSGTSELDRSLLTGESAPV 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 163 IKESGgdfDGVIGGTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTP-NEIALFTLLTTLTIIFLVVIVTlypIAS 241
Cdd:cd02092  185 TVAPG---DLVQAGAMNLSGPLRLRATAAGDDTLLAEIARLMEAAEQGRSRyVRLADRAARLYAPVVHLLALLT---FVG 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 242 YLHLILPI--AMLIALTVCLI--PTTIGGLLSAIGIAGMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTITYGnriAS 317
Cdd:cd02092  259 WVAAGGDWrhALLIAVAVLIItcPCALGLAVPAVQVVASGRLFRRGVLVKDGTALERLAEVDTVVFDKTGTLTLG---SP 335
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 318 EFLPVNQQMMEKLIVAAYMS---------SIYDDTPEGKSIVRLAKqmyinELP-KDIDGTYKPFTAetRMsgiitneis 387
Cdd:cd02092  336 RLVGAHAISADLLALAAALAqasrhplsrALAAAAGARPVELDDAR-----EVPgRGVEGRIDGARV--RL--------- 399
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 388 vfkGAPNSMINLVKQQQGNIplniesicmDVSSKGGTPLIviennvmlgVIYLKDVIKDGLVERFAELRKMGIETVMCTG 467
Cdd:cd02092  400 ---GRPAWLGASAGVSTASE---------LALSKGGEEAA---------RFPFEDRPRPDAREAISALRALGLSVEILSG 458
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 468 DNALTAATIAKEAGVDRFVAECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAANLIDLD 547
Cdd:cd02092  459 DREPAVRALARALGIEDWRAGLTPAEKVARIEELKAQGRRVLMVGDGLNDAPALAAAHVSMAPASAVDASRSAADIVFLG 538
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446468755 548 SNPTKLIEVVKIGKQllMTRGALTTFSLA---NDVAKYFAIL-------PALMMSTIPEMTSLNIMHL 605
Cdd:cd02092  539 DSLAPVPEAIEIARR--ARRLIRQNFALAigyNVIAVPLAIAgyvtpliAALAMSTSSIVVVLNALRL 604
P-type_ATPase_HM cd07553
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
98-607 2.78e-40

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: 156.52  E-value: 2.78e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  98 RQAQSNLTARLIE---ENGAYRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGESAPVIKESGgdfDGVI 174
Cdd:cd07553  118 RLADSRLEAPITEietGSGSRIKTRADQIKSGDVYLVASGQRVPVDGKLLSEQASIDMSWLTGESLPRIVERG---DKVP 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 175 GGTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTPneialFTLLTTLTIIFLVVIVTLYPIASYLHLI---LPIAM 251
Cdd:cd07553  195 AGTSLENQAFEIRVEHSLAESWSGSILQKVEAQEARKTP-----RDLLADKIIHYFTVIALLIAVAGFGVWLaidLSIAL 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 252 LIALTVCLI--PTTIgGLLSAIGIA-GMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTITYGNriaSEFLPVNQQMME 328
Cdd:cd07553  270 KVFTSVLIVacPCAL-ALATPFTDEiALARLKKKGVLIKNASSLERLSRVRTIVFDKTGTLTRGK---SSFVMVNPEGID 345
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 329 KL-IVAAYMSSIYDDTPEGKSIVRlakqmyinELPKdiDGTYKPFTAETRmsgiitnEISVFKGAPNSMINLVKqqqgni 407
Cdd:cd07553  346 RLaLRAISAIEAHSRHPISRAIRE--------HLMA--KGLIKAGASELV-------EIVGKGVSGNSSGSLWK------ 402
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 408 plnIESICmDVSSKGGTPLIVIENNVMLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEAGVD--RF 485
Cdd:cd07553  403 ---LGSAP-DACGIQESGVVIARDGRQLLDLSFNDLLRPDSNREIEELKKGGLSIAILSGDNEEKVRLVGDSLGLDprQL 478
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 486 VAECKPEDKIKVIKDEQAKGhiVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAANLIDLDSNPTKLIEVVKIGKQLLM 565
Cdd:cd07553  479 FGNLSPEEKLAWIESHSPEN--TLMVGDGANDALALASAFVGIAVAGEVGVSLEAADIYYAGNGIGGIRDLLTLSKQTIK 556
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|...
gi 446468755 566 TRGALTTFSLA-NDVAKYFAilpalMMSTIPEMTSLNIMHLSS 607
Cdd:cd07553  557 AIKGLFAFSLLyNLVAIGLA-----LSGWISPLVAAILMPLSS 594
P-type_ATPase cd02609
uncharacterized subfamily of P-type ATPase transporter, similar to uncharacterized ...
85-562 8.17e-39

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: 152.43  E-value: 8.17e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  85 FAEGRGKAQADSLrqAQSNLTARLIEENGAYRIVNATELKAGQNIRVENGETIPADGVVINGL-ATVDESAITGESAPVI 163
Cdd:cd02609   74 VQEIRAKRQLDKL--SILNAPKVTVIRDGQEVKIPPEELVLDDILILKPGEQIPADGEVVEGGgLEVDESLLTGESDLIP 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 164 KESGgdfDGVIGGTLVTSDWLEIRVESEAGTSFLDKMIAlvEGAERNKTPNEIalftllttLTIIFLVVIVTLYpiasyl 243
Cdd:cd02609  152 KKAG---DKLLSGSFVVSGAAYARVTAVGAESYAAKLTL--EAKKHKLINSEL--------LNSINKILKFTSF------ 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 244 hLILPIAmlIALTVCLIPTTIGGLLSAI-----GIAGM-----------------DRVTQFNVLAKSGRAVEVCGDVDVM 301
Cdd:cd02609  213 -IIIPLG--LLLFVEALFRRGGGWRQAVvstvaALLGMipeglvlltsvalavgaIRLAKKKVLVQELYSIETLARVDVL 289
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 302 ILDKTGTITYGNRIASEFLPVNQQMME--KLIVAAYMSSIYDDTPEGKSIvRLAKQMYINELPKDIdgtyKPFTAETRMS 379
Cdd:cd02609  290 CLDKTGTITEGKMKVERVEPLDEANEAeaAAALAAFVAASEDNNATMQAI-RAAFFGNNRFEVTSI----IPFSSARKWS 364
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 380 GIITNEIS---------VFKGAPNSMINLVK--QQQGNIPLNIesicmdVSSKGGTPLIVIENNVM-LGVIYLKDVIKDG 447
Cdd:cd02609  365 AVEFRDGGtwvlgapevLLGDLPSEVLSRVNelAAQGYRVLLL------ARSAGALTHEQLPVGLEpLALILLTDPIRPE 438
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 448 LVERFAELRKMGIETVMCTGDNALTAATIAKEAGV---DRFVAECK---------------------PEDKIKVIKDEQA 503
Cdd:cd02609  439 AKETLAYFAEQGVAVKVISGDNPVTVSAIAKRAGLegaESYIDASTlttdeelaeavenytvfgrvtPEQKRQLVQALQA 518
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446468755 504 KGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAANLIDLDSNPTKLIEVVKIGKQ 562
Cdd:cd02609  519 LGHTVAMTGDGVNDVLALKEADCSIAMASGSDATRQVAQVVLLDSDFSALPDVVFEGRR 577
P-type_ATPase_cation cd02080
P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, ...
90-618 2.64e-35

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: 142.79  E-value: 2.64e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  90 GKAQA--DSLRQAQSNLTARLIeeNGAYRIVNATELKAGQNIRVENGETIPADGVVI--NGLAtVDESAITGESAPVIKE 165
Cdd:cd02080   78 GKAEKalAAIKNMLSPEATVLR--DGKKLTIDAEELVPGDIVLLEAGDKVPADLRLIeaRNLQ-IDESALTGESVPVEKQ 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 166 SGG-DFDGVIG--------GTLVTS-DWLEIRVESEAGTSfLDKMIALVEGAERNKTPnEIALFTLLTTLTIIFLVVIVT 235
Cdd:cd02080  155 EGPlEEDTPLGdrknmaysGTLVTAgSATGVVVATGADTE-IGRINQLLAEVEQLATP-LTRQIAKFSKALLIVILVLAA 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 236 LYPIASYLHLILPIA----MLIALTVCLIPTtigGLLSAIGIA---GMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGT 308
Cdd:cd02080  233 LTFVFGLLRGDYSLVelfmAVVALAVAAIPE---GLPAVITITlaiGVQRMAKRNAIIRRLPAVETLGSVTVICSDKTGT 309
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 309 ITYgnriaseflpvNQQMMEKLIVAAYMSSIYD---------DTPEGKSIVrLAKQMYINelPKDIDGTYK-----PFTA 374
Cdd:cd02080  310 LTR-----------NEMTVQAIVTLCNDAQLHQedghwkitgDPTEGALLV-LAAKAGLD--PDRLASSYPrvdkiPFDS 375
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 375 ETRMSGIIT---NEISVF-KGAPNSMINLVKQQQGNIPLN------IESICMDVSSKG------------GTPLIVIENN 432
Cdd:cd02080  376 AYRYMATLHrddGQRVIYvKGAPERLLDMCDQELLDGGVSpldrayWEAEAEDLAKQGlrvlafayrevdSEVEEIDHAD 455
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 433 V-----MLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEAG-------------------------- 481
Cdd:cd02080  456 LeggltFLGLQGMIDPPRPEAIAAVAECQSAGIRVKMITGDHAETARAIGAQLGlgdgkkvltgaeldalddeelaeavd 535
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 482 -VDRFvAECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAM-NSGTISAKEAANLIDLDSNPTKLIEVVKI 559
Cdd:cd02080  536 eVDVF-ARTSPEHKLRLVRALQARGEVVAMTGDGVNDAPALKQADIGIAMgIKGTEVAKEAADMVLADDNFATIAAAVEE 614
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446468755 560 GKQLLMTRGALTTFSLANDVAKYFAILPALMMS-TIPeMTSLNIMHLSSPKSAIIS-ALIF 618
Cdd:cd02080  615 GRRVYDNLKKFILFTLPTNLGEGLVIIVAILFGvTLP-LTPVQILWINMVTAITLGlALAF 674
ATPase-IIIA_H TIGR01647
plasma-membrane proton-efflux P-type ATPase; This model describes the plasma membrane proton ...
32-563 8.29e-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: 135.15  E-value: 8.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755   32 NPIMFVVEVGMLLTLILICFPDIFGTSYLsrgylitifiillitiLFANFSEAFAEGRGKAQADSLRQAQSNLTARLIEE 111
Cdd:TIGR01647  36 NPLSWVMEAAAIIAIALENWVDFVIILGL----------------LLLNATIGFIEENKAGNAVEALKQSLAPKARVLRD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  112 nGAYRIVNATELKAGQNIRVENGETIPADGVVING-LATVDESAITGESAPVIKESGgdfDGVIGGTLVTSDWLEIRVES 190
Cdd:TIGR01647 100 -GKWQEIPASELVPGDVVRLKIGDIVPADCRLFEGdYIQVDQAALTGESLPVTKKTG---DIAYSGSTVKQGEAEAVVTA 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  191 EAGTSFLDKMIALVEGAERN-----KTPNEIALFTLLTTLTIIFLVVIVTLYPIASYLHLILPIAMliALTVCLIPTTIG 265
Cdd:TIGR01647 176 TGMNTFFGKAAALVQSTETGsghlqKILSKIGLFLIVLIGVLVLIELVVLFFGRGESFREGLQFAL--VLLVGGIPIAMP 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  266 GLLSAIGIAGMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTITYGNRIASEFLPV-NQQMMEKLIV-AAYMSSIYDDT 343
Cdd:TIGR01647 254 AVLSVTMAVGAAELAKKKAIVTRLTAIEELAGMDILCSDKTGTLTLNKLSIDEILPFfNGFDKDDVLLyAALASREEDQD 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  344 PEGKSIVRLAKQmyinelPKDIDGTYK-----PF------TAETRMSGIITNEISVFKGAPNSMINLVKQQQgNIPLNIE 412
Cdd:TIGR01647 334 AIDTAVLGSAKD------LKEARDGYKvlefvPFdpvdkrTEATVEDPETGKRFKVTKGAPQVILDLCDNKK-EIEEKVE 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  413 SICMDVSSKGGTPLIVI---ENNV--MLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAK--------- 478
Cdd:TIGR01647 407 EKVDELASRGYRALGVArtdEEGRwhFLGLLPLFDPPRHDTKETIERARHLGVEVKMVTGDHLAIAKETARrlglgtniy 486
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  479 --------------EAGVDRFV------AECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAK 538
Cdd:TIGR01647 487 tadvllkgdnrddlPSGLGEMVedadgfAEVFPEHKYEIVEILQKRGHLVGMTGDGVNDAPALKKADVGIAVAGATDAAR 566
                         570       580
                  ....*....|....*....|....*
gi 446468755  539 EAANLIDLDSNPTKLIEVVKIGKQL 563
Cdd:TIGR01647 567 SAADIVLTEPGLSVIVDAILESRKI 591
P-type_ATPase_Ca_PMCA-like cd02081
animal plasma membrane Ca2(+)-ATPases (PMCA), similar to human ATP2B1-4/PMCA1-4, and related ...
118-560 6.08e-30

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: 126.16  E-value: 6.08e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 118 VNATELKAGQNIRVENGETIPADGVVINGLA-TVDESAITGESAPVIKesGGDFDG----VIGGTLVTSDWLEIRVESEA 192
Cdd:cd02081  113 ISVFDIVVGDIVQLKYGDLIPADGLLIEGNDlKIDESSLTGESDPIKK--TPDNQIpdpfLLSGTKVLEGSGKMLVTAVG 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 193 GTSFLDKMIALVEGAERNKTP-----NEIALFTLLTTLTIIFLVVIVTL-------------YPIASYLHLILPIAMlIA 254
Cdd:cd02081  191 VNSQTGKIMTLLRAENEEKTPlqeklTKLAVQIGKVGLIVAALTFIVLIirfiidgfvndgkSFSAEDLQEFVNFFI-IA 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 255 LT--VCLIPTtigGLLSAIGIA---GMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTITYgNRIAseflpvnqqmmek 329
Cdd:cd02081  270 VTiiVVAVPE---GLPLAVTLSlaySVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTQ-NRMT------------- 332
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 330 lIVAAYMSSiyddtpegK------SIVRLAKQMYINELPKDIDGTYK--PFTAET-RMSGIITNEISVF----KGAPNSM 396
Cdd:cd02081  333 -VVQGYIGN--------KtecallGFVLELGGDYRYREKRPEEKVLKvyPFNSARkRMSTVVRLKDGGYrlyvKGASEIV 403
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 397 I---NLVKQQQGNIPLNIE-------------------SICM---DVSSKGGTPLIVIENN--------VMLGVIYLKDV 443
Cdd:cd02081  404 LkkcSYILNSDGEVVFLTSekkeeikrviepmasdslrTIGLayrDFSPDEEPTAERDWDDeediesdlTFIGIVGIKDP 483
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 444 IKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEAG-------------------VD------------------RFV 486
Cdd:cd02081  484 LRPEVPEAVAKCQRAGITVRMVTGDNINTARAIARECGiltegedglvlegkefrelIDeevgevcqekfdkiwpklRVL 563
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446468755 487 AECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMN-SGTISAKEAANLIDLDSNPTKLIEVVKIG 560
Cdd:cd02081  564 ARSSPEDKYTLVKGLKDSGEVVAVTGDGTNDAPALKKADVGFAMGiAGTEVAKEASDIILLDDNFSSIVKAVMWG 638
ATPase-IIB_Ca TIGR01517
plasma-membrane calcium-translocating P-type ATPase; This model describes the P-type ATPase ...
112-561 1.71e-26

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: 115.65  E-value: 1.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  112 NGAYRIVNATELKAGQNIRVENGETIPADGVVINGLATV-DESAITGESAPvIKESGGDFDGVIGGTLVTSDWLEIRVES 190
Cdd:TIGR01517 176 GGQEQQISIHDIVVGDIVSLSTGDVVPADGVFISGLSLEiDESSITGESDP-IKKGPVQDPFLLSGTVVNEGSGRMLVTA 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  191 EAGTSFLDKMIALVEGAERNKTP-----NEIALFTLLT--TLTIIFLVVIVTLYPIASYLH----LILPIAMLIALTVCL 259
Cdd:TIGR01517 255 VGVNSFGGKLMMELRQAGEEETPlqeklSELAGLIGKFgmGSAVLLFLVLSLRYVFRIIRGdgrfEDTEEDAQTFLDHFI 334
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  260 IPTTI------GGLLSAIGIA---GMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTITY----------GNRIASEFL 320
Cdd:TIGR01517 335 IAVTIvvvavpEGLPLAVTIAlaySMKKMMKDNNLVRHLAACETMGSATAICSDKTGTLTQnvmsvvqgyiGEQRFNVRD 414
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  321 PVNQQMMEK-----LIVAAYMSSIyddTPEGKSIVRLAK------QMYINELPKDIDGTYKPFTAETRMSGIItnEISVF 389
Cdd:TIGR01517 415 EIVLRNLPAavrniLVEGISLNSS---SEEVVDRGGKRAfigsktECALLDFGLLLLLQSRDVQEVRAEEKVV--KIYPF 489
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  390 KGAPNSMINLVKQQQGNI--------------------------PLNIE------------------SICMDVSSKGGTP 425
Cdd:TIGR01517 490 NSERKFMSVVVKHSGGKYrefrkgaseivlkpcrkrldsngeatPISEDdkdrcadvieplasdalrTICLAYRDFAPEE 569
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  426 LIVIENN----VMLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEAGVD------------------ 483
Cdd:TIGR01517 570 FPRKDYPnkglTLIGVVGIKDPLRPGVREAVQECQRAGITVRMVTGDNIDTAKAIARNCGILtfgglamegkefrslvye 649
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  484 ---------RFVAECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMN-SGTISAKEAANLIDLDSNPTKL 553
Cdd:TIGR01517 650 emdpilpklRVLARSSPLDKQLLVLMLKDMGEVVAVTGDGTNDAPALKLADVGFSMGiSGTEVAKEASDIILLDDNFASI 729

                  ....*...
gi 446468755  554 IEVVKIGK 561
Cdd:TIGR01517 730 VRAVKWGR 737
P-type_ATPase_SPCA cd02085
golgi-associated secretory pathway Ca(2+) transport ATPases, similar to human ATPase secretory ...
120-605 8.66e-25

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: 110.18  E-value: 8.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 120 ATELKAGQNIRVENGETIPADGVVINGLA-TVDESAITGESAPVIKESGGDFDGVIG-----------GTLVTSDWLEIR 187
Cdd:cd02085   99 ARELVPGDLVCLSIGDRIPADLRLFEATDlSIDESSLTGETEPCSKTTEVIPKASNGdlttrsniafmGTLVRCGHGKGI 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 188 VESEAGTSFLDKMIALVEGAERNKTPNEIALFTLLTTLTIIFLVVIVTLYPIASYL--HLILPIAMLIALTVCLIPTTIG 265
Cdd:cd02085  179 VIGTGENSEFGEVFKMMQAEEAPKTPLQKSMDKLGKQLSLYSFIIIGVIMLIGWLQgkNLLEMFTIGVSLAVAAIPEGLP 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 266 GLLSAIGIAGMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTITygnriaseflpVNQQMMEKLIVAAYM--SSIYDDT 343
Cdd:cd02085  259 IVVTVTLALGVMRMAKRRAIVKKLPIVETLGCVNVICSDKTGTLT-----------KNEMTVTKIVTGCVCnnAVIRNNT 327
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 344 PEGK----SIVRLAKQMYInelpKDIDGTYK-----PFTAETRMSGI-------ITNEISVF-KGAPNSMIN----LVKQ 402
Cdd:cd02085  328 LMGQptegALIALAMKMGL----SDIRETYIrkqeiPFSSEQKWMAVkcipkynSDNEEIYFmKGALEQVLDycttYNSS 403
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 403 QQGNIPLN------IESICMDVSSKGGTPL-----IVIENNVMLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNAL 471
Cdd:cd02085  404 DGSALPLTqqqrseINEEEKEMGSKGLRVLalasgPELGDLTFLGLVGINDPPRPGVREAIQILLESGVRVKMITGDAQE 483
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 472 TAATIAKEAGVDRFVAEC---------------------------KPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQA 524
Cdd:cd02085  484 TAIAIGSSLGLYSPSLQAlsgeevdqmsdsqlasvvrkvtvfyraSPRHKLKIVKALQKSGAVVAMTGDGVNDAVALKSA 563
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 525 NIGLAMN-SGTISAKEAANLIDLDSNPTKLIEVVKIGKQLLMTRGALTTFSLANDVAKYFAILPALMMStIPemTSLNIM 603
Cdd:cd02085  564 DIGIAMGrTGTDVCKEAADMILVDDDFSTILAAIEEGKGIFYNIKNFVRFQLSTSIAALSLIALSTLFN-LP--NPLNAM 640

                 ..
gi 446468755 604 HL 605
Cdd:cd02085  641 QI 642
E1-E2_ATPase pfam00122
E1-E2 ATPase;
105-278 4.14e-24

E1-E2 ATPase;


Pssm-ID: 425475 [Multi-domain]  Cd Length: 181  Bit Score: 99.95  E-value: 4.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  105 TARLIEeNGAYRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGESAPVIKESGgdfDGVIGGTLVTSDWL 184
Cdd:pfam00122   6 TATVLR-DGTEEEVPADELVPGDIVLLKPGERVPADGRIVEGSASVDESLLTGESLPVEKKKG---DMVYSGTVVVSGSA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  185 EIRVESEAGTSFLDKMIALVEGAERNKTPNEIALFTLLTTLTIIFLVVIVTLYPIASYLHLILPIAMLIALTVCL--IPT 262
Cdd:pfam00122  82 KAVVTATGEDTELGRIARLVEEAKSKKTPLQRLLDRLGKYFSPVVLLIALAVFLLWLFVGGPPLRALLRALAVLVaaCPC 161
                         170
                  ....*....|....*.
gi 446468755  263 TIGGLLSAIGIAGMDR 278
Cdd:pfam00122 162 ALPLATPLALAVGARR 177
P-type_ATPase_Mg cd02077
magnesium transporting ATPase (MgtA), similar to Escherichia coli MgtA and Salmonella ...
87-562 2.90e-22

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: 101.94  E-value: 2.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  87 EGRGKAQADSLRQAQSNlTARLIEENGAYRIVNATELKAGQNIRVENGETIPADGVVI--NGLaTVDESAITGESAPVIK 164
Cdd:cd02077   85 EIRSLKAAEKLKKMVKN-TATVIRDGSKYMEIPIDELVPGDIVYLSAGDMIPADVRIIqsKDL-FVSQSSLTGESEPVEK 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 165 --ESGGDFDG--------VIGGTLVTS-DWLEIRVESEAGTSFLDKMIALVEgaERNKTPNEIALFTLLTTLTIIFLVVI 233
Cdd:cd02077  163 haTAKKTKDEsileleniCFMGTNVVSgSALAVVIATGNDTYFGSIAKSITE--KRPETSFDKGINKVSKLLIRFMLVMV 240
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 234 VTLYPIASYLH------LILPIAMLIALTVCLIPTTIGGLLSAigiaGMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTG 307
Cdd:cd02077  241 PVVFLINGLTKgdwleaLLFALAVAVGLTPEMLPMIVTSNLAK----GAVRMSKRKVIVKNLNAIQNFGAMDILCTDKTG 316
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 308 TITYGNRIASEFLPVNQQMMEKLIVAAYMSSIYD---DTPEGKSIVRLAKQMYINELPKDIdgtYK----PFTAETR-MS 379
Cdd:cd02077  317 TLTQDKIVLERHLDVNGKESERVLRLAYLNSYFQtglKNLLDKAIIDHAEEANANGLIQDY---TKideiPFDFERRrMS 393
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 380 GIITNEIS----VFKGAPNSMINL---VKQQQGNIPLN------IESICMDVSSKG---------------GTPLIVIEN 431
Cdd:cd02077  394 VVVKDNDGkhllITKGAVEEILNVcthVEVNGEVVPLTdtlrekILAQVEELNREGlrvlaiaykklpapeGEYSVKDEK 473
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 432 N-VMLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEAG--VDRFV---------------------- 486
Cdd:cd02077  474 ElILIGFLAFLDPPKESAAQAIKALKKNGVNVKILTGDNEIVTKAICKQVGldINRVLtgseiealsdeelakiveetni 553
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446468755 487 -AECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAANLIDLDSNPTKLIEVVKIGKQ 562
Cdd:cd02077  554 fAKLSPLQKARIIQALKKNGHVVGFMGDGINDAPALRQADVGISVDSAVDIAKEAADIILLEKDLMVLEEGVIEGRK 630
P-type_ATPase_Na_ENA cd02086
fungal-type Na(+)-ATPase, similar to the plasma membrane sodium transporters Saccharomyces ...
85-563 1.24e-21

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: 100.22  E-value: 1.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  85 FAEGRGKAQADSLRqAQSNLTARLIEeNGAYRIVNATELKAGQNIRVENGETIPADGVVINGLA-TVDESAITGESAPVI 163
Cdd:cd02086   75 IQEYKAEKTMDSLR-NLSSPNAHVIR-SGKTETISSKDVVPGDIVLLKVGDTVPADLRLIETKNfETDEALLTGESLPVI 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 164 KESGGDFDG------------VIGGTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTPNEIALFTLLTTLTIIFLV 231
Cdd:cd02086  153 KDAELVFGKeedvsvgdrlnlAYSSSTVTKGRAKGIVVATGMNTEIGKIAKALRGKGGLISRDRVKSWLYGTLIVTWDAV 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 232 VIVTLYPIASYLH--------LILPIAML---------------------IALTVCLIPTTIGGLLSAIGIAGMDRVTQF 282
Cdd:cd02086  233 GRFLGTNVGTPLQrklsklayLLFFIAVIlaiivfavnkfdvdneviiyaIALAISMIPESLVAVLTITMAVGAKRMVKR 312
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 283 NVLAKSGRAVEVCGDVDVMILDKTGTITYGNRIASE-FLPV---NQQMMEKLIVAAYMSSIYDDTPEGKSIVRLAKQMYI 358
Cdd:cd02086  313 NVIVRKLDALEALGAVTDICSDKTGTLTQGKMVVRQvWIPAalcNIATVFKDEETDCWKAHGDPTEIALQVFATKFDMGK 392
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 359 NELPKDIDGTYK-----PFTAET-RMSGIITN----EISVF-KGAPNSMINL---VKQQQGNIPL----------NIESI 414
Cdd:cd02086  393 NALTKGGSAQFQhvaefPFDSTVkRMSVVYYNnqagDYYAYmKGAVERVLECcssMYGKDGIIPLddefrktiikNVESL 472
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 415 C--------------------MDVSSKGGTPLIVIENN-VMLGVIYLKDVIKD---GLVERFAElrkMGIETVMCTGDNA 470
Cdd:cd02086  473 AsqglrvlafasrsftkaqfnDDQLKNITLSRADAESDlTFLGLVGIYDPPRNesaGAVEKCHQ---AGITVHMLTGDHP 549
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 471 LTAATIAKEAG-VDRF------------------------------------VAECKPEDKIKVIKDEQAKGHIVAMTGD 513
Cdd:cd02086  550 GTAKAIAREVGiLPPNsyhysqeimdsmvmtasqfdglsdeevdalpvlplvIARCSPQTKVRMIEALHRRKKFCAMTGD 629
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446468755 514 GTNDAPALAQANIGLAMN-SGTISAKEAANLIDLDSNPTKLIEVVKIGKQL 563
Cdd:cd02086  630 GVNDSPSLKMADVGIAMGlNGSDVAKDASDIVLTDDNFASIVNAIEEGRRM 680
ATPase-IIIB_Mg TIGR01524
magnesium-translocating P-type ATPase; This model describes the magnesium translocating P-type ...
87-562 4.13e-21

magnesium-translocating P-type ATPase; This model describes the magnesium translocating P-type ATPase found in a limited number of bacterial species and best described in Salmonella typhimurium, which contains two isoforms. These transporters are active in low external Mg2+ concentrations and pump the ion into the cytoplasm. The magnesium ATPases have been classified as type IIIB by a phylogenetic analysis. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 130587 [Multi-domain]  Cd Length: 867  Bit Score: 98.40  E-value: 4.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755   87 EGRGKAQADSLRQAQSNLTA--RLIEEN--GAYRIVNATELKAGQNIRVENGETIPADGVVINGLAT-VDESAITGESAP 161
Cdd:TIGR01524 109 ESRAERAAYALKNMVKNTATvlRVINENgnGSMDEVPIDALVPGDLIELAAGDIIPADARVISARDLfINQSALTGESLP 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  162 VIK---------ESGGDFDGV-IGGTLVTSDWLE-IRVESEAGTSFLDKMIALVEGAERN---KTPNEIALFTLLTTLTI 227
Cdd:TIGR01524 189 VEKfvedkrardPEILERENLcFMGTNVLSGHAQaVVLATGSSTWFGSLAIAATERRGQTafdKGVKSVSKLLIRFMLVM 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  228 IFLVVIVTLYPIASYLHLIL-PIAMLIALTVCLIPTTIGGLLSAIGIAgmdrVTQFNVLAKSGRAVEVCGDVDVMILDKT 306
Cdd:TIGR01524 269 VPVVLMINGLMKGDWLEAFLfALAVAVGLTPEMLPMIVSSNLAKGAIN----MSKKKVIVKELSAIQNFGAMDILCTDKT 344
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  307 GTITYGNRIASEFLPVNQQMMEKLIVAAYMSSIY----------------DDTPEGKSIVRLAKqmyINELPKDIDgtyk 370
Cdd:TIGR01524 345 GTLTQDKIELEKHIDSSGETSERVLKMAWLNSYFqtgwknvldhavlaklDESAARQTASRWKK---VDEIPFDFD---- 417
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  371 pftaETRMSGIITNEIS----VFKGAPNSMINLVKQQQGN---IPLN------IESICMDVSSKGGTPLIVI-------E 430
Cdd:TIGR01524 418 ----RRRLSVVVENRAEvtrlICKGAVEEMLTVCTHKRFGgavVTLSesekseLQDMTAEMNRQGIRVIAVAtktlkvgE 493
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  431 NN---------VMLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEAGVD------------------ 483
Cdd:TIGR01524 494 ADftktdeeqlIIEGFLGFLDPPKESTKEAIAALFKNGINVKVLTGDNEIVTARICQEVGIDandfllgadieelsdeel 573
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  484 -------RFVAECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAANLIDLDSNPTKLIEV 556
Cdd:TIGR01524 574 arelrkyHIFARLTPMQKSRIIGLLKKAGHTVGFLGDGINDAPALRKADVGISVDTAADIAKEASDIILLEKSLMVLEEG 653

                  ....*.
gi 446468755  557 VKIGKQ 562
Cdd:TIGR01524 654 VIEGRN 659
P-type_ATPase_Na-K_like cd02608
alpha-subunit of Na(+)/K(+)-ATPases and of gastric H(+)/K(+)-ATPase, similar to the human Na(+) ...
108-549 1.34e-20

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


Pssm-ID: 319794 [Multi-domain]  Cd Length: 905  Bit Score: 97.03  E-value: 1.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 108 LIEENGAYRIVNATELKAGQNIRVENGETIPADGVVI--NGLaTVDESAITGESAPviKESGGDFdgviggtlvTSD-WL 184
Cdd:cd02608  109 LVIRDGEKMQINAEELVVGDLVEVKGGDRIPADIRIIsaHGC-KVDNSSLTGESEP--QTRSPEF---------THEnPL 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 185 EIR---------VESEA-----GT---SFLDKMIALVEGAERNKTPneIALFTLLTTLTIIFLVVI--VTLYPIASYL-- 243
Cdd:cd02608  177 ETKniaffstncVEGTArgiviNTgdrTVMGRIATLASGLEVGKTP--IAREIEHFIHIITGVAVFlgVSFFILSLILgy 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 244 HLILPIAMLIALTVCLIPTtigGLLSAIGIA---GMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTITYgNRIASEFL 320
Cdd:cd02608  255 TWLEAVIFLIGIIVANVPE---GLLATVTVCltlTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQ-NRMTVAHM 330
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 321 PVNQQMMEKLIVAAYMSSIYDDTPEG-KSIVRLA----------KQMYINELPKDIDG---------------------- 367
Cdd:cd02608  331 WFDNQIHEADTTEDQSGASFDKSSATwLALSRIAglcnraefkaGQENVPILKRDVNGdasesallkcielscgsvmemr 410
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 368 ------TYKPF--TAETRMSgIITNE-------ISVFKGAPNSMINLVKqqqgNIPLNIESICMDVSSK----------G 422
Cdd:cd02608  411 ernpkvAEIPFnsTNKYQLS-IHENEdpgdpryLLVMKGAPERILDRCS----TILINGKEQPLDEEMKeafqnaylelG 485
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 423 G---------------------------TPLIVIENNVMLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAAT 475
Cdd:cd02608  486 GlgervlgfchlylpddkfpegfkfdtdEVNFPTENLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKA 565
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446468755 476 IAKEAGVDRFvAECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMN-SGTISAKEAANLIDLDSN 549
Cdd:cd02608  566 IAKGVGIIVF-ARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGiAGSDVSKQAADMILLDDN 639
P-type_ATPase_SERCA cd02083
sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; ...
456-549 7.70e-19

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: 91.20  E-value: 7.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 456 RKMGIETVMCTGDNALTAATIAKEAGV-------------------------------DRFVAECKPEDKIKVIKDEQAK 504
Cdd:cd02083  605 RDAGIRVIVITGDNKGTAEAICRRIGIfgededttgksytgrefddlspeeqreacrrARLFSRVEPSHKSKIVELLQSQ 684
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446468755 505 GHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAANLIDLDSN 549
Cdd:cd02083  685 GEITAMTGDGVNDAPALKKAEIGIAMGSGTAVAKSASDMVLADDN 729
ATPase-IIA1_Ca TIGR01116
sarco/endoplasmic reticulum calcium-translocating P-type ATPase; This model describes the ...
436-561 2.19e-17

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: 86.76  E-value: 2.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  436 GVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEAGV-------------------------------DR 484
Cdd:TIGR01116 530 GVVGMLDPPRPEVADAIEKCRTAGIRVIMITGDNKETAEAICRRIGIfspdedvtfksftgrefdemgpakqraacrsAV 609
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446468755  485 FVAECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAANLIDLDSNPTKLIEVVKIGK 561
Cdd:TIGR01116 610 LFSRVEPSHKSELVELLQEQGEIVAMTGDGVNDAPALKKADIGIAMGSGTEVAKEASDMVLADDNFATIVAAVEEGR 686
P-type_ATPase_cation cd02082
P-type cation-transporting ATPases, similar to human ATPase type 13A1-A4 (ATP13A1-A4) proteins ...
89-586 2.58e-17

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: 86.11  E-value: 2.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  89 RGKAQADSLRQAQSNLTARLIEENGAYRIVNATELKAGQNIRV-ENGETIPADGVVINGLATVDESAITGESAPVIKESG 167
Cdd:cd02082   71 RGVMQKELKDACLNNTSVIVQRHGYQEITIASNMIVPGDIVLIkRREVTLPCDCVLLEGSCIVTEAMLTGESVPIGKCQI 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 168 GDF--DGVI------------GGTLV------TSDWLEIRVESEAGTSFLDKMI-ALVEGAERNKTPNEIALFTLLTTLT 226
Cdd:cd02082  151 PTDshDDVLfkyesskshtlfQGTQVmqiippEDDILKAIVVRTGFGTSKGQLIrAILYPKPFNKKFQQQAVKFTLLLAT 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 227 IIFLVVIVTLypIASYLHLILPIAMLIALTVCLIPTTIGGLLSAIGIA---GMDRVTQFNVLAKSGRAVEVCGDVDVMIL 303
Cdd:cd02082  231 LALIGFLYTL--IRLLDIELPPLFIAFEFLDILTYSVPPGLPMLIAITnfvGLKRLKKNQILCQDPNRISQAGRIQTLCF 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 304 DKTGTIT---------YGNRIASEFLPV-NQQMMEKLIVAAYMSSIYDDTPEGKSIV--RLAKQMY------------IN 359
Cdd:cd02082  309 DKTGTLTedkldligyQLKGQNQTFDPIqCQDPNNISIEHKLFAICHSLTKINGKLLgdPLDVKMAeastwdldydheAK 388
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 360 ELPKDIdGTYK-------PFTAE-TRMS------GIITNE---ISVFKGAPNSMINLVKQqqgnIPLNIESICMDVSSKG 422
Cdd:cd02082  389 QHYSKS-GTKRfyiiqvfQFHSAlQRMSvvakevDMITKDfkhYAFIKGAPEKIQSLFSH----VPSDEKAQLSTLINEG 463
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 423 GTPLIV--------------------IENNV-MLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEAG 481
Cdd:cd02082  464 YRVLALgykelpqseidafldlsreaQEANVqFLGFIIYKNNLKPDTQAVIKEFKEACYRIVMITGDNPLTALKVAQELE 543
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 482 V----------------DRFVAECK--------------PEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMN 531
Cdd:cd02082  544 IinrknptiiihllipeIQKDNSTQwiliihtnvfartaPEQKQTIIRLLKESDYIVCMCGDGANDCGALKEADVGISLA 623
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446468755 532 SGtiSAKEAANLIDLDSNPTKLIEVVKIGKQLLMTRGALTTFSLANDVAKYFAIL 586
Cdd:cd02082  624 EA--DASFASPFTSKSTSISCVKRVILEGRVNLSTSVEIFKGYALVALIRYLSFL 676
PRK10517 PRK10517
magnesium-transporting P-type ATPase MgtA;
87-547 3.89e-17

magnesium-transporting P-type ATPase MgtA;


Pssm-ID: 236705 [Multi-domain]  Cd Length: 902  Bit Score: 85.89  E-value: 3.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  87 EGRGKAQADSLRQAQSNlTA---RLIEENGAYRIVNA--TELKAGQNIRVENGETIPADGVVINGLAT-VDESAITGESA 160
Cdd:PRK10517 143 EARSTKAADALKAMVSN-TAtvlRVINDKGENGWLEIpiDQLVPGDIIKLAAGDMIPADLRILQARDLfVAQASLTGESL 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 161 PVIK-------ESGGDFDG---VIGGTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTP-----NEIALFTLLTTL 225
Cdd:PRK10517 222 PVEKfattrqpEHSNPLECdtlCFMGTNVVSGTAQAVVIATGANTWFGQLAGRVSEQDSEPNAfqqgiSRVSWLLIRFML 301
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 226 TIIFLVVIVTLYPIASYLHlilpiAMLIALTVC--LIPTTIGGLLSAIGIAGMDRVTQFNVLAKSGRAVEVCGDVDVMIL 303
Cdd:PRK10517 302 VMAPVVLLINGYTKGDWWE-----AALFALSVAvgLTPEMLPMIVTSTLARGAVKLSKQKVIVKRLDAIQNFGAMDILCT 376
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 304 DKTGTITYgNRIASE-FLPVNQQMMEKLIVAAYMSSIYD-------DTP--EGksiVRLAKQMYINELPKDIDGTykPFT 373
Cdd:PRK10517 377 DKTGTLTQ-DKIVLEnHTDISGKTSERVLHSAWLNSHYQtglknllDTAvlEG---VDEESARSLASRWQKIDEI--PFD 450
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 374 AETR-MSGIITNEIS----VFKGAPNSMINL---VKQQQGNIPLN------IESICMDVSSKG---------------GT 424
Cdd:PRK10517 451 FERRrMSVVVAENTEhhqlICKGALEEILNVcsqVRHNGEIVPLDdimlrrIKRVTDTLNRQGlrvvavatkylpareGD 530
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 425 PLIVIENNVML-GVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEAGVD-------------------- 483
Cdd:PRK10517 531 YQRADESDLILeGYIAFLDPPKETTAPALKALKASGVTVKILTGDSELVAAKVCHEVGLDagevligsdietlsddelan 610
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446468755 484 -----RFVAECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAANLIDLD 547
Cdd:PRK10517 611 laertTLFARLTPMHKERIVTLLKREGHVVGFMGDGINDAPALRAADIGISVDGAVDIAREAADIILLE 679
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
298-525 3.19e-16

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: 77.24  E-value: 3.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  298 VDVMILDKTGTITYGNRIASEFLPvnqqmmeklivaaymsSIYDDTPEGKSIVRLAKQMYINelpkdidgtykpftaetr 377
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIA----------------ELASEHPLAKAIVAAAEDLPIP------------------ 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  378 msgIITNEISVFKGAPNSMINLVKQQQGNIPLNIEsicmdvsskggTPLIVIENNVMLGVIYLKDVIKDGLVERFAELRK 457
Cdd:pfam00702  47 ---VEDFTARLLLGKRDWLEELDILRGLVETLEAE-----------GLTVVLVELLGVIALADELKLYPGAAEALKALKE 112
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446468755  458 MGIETVMCTGDNALTAATIAKEAGVDRF-----------VAECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQAN 525
Cdd:pfam00702 113 RGIKVAILTGDNPEAAEALLRLLGLDDYfdvvisgddvgVGKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
P-type_ATPase_cation cd07542
P-type cation-transporting ATPases, similar to human ATPase type 13A2 (ATP13A2) protein and ...
112-527 3.72e-16

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: 82.30  E-value: 3.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 112 NGAYRIVNATELKAGQNIRV-ENGETIPADGVVINGLATVDESAITGESAPVIKESGGDFDGVIggtlvtsdWLEIRVES 190
Cdd:cd07542   94 DGEWQTISSSELVPGDILVIpDNGTLLPCDAILLSGSCIVNESMLTGESVPVTKTPLPDESNDS--------LWSIYSIE 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 191 E-------AGTSFLDkmialvegAERNKTPNEIALFTLLTTLTIIFLVVIVTLYPIAS----YLHLILPIAMLIAL---- 255
Cdd:cd07542  166 DhskhtlfCGTKVIQ--------TRAYEGKPVLAVVVRTGFNTTKGQLVRSILYPKPVdfkfYRDSMKFILFLAIIalig 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 256 ---TVC------------------LIPTTIGGLLSA---IGIA-GMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTIT 310
Cdd:cd07542  238 fiyTLIililngeslgeiiiraldIITIVVPPALPAaltVGIIyAQSRLKKKGIFCISPQRINICGKINLVCFDKTGTLT 317
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 311 ------YGNRIASeflPVNQQMMEKLIVAAYMSSIYDDTPEGKSIVRLAKQMYIN-EL---PKDI------DGTYK---- 370
Cdd:cd07542  318 edgldlWGVRPVS---GNNFGDLEVFSLDLDLDSSLPNGPLLRAMATCHSLTLIDgELvgdPLDLkmfeftGWSLEilrq 394
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 371 -PFTAE-TRMSGIIT----NEISVF-KGAPNSMINLVKQQqgNIPLNIESICMDVSSKG-------GTPLIV-------- 428
Cdd:cd07542  395 fPFSSAlQRMSVIVKtpgdDSMMAFtKGAPEMIASLCKPE--TVPSNFQEVLNEYTKQGfrvialaYKALESktwllqkl 472
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 429 ----IENNV-MLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEAGV---DRFV-------------- 486
Cdd:cd07542  473 sreeVESDLeFLGLIVMENRLKPETAPVINELNRANIRTVMVTGDNLLTAISVARECGMispSKKVilieavkpedddsa 552
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446468755 487 -------------AECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIG 527
Cdd:cd07542  553 sltwtlllkgtvfARMSPDQKSELVEELQKLDYTVGMCGDGANDCGALKAADVG 606
PRK15122 PRK15122
magnesium-transporting ATPase; Provisional
250-604 8.44e-16

magnesium-transporting ATPase; Provisional


Pssm-ID: 237914 [Multi-domain]  Cd Length: 903  Bit Score: 81.61  E-value: 8.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 250 AMLIALTVC--LIPTTIGGLLS---AIGIAGMDRVtqfNVLAKSGRAVEVCGDVDVMILDKTGTITYGNRIASEFLPVNQ 324
Cdd:PRK15122 319 ALLFALAVAvgLTPEMLPMIVSsnlAKGAIAMARR---KVVVKRLNAIQNFGAMDVLCTDKTGTLTQDRIILEHHLDVSG 395
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 325 QMMEKLIVAAYMSSIY----------------DDTPEGKSIVRLAKqmyINELPKDIdgtykpftAETRMSGIITNEIS- 387
Cdd:PRK15122 396 RKDERVLQLAWLNSFHqsgmknlmdqavvafaEGNPEIVKPAGYRK---VDELPFDF--------VRRRLSVVVEDAQGq 464
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 388 ---VFKGAPNSMINL---VKQQQGNIPLN------IESICMDVSSKGGTPLIVI-----------------ENN-VMLGV 437
Cdd:PRK15122 465 hllICKGAVEEMLAVathVRDGDTVRPLDearrerLLALAEAYNADGFRVLLVAtreipggesraqystadERDlVIRGF 544
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 438 IYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEAGVD-------------------RFVAEC------KPE 492
Cdd:PRK15122 545 LTFLDPPKESAAPAIAALRENGVAVKVLTGDNPIVTAKICREVGLEpgepllgteieamddaalaREVEERtvfaklTPL 624
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 493 DKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAANLIDLDSNPTKLIE-VVK-------IGKQLL 564
Cdd:PRK15122 625 QKSRVLKALQANGHTVGFLGDGINDAPALRDADVGISVDSGADIAKESADIILLEKSLMVLEEgVIKgretfgnIIKYLN 704
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 446468755 565 MTrgALTTFSLANDVAKYFAILPALMMSTIpEMTSLNIMH 604
Cdd:PRK15122 705 MT--ASSNFGNVFSVLVASAFIPFLPMLAI-HLLLQNLMY 741
P-ATPase-V TIGR01657
P-type ATPase of unknown pump specificity (type V); These P-type ATPases form a distinct clade ...
112-530 1.03e-15

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: 81.26  E-value: 1.03e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755   112 NGAYRIVNATELKAGQ--NIRVENGETIPADGVVINGLATVDESAITGESAPVIKES---GGDFDGVI------------ 174
Cdd:TIGR01657  236 NGKWVTIASDELVPGDivSIPRPEEKTMPCDSVLLSGSCIVNESMLTGESVPVLKFPipdNGDDDEDLflyetskkhvlf 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755   175 GGTLV------TSDW--LEIRVESEAGTSFLDKMIALVEGAERNKTPNE-----IALFTLLTTLTIIFLVVIVTLYPiAS 241
Cdd:TIGR01657  316 GGTKIlqirpyPGDTgcLAIVVRTGFSTSKGQLVRSILYPKPRVFKFYKdsfkfILFLAVLALIGFIYTIIELIKDG-RP 394
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755   242 YLHLILPIAMLIALTVcliPTTIGGLLSAIGIAGMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTIT---------YG 312
Cdd:TIGR01657  395 LGKIILRSLDIITIVV---PPALPAELSIGINNSLARLKKKGIFCTSPFRINFAGKIDVCCFDKTGTLTedgldlrgvQG 471
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755   313 NRIASEFLPVNQQMME-------KLIVAAYMSSIYDDTPEGKSI-VRLAKQM--------------YINELPKDIDGTYK 370
Cdd:TIGR01657  472 LSGNQEFLKIVTEDSSlkpsithKALATCHSLTKLEGKLVGDPLdKKMFEATgwtleeddesaeptSILAVVRTDDPPQE 551
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755   371 -------PFTAE-TRMSGI--ITNEISVF---KGAPNSMINLVKQQQgnIPLNIESICMDVSSKG-------GTPLIV-- 428
Cdd:TIGR01657  552 lsiirrfQFSSAlQRMSVIvsTNDERSPDafvKGAPETIQSLCSPET--VPSDYQEVLKSYTREGyrvlalaYKELPKlt 629
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755   429 -----------IENNV-MLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEAG--------------- 481
Cdd:TIGR01657  630 lqkaqdlsrdaVESNLtFLGFIVFENPLKPDTKEVIKELKRASIRTVMITGDNPLTAVHVARECGivnpsntlilaeaep 709
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755   482 --------------------------------------------------------------VDRFVAECK------PED 493
Cdd:TIGR01657  710 pesgkpnqikfevidsipfastqveipyplgqdsvedllasryhlamsgkafavlqahspelLLRLLSHTTvfarmaPDQ 789
                          570       580       590
                   ....*....|....*....|....*....|....*..
gi 446468755   494 KIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAM 530
Cdd:TIGR01657  790 KETLVELLQKLDYTVGMCGDGANDCGALKQADVGISL 826
ATPase-IIC_X-K TIGR01106
sodium or proton efflux -- potassium uptake antiporter, P-type ATPase, alpha subunit; This ...
108-561 9.22e-15

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


Pssm-ID: 273445 [Multi-domain]  Cd Length: 997  Bit Score: 78.29  E-value: 9.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  108 LIEENGAYRIVNATELKAGQNIRVENGETIPADGVVI--NGLaTVDESAITGESAPviKESGGDF--------------- 170
Cdd:TIGR01106 144 LVIRDGEKMSINAEQVVVGDLVEVKGGDRIPADLRIIsaQGC-KVDNSSLTGESEP--QTRSPEFthenpletrniaffs 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  171 ----DGVIGGTLV-TSDwleirveseagTSFLDKMIALVEGAERNKTPNEIALFTLLTTLTIIFLVVIVTLYPIASYL-- 243
Cdd:TIGR01106 221 tncvEGTARGIVVnTGD-----------RTVMGRIASLASGLENGKTPIAIEIEHFIHIITGVAVFLGVSFFILSLILgy 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  244 HLILPIAMLIALTVCLIPTtigGLLSAIGIA---GMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTITYgNRIASEFL 320
Cdd:TIGR01106 290 TWLEAVIFLIGIIVANVPE---GLLATVTVCltlTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQ-NRMTVAHM 365
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  321 PVNQQMMEKLIVAAYMSSIYDDTPEG-KSIVRLAK----------QMYINELPKDIDG---------------------- 367
Cdd:TIGR01106 366 WFDNQIHEADTTEDQSGVSFDKSSATwLALSRIAGlcnravfkagQENVPILKRAVAGdasesallkcielclgsvmemr 445
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  368 ------TYKPFTAETRMS-GIITNEIS-------VFKGAPNSMIN-----LVKQQQgnIPLNIESI------CMDVSSKG 422
Cdd:TIGR01106 446 ernpkvVEIPFNSTNKYQlSIHENEDPrdprhllVMKGAPERILErcssiLIHGKE--QPLDEELKeafqnaYLELGGLG 523
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  423 GTPL------------------------IVIENNVMLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAK 478
Cdd:TIGR01106 524 ERVLgfchlylpdeqfpegfqfdtddvnFPTDNLCFVGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAK 603
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  479 EAGV-----------------------------------------------------DRFVAECKPEDKIKVIKDEQAKG 505
Cdd:TIGR01106 604 GVGIisegnetvediaarlnipvsqvnprdakacvvhgsdlkdmtseqldeilkyhtEIVFARTSPQQKLIIVEGCQRQG 683
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446468755  506 HIVAMTGDGTNDAPALAQANIGLAMN-SGTISAKEAANLIDLDSNPTKLIEVVKIGK 561
Cdd:TIGR01106 684 AIVAVTGDGVNDSPALKKADIGVAMGiAGSDVSKQAADMILLDDNFASIVTGVEEGR 740
ATPase-IID_K-Na TIGR01523
potassium and/or sodium efflux P-type ATPase, fungal-type; Initially described as a calcium ...
447-563 3.60e-13

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: 73.12  E-value: 3.60e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755   447 GLVERFaelRKMGIETVMCTGDNALTAATIAKEAGV-------DR------------------------------FVAEC 489
Cdd:TIGR01523  653 GAVEKC---HQAGINVHMLTGDFPETAKAIAQEVGIippnfihDRdeimdsmvmtgsqfdalsdeevddlkalclVIARC 729
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446468755   490 KPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMN-SGTISAKEAANLIDLDSNPTKLIEVVKIGKQL 563
Cdd:TIGR01523  730 APQTKVKMIEALHRRKAFCAMTGDGVNDSPSLKMANVGIAMGiNGSDVAKDASDIVLSDDNFASILNAIEEGRRM 804
P-type_ATPase_cation cd07543
P-type cation-transporting ATPases, similar to human cation-transporting ATPase type 13A1 ...
444-530 5.27e-09

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: 59.32  E-value: 5.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 444 IKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEAG-VDRFV-----------------------AECKPEDKIKVIK 499
Cdd:cd07543  510 LKPDSKETIKELNNSSHRVVMITGDNPLTACHVAKELGiVDKPVlililseegksnewkliphvkvfARVAPKQKEFIIT 589
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446468755 500 DEQAKGHIVAMTGDGTNDAPALAQANIGLAM 530
Cdd:cd07543  590 TLKELGYVTLMCGDGTNDVGALKHAHVGVAL 620
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
444-531 5.26e-05

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: 44.83  E-value: 5.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 444 IKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEAGVDRFVA---E--------------CKPEDKIKVIKDEQAK-- 504
Cdd:COG0560   89 LYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIAnelEvedgrltgevvgpiVDGEGKAEALRELAAElg 168
                         90       100       110
                 ....*....|....*....|....*....|
gi 446468755 505 ---GHIVAMtGDGTNDAPALAQANIGLAMN 531
Cdd:COG0560  169 idlEQSYAY-GDSANDLPMLEAAGLPVAVN 197
HAD pfam12710
haloacid dehalogenase-like hydrolase;
440-521 1.12e-03

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 40.59  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755  440 LKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEAGVDRFVAE-------------------CKPEDKIKVIKD 500
Cdd:pfam12710  81 ALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLATelevddgrftgelrligppCAGEGKVRRLRA 160
                          90       100
                  ....*....|....*....|....*...
gi 446468755  501 -------EQAKGHIVAMtGDGTNDAPAL 521
Cdd:pfam12710 161 wlaarglGLDLADSVAY-GDSPSDLPML 187
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
441-544 1.70e-03

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: 39.11  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 441 KDVIKDGLVERFAELRKMGIETVMCTGdNALTAA-TIAKEAGVDR-FVAECKPEDK---IKVIKDEQA--KGHIVAMtGD 513
Cdd:cd07514   14 RRSIDLRAIEAIRKLEKAGIPVVLVTG-NSLPVArALAKYLGLSGpVVAENGGVDKgtgLEKLAERLGidPEEVLAI-GD 91
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446468755 514 GTNDAPALAQANIGLAMNSGTISAKEAANLI 544
Cdd:cd07514   92 SENDIEMFKVAGFKVAVANADEELKEAADYV 122
P-type_ATPase_APLT cd07536
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ...
429-511 2.81e-03

Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, Neo1p, and human ATP8A2, -9B, -10D, -11B, and -11C; Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. Yeast Dnf1 and Dnf2 mediate the transport of phosphatidylethanolamine, phosphatidylserine, and phosphatidylcholine from the outer to the inner leaflet of the plasma membrane. Mammalian ATP11C may selectively transports PS and PE from the outer leaflet of the plasma membrane to the inner leaflet. The yeast Neo1p localizes to the endoplasmic reticulum and the Golgi complex and plays a role in membrane trafficking within the endomembrane system. Human putative ATPase phospholipid transporting 9B, ATP9B, localizes to the trans-golgi network in a CDC50 protein-independent manner. It also includes Arabidopsis phospholipid flippases including ALA1, and Caenorhabditis elegans flippases, including TAT-1, the latter has been shown to facilitate the inward transport of phosphatidylserine. 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: 319838 [Multi-domain]  Cd Length: 805  Bit Score: 41.05  E-value: 2.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446468755 429 IENNV-MLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEAgvdRFVAeckPEDKIKVIKDEQAKGHI 507
Cdd:cd07536  497 LERELeLLGLTAIEDRLQAGVPETIETLRKAGIKIWMLTGDKQETAICIAKSC---HLVS---RTQDIHLLRQDTSRGER 570

                 ....
gi 446468755 508 VAMT 511
Cdd:cd07536  571 AAIT 574
 
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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