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Conserved domains on  [gi|15234666|ref|NP_194748|]
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H[+]-ATPase 2 [Arabidopsis thaliana]

Protein Classification

plasma-membrane proton-efflux P-type ATPase( domain architecture ID 11492973)

plasma-membrane proton-efflux P-type ATPase generates the proton motive force across the plasma membrane that is necessary to activate most of the ion and metabolite transport

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ATPase-IIIA_H TIGR01647
plasma-membrane proton-efflux P-type ATPase; This model describes the plasma membrane proton ...
32-804 0e+00

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: 1159.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    32 GLTTQEGEDRIQIFGPNKLEEKKESKLLKFLGFMWNPLSWVMEMAAIMAIALANgdgrppdWQDFVGIICLLVINSTISF 111
Cdd:TIGR01647   1 GLTSAEAKKRLAKYGPNELPEKKVSPLLKFLGFFWNPLSWVMEAAAIIAIALEN-------WVDFVIILGLLLLNATIGF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   112 IEENNAGNAAAALMAGLAPKTKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLKVDQSALTGESLPVTKH 191
Cdd:TIGR01647  74 IEENKAGNAVEALKQSLAPKARVLRDGKWQEIPASELVPGDVVRLKIGDIVPADCRLFEGDYIQVDQAALTGESLPVTKK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   192 PGQEVFSGSTCKQGEIEAVVIATGVHTFFGKAAHLVDSTN-QVGHFQKVLTAIGNFCICSIAIGMVIEIIVMYPIQRRKY 270
Cdd:TIGR01647 154 TGDIAYSGSTVKQGEAEAVVTATGMNTFFGKAAALVQSTEtGSGHLQKILSKIGLFLIVLIGVLVLIELVVLFFGRGESF 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   271 RDGIDNLLVLLIGGIPIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDKNLVevFC 350
Cdd:TIGR01647 234 REGLQFALVLLVGGIPIAMPAVLSVTMAVGAAELAKKKAIVTRLTAIEELAGMDILCSDKTGTLTLNKLSIDEILP--FF 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   351 KGVEKDQVLLFAAMASRVENQDAIDAAMVGMLADPKEARAGIREVHFLPFNPVDKRTALTYIDG-SGNWHRVSKGAPEQI 429
Cdd:TIGR01647 312 NGFDKDDVLLYAALASREEDQDAIDTAVLGSAKDLKEARDGYKVLEFVPFDPVDKRTEATVEDPeTGKRFKVTKGAPQVI 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   430 LELAKASNDLSKKVLSIIDKYAERGLRSLAVARQvvpektkeSPGAPWEFVGLLPLFDPPRHDSAETIRRALNLGVNVKM 509
Cdd:TIGR01647 392 LDLCDNKKEIEEKVEEKVDELASRGYRALGVART--------DEEGRWHFLGLLPLFDPPRHDTKETIERARHLGVEVKM 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   510 ITGDQLAIGKETGRRLGMGTNMYPSSALLGTHKDANLASiPVEELIEKADGFAGVFPEHKYEIVKKLQERKHIVGMTGDG 589
Cdd:TIGR01647 464 VTGDHLAIAKETARRLGLGTNIYTADVLLKGDNRDDLPS-GLGEMVEDADGFAEVFPEHKYEIVEILQKRGHLVGMTGDG 542
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   590 VNDAPALKKADIGIAVADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITIRIVFGFMLIALIWEF 669
Cdd:TIGR01647 543 VNDAPALKKADVGIAVAGATDAARSAADIVLTEPGLSVIVDAILESRKIFQRMKSYVIYRIAETIRIVFFFGLLILILNF 622
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   670 DFSAFMVLIIAILNDGTIMTISKDRVKPSPTPDSWKLKEIFATGVVLGGYQAIMTVIFFWAAHKTDFFSDTFGVRSIRDN 749
Cdd:TIGR01647 623 YFPPIMVVIIAILNDGTIMTIAYDNVKPSKLPQRWNLREVFTMSTVLGIYLVISTFLLLAIALDTTFFIDKFGLQLLHGN 702
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15234666   750 nheLMGAVYLQVSIISQALIFVTRSRSWSFVERPGALLMIAFLIAQLIATLIAVY 804
Cdd:TIGR01647 703 ---LQSFIYLQVSISGHATIFVTRTHGFFWSERPGKLLFGAFVIAQIIATFIAVY 754
 
Name Accession Description Interval E-value
ATPase-IIIA_H TIGR01647
plasma-membrane proton-efflux P-type ATPase; This model describes the plasma membrane proton ...
32-804 0e+00

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: 1159.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    32 GLTTQEGEDRIQIFGPNKLEEKKESKLLKFLGFMWNPLSWVMEMAAIMAIALANgdgrppdWQDFVGIICLLVINSTISF 111
Cdd:TIGR01647   1 GLTSAEAKKRLAKYGPNELPEKKVSPLLKFLGFFWNPLSWVMEAAAIIAIALEN-------WVDFVIILGLLLLNATIGF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   112 IEENNAGNAAAALMAGLAPKTKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLKVDQSALTGESLPVTKH 191
Cdd:TIGR01647  74 IEENKAGNAVEALKQSLAPKARVLRDGKWQEIPASELVPGDVVRLKIGDIVPADCRLFEGDYIQVDQAALTGESLPVTKK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   192 PGQEVFSGSTCKQGEIEAVVIATGVHTFFGKAAHLVDSTN-QVGHFQKVLTAIGNFCICSIAIGMVIEIIVMYPIQRRKY 270
Cdd:TIGR01647 154 TGDIAYSGSTVKQGEAEAVVTATGMNTFFGKAAALVQSTEtGSGHLQKILSKIGLFLIVLIGVLVLIELVVLFFGRGESF 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   271 RDGIDNLLVLLIGGIPIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDKNLVevFC 350
Cdd:TIGR01647 234 REGLQFALVLLVGGIPIAMPAVLSVTMAVGAAELAKKKAIVTRLTAIEELAGMDILCSDKTGTLTLNKLSIDEILP--FF 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   351 KGVEKDQVLLFAAMASRVENQDAIDAAMVGMLADPKEARAGIREVHFLPFNPVDKRTALTYIDG-SGNWHRVSKGAPEQI 429
Cdd:TIGR01647 312 NGFDKDDVLLYAALASREEDQDAIDTAVLGSAKDLKEARDGYKVLEFVPFDPVDKRTEATVEDPeTGKRFKVTKGAPQVI 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   430 LELAKASNDLSKKVLSIIDKYAERGLRSLAVARQvvpektkeSPGAPWEFVGLLPLFDPPRHDSAETIRRALNLGVNVKM 509
Cdd:TIGR01647 392 LDLCDNKKEIEEKVEEKVDELASRGYRALGVART--------DEEGRWHFLGLLPLFDPPRHDTKETIERARHLGVEVKM 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   510 ITGDQLAIGKETGRRLGMGTNMYPSSALLGTHKDANLASiPVEELIEKADGFAGVFPEHKYEIVKKLQERKHIVGMTGDG 589
Cdd:TIGR01647 464 VTGDHLAIAKETARRLGLGTNIYTADVLLKGDNRDDLPS-GLGEMVEDADGFAEVFPEHKYEIVEILQKRGHLVGMTGDG 542
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   590 VNDAPALKKADIGIAVADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITIRIVFGFMLIALIWEF 669
Cdd:TIGR01647 543 VNDAPALKKADVGIAVAGATDAARSAADIVLTEPGLSVIVDAILESRKIFQRMKSYVIYRIAETIRIVFFFGLLILILNF 622
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   670 DFSAFMVLIIAILNDGTIMTISKDRVKPSPTPDSWKLKEIFATGVVLGGYQAIMTVIFFWAAHKTDFFSDTFGVRSIRDN 749
Cdd:TIGR01647 623 YFPPIMVVIIAILNDGTIMTIAYDNVKPSKLPQRWNLREVFTMSTVLGIYLVISTFLLLAIALDTTFFIDKFGLQLLHGN 702
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15234666   750 nheLMGAVYLQVSIISQALIFVTRSRSWSFVERPGALLMIAFLIAQLIATLIAVY 804
Cdd:TIGR01647 703 ---LQSFIYLQVSISGHATIFVTRTHGFFWSERPGKLLFGAFVIAQIIATFIAVY 754
P-type_ATPase_H cd02076
plant and fungal plasma membrane H(+)-ATPases, and related bacterial and archaeal putative H(+) ...
32-839 0e+00

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: 1136.95  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  32 GLTTQEGEDRIQIFGPNKLEEKKESKLLKFLGFMWNPLSWVMEMAAIMAIAlangdgrPPDWQDFVGIICLLVINSTISF 111
Cdd:cd02076   1 GLTSEEAAKRLKEYGPNELPEKKENPILKFLSFFWGPIPWMLEAAAILAAA-------LGDWVDFAIILLLLLINAGIGF 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 112 IEENNAGNAAAALMAGLAPKTKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLKVDQSALTGESLPVTKH 191
Cdd:cd02076  74 IEERQAGNAVAALKKSLAPKARVLRDGQWQEIDAKELVPGDIVSLKIGDIVPADARLLTGDALQVDQSALTGESLPVTKH 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 192 PGQEVFSGSTCKQGEIEAVVIATGVHTFFGKAAHLVDSTNQVGHFQKVLTAIGNFCICSIAIGMVIEIIVMYPIQRRkYR 271
Cdd:cd02076 154 PGDEAYSGSIVKQGEMLAVVTATGSNTFFGKTAALVASAEEQGHLQKVLNKIGNFLILLALILVLIIVIVALYRHDP-FL 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 272 DGIDNLLVLLIGGIPIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDKNLVevfCK 351
Cdd:cd02076 233 EILQFVLVLLIASIPVAMPAVLTVTMAVGALELAKKKAIVSRLSAIEELAGVDILCSDKTGTLTLNKLSLDEPYS---LE 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 352 GVEKDQVLLFAAMASRVENQDAIDAAMVGMLADPKEARAGIREVHFLPFNPVDKRTALTYIDGSGNWHRVSKGAPEQILE 431
Cdd:cd02076 310 GDGKDELLLLAALASDTENPDAIDTAILNALDDYKPDLAGYKQLKFTPFDPVDKRTEATVEDPDGERFKVTKGAPQVILE 389
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 432 LAKASNDLSKKVLSIIDKYAERGLRSLAVARQVVpektkespGAPWEFVGLLPLFDPPRHDSAETIRRALNLGVNVKMIT 511
Cdd:cd02076 390 LVGNDEAIRQAVEEKIDELASRGYRSLGVARKED--------GGRWELLGLLPLFDPPRPDSKATIARAKELGVRVKMIT 461
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 512 GDQLAIGKETGRRLGMGTNMYPSSALLGTHKDANLASIPVEELIEKADGFAGVFPEHKYEIVKKLQERKHIVGMTGDGVN 591
Cdd:cd02076 462 GDQLAIAKETARQLGMGTNILSAERLKLGGGGGGMPGSELIEFIEDADGFAEVFPEHKYRIVEALQQRGHLVGMTGDGVN 541
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 592 DAPALKKADIGIAVADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITIRIVFGFMLIALIWEF-D 670
Cdd:cd02076 542 DAPALKKADVGIAVSGATDAARAAADIVLTAPGLSVIIDAIKTSRQIFQRMKSYVIYRIAETLRILVFFTLGILILNFyP 621
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 671 FSAFMVLIIAILNDGTIMTISKDRVKPSPTPDSWKLKEIFATGVVLGGYQAIMTVIFFWAAHKTDFFSDtfgvrsIRDNN 750
Cdd:cd02076 622 LPLIMIVLIAILNDGATLTIAYDNVPPSPRPVRWNMPELLGIATVLGVVLTISSFLLLWLLDDQGWFED------IVLSA 695
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 751 HELMGAVYLQVSIISQALIFVTRSRSWSFVERPGALLMIAFLIAQLIATLIAVYANWEFAkirGIGWGWAGVIWLYSIVT 830
Cdd:cd02076 696 GELQTILYLQLSISGHLTIFVTRTRGPFWRPRPSPLLFIAVVLTQILATLLAVYGWFMFA---GIGWGWALLVWIYALVW 772

                ....*....
gi 15234666 831 YFPLDVFKF 839
Cdd:cd02076 773 FVVLDFVKL 781
MgtA COG0474
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism];
8-842 0e+00

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


Pssm-ID: 440242 [Multi-domain]  Cd Length: 874  Bit Score: 610.19  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   8 KNETVDLEKIPIEEVFQQLKCSREGLTTQEGEDRIQIFGPNKL-EEKKESKLLKFLGFMWNPL----------SWVMEma 76
Cdd:COG0474   2 ATALKDWHALSAEEVLAELGTSEEGLSSEEAARRLARYGPNELpEEKKRSLLRRFLEQFKNPLilillaaaviSALLG-- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  77 aimaialangdgrppDWQDFVGIICLLVINSTISFIEENNAGNAAAALMAGLAPKTKVLRDGKWSEQEAAILVPGDIVSI 156
Cdd:COG0474  80 ---------------DWVDAIVILAVVLLNAIIGFVQEYRAEKALEALKKLLAPTARVLRDGKWVEIPAEELVPGDIVLL 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 157 KLGDIIPADARLLEGDPLKVDQSALTGESLPVTKHPGQE------------VFSGSTCKQGEIEAVVIATGVHTFFGKAA 224
Cdd:COG0474 145 EAGDRVPADLRLLEAKDLQVDESALTGESVPVEKSADPLpedaplgdrgnmVFMGTLVTSGRGTAVVVATGMNTEFGKIA 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 225 HLVDSTNQV-GHFQKVLTAIGNFCIcSIAIGMVIEIIVMYPIQRrkyRDGIDNLLV---LLIGGIPIAMPTVLSVTMAIG 300
Cdd:COG0474 225 KLLQEAEEEkTPLQKQLDRLGKLLA-IIALVLAALVFLIGLLRG---GPLLEALLFavaLAVAAIPEGLPAVVTITLALG 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 301 SHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVdknlVEVFCKGVEKD----------QVLLFAAMAS---- 366
Cdd:COG0474 301 AQRMAKRNAIVRRLPAVETLGSVTVICTDKTGTLTQNKMTV----ERVYTGGGTYEvtgefdpaleELLRAAALCSdaql 376
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 367 --RVENQDAIDAAMVGMLA----DPKEARAGIREVHFLPFNPVDKRTALTYIDGSGNWHRVSKGAPEQILELAKA----- 435
Cdd:COG0474 377 eeETGLGDPTEGALLVAAAkaglDVEELRKEYPRVDEIPFDSERKRMSTVHEDPDGKRLLIVKGAPEVVLALCTRvltgg 456
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 436 -----SNDLSKKVLSIIDKYAERGLRSLAVARQVVPEKTKESPGAP---WEFVGLLPLFDPPRHDSAETIRRALNLGVNV 507
Cdd:COG0474 457 gvvplTEEDRAEILEAVEELAAQGLRVLAVAYKELPADPELDSEDDesdLTFLGLVGMIDPPRPEAKEAIAECRRAGIRV 536
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 508 KMITGDQLAIGKETGRRLGMGTNmyPSSALLGthkdANLASIPVEEL---IEKADGFAGVFPEHKYEIVKKLQERKHIVG 584
Cdd:COG0474 537 KMITGDHPATARAIARQLGLGDD--GDRVLTG----AELDAMSDEELaeaVEDVDVFARVSPEHKLRIVKALQANGHVVA 610
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 585 MTGDGVNDAPALKKADIGIAV-ADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITIRIVFgFMLI 663
Cdd:COG0474 611 MTGDGVNDAPALKAADIGIAMgITGTDVAKEAADIVLLDDNFATIVAAVEEGRRIYDNIRKFIKYLLSSNFGEVL-SVLL 689
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 664 ALIWEFD--FSAFMVLIIAILNDGT-IMTISKDRVKPS-----PTPDSWKL--KEIFATGVVLGGYQAIMTVIFFWAAHK 733
Cdd:COG0474 690 ASLLGLPlpLTPIQILWINLVTDGLpALALGFEPVEPDvmkrpPRWPDEPIlsRFLLLRILLLGLLIAIFTLLTFALALA 769
                       810       820       830       840       850       860       870       880
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 734 TDFfsdtfgvrsirdnNHELMGAVYLQVSIISQ-ALIFVTRSRSWSFVER---PGALLMIAFLIAQLIATLIaVYANW-- 807
Cdd:COG0474 770 RGA-------------SLALARTMAFTTLVLSQlFNVFNCRSERRSFFKSglfPNRPLLLAVLLSLLLQLLL-IYVPPlq 835
                       890       900       910
                ....*....|....*....|....*....|....*
gi 15234666 808 EFAKIRGIGWGWAGVIWLYSIVTYFPLDVFKFAIR 842
Cdd:COG0474 836 ALFGTVPLPLSDWLLILGLALLYLLLVELVKLLRR 870
PRK10517 PRK10517
magnesium-transporting P-type ATPase MgtA;
12-675 6.05e-78

magnesium-transporting P-type ATPase MgtA;


Pssm-ID: 236705 [Multi-domain]  Cd Length: 902  Bit Score: 273.10  E-value: 6.05e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   12 VDLEKIPIEEVFQQLKCSREGLTTQEGEDRIQIFGPNKLEEKKESKLLKFLgfmW----NP----------LSWVMEMAA 77
Cdd:PRK10517  47 LKAAVMPEEELWKTFDTHPEGLNEAEVESAREQHGENELPAQKPLPWWVHL---WvcyrNPfnilltilgaISYATEDLF 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   78 IMaialangdgrppdwqdfvGIICLLVINST-ISFIEENNAGNAAAALMAGLAPKTKVLR------DGKWSEQEAAILVP 150
Cdd:PRK10517 124 AA------------------GVIALMVAISTlLNFIQEARSTKAADALKAMVSNTATVLRvindkgENGWLEIPIDQLVP 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  151 GDIVSIKLGDIIPADARLLEGDPLKVDQSALTGESLPVTKHPGQE-------------VFSGSTCKQGEIEAVVIATGVH 217
Cdd:PRK10517 186 GDIIKLAAGDMIPADLRILQARDLFVAQASLTGESLPVEKFATTRqpehsnplecdtlCFMGTNVVSGTAQAVVIATGAN 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  218 TFFGKAAHLVDST-NQVGHFQKvltaignfCICSIAIGMVIEIIVMYPIqrrkyrdgidnllVLLIGGI----------- 285
Cdd:PRK10517 266 TWFGQLAGRVSEQdSEPNAFQQ--------GISRVSWLLIRFMLVMAPV-------------VLLINGYtkgdwweaalf 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  286 ---------PIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDKNlVEVFckGVEKD 356
Cdd:PRK10517 325 alsvavgltPEMLPMIVTSTLARGAVKLSKQKVIVKRLDAIQNFGAMDILCTDKTGTLTQDKIVLENH-TDIS--GKTSE 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  357 QVLLFAAMASRVEN--QDAIDAAMVGMLADPKEARAGI--REVHFLPFNpVDKRTALTYIDGSGNWHR-VSKGAPEQIL- 430
Cdd:PRK10517 402 RVLHSAWLNSHYQTglKNLLDTAVLEGVDEESARSLASrwQKIDEIPFD-FERRRMSVVVAENTEHHQlICKGALEEILn 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  431 ---------ELAKASNDLSKKVLSIIDKYAERGLRSLAVARQVVPEkTKESPGAPWE----FVGLLPLFDPPRHDSAETI 497
Cdd:PRK10517 481 vcsqvrhngEIVPLDDIMLRRIKRVTDTLNRQGLRVVAVATKYLPA-REGDYQRADEsdliLEGYIAFLDPPKETTAPAL 559
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  498 RRALNLGVNVKMITGDQLAIGKETGRRLGMGTNMYPSSALLGTHKDANLAsipveELIEKADGFAGVFPEHKYEIVKKLQ 577
Cdd:PRK10517 560 KALKASGVTVKILTGDSELVAAKVCHEVGLDAGEVLIGSDIETLSDDELA-----NLAERTTLFARLTPMHKERIVTLLK 634
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  578 ERKHIVGMTGDGVNDAPALKKADIGIAVADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITIRIV 657
Cdd:PRK10517 635 REGHVVGFMGDGINDAPALRAADIGISVDGAVDIAREAADIILLEKSLMVLEEGVIEGRRTFANMLKYIKMTASSNFGNV 714
                        730
                 ....*....|....*...
gi 15234666  658 FGfMLIAliwefdfSAFM 675
Cdd:PRK10517 715 FS-VLVA-------SAFL 724
E1-E2_ATPase pfam00122
E1-E2 ATPase;
130-307 2.38e-45

E1-E2 ATPase;


Pssm-ID: 425475 [Multi-domain]  Cd Length: 181  Bit Score: 161.20  E-value: 2.38e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   130 PKTKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLkVDQSALTGESLPVTKHPGQEVFSGSTCKQGEIEA 209
Cdd:pfam00122   5 PTATVLRDGTEEEVPADELVPGDIVLLKPGERVPADGRIVEGSAS-VDESLLTGESLPVEKKKGDMVYSGTVVVSGSAKA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   210 VVIATGVHTFFGKAAHLVDSTNQV-GHFQKVLTAIGNFCICsIAIGMVIEIIVMYPIQRRKYRDGIDNLLVLLIGGIPIA 288
Cdd:pfam00122  84 VVTATGEDTELGRIARLVEEAKSKkTPLQRLLDRLGKYFSP-VVLLIALAVFLLWLFVGGPPLRALLRALAVLVAACPCA 162
                         170
                  ....*....|....*....
gi 15234666   289 MPTVLSVTMAIGSHRLSQQ 307
Cdd:pfam00122 163 LPLATPLALAVGARRLAKK 181
Cation_ATPase_N smart00831
Cation transporter/ATPase, N-terminus; This entry represents the conserved N-terminal region ...
12-74 2.28e-14

Cation transporter/ATPase, N-terminus; This entry represents the conserved N-terminal region found in several classes of cation-transporting P-type ATPases, including those that transport H+, Na+, Ca2+, Na+/K+, and H+/K+. In the H+/K+- and Na+/K+-exchange P-ATPases, this domain is found in the catalytic alpha chain. In gastric H+/K+-ATPases, this domain undergoes reversible sequential phosphorylation inducing conformational changes that may be important for regulating the function of these ATPases.


Pssm-ID: 214842 [Multi-domain]  Cd Length: 75  Bit Score: 68.76  E-value: 2.28e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15234666     12 VDLEKIPIEEVFQQLKCSRE-GLTTQEGEDRIQIFGPNKLEE-KKESKLLKFLGFMWNPLSWVME 74
Cdd:smart00831   2 LDWHALSLEEVLERLQTDLEkGLSSEEAARRLERYGPNELPPpKKTSPLLRFLRQFHNPLIYILL 66
 
Name Accession Description Interval E-value
ATPase-IIIA_H TIGR01647
plasma-membrane proton-efflux P-type ATPase; This model describes the plasma membrane proton ...
32-804 0e+00

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: 1159.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    32 GLTTQEGEDRIQIFGPNKLEEKKESKLLKFLGFMWNPLSWVMEMAAIMAIALANgdgrppdWQDFVGIICLLVINSTISF 111
Cdd:TIGR01647   1 GLTSAEAKKRLAKYGPNELPEKKVSPLLKFLGFFWNPLSWVMEAAAIIAIALEN-------WVDFVIILGLLLLNATIGF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   112 IEENNAGNAAAALMAGLAPKTKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLKVDQSALTGESLPVTKH 191
Cdd:TIGR01647  74 IEENKAGNAVEALKQSLAPKARVLRDGKWQEIPASELVPGDVVRLKIGDIVPADCRLFEGDYIQVDQAALTGESLPVTKK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   192 PGQEVFSGSTCKQGEIEAVVIATGVHTFFGKAAHLVDSTN-QVGHFQKVLTAIGNFCICSIAIGMVIEIIVMYPIQRRKY 270
Cdd:TIGR01647 154 TGDIAYSGSTVKQGEAEAVVTATGMNTFFGKAAALVQSTEtGSGHLQKILSKIGLFLIVLIGVLVLIELVVLFFGRGESF 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   271 RDGIDNLLVLLIGGIPIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDKNLVevFC 350
Cdd:TIGR01647 234 REGLQFALVLLVGGIPIAMPAVLSVTMAVGAAELAKKKAIVTRLTAIEELAGMDILCSDKTGTLTLNKLSIDEILP--FF 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   351 KGVEKDQVLLFAAMASRVENQDAIDAAMVGMLADPKEARAGIREVHFLPFNPVDKRTALTYIDG-SGNWHRVSKGAPEQI 429
Cdd:TIGR01647 312 NGFDKDDVLLYAALASREEDQDAIDTAVLGSAKDLKEARDGYKVLEFVPFDPVDKRTEATVEDPeTGKRFKVTKGAPQVI 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   430 LELAKASNDLSKKVLSIIDKYAERGLRSLAVARQvvpektkeSPGAPWEFVGLLPLFDPPRHDSAETIRRALNLGVNVKM 509
Cdd:TIGR01647 392 LDLCDNKKEIEEKVEEKVDELASRGYRALGVART--------DEEGRWHFLGLLPLFDPPRHDTKETIERARHLGVEVKM 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   510 ITGDQLAIGKETGRRLGMGTNMYPSSALLGTHKDANLASiPVEELIEKADGFAGVFPEHKYEIVKKLQERKHIVGMTGDG 589
Cdd:TIGR01647 464 VTGDHLAIAKETARRLGLGTNIYTADVLLKGDNRDDLPS-GLGEMVEDADGFAEVFPEHKYEIVEILQKRGHLVGMTGDG 542
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   590 VNDAPALKKADIGIAVADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITIRIVFGFMLIALIWEF 669
Cdd:TIGR01647 543 VNDAPALKKADVGIAVAGATDAARSAADIVLTEPGLSVIVDAILESRKIFQRMKSYVIYRIAETIRIVFFFGLLILILNF 622
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   670 DFSAFMVLIIAILNDGTIMTISKDRVKPSPTPDSWKLKEIFATGVVLGGYQAIMTVIFFWAAHKTDFFSDTFGVRSIRDN 749
Cdd:TIGR01647 623 YFPPIMVVIIAILNDGTIMTIAYDNVKPSKLPQRWNLREVFTMSTVLGIYLVISTFLLLAIALDTTFFIDKFGLQLLHGN 702
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15234666   750 nheLMGAVYLQVSIISQALIFVTRSRSWSFVERPGALLMIAFLIAQLIATLIAVY 804
Cdd:TIGR01647 703 ---LQSFIYLQVSISGHATIFVTRTHGFFWSERPGKLLFGAFVIAQIIATFIAVY 754
P-type_ATPase_H cd02076
plant and fungal plasma membrane H(+)-ATPases, and related bacterial and archaeal putative H(+) ...
32-839 0e+00

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: 1136.95  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  32 GLTTQEGEDRIQIFGPNKLEEKKESKLLKFLGFMWNPLSWVMEMAAIMAIAlangdgrPPDWQDFVGIICLLVINSTISF 111
Cdd:cd02076   1 GLTSEEAAKRLKEYGPNELPEKKENPILKFLSFFWGPIPWMLEAAAILAAA-------LGDWVDFAIILLLLLINAGIGF 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 112 IEENNAGNAAAALMAGLAPKTKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLKVDQSALTGESLPVTKH 191
Cdd:cd02076  74 IEERQAGNAVAALKKSLAPKARVLRDGQWQEIDAKELVPGDIVSLKIGDIVPADARLLTGDALQVDQSALTGESLPVTKH 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 192 PGQEVFSGSTCKQGEIEAVVIATGVHTFFGKAAHLVDSTNQVGHFQKVLTAIGNFCICSIAIGMVIEIIVMYPIQRRkYR 271
Cdd:cd02076 154 PGDEAYSGSIVKQGEMLAVVTATGSNTFFGKTAALVASAEEQGHLQKVLNKIGNFLILLALILVLIIVIVALYRHDP-FL 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 272 DGIDNLLVLLIGGIPIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDKNLVevfCK 351
Cdd:cd02076 233 EILQFVLVLLIASIPVAMPAVLTVTMAVGALELAKKKAIVSRLSAIEELAGVDILCSDKTGTLTLNKLSLDEPYS---LE 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 352 GVEKDQVLLFAAMASRVENQDAIDAAMVGMLADPKEARAGIREVHFLPFNPVDKRTALTYIDGSGNWHRVSKGAPEQILE 431
Cdd:cd02076 310 GDGKDELLLLAALASDTENPDAIDTAILNALDDYKPDLAGYKQLKFTPFDPVDKRTEATVEDPDGERFKVTKGAPQVILE 389
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 432 LAKASNDLSKKVLSIIDKYAERGLRSLAVARQVVpektkespGAPWEFVGLLPLFDPPRHDSAETIRRALNLGVNVKMIT 511
Cdd:cd02076 390 LVGNDEAIRQAVEEKIDELASRGYRSLGVARKED--------GGRWELLGLLPLFDPPRPDSKATIARAKELGVRVKMIT 461
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 512 GDQLAIGKETGRRLGMGTNMYPSSALLGTHKDANLASIPVEELIEKADGFAGVFPEHKYEIVKKLQERKHIVGMTGDGVN 591
Cdd:cd02076 462 GDQLAIAKETARQLGMGTNILSAERLKLGGGGGGMPGSELIEFIEDADGFAEVFPEHKYRIVEALQQRGHLVGMTGDGVN 541
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 592 DAPALKKADIGIAVADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITIRIVFGFMLIALIWEF-D 670
Cdd:cd02076 542 DAPALKKADVGIAVSGATDAARAAADIVLTAPGLSVIIDAIKTSRQIFQRMKSYVIYRIAETLRILVFFTLGILILNFyP 621
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 671 FSAFMVLIIAILNDGTIMTISKDRVKPSPTPDSWKLKEIFATGVVLGGYQAIMTVIFFWAAHKTDFFSDtfgvrsIRDNN 750
Cdd:cd02076 622 LPLIMIVLIAILNDGATLTIAYDNVPPSPRPVRWNMPELLGIATVLGVVLTISSFLLLWLLDDQGWFED------IVLSA 695
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 751 HELMGAVYLQVSIISQALIFVTRSRSWSFVERPGALLMIAFLIAQLIATLIAVYANWEFAkirGIGWGWAGVIWLYSIVT 830
Cdd:cd02076 696 GELQTILYLQLSISGHLTIFVTRTRGPFWRPRPSPLLFIAVVLTQILATLLAVYGWFMFA---GIGWGWALLVWIYALVW 772

                ....*....
gi 15234666 831 YFPLDVFKF 839
Cdd:cd02076 773 FVVLDFVKL 781
MgtA COG0474
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism];
8-842 0e+00

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


Pssm-ID: 440242 [Multi-domain]  Cd Length: 874  Bit Score: 610.19  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   8 KNETVDLEKIPIEEVFQQLKCSREGLTTQEGEDRIQIFGPNKL-EEKKESKLLKFLGFMWNPL----------SWVMEma 76
Cdd:COG0474   2 ATALKDWHALSAEEVLAELGTSEEGLSSEEAARRLARYGPNELpEEKKRSLLRRFLEQFKNPLilillaaaviSALLG-- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  77 aimaialangdgrppDWQDFVGIICLLVINSTISFIEENNAGNAAAALMAGLAPKTKVLRDGKWSEQEAAILVPGDIVSI 156
Cdd:COG0474  80 ---------------DWVDAIVILAVVLLNAIIGFVQEYRAEKALEALKKLLAPTARVLRDGKWVEIPAEELVPGDIVLL 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 157 KLGDIIPADARLLEGDPLKVDQSALTGESLPVTKHPGQE------------VFSGSTCKQGEIEAVVIATGVHTFFGKAA 224
Cdd:COG0474 145 EAGDRVPADLRLLEAKDLQVDESALTGESVPVEKSADPLpedaplgdrgnmVFMGTLVTSGRGTAVVVATGMNTEFGKIA 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 225 HLVDSTNQV-GHFQKVLTAIGNFCIcSIAIGMVIEIIVMYPIQRrkyRDGIDNLLV---LLIGGIPIAMPTVLSVTMAIG 300
Cdd:COG0474 225 KLLQEAEEEkTPLQKQLDRLGKLLA-IIALVLAALVFLIGLLRG---GPLLEALLFavaLAVAAIPEGLPAVVTITLALG 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 301 SHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVdknlVEVFCKGVEKD----------QVLLFAAMAS---- 366
Cdd:COG0474 301 AQRMAKRNAIVRRLPAVETLGSVTVICTDKTGTLTQNKMTV----ERVYTGGGTYEvtgefdpaleELLRAAALCSdaql 376
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 367 --RVENQDAIDAAMVGMLA----DPKEARAGIREVHFLPFNPVDKRTALTYIDGSGNWHRVSKGAPEQILELAKA----- 435
Cdd:COG0474 377 eeETGLGDPTEGALLVAAAkaglDVEELRKEYPRVDEIPFDSERKRMSTVHEDPDGKRLLIVKGAPEVVLALCTRvltgg 456
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 436 -----SNDLSKKVLSIIDKYAERGLRSLAVARQVVPEKTKESPGAP---WEFVGLLPLFDPPRHDSAETIRRALNLGVNV 507
Cdd:COG0474 457 gvvplTEEDRAEILEAVEELAAQGLRVLAVAYKELPADPELDSEDDesdLTFLGLVGMIDPPRPEAKEAIAECRRAGIRV 536
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 508 KMITGDQLAIGKETGRRLGMGTNmyPSSALLGthkdANLASIPVEEL---IEKADGFAGVFPEHKYEIVKKLQERKHIVG 584
Cdd:COG0474 537 KMITGDHPATARAIARQLGLGDD--GDRVLTG----AELDAMSDEELaeaVEDVDVFARVSPEHKLRIVKALQANGHVVA 610
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 585 MTGDGVNDAPALKKADIGIAV-ADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITIRIVFgFMLI 663
Cdd:COG0474 611 MTGDGVNDAPALKAADIGIAMgITGTDVAKEAADIVLLDDNFATIVAAVEEGRRIYDNIRKFIKYLLSSNFGEVL-SVLL 689
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 664 ALIWEFD--FSAFMVLIIAILNDGT-IMTISKDRVKPS-----PTPDSWKL--KEIFATGVVLGGYQAIMTVIFFWAAHK 733
Cdd:COG0474 690 ASLLGLPlpLTPIQILWINLVTDGLpALALGFEPVEPDvmkrpPRWPDEPIlsRFLLLRILLLGLLIAIFTLLTFALALA 769
                       810       820       830       840       850       860       870       880
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 734 TDFfsdtfgvrsirdnNHELMGAVYLQVSIISQ-ALIFVTRSRSWSFVER---PGALLMIAFLIAQLIATLIaVYANW-- 807
Cdd:COG0474 770 RGA-------------SLALARTMAFTTLVLSQlFNVFNCRSERRSFFKSglfPNRPLLLAVLLSLLLQLLL-IYVPPlq 835
                       890       900       910
                ....*....|....*....|....*....|....*
gi 15234666 808 EFAKIRGIGWGWAGVIWLYSIVTYFPLDVFKFAIR 842
Cdd:COG0474 836 ALFGTVPLPLSDWLLILGLALLYLLLVELVKLLRR 870
ATPase_P-type TIGR01494
ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large ...
134-666 8.08e-119

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: 373.58  E-value: 8.08e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   134 VLRDGkWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDpLKVDQSALTGESLPVTKHP---GQEVFSGSTCKQGEIEAV 210
Cdd:TIGR01494  39 VLRNG-WKEISSKDLVPGDVVLVKSGDTVPADGVLLSGS-AFVDESSLTGESLPVLKTAlpdGDAVFAGTINFGGTLIVK 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   211 VIATGVHTFFGKAAHLVDSTNQ-VGHFQKVLTAIGNFcICSIAIGMVIEIIVMYPI----QRRKYRDGIDNLLVLLIGGI 285
Cdd:TIGR01494 117 VTATGILTTVGKIAVVVYTGFStKTPLQSKADKFENF-IFILFLLLLALAVFLLLPiggwDGNSIYKAILRALAVLVIAI 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   286 PIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDKNLVEVFCKGVEKDQVLLFAAMA 365
Cdd:TIGR01494 196 PCALPLAVSVALAVGDARMAKKGILVKNLNALEELGKVDVICFDKTGTLTTNKMTLQKVIIIGGVEEASLALALLAASLE 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   366 SRVEnqDAIDAAMV---GMLADPKEARAGIREVHFLPFNPVDKRTALTYIDGSGNWHRVSKGAPEQILELAKASNDLSKK 442
Cdd:TIGR01494 276 YLSG--HPLERAIVksaEGVIKSDEINVEYKILDVFPFSSVLKRMGVIVEGANGSDLLFVKGAPEFVLERCNNENDYDEK 353
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   443 VLSiidkYAERGLRSLAVARQVVPEktkespgaPWEFVGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGKETG 522
Cdd:TIGR01494 354 VDE----YARQGLRVLAFASKKLPD--------DLEFLGLLTFEDPLRPDAKETIEALRKAGIKVVMLTGDNVLTAKAIA 421
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   523 RRLGMgtnmypssallgthkdanlasipveeliekaDGFAGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIG 602
Cdd:TIGR01494 422 KELGI-------------------------------DVFARVKPEEKAAIVEALQEKGRTVAMTGDGVNDAPALKKADVG 470
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15234666   603 IAVADAtDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITIRIVFGFMLIALI 666
Cdd:TIGR01494 471 IAMGSG-DVAKAAADIVLLDDDLSTIVEAVKEGRKTFSNIKKNIFWAIAYNLILIPLALLLIVI 533
P-type_ATPase_Ca_prok cd02089
prokaryotic P-type Ca(2+)-ATPase similar to Synechococcus elongatus sp. strain PCC 7942 PacL ...
32-685 3.05e-115

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: 368.48  E-value: 3.05e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  32 GLTTQEGEDRIQIFGPNKLEE-KKESKLLKFLGFMWNPLSWVMEMAAIMAIALANgdgrppdWQDFVGIICLLVINSTIS 110
Cdd:cd02089   1 GLSEEEAERRLAKYGPNELVEkKKRSPWKKFLEQFKDFMVIVLLAAAVISGVLGE-------YVDAIVIIAIVILNAVLG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 111 FIEENNAGNAAAALMAGLAPKTKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLKVDQSALTGESLPVTK 190
Cdd:cd02089  74 FVQEYKAEKALAALKKMSAPTAKVLRDGKKQEIPARELVPGDIVLLEAGDYVPADGRLIESASLRVEESSLTGESEPVEK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 191 HPGQE-------------VFSGSTCKQGEIEAVVIATGVHTFFGKAAHLVDST-NQVGHFQKVLTAIGNfcicSIAIGMV 256
Cdd:cd02089 154 DADTLleedvplgdrknmVFSGTLVTYGRGRAVVTATGMNTEMGKIATLLEETeEEKTPLQKRLDQLGK----RLAIAAL 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 257 IEIIVMYPIQRRKYRDGIDNLLV---LLIGGIPIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGT 333
Cdd:cd02089 230 IICALVFALGLLRGEDLLDMLLTavsLAVAAIPEGLPAIVTIVLALGVQRMAKRNAIIRKLPAVETLGSVSVICSDKTGT 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 334 LTLNKLSVDKnlveVFCKGvekdqvllfaamasrvenqDAIDAAMVGMLADPKEARAGIREVHF----LPFNPVDKRTAl 409
Cdd:cd02089 310 LTQNKMTVEK----IYTIG-------------------DPTETALIRAARKAGLDKEELEKKYPriaeIPFDSERKLMT- 365
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 410 TYIDGSGNWHRVSKGAPEQILELAKA----------SNDLSKKVLSIIDKYAERGLRSLAVARQVVPEKTKESPGAPWE- 478
Cdd:cd02089 366 TVHKDAGKYIVFTKGAPDVLLPRCTYiyingqvrplTEEDRAKILAVNEEFSEEALRVLAVAYKPLDEDPTESSEDLENd 445
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 479 --FVGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGKETGRRLGMGTNmyPSSALLGThkdaNLASIPVEEL-- 554
Cdd:cd02089 446 liFLGLVGMIDPPRPEVKDAVAECKKAGIKTVMITGDHKLTARAIAKELGILED--GDKALTGE----ELDKMSDEELek 519
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 555 -IEKADGFAGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIGIAVA-DATDAARGASDIVLTEPGLSVIISAV 632
Cdd:cd02089 520 kVEQISVYARVSPEHKLRIVKALQRKGKIVAMTGDGVNDAPALKAADIGVAMGiTGTDVAKEAADMILTDDNFATIVAAV 599
                       650       660       670       680       690
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15234666 633 LTSRAIFQRMKNYTIYAVSITIRIVFGfMLIALI--WEFDFSAFMVLIIAILNDG 685
Cdd:cd02089 600 EEGRTIYDNIRKFIRYLLSGNVGEILT-MLLAPLlgWPVPLLPIQLLWINLLTDG 653
P-type_ATPase_cation cd02080
P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, ...
32-662 7.93e-113

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: 366.20  E-value: 7.93e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  32 GLTTQEGEDRIQIFGPNKLEEKK-ESKLLKFLGFMWNPLSWVMEMAAIMAIALANgdgrppdWQDFVGIICLLVINSTIS 110
Cdd:cd02080   1 GLTSEEAAERLERYGPNRLPEKKtKSPLLRFLRQFNNPLIYILLAAAVVTAFLGH-------WVDAIVIFGVVLINAIIG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 111 FIEENNAGNAAAALMAGLAPKTKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLKVDQSALTGESLPVTK 190
Cdd:cd02080  74 YIQEGKAEKALAAIKNMLSPEATVLRDGKKLTIDAEELVPGDIVLLEAGDKVPADLRLIEARNLQIDESALTGESVPVEK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 191 H--PGQE----------VFSGSTCKQGEIEAVVIATGVHTFFGKAAHLVDS--------TNQVGHFQKVLTAIgnfcics 250
Cdd:cd02080 154 QegPLEEdtplgdrknmAYSGTLVTAGSATGVVVATGADTEIGRINQLLAEveqlatplTRQIAKFSKALLIV------- 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 251 IAIGMVIEIIVMYPIQRRKYRDGIDNLLVLLIGGIPIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDK 330
Cdd:cd02080 227 ILVLAALTFVFGLLRGDYSLVELFMAVVALAVAAIPEGLPAVITITLAIGVQRMAKRNAIIRRLPAVETLGSVTVICSDK 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 331 TGTLTLNKLSVDKnlVEVFCkgveKDQVLLFAAMASRVENqDAIDAAM--VGMLA--DPKEARAGIREVHFLPFNPVDKR 406
Cdd:cd02080 307 TGTLTRNEMTVQA--IVTLC----NDAQLHQEDGHWKITG-DPTEGALlvLAAKAglDPDRLASSYPRVDKIPFDSAYRY 379
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 407 TALTYIDGSGNWHRVsKGAPEQILELAKASNDLS-------KKVLSIIDKYAERGLRSLAVARQVVPEKTKESPGAPWE- 478
Cdd:cd02080 380 MATLHRDDGQRVIYV-KGAPERLLDMCDQELLDGgvspldrAYWEAEAEDLAKQGLRVLAFAYREVDSEVEEIDHADLEg 458
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 479 ---FVGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGKETGRRLGMGTNmypSSALLGthkdANLASIPVEELI 555
Cdd:cd02080 459 gltFLGLQGMIDPPRPEAIAAVAECQSAGIRVKMITGDHAETARAIGAQLGLGDG---KKVLTG----AELDALDDEELA 531
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 556 EKADG---FAGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIGIAVA-DATDAARGASDIVLTEPGLSVIISA 631
Cdd:cd02080 532 EAVDEvdvFARTSPEHKLRLVRALQARGEVVAMTGDGVNDAPALKQADIGIAMGiKGTEVAKEAADMVLADDNFATIAAA 611
                       650       660       670
                ....*....|....*....|....*....|....*....
gi 15234666 632 VLTSRAIFQRMKNYTIY--------AVSITIRIVFGFML 662
Cdd:cd02080 612 VEEGRRVYDNLKKFILFtlptnlgeGLVIIVAILFGVTL 650
P-type_ATPase_Mg cd02077
magnesium transporting ATPase (MgtA), similar to Escherichia coli MgtA and Salmonella ...
32-779 3.44e-106

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: 346.93  E-value: 3.44e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  32 GLTTQEGEDRIQIFGPNKLE-EKKESKLLKFLGFMWNPLSWVMemAAIMAIALANGDGRPPDWQDFVGIICLLV---INS 107
Cdd:cd02077   1 GLTNEEAEERLEKYGPNEIShEKFPSWFKLLLKAFINPFNIVL--LVLALVSFFTDVLLAPGEFDLVGALIILLmvlISG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 108 TISFIEENNAGNAAAALMAGLAPKTKVLRDG-KWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLKVDQSALTGESL 186
Cdd:cd02077  79 LLDFIQEIRSLKAAEKLKKMVKNTATVIRDGsKYMEIPIDELVPGDIVYLSAGDMIPADVRIIQSKDLFVSQSSLTGESE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 187 PVTKHPGQE-------------VFSGSTCKQGEIEAVVIATGVHTFFGKAAHLVDSTNQVGHFQKVLTAIGNFCIcsiaI 253
Cdd:cd02077 159 PVEKHATAKktkdesileleniCFMGTNVVSGSALAVVIATGNDTYFGSIAKSITEKRPETSFDKGINKVSKLLI----R 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 254 GMVIEIIVMYPIQRRKYRDGIDNLLVLL---IGGIPIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDK 330
Cdd:cd02077 235 FMLVMVPVVFLINGLTKGDWLEALLFALavaVGLTPEMLPMIVTSNLAKGAVRMSKRKVIVKNLNAIQNFGAMDILCTDK 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 331 TGTLTLNKLSVDKNLvEVFCKgvEKDQVLLFAAMASRVEN--QDAIDAAMV--GMLADPKEARAGIREVHFLPFNPVDKR 406
Cdd:cd02077 315 TGTLTQDKIVLERHL-DVNGK--ESERVLRLAYLNSYFQTglKNLLDKAIIdhAEEANANGLIQDYTKIDEIPFDFERRR 391
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 407 TALTYIDGSGNWHRVSKGAPEQILELA----------KASNDLSKKVLSIIDKYAERGLRSLAVArqvvpekTKESPGAP 476
Cdd:cd02077 392 MSVVVKDNDGKHLLITKGAVEEILNVCthvevngevvPLTDTLREKILAQVEELNREGLRVLAIA-------YKKLPAPE 464
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 477 WEF----------VGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGKETGRRLGMGTNmypsSALLGTHKDAnL 546
Cdd:cd02077 465 GEYsvkdekelilIGFLAFLDPPKESAAQAIKALKKNGVNVKILTGDNEIVTKAICKQVGLDIN----RVLTGSEIEA-L 539
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 547 ASIPVEELIEKADGFAGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIGIAVADATDAARGASDIVLTEPGLS 626
Cdd:cd02077 540 SDEELAKIVEETNIFAKLSPLQKARIIQALKKNGHVVGFMGDGINDAPALRQADVGISVDSAVDIAKEAADIILLEKDLM 619
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 627 VIISAVLTSRAIFQRMKNYTIYAVSITIRIVFGfMLIALIWeFDFSAFMVLIIAILN---DGTIMTISKDRVKPSPT--P 701
Cdd:cd02077 620 VLEEGVIEGRKTFGNILKYIKMTASSNFGNVFS-VLVASAF-LPFLPMLPIQLLLQNllyDFSQLAIPFDNVDEEFLkkP 697
                       730       740       750       760       770       780       790
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15234666 702 DSWKLKEIFATGVVLGGYQAIMTVIFFWAAHktdffsdtFGVRSIRDNNHELMGAVYLQVSIISQAL-IFVTRSRSWSF 779
Cdd:cd02077 698 QKWDIKNIGRFMIWIGPISSIFDILTFLVMW--------FVFKANTAASQALFQTGWFIEGLLTQTLvVHMIRTEKIPF 768
P-type_ATPase_SPCA cd02085
golgi-associated secretory pathway Ca(2+) transport ATPases, similar to human ATPase secretory ...
41-685 3.64e-86

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: 293.92  E-value: 3.64e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  41 RIQIFGPNKLEEKKESKLLK-FLGFMWNPLSWVMEMAAIMAIALANGDgrppdwqDFVGIICLLVINSTISFIEENNAGN 119
Cdd:cd02085   1 RRKLHGPNEFKVEDEEPLWKkYLEQFKNPLILLLLGSAVVSVVMKQYD-------DAVSITVAILIVVTVAFVQEYRSEK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 120 AAAALMAGLAPKTKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLKVDQSALTGESLPVTK--------- 190
Cdd:cd02085  74 SLEALNKLVPPECHCLRDGKLEHFLARELVPGDLVCLSIGDRIPADLRLFEATDLSIDESSLTGETEPCSKttevipkas 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 191 -----HPGQEVFSGSTCKQGEIEAVVIATGVHTFFG---KAAH--------LVDSTNQVGhfqKVLTAIgNFCIcsIAIG 254
Cdd:cd02085 154 ngdltTRSNIAFMGTLVRCGHGKGIVIGTGENSEFGevfKMMQaeeapktpLQKSMDKLG---KQLSLY-SFII--IGVI 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 255 MVIEIIvmypiQRRKYRDGIDNLLVLLIGGIPIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTL 334
Cdd:cd02085 228 MLIGWL-----QGKNLLEMFTIGVSLAVAAIPEGLPIVVTVTLALGVMRMAKRRAIVKKLPIVETLGCVNVICSDKTGTL 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 335 TLNKLSVDKnlveVFCKGVEKDQVLLFAAMASRVENQDAIDAAMVGMLADPKEARAGIREVhflPFNPVDKRTALTYIDG 414
Cdd:cd02085 303 TKNEMTVTK----IVTGCVCNNAVIRNNTLMGQPTEGALIALAMKMGLSDIRETYIRKQEI---PFSSEQKWMAVKCIPK 375
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 415 SGNWHR---VSKGAPEQILELAKASND-------LSKK----VLSIIDKYAERGLRSLAVARQVVPEKTKespgapweFV 480
Cdd:cd02085 376 YNSDNEeiyFMKGALEQVLDYCTTYNSsdgsalpLTQQqrseINEEEKEMGSKGLRVLALASGPELGDLT--------FL 447
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 481 GLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGKETGRRLGMGTNmyPSSALLGTHKDAnLASIPVEELIEKADG 560
Cdd:cd02085 448 GLVGINDPPRPGVREAIQILLESGVRVKMITGDAQETAIAIGSSLGLYSP--SLQALSGEEVDQ-MSDSQLASVVRKVTV 524
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 561 FAGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIGIAVA-DATDAARGASDIVLTEPGLSVIISAVLTSRAIF 639
Cdd:cd02085 525 FYRASPRHKLKIVKALQKSGAVVAMTGDGVNDAVALKSADIGIAMGrTGTDVCKEAADMILVDDDFSTILAAIEEGKGIF 604
                       650       660       670       680       690
                ....*....|....*....|....*....|....*....|....*....|
gi 15234666 640 QRMKNYTIYAVSITIRivfGFMLIALIWEFDF----SAFMVLIIAILNDG 685
Cdd:cd02085 605 YNIKNFVRFQLSTSIA---ALSLIALSTLFNLpnplNAMQILWINIIMDG 651
ATPase-IIA2_Ca TIGR01522
golgi membrane calcium-translocating P-type ATPase; This model describes the P-type ATPase ...
17-729 1.96e-85

golgi membrane calcium-translocating P-type ATPase; This model describes the P-type ATPase responsible for translocating calcium ions across the golgi membrane of fungi and animals, and is of particular importance in the sarcoplasmic reticulum of skeletal and cardiac muscle in vertebrates. 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 former of which is modelled by TIGR01116.


Pssm-ID: 130585 [Multi-domain]  Cd Length: 884  Bit Score: 293.66  E-value: 1.96e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    17 IPIEEVFQQLKCSRE-GLTT-QEGEDRIQIFGPNKLE-EKKESKLLKFLG-FMWNPLSWVMEMAAIMAIALANGDgrppd 92
Cdd:TIGR01522   7 LSVEETCSKLQTDLQnGLNSsQEASHRRAFHGWNEFDvEEDESLWKKFLSqFVKNPLILLLIASAVISVFMGNID----- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    93 wqDFVGIICLLVINSTISFIEENNAGNAAAALMAGLAPKTKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGD 172
Cdd:TIGR01522  82 --DAVSITLAILIVVTVGFVQEYRSEKSLEALNKLVPPECHLIREGKLEHVLASTLVPGDLVCLSVGDRVPADLRIVEAV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   173 PLKVDQSALTGESLPVTKHPGQE--------------VFSGSTCKQGEIEAVVIATGVHTFFGKAAHLVDSTNQVGH-FQ 237
Cdd:TIGR01522 160 DLSIDESNLTGETTPVSKVTAPIpaatngdlaersniAFMGTLVRCGHGKGIVVGTGSNTEFGAVFKMMQAIEKPKTpLQ 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   238 KVLTAIGN--FCICSIAIGMvieIIVMYPIQRRKYRDGIDNLLVLLIGGIPIAMPTVLSVTMAIGSHRLSQQGAITKRMT 315
Cdd:TIGR01522 240 KSMDLLGKqlSLVSFGVIGV---ICLVGWFQGKDWLEMFTISVSLAVAAIPEGLPIIVTVTLALGVLRMSKKRAIVRKLP 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   316 AIEEMAGMDVLCSDKTGTLTLNKLSVDK--------NLVEVF----CKGVEKD-------------QVLLFAAMA--SRV 368
Cdd:TIGR01522 317 SVETLGSVNVICSDKTGTLTKNHMTVTKiwtsdglhTMLNAVslnqFGEVIVDgdvlhgfytvavsRILEAGNLCnnAKF 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   369 ENQDAI------DAAMVGMLA-----DPKEARAGIREVhflPFNPVDKRTALTYIDGSGNWHRVS-KGAPEQILEL---- 432
Cdd:TIGR01522 397 RNEADTllgnptDVALIELLMkfgldDLRETYIRVAEV---PFSSERKWMAVKCVHRQDRSEMCFmKGAYEQVLKYctyy 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   433 -------AKASNDLSKKVLSIIDKYAERGLRSLAVARQvvPEKTKESpgapweFVGLLPLFDPPRHDSAETIRRALNLGV 505
Cdd:TIGR01522 474 qkkdgktLTLTQQQRDVIQEEAAEMASAGLRVIAFASG--PEKGQLT------FLGLVGINDPPRPGVKEAVTTLITGGV 545
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   506 NVKMITGDQLAIGKETGRRLGMGtnMYPSSALLGTHKDAnLASIPVEELIEKADGFAGVFPEHKYEIVKKLQERKHIVGM 585
Cdd:TIGR01522 546 RIIMITGDSQETAVSIARRLGMP--SKTSQSVSGEKLDA-MDDQQLSQIVPKVAVFARASPEHKMKIVKALQKRGDVVAM 622
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   586 TGDGVNDAPALKKADIGIAVAD-ATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITIRivfGFMLIA 664
Cdd:TIGR01522 623 TGDGVNDAPALKLADIGVAMGQtGTDVAKEAADMILTDDDFATILSAIEEGKGIFNNIKNFITFQLSTSVA---ALSLIA 699
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   665 LIWEFDF----SAFMVLIIAILNDGT------IMTISKDRVKPSPTPDSWK------LKEIFATGVVLggyqAIMTVIFF 728
Cdd:TIGR01522 700 LATLMGFpnplNAMQILWINILMDGPpaqslgVEPVDKDVMRKPPRPRNDKiltkdlIKKILVSAIII----VVGTLFVF 775

                  .
gi 15234666   729 W 729
Cdd:TIGR01522 776 V 776
P-type_ATPase cd07539
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ...
95-652 1.58e-84

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: 285.08  E-value: 1.58e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  95 DFVGIICLLVINSTISFIEENNAGNAAAALMAGLAPKTKVLRDGKWSEQE--AAILVPGDIVSIKLGDIIPADARLLEGD 172
Cdd:cd07539  59 DAVLIVGVLTVNAVIGGVQRLRAERALAALLAQQQQPARVVRAPAGRTQTvpAESLVPGDVIELRAGEVVPADARLLEAD 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 173 PLKVDQSALTGESLPVTKH----PGQE-------VFSGSTCKQGEIEAVVIATGVHTFFGKAAHLVDSTNQVGHFQKVLT 241
Cdd:cd07539 139 DLEVDESALTGESLPVDKQvaptPGAPladracmLYEGTTVVSGQGRAVVVATGPHTEAGRAQSLVAPVETATGVQAQLR 218
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 242 AIGN-FCICSIAIG-MVIEIIVM--YPIqRRKYRDGIDnllvLLIGGIPIAMPTVLSVTMAIGSHRLSQQGAITKRMTAI 317
Cdd:cd07539 219 ELTSqLLPLSLGGGaAVTGLGLLrgAPL-RQAVADGVS----LAVAAVPEGLPLVATLAQLAAARRLSRRGVLVRSPRTV 293
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 318 EEMAGMDVLCSDKTGTLTLNKLSvdknlvevfckgvekdqvllfaamasrvenqdaidaamVGMLADPkearagireVHF 397
Cdd:cd07539 294 EALGRVDTICFDKTGTLTENRLR--------------------------------------VVQVRPP---------LAE 326
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 398 LPFNPvDKRTALTYIDGSGNWHRVS-KGAPEQILEL----------AKASNDLSKKVLSIIDKYAERGLRSLAVARQVVP 466
Cdd:cd07539 327 LPFES-SRGYAAAIGRTGGGIPLLAvKGAPEVVLPRcdrrmtggqvVPLTEADRQAIEEVNELLAGQGLRVLAVAYRTLD 405
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 467 EKTKESPGA---PWEFVGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGKETGRRLGMGTNMypsSALLGTHKD 543
Cdd:cd07539 406 AGTTHAVEAvvdDLELLGLLGLADTARPGAAALIAALHDAGIDVVMITGDHPITARAIAKELGLPRDA---EVVTGAELD 482
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 544 AnLASIPVEELIEKADGFAGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIGIAV-ADATDAARGASDIVLTE 622
Cdd:cd07539 483 A-LDEEALTGLVADIDVFARVSPEQKLQIVQALQAAGRVVAMTGDGANDAAAIRAADVGIGVgARGSDAAREAADLVLTD 561
                       570       580       590
                ....*....|....*....|....*....|
gi 15234666 623 PGLSVIISAVLTSRAIFQRMKNytiyAVSI 652
Cdd:cd07539 562 DDLETLLDAVVEGRTMWQNVRD----AVHV 587
P-type_ATPase cd07538
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ...
32-666 3.14e-83

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: 282.02  E-value: 3.14e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  32 GLTTQEGEDRIQIFGPNKLEEKKESKLLKFLgfmWNPLSWVMEMAAIMAIALANGDGRPpdwQDFVGIICLLVINSTISF 111
Cdd:cd07538   1 GLTEAEARRRLESGGKNELPQPKKRTLLASI---LDVLREPMFLLLLAAALIYFVLGDP---REGLILLIFVVVIIAIEV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 112 IEENNAGNAAAALMAGLAPKTKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLKVDQSALTGESLPVTKH 191
Cdd:cd07538  75 VQEWRTERALEALKNLSSPRATVIRDGRERRIPSRELVPGDLLILGEGERIPADGRLLENDDLGVDESTLTGESVPVWKR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 192 PGQE------------VFSGSTCKQGEIEAVVIATGVHTFFGK----AAHLVDS----TNQVGHFQKVLtAIGNFCICSI 251
Cdd:cd07538 155 IDGKamsapggwdknfCYAGTLVVRGRGVAKVEATGSRTELGKigksLAEMDDEptplQKQTGRLVKLC-ALAALVFCAL 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 252 aigmvieIIVMYPIQRRKYRDGIDNLLVLLIGGIPIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKT 331
Cdd:cd07538 234 -------IVAVYGVTRGDWIQAILAGITLAMAMIPEEFPVILTVFMAMGAWRLAKKNVLVRRAAAVETLGSITVLCVDKT 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 332 GTLTLNKLSVdknlvevfckgvekdqvllfaamasrvenqdaidaamvgmladpKEARAGIREvhfLPFNPvDKRTALTY 411
Cdd:cd07538 307 GTLTKNQMEV--------------------------------------------VELTSLVRE---YPLRP-ELRMMGQV 338
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 412 IDGSGNWHRVSKGAPEQILELAKASNDLSKKVLSIIDKYAERGLRSLAVArqVVPEKTKESPGAPWE----FVGLLPLFD 487
Cdd:cd07538 339 WKRPEGAFAAAKGSPEAIIRLCRLNPDEKAAIEDAVSEMAGEGLRVLAVA--ACRIDESFLPDDLEDavfiFVGLIGLAD 416
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 488 PPRHDSAETIRRALNLGVNVKMITGDQLAIGKETGRRLGMGTNMypssallGTHKDANLASIPVEELIEKADG---FAGV 564
Cdd:cd07538 417 PLREDVPEAVRICCEAGIRVVMITGDNPATAKAIAKQIGLDNTD-------NVITGQELDAMSDEELAEKVRDvniFARV 489
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 565 FPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIGIAVAD-ATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMK 643
Cdd:cd07538 490 VPEQKLRIVQAFKANGEIVAMTGDGVNDAPALKAAHIGIAMGKrGTDVAREASDIVLLDDNFSSIVSTIRLGRRIYDNLK 569
                       650       660
                ....*....|....*....|...
gi 15234666 644 NYTIYAVSITIRIvFGFMLIALI 666
Cdd:cd07538 570 KAITYVFAIHVPI-AGLALLPPL 591
P-type_ATPases cd01431
ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, ...
325-688 1.98e-81

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: 266.24  E-value: 1.98e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 325 VLCSDKTGTLTLNKLSVdknlVEVFckgvekdqvllfaamasrvenqdaidaamvgmladpkearagireVHFLPFNPVD 404
Cdd:cd01431   1 VICSDKTGTLTKNGMTV----TKLF---------------------------------------------IEEIPFNSTR 31
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 405 KRTALTYIDGsGNWHRVSKGAPEQILELAK--ASNDLSKKVLSIIDKYAERGLRSLAVARQVVPEKT-KESPGAPWEFVG 481
Cdd:cd01431  32 KRMSVVVRLP-GRYRAIVKGAPETILSRCShaLTEEDRNKIEKAQEESAREGLRVLALAYREFDPETsKEAVELNLVFLG 110
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 482 LLPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGKETGRRLGMGTNMYPSSALLGTHkdaNLASIPVEELIEKADGF 561
Cdd:cd01431 111 LIGLQDPPRPEVKEAIAKCRTAGIKVVMITGDNPLTAIAIAREIGIDTKASGVILGEEAD---EMSEEELLDLIAKVAVF 187
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 562 AGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIGIAVA-DATDAARGASDIVLTEPGLSVIISAVLTSRAIFQ 640
Cdd:cd01431 188 ARVTPEQKLRIVKALQARGEVVAMTGDGVNDAPALKQADVGIAMGsTGTDVAKEAADIVLLDDNFATIVEAVEEGRAIYD 267
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 15234666 641 RMKNYTIYAVSITIRIVFGFML-IALIWEFDFSAFMVLIIAILNDGTIM 688
Cdd:cd01431 268 NIKKNITYLLANNVAEVFAIALaLFLGGPLPLLAFQILWINLVTDLIPA 316
ATPase-IIIB_Mg TIGR01524
magnesium-translocating P-type ATPase; This model describes the magnesium translocating P-type ...
18-801 4.71e-80

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: 278.29  E-value: 4.71e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    18 PIEEVFQQLKCSREGLTTQEGEDRIQIFGPNKL-EEKKESKLLKFLGFMWNPLSWVMEMAAIMAIALANGDGrppdwqdf 96
Cdd:TIGR01524  19 GKETLLRKLGVHETGLTNVEVTERLAEFGPNQTvEEKKVPNLRLLIRAFNNPFIYILAMLMGVSYLTDDLEA-------- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    97 VGIICLLVINSTI-SFIEENNAGNAAAALMAGLAPKTKVLR------DGKWSEQEAAILVPGDIVSIKLGDIIPADARLL 169
Cdd:TIGR01524  91 TVIIALMVLASGLlGFIQESRAERAAYALKNMVKNTATVLRvinengNGSMDEVPIDALVPGDLIELAAGDIIPADARVI 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   170 EGDPLKVDQSALTGESLPV-----TKHPGQE--------VFSGSTCKQGEIEAVVIATGVHTFFGKAAHLVDSTNQVGHF 236
Cdd:TIGR01524 171 SARDLFINQSALTGESLPVekfveDKRARDPeilerenlCFMGTNVLSGHAQAVVLATGSSTWFGSLAIAATERRGQTAF 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   237 QKVLTAIGNFCICSIAIgMVIEIIVMYPIQRRKYRDGIDNLLVLLIGGIPIAMPTVLSVTMAIGSHRLSQQGAITKRMTA 316
Cdd:TIGR01524 251 DKGVKSVSKLLIRFMLV-MVPVVLMINGLMKGDWLEAFLFALAVAVGLTPEMLPMIVSSNLAKGAINMSKKKVIVKELSA 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   317 IEEMAGMDVLCSDKTGTLTLNKLSVDKNLVevfCKGVEKDQVLLFAAMASRVEN--QDAIDAAMVGMLAD--PKEARAGI 392
Cdd:TIGR01524 330 IQNFGAMDILCTDKTGTLTQDKIELEKHID---SSGETSERVLKMAWLNSYFQTgwKNVLDHAVLAKLDEsaARQTASRW 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   393 REVHFLPFNPVDKRTALTYIDGSGNWHRVSKGAPEQILELAKA----------SNDLSKKVLSIIDKYAERGLRSLAVAR 462
Cdd:TIGR01524 407 KKVDEIPFDFDRRRLSVVVENRAEVTRLICKGAVEEMLTVCTHkrfggavvtlSESEKSELQDMTAEMNRQGIRVIAVAT 486
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   463 QVVP------EKTKESPgapWEFVGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGKETGRRLGMGTNMYPSSA 536
Cdd:TIGR01524 487 KTLKvgeadfTKTDEEQ---LIIEGFLGFLDPPKESTKEAIAALFKNGINVKVLTGDNEIVTARICQEVGIDANDFLLGA 563
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   537 LLGTHKDANLASipveeLIEKADGFAGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIGIAVADATDAARGAS 616
Cdd:TIGR01524 564 DIEELSDEELAR-----ELRKYHIFARLTPMQKSRIIGLLKKAGHTVGFLGDGINDAPALRKADVGISVDTAADIAKEAS 638
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   617 DIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITIRIVFGFMLI-ALIWEFDFSAFMVLIIAILNDGTIMTISKDRV 695
Cdd:TIGR01524 639 DIILLEKSLMVLEEGVIEGRNTFGNILKYLKMTASSNFGNVFSVLVAsAFIPFLPMLSLHLLIQNLLYDFSQLTLPWDKM 718
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   696 KPS--PTPDSWKLKEIFATGVVLGGYQAIMTVIFF---WAAhktdFFSDTFGVRSirdnnheLMGAVYLQVSIISQALIF 770
Cdd:TIGR01524 719 DREflKKPHQWEQKGMGRFMLCIGPVSSIFDIATFllmWFV----FSANTVEEQA-------LFQSGWFVVGLLSQTLVV 787
                         810       820       830
                  ....*....|....*....|....*....|...
gi 15234666   771 -VTRSRSWSFVE-RPGALLMIAFLIAQLIATLI 801
Cdd:TIGR01524 788 hMIRTEKIPFIQsRAAAPVMIATLLVMALGIII 820
P-type_ATPase cd02609
uncharacterized subfamily of P-type ATPase transporter, similar to uncharacterized ...
96-681 1.69e-78

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: 269.15  E-value: 1.69e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  96 FVGIICllvINSTISFIEENNAGNAAAALMAGLAPKTKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLK 175
Cdd:cd02609  61 FLGVII---VNTVIGIVQEIRAKRQLDKLSILNAPKVTVIRDGQEVKIPPEELVLDDILILKPGEQIPADGEVVEGGGLE 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 176 VDQSALTGESLPVTKHPGQEVFSGSTCKQGEIEAVVIATGVHTFFGKAA-----------HLVDSTNQVghfQKVLTAIg 244
Cdd:cd02609 138 VDESLLTGESDLIPKKAGDKLLSGSFVVSGAAYARVTAVGAESYAAKLTleakkhklinsELLNSINKI---LKFTSFI- 213
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 245 nfcicSIAIGmVIEIIVMYPIQRRKYRDGIDNLLVLLIGGIPIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMD 324
Cdd:cd02609 214 -----IIPLG-LLLFVEALFRRGGGWRQAVVSTVAALLGMIPEGLVLLTSVALAVGAIRLAKKKVLVQELYSIETLARVD 287
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 325 VLCSDKTGTLTLNKLSVDKnLVEVFCKGVEKDQVLLFAAMASRVENQDAIDAAMVGMLADPkeaRAGIREVhfLPFNPVD 404
Cdd:cd02609 288 VLCLDKTGTITEGKMKVER-VEPLDEANEAEAAAALAAFVAASEDNNATMQAIRAAFFGNN---RFEVTSI--IPFSSAR 361
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 405 KRTALTYiDGSGNWHRvskGAPEQILelakasNDLSKKVLSIIDKYAERGLRSLAVARqVVPEKTKESPGAPWEFVGLLP 484
Cdd:cd02609 362 KWSAVEF-RDGGTWVL---GAPEVLL------GDLPSEVLSRVNELAAQGYRVLLLAR-SAGALTHEQLPVGLEPLALIL 430
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 485 LFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGKETGRRLGM-GTNMYPSSALLGTHKDANlasipveELIEKADGFAG 563
Cdd:cd02609 431 LTDPIRPEAKETLAYFAEQGVAVKVISGDNPVTVSAIAKRAGLeGAESYIDASTLTTDEELA-------EAVENYTVFGR 503
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 564 VFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIGIAVADATDAARGASDIVLTEPGLSVIISAVLTSRAIfqrMK 643
Cdd:cd02609 504 VTPEQKRQLVQALQALGHTVAMTGDGVNDVLALKEADCSIAMASGSDATRQVAQVVLLDSDFSALPDVVFEGRRV---VN 580
                       570       580       590
                ....*....|....*....|....*....|....*...
gi 15234666 644 NYTIYAVSITIRIVFGFMLiALIWEFDFSAFMVLIIAI 681
Cdd:cd02609 581 NIERVASLFLVKTIYSVLL-ALICVITALPFPFLPIQI 617
PRK10517 PRK10517
magnesium-transporting P-type ATPase MgtA;
12-675 6.05e-78

magnesium-transporting P-type ATPase MgtA;


Pssm-ID: 236705 [Multi-domain]  Cd Length: 902  Bit Score: 273.10  E-value: 6.05e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   12 VDLEKIPIEEVFQQLKCSREGLTTQEGEDRIQIFGPNKLEEKKESKLLKFLgfmW----NP----------LSWVMEMAA 77
Cdd:PRK10517  47 LKAAVMPEEELWKTFDTHPEGLNEAEVESAREQHGENELPAQKPLPWWVHL---WvcyrNPfnilltilgaISYATEDLF 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   78 IMaialangdgrppdwqdfvGIICLLVINST-ISFIEENNAGNAAAALMAGLAPKTKVLR------DGKWSEQEAAILVP 150
Cdd:PRK10517 124 AA------------------GVIALMVAISTlLNFIQEARSTKAADALKAMVSNTATVLRvindkgENGWLEIPIDQLVP 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  151 GDIVSIKLGDIIPADARLLEGDPLKVDQSALTGESLPVTKHPGQE-------------VFSGSTCKQGEIEAVVIATGVH 217
Cdd:PRK10517 186 GDIIKLAAGDMIPADLRILQARDLFVAQASLTGESLPVEKFATTRqpehsnplecdtlCFMGTNVVSGTAQAVVIATGAN 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  218 TFFGKAAHLVDST-NQVGHFQKvltaignfCICSIAIGMVIEIIVMYPIqrrkyrdgidnllVLLIGGI----------- 285
Cdd:PRK10517 266 TWFGQLAGRVSEQdSEPNAFQQ--------GISRVSWLLIRFMLVMAPV-------------VLLINGYtkgdwweaalf 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  286 ---------PIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDKNlVEVFckGVEKD 356
Cdd:PRK10517 325 alsvavgltPEMLPMIVTSTLARGAVKLSKQKVIVKRLDAIQNFGAMDILCTDKTGTLTQDKIVLENH-TDIS--GKTSE 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  357 QVLLFAAMASRVEN--QDAIDAAMVGMLADPKEARAGI--REVHFLPFNpVDKRTALTYIDGSGNWHR-VSKGAPEQIL- 430
Cdd:PRK10517 402 RVLHSAWLNSHYQTglKNLLDTAVLEGVDEESARSLASrwQKIDEIPFD-FERRRMSVVVAENTEHHQlICKGALEEILn 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  431 ---------ELAKASNDLSKKVLSIIDKYAERGLRSLAVARQVVPEkTKESPGAPWE----FVGLLPLFDPPRHDSAETI 497
Cdd:PRK10517 481 vcsqvrhngEIVPLDDIMLRRIKRVTDTLNRQGLRVVAVATKYLPA-REGDYQRADEsdliLEGYIAFLDPPKETTAPAL 559
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  498 RRALNLGVNVKMITGDQLAIGKETGRRLGMGTNMYPSSALLGTHKDANLAsipveELIEKADGFAGVFPEHKYEIVKKLQ 577
Cdd:PRK10517 560 KALKASGVTVKILTGDSELVAAKVCHEVGLDAGEVLIGSDIETLSDDELA-----NLAERTTLFARLTPMHKERIVTLLK 634
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  578 ERKHIVGMTGDGVNDAPALKKADIGIAVADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITIRIV 657
Cdd:PRK10517 635 REGHVVGFMGDGINDAPALRAADIGISVDGAVDIAREAADIILLEKSLMVLEEGVIEGRRTFANMLKYIKMTASSNFGNV 714
                        730
                 ....*....|....*...
gi 15234666  658 FGfMLIAliwefdfSAFM 675
Cdd:PRK10517 715 FS-VLVA-------SAFL 724
P-type_ATPase_Na_ENA cd02086
fungal-type Na(+)-ATPase, similar to the plasma membrane sodium transporters Saccharomyces ...
32-665 8.72e-78

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: 272.79  E-value: 8.72e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  32 GLTTQEGEDRIQIFGPNKLEEKKESKLLK-FLGFMWNPLSWVMEMAAIMAIALAngdgrppDWQDFVGIICLLVINSTIS 110
Cdd:cd02086   1 GLTNDEAERRLKEYGENELEGDTGVSAWKiLLRQVANAMTLVLIIAMALSFAVK-------DWIEGGVIAAVIALNVIVG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 111 FIEENNAGNAAAALMAGLAPKTKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLKVDQSALTGESLPVTK 190
Cdd:cd02086  74 FIQEYKAEKTMDSLRNLSSPNAHVIRSGKTETISSKDVVPGDIVLLKVGDTVPADLRLIETKNFETDEALLTGESLPVIK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 191 HPGQE---------------VFSGSTCKQGEIEAVVIATGVHTFFGK-AAHLVDSTNQVGHFQKVLTAIGNFCICSIAIG 254
Cdd:cd02086 154 DAELVfgkeedvsvgdrlnlAYSSSTVTKGRAKGIVVATGMNTEIGKiAKALRGKGGLISRDRVKSWLYGTLIVTWDAVG 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 255 MVIEIIVMYPIQRRkyrdgIDNLLVLL-------------------------------IGGIPIAMPTVLSVTMAIGSHR 303
Cdd:cd02086 234 RFLGTNVGTPLQRK-----LSKLAYLLffiavilaiivfavnkfdvdneviiyaialaISMIPESLVAVLTITMAVGAKR 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 304 LSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDK--------NLVEVFckgvEKDQVLLFAAMASRVENQDAID 375
Cdd:cd02086 309 MVKRNVIVRKLDALEALGAVTDICSDKTGTLTQGKMVVRQvwipaalcNIATVF----KDEETDCWKAHGDPTEIALQVF 384
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 376 AAMVGM--LADPKEARAGIREVHFLPFNPVDKRTALTYIDGSGNWHRV-SKGAPEQILELAKASNDLS----------KK 442
Cdd:cd02086 385 ATKFDMgkNALTKGGSAQFQHVAEFPFDSTVKRMSVVYYNNQAGDYYAyMKGAVERVLECCSSMYGKDgiiplddefrKT 464
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 443 VLSIIDKYAERGLRSLAVARQVVPE--KTKESPGAP----------WEFVGLLPLFDPPRHDSAETIRRALNLGVNVKMI 510
Cdd:cd02086 465 IIKNVESLASQGLRVLAFASRSFTKaqFNDDQLKNItlsradaesdLTFLGLVGIYDPPRNESAGAVEKCHQAGITVHML 544
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 511 TGDQ----LAIGKETG---RRLGMGTNMYPSSALL-GTHKDAnLASIPVEELIEKADGFAGVFPEHKYEIVKKLQERKHI 582
Cdd:cd02086 545 TGDHpgtaKAIAREVGilpPNSYHYSQEIMDSMVMtASQFDG-LSDEEVDALPVLPLVIARCSPQTKVRMIEALHRRKKF 623
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 583 VGMTGDGVNDAPALKKADIGIAV-ADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITIRIVfGFM 661
Cdd:cd02086 624 CAMTGDGVNDSPSLKMADVGIAMgLNGSDVAKDASDIVLTDDNFASIVNAIEEGRRMFDNIQKFVLHLLAENVAQV-ILL 702

                ....
gi 15234666 662 LIAL 665
Cdd:cd02086 703 LIGL 706
ATPase-IIA1_Ca TIGR01116
sarco/endoplasmic reticulum calcium-translocating P-type ATPase; This model describes the ...
91-685 2.87e-73

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: 260.10  E-value: 2.87e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    91 PDWQDFVGIICLLVINSTISFIEENNAGNAAAALMAGLAPKTKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLE 170
Cdd:TIGR01116  34 TAFVEPFVILLILVANAIVGVWQERNAEKAIEALKEYESEHAKVLRDGRWSVIKAKDLVPGDIVELAVGDKVPADIRVLS 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   171 GDPLKVDQSALTGESLPVTKH----PGQE---------VFSGSTCKQGEIEAVVIATGVHTFFGK-AAHLVDSTNQVGHF 236
Cdd:TIGR01116 114 LKTLRVDQSILTGESVSVNKHtesvPDERavnqdkknmLFSGTLVVAGKARGVVVRTGMSTEIGKiRDEMRAAEQEDTPL 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   237 QKVLTAIGNFC------ICSIAIGMVIEIIVMYPIQRRKYRDGIDNLLV---LLIGGIPIAMPTVLSVTMAIGSHRLSQQ 307
Cdd:TIGR01116 194 QKKLDEFGELLskviglICILVWVINIGHFNDPALGGGWIQGAIYYFKIavaLAVAAIPEGLPAVITTCLALGTRKMAKK 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   308 GAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSV----------------------------------------DKNLVE 347
Cdd:TIGR01116 274 NAIVRKLPSVETLGCTTVICSDKTGTLTTNQMSVckvvaldpsssslnefcvtgttyapeggvikddgpvaggqDAGLEE 353
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   348 VF-CKGVEKDQVLLFAAMASRVENQ-DAIDAAM-------------VGMLADPKEA-------RAGIREVHFLPFNPvDK 405
Cdd:TIGR01116 354 LAtIAALCNDSSLDFNERKGVYEKVgEATEAALkvlvekmglpatkNGVSSKRRPAlgcnsvwNDKFKKLATLEFSR-DR 432
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   406 RTALTYIDGSGNWHRVSKGAPEQILE-----------LAKASNDLSKKVLSIIDKYAER-GLRSLAVARQVVPEKTKESP 473
Cdd:TIGR01116 433 KSMSVLCKPSTGNKLFVKGAPEGVLErcthilngdgrAVPLTDKMKNTILSVIKEMGTTkALRCLALAFKDIPDPREEDL 512
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   474 G------APWE----FVGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGKETGRRLGMgtnMYPSSALLGThkd 543
Cdd:TIGR01116 513 LsdpanfEAIEsdltFIGVVGMLDPPRPEVADAIEKCRTAGIRVIMITGDNKETAEAICRRIGI---FSPDEDVTFK--- 586
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   544 aNLASIPVEELIEKADG--------FAGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIGIAVADATDAARGA 615
Cdd:TIGR01116 587 -SFTGREFDEMGPAKQRaacrsavlFSRVEPSHKSELVELLQEQGEIVAMTGDGVNDAPALKKADIGIAMGSGTEVAKEA 665
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15234666   616 SDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITI-RIVFGFMLIALIWEFDFSAFMVLIIAILNDG 685
Cdd:TIGR01116 666 SDMVLADDNFATIVAAVEEGRAIYNNMKQFIRYMISSNIgEVVCIFLTAALGIPEGLIPVQLLWVNLVTDG 736
P-type_ATPase_Ca_PMCA-like cd02081
animal plasma membrane Ca2(+)-ATPases (PMCA), similar to human ATP2B1-4/PMCA1-4, and related ...
39-640 4.32e-72

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: 252.89  E-value: 4.32e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  39 EDRIQIFGPNKLEEKKESKLLKFlgfMWNPLSWVMEMA---------AIMAIALANGDGRPPDWQDFVGI-ICLLVINST 108
Cdd:cd02081   2 EHRREVYGKNEIPPKPPKSFLQL---VWEALQDPTLIIlliaaivslGLGFYTPFGEGEGKTGWIEGVAIlVAVILVVLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 109 ISFIEENNAGNAAAALMAGLAPKTKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLKVDQSALTGESLPV 188
Cdd:cd02081  79 TAGNDYQKEKQFRKLNSKKEDQKVTVIRDGEVIQISVFDIVVGDIVQLKYGDLIPADGLLIEGNDLKIDESSLTGESDPI 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 189 TKHPGQE-----VFSGSTCKQGEIEAVVIATGVHTFFGKAAHLVDSTNQV-----GHFQKVLTAIGNF-CICSIA--IGM 255
Cdd:cd02081 159 KKTPDNQipdpfLLSGTKVLEGSGKMLVTAVGVNSQTGKIMTLLRAENEEktplqEKLTKLAVQIGKVgLIVAALtfIVL 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 256 VIEIIVMYPIQRRKYRDGID-----NLLVLLIGGIPIAMPT--VLSVTM--AIGSHRLSQQGAITKRMTAIEEMAGMDVL 326
Cdd:cd02081 239 IIRFIIDGFVNDGKSFSAEDlqefvNFFIIAVTIIVVAVPEglPLAVTLslAYSVKKMMKDNNLVRHLDACETMGNATAI 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 327 CSDKTGTLTLNKLSVDKnlvevFCKGVEKDQVLLFAAMAsrvenqdaidaamVGMLADPKEARAGIREVHFLPFNPVDKR 406
Cdd:cd02081 319 CSDKTGTLTQNRMTVVQ-----GYIGNKTECALLGFVLE-------------LGGDYRYREKRPEEKVLKVYPFNSARKR 380
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 407 TALTYIDGSGNWHRVSKGAPEQILEL-----------AKASNDLSKKVLSIIDKYAERGLRSLAVARQVVPEKTKESPGA 475
Cdd:cd02081 381 MSTVVRLKDGGYRLYVKGASEIVLKKcsyilnsdgevVFLTSEKKEEIKRVIEPMASDSLRTIGLAYRDFSPDEEPTAER 460
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 476 PWE----------FVGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGKETGRRLGMGTNMYPSSALLGthKDAN 545
Cdd:cd02081 461 DWDdeediesdltFIGIVGIKDPLRPEVPEAVAKCQRAGITVRMVTGDNINTARAIARECGILTEGEDGLVLEG--KEFR 538
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 546 LASipVEELIEKADG-FAGVF----------PEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIGIAVADA-TDAAR 613
Cdd:cd02081 539 ELI--DEEVGEVCQEkFDKIWpklrvlarssPEDKYTLVKGLKDSGEVVAVTGDGTNDAPALKKADVGFAMGIAgTEVAK 616
                       650       660
                ....*....|....*....|....*..
gi 15234666 614 GASDIVLTEPGLSVIISAVLTSRAIFQ 640
Cdd:cd02081 617 EASDIILLDDNFSSIVKAVMWGRNVYD 643
PRK15122 PRK15122
magnesium-transporting ATPase; Provisional
18-639 7.83e-70

magnesium-transporting ATPase; Provisional


Pssm-ID: 237914 [Multi-domain]  Cd Length: 903  Bit Score: 249.94  E-value: 7.83e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   18 PIEEVFQQLKCSREGLTTQEGEDRIQIFGPNKL-EEKKESKLLKFLGFMWNPLSWVMEMAAIMAIALANG----DGRPPD 92
Cdd:PRK15122  31 SLEETLANLNTHRQGLTEEDAAERLQRYGPNEVaHEKPPHALVQLLQAFNNPFIYVLMVLAAISFFTDYWlplrRGEETD 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   93 WqdfVGIICLLV---INSTISFIEENNAGNAAAALMAGLAPKTKVLR----DGKWSEQEAAI--LVPGDIVSIKLGDIIP 163
Cdd:PRK15122 111 L---TGVIIILTmvlLSGLLRFWQEFRSNKAAEALKAMVRTTATVLRrghaGAEPVRREIPMreLVPGDIVHLSAGDMIP 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  164 ADARLLEGDPLKVDQSALTGESLPVTKH--------------PGQEV---------FSGSTCKQGEIEAVVIATGVHTFF 220
Cdd:PRK15122 188 ADVRLIESRDLFISQAVLTGEALPVEKYdtlgavagksadalADDEGslldlpnicFMGTNVVSGTATAVVVATGSRTYF 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  221 GKAAHLVDSTNQVGHFQKvltaignfCICSIAIGMVIEIIVMYPIqrrkyrdgidnllVLLIGGI--------------- 285
Cdd:PRK15122 268 GSLAKSIVGTRAQTAFDR--------GVNSVSWLLIRFMLVMVPV-------------VLLINGFtkgdwleallfalav 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  286 -----PIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDKNLVevfCKGVEKDQVLL 360
Cdd:PRK15122 327 avgltPEMLPMIVSSNLAKGAIAMARRKVVVKRLNAIQNFGAMDVLCTDKTGTLTQDRIILEHHLD---VSGRKDERVLQ 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  361 FAAMASRVEN--QDAIDAAMV--GMLADPKEARAGIREVHFLPFNPVDKRTALTYIDGSGNWHRVSKGAPEQILELAKAS 436
Cdd:PRK15122 404 LAWLNSFHQSgmKNLMDQAVVafAEGNPEIVKPAGYRKVDELPFDFVRRRLSVVVEDAQGQHLLICKGAVEEMLAVATHV 483
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  437 ND----------LSKKVLSIIDKYAERGLRSLAVARQVVPEKTKESP---GAPWEFV--GLLPLFDPPRHDSAETIRrAL 501
Cdd:PRK15122 484 RDgdtvrpldeaRRERLLALAEAYNADGFRVLLVATREIPGGESRAQystADERDLVirGFLTFLDPPKESAAPAIA-AL 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  502 N-LGVNVKMITGDQLAIGKETGRRLGMGtnmyPSSALLGTHKDAnLASIPVEELIEKADGFAGVFPEHKYEIVKKLQERK 580
Cdd:PRK15122 563 ReNGVAVKVLTGDNPIVTAKICREVGLE----PGEPLLGTEIEA-MDDAALAREVEERTVFAKLTPLQKSRVLKALQANG 637
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15234666  581 HIVGMTGDGVNDAPALKKADIGIAVADATDAARGASDIVLTEPGLSVIISAVLTSRAIF 639
Cdd:PRK15122 638 HTVGFLGDGINDAPALRDADVGISVDSGADIAKESADIILLEKSLMVLEEGVIKGRETF 696
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
130-643 2.54e-68

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 241.97  E-value: 2.54e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 130 PKT-KVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLkVDQSALTGESLPVTKHPGQEVFSGSTCKQGEIE 208
Cdd:COG2217 212 PKTaRVLRDGEEVEVPVEELRVGDRVLVRPGERIPVDGVVLEGESS-VDESMLTGESLPVEKTPGDEVFAGTINLDGSLR 290
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 209 AVVIATGVHTFFGKAAHLV-DSTNQVGHFQKVLTAI-GNFCICSIAIGMVIeIIVMYPIQRRkYRDGIDNLLVLLIggip 286
Cdd:COG2217 291 VRVTKVGSDTTLARIIRLVeEAQSSKAPIQRLADRIaRYFVPAVLAIAALT-FLVWLLFGGD-FSTALYRAVAVLV---- 364
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 287 IAMPT--VLSVTMAI--GSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDKnlVEVFcKGVEKDQVLlfa 362
Cdd:COG2217 365 IACPCalGLATPTAImvGTGRAARRGILIKGGEALERLAKVDTVVFDKTGTLTEGKPEVTD--VVPL-DGLDEDELL--- 438
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 363 AMASRVENQ------DAIDAAmvgmladpkearAGIREVHFLPfnpVDKRTALT------YIDGsgnwHRVSKGAPEQIL 430
Cdd:COG2217 439 ALAAALEQGsehplaRAIVAA------------AKERGLELPE---VEDFEAIPgkgveaTVDG----KRVLVGSPRLLE 499
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 431 ELAKasnDLSKKVLSIIDKYAERGLRSLAVARQvvpektkespGapwEFVGLLPLFDPPRHDSAETIRRALNLGVNVKMI 510
Cdd:COG2217 500 EEGI---DLPEALEERAEELEAEGKTVVYVAVD----------G---RLLGLIALADTLRPEAAEAIAALKALGIRVVML 563
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 511 TGDQLAIGKETGRRLGmgtnmypssallgthkdanlasipveelIEKAdgFAGVFPEHKYEIVKKLQERKHIVGMTGDGV 590
Cdd:COG2217 564 TGDNERTAEAVARELG----------------------------IDEV--RAEVLPEDKAAAVRELQAQGKKVAMVGDGI 613
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|...
gi 15234666 591 NDAPALKKADIGIAVADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMK 643
Cdd:COG2217 614 NDAPALAAADVGIAMGSGTDVAIEAADIVLMRDDLRGVPDAIRLSRATMRIIR 666
P-type_ATPase_SERCA cd02083
sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; ...
18-654 1.44e-67

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: 244.51  E-value: 1.44e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  18 PIEEVFQQLKCSRE-GLTTQEGEDRIQIFGPNKL--EEKK----------ESKLLKFL------GFMwnpLSWVMEMAAI 78
Cdd:cd02083   4 TVEEVLAYFGVDPTrGLSDEQVKRRREKYGPNELpaEEGKslwelvleqfDDLLVRILllaaiiSFV---LALFEEGEEG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  79 maialangdgrppdWQDFVG---IICLLVINSTISFIEENNAGNAAAALMAGLAPKTKVLRDGK-WSEQEAAILVPGDIV 154
Cdd:cd02083  81 --------------VTAFVEpfvILLILIANAVVGVWQERNAEKAIEALKEYEPEMAKVLRNGKgVQRIRARELVPGDIV 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 155 SIKLGDIIPADARLLE--GDPLKVDQSALTGESLPVTKH----PGQE---------VFSGSTCKQGEIEAVVIATGVHTF 219
Cdd:cd02083 147 EVAVGDKVPADIRIIEikSTTLRVDQSILTGESVSVIKHtdvvPDPRavnqdkknmLFSGTNVAAGKARGVVVGTGLNTE 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 220 FGKAAHLVDSTNQV-----------GHF-QKVLTAIgnfCICSIAI-----------GMVIEIIVMY-PIQrrkyrdgid 275
Cdd:cd02083 227 IGKIRDEMAETEEEktplqqkldefGEQlSKVISVI---CVAVWAInighfndpahgGSWIKGAIYYfKIA--------- 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 276 nlLVLLIGGIPIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDK-----------N 344
Cdd:cd02083 295 --VALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVSRmfildkveddsS 372
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 345 LVEVFCKGV-----------------EKDQVLLFAAMASRVENQDAID----------------AA---MVGMLADPKEA 388
Cdd:cd02083 373 LNEFEVTGStyapegevfkngkkvkaGQYDGLVELATICALCNDSSLDyneskgvyekvgeateTAltvLVEKMNVFNTD 452
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 389 RAG-IREVHFLPFNPV---------------DKRTALTYI--DGSGNWHRV-SKGAPEQILE-------------LAKAS 436
Cdd:cd02083 453 KSGlSKRERANACNDVieqlwkkeftlefsrDRKSMSVYCspTKASGGNKLfVKGAPEGVLErcthvrvgggkvvPLTAA 532
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 437 ndLSKKVLSIIDKYAERGLRSLAVARQVVPEKTKE------SPGAPWE----FVGLLPLFDPPRHDSAETIRRALNLGVN 506
Cdd:cd02083 533 --IKILILKKVWGYGTDTLRCLALATKDTPPKPEDmdledsTKFYKYEtdltFVGVVGMLDPPRPEVRDSIEKCRDAGIR 610
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 507 VKMITGDQLAIGKETGRRLGMGTNMYPSSALLGTHKDanLASIPVEELIE---KADGFAGVFPEHKYEIVKKLQERKHIV 583
Cdd:cd02083 611 VIVITGDNKGTAEAICRRIGIFGEDEDTTGKSYTGRE--FDDLSPEEQREacrRARLFSRVEPSHKSKIVELLQSQGEIT 688
                       730       740       750       760       770       780       790
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15234666 584 GMTGDGVNDAPALKKADIGIAVADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITI 654
Cdd:cd02083 689 AMTGDGVNDAPALKKAEIGIAMGSGTAVAKSASDMVLADDNFATIVAAVEEGRAIYNNMKQFIRYLISSNI 759
ATPase-IB_hvy TIGR01525
heavy metal translocating P-type ATPase; This model encompasses two equivalog models for the ...
130-683 7.11e-61

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: 217.50  E-value: 7.11e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   130 PKTKVLRDGKWSEQEAAI--LVPGDIVSIKLGDIIPADARLLEGDPLkVDQSALTGESLPVTKHPGQEVFSGSTCKQGEI 207
Cdd:TIGR01525  54 PSTARVLQGDGSEEEVPVeeLQVGDIVIVRPGERIPVDGVVISGESE-VDESALTGESMPVEKKEGDEVFAGTINGDGSL 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   208 EAVVIATGVHTFFGKAAHLV-DSTNQVGHFQKVLTAI-GNFCICSIAIGMVIeiIVMYPIQRRKYRDGIDNLLVLLIGGI 285
Cdd:TIGR01525 133 TIRVTKLGEDSTLAQIVELVeEAQSSKAPIQRLADRIaSYYVPAVLAIALLT--FVVWLALGALWREALYRALTVLVVAC 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   286 PIAMptVLSVTMAI--GSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDKnlVEVFcKGVEKDQVL-LFA 362
Cdd:TIGR01525 211 PCAL--GLATPVAIlvAIGAAARRGILIKGGDALEKLAKVKTVVFDKTGTLTTGKPTVVD--IEPL-DDASEEELLaLAA 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   363 AMASRVEN------QDAIDAAMVGMLADPKEARAGIR-EVHflpfnpvdkrtaltyIDGSGNWhRVSKGAPEQILELAKA 435
Cdd:TIGR01525 286 ALEQSSSHplaraiVRYAKERGLELPPEDVEEVPGKGvEAT---------------VDGGREV-RIGNPRFLGNRELAIE 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   436 SNDLSKKVLsiiDKYAERGLRSLAVARQVvpektkespgapwEFVGLLPLFDPPRHDSAETIRRALNLGV-NVKMITGDQ 514
Cdd:TIGR01525 350 PISASPDLL---NEGESQGKTVVFVAVDG-------------ELLGVIALRDQLRPEAKEAIAALKRAGGiKLVMLTGDN 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   515 LAIGKETGRRLGMGTNMYpssallgthkdanlasipveeliekadgfAGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAP 594
Cdd:TIGR01525 414 RSAAEAVAAELGIDDEVH-----------------------------AELLPEDKLAIVKKLQEEGGPVAMVGDGINDAP 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   595 ALKKADIGIAVADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMK-NYTIYAVSITIRIVFGFMLIALIWEfdFSA 673
Cdd:TIGR01525 465 ALAAADVGIAMGSGSDVAIEAADIVLLNDDLRSLPTAIDLSRKTRRIIKqNLAWALGYNLVAIPLAAGGLLPLWL--AVL 542
                         570
                  ....*....|..
gi 15234666   674 FMVL--IIAILN 683
Cdd:TIGR01525 543 LHEGstVLVVLN 554
P-type_ATPase_Cu-like cd02094
P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A ...
130-643 3.48e-57

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: 208.87  E-value: 3.48e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 130 PKT-KVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLkVDQSALTGESLPVTKHPGQEVFSGSTCKQGEIE 208
Cdd:cd02094 138 PKTaRVIRDGKEVEVPIEEVQVGDIVRVRPGEKIPVDGVVVEGESS-VDESMLTGESLPVEKKPGDKVIGGTINGNGSLL 216
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 209 AVVIATGVHTFFGKAAHLVDSTnQVGH--FQK-------------VLTAIGNFCICSIAIG-MVIEIIVMYPIQrrkyrd 272
Cdd:cd02094 217 VRATRVGADTTLAQIIRLVEEA-QGSKapIQRladrvsgvfvpvvIAIAILTFLVWLLLGPePALTFALVAAVA------ 289
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 273 gidnllVLLIG---GIPIAMPTVLSVtmaiGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDKnlVEVF 349
Cdd:cd02094 290 ------VLVIAcpcALGLATPTAIMV----GTGRAAELGILIKGGEALERAHKVDTVVFDKTGTLTEGKPEVTD--VVPL 357
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 350 cKGVEKDQVLLFAAMasrVENQDA--IDAAMVgmladpkeARAGIREvhfLPFNPVDKRTALTY--IDGSGNWHRVSKGA 425
Cdd:cd02094 358 -PGDDEDELLRLAAS---LEQGSEhpLAKAIV--------AAAKEKG---LELPEVEDFEAIPGkgVRGTVDGRRVLVGN 422
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 426 PEQILELAkasNDLSKKVlSIIDKYAERGLRSLAVARqvvpektkespgaPWEFVGLLPLFDPPRHDSAETIRRALNLGV 505
Cdd:cd02094 423 RRLMEENG---IDLSALE-AEALALEEEGKTVVLVAV-------------DGELAGLIAVADPLKPDAAEAIEALKKMGI 485
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 506 NVKMITGDQLAIGKETGRRLGmgtnmypssallgthkdanlasipveelIEKAdgFAGVFPEHKYEIVKKLQERKHIVGM 585
Cdd:cd02094 486 KVVMLTGDNRRTARAIAKELG----------------------------IDEV--IAEVLPEDKAEKVKKLQAQGKKVAM 535
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15234666 586 TGDGVNDAPALKKADIGIAVADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMK 643
Cdd:cd02094 536 VGDGINDAPALAQADVGIAIGSGTDVAIESADIVLMRGDLRGVVTAIDLSRATMRNIK 593
ATPase-IIB_Ca TIGR01517
plasma-membrane calcium-translocating P-type ATPase; This model describes the P-type ATPase ...
2-657 4.22e-57

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: 213.10  E-value: 4.22e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666     2 SSLEDIKNETVDL-EKI-PIEEVFQQLKCS-REGL--TTQEGEDRIQIFGPNKLEEKKEsklLKFLGFMWNPLSWVM--- 73
Cdd:TIGR01517  26 TDLTDIFKKAMPLyEKLgGAEGIATKLKTDlNEGVrlSSSTLERREKVYGKNELPEKPP---KSFLQIVWAALSDQTlil 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    74 ---------EMAAIMAIALANGDGRPPDWQDFVGIICLLVINSTISFIEENNAGNA-AAALMAGLAPKTKVLRDGkwSEQ 143
Cdd:TIGR01517 103 lsvaavvslVLGLYVPSVGEDKADTETGWIEGVAILVSVILVVLVTAVNDYKKELQfRQLNREKSAQKIAVIRGG--QEQ 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   144 EAAI--LVPGDIVSIKLGDIIPADARLLEGDPLKVDQSALTGESLPVTKHPGQEVF--SGSTCKQGEIEAVVIATGVHTF 219
Cdd:TIGR01517 181 QISIhdIVVGDIVSLSTGDVVPADGVFISGLSLEIDESSITGESDPIKKGPVQDPFllSGTVVNEGSGRMLVTAVGVNSF 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   220 FGKaahLVDSTNQVG--------HFQKVLTAIGNFCICSIAIGMVI----EIIVMYPIQRRKYRDGID-----NLLVLLI 282
Cdd:TIGR01517 261 GGK---LMMELRQAGeeetplqeKLSELAGLIGKFGMGSAVLLFLVlslrYVFRIIRGDGRFEDTEEDaqtflDHFIIAV 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   283 GGIPIAMPTV--LSVTMAI--GSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDKNLV-EVFCKGVEKD- 356
Cdd:TIGR01517 338 TIVVVAVPEGlpLAVTIALaySMKKMMKDNNLVRHLAACETMGSATAICSDKTGTLTQNVMSVVQGYIgEQRFNVRDEIv 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   357 --------QVLLFAAMA---SRVENQDA----------IDAAMVGML-------ADPKEARAGIREVHFLPFNPVDKRTA 408
Cdd:TIGR01517 418 lrnlpaavRNILVEGISlnsSSEEVVDRggkrafigskTECALLDFGlllllqsRDVQEVRAEEKVVKIYPFNSERKFMS 497
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   409 LTyIDGSGNWHRV-SKGAPEQIL-----------ELAKASNDLSKKVLSIIDKYAERGLRSLAVA---RQVVPEKTKESP 473
Cdd:TIGR01517 498 VV-VKHSGGKYREfRKGASEIVLkpcrkrldsngEATPISEDDKDRCADVIEPLASDALRTICLAyrdFAPEEFPRKDYP 576
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   474 GAPWEFVGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGKETGRRLGMGTnmYPSSALLGThkdaNLASIPVEE 553
Cdd:TIGR01517 577 NKGLTLIGVVGIKDPLRPGVREAVQECQRAGITVRMVTGDNIDTAKAIARNCGILT--FGGLAMEGK----EFRSLVYEE 650
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   554 LI---EKADGFAGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIGIAVADA-TDAARGASDIVLTEPGLSVII 629
Cdd:TIGR01517 651 MDpilPKLRVLARSSPLDKQLLVLMLKDMGEVVAVTGDGTNDAPALKLADVGFSMGISgTEVAKEASDIILLDDNFASIV 730
                         730       740       750
                  ....*....|....*....|....*....|...
gi 15234666   630 SAVLTSRAIFQRMKNY-----TIYAVSITIRIV 657
Cdd:TIGR01517 731 RAVKWGRNVYDNIRKFlqfqlTVNVVAVILTFV 763
ATPase-IID_K-Na TIGR01523
potassium and/or sodium efflux P-type ATPase, fungal-type; Initially described as a calcium ...
31-718 3.03e-56

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: 211.41  E-value: 3.03e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666     31 EGLTTQEGEDRIQIFGPNKLE-EKKESKLLKFLGFMWNPLSWVMEMAAIMAIALAngdgrppDWQDFVGIICLLVINSTI 109
Cdd:TIGR01523   25 EGLTHDEAQHRLKEVGENRLEaDSGIDAKAMLLHQVCNAMCMVLIIAAAISFAMH-------DWIEGGVISAIIALNILI 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    110 SFIEENNAGNAAAALMAGLAPKTKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLKVDQSALTGESLPVT 189
Cdd:TIGR01523   98 GFIQEYKAEKTMDSLKNLASPMAHVIRNGKSDAIDSHDLVPGDICLLKTGDTIPADLRLIETKNFDTDEALLTGESLPVI 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    190 KHP----GQE-----------VFSGSTCKQGEIEAVVIATGVHTFFGKAA---------------------------HLV 227
Cdd:TIGR01523  178 KDAhatfGKEedtpigdrinlAFSSSAVTKGRAKGICIATALNSEIGAIAaglqgdgglfqrpekddpnkrrklnkwILK 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    228 DSTNQVGHF---------QKVLTAIGNFCICsiaIGMVIEIIVMypiqrRKYRDGIDN-----LLVLLIGGIPIAMPTVL 293
Cdd:TIGR01523  258 VTKKVTGAFlglnvgtplHRKLSKLAVILFC---IAIIFAIIVM-----AAHKFDVDKevaiyAICLAISIIPESLIAVL 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    294 SVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKL-----------------SVDKN--------LVEV 348
Cdd:TIGR01523  330 SITMAMGAANMSKRNVIVRKLDALEALGAVNDICSDKTGTITQGKMiarqiwiprfgtisidnSDDAFnpnegnvsGIPR 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    349 FC-----------KGV---------EKD-----------QVLLFAAMA--SRVENQDAIDAAMVGmlADPKE-------- 387
Cdd:TIGR01523  410 FSpyeyshneaadQDIlkefkdelkEIDlpedidmdlfiKLLETAALAniATVFKDDATDCWKAH--GDPTEiaihvfak 487
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    388 ------------------------------ARAGIREVHFL---PFNPVDKRTALTYIDGSGNWHRV-SKGAPEQILELA 433
Cdd:TIGR01523  488 kfdlphnaltgeedllksnendqsslsqhnEKPGSAQFEFIaefPFDSEIKRMASIYEDNHGETYNIyAKGAFERIIECC 567
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    434 KASNDLSKKVLSIIDK------------YAERGLRSLAVARQVV---------------PEKTKESPgapWEFVGLLPLF 486
Cdd:TIGR01523  568 SSSNGKDGVKISPLEDcdreliianmesLAAEGLRVLAFASKSFdkadnnddqlknetlNRATAESD---LEFLGLIGIY 644
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    487 DPPRHDSAETIRRALNLGVNVKMITGDQLAIGKETGRRLG-MGTNMYPSS-------ALLGTHKDAnLASIPVEELIEKA 558
Cdd:TIGR01523  645 DPPRNESAGAVEKCHQAGINVHMLTGDFPETAKAIAQEVGiIPPNFIHDRdeimdsmVMTGSQFDA-LSDEEVDDLKALC 723
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    559 DGFAGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIGIAVA-DATDAARGASDIVLTEPGLSVIISAVLTSRA 637
Cdd:TIGR01523  724 LVIARCAPQTKVKMIEALHRRKAFCAMTGDGVNDSPSLKMANVGIAMGiNGSDVAKDASDIVLSDDNFASILNAIEEGRR 803
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    638 IFQRMKNYTIYAVSITIRIVFgFMLIALIWE-------FDFSAFMVL-IIAILNDGTIMTISKDRVKPS----PTPDS-- 703
Cdd:TIGR01523  804 MFDNIMKFVLHLLAENVAEAI-LLIIGLAFRdengksvFPLSPVEILwCIMITSCFPAMGLGLEKAAPDlmdrLPHDNev 882
                          890       900
                   ....*....|....*....|
gi 15234666    704 ----WKL-KEIFATGVVLGG 718
Cdd:TIGR01523  883 gifqKELiIDMFAYGFFLGG 902
P-type_ATPase_HM cd02079
P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) ...
131-643 6.43e-56

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: 204.76  E-value: 6.43e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 131 KTKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLkVDQSALTGESLPVTKHPGQEVFSGSTCKQGEIEAV 210
Cdd:cd02079 126 TATVLEDGSTEEVPVDDLKVGDVVLVKPGERIPVDGVVVSGESS-VDESSLTGESLPVEKGAGDTVFAGTINLNGPLTIE 204
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 211 VIATGVHTFFGKAAHLVDST-NQVGHFQKVLTAI-GNFCICSIAIGMVIEIIvmYPIQRRKYRDGIDNLLVLLIGGIP-- 286
Cdd:cd02079 205 VTKTGEDTTLAKIIRLVEEAqSSKPPLQRLADRFaRYFTPAVLVLAALVFLF--WPLVGGPPSLALYRALAVLVVACPca 282
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 287 --IAMPTVLSVtmaiGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVdknlVEVFC-KGVEKDQVLlfaA 363
Cdd:cd02079 283 lgLATPTAIVA----GIGRAARKGILIKGGDVLETLAKVDTVAFDKTGTLTEGKPEV----TEIEPlEGFSEDELL---A 351
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 364 MASRVENQD------AIDAAMVGMLADPKEAragirevhflpfnpvdkrTALTYIDGSG-----NWHRVSKGAPEQILEL 432
Cdd:cd02079 352 LAAALEQHSehplarAIVEAAEEKGLPPLEV------------------EDVEEIPGKGisgevDGREVLIGSLSFAEEE 413
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 433 A---KASNDLSKKVLSIIdkyaerglrSLAVARQVvpektkespgapwefVGLLPLFDPPRHDSAETIRRALNLGVNVKM 509
Cdd:cd02079 414 GlveAADALSDAGKTSAV---------YVGRDGKL---------------VGLFALEDQLRPEAKEVIAELKSGGIKVVM 469
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 510 ITGDQLAIGKETGRRLGMgtnmypssallgthkdanlasipveeliekADGFAGVFPEHKYEIVKKLQERKHIVGMTGDG 589
Cdd:cd02079 470 LTGDNEAAAQAVAKELGI------------------------------DEVHAGLLPEDKLAIVKALQAEGGPVAMVGDG 519
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....
gi 15234666 590 VNDAPALKKADIGIAVADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMK 643
Cdd:cd02079 520 INDAPALAQADVGIAMGSGTDVAIETADIVLLSNDLSKLPDAIRLARRTRRIIK 573
ATPase-IIC_X-K TIGR01106
sodium or proton efflux -- potassium uptake antiporter, P-type ATPase, alpha subunit; This ...
4-654 1.49e-55

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: 208.88  E-value: 1.49e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666     4 LEDIKNE-TVDLEKIPIEEVFQQLKCSRE-GLTTQEGEDRIQIFGPNKLEEKKES-KLLKFLGFMWNPLS---WVMEMAA 77
Cdd:TIGR01106   6 LDELKKEvEMDDHKLSLDELERKYGTDLSkGLSAARAAEILARDGPNALTPPPTTpEWVKFCRQLFGGFSmllWIGAILC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    78 IMAIALANG-DGRPPDWQDFVGIICLLVINST--ISFIEENNAGNAAAALMAGLAPKTKVLRDGKWSEQEAAILVPGDIV 154
Cdd:TIGR01106  86 FLAYGIQAStEEEPQNDNLYLGVVLSAVVIITgcFSYYQEAKSSKIMESFKNMVPQQALVIRDGEKMSINAEQVVVGDLV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   155 SIKLGDIIPADARLLEGDPLKVDQSALTGESLPVTKHPG----------QEVFSGSTCKQGEIEAVVIATGVHTFFGKAA 224
Cdd:TIGR01106 166 EVKGGDRIPADLRIISAQGCKVDNSSLTGESEPQTRSPEfthenpletrNIAFFSTNCVEGTARGIVVNTGDRTVMGRIA 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   225 HLVDSTN--------QVGHFQKVLTAIGNFcicsiaIGMVIEIIVMypIQRRKYRDGIDNLLVLLIGGIPIAMPTVLSVT 296
Cdd:TIGR01106 246 SLASGLEngktpiaiEIEHFIHIITGVAVF------LGVSFFILSL--ILGYTWLEAVIFLIGIIVANVPEGLLATVTVC 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   297 MAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSV-----DKNLVE----------VFCKGVEKDQVLL- 360
Cdd:TIGR01106 318 LTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVahmwfDNQIHEadttedqsgvSFDKSSATWLALSr 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   361 FAAMASRVE---NQDAI---------DAAMVGML-------ADPKEARAGIREVHFLPFNPVDKR--TALTYIDGSGNWH 419
Cdd:TIGR01106 398 IAGLCNRAVfkaGQENVpilkravagDASESALLkcielclGSVMEMRERNPKVVEIPFNSTNKYqlSIHENEDPRDPRH 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   420 -RVSKGAPEQILElaKASNDLSKKVLSIIDK---------YAE---RGLRSLAVARQVVPEKtKESPGAPWE-------- 478
Cdd:TIGR01106 478 lLVMKGAPERILE--RCSSILIHGKEQPLDEelkeafqnaYLElggLGERVLGFCHLYLPDE-QFPEGFQFDtddvnfpt 554
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   479 ----FVGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQ----LAIGKETG-------------RRLGMG-TNMYPSSA 536
Cdd:TIGR01106 555 dnlcFVGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHpitaKAIAKGVGiisegnetvediaARLNIPvSQVNPRDA 634
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   537 LLGTHKDANLASIPVEELIEKADG-----FAGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIGIAVADA-TD 610
Cdd:TIGR01106 635 KACVVHGSDLKDMTSEQLDEILKYhteivFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIAgSD 714
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....
gi 15234666   611 AARGASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITI 654
Cdd:TIGR01106 715 VSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNI 758
P-type_ATPase_Na-K_like cd02608
alpha-subunit of Na(+)/K(+)-ATPases and of gastric H(+)/K(+)-ATPase, similar to the human Na(+) ...
32-654 5.71e-55

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: 206.43  E-value: 5.71e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  32 GLTTQEGEDRIQIFGPNKLE-EKKESKLLKFLGFMWNPLS---WV----------MEMAAimaialangDGRPPDWQDFV 97
Cdd:cd02608   1 GLTSARAAEILARDGPNALTpPPTTPEWVKFCKQLFGGFSmllWIgailcflaygIQAAT---------EEEPSNDNLYL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  98 GIICLLVINST--ISFIEENNAGNAAAALMAGLAPKTKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLK 175
Cdd:cd02608  72 GIVLAAVVIVTgcFSYYQEAKSSKIMDSFKNMVPQQALVIRDGEKMQINAEELVVGDLVEVKGGDRIPADIRIISAHGCK 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 176 VDQSALTGESLPVTKHPG----------QEVFSGSTCKQGEIEAVVIATGVHTFFGKAAHLVDSTN--------QVGHFQ 237
Cdd:cd02608 152 VDNSSLTGESEPQTRSPEfthenpletkNIAFFSTNCVEGTARGIVINTGDRTVMGRIATLASGLEvgktpiarEIEHFI 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 238 KVLTAIGNFCICSIAIgmvIEIIVMYPiqrrkYRDGIdnllVLLIgGIPIA------MPTVlSVTMAIGSHRLSQQGAIT 311
Cdd:cd02608 232 HIITGVAVFLGVSFFI---LSLILGYT-----WLEAV----IFLI-GIIVAnvpeglLATV-TVCLTLTAKRMARKNCLV 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 312 KRMTAIEEMAGMDVLCSDKTGTLTLNKLSV-----DKNLVEV----------FCKGVEKDQVLL-FAAMASRVE---NQD 372
Cdd:cd02608 298 KNLEAVETLGSTSTICSDKTGTLTQNRMTVahmwfDNQIHEAdttedqsgasFDKSSATWLALSrIAGLCNRAEfkaGQE 377
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 373 AI---------DAAMVGML-------ADPKEARAGIREVHFLPFNPVDKRTALTYIDGSGNWHR---VSKGAPEQILELA 433
Cdd:cd02608 378 NVpilkrdvngDASESALLkcielscGSVMEMRERNPKVAEIPFNSTNKYQLSIHENEDPGDPRyllVMKGAPERILDRC 457
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 434 kASNDLSKKVLSIIDKYAER-----------GLRSLAVARQVVPEK--------TKESPGAPWE---FVGLLPLFDPPRH 491
Cdd:cd02608 458 -STILINGKEQPLDEEMKEAfqnaylelgglGERVLGFCHLYLPDDkfpegfkfDTDEVNFPTEnlcFVGLMSMIDPPRA 536
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 492 DSAETIRRALNLGVNVKMITGDQ----LAIGKETGrrlgmgtnmypssallgthkdanlasIPVeeliekadgFAGVFPE 567
Cdd:cd02608 537 AVPDAVGKCRSAGIKVIMVTGDHpitaKAIAKGVG--------------------------IIV---------FARTSPQ 581
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 568 HKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIGIAVADA-TDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMKNYT 646
Cdd:cd02608 582 QKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIAgSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSI 661

                ....*...
gi 15234666 647 IYAVSITI 654
Cdd:cd02608 662 AYTLTSNI 669
P-type_ATPase_HM cd07550
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
134-663 1.28e-53

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: 197.50  E-value: 1.28e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 134 VLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLkVDQSALTGESLPVTKHPGQEVFSGSTCKQGEIEAVVIA 213
Cdd:cd07550 104 VERDGVEVEVPADEVQPGDTVVVGAGDVIPVDGTVLSGEAL-IDQASLTGESLPVEKREGDLVFASTVVEEGQLVIRAER 182
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 214 TGVHTFFGKAAHLVDSTNQV-GHFQKVLTAIGNFCIC-SIAIGMVIEIIVmypiqrRKYRDGIDNLLVLLIGGIPIAMPT 291
Cdd:cd07550 183 VGRETRAARIAELIEQSPSLkARIQNYAERLADRLVPpTLGLAGLVYALT------GDISRAAAVLLVDFSCGIRLSTPV 256
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 292 VLSVTMAIGSHRlsqqGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDKnlVEVFCKGVEKDQVLLFAAMASRVENQ 371
Cdd:cd07550 257 AVLSALNHAARH----GILVKGGRALELLAKVDTVVFDKTGTLTEGEPEVTA--IITFDGRLSEEDLLYLAASAEEHFPH 330
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 372 dAIDAAMVgmladpKEARAgiREVHFLPFNPVDkrtaltYIDGSG-----NWHRVSKGAP-----EQIlelakasnDLSK 441
Cdd:cd07550 331 -PVARAIV------REAEE--RGIEHPEHEEVE------YIVGHGiastvDGKRIRVGSRhfmeeEEI--------ILIP 387
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 442 KVLSIIDKYAERGLRSLAVARQvvpektkespgapWEFVGLLPLFDPPRHDSAETIRRALNLGV-NVKMITGDQLAIGKE 520
Cdd:cd07550 388 EVDELIEDLHAEGKSLLYVAID-------------GRLIGVIGLSDPLRPEAAEVIARLRALGGkRIIMLTGDHEQRARA 454
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 521 TGRRLGMGTNmypssallgthkdanlasipveeliekadgFAGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKAD 600
Cdd:cd07550 455 LAEQLGIDRY------------------------------HAEALPEDKAEIVEKLQAEGRTVAFVGDGINDSPALSYAD 504
                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15234666 601 IGIAVADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMK-NYTIYAVSITIRIVFGFMLI 663
Cdd:cd07550 505 VGISMRGGTDIARETADVVLLEDDLRGLAEAIELARETMALIKrNIALVVGPNTAVLAGGVFGL 568
ATPase-IB2_Cd TIGR01512
heavy metal-(Cd/Co/Hg/Pb/Zn)-translocating P-type ATPase; This model describes the P-type ...
134-683 2.83e-52

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: 192.54  E-value: 2.83e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   134 VLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLkVDQSALTGESLPVTKHPGQEVFSGSTCKQGEIEAVVIA 213
Cdd:TIGR01512  59 RLQGDSLEEVAVEELKVGDVVVVKPGERVPVDGEVLSGTSS-VDESALTGESVPVEKAPGDEVFAGAINLDGVLTIEVTK 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   214 TGVHTFFGKAAHLV-DSTNQVGHFQKVLTAIG-NFCICSIAIGMVIeIIVMYPIQRRKYRDGIDNLLVLLIGGIPIAMpt 291
Cdd:TIGR01512 138 LPADSTIAKIVNLVeEAQSRKAPTQRFIDRFArYYTPAVLAIALAA-ALVPPLLGAGPFLEWIYRALVLLVVASPCAL-- 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   292 VLSVTMAI--GSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDKnlVEVFcKGVEKDQVL-LFAAMASRV 368
Cdd:TIGR01512 215 VISAPAAYlsAISAAARHGILIKGGAALEALAKIKTVAFDKTGTLTTGKPKVTD--VHPA-DGHSESEVLrLAAAAEQGS 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   369 EN--QDAIDAAMVGMLADP--KEARA----GIREVhflpfnpVDKRTALTyidGSGNWHRVSKGAPEQILElaKASNDLS 440
Cdd:TIGR01512 292 THplARAIVDYARARELAPpvEDVEEvpgeGVRAV-------VDGGEVRI---GNPRSLSEAVGASIAVPE--SAGKTIV 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   441 kkVLSIIDKYaerglrslavarqvvpektkespgapwefVGLLPLFDPPRHDSAETIRRALNLGV-NVKMITGDQLAIGK 519
Cdd:TIGR01512 360 --LVARDGTL-----------------------------LGYIALSDELRPDAAEAIAELKALGIkRLVMLTGDRRAVAE 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   520 ETGRRLGmgtnmypssallgthkdanlasipVEELiekadgFAGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKA 599
Cdd:TIGR01512 409 AVARELG------------------------IDEV------HAELLPEDKLEIVKELREKAGPVAMVGDGINDAPALAAA 458
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   600 DIGIAV-ADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMK-NYTIYAVSITIRIVFGFMLIALIWEFDFSAFMVL 677
Cdd:TIGR01512 459 DVGIAMgASGSDVALETADVVLLNDDLSRLPQAIRLARRTRRIIKqNVVIALGIILVLILLALFGVLPLWLAVLGHEGST 538

                  ....*.
gi 15234666   678 IIAILN 683
Cdd:TIGR01512 539 VLVILN 544
ATPase-IB1_Cu TIGR01511
copper-(or silver)-translocating P-type ATPase; This model describes the P-type ATPase ...
132-663 6.34e-52

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: 191.72  E-value: 6.34e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   132 TKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPlKVDQSALTGESLPVTKHPGQEVFSGSTCKQGEIEAVV 211
Cdd:TIGR01511  94 TLLTKDGSIEEVPVALLQPGDIVKVLPGEKIPVDGTVIEGES-EVDESLVTGESLPVPKKVGDPVIAGTVNGTGSLVVRA 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   212 IATGVHTFFGKAAHLVD----STNQVGHFQKVLTAIgnFCICSIAIGMVIEIIVMYPIQRrkyrdgidNLLVLLIG---G 284
Cdd:TIGR01511 173 TATGEDTTLAQIVRLVRqaqqSKAPIQRLADKVAGY--FVPVVIAIALITFVIWLFALEF--------AVTVLIIAcpcA 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   285 IPIAMPTVLsvtmAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVdkNLVEVFCKGVEKDQVLLFAAM 364
Cdd:TIGR01511 243 LGLATPTVI----AVATGLAAKNGVLIKDGDALERAANIDTVVFDKTGTLTQGKPTV--TDVHVFGDRDRTELLALAAAL 316
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   365 ASRVENqdAIDAAMVGMLadpkearagiREVHFLPFNPVDKRTaltyIDGSGNW-----HRVSKGAPEQILELAKAsndl 439
Cdd:TIGR01511 317 EAGSEH--PLAKAIVSYA----------KEKGITLVTVSDFKA----IPGIGVEgtvegTKIQLGNEKLLGENAIK---- 376
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   440 skkvlsiIDKYAERGLRSLAVARQvvpektkespgapWEFVGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGK 519
Cdd:TIGR01511 377 -------IDGKAGQGSTVVLVAVN-------------GELAGVFALEDQLRPEAKEVIQALKRRGIEPVMLTGDNRKTAK 436
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   520 ETGRRLGMgtnmypssallgthkdanlasipveeliekaDGFAGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKA 599
Cdd:TIGR01511 437 AVAKELGI-------------------------------DVRAEVLPDDKAALIKKLQEKGPVVAMVGDGINDAPALAQA 485
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15234666   600 DIGIAVADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMKN-------YTIYAVSITIRIVFGFMLI 663
Cdd:TIGR01511 486 DVGIAIGAGTDVAIEAADVVLLRNDLNDVATAIDLSRKTLRRIKQnllwafgYNVIAIPIAAGVLYPIGIL 556
E1-E2_ATPase pfam00122
E1-E2 ATPase;
130-307 2.38e-45

E1-E2 ATPase;


Pssm-ID: 425475 [Multi-domain]  Cd Length: 181  Bit Score: 161.20  E-value: 2.38e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   130 PKTKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLkVDQSALTGESLPVTKHPGQEVFSGSTCKQGEIEA 209
Cdd:pfam00122   5 PTATVLRDGTEEEVPADELVPGDIVLLKPGERVPADGRIVEGSAS-VDESLLTGESLPVEKKKGDMVYSGTVVVSGSAKA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   210 VVIATGVHTFFGKAAHLVDSTNQV-GHFQKVLTAIGNFCICsIAIGMVIEIIVMYPIQRRKYRDGIDNLLVLLIGGIPIA 288
Cdd:pfam00122  84 VVTATGEDTELGRIARLVEEAKSKkTPLQRLLDRLGKYFSP-VVLLIALAVFLLWLFVGGPPLRALLRALAVLVAACPCA 162
                         170
                  ....*....|....*....
gi 15234666   289 MPTVLSVTMAIGSHRLSQQ 307
Cdd:pfam00122 163 LPLATPLALAVGARRLAKK 181
P-type_ATPase_Cu-like cd07552
P-type heavy metal-transporting ATPase, similar to Archaeoglobus fulgidus CopB, a Cu(2+) ...
130-662 2.80e-45

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: 173.64  E-value: 2.80e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 130 PKT-KVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLkVDQSALTGESLPVTKHPGQEVFSGSTCKQGEIE 208
Cdd:cd07552 130 PKTaHLVTDGSIEDVPVSELKVGDVVLVRAGEKIPADGTILEGESS-VNESMVTGESKPVEKKPGDEVIGGSVNGNGTLE 208
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 209 AVVIATGVHTFFGKAAHLVDSTNQVGHFQKVLTAIGNFCICSIAIGM-VIEIIVMYPIQrrKYRDGIDNLLVLLIGGIP- 286
Cdd:cd07552 209 VKVTKTGEDSYLSQVMELVAQAQASKSRAENLADKVAGWLFYIALGVgIIAFIIWLILG--DLAFALERAVTVLVIACPh 286
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 287 ---IAMPTVLSVTMAIGSHRlsqqGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVdkNLVEVFCKGVEKDQVLLFAA 363
Cdd:cd07552 287 algLAIPLVVARSTSIAAKN----GLLIRNREALERARDIDVVLFDKTGTLTEGKFGV--TDVITFDEYDEDEILSLAAA 360
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 364 MASRVENQDAIdaamvGMLADPKEAraGIREVHFLPFNPVDKRTaltyIDGSGNWHRVSKGAPEQILELAKASNDlskkv 443
Cdd:cd07552 361 LEAGSEHPLAQ-----AIVSAAKEK--GIRPVEVENFENIPGVG----VEGTVNGKRYQVVSPKYLKELGLKYDE----- 424
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 444 lSIIDKYAERG--LRSLAVARQVVpektkespgapwefvGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGKET 521
Cdd:cd07552 425 -ELVKRLAQQGntVSFLIQDGEVI---------------GAIALGDEIKPESKEAIRALKAQGITPVMLTGDNEEVAQAV 488
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 522 GRRLGMgtnmypssallgthkdanlasipveeliekADGFAGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADI 601
Cdd:cd07552 489 AEELGI------------------------------DEYFAEVLPEDKAKKVKELQAEGKKVAMVGDGVNDAPALAQADV 538
                       490       500       510       520       530       540       550
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 602 GIAVADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMKN-------YTIYAVSITIRIV--FGFML 662
Cdd:cd07552 539 GIAIGAGTDVAIESADVVLVKSDPRDIVDFLELAKATYRKMKQnlwwgagYNVIAIPLAAGVLapIGIIL 608
P-ATPase-V TIGR01657
P-type ATPase of unknown pump specificity (type V); These P-type ATPases form a distinct clade ...
134-675 4.06e-44

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: 173.32  E-value: 4.06e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    134 VLRDGKWSEQEAAILVPGDIVSIKL--GDIIPADARLLEGDPLkVDQSALTGESLPVTKHP------------GQEVFSG 199
Cdd:TIGR01657  233 VIRNGKWVTIASDELVPGDIVSIPRpeEKTMPCDSVLLSGSCI-VNESMLTGESVPVLKFPipdngdddedlfLYETSKK 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    200 STC-------------KQGEIEAVVIATGVHTFFGKAAH-LVDSTNQVGHFQKVLTAIGNFCICSIAIGMVIEIIVMYPI 265
Cdd:TIGR01657  312 HVLfggtkilqirpypGDTGCLAIVVRTGFSTSKGQLVRsILYPKPRVFKFYKDSFKFILFLAVLALIGFIYTIIELIKD 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    266 QRRKYRDGIDNLLVLLIGgIPIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVD--- 342
Cdd:TIGR01657  392 GRPLGKIILRSLDIITIV-VPPALPAELSIGINNSLARLKKKGIFCTSPFRINFAGKIDVCCFDKTGTLTEDGLDLRgvq 470
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    343 -KNLVEVFCKGVEKDQVL----LFAAMAS-----RVENQ---DAIDAAMV---------------------GMLADPKEA 388
Cdd:TIGR01657  471 gLSGNQEFLKIVTEDSSLkpsiTHKALATchsltKLEGKlvgDPLDKKMFeatgwtleeddesaeptsilaVVRTDDPPQ 550
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    389 RAGIreVHFLPFNPVDKRTA-LTYIDGSGNWHRVSKGAPEQILELAKaSNDLSKKVLSIIDKYAERGLRSLAVARQVVPE 467
Cdd:TIGR01657  551 ELSI--IRRFQFSSALQRMSvIVSTNDERSPDAFVKGAPETIQSLCS-PETVPSDYQEVLKSYTREGYRVLALAYKELPK 627
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    468 KT--------KESPGAPWEFVGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGKETGRRLGMGTN---MYPSSA 536
Cdd:TIGR01657  628 LTlqkaqdlsRDAVESNLTFLGFIVFENPLKPDTKEVIKELKRASIRTVMITGDNPLTAVHVARECGIVNPsntLILAEA 707
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    537 LLGTHKDANL---------------ASIP-----------------------------------VEELIEKADGFAGVFP 566
Cdd:TIGR01657  708 EPPESGKPNQikfevidsipfastqVEIPyplgqdsvedllasryhlamsgkafavlqahspelLLRLLSHTTVFARMAP 787
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666    567 EHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIGIAV--ADATDAARGASDIVLTEPGLSVII---SAVLTSRAIFQR 641
Cdd:TIGR01657  788 DQKETLVELLQKLDYTVGMCGDGANDCGALKQADVGISLseAEASVAAPFTSKLASISCVPNVIRegrCALVTSFQMFKY 867
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 15234666    642 MKNYT-IYAVSITIRIVFG-------FMLIALIWEFDFSAFM 675
Cdd:TIGR01657  868 MALYSlIQFYSVSILYLIGsnlgdgqFLTIDLLLIFPVALLM 909
P-type_ATPase_HM_ZosA_PfeT-like cd07551
P-type heavy metal-transporting ATPase, similar to Bacillus subtilis ZosA/PfeT which ...
132-665 1.18e-43

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: 168.20  E-value: 1.18e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 132 TKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPlKVDQSALTGESLPVTKHPGQEVFSGSTCKQGEIEAVV 211
Cdd:cd07551 115 RRIQRDGEIEEVPVEELQIGDRVQVRPGERVPADGVILSGSS-SIDEASITGESIPVEKTPGDEVFAGTINGSGALTVRV 193
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 212 IATGVHTFFGKAAHLVDSTNQvgHFQKVLTAIGNF-CICSIAIGMVIE--IIVMYPIQRRKYRDGIDNLLVLLIGGIPIA 288
Cdd:cd07551 194 TKLSSDTVFAKIVQLVEEAQS--EKSPTQSFIERFeRIYVKGVLLAVLllLLLPPFLLGWTWADSFYRAMVFLVVASPCA 271
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 289 -----MPTVLSvtmAIGshRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVdknlVEV-FCKGVEKDQVLLFA 362
Cdd:cd07551 272 lvastPPATLS---AIA--NAARQGVLFKGGVHLENLGSVKAIAFDKTGTLTEGKPRV----TDViPAEGVDEEELLQVA 342
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 363 AMASRVENQdAIDAAMVGMLADPKEARAGIREVHFLPfnpvdkrtaltyidGSGNWHRVSkgapEQILELAKAS----ND 438
Cdd:cd07551 343 AAAESQSEH-PLAQAIVRYAEERGIPRLPAIEVEAVT--------------GKGVTATVD----GQTYRIGKPGffgeVG 403
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 439 LSKKVLSIIDKYAERGLRSLAVARQVVpektkespgapweFVGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIG 518
Cdd:cd07551 404 IPSEAAALAAELESEGKTVVYVARDDQ-------------VVGLIALMDTPRPEAKEAIAALRLGGIKTIMLTGDNERTA 470
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 519 KETGRRLGMgtnmypssallgthkdanlasipveeliekADGFAGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKK 598
Cdd:cd07551 471 EAVAKELGI------------------------------DEVVANLLPEDKVAIIRELQQEYGTVAMVGDGINDAPALAN 520
                       490       500       510       520       530       540       550
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15234666 599 ADIGIAVADATDAARGASDIVLTEPGLSVIISAVLTSRA----IFQrmkNYTIYAVSITIRIV---FGFMLIAL 665
Cdd:cd07551 521 ADVGIAMGAGTDVALETADVVLMKDDLSKLPYAIRLSRKmrriIKQ---NLIFALAVIALLIVanlFGLLNLPL 591
P-type_ATPase_cation cd07542
P-type cation-transporting ATPases, similar to human ATPase type 13A2 (ATP13A2) protein and ...
133-647 5.72e-42

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: 165.11  E-value: 5.72e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 133 KVLRDGKWSEQEAAILVPGDIVSIKL-GDIIPADARLLEGDPLkVDQSALTGESLPVTKHPGQE---------------- 195
Cdd:cd07542  90 RVIRDGEWQTISSSELVPGDILVIPDnGTLLPCDAILLSGSCI-VNESMLTGESVPVTKTPLPDesndslwsiysiedhs 168
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 196 ---VFSGSTC------KQGEIEAVVIATGVHTFFGKaahLVDS-----------TNQVGHFQKVLTAIGnfcicsiAIGM 255
Cdd:cd07542 169 khtLFCGTKViqtrayEGKPVLAVVVRTGFNTTKGQ---LVRSilypkpvdfkfYRDSMKFILFLAIIA-------LIGF 238
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 256 VIEIIVMYPIQRRKYRDGIDNLLVLLIGgIPIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEeMAGM-DVLCSDKTGTL 334
Cdd:cd07542 239 IYTLIILILNGESLGEIIIRALDIITIV-VPPALPAALTVGIIYAQSRLKKKGIFCISPQRIN-ICGKiNLVCFDKTGTL 316
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 335 TLNKLSV---------DKNLVEVFCKGVEKDQVL----LFAAMA-----SRVENQ---DAIDAAMVgmladpkEARAGIR 393
Cdd:cd07542 317 TEDGLDLwgvrpvsgnNFGDLEVFSLDLDLDSSLpngpLLRAMAtchslTLIDGElvgDPLDLKMF-------EFTGWSL 389
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 394 EV-HFLPFNPVDKR-TALTYIDGSGNWHRVSKGAPEQILELAKASNdLSKKVLSIIDKYAERGLRSLAVARQVVPEKTKE 471
Cdd:cd07542 390 EIlRQFPFSSALQRmSVIVKTPGDDSMMAFTKGAPEMIASLCKPET-VPSNFQEVLNEYTKQGFRVIALAYKALESKTWL 468
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 472 SPGAP-------WEFVGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGKETGRRLGMgtnMYPS-SALLGTH-- 541
Cdd:cd07542 469 LQKLSreevesdLEFLGLIVMENRLKPETAPVINELNRANIRTVMVTGDNLLTAISVARECGM---ISPSkKVILIEAvk 545
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 542 -KDANLASIPVEELIeKADGFAGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIGIAVADAtdAARGASDIVL 620
Cdd:cd07542 546 pEDDDSASLTWTLLL-KGTVFARMSPDQKSELVEELQKLDYTVGMCGDGANDCGALKAADVGISLSEA--EASVAAPFTS 622
                       570       580       590
                ....*....|....*....|....*....|....
gi 15234666 621 TEPGLS----VII---SAVLTSRAIFQRMKNYTI 647
Cdd:cd07542 623 KVPDIScvptVIKegrAALVTSFSCFKYMALYSL 656
P-type_ATPase_Cd-like cd07545
P-type heavy metal-transporting ATPase, similar to Staphylococcus aureus plasmid pI258 CadA, a ...
130-684 2.99e-41

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: 161.05  E-value: 2.99e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 130 PKTK-VLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLkVDQSALTGESLPVTKHPGQEVFSGSTCKQGEIE 208
Cdd:cd07545  95 PKTAlVRRDGQEREVPVAEVAVGDRMIVRPGERIAMDGIIVRGESS-VNQAAITGESLPVEKGVGDEVFAGTLNGEGALE 173
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 209 AVVIATGVHTFFGKAAHLVDSTNQ--------VGHFQKVLTAIgnfcICSIAIGMVIEIIVMYPIQrrkYRDGIDNLLVL 280
Cdd:cd07545 174 VRVTKPAEDSTIARIIHLVEEAQAeraptqafVDRFARYYTPV----VMAIAALVAIVPPLFFGGA---WFTWIYRGLAL 246
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 281 LIGGIPIAM--PTVLSVTMAIGShrLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDKnlVEVFCKGVEKDQV 358
Cdd:cd07545 247 LVVACPCALviSTPVSIVSAIGN--AARKGVLIKGGVYLEELGRLKTVAFDKTGTLTKGKPVVTD--VVVLGGQTEKELL 322
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 359 LLFAAMASRVENQDAidAAMVGmladpKEARAGIrevhflPFNPVDKRTALT------YIDGS----GNWHRVSKGAPEQ 428
Cdd:cd07545 323 AIAAALEYRSEHPLA--SAIVK-----KAEQRGL------TLSAVEEFTALTgrgvrgVVNGTtyyiGSPRLFEELNLSE 389
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 429 ILELA---KASNDLSKKVLSIIDkyAERGLRSLAVARQVVPEktkespgapwefvgllplfdpprhdSAETIRRALNLGV 505
Cdd:cd07545 390 SPALEaklDALQNQGKTVMILGD--GERILGVIAVADQVRPS-------------------------SRNAIAALHQLGI 442
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 506 -NVKMITGDQLAIGKETGRRLGMgtnmypssallgthkdanlasipveeliekADGFAGVFPEHKYEIVKKLQERKHIVG 584
Cdd:cd07545 443 kQTVMLTGDNPQTAQAIAAQVGV------------------------------SDIRAELLPQDKLDAIEALQAEGGRVA 492
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 585 MTGDGVNDAPALKKADIGIAVADA-TDAARGASDIVLTEPGLSVIISAVLTSRaifqrmKNYTIYAVSITIRIvfGFMLI 663
Cdd:cd07545 493 MVGDGVNDAPALAAADVGIAMGAAgTDTALETADIALMGDDLRKLPFAVRLSR------KTLAIIKQNIAFAL--GIKLI 564
                       570       580
                ....*....|....*....|.
gi 15234666 664 ALIweFDFSAFMVLIIAILND 684
Cdd:cd07545 565 ALL--LVIPGWLTLWMAVFAD 583
P-type_ATPase_HM cd07544
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
134-664 5.50e-41

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: 160.18  E-value: 5.50e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 134 VLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLkVDQSALTGESLPVTKHPGQEVFSGSTCKQGEIEAVVIA 213
Cdd:cd07544 114 RLVGGQLEEVPVEEVTVGDRLLVRPGEVVPVDGEVVSGTAT-LDESSLTGESKPVSKRPGDRVMSGAVNGDSALTMVATK 192
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 214 TGVHTFFGKAAHLVDST-NQVGHFQKVLTAIGN-FCICSIAIGMVIEIIVMYPIQrrkyrdgidnLLVLLIGGIPIamPT 291
Cdd:cd07544 193 LAADSQYAGIVRLVKEAqANPAPFVRLADRYAVpFTLLALAIAGVAWAVSGDPVR----------FAAVLVVATPC--PL 260
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 292 VLSVTMAI--GSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDKNLVEvfcKGVEKDQVLLFAAMASRvE 369
Cdd:cd07544 261 ILAAPVAIvsGMSRSSRRGILVKDGGVLEKLARAKTVAFDKTGTLTYGQPKVVDVVPA---PGVDADEVLRLAASVEQ-Y 336
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 370 NQDAIDAAMVgmladpKEARAgiREVHFLPFNPVDKRTALTyIDGSGNWHRVSKGAPEQILELAKASNDLSKKVLSIIDK 449
Cdd:cd07544 337 SSHVLARAIV------AAARE--RELQLSAVTELTEVPGAG-VTGTVDGHEVKVGKLKFVLARGAWAPDIRNRPLGGTAV 407
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 450 YAerglrslavarqvvpektkespGAPWEFVGLLPLFDPPRHDSAETIRRALNLGVN-VKMITGDQLAIGKETGRRLGMg 528
Cdd:cd07544 408 YV----------------------SVDGKYAGAITLRDEVRPEAKETLAHLRKAGVErLVMLTGDRRSVAEYIASEVGI- 464
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 529 tnmypssallgthkdanlasipveeliekADGFAGVFPEHKYEIVKKLQERkHIVGMTGDGVNDAPALKKADIGIAV-AD 607
Cdd:cd07544 465 -----------------------------DEVRAELLPEDKLAAVKEAPKA-GPTIMVGDGVNDAPALAAADVGIAMgAR 514
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15234666 608 ATDAARGASDIVLTEPGLSVIISAVltsrAIFQRMKNYTIYAVSITIRIVFGFMLIA 664
Cdd:cd07544 515 GSTAASEAADVVILVDDLDRVVDAV----AIARRTRRIALQSVLIGMALSIIGMLIA 567
P-type_ATPase_Pb_Zn_Cd2-like cd07546
P-type heavy metal-transporting ATPase, similar to Escherichia coli ZntA which is selective ...
130-637 2.69e-39

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: 154.87  E-value: 2.69e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 130 PKT-KVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPlKVDQSALTGESLPVTKHPGQEVFSGSTCKQGEIE 208
Cdd:cd07546  98 PETaLREENGERREVPADSLRPGDVIEVAPGGRLPADGELLSGFA-SFDESALTGESIPVEKAAGDKVFAGSINVDGVLR 176
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 209 AVVIATGVHTFFGKAAHLVDSTNQ--------VGHFQKVLTAIgnFCICSIAIGMVIEIIVMYPIQRRKYRDgidnlLVL 280
Cdd:cd07546 177 IRVTSAPGDNAIDRILHLIEEAEErrapierfIDRFSRWYTPA--IMAVALLVIVVPPLLFGADWQTWIYRG-----LAL 249
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 281 LIGGIPIAMptVLSVTMAIGSHrLS---QQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVdknlVEVFCKGVEKDQ 357
Cdd:cd07546 250 LLIGCPCAL--VISTPAAITSG-LAaaaRRGALIKGGAALEQLGRVTTVAFDKTGTLTRGKPVV----TDVVPLTGISEA 322
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 358 VLLfaAMASRVENQDAidaamvGMLADPKEARAGIREvhfLPFNPVDKRTALT--YIDGSGNWHRVSKGAPEQilelakA 435
Cdd:cd07546 323 ELL--ALAAAVEMGSS------HPLAQAIVARAQAAG---LTIPPAEEARALVgrGIEGQVDGERVLIGAPKF------A 385
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 436 SNDLSKKVLSIIDKYAERGLRSLAVARQVVPektkespgapwefVGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQL 515
Cdd:cd07546 386 ADRGTLEVQGRIAALEQAGKTVVVVLANGRV-------------LGLIALRDELRPDAAEAVAELNALGIKALMLTGDNP 452
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 516 AIGKETGRRLGMGTNmypssallgthkdanlasipveeliekadgfAGVFPEHKYEIVKKLQERKHiVGMTGDGVNDAPA 595
Cdd:cd07546 453 RAAAAIAAELGLDFR-------------------------------AGLLPEDKVKAVRELAQHGP-VAMVGDGINDAPA 500
                       490       500       510       520
                ....*....|....*....|....*....|....*....|..
gi 15234666 596 LKKADIGIAVADATDAARGASDIVLTEPGLSVIISAVLTSRA 637
Cdd:cd07546 501 MKAASIGIAMGSGTDVALETADAALTHNRLGGVAAMIELSRA 542
P-type_ATPase_K cd02078
potassium-transporting ATPase ATP-binding subunit, KdpB, a subunit of the prokaryotic ...
133-619 2.65e-37

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: 149.72  E-value: 2.65e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 133 KVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLkVDQSALTGESLPVTKHPGQEVFS---GSTCKQGEIEA 209
Cdd:cd02078  99 RLRNDGKIEKVPATDLKKGDIVLVEAGDIIPADGEVIEGVAS-VDESAITGESAPVIRESGGDRSSvtgGTKVLSDRIKV 177
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 210 VVIATGVHTFFGKAAHLVDSTNQvghfQKVLTAIG-NFCICSIAIGMVIEIIVMYPIQrrKYRDG---IDNLLVLLIGGI 285
Cdd:cd02078 178 RITANPGETFLDRMIALVEGASR----QKTPNEIAlTILLVGLTLIFLIVVATLPPFA--EYSGApvsVTVLVALLVCLI 251
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 286 PIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTL-NKLSVDknLVEVfcKGVEKDQVLLFAAM 364
Cdd:cd02078 252 PTTIGGLLSAIGIAGMDRLLRFNVIAKSGRAVEAAGDVDTLLLDKTGTITLgNRQATE--FIPV--GGVDEKELADAAQL 327
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 365 ASRV----ENQDAIDAA--MVGMLADPkearaGIREVHFLPFNPvdkRTALTYIDGSGNwHRVSKGAPEQILELAKASN- 437
Cdd:cd02078 328 ASLAdetpEGRSIVILAkqLGGTERDL-----DLSGAEFIPFSA---ETRMSGVDLPDG-TEIRKGAVDAIRKYVRSLGg 398
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 438 DLSKKVLSIIDKYAERGLRSLAVARQVvpektkespgapwEFVGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQ--- 514
Cdd:cd02078 399 SIPEELEAIVEEISKQGGTPLVVAEDD-------------RVLGVIYLKDIIKPGIKERFAELRKMGIKTVMITGDNplt 465
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 515 -LAIGKETGrrlgmgtnmypssallgthkdanlasipVEELIEKADgfagvfPEHKYEIVKKLQERKHIVGMTGDGVNDA 593
Cdd:cd02078 466 aAAIAAEAG----------------------------VDDFLAEAK------PEDKLELIRKEQAKGKLVAMTGDGTNDA 511
                       490       500
                ....*....|....*....|....*.
gi 15234666 594 PALKKADIGIAVADATDAARGASDIV 619
Cdd:cd02078 512 PALAQADVGVAMNSGTQAAKEAGNMV 537
P-type_ATPase_cation cd02082
P-type cation-transporting ATPases, similar to human ATPase type 13A1-A4 (ATP13A1-A4) proteins ...
139-719 4.44e-36

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: 146.97  E-value: 4.44e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 139 KWSEQEAAILVPGDIVSIKL-GDIIPADARLLEGDpLKVDQSALTGESLPVTK-----------------HPGQEVFSGS 200
Cdd:cd02082  96 QEITIASNMIVPGDIVLIKRrEVTLPCDCVLLEGS-CIVTEAMLTGESVPIGKcqiptdshddvlfkyesSKSHTLFQGT 174
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 201 TCKQ-----GEI-EAVVIATGVHTFFGKAAHLV---DSTNQVGHFQKVLtaignFCICSIA---IGMVIEIIVMYPIQRR 268
Cdd:cd02082 175 QVMQiippeDDIlKAIVVRTGFGTSKGQLIRAIlypKPFNKKFQQQAVK-----FTLLLATlalIGFLYTLIRLLDIELP 249
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 269 KYRDGIDNLLVLLIGgIPIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSV------- 341
Cdd:cd02082 250 PLFIAFEFLDILTYS-VPPGLPMLIAITNFVGLKRLKKNQILCQDPNRISQAGRIQTLCFDKTGTLTEDKLDLigyqlkg 328
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 342 -DKNL--VEVFCKGVEKDQVLLFAAMAS--RVENQ---DAIDAAM---VGMLADPKE---------ARAGIREVHFLPFN 401
Cdd:cd02082 329 qNQTFdpIQCQDPNNISIEHKLFAICHSltKINGKllgDPLDVKMaeaSTWDLDYDHeakqhysksGTKRFYIIQVFQFH 408
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 402 PVDKR-TALTYIDGSGNWHR----VSKGAPEQILELAKASNDLSKKVLSIIDKyaeRGLRSLAVARQVVPEKT------- 469
Cdd:cd02082 409 SALQRmSVVAKEVDMITKDFkhyaFIKGAPEKIQSLFSHVPSDEKAQLSTLIN---EGYRVLALGYKELPQSEidafldl 485
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 470 -KESPGAPWEFVGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGKETGRRLGMgtnMYPSSALLGTH----KDA 544
Cdd:cd02082 486 sREAQEANVQFLGFIIYKNNLKPDTQAVIKEFKEACYRIVMITGDNPLTALKVAQELEI---INRKNPTIIIHllipEIQ 562
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 545 NLASIPVEeLIEKADGFAGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIGIAVADATdaARGASDIVLTEPG 624
Cdd:cd02082 563 KDNSTQWI-LIIHTNVFARTAPEQKQTIIRLLKESDYIVCMCGDGANDCGALKEADVGISLAEAD--ASFASPFTSKSTS 639
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 625 LSVIISAVLTSRAI----FQRMKNYTIYAvsitIRIVFGFMLIALIWEfDFSAFMVLIIAILNDGTIMTISKdrvKPSPT 700
Cdd:cd02082 640 ISCVKRVILEGRVNlstsVEIFKGYALVA----LIRYLSFLTLYYFYS-SYSSSGQMDWQLLAAGYFLVYLR---LGCNT 711
                       650       660
                ....*....|....*....|....
gi 15234666 701 PDSWKLKE-----IFATGVVLGGY 719
Cdd:cd02082 712 PLKKLEKDdnlfsIYNVTSVLFGF 735
P-type_ATPase-Cd_Zn_Co_like cd07548
P-type heavy metal-transporting ATPase, similar to Bacillus subtilis CadA which appears to ...
134-683 8.93e-34

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: 138.14  E-value: 8.93e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 134 VLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLkVDQSALTGESLPVTKHPGQEVFSGSTCKQGEIEAVVIA 213
Cdd:cd07548 113 LKRNNELKDVKPEEVQIGDIIVVKPGEKIPLDGVVLKGESF-LDTSALTGESVPVEVKEGSSVLAGFINLNGVLEIKVTK 191
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 214 TGVHTFFGKAAHLV-DSTNQVGHFQKVLTAIGNF-----CICSIAIGMVIEIIVMYPIqrrkYRDGIDNLLVLLIGGIPI 287
Cdd:cd07548 192 PFKDSAVAKILELVeNASARKAPTEKFITKFARYytpivVFLALLLAVIPPLFSPDGS----FSDWIYRALVFLVISCPC 267
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 288 AMptVLSVTMA--IGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDKNLVEvfcKGVEKDQVLLFAAMA 365
Cdd:cd07548 268 AL--VISIPLGyfGGIGAASRKGILIKGSNYLEALSQVKTVVFDKTGTLTKGVFKVTEIVPA---PGFSKEELLKLAALA 342
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 366 SRVENQ---DAIDAAMVGMLaDPKEARA-------GIREVhflpfnpVDKRTALtyidgSGNwhrvskgapEQILELAKA 435
Cdd:cd07548 343 ESNSNHpiaRSIQKAYGKMI-DPSEIEDyeeiaghGIRAV-------VDGKEIL-----VGN---------EKLMEKFNI 400
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 436 SNDLSKKVLSIIdkYAERGLRslavarqvvpektkespgapweFVGLLPLFDPPRHDSAETIRRALNLGV-NVKMITGDQ 514
Cdd:cd07548 401 EHDEDEIEGTIV--HVALDGK----------------------YVGYIVISDEIKEDAKEAIKGLKELGIkNLVMLTGDR 456
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 515 LAIGKETGRRLGMGtnmypssallgthkdanlasipveeliekaDGFAGVFPEHKYEIVKKLQER-KHIVGMTGDGVNDA 593
Cdd:cd07548 457 KSVAEKVAKKLGID------------------------------EVYAELLPEDKVEKVEELKAEsKGKVAFVGDGINDA 506
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 594 PALKKADIGIAV-ADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSI-TIRIVFGFMLIALIWEFDF 671
Cdd:cd07548 507 PVLARADVGIAMgGLGSDAAIEAADVVLMNDEPSKVAEAIKIARKTRRIVWQNIILALGVkAIVLILGALGLATMWEAVF 586
                       570
                ....*....|..
gi 15234666 672 SAFMVLIIAILN 683
Cdd:cd07548 587 ADVGVALLAILN 598
P-type_ATPase_FixI-like cd02092
Rhizobium meliloti FixI and related proteins; belongs to P-type heavy metal-transporting ...
132-654 1.80e-33

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: 137.49  E-value: 1.80e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 132 TKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLkVDQSALTGESLPVTKHPGQEVFSGSTCKQGEIEAVV 211
Cdd:cd02092 129 QRLQADGSREYVPVAEIRPGDRVLVAAGERIPVDGTVVSGTSE-LDRSLLTGESAPVTVAPGDLVQAGAMNLSGPLRLRA 207
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 212 IATGVHTFFGKAAHLVDSTNQ------------------VGHFQKVLTAIGnfcicSIAIGMVIeiivmypiqrrkyRDG 273
Cdd:cd02092 208 TAAGDDTLLAEIARLMEAAEQgrsryvrladraarlyapVVHLLALLTFVG-----WVAAGGDW-------------RHA 269
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 274 IDNLLVLLIGGIP----IAMPTVlsVTMAIGshRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSvdknLVEVf 349
Cdd:cd02092 270 LLIAVAVLIITCPcalgLAVPAV--QVVASG--RLFRRGVLVKDGTALERLAEVDTVVFDKTGTLTLGSPR----LVGA- 340
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 350 cKGVEKDQVLLFAAMAsRVENQDAIDAamvgmLADPKEARA----GIREVHflPFNPVDKRTALTYIDGSGNWHRVSKGA 425
Cdd:cd02092 341 -HAISADLLALAAALA-QASRHPLSRA-----LAAAAGARPveldDAREVP--GRGVEGRIDGARVRLGRPAWLGASAGV 411
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 426 PEQilelakasndlSKKVLSIIDKYAerglrslavarqvvpektkespgapwefvGLLPLFDPPRHDSAETIRRALNLGV 505
Cdd:cd02092 412 STA-----------SELALSKGGEEA-----------------------------ARFPFEDRPRPDAREAISALRALGL 451
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 506 NVKMITGDQLAIGKETGRRLGMgtnmypssallgthkdanlasipveeliekADGFAGVFPEHKYEIVKKLQERKHIVGM 585
Cdd:cd02092 452 SVEILSGDREPAVRALARALGI------------------------------EDWRAGLTPAEKVARIEELKAQGRRVLM 501
                       490       500       510       520       530       540       550
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15234666 586 TGDGVNDAPALKKADIGIAVADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMKN-------YTIYAVSITI 654
Cdd:cd02092 502 VGDGLNDAPALAAAHVSMAPASAVDASRSAADIVFLGDSLAPVPEAIEIARRARRLIRQnfalaigYNVIAVPLAI 577
kdpB TIGR01497
K+-transporting ATPase, B subunit; This model describes the P-type ATPase subunit of the ...
133-619 1.72e-30

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: 128.85  E-value: 1.72e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   133 KVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPlKVDQSALTGESLPVTKHPGQEVFS---GSTCKQGEIEA 209
Cdd:TIGR01497 109 LLRDDGAIDKVPADQLKKGDIVLVEAGDVIPCDGEVIEGVA-SVDESAITGESAPVIKESGGDFASvtgGTRILSDWLVV 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   210 VVIATGVHTFFGKAAHLVDSTNQvghfQKVLTAIG-NFCICSIAIGMVIEIIVMYPIQrrKYRD---GIDNLLVLLIGGI 285
Cdd:TIGR01497 188 ECTANPGETFLDRMIALVEGAQR----RKTPNEIAlTILLIALTLVFLLVTATLWPFA--AYGGnaiSVTVLVALLVCLI 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   286 PIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTL-NKLSVDKnlveVFCKGVEKDQVLLFAAM 364
Cdd:TIGR01497 262 PTTIGGLLSAIGIAGMDRVLGFNVIATSGRAVEACGDVDTLLLDKTGTITLgNRLASEF----IPAQGVDEKTLADAAQL 337
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   365 ASRVEnqDAIDAAMVGMLADpkeaRAGIRE-------VHFLPFnpvdkrTALTYIDGSG--NWHRVSKGAPEQILELAKA 435
Cdd:TIGR01497 338 ASLAD--DTPEGKSIVILAK----QLGIREddvqslhATFVEF------TAQTRMSGINldNGRMIRKGAVDAIKRHVEA 405
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   436 SND-LSKKVLSIIDKYAERGLRSLAVARQVvpektkespgapwEFVGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQ 514
Cdd:TIGR01497 406 NGGhIPTDLDQAVDQVARQGGTPLVVCEDN-------------RIYGVIYLKDIVKGGIKERFAQLRKMGIKTIMITGDN 472
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   515 ----LAIGKETGrrlgmgtnmypssallgthkdanlasipveeliekADGF-AGVFPEHKYEIVKKLQERKHIVGMTGDG 589
Cdd:TIGR01497 473 rltaAAIAAEAG-----------------------------------VDDFiAEATPEDKIALIRQEQAEGKLVAMTGDG 517
                         490       500       510
                  ....*....|....*....|....*....|
gi 15234666   590 VNDAPALKKADIGIAVADATDAARGASDIV 619
Cdd:TIGR01497 518 TNDAPALAQADVGVAMNSGTQAAKEAANMV 547
zntA PRK11033
zinc/cadmium/mercury/lead-transporting ATPase; Provisional
134-637 1.91e-29

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


Pssm-ID: 236827 [Multi-domain]  Cd Length: 741  Bit Score: 125.88  E-value: 1.91e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  134 VLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLegDPL-KVDQSALTGESLPVTKHPGQEVFSGSTCKQGEIEAVVI 212
Cdd:PRK11033 247 RLRDGEREEVAIADLRPGDVIEVAAGGRLPADGKLL--SPFaSFDESALTGESIPVERATGEKVPAGATSVDRLVTLEVL 324
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  213 ATGVHTFFGKAAHLVDSTNQ--------VGHFQKVLT-AIgnfcicsiaigMVIEIIVMY--------PIQRRKYRdgid 275
Cdd:PRK11033 325 SEPGASAIDRILHLIEEAEErrapierfIDRFSRIYTpAI-----------MLVALLVILvppllfaaPWQEWIYR---- 389
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  276 NLLVLLIgGIPIAMptVLSVTMAIGS--HRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDKnlVEVFcKGV 353
Cdd:PRK11033 390 GLTLLLI-GCPCAL--VISTPAAITSglAAAARRGALIKGGAALEQLGRVTTVAFDKTGTLTEGKPQVTD--IHPA-TGI 463
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  354 EKDQVLLFAAmasrvenqdAIDAAMVGMLADPKEARAGIREVhFLPfnPVDKRTALTyidGSG-----NWHRVSKGAPEQ 428
Cdd:PRK11033 464 SESELLALAA---------AVEQGSTHPLAQAIVREAQVRGL-AIP--EAESQRALA---GSGiegqvNGERVLICAPGK 528
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  429 ILELakaSNDLSKKVLSIidkyaERGLRSLAVARQvvpektkespgaPWEFVGLLPLFDPPRHDSAETIRRALNLGVNVK 508
Cdd:PRK11033 529 LPPL---ADAFAGQINEL-----ESAGKTVVLVLR------------NDDVLGLIALQDTLRADARQAISELKALGIKGV 588
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  509 MITGDQlaigketgrrlgmgtnmyPSSAllgthkdanlASIPVEELIekaDGFAGVFPEHKYEIVKKLQErKHIVGMTGD 588
Cdd:PRK11033 589 MLTGDN------------------PRAA----------AAIAGELGI---DFRAGLLPEDKVKAVTELNQ-HAPLAMVGD 636
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 15234666  589 GVNDAPALKKADIGIAVADATDAARGASDIVLTEPGLSVIISAVLTSRA 637
Cdd:PRK11033 637 GINDAPAMKAASIGIAMGSGTDVALETADAALTHNRLRGLAQMIELSRA 685
copA PRK10671
copper-exporting P-type ATPase CopA;
150-643 4.50e-29

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 124.85  E-value: 4.50e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  150 PGDIVSIKLGDIIPADARLLEGDPLkVDQSALTGESLPVTKHPGQEVFSGSTCKQGEIEAVVIATGVHTFFGKAAHLV-- 227
Cdd:PRK10671 343 PGMLLRLTTGDRVPVDGEITQGEAW-LDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVrq 421
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  228 --DSTNQVGHFQKVLTAIgnFCICSIAIGMVIEIIVMY--PIQRRKYRdgidnlLVLLIGGIPIAMPTVLSVT--MAI-- 299
Cdd:PRK10671 422 aqSSKPEIGQLADKISAV--FVPVVVVIALVSAAIWYFfgPAPQIVYT------LVIATTVLIIACPCALGLAtpMSIis 493
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  300 GSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVdknlVEVFC-KGVEKDQVLLFAAMASRVENQDAidaam 378
Cdd:PRK10671 494 GVGRAAEFGVLVRDADALQRASTLDTLVFDKTGTLTEGKPQV----VAVKTfNGVDEAQALRLAAALEQGSSHPL----- 564
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  379 vgmladpkeARAGIREVHFLPFNPVDK-RT-ALTYIDGSGNWHRVSKGAPEQILELAKASNDLSkkvlSIIDKYAERGLR 456
Cdd:PRK10671 565 ---------ARAILDKAGDMTLPQVNGfRTlRGLGVSGEAEGHALLLGNQALLNEQQVDTKALE----AEITAQASQGAT 631
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  457 SLAVArqvvpektkespgAPWEFVGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQL----AIGKETGrrlgmgtnmy 532
Cdd:PRK10671 632 PVLLA-------------VDGKAAALLAIRDPLRSDSVAALQRLHKAGYRLVMLTGDNPttanAIAKEAG---------- 688
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  533 pssallgthkdanlasipVEELIekadgfAGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIGIAVADATDAA 612
Cdd:PRK10671 689 ------------------IDEVI------AGVLPDGKAEAIKRLQSQGRQVAMVGDGINDAPALAQADVGIAMGGGSDVA 744
                        490       500       510
                 ....*....|....*....|....*....|.
gi 15234666  613 RGASDIVLTEPGLSVIISAVLTSRAIFQRMK 643
Cdd:PRK10671 745 IETAAITLMRHSLMGVADALAISRATLRNMK 775
PRK14010 PRK14010
K(+)-transporting ATPase subunit B;
133-661 8.85e-29

K(+)-transporting ATPase subunit B;


Pssm-ID: 184448 [Multi-domain]  Cd Length: 673  Bit Score: 123.27  E-value: 8.85e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  133 KVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGdPLKVDQSALTGESLPVTKHPGQE---VFSGSTCKQGEIEA 209
Cdd:PRK14010 108 RIKQDGSYEMIDASDLKKGHIVRVATGEQIPNDGKVIKG-LATVDESAITGESAPVIKESGGDfdnVIGGTSVASDWLEV 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  210 VVIATGVHTFFGKAAHLVDSTNQvghfQKVLTAIGNFCIC-SIAIGMVIEIIVMYPIQR-RKYRDGIDNLLVLLIGGIPI 287
Cdd:PRK14010 187 EITSEPGHSFLDKMIGLVEGATR----KKTPNEIALFTLLmTLTIIFLVVILTMYPLAKfLNFNLSIAMLIALAVCLIPT 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  288 AMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTL-NKLSVDknLVEVFCKGVEKdqvLLFAAMAS 366
Cdd:PRK14010 263 TIGGLLSAIGIAGMDRVTQFNILAKSGRSVETCGDVNVLILDKTGTITYgNRMADA--FIPVKSSSFER---LVKAAYES 337
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  367 RVENqDAIDAAMVGMLADPKEARAGIREVHFLPFnpvdkrTALTYIDGSGNWHR-VSKGAPEQILELAK-ASNDLSKKVL 444
Cdd:PRK14010 338 SIAD-DTPEGRSIVKLAYKQHIDLPQEVGEYIPF------TAETRMSGVKFTTReVYKGAPNSMVKRVKeAGGHIPVDLD 410
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  445 SIIDKYAERGLRSLAVARQVVpektkespgapweFVGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGKETGRR 524
Cdd:PRK14010 411 ALVKGVSKKGGTPLVVLEDNE-------------ILGVIYLKDVIKDGLVERFRELREMGIETVMCTGDNELTAATIAKE 477
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666  525 LGmgtnmypssallgthkdanlasipVEELIEKADgfagvfPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIGIA 604
Cdd:PRK14010 478 AG------------------------VDRFVAECK------PEDKINVIREEQAKGHIVAMTGDGTNDAPALAEANVGLA 527
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15234666  605 VADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITIRIVFGFM 661
Cdd:PRK14010 528 MNSGTMSAKEAANLIDLDSNPTKLMEVVLIGKQLLMTRGSLTTFSIANDIAKYFAIL 584
P-type_ATPase_cation cd07543
P-type cation-transporting ATPases, similar to human cation-transporting ATPase type 13A1 ...
134-612 3.85e-28

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: 122.11  E-value: 3.85e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 134 VLRDGKWSEQEAAILVPGDIVSI---KLGDIIPADARLLEGdPLKVDQSALTGESLPVTKHP------------------ 192
Cdd:cd07543  90 VYRDGKWVPISSDELLPGDLVSIgrsAEDNLVPCDLLLLRG-SCIVNEAMLTGESVPLMKEPiedrdpedvldddgddkl 168
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 193 -----GQEV-------FSGSTCKQGEIEAVVIATGVHTFFGKAAH-LVDSTNQVghfqkvlTAIGNFCICSIAIGMVIEI 259
Cdd:cd07543 169 hvlfgGTKVvqhtppgKGGLKPPDGGCLAYVLRTGFETSQGKLLRtILFSTERV-------TANNLETFIFILFLLVFAI 241
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 260 IVMYPIQRRKYRDGIDN---LL--VLLIGG-IPIAMPTVLSvtMAIGShrlsQQGAITKRMTAIEE-----MAG-MDVLC 327
Cdd:cd07543 242 AAAAYVWIEGTKDGRSRyklFLecTLILTSvVPPELPMELS--LAVNT----SLIALAKLYIFCTEpfripFAGkVDICC 315
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 328 SDKTGTLTLNKLSV-------DKNLVEVFCKGVEKDQVLLFAAMASRVEnqdAIDAAMVGmlaDPKE------------- 387
Cdd:cd07543 316 FDKTGTLTSDDLVVegvaglnDGKEVIPVSSIEPVETILVLASCHSLVK---LDDGKLVG---DPLEkatleavdwtltk 389
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 388 ------ARAGIREVHFL---PFNPVDKR-----TALTYIDGSGNWHRVSKGAPEQILELAKasnDLSKKVLSIIDKYAER 453
Cdd:cd07543 390 dekvfpRSKKTKGLKIIqrfHFSSALKRmsvvaSYKDPGSTDLKYIVAVKGAPETLKSMLS---DVPADYDEVYKEYTRQ 466
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 454 GLRSLAVA--------RQVVPEKTKESPGAPWEFVGLLpLFDPP-RHDSAETIRRALNLGVNVKMITGDQLAIGKETGRR 524
Cdd:cd07543 467 GSRVLALGykelghltKQQARDYKREDVESDLTFAGFI-VFSCPlKPDSKETIKELNNSSHRVVMITGDNPLTACHVAKE 545
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 525 LGMGTNMYPSSALLGTHKDANLasipveELIEKADGFAGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIGIA 604
Cdd:cd07543 546 LGIVDKPVLILILSEEGKSNEW------KLIPHVKVFARVAPKQKEFIITTLKELGYVTLMCGDGTNDVGALKHAHVGVA 619
                       570
                ....*....|.
gi 15234666 605 V---ADATDAA 612
Cdd:cd07543 620 LlklGDASIAA 630
P-type_ATPase_HM cd07553
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
148-636 4.79e-25

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: 111.07  E-value: 4.79e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 148 LVPGDIVSIKLGDIIPADARLLEGDpLKVDQSALTGESLPVTKHPGQEVFSGSTCKQGEIEAVVIATGVHTFFG------ 221
Cdd:cd07553 146 IKSGDVYLVASGQRVPVDGKLLSEQ-ASIDMSWLTGESLPRIVERGDKVPAGTSLENQAFEIRVEHSLAESWSGsilqkv 224
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 222 -----KAAHLVDSTNQVGHFQKVLtaignfcICSIAIGMVIEIIVMypiqrrKYRDGIDNLLVLLIGGIPIAMPTVLSVT 296
Cdd:cd07553 225 eaqeaRKTPRDLLADKIIHYFTVI-------ALLIAVAGFGVWLAI------DLSIALKVFTSVLIVACPCALALATPFT 291
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 297 MAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKlsvdKNLVEVFCKGVEKDQVLLFAAMASRVENQDAIda 376
Cdd:cd07553 292 DEIALARLKKKGVLIKNASSLERLSRVRTIVFDKTGTLTRGK----SSFVMVNPEGIDRLALRAISAIEAHSRHPISR-- 365
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 377 AMVGMLADPKEARAGIREvhflpfnpvdkrtaLTYIDGSGnwhrvskgapeqileLAKASNDLSKKVLSIIDkYAERGLR 456
Cdd:cd07553 366 AIREHLMAKGLIKAGASE--------------LVEIVGKG---------------VSGNSSGSLWKLGSAPD-ACGIQES 415
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 457 SLAVARQVVpektkespgapweFVGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGKETGRRLGMGtnmyPSSA 536
Cdd:cd07553 416 GVVIARDGR-------------QLLDLSFNDLLRPDSNREIEELKKGGLSIAILSGDNEEKVRLVGDSLGLD----PRQL 478
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 537 llgthkdanlasipveeliekadgFAGVFPEHKYEIVKKLQERKHIvgMTGDGVNDAPALKKADIGIAVADATDAARGAS 616
Cdd:cd07553 479 ------------------------FGNLSPEEKLAWIESHSPENTL--MVGDGANDALALASAFVGIAVAGEVGVSLEAA 532
                       490       500
                ....*....|....*....|
gi 15234666 617 DIVLTEPGLSVIISAVLTSR 636
Cdd:cd07553 533 DIYYAGNGIGGIRDLLTLSK 552
Cation_ATPase_N smart00831
Cation transporter/ATPase, N-terminus; This entry represents the conserved N-terminal region ...
12-74 2.28e-14

Cation transporter/ATPase, N-terminus; This entry represents the conserved N-terminal region found in several classes of cation-transporting P-type ATPases, including those that transport H+, Na+, Ca2+, Na+/K+, and H+/K+. In the H+/K+- and Na+/K+-exchange P-ATPases, this domain is found in the catalytic alpha chain. In gastric H+/K+-ATPases, this domain undergoes reversible sequential phosphorylation inducing conformational changes that may be important for regulating the function of these ATPases.


Pssm-ID: 214842 [Multi-domain]  Cd Length: 75  Bit Score: 68.76  E-value: 2.28e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15234666     12 VDLEKIPIEEVFQQLKCSRE-GLTTQEGEDRIQIFGPNKLEE-KKESKLLKFLGFMWNPLSWVME 74
Cdd:smart00831   2 LDWHALSLEEVLERLQTDLEkGLSSEEAARRLERYGPNELPPpKKTSPLLRFLRQFHNPLIYILL 66
Cation_ATPase_N pfam00690
Cation transporter/ATPase, N-terminus; Members of this families are involved in Na+/K+, H+/K+, ...
16-74 3.68e-12

Cation transporter/ATPase, N-terminus; Members of this families are involved in Na+/K+, H+/K+, Ca++ and Mg++ transport.


Pssm-ID: 459907 [Multi-domain]  Cd Length: 68  Bit Score: 62.19  E-value: 3.68e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15234666    16 KIPIEEVFQQLKCSRE-GLTTQEGEDRIQIFGPNKL-EEKKESKLLKFLGFMWNPLSWVME 74
Cdd:pfam00690   3 ALSVEEVLKKLGTDLEkGLTEAEAEKRLKKYGPNELpEKKPKSLWKLFLRQFKDPLIIILL 63
P-type_ATPase_APLT_Dnf-like cd02073
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ...
131-617 5.32e-11

Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2, -10D, -11B, -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. This subfamily includes mammalian flippases such as ATP11C which may selectively transports PS and PE from the outer leaflet of the plasma membrane to the inner leaflet. 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: 319770 [Multi-domain]  Cd Length: 836  Bit Score: 66.81  E-value: 5.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 131 KTKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLL---EGDPL-KVDQSALTGES-------LPVT---------- 189
Cdd:cd02073  84 PVQVLRGGKFVKKKWKDIRVGDIVRVKNDEFVPADLLLLsssEPDGLcYVETANLDGETnlkirqaLPETalllseedla 163
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 190 ----------------------KHPGQEVFS---------GSTCKQGE-IEAVVIATGVHTffgKAAhlvdsTNQVG--- 234
Cdd:cd02073 164 rfsgeieceqpnndlytfngtlELNGGRELPlspdnlllrGCTLRNTEwVYGVVVYTGHET---KLM-----LNSGGtpl 235
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 235 ---HFQKVLTA--IGNFCI----CSI-AIGMVI--------EIIVMYPIQRRKYRDGIDNLLVLLI---GGIPIAmptvL 293
Cdd:cd02073 236 krsSIEKKMNRfiIAIFCIlivmCLIsAIGKGIwlskhgrdLWYLLPKEERSPALEFFFDFLTFIIlynNLIPIS----L 311
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 294 SVTM----AIGSHRLSQ----------QGAITKRMTAIEEMAGMDVLCSDKTGTLTLN-----KLSVDKNLVEVFckgve 354
Cdd:cd02073 312 YVTIevvkFLQSFFINWdldmydeetdTPAEARTSNLNEELGQVEYIFSDKTGTLTENimefkKCSINGVDYGFF----- 386
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 355 kdqvLLFA----AMASRVENQDAID--------------AAMVGMLA---DPK----EARAGIRE---VHFLPFNPVDKR 406
Cdd:cd02073 387 ----LALAlchtVVPEKDDHPGQLVyqasspdeaalveaARDLGFVFlsrTPDtvtiNALGEEEEyeiLHILEFNSDRKR 462
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 407 TALTYIDGSGNWHRVSKGAPEQILE-LAKASNDLSKKVLSIIDKYAERGLRSLAVARQVVPEKtkespgapwEFVGLLPL 485
Cdd:cd02073 463 MSVIVRDPDGRILLYCKGADSVIFErLSPSSLELVEKTQEHLEDFASEGLRTLCLAYREISEE---------EYEEWNEK 533
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 486 FDPPR----------HDSAETIRRALNL------------------------GVNVKMITGDQlaigKETGRRLGMGTNM 531
Cdd:cd02073 534 YDEAStalqnreellDEVAEEIEKDLILlgataiedklqdgvpetiealqraGIKIWVLTGDK----QETAINIGYSCRL 609
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 532 YPSS----ALL---GTHKDANLASIPVE--ELIEKADGF--AGVFPEHKYEIVKKLQER-KHIVGMTGDGVNDAPALKKA 599
Cdd:cd02073 610 LSEDmenlALVidgKTLTYALDPELERLflELALKCKAVicCRVSPLQKALVVKLVKKSkKAVTLAIGDGANDVSMIQEA 689
                       650       660
                ....*....|....*....|
gi 15234666 600 DIGIAVA--DATDAARgASD 617
Cdd:cd02073 690 HVGVGISgqEGMQAAR-ASD 708
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
427-600 2.41e-07

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: 52.20  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   427 EQILELAKASNDLSKKVLSIIDKYAERGLRSLAVARQVVPEKTKESPGAPW-EFVGLLPLFDP--PRHDSAETIRRALNL 503
Cdd:pfam00702  34 KAIVAAAEDLPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEGLTVVLvELLGVIALADElkLYPGAAEALKALKER 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   504 GVNVKMITGDQLAIGKETGRRLGMgtnmypssallgthKDANLASIPVEEliekaDGFAGVFPEHKYEIVKKLQERKHIV 583
Cdd:pfam00702 114 GIKVAILTGDNPEAAEALLRLLGL--------------DDYFDVVISGDD-----VGVGKPKPEIYLAALERLGVKPEEV 174
                         170
                  ....*....|....*..
gi 15234666   584 GMTGDGVNDAPALKKAD 600
Cdd:pfam00702 175 LMVGDGVNDIPAAKAAG 191
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
492-623 1.08e-06

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


Pssm-ID: 319816 [Multi-domain]  Cd Length: 139  Bit Score: 48.74  E-value: 1.08e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 492 DSAETIRRALNLGVNVKMITGDQLAIgketgrrlgmgtnMYPSSALLGThkdanlasipveeliekaDGfaGVFPEH--- 568
Cdd:cd07514  20 RAIEAIRKLEKAGIPVVLVTGNSLPV-------------ARALAKYLGL------------------SG--PVVAENggv 66
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 569 -KYEIVKKLQERKHI----VGMTGDGVNDAPALKKADIGIAVADATDAARGASDIVLTEP 623
Cdd:cd07514  67 dKGTGLEKLAERLGIdpeeVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDAS 126
P-type_ATPase_APLT_Neo1-like cd07541
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Neo1p and human ...
132-605 1.26e-04

Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Neo1p and human putative APLT, ATP9B; Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as a flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. The yeast Neo1 gene is an essential gene; Neo1p localizes to the endoplasmic reticulum and the Golgi complex and plays a role in membrane trafficking within the endomembrane system. Also included in this sub family is human putative ATPase phospholipid transporting 9B, ATP9B, which localizes to the trans-golgi network in a CDC50 protein-independent manner. Levels of ATP9B, along with levels of other ATPase genes, may contribute to expressivity of and atypical presentations of Hailey-Hailey disease (HHD), and the ATP9B gene has recently been identified as a putative Alzheimer's disease loci. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319841 [Multi-domain]  Cd Length: 792  Bit Score: 45.86  E-value: 1.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 132 TKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDP------LKVDQsaLTGES-------LPVTKH------- 191
Cdd:cd07541  83 EKLTVRGETVEIPSSDIKVGDLIIVEKNQRIPADMVLLRTSEksgscfIRTDQ--LDGETdwklriaVPCTQKlpeegil 160
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 192 ----------PGQEV--FSGSTCKQGEIE------------AVVIA----TGVHTFFGKAAHLVDSTNQVGHFQKVLTAI 243
Cdd:cd07541 161 nsisavyaeaPQKDIhsFYGTFTINDDPTseslsventlwaNTVVAsgtvIGVVVYTGKETRSVMNTSQPKNKVGLLDLE 240
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 244 GNF---CICSIAIGMVIEIIVMYPIQRRKYRDgIDNLLVLLIGGIPIAMPTVLSVTMAIGSHRLSQ----QGAITKRMTA 316
Cdd:cd07541 241 INFltkILFCAVLALSIVMVALQGFQGPWYIY-LFRFLILFSSIIPISLRVNLDMAKIVYSWQIEHdkniPGTVVRTSTI 319
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 317 IEEMAGMDVLCSDKTGTLTLNKLSVDKnlvevFCKGVE--KDQVLLFAAMasrvenqdaidaamvgmladpkearagire 394
Cdd:cd07541 320 PEELGRIEYLLSDKTGTLTQNEMVFKK-----LHLGTVsyGGQNLNYEIL------------------------------ 364
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 395 vHFLPFNPVDKRTALTYID-GSGNWHRVSKGAPEQILELAKASNDLSKKVLSIidkyAERGLRSLAVARQVVPEKTKESP 473
Cdd:cd07541 365 -QIFPFTSESKRMGIIVREeKTGEITFYMKGADVVMSKIVQYNDWLEEECGNM----AREGLRTLVVAKKKLSEEEYQAF 439
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 474 GAPW-------------------------EFVGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQL----AIGKETG-- 522
Cdd:cd07541 440 EKRYnaaklsihdrdlkvaevveslerelELLCLTGVEDKLQEDVKPTLELLRNAGIKIWMLTGDKLetatCIAKSSKlv 519
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 523 ---------RRLGMGTNMYPSSALLGTHKDANLA----SIPV------EELIEKADGFAGVF-----PEHKYEIVKKLQE 578
Cdd:cd07541 520 srgqyihvfRKVTTREEAHLELNNLRRKHDCALVidgeSLEVclkyyeHEFIELACQLPAVVccrcsPTQKAQIVRLIQK 599
                       570       580
                ....*....|....*....|....*...
gi 15234666 579 RKHI-VGMTGDGVNDAPALKKADIGIAV 605
Cdd:cd07541 600 HTGKrTCAIGDGGNDVSMIQAADVGVGI 627
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
571-624 4.80e-04

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


Pssm-ID: 319769 [Multi-domain]  Cd Length: 146  Bit Score: 41.35  E-value: 4.80e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 15234666 571 EIVKKLQERKHIVGMTGDGVNDAPALKKADIGIAVADATDAARGASDIVLTEPG 624
Cdd:cd01630  83 ELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARG 136
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
587-623 1.08e-03

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 41.50  E-value: 1.08e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 15234666  587 GDGVNDAPALKKADIGIAVADATDAARGASDIVLTEP 623
Cdd:PRK01158 180 GDSENDLEMFEVAGFGVAVANADEELKEAADYVTEKS 216
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
573-619 2.96e-03

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


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 39.73  E-value: 2.96e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 15234666 573 VKKLQER-----KHIVGMtGDGVNDAPALKKADIGIAVADATDAARGASDIV 619
Cdd:COG0561 126 LKKLAERlgippEEVIAF-GDSGNDLEMLEAAGLGVAMGNAPPEVKAAADYV 176
COG4087 COG4087
Soluble P-type ATPase [General function prediction only];
546-623 4.91e-03

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


Pssm-ID: 443263 [Multi-domain]  Cd Length: 156  Bit Score: 38.60  E-value: 4.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666 546 LASIPVE-ELIEKADGfagvfPEHKYEIVKKLqERKHIVGMtGDGVNDAPALKKADIGIAVADATDAARGA---SDIVLT 621
Cdd:COG4087  63 LAGLPVElHILPSGDQ-----AEEKLEFVEKL-GAETTVAI-GNGRNDVLMLKEAALGIAVIGPEGASVKAllaADIVVK 135

                ..
gi 15234666 622 EP 623
Cdd:COG4087 136 SI 137
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
541-619 5.08e-03

sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP equivalog model (TIGR01485), encompassing plants and cyanobacteria, as well as those archaeal sequences which are the closest relatives (TIGR01487). It remains to be shown whether these archaeal sequences catalyze the same reaction as SPP.


Pssm-ID: 273650 [Multi-domain]  Cd Length: 225  Bit Score: 39.37  E-value: 5.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   541 HKDANLASIPVEELIEKADGFAGVFPEH-------KYEIVKKLQERKHI----VGMTGDGVNDAPALKKADIGIAVADAT 609
Cdd:TIGR01482 115 GIDVDTVREIIKELGLNLVAVDSGFDIHilpqgvnKGVAVKKLKEKLGIkpgeTLVCGDSENDIDLFEVPGFGVAVANAQ 194
                          90
                  ....*....|
gi 15234666   610 DAARGASDIV 619
Cdd:TIGR01482 195 PELKEWADYV 204
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
553-630 5.74e-03

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


Pssm-ID: 273022 [Multi-domain]  Cd Length: 219  Bit Score: 39.26  E-value: 5.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234666   553 ELIEKADGFAG------VFPEHKYEIVKKLQER-----KHIVgMTGDGVNDAPALKKADIGIAVaDATDAARGASDIVLT 621
Cdd:TIGR00338 131 RLEVEDGKLTGlvegpiVDASYKGKTLLILLRKegispENTV-AVGDGANDLSMIKAAGLGIAF-NAKPKLQQKADICIN 208

                  ....*....
gi 15234666   622 EPGLSVIIS 630
Cdd:TIGR00338 209 KKDLTDILP 217
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
568-619 7.96e-03

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


Pssm-ID: 272905 [Multi-domain]  Cd Length: 256  Bit Score: 39.17  E-value: 7.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15234666   568 HKYEIVKKLQERKHI----VGMTGDGVNDAPALKKADIGIAVADATDAARGASDIV 619
Cdd:TIGR00099 188 SKGSALQSLAEALGIsledVIAFGDGMNDIEMLEAAGYGVAMGNADEELKALADYV 243
 
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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