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Conserved domains on  [gi|1489866104|ref|NP_001353581|]
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phospholipid-transporting ATPase VB isoform 1 [Homo sapiens]

Protein Classification

phospholipid-transporting P-type ATPase( domain architecture ID 11550343)

phospholipid-transporting P-type ATPase is the catalytic component of a P4-ATPase flippase which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids, and is distinguished from other transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P-type_ATPase_APLT_Dnf-like cd02073
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ...
68-1213 0e+00

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: 1193.52  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104   68 GNRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITMLPLAIVLFVIMIKDGMEDFKRHRFDKAI 147
Cdd:cd02073      1 DNRISTTKYTVFTFLPKNLFEQFRRVANLYFLFIAILQQIPGISPTGPYTTLLPLLFVLGVTAIKEGYEDIRRHKSDNEV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  148 NCSNIRIYERKEqtYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVKGFSQQEV 227
Cdd:cd02073     81 NNRPVQVLRGGK--FVKKKWKDIRVGDIVRVKNDEFVPADLLLLSSSEPDGLCYVETANLDGETNLKIRQALPETALLLS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  228 QFEPELFHNTIVCEKPNNHLNKFKGYMEHPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKAMLNNSGPRYKRS 307
Cdd:cd02073    159 EEDLARFSGEIECEQPNNDLYTFNGTLELNGGRELPLSPDNLLLRGCTLRNTEWVYGVVVYTGHETKLMLNSGGTPLKRS 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  308 KIERRMNIDIFFCIGILILMCLIGAVGHSIWNGTFEEHPPFDVPDANGSflpSALGGFYMFLTMIILLQVLIPISLYVSI 387
Cdd:cd02073    239 SIEKKMNRFIIAIFCILIVMCLISAIGKGIWLSKHGRDLWYLLPKEERS---PALEFFFDFLTFIILYNNLIPISLYVTI 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  388 ELVKLGQVFFLSNDLDLYDEETDLSIQCRALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYshqenakrletp 467
Cdd:cd02073    316 EVVKFLQSFFINWDLDMYDEETDTPAEARTSNLNEELGQVEYIFSDKTGTLTENIMEFKKCSINGVDY------------ 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  468 keldsdgeewtqyqclsfsarwaqdpatmrsqkgaqplrrsqsarvpiqghyrqrsmghressqppvafsssiekdvtpd 547
Cdd:cd02073        --------------------------------------------------------------------------------
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  548 knlltkvrdaalwletlsdsrpakaslsttssiaDFFLALTICNSVMVSTTTEPRQrvtikpsskalgtslekiqqlfqk 627
Cdd:cd02073    384 ----------------------------------GFFLALALCHTVVPEKDDHPGQ------------------------ 405
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  628 lkllslsqsfsstapsdtdlgeslganvattdsderddasvcsggdstddggyrssmwdqgdilesgsgtsleealeapa 707
Cdd:cd02073        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  708 tdlarpeFCYEAESPDEAALVHAAHAYSFTLVSRTPEQVTVRlPQGTCLTFSLLCTLGFDSVRKRMSVVVRHPlTGEIVV 787
Cdd:cd02073    406 -------LVYQASSPDEAALVEAARDLGFVFLSRTPDTVTIN-ALGEEEEYEILHILEFNSDRKRMSVIVRDP-DGRILL 476
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  788 YTKGADSVIMDLLEDpacvpdinmekKLRKIRARTQKHLDLYARDGLRTLCIAKKVVSEEDFRRWASFRREAEASLDNRD 867
Cdd:cd02073    477 YCKGADSVIFERLSP-----------SSLELVEKTQEHLEDFASEGLRTLCLAYREISEEEYEEWNEKYDEASTALQNRE 545
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  868 ELLMETAQHLENQLTLLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDKQETAVNIAHSCRLLnqtdtvytinTENQE 947
Cdd:cd02073    546 ELLDEVAEEIEKDLILLGATAIEDKLQDGVPETIEALQRAGIKIWVLTGDKQETAINIGYSCRLL----------SEDME 615
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  948 TCesilncaleelkqfrelqkpdrklfgfrlpsktpsitseavvpeaGLVIDGKTLNAIFQGKLEKKFLELTQYCRSVLC 1027
Cdd:cd02073    616 NL---------------------------------------------ALVIDGKTLTYALDPELERLFLELALKCKAVIC 650
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1028 CRSTPLQKSMIVKLVRDKLRVMTLSIGDGANDVSMIQAADIGIGISGQEGMQAVMSSDFAITRFKHLKKLLLVHGHWCYS 1107
Cdd:cd02073    651 CRVSPLQKALVVKLVKKSKKAVTLAIGDGANDVSMIQEAHVGVGISGQEGMQAARASDYAIAQFRFLRRLLLVHGRWSYQ 730
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1108 RLARMVVYYLYKNVCYVNLLFWYQFFCGFSSSTMIDYWQMIFFNLFFTSLPPLVFGVLDKDISAETLLALPELYKSGQNS 1187
Cdd:cd02073    731 RLAKLILYFFYKNIAFYLTQFWYQFFNGFSGQTLYDSWYLTLYNVLFTSLPPLVIGIFDQDVSAETLLRYPELYKPGQLN 810
                         1130      1140
                   ....*....|....*....|....*.
gi 1489866104 1188 ECYNLSTFWISMVDAFYQSLICFFIP 1213
Cdd:cd02073    811 ELFNWKVFLYWILDGIYQSLIIFFVP 836
 
Name Accession Description Interval E-value
P-type_ATPase_APLT_Dnf-like cd02073
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ...
68-1213 0e+00

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: 1193.52  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104   68 GNRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITMLPLAIVLFVIMIKDGMEDFKRHRFDKAI 147
Cdd:cd02073      1 DNRISTTKYTVFTFLPKNLFEQFRRVANLYFLFIAILQQIPGISPTGPYTTLLPLLFVLGVTAIKEGYEDIRRHKSDNEV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  148 NCSNIRIYERKEqtYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVKGFSQQEV 227
Cdd:cd02073     81 NNRPVQVLRGGK--FVKKKWKDIRVGDIVRVKNDEFVPADLLLLSSSEPDGLCYVETANLDGETNLKIRQALPETALLLS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  228 QFEPELFHNTIVCEKPNNHLNKFKGYMEHPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKAMLNNSGPRYKRS 307
Cdd:cd02073    159 EEDLARFSGEIECEQPNNDLYTFNGTLELNGGRELPLSPDNLLLRGCTLRNTEWVYGVVVYTGHETKLMLNSGGTPLKRS 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  308 KIERRMNIDIFFCIGILILMCLIGAVGHSIWNGTFEEHPPFDVPDANGSflpSALGGFYMFLTMIILLQVLIPISLYVSI 387
Cdd:cd02073    239 SIEKKMNRFIIAIFCILIVMCLISAIGKGIWLSKHGRDLWYLLPKEERS---PALEFFFDFLTFIILYNNLIPISLYVTI 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  388 ELVKLGQVFFLSNDLDLYDEETDLSIQCRALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYshqenakrletp 467
Cdd:cd02073    316 EVVKFLQSFFINWDLDMYDEETDTPAEARTSNLNEELGQVEYIFSDKTGTLTENIMEFKKCSINGVDY------------ 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  468 keldsdgeewtqyqclsfsarwaqdpatmrsqkgaqplrrsqsarvpiqghyrqrsmghressqppvafsssiekdvtpd 547
Cdd:cd02073        --------------------------------------------------------------------------------
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  548 knlltkvrdaalwletlsdsrpakaslsttssiaDFFLALTICNSVMVSTTTEPRQrvtikpsskalgtslekiqqlfqk 627
Cdd:cd02073    384 ----------------------------------GFFLALALCHTVVPEKDDHPGQ------------------------ 405
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  628 lkllslsqsfsstapsdtdlgeslganvattdsderddasvcsggdstddggyrssmwdqgdilesgsgtsleealeapa 707
Cdd:cd02073        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  708 tdlarpeFCYEAESPDEAALVHAAHAYSFTLVSRTPEQVTVRlPQGTCLTFSLLCTLGFDSVRKRMSVVVRHPlTGEIVV 787
Cdd:cd02073    406 -------LVYQASSPDEAALVEAARDLGFVFLSRTPDTVTIN-ALGEEEEYEILHILEFNSDRKRMSVIVRDP-DGRILL 476
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  788 YTKGADSVIMDLLEDpacvpdinmekKLRKIRARTQKHLDLYARDGLRTLCIAKKVVSEEDFRRWASFRREAEASLDNRD 867
Cdd:cd02073    477 YCKGADSVIFERLSP-----------SSLELVEKTQEHLEDFASEGLRTLCLAYREISEEEYEEWNEKYDEASTALQNRE 545
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  868 ELLMETAQHLENQLTLLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDKQETAVNIAHSCRLLnqtdtvytinTENQE 947
Cdd:cd02073    546 ELLDEVAEEIEKDLILLGATAIEDKLQDGVPETIEALQRAGIKIWVLTGDKQETAINIGYSCRLL----------SEDME 615
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  948 TCesilncaleelkqfrelqkpdrklfgfrlpsktpsitseavvpeaGLVIDGKTLNAIFQGKLEKKFLELTQYCRSVLC 1027
Cdd:cd02073    616 NL---------------------------------------------ALVIDGKTLTYALDPELERLFLELALKCKAVIC 650
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1028 CRSTPLQKSMIVKLVRDKLRVMTLSIGDGANDVSMIQAADIGIGISGQEGMQAVMSSDFAITRFKHLKKLLLVHGHWCYS 1107
Cdd:cd02073    651 CRVSPLQKALVVKLVKKSKKAVTLAIGDGANDVSMIQEAHVGVGISGQEGMQAARASDYAIAQFRFLRRLLLVHGRWSYQ 730
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1108 RLARMVVYYLYKNVCYVNLLFWYQFFCGFSSSTMIDYWQMIFFNLFFTSLPPLVFGVLDKDISAETLLALPELYKSGQNS 1187
Cdd:cd02073    731 RLAKLILYFFYKNIAFYLTQFWYQFFNGFSGQTLYDSWYLTLYNVLFTSLPPLVIGIFDQDVSAETLLRYPELYKPGQLN 810
                         1130      1140
                   ....*....|....*....|....*.
gi 1489866104 1188 ECYNLSTFWISMVDAFYQSLICFFIP 1213
Cdd:cd02073    811 ELFNWKVFLYWILDGIYQSLIIFFVP 836
ATPase-Plipid TIGR01652
phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase ...
66-1332 0e+00

phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase responsible for transporting phospholipids from one leaflet of bilayer membranes to the other. These ATPases are found only in eukaryotes.


Pssm-ID: 273734 [Multi-domain]  Cd Length: 1057  Bit Score: 1039.26  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104   66 YPGNRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITMLPLAIVLFVIMIKDGMEDFKRHRFDK 145
Cdd:TIGR01652    1 FCSNKISTTKYTVLTFLPKNLFEQFKRFANLYFLVVALLQQVPILSPTYRGTSIVPLAFVLIVTAIKEAIEDIRRRRRDK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  146 AINCSNIRIYERKeQTYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVKGFSQQ 225
Cdd:TIGR01652   81 EVNNRLTEVLEGH-GQFVEIPWKDLRVGDIVKVKKDERIPADLLLLSSSEPDGVCYVETANLDGETNLKLRQALEETQKM 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  226 EVQFEPELFHNTIVCEKPNNHLNKFKGYMEHPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKAMLNNSGPRYK 305
Cdd:TIGR01652  160 LDEDDIKNFSGEIECEQPNASLYSFQGNMTINGDRQYPLSPDNILLRGCTLRNTDWVIGVVVYTGHDTKLMRNATQAPSK 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  306 RSKIERRMNIDIFFCIGILILMCLIGAVGHSIWNGTFEEHPPFDVPDanGSFLPSALGGFYMFLTMIILLQVLIPISLYV 385
Cdd:TIGR01652  240 RSRLEKELNFLIIILFCLLFVLCLISSVGAGIWNDAHGKDLWYIRLD--VSERNAAANGFFSFLTFLILFSSLIPISLYV 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  386 SIELVKLGQVFFLSNDLDLYDEETDLSIQCRALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYSHQENAKRLE 465
Cdd:TIGR01652  318 SLELVKSVQAYFINSDLQMYHEKTDTPASVRTSNLNEELGQVEYIFSDKTGTLTQNIMEFKKCSIAGVSYGDGFTEIKDG 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  466 TPKELDSDGEEWTQYQcLSFSARWAQDPATMRSQKGAQPlrrsqsarvpiqghyrqrsmghressQPPVAFsssiekdvt 545
Cdd:TIGR01652  398 IRERLGSYVENENSML-VESKGFTFVDPRLVDLLKTNKP--------------------------NAKRIN--------- 441
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  546 pdknlltkvrdaalwletlsdsrpakaslsttssiaDFFLALTICNSVMVSTTTEPRQRVTikpsskalgtslekiqqlf 625
Cdd:TIGR01652  442 ------------------------------------EFFLALALCHTVVPEFNDDGPEEIT------------------- 466
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  626 qklkllslsqsfsstapsdtdlgeslganvattdsderddasvcsggdstddggyrssmwdqgdilesgsgtsleealea 705
Cdd:TIGR01652      --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  706 patdlarpefcYEAESPDEAALVHAAHAYSFTLVSRTPEQVTVRLP-QGTCLTFSLLCTLGFDSVRKRMSVVVRHPlTGE 784
Cdd:TIGR01652  467 -----------YQAASPDEAALVKAARDVGFVFFERTPKSISLLIEmHGETKEYEILNVLEFNSDRKRMSVIVRNP-DGR 534
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  785 IVVYTKGADSVIMDLLEDpacvpdinmekKLRKIRARTQKHLDLYARDGLRTLCIAKKVVSEEDFRRWASFRREAEASLD 864
Cdd:TIGR01652  535 IKLLCKGADTVIFKRLSS-----------GGNQVNEETKEHLENYASEGLRTLCIAYRELSEEEYEEWNEEYNEASTALT 603
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  865 NRDELLMETAQHLENQLTLLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDKQETAVNIAHSCRLLNQTDTVYTINTE 944
Cdd:TIGR01652  604 DREEKLDVVAESIEKDLILLGATAIEDKLQEGVPETIELLRQAGIKIWVLTGDKVETAINIGYSCRLLSRNMEQIVITSD 683
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  945 NQETCESIlncaleelkqFRELQKPDRKLFgfrlpsktPSITSEAVVPEAGLVIDGKTLNAIFQGKLEKKFLELTQYCRS 1024
Cdd:TIGR01652  684 SLDATRSV----------EAAIKFGLEGTS--------EEFNNLGDSGNVALVIDGKSLGYALDEELEKEFLQLALKCKA 745
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1025 VLCCRSTPLQKSMIVKLVRDKLRVMTLSIGDGANDVSMIQAADIGIGISGQEGMQAVMSSDFAITRFKHLKKLLLVHGHW 1104
Cdd:TIGR01652  746 VICCRVSPSQKADVVRLVKKSTGKTTLAIGDGANDVSMIQEADVGVGISGKEGMQAVMASDFAIGQFRFLTKLLLVHGRW 825
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1105 CYSRLARMVVYYLYKNVCYVNLLFWYQFFCGFSSSTMIDYWQMIFFNLFFTSLPPLVFGVLDKDISAETLLALPELYKSG 1184
Cdd:TIGR01652  826 SYKRISKMILYFFYKNLIFAIIQFWYSFYNGFSGQTLYEGWYMVLYNVFFTALPVISLGVFDQDVSASLSLRYPQLYREG 905
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1185 QNSECYNLSTFWISMVDAFYQSLICFFIPYLAYKGSD------IDVFTF-GTPINTISLTTILLHQAMEMKTWTIFHGVV 1257
Cdd:TIGR01652  906 QKGQGFSTKTFWGWMLDGIYQSLVIFFFPMFAYILGDfvssgsVDDFSSvGVIVFTALVVIVNLKIALEINRWNWISLIT 985
                         1210      1220      1230      1240      1250      1260      1270
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1489866104 1258 LLGSFLMYFLvsllynATCVICNSPTNP--YWVMEGQLSNPTFYLVCFLTPVVALLPRYFFLSLQGTCGKSLISKAQ 1332
Cdd:TIGR01652  986 IWGSILVWLI------FVIVYSSIFPSPafYKAAPRVMGTFGFWLVLLVIVLISLLPRFTYKAIQRLFRPPDYDIVQ 1056
PLN03190 PLN03190
aminophospholipid translocase; Provisional
54-1314 0e+00

aminophospholipid translocase; Provisional


Pssm-ID: 215623 [Multi-domain]  Cd Length: 1178  Bit Score: 821.45  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104   54 IFHQDWEEVSRRY--PGNRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITMLPLAIVLFVIMI 131
Cdd:PLN03190    73 VYLNDPEKSNERFefAGNSIRTAKYSVFSFLPRNLFEQFHRVAYIYFLVIAVLNQLPQLAVFGRGASILPLAFVLLVTAV 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  132 KDGMEDFKRHRFDKAINCSNIRIYERKEqtYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGET 211
Cdd:PLN03190   153 KDAYEDWRRHRSDRIENNRLAWVLVDDQ--FQEKKWKDIRVGEIIKIQANDTLPCDMVLLSTSDPTGVAYVQTINLDGES 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  212 NLKQRcvvkgFSQQEVQF---EPELFHNTIVCEKPNNHLNKFKGYMEhPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIY 288
Cdd:PLN03190   231 NLKTR-----YAKQETLSkipEKEKINGLIKCEKPNRNIYGFQANME-VDGKRLSLGPSNIILRGCELKNTAWAIGVAVY 304
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  289 AGHETKAMLNNSGPRYKRSKIERRMNIDIFFCIGILILMCLIGAVGHSIWNGT---------FEEHPPFDVPDA-NGSFL 358
Cdd:PLN03190   305 CGRETKAMLNNSGAPSKRSRLETRMNLEIIILSLFLIALCTIVSVCAAVWLRRhrdeldtipFYRRKDFSEGGPkNYNYY 384
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  359 PSALGGFYMFLTMIILLQVLIPISLYVSIELVKLGQVFFLSNDLDLYDEETDLSIQCRALNIAEDLGQIQYIFSDKTGTL 438
Cdd:PLN03190   385 GWGWEIFFTFLMSVIVFQIMIPISLYISMELVRVGQAYFMIRDDQMYDEASNSRFQCRALNINEDLGQIKYVFSDKTGTL 464
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  439 TENKMVFRRCTIMGSEYShqenakrletpkeldsDGEEWTQyqclsfsarwaQDPATMRSQKGAQPLRRSQSARVpiqgh 518
Cdd:PLN03190   465 TENKMEFQCASIWGVDYS----------------DGRTPTQ-----------NDHAGYSVEVDGKILRPKMKVKV----- 512
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  519 yrqrsmghressqppvafsssiekdvtpDKNLLTKVRDAalwletlSDSRPAKaslsttsSIADFFLALTICNsvmvstt 598
Cdd:PLN03190   513 ----------------------------DPQLLELSKSG-------KDTEEAK-------HVHDFFLALAACN------- 543
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  599 teprqrvTIKPSskalgtslekiqqlfqklkllslsqsfsstapsdtdlgeslganVATTDSDerddasvcsggdstddg 678
Cdd:PLN03190   544 -------TIVPI--------------------------------------------VVDDTSD----------------- 555
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  679 gyrssmwdqgdilesgsgtsleealeaPATDLARpefcYEAESPDEAALVHAAHAYSFTLVSRTPEQVTVRLpQGTCLTF 758
Cdd:PLN03190   556 ---------------------------PTVKLMD----YQGESPDEQALVYAAAAYGFMLIERTSGHIVIDI-HGERQRF 603
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  759 SLLCTLGFDSVRKRMSVVVRHPlTGEIVVYTKGADSVIMDLLEDpacvpDINMekklRKIRArTQKHLDLYARDGLRTLC 838
Cdd:PLN03190   604 NVLGLHEFDSDRKRMSVILGCP-DKTVKVFVKGADTSMFSVIDR-----SLNM----NVIRA-TEAHLHTYSSLGLRTLV 672
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  839 IAKKVVSEEDFRRWASFRREAEASLDNRDELLMETAQHLENQLTLLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDK 918
Cdd:PLN03190   673 VGMRELNDSEFEQWHFSFEAASTALIGRAALLRKVASNVENNLTILGASAIEDKLQQGVPEAIESLRTAGIKVWVLTGDK 752
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  919 QETAVNIAHSCRLLNQTDTVYTINTENQETCESILNCALEELKqfrelqkpdrKLFGFRLPSKTPSITSEAVVPEAGLVI 998
Cdd:PLN03190   753 QETAISIGYSSKLLTNKMTQIIINSNSKESCRKSLEDALVMSK----------KLTTVSGISQNTGGSSAAASDPVALII 822
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  999 DGKTLNAIFQGKLEKKFLELTQYCRSVLCCRSTPLQKSMIVKLVRDKLRVMTLSIGDGANDVSMIQAADIGIGISGQEGM 1078
Cdd:PLN03190   823 DGTSLVYVLDSELEEQLFQLASKCSVVLCCRVAPLQKAGIVALVKNRTSDMTLAIGDGANDVSMIQMADVGVGISGQEGR 902
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1079 QAVMSSDFAITRFKHLKKLLLVHGHWCYSRLARMVVYYLYKNVCYVNLLFWYQFFCGFSSSTMIDYWQMIFFNLFFTSLP 1158
Cdd:PLN03190   903 QAVMASDFAMGQFRFLVPLLLVHGHWNYQRMGYMILYNFYRNAVFVLVLFWYVLFTCFTLTTAINEWSSVLYSVIYTALP 982
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1159 PLVFGVLDKDISAETLLALPELYKSGQNSECYNLSTFWISMVDAFYQSLICFFIPYLAYKGSDIDVFTFGTPINTISLTT 1238
Cdd:PLN03190   983 TIVVGILDKDLSRRTLLKYPQLYGAGQRQEAYNSKLFWLTMIDTLWQSAVVFFVPLFAYWASTIDGSSIGDLWTLAVVIL 1062
                         1210      1220      1230      1240      1250      1260      1270
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1489866104 1239 ILLHQAMEMKTWT-IFHGvVLLGSFLMYFLVSLLYNATcvicnsPTNP-YWVMEGQLSNPTFYLVCFLTPVVALLPRY 1314
Cdd:PLN03190  1063 VNLHLAMDIIRWNwITHA-AIWGSIVATFICVIVIDAI------PTLPgYWAIFHIAKTGSFWLCLLAIVVAALLPRF 1133
PhoLip_ATPase_C pfam16212
Phospholipid-translocating P-type ATPase C-terminal; PhoLip_ATPase_C is found at the ...
1081-1320 4.54e-107

Phospholipid-translocating P-type ATPase C-terminal; PhoLip_ATPase_C is found at the C-terminus of a number of phospholipid-translocating ATPases. It is found in higher eukaryotes.


Pssm-ID: 465071 [Multi-domain]  Cd Length: 250  Bit Score: 339.87  E-value: 4.54e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1081 VMSSDFAITRFKHLKKLLLVHGHWCYSRLARMVVYYLYKNVCYVNLLFWYQFFCGFSSSTMIDYWQMIFFNLFFTSLPPL 1160
Cdd:pfam16212    1 ARASDYAIAQFRFLKRLLLVHGRWSYRRTSKLILYFFYKNIVFTLTQFWYQFYNGFSGQSLYESWYLTLYNLLFTSLPVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1161 VFGVLDKDISAETLLALPELYKSGQNSECYNLSTFWISMVDAFYQSLICFFIPYLAY------KGSDIDVFTFGTPINTI 1234
Cdd:pfam16212   81 VLGIFDQDVSAETLLAYPELYKLGQKNKFFNLKTFLGWMLDGIYQSLIIFFIPYLAYgdsvfsGGKDADLWAFGTTVFTA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1235 SLTTILLHQAMEMKTWTIFHGVVLLGSFLMYFLVSLLYNATCVICNSptNPYWVMEGQLSNPTFYLVCFLTPVVALLPRY 1314
Cdd:pfam16212  161 LVLVVNLKLALETHYWTWITHLAIWGSILLYFLFTLIYSSIYPSSYS--VFYGVASRLFGSPSFWLTLLLIVVVALLPDF 238

                   ....*.
gi 1489866104 1315 FFLSLQ 1320
Cdd:pfam16212  239 AYKALK 244
MgtA COG0474
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism];
722-1074 5.71e-30

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


Pssm-ID: 440242 [Multi-domain]  Cd Length: 874  Bit Score: 129.07  E-value: 5.71e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  722 PDEAALVHAAHAYSFTLVSRTPEqvtvrlpqgtcltFSLLCTLGFDSVRKRMSVVVRHPlTGEIVVYTKGADSVIMDL-- 799
Cdd:COG0474    385 PTEGALLVAAAKAGLDVEELRKE-------------YPRVDEIPFDSERKRMSTVHEDP-DGKRLLIVKGAPEVVLALct 450
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  800 -LEDPACVPDINMEkklrkIRARTQKHLDLYARDGLRTLCIAKKVVSEEDFrrwasfrreaeasldnrdellmETAQHLE 878
Cdd:COG0474    451 rVLTGGGVVPLTEE-----DRAEILEAVEELAAQGLRVLAVAYKELPADPE----------------------LDSEDDE 503
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  879 NQLTLLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDKQETAVNIAHSCRLLNQTDTVYTIntenqetcesilncale 958
Cdd:COG0474    504 SDLTFLGLVGMIDPPRPEAKEAIAECRRAGIRVKMITGDHPATARAIARQLGLGDDGDRVLTG----------------- 566
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  959 elkqfRELQK-PDRKLfgfrlpsktpsitsEAVVPEAglvidgktlnAIFqgklekkfleltqycrsvlcCRSTPLQKSM 1037
Cdd:COG0474    567 -----AELDAmSDEEL--------------AEAVEDV----------DVF--------------------ARVSPEHKLR 597
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1489866104 1038 IVKLVRDKLRV--MTlsiGDGANDVSMIQAADIGI--GISG 1074
Cdd:COG0474    598 IVKALQANGHVvaMT---GDGVNDAPALKAADIGIamGITG 635
 
Name Accession Description Interval E-value
P-type_ATPase_APLT_Dnf-like cd02073
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ...
68-1213 0e+00

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: 1193.52  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104   68 GNRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITMLPLAIVLFVIMIKDGMEDFKRHRFDKAI 147
Cdd:cd02073      1 DNRISTTKYTVFTFLPKNLFEQFRRVANLYFLFIAILQQIPGISPTGPYTTLLPLLFVLGVTAIKEGYEDIRRHKSDNEV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  148 NCSNIRIYERKEqtYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVKGFSQQEV 227
Cdd:cd02073     81 NNRPVQVLRGGK--FVKKKWKDIRVGDIVRVKNDEFVPADLLLLSSSEPDGLCYVETANLDGETNLKIRQALPETALLLS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  228 QFEPELFHNTIVCEKPNNHLNKFKGYMEHPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKAMLNNSGPRYKRS 307
Cdd:cd02073    159 EEDLARFSGEIECEQPNNDLYTFNGTLELNGGRELPLSPDNLLLRGCTLRNTEWVYGVVVYTGHETKLMLNSGGTPLKRS 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  308 KIERRMNIDIFFCIGILILMCLIGAVGHSIWNGTFEEHPPFDVPDANGSflpSALGGFYMFLTMIILLQVLIPISLYVSI 387
Cdd:cd02073    239 SIEKKMNRFIIAIFCILIVMCLISAIGKGIWLSKHGRDLWYLLPKEERS---PALEFFFDFLTFIILYNNLIPISLYVTI 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  388 ELVKLGQVFFLSNDLDLYDEETDLSIQCRALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYshqenakrletp 467
Cdd:cd02073    316 EVVKFLQSFFINWDLDMYDEETDTPAEARTSNLNEELGQVEYIFSDKTGTLTENIMEFKKCSINGVDY------------ 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  468 keldsdgeewtqyqclsfsarwaqdpatmrsqkgaqplrrsqsarvpiqghyrqrsmghressqppvafsssiekdvtpd 547
Cdd:cd02073        --------------------------------------------------------------------------------
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  548 knlltkvrdaalwletlsdsrpakaslsttssiaDFFLALTICNSVMVSTTTEPRQrvtikpsskalgtslekiqqlfqk 627
Cdd:cd02073    384 ----------------------------------GFFLALALCHTVVPEKDDHPGQ------------------------ 405
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  628 lkllslsqsfsstapsdtdlgeslganvattdsderddasvcsggdstddggyrssmwdqgdilesgsgtsleealeapa 707
Cdd:cd02073        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  708 tdlarpeFCYEAESPDEAALVHAAHAYSFTLVSRTPEQVTVRlPQGTCLTFSLLCTLGFDSVRKRMSVVVRHPlTGEIVV 787
Cdd:cd02073    406 -------LVYQASSPDEAALVEAARDLGFVFLSRTPDTVTIN-ALGEEEEYEILHILEFNSDRKRMSVIVRDP-DGRILL 476
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  788 YTKGADSVIMDLLEDpacvpdinmekKLRKIRARTQKHLDLYARDGLRTLCIAKKVVSEEDFRRWASFRREAEASLDNRD 867
Cdd:cd02073    477 YCKGADSVIFERLSP-----------SSLELVEKTQEHLEDFASEGLRTLCLAYREISEEEYEEWNEKYDEASTALQNRE 545
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  868 ELLMETAQHLENQLTLLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDKQETAVNIAHSCRLLnqtdtvytinTENQE 947
Cdd:cd02073    546 ELLDEVAEEIEKDLILLGATAIEDKLQDGVPETIEALQRAGIKIWVLTGDKQETAINIGYSCRLL----------SEDME 615
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  948 TCesilncaleelkqfrelqkpdrklfgfrlpsktpsitseavvpeaGLVIDGKTLNAIFQGKLEKKFLELTQYCRSVLC 1027
Cdd:cd02073    616 NL---------------------------------------------ALVIDGKTLTYALDPELERLFLELALKCKAVIC 650
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1028 CRSTPLQKSMIVKLVRDKLRVMTLSIGDGANDVSMIQAADIGIGISGQEGMQAVMSSDFAITRFKHLKKLLLVHGHWCYS 1107
Cdd:cd02073    651 CRVSPLQKALVVKLVKKSKKAVTLAIGDGANDVSMIQEAHVGVGISGQEGMQAARASDYAIAQFRFLRRLLLVHGRWSYQ 730
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1108 RLARMVVYYLYKNVCYVNLLFWYQFFCGFSSSTMIDYWQMIFFNLFFTSLPPLVFGVLDKDISAETLLALPELYKSGQNS 1187
Cdd:cd02073    731 RLAKLILYFFYKNIAFYLTQFWYQFFNGFSGQTLYDSWYLTLYNVLFTSLPPLVIGIFDQDVSAETLLRYPELYKPGQLN 810
                         1130      1140
                   ....*....|....*....|....*.
gi 1489866104 1188 ECYNLSTFWISMVDAFYQSLICFFIP 1213
Cdd:cd02073    811 ELFNWKVFLYWILDGIYQSLIIFFVP 836
ATPase-Plipid TIGR01652
phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase ...
66-1332 0e+00

phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase responsible for transporting phospholipids from one leaflet of bilayer membranes to the other. These ATPases are found only in eukaryotes.


Pssm-ID: 273734 [Multi-domain]  Cd Length: 1057  Bit Score: 1039.26  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104   66 YPGNRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITMLPLAIVLFVIMIKDGMEDFKRHRFDK 145
Cdd:TIGR01652    1 FCSNKISTTKYTVLTFLPKNLFEQFKRFANLYFLVVALLQQVPILSPTYRGTSIVPLAFVLIVTAIKEAIEDIRRRRRDK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  146 AINCSNIRIYERKeQTYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVKGFSQQ 225
Cdd:TIGR01652   81 EVNNRLTEVLEGH-GQFVEIPWKDLRVGDIVKVKKDERIPADLLLLSSSEPDGVCYVETANLDGETNLKLRQALEETQKM 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  226 EVQFEPELFHNTIVCEKPNNHLNKFKGYMEHPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKAMLNNSGPRYK 305
Cdd:TIGR01652  160 LDEDDIKNFSGEIECEQPNASLYSFQGNMTINGDRQYPLSPDNILLRGCTLRNTDWVIGVVVYTGHDTKLMRNATQAPSK 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  306 RSKIERRMNIDIFFCIGILILMCLIGAVGHSIWNGTFEEHPPFDVPDanGSFLPSALGGFYMFLTMIILLQVLIPISLYV 385
Cdd:TIGR01652  240 RSRLEKELNFLIIILFCLLFVLCLISSVGAGIWNDAHGKDLWYIRLD--VSERNAAANGFFSFLTFLILFSSLIPISLYV 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  386 SIELVKLGQVFFLSNDLDLYDEETDLSIQCRALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYSHQENAKRLE 465
Cdd:TIGR01652  318 SLELVKSVQAYFINSDLQMYHEKTDTPASVRTSNLNEELGQVEYIFSDKTGTLTQNIMEFKKCSIAGVSYGDGFTEIKDG 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  466 TPKELDSDGEEWTQYQcLSFSARWAQDPATMRSQKGAQPlrrsqsarvpiqghyrqrsmghressQPPVAFsssiekdvt 545
Cdd:TIGR01652  398 IRERLGSYVENENSML-VESKGFTFVDPRLVDLLKTNKP--------------------------NAKRIN--------- 441
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  546 pdknlltkvrdaalwletlsdsrpakaslsttssiaDFFLALTICNSVMVSTTTEPRQRVTikpsskalgtslekiqqlf 625
Cdd:TIGR01652  442 ------------------------------------EFFLALALCHTVVPEFNDDGPEEIT------------------- 466
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  626 qklkllslsqsfsstapsdtdlgeslganvattdsderddasvcsggdstddggyrssmwdqgdilesgsgtsleealea 705
Cdd:TIGR01652      --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  706 patdlarpefcYEAESPDEAALVHAAHAYSFTLVSRTPEQVTVRLP-QGTCLTFSLLCTLGFDSVRKRMSVVVRHPlTGE 784
Cdd:TIGR01652  467 -----------YQAASPDEAALVKAARDVGFVFFERTPKSISLLIEmHGETKEYEILNVLEFNSDRKRMSVIVRNP-DGR 534
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  785 IVVYTKGADSVIMDLLEDpacvpdinmekKLRKIRARTQKHLDLYARDGLRTLCIAKKVVSEEDFRRWASFRREAEASLD 864
Cdd:TIGR01652  535 IKLLCKGADTVIFKRLSS-----------GGNQVNEETKEHLENYASEGLRTLCIAYRELSEEEYEEWNEEYNEASTALT 603
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  865 NRDELLMETAQHLENQLTLLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDKQETAVNIAHSCRLLNQTDTVYTINTE 944
Cdd:TIGR01652  604 DREEKLDVVAESIEKDLILLGATAIEDKLQEGVPETIELLRQAGIKIWVLTGDKVETAINIGYSCRLLSRNMEQIVITSD 683
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  945 NQETCESIlncaleelkqFRELQKPDRKLFgfrlpsktPSITSEAVVPEAGLVIDGKTLNAIFQGKLEKKFLELTQYCRS 1024
Cdd:TIGR01652  684 SLDATRSV----------EAAIKFGLEGTS--------EEFNNLGDSGNVALVIDGKSLGYALDEELEKEFLQLALKCKA 745
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1025 VLCCRSTPLQKSMIVKLVRDKLRVMTLSIGDGANDVSMIQAADIGIGISGQEGMQAVMSSDFAITRFKHLKKLLLVHGHW 1104
Cdd:TIGR01652  746 VICCRVSPSQKADVVRLVKKSTGKTTLAIGDGANDVSMIQEADVGVGISGKEGMQAVMASDFAIGQFRFLTKLLLVHGRW 825
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1105 CYSRLARMVVYYLYKNVCYVNLLFWYQFFCGFSSSTMIDYWQMIFFNLFFTSLPPLVFGVLDKDISAETLLALPELYKSG 1184
Cdd:TIGR01652  826 SYKRISKMILYFFYKNLIFAIIQFWYSFYNGFSGQTLYEGWYMVLYNVFFTALPVISLGVFDQDVSASLSLRYPQLYREG 905
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1185 QNSECYNLSTFWISMVDAFYQSLICFFIPYLAYKGSD------IDVFTF-GTPINTISLTTILLHQAMEMKTWTIFHGVV 1257
Cdd:TIGR01652  906 QKGQGFSTKTFWGWMLDGIYQSLVIFFFPMFAYILGDfvssgsVDDFSSvGVIVFTALVVIVNLKIALEINRWNWISLIT 985
                         1210      1220      1230      1240      1250      1260      1270
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1489866104 1258 LLGSFLMYFLvsllynATCVICNSPTNP--YWVMEGQLSNPTFYLVCFLTPVVALLPRYFFLSLQGTCGKSLISKAQ 1332
Cdd:TIGR01652  986 IWGSILVWLI------FVIVYSSIFPSPafYKAAPRVMGTFGFWLVLLVIVLISLLPRFTYKAIQRLFRPPDYDIVQ 1056
PLN03190 PLN03190
aminophospholipid translocase; Provisional
54-1314 0e+00

aminophospholipid translocase; Provisional


Pssm-ID: 215623 [Multi-domain]  Cd Length: 1178  Bit Score: 821.45  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104   54 IFHQDWEEVSRRY--PGNRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITMLPLAIVLFVIMI 131
Cdd:PLN03190    73 VYLNDPEKSNERFefAGNSIRTAKYSVFSFLPRNLFEQFHRVAYIYFLVIAVLNQLPQLAVFGRGASILPLAFVLLVTAV 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  132 KDGMEDFKRHRFDKAINCSNIRIYERKEqtYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGET 211
Cdd:PLN03190   153 KDAYEDWRRHRSDRIENNRLAWVLVDDQ--FQEKKWKDIRVGEIIKIQANDTLPCDMVLLSTSDPTGVAYVQTINLDGES 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  212 NLKQRcvvkgFSQQEVQF---EPELFHNTIVCEKPNNHLNKFKGYMEhPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIY 288
Cdd:PLN03190   231 NLKTR-----YAKQETLSkipEKEKINGLIKCEKPNRNIYGFQANME-VDGKRLSLGPSNIILRGCELKNTAWAIGVAVY 304
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  289 AGHETKAMLNNSGPRYKRSKIERRMNIDIFFCIGILILMCLIGAVGHSIWNGT---------FEEHPPFDVPDA-NGSFL 358
Cdd:PLN03190   305 CGRETKAMLNNSGAPSKRSRLETRMNLEIIILSLFLIALCTIVSVCAAVWLRRhrdeldtipFYRRKDFSEGGPkNYNYY 384
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  359 PSALGGFYMFLTMIILLQVLIPISLYVSIELVKLGQVFFLSNDLDLYDEETDLSIQCRALNIAEDLGQIQYIFSDKTGTL 438
Cdd:PLN03190   385 GWGWEIFFTFLMSVIVFQIMIPISLYISMELVRVGQAYFMIRDDQMYDEASNSRFQCRALNINEDLGQIKYVFSDKTGTL 464
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  439 TENKMVFRRCTIMGSEYShqenakrletpkeldsDGEEWTQyqclsfsarwaQDPATMRSQKGAQPLRRSQSARVpiqgh 518
Cdd:PLN03190   465 TENKMEFQCASIWGVDYS----------------DGRTPTQ-----------NDHAGYSVEVDGKILRPKMKVKV----- 512
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  519 yrqrsmghressqppvafsssiekdvtpDKNLLTKVRDAalwletlSDSRPAKaslsttsSIADFFLALTICNsvmvstt 598
Cdd:PLN03190   513 ----------------------------DPQLLELSKSG-------KDTEEAK-------HVHDFFLALAACN------- 543
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  599 teprqrvTIKPSskalgtslekiqqlfqklkllslsqsfsstapsdtdlgeslganVATTDSDerddasvcsggdstddg 678
Cdd:PLN03190   544 -------TIVPI--------------------------------------------VVDDTSD----------------- 555
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  679 gyrssmwdqgdilesgsgtsleealeaPATDLARpefcYEAESPDEAALVHAAHAYSFTLVSRTPEQVTVRLpQGTCLTF 758
Cdd:PLN03190   556 ---------------------------PTVKLMD----YQGESPDEQALVYAAAAYGFMLIERTSGHIVIDI-HGERQRF 603
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  759 SLLCTLGFDSVRKRMSVVVRHPlTGEIVVYTKGADSVIMDLLEDpacvpDINMekklRKIRArTQKHLDLYARDGLRTLC 838
Cdd:PLN03190   604 NVLGLHEFDSDRKRMSVILGCP-DKTVKVFVKGADTSMFSVIDR-----SLNM----NVIRA-TEAHLHTYSSLGLRTLV 672
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  839 IAKKVVSEEDFRRWASFRREAEASLDNRDELLMETAQHLENQLTLLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDK 918
Cdd:PLN03190   673 VGMRELNDSEFEQWHFSFEAASTALIGRAALLRKVASNVENNLTILGASAIEDKLQQGVPEAIESLRTAGIKVWVLTGDK 752
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  919 QETAVNIAHSCRLLNQTDTVYTINTENQETCESILNCALEELKqfrelqkpdrKLFGFRLPSKTPSITSEAVVPEAGLVI 998
Cdd:PLN03190   753 QETAISIGYSSKLLTNKMTQIIINSNSKESCRKSLEDALVMSK----------KLTTVSGISQNTGGSSAAASDPVALII 822
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  999 DGKTLNAIFQGKLEKKFLELTQYCRSVLCCRSTPLQKSMIVKLVRDKLRVMTLSIGDGANDVSMIQAADIGIGISGQEGM 1078
Cdd:PLN03190   823 DGTSLVYVLDSELEEQLFQLASKCSVVLCCRVAPLQKAGIVALVKNRTSDMTLAIGDGANDVSMIQMADVGVGISGQEGR 902
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1079 QAVMSSDFAITRFKHLKKLLLVHGHWCYSRLARMVVYYLYKNVCYVNLLFWYQFFCGFSSSTMIDYWQMIFFNLFFTSLP 1158
Cdd:PLN03190   903 QAVMASDFAMGQFRFLVPLLLVHGHWNYQRMGYMILYNFYRNAVFVLVLFWYVLFTCFTLTTAINEWSSVLYSVIYTALP 982
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1159 PLVFGVLDKDISAETLLALPELYKSGQNSECYNLSTFWISMVDAFYQSLICFFIPYLAYKGSDIDVFTFGTPINTISLTT 1238
Cdd:PLN03190   983 TIVVGILDKDLSRRTLLKYPQLYGAGQRQEAYNSKLFWLTMIDTLWQSAVVFFVPLFAYWASTIDGSSIGDLWTLAVVIL 1062
                         1210      1220      1230      1240      1250      1260      1270
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1489866104 1239 ILLHQAMEMKTWT-IFHGvVLLGSFLMYFLVSLLYNATcvicnsPTNP-YWVMEGQLSNPTFYLVCFLTPVVALLPRY 1314
Cdd:PLN03190  1063 VNLHLAMDIIRWNwITHA-AIWGSIVATFICVIVIDAI------PTLPgYWAIFHIAKTGSFWLCLLAIVVAALLPRF 1133
P-type_ATPase_APLT cd07536
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ...
753-1211 9.20e-123

Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, Neo1p, and human ATP8A2, -9B, -10D, -11B, and -11C; Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. Yeast Dnf1 and Dnf2 mediate the transport of phosphatidylethanolamine, phosphatidylserine, and phosphatidylcholine from the outer to the inner leaflet of the plasma membrane. Mammalian ATP11C may selectively transports PS and PE from the outer leaflet of the plasma membrane to the inner leaflet. The yeast Neo1p localizes to the endoplasmic reticulum and the Golgi complex and plays a role in membrane trafficking within the endomembrane system. Human putative ATPase phospholipid transporting 9B, ATP9B, localizes to the trans-golgi network in a CDC50 protein-independent manner. It also includes Arabidopsis phospholipid flippases including ALA1, and Caenorhabditis elegans flippases, including TAT-1, the latter has been shown to facilitate the inward transport of phosphatidylserine. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319838 [Multi-domain]  Cd Length: 805  Bit Score: 403.13  E-value: 9.20e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  753 GTCLTFSLLCTLGFDSVRKRMSVVVRHPLTGEIVVYTKGADSVIMDLLEDPACVPDINmekklrkirartqKHLDLYARD 832
Cdd:cd07536    386 GQVLSFCILQLLEFTSDRKRMSVIVRDESTGEITLYMKGADVAISPIVSKDSYMEQYN-------------DWLEEECGE 452
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  833 GLRTLCIAKKVVSEEDFRRWASFRREAEASLDNRDELLMETAQHLENQLTLLGATGIEDRLQEGVPDTIATLREAGIQLW 912
Cdd:cd07536    453 GLRTLCVAKKALTENEYQEWESRYTEASLSLHDRSLRVAEVVESLERELELLGLTAIEDRLQAGVPETIETLRKAGIKIW 532
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  913 VLTGDKQETAVNIAHSCRLLNQTDTVYTINTEN-QETCESILNCALEELKQFRELQkpdrklfgfrlpsktpsitseavv 991
Cdd:cd07536    533 MLTGDKQETAICIAKSCHLVSRTQDIHLLRQDTsRGERAAITQHAHLELNAFRRKH------------------------ 588
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  992 pEAGLVIDGKTLNAIFQgKLEKKFLELTQYCRSVLCCRSTPLQKSMIVKLVRDKLRVMTLSIGDGANDVSMIQAADIGIG 1071
Cdd:cd07536    589 -DVALVIDGDSLEVALK-YYRHEFVELACQCPAVICCRVSPTQKARIVTLLKQHTGRRTLAIGDGGNDVSMIQAADCGVG 666
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1072 ISGQEGMQAVMSSDFAITRFKHLKKLLLVHGHWCYSRLARMVVYYLYKNVCYVNLLFWYQFFCGFSSSTMIDYWQMIFFN 1151
Cdd:cd07536    667 ISGKEGKQASLAADYSITQFRHLGRLLLVHGRNSYNRSAALGQYVFYKGLIISTIQAVFSFVFGFSGVPLFQGFLMVGYN 746
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1152 LFFTSLPPLVFgVLDKDISAETLLALPELYKSGQNSECYNLSTFWISMVDAFYQSLICFF 1211
Cdd:cd07536    747 VIYTMFPVFSL-VIDQDVKPESAMLYPQLYKDLQKGRSLNFKTFLGWVLISLYHGGILFY 805
PhoLip_ATPase_C pfam16212
Phospholipid-translocating P-type ATPase C-terminal; PhoLip_ATPase_C is found at the ...
1081-1320 4.54e-107

Phospholipid-translocating P-type ATPase C-terminal; PhoLip_ATPase_C is found at the C-terminus of a number of phospholipid-translocating ATPases. It is found in higher eukaryotes.


Pssm-ID: 465071 [Multi-domain]  Cd Length: 250  Bit Score: 339.87  E-value: 4.54e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1081 VMSSDFAITRFKHLKKLLLVHGHWCYSRLARMVVYYLYKNVCYVNLLFWYQFFCGFSSSTMIDYWQMIFFNLFFTSLPPL 1160
Cdd:pfam16212    1 ARASDYAIAQFRFLKRLLLVHGRWSYRRTSKLILYFFYKNIVFTLTQFWYQFYNGFSGQSLYESWYLTLYNLLFTSLPVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1161 VFGVLDKDISAETLLALPELYKSGQNSECYNLSTFWISMVDAFYQSLICFFIPYLAY------KGSDIDVFTFGTPINTI 1234
Cdd:pfam16212   81 VLGIFDQDVSAETLLAYPELYKLGQKNKFFNLKTFLGWMLDGIYQSLIIFFIPYLAYgdsvfsGGKDADLWAFGTTVFTA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1235 SLTTILLHQAMEMKTWTIFHGVVLLGSFLMYFLVSLLYNATCVICNSptNPYWVMEGQLSNPTFYLVCFLTPVVALLPRY 1314
Cdd:pfam16212  161 LVLVVNLKLALETHYWTWITHLAIWGSILLYFLFTLIYSSIYPSSYS--VFYGVASRLFGSPSFWLTLLLIVVVALLPDF 238

                   ....*.
gi 1489866104 1315 FFLSLQ 1320
Cdd:pfam16212  239 AYKALK 244
P-type_ATPase_APLT cd07536
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ...
69-459 5.88e-93

Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, Neo1p, and human ATP8A2, -9B, -10D, -11B, and -11C; Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. Yeast Dnf1 and Dnf2 mediate the transport of phosphatidylethanolamine, phosphatidylserine, and phosphatidylcholine from the outer to the inner leaflet of the plasma membrane. Mammalian ATP11C may selectively transports PS and PE from the outer leaflet of the plasma membrane to the inner leaflet. The yeast Neo1p localizes to the endoplasmic reticulum and the Golgi complex and plays a role in membrane trafficking within the endomembrane system. Human putative ATPase phospholipid transporting 9B, ATP9B, localizes to the trans-golgi network in a CDC50 protein-independent manner. It also includes Arabidopsis phospholipid flippases including ALA1, and Caenorhabditis elegans flippases, including TAT-1, the latter has been shown to facilitate the inward transport of phosphatidylserine. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319838 [Multi-domain]  Cd Length: 805  Bit Score: 319.55  E-value: 5.88e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104   69 NRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITMLPLAIVLFVIMIKDGMEDFKRHRFDKAIN 148
Cdd:cd07536      2 NSISNQKYNVFTFLPGVLYEQFKRFLNLYFLVIACLQFVPALKPGYLYTTWAPLIFILAVTMTKEAIDDFRRFQRDKEVN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  149 CSniRIYERKEQTYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVkgfsqQEVQ 228
Cdd:cd07536     82 KK--QLYSKLTGRKVQIKSSDIQVGDIVIVEKNQRIPSDMVLLRTSEPQGSCYVETAQLDGETDLKLRVAV-----SCTQ 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  229 FEPELFH-----NTIVCEKPNNHLNKFKGYM--EHPD-QTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKAMLNNS 300
Cdd:cd07536    155 QLPALGDlmkisAYVECQKPQMDIHSFEGNFtlEDSDpPIHESLSIENTLLRASTLRNTGWVIGVVVYTGKETKLVMNTS 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  301 GPRYKRSKIERRMNIDIFFCIGILILMCLIGAVGHSIWNGTFEEHPPFDVPDANGSFlpsalGGFYMFLTMIILLQVLIP 380
Cdd:cd07536    235 NAKNKVGLLDLELNRLTKALFLALVVLSLVMVTLQGFWGPWYGEKNWYIKKMDTTSD-----NFGRNLLRFLLLFSYIIP 309
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1489866104  381 ISLYVSIELVKLGQVFFLSNDLDLYDEETDLSIQCRALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYSHQE 459
Cdd:cd07536    310 ISLRVNLDMVKAVYAWFIMWDENMYYIGNDTGTVARTSTIPEELGQVVYLLTDKTGTLTQNEMIFKRCHIGGVSYGGQV 388
P-type_ATPase_APLT_Neo1-like cd07541
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Neo1p and human ...
753-1216 2.19e-90

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: 312.04  E-value: 2.19e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  753 GTCLTFSLLCTLGFDSVRKRMSVVVRHPLTGEIVVYTKGADSVIMDLLE-----DPACVpdiNMekklrkirartqkhld 827
Cdd:cd07541    356 GQNLNYEILQIFPFTSESKRMGIIVREEKTGEITFYMKGADVVMSKIVQyndwlEEECG---NM---------------- 416
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  828 lyARDGLRTLCIAKKVVSEEDFRRWASFRREAEASLDNRDELLMETAQHLENQLTLLGATGIEDRLQEGVPDTIATLREA 907
Cdd:cd07541    417 --AREGLRTLVVAKKKLSEEEYQAFEKRYNAAKLSIHDRDLKVAEVVESLERELELLCLTGVEDKLQEDVKPTLELLRNA 494
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  908 GIQLWVLTGDKQETAVNIAHSCRLLNQTDTVYTINTEnqetceSILNCALEELKQFRelQKPDrklfgfrlpsktpsits 987
Cdd:cd07541    495 GIKIWMLTGDKLETATCIAKSSKLVSRGQYIHVFRKV------TTREEAHLELNNLR--RKHD----------------- 549
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  988 eavvpeAGLVIDGKTLNaIFQGKLEKKFLELTQYCRSVLCCRSTPLQKSMIVKLVRDKLRVMTLSIGDGANDVSMIQAAD 1067
Cdd:cd07541    550 ------CALVIDGESLE-VCLKYYEHEFIELACQLPAVVCCRCSPTQKAQIVRLIQKHTGKRTCAIGDGGNDVSMIQAAD 622
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1068 IGIGISGQEGMQAVMSSDFAITRFKHLKKLLLVHGHWCYSRLARMVVYYLYKNVCY--VNLLFWYQFFcgFSSSTMIDYW 1145
Cdd:cd07541    623 VGVGIEGKEGKQASLAADFSITQFSHIGRLLLWHGRNSYKRSAKLAQFVMHRGLIIsiMQAVFSSVFY--FAPIALYQGF 700
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1489866104 1146 QMIFFNLFFTSLPplVFG-VLDKDISAETLLALPELYKSGQNSECYNLSTFWISMVDAFYQSLIcffIPYLA 1216
Cdd:cd07541    701 LMVGYSTIYTMAP--VFSlVLDQDVSEELAMLYPELYKELTKGRSLSYKTFFIWVLISIYQGGI---IMYGA 767
P-type_ATPase_APLT_Neo1-like cd07541
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Neo1p and human ...
69-447 5.58e-53

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: 200.71  E-value: 5.58e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104   69 NRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITMLPLAIVLFVIMIKDGMEDFKRHRFDKAIN 148
Cdd:cd07541      2 NEVRNQKYNIFTFLPKVLYEQFKFFYNLYFLVVALSQFVPALKIGYLYTYWAPLGFVLAVTMAKEAVDDIRRRRRDKEQN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  149 csniriYERKEQ--TYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVkGFSQQe 226
Cdd:cd07541     82 ------YEKLTVrgETVEIPSSDIKVGDLIIVEKNQRIPADMVLLRTSEKSGSCFIRTDQLDGETDWKLRIAV-PCTQK- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  227 VQFEPELFH-NTIVCEKPNNHLNKFKG-YMEHPDQTRTGFGCESLLLrGCTIRNTEMAVGIVIYAGHETKAMLNNSGPRY 304
Cdd:cd07541    154 LPEEGILNSiSAVYAEAPQKDIHSFYGtFTINDDPTSESLSVENTLW-ANTVVASGTVIGVVVYTGKETRSVMNTSQPKN 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  305 KRSKIERRMN--IDIFFC--IGILILMCLIGAVGHSiWngtfeehppfdvpdangsflpsalggfYMFLT-MIILLQVLI 379
Cdd:cd07541    233 KVGLLDLEINflTKILFCavLALSIVMVALQGFQGP-W---------------------------YIYLFrFLILFSSII 284
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1489866104  380 PISLYVSIELVKLGQVFFLSNDLDLydEETDLsiqcRALNIAEDLGQIQYIFSDKTGTLTENKMVFRR 447
Cdd:cd07541    285 PISLRVNLDMAKIVYSWQIEHDKNI--PGTVV----RTSTIPEELGRIEYLLSDKTGTLTQNEMVFKK 346
ATPase_P-type TIGR01494
ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large ...
117-456 4.87e-46

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: 175.20  E-value: 4.87e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  117 ITMLPLAIVLFVIMIKDGMEDFKRHRFDKAINCSNIRIYeRKEQTYVQKcwKDVRVGDFIQMKCNEIVPADILLLFSSdp 196
Cdd:TIGR01494    2 ILFLVLLFVLLEVKQKLKAEDALRSLKDSLVNTATVLVL-RNGWKEISS--KDLVPGDVVLVKSGDTVPADGVLLSGS-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  197 ngiCHLETASLDGETNLKQRCVVKGfsqqevqfepelfhntivCEKPNNHLNKFKGYMEHpdQTRTGFGCeslllrgcti 276
Cdd:TIGR01494   77 ---AFVDESSLTGESLPVLKTALPD------------------GDAVFAGTINFGGTLIV--KVTATGIL---------- 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  277 rNTEMAVGIVIYAGHETKAMLNNsgpryKRSKIERrmniDIFFCIGILILMCLIGAVGHSIWNGTfeehppfdvpdangs 356
Cdd:TIGR01494  124 -TTVGKIAVVVYTGFSTKTPLQS-----KADKFEN----FIFILFLLLLALAVFLLLPIGGWDGN--------------- 178
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  357 flpsalGGFYMFLTMIILLQVLIPISLYVSIELVKLGQvfflsnDLDLYDEetdlSIQCRALNIAEDLGQIQYIFSDKTG 436
Cdd:TIGR01494  179 ------SIYKAILRALAVLVIAIPCALPLAVSVALAVG------DARMAKK----GILVKNLNALEELGKVDVICFDKTG 242
                          330       340
                   ....*....|....*....|
gi 1489866104  437 TLTENKMVFRRCTIMGSEYS 456
Cdd:TIGR01494  243 TLTTNKMTLQKVIIIGGVEE 262
ATPase_P-type TIGR01494
ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large ...
717-1124 2.60e-32

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: 133.98  E-value: 2.60e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  717 YEAESPDEAALVHAAHaysftlvsrtpeqvTVRLPQGTCLTFSLLCTLGFDSVRKRMSVVVRHPlTGEIVVYTKGADSVI 796
Cdd:TIGR01494  276 YLSGHPLERAIVKSAE--------------GVIKSDEINVEYKILDVFPFSSVLKRMGVIVEGA-NGSDLLFVKGAPEFV 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  797 MDLLEDPACVpdinmekklrkirartQKHLDLYARDGLRTLCIAKKvvseedfrrwasfrreaeasldnrdellmetaqH 876
Cdd:TIGR01494  341 LERCNNENDY----------------DEKVDEYARQGLRVLAFASK---------------------------------K 371
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  877 LENQLTLLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDKQETAVNIAHSCRLlnqtdtvytintenqetcesilnca 956
Cdd:TIGR01494  372 LPDDLEFLGLLTFEDPLRPDAKETIEALRKAGIKVVMLTGDNVLTAKAIAKELGI------------------------- 426
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  957 leelkqfrelqkpdrklfgfrlpsktpsitseavvpeaglvidgktlnaifqgklekkfleltqycrsVLCCRSTPLQKS 1036
Cdd:TIGR01494  427 --------------------------------------------------------------------DVFARVKPEEKA 438
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1037 MIVKLVRDKLRVmTLSIGDGANDVSMIQAADIGIGISGqeGMQAVMSSDFAITRFK-HLKKLLLVHGHWCYSRlarmvvy 1115
Cdd:TIGR01494  439 AIVEALQEKGRT-VAMTGDGVNDAPALKKADVGIAMGS--GDVAKAAADIVLLDDDlSTIVEAVKEGRKTFSN------- 508

                   ....*....
gi 1489866104 1116 yLYKNVCYV 1124
Cdd:TIGR01494  509 -IKKNIFWA 516
P-type_ATPase_Ca_PMCA-like cd02081
animal plasma membrane Ca2(+)-ATPases (PMCA), similar to human ATP2B1-4/PMCA1-4, and related ...
760-1076 1.13e-30

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


Pssm-ID: 319776 [Multi-domain]  Cd Length: 721  Bit Score: 130.79  E-value: 1.13e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  760 LLCTLGFDSVRKRMSVVVRHPlTGEIVVYTKGADSVIMDLLE---DPACVPDINMEKKLRKIRARTQKhldlYARDGLRT 836
Cdd:cd02081    368 VLKVYPFNSARKRMSTVVRLK-DGGYRLYVKGASEIVLKKCSyilNSDGEVVFLTSEKKEEIKRVIEP----MASDSLRT 442
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  837 LCIAKKVVSEEDfrrwasfRREAEASLDNRDELlmetaqhlENQLTLLGATGIEDRLQEGVPDTIATLREAGIQLWVLTG 916
Cdd:cd02081    443 IGLAYRDFSPDE-------EPTAERDWDDEEDI--------ESDLTFIGIVGIKDPLRPEVPEAVAKCQRAGITVRMVTG 507
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  917 DKQETAVNIAHSCRLLnqtdtvytintenQETCESIlncALEElKQFRELqkpdrklfgfrlpsktpsitseavvpeagl 996
Cdd:cd02081    508 DNINTARAIARECGIL-------------TEGEDGL---VLEG-KEFREL------------------------------ 540
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  997 vIDGKtLNAIFQGKLEKKFLELtqycrSVLcCRSTPLQKSMIVKLVRDKLRVMTLSiGDGANDVSMIQAADIGI--GISG 1074
Cdd:cd02081    541 -IDEE-VGEVCQEKFDKIWPKL-----RVL-ARSSPEDKYTLVKGLKDSGEVVAVT-GDGTNDAPALKKADVGFamGIAG 611

                   ..
gi 1489866104 1075 QE 1076
Cdd:cd02081    612 TE 613
P-type_ATPases cd01431
ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, ...
766-1153 1.48e-30

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: 123.72  E-value: 1.48e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  766 FDSVRKRMSVVVRHPltGEIVVYTKGADSVIMDLLEDPAcvPDINMEKKLRKIrartqkhlDLYARDGLRTLCIAKKVVS 845
Cdd:cd01431     27 FNSTRKRMSVVVRLP--GRYRAIVKGAPETILSRCSHAL--TEEDRNKIEKAQ--------EESAREGLRVLALAYREFD 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  846 EEDfrrwasfrreaeasldnrdellmeTAQHLENQLTLLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDKQETAVNI 925
Cdd:cd01431     95 PET------------------------SKEAVELNLVFLGLIGLQDPPRPEVKEAIAKCRTAGIKVVMITGDNPLTAIAI 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  926 AHSCRLLNQTDTVYTInTENQETCESILNCALEElkqfrelqkpdrklfgfrlpsktpsitseavvpeaglvidgktlNA 1005
Cdd:cd01431    151 AREIGIDTKASGVILG-EEADEMSEEELLDLIAK--------------------------------------------VA 185
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1006 IFqgklekkfleltqycrsvlcCRSTPLQKSMIVKLVRDKLRVmTLSIGDGANDVSMIQAADIGIGIsGQEGMQAVM-SS 1084
Cdd:cd01431    186 VF--------------------ARVTPEQKLRIVKALQARGEV-VAMTGDGVNDAPALKQADVGIAM-GSTGTDVAKeAA 243
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1489866104 1085 DFAITrFKHLKKLL--LVHGHWCYSRLARMVVYYLYKNVCYVNLLFWYQFFCGFSS-STMIDYWQMIFFNLF 1153
Cdd:cd01431    244 DIVLL-DDNFATIVeaVEEGRAIYDNIKKNITYLLANNVAEVFAIALALFLGGPLPlLAFQILWINLVTDLI 314
MgtA COG0474
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism];
722-1074 5.71e-30

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


Pssm-ID: 440242 [Multi-domain]  Cd Length: 874  Bit Score: 129.07  E-value: 5.71e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  722 PDEAALVHAAHAYSFTLVSRTPEqvtvrlpqgtcltFSLLCTLGFDSVRKRMSVVVRHPlTGEIVVYTKGADSVIMDL-- 799
Cdd:COG0474    385 PTEGALLVAAAKAGLDVEELRKE-------------YPRVDEIPFDSERKRMSTVHEDP-DGKRLLIVKGAPEVVLALct 450
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  800 -LEDPACVPDINMEkklrkIRARTQKHLDLYARDGLRTLCIAKKVVSEEDFrrwasfrreaeasldnrdellmETAQHLE 878
Cdd:COG0474    451 rVLTGGGVVPLTEE-----DRAEILEAVEELAAQGLRVLAVAYKELPADPE----------------------LDSEDDE 503
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  879 NQLTLLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDKQETAVNIAHSCRLLNQTDTVYTIntenqetcesilncale 958
Cdd:COG0474    504 SDLTFLGLVGMIDPPRPEAKEAIAECRRAGIRVKMITGDHPATARAIARQLGLGDDGDRVLTG----------------- 566
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  959 elkqfRELQK-PDRKLfgfrlpsktpsitsEAVVPEAglvidgktlnAIFqgklekkfleltqycrsvlcCRSTPLQKSM 1037
Cdd:COG0474    567 -----AELDAmSDEEL--------------AEAVEDV----------DVF--------------------ARVSPEHKLR 597
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1489866104 1038 IVKLVRDKLRV--MTlsiGDGANDVSMIQAADIGI--GISG 1074
Cdd:COG0474    598 IVKALQANGHVvaMT---GDGVNDAPALKAADIGIamGITG 635
PhoLip_ATPase_N pfam16209
Phospholipid-translocating ATPase N-terminal; PhoLip_ATPase_N is found at the N-terminus of a ...
48-119 1.65e-24

Phospholipid-translocating ATPase N-terminal; PhoLip_ATPase_N is found at the N-terminus of a number of phospholipid-translocating ATPases. It is found in higher eukaryotes.


Pssm-ID: 465069 [Multi-domain]  Cd Length: 67  Bit Score: 97.93  E-value: 1.65e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1489866104   48 VFPNNSIFHQDweevsRRYPGNRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITM 119
Cdd:pfam16209    1 VYINDPEKNSE-----FKYPSNKISTSKYTLLTFLPKNLFEQFRRVANLYFLLIAILQLIPGISPTGPYTTI 67
P-type_ATPase_Ca_prok cd02089
prokaryotic P-type Ca(2+)-ATPase similar to Synechococcus elongatus sp. strain PCC 7942 PacL ...
722-1076 1.04e-21

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: 101.92  E-value: 1.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  722 PDEAALVHAAHAYSFTLvsRTPEQVTVRLPQgtcltfsllctLGFDSVRKRMSVVvrHPLTGEIVVYTKGADSVimdLLE 801
Cdd:cd02089    326 PTETALIRAARKAGLDK--EELEKKYPRIAE-----------IPFDSERKLMTTV--HKDAGKYIVFTKGAPDV---LLP 387
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  802 DPACVPDINMEKKL-RKIRARTQKHLDLYARDGLRTLCIAkkvvseedFRRWasfrreaeasldnrDELLMETAQHLENQ 880
Cdd:cd02089    388 RCTYIYINGQVRPLtEEDRAKILAVNEEFSEEALRVLAVA--------YKPL--------------DEDPTESSEDLEND 445
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  881 LTLLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDKQETAVNIAhscrllnqtdtvytintenqetcesilncaleel 960
Cdd:cd02089    446 LIFLGLVGMIDPPRPEVKDAVAECKKAGIKTVMITGDHKLTARAIA---------------------------------- 491
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  961 kqfRELqkpdrklfgfrlpsktpsitseAVVPEAGLVIDGKTLNAIFQGKLEKKFLELTQYcrsvlcCRSTPLQKSMIVK 1040
Cdd:cd02089    492 ---KEL----------------------GILEDGDKALTGEELDKMSDEELEKKVEQISVY------ARVSPEHKLRIVK 540
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1489866104 1041 LVRDKLRV--MTlsiGDGANDVSMIQAADIGI--GISGQE 1076
Cdd:cd02089    541 ALQRKGKIvaMT---GDGVNDAPALKAADIGVamGITGTD 577
P-ATPase-V TIGR01657
P-type ATPase of unknown pump specificity (type V); These P-type ATPases form a distinct clade ...
766-1272 4.77e-20

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: 97.05  E-value: 4.77e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  766 FDSVRKRMSVVVRHPLTGEIVVYTKGADSVIMDLLeDPACVPdinmekklrkirARTQKHLDLYARDGLRTLCIAKKVVS 845
Cdd:TIGR01657  560 FSSALQRMSVIVSTNDERSPDAFVKGAPETIQSLC-SPETVP------------SDYQEVLKSYTREGYRVLALAYKELP 626
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  846 eedfrrwasfRREAEASLD-NRDELlmetaqhlENQLTLLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDKQETAVN 924
Cdd:TIGR01657  627 ----------KLTLQKAQDlSRDAV--------ESNLTFLGFIVFENPLKPDTKEVIKELKRASIRTVMITGDNPLTAVH 688
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  925 IAHSCRLLNQTDTVYTINTENQETCESilncaleELKQFRELQKPDRKLFGFRLPSKTPSITSE-AVVPEAGLVIDGKTL 1003
Cdd:TIGR01657  689 VARECGIVNPSNTLILAEAEPPESGKP-------NQIKFEVIDSIPFASTQVEIPYPLGQDSVEdLLASRYHLAMSGKAF 761
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1004 nAIFQGKLEKKFLELTQYCRsVLcCRSTPLQKSMIVKLVRdKLRVMTLSIGDGANDVSMIQAADIGIGISGQEgmqAVMS 1083
Cdd:TIGR01657  762 -AVLQAHSPELLLRLLSHTT-VF-ARMAPDQKETLVELLQ-KLDYTVGMCGDGANDCGALKQADVGISLSEAE---ASVA 834
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1084 SDFA--ITRFKHLKKLL------LVHGHWCYSRLArmvvyyLYKNVCYVNLLFWYQFFCGFSSStmidywQMIFFNLFFT 1155
Cdd:TIGR01657  835 APFTskLASISCVPNVIregrcaLVTSFQMFKYMA------LYSLIQFYSVSILYLIGSNLGDG------QFLTIDLLLI 902
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1156 SLPPLVFG------VLDKDISAETLLALpelyksgqnsecYNLSTFWISMVDAFYQSLICFFI-----PYLAYKGSDIDV 1224
Cdd:TIGR01657  903 FPVALLMSrnkplkKLSKERPPSNLFSV------------YILTSVLIQFVLHILSQVYLVFElhaqpWYKPENPVDLEK 970
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1489866104 1225 FTF----GTPINTISL-----TTILLHQAMEMKT--WTIFHGVVLLGSFLMYFLVSLLY 1272
Cdd:TIGR01657  971 ENFpnllNTVLFFVSSfqyliTAIVNSKGPPFREpiYKNKPFVYLLITGLGLLLVLLLD 1029
P-type_ATPase_cation cd07542
P-type cation-transporting ATPases, similar to human ATPase type 13A2 (ATP13A2) protein and ...
754-1076 5.48e-17

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: 86.92  E-value: 5.48e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  754 TCLTFSLLCTLGFDSVRKRMSVVVRHPLTGEIVVYTKGADSVIMDLLeDPACVPDiNMEKKLRKirartqkhldlYARDG 833
Cdd:cd07542    385 TGWSLEILRQFPFSSALQRMSVIVKTPGDDSMMAFTKGAPEMIASLC-KPETVPS-NFQEVLNE-----------YTKQG 451
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  834 LRTLCIAKKvvseedfrrwasfrreaeaSLDNRDELLMETAQH-LENQLTLLGATGIEDRLQEGVPDTIATLREAGIQLW 912
Cdd:cd07542    452 FRVIALAYK-------------------ALESKTWLLQKLSREeVESDLEFLGLIVMENRLKPETAPVINELNRANIRTV 512
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  913 VLTGDKQETAVNIAHSCRLLNQTDTVYTIntenqetcesilncaleelkqfrelqkpdrklfgfrlpsktpsitsEAVVP 992
Cdd:cd07542    513 MVTGDNLLTAISVARECGMISPSKKVILI----------------------------------------------EAVKP 546
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  993 EAGlvidgktlnaiFQGKLEKKFLeltqyCRSVLCCRSTPLQKSMIVKLVRdKLRVMTLSIGDGANDVSMIQAADIGIGI 1072
Cdd:cd07542    547 EDD-----------DSASLTWTLL-----LKGTVFARMSPDQKSELVEELQ-KLDYTVGMCGDGANDCGALKAADVGISL 609

                   ....
gi 1489866104 1073 SGQE 1076
Cdd:cd07542    610 SEAE 613
P-type_ATPase cd07539
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ...
766-1121 6.88e-15

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: 79.77  E-value: 6.88e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  766 FDSVRKRMSVVVRHPlTGEIVVYTKGADSVIMdlledPAC---VPDINMEKKLRKIRARTQKHLDLYARDGLRTLCIAKK 842
Cdd:cd07539    329 FESSRGYAAAIGRTG-GGIPLLAVKGAPEVVL-----PRCdrrMTGGQVVPLTEADRQAIEEVNELLAGQGLRVLAVAYR 402
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  843 vvseedfrrwasfrreaeaSLDNRDELLMETAqhlENQLTLLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDKQETA 922
Cdd:cd07539    403 -------------------TLDAGTTHAVEAV---VDDLELLGLLGLADTARPGAAALIAALHDAGIDVVMITGDHPITA 460
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  923 VNIAhscrllnqtdtvytintenqetcesilncaleelkqfRELQkpdrklfgfrlpsktpsitseavVPEAGLVIDGKT 1002
Cdd:cd07539    461 RAIA-------------------------------------KELG-----------------------LPRDAEVVTGAE 480
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1003 LNAIFQGKLEKKFLELTQYcrsvlcCRSTPLQKSMIVKLVRDKLRV--MTlsiGDGANDVSMIQAADIGIGISGQEGMQA 1080
Cdd:cd07539    481 LDALDEEALTGLVADIDVF------ARVSPEQKLQIVQALQAAGRVvaMT---GDGANDAAAIRAADVGIGVGARGSDAA 551
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1489866104 1081 VMSSDFAITRfKHLKKLL--LVHGHWCYSRLARMVVYYLYKNV 1121
Cdd:cd07539    552 REAADLVLTD-DDLETLLdaVVEGRTMWQNVRDAVHVLLGGNL 593
P-type_ATPase_Na_ENA cd02086
fungal-type Na(+)-ATPase, similar to the plasma membrane sodium transporters Saccharomyces ...
749-1127 1.00e-14

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: 79.81  E-value: 1.00e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  749 RLPQGTCLTFSLLCTLGFDSVRKRMSVVVRHPLTGEIVVYTKGADSVIMdlledPACVpdiNMEKKLRKI------RART 822
Cdd:cd02086    394 ALTKGGSAQFQHVAEFPFDSTVKRMSVVYYNNQAGDYYAYMKGAVERVL-----ECCS---SMYGKDGIIplddefRKTI 465
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  823 QKHLDLYARDGLRTLCIAKKVVSEEDFrrwasfrreaEASLDNRDELLMETAqhlENQLTLLGATGIEDRLQEGVPDTIA 902
Cdd:cd02086    466 IKNVESLASQGLRVLAFASRSFTKAQF----------NDDQLKNITLSRADA---ESDLTFLGLVGIYDPPRNESAGAVE 532
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  903 TLREAGIQLWVLTGDKQETAVNIAhscrllnqtdtvytintenqetCE-SILNcaleelkqfrelqkpdrklfgfrlpsk 981
Cdd:cd02086    533 KCHQAGITVHMLTGDHPGTAKAIA----------------------REvGILP--------------------------- 563
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  982 tPSITSEAVVPEAGLVIDGktlnAIFQGKLEKKFLELTQYCrsVLCCRSTPLQK-SMIVKL-VRDKLRVMTlsiGDGAND 1059
Cdd:cd02086    564 -PNSYHYSQEIMDSMVMTA----SQFDGLSDEEVDALPVLP--LVIARCSPQTKvRMIEALhRRKKFCAMT---GDGVND 633
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1489866104 1060 VSMIQAADIGIGIsGQEGMQ-AVMSSDFAIT--RFKHLKKlLLVHGHWCYSRLARMVVYYLYKNVCYVNLL 1127
Cdd:cd02086    634 SPSLKMADVGIAM-GLNGSDvAKDASDIVLTddNFASIVN-AIEEGRRMFDNIQKFVLHLLAENVAQVILL 702
P-type_ATPase_SERCA cd02083
sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; ...
761-1076 1.21e-13

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: 76.18  E-value: 1.21e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  761 LCTLGFDSVRKRMSVVVRHPLTGE-IVVYTKGA-DSVI----MDLLEDPACVP-DINMEKKLrkirartQKHLDLYARDG 833
Cdd:cd02083    476 EFTLEFSRDRKSMSVYCSPTKASGgNKLFVKGApEGVLerctHVRVGGGKVVPlTAAIKILI-------LKKVWGYGTDT 548
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  834 LRTLCIAKKvvseedfrrwasfrreaEASLDNRDELLMETAQ--HLENQLTLLGATGIEDRLQEGVPDTIATLREAGIQL 911
Cdd:cd02083    549 LRCLALATK-----------------DTPPKPEDMDLEDSTKfyKYETDLTFVGVVGMLDPPRPEVRDSIEKCRDAGIRV 611
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  912 WVLTGDKQETAVNIahsCRLLNqtdtvytINTENqetcESILNCALEElKQFRELqkpdrklfgfrlpskTPSITSEAVV 991
Cdd:cd02083    612 IVITGDNKGTAEAI---CRRIG-------IFGED----EDTTGKSYTG-REFDDL---------------SPEEQREACR 661
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  992 peaglvidgktlnaifqgklekkfleltqycRSVLCCRSTPLQKSMIVKLVRDKLRV--MTlsiGDGANDVSMIQAADIG 1069
Cdd:cd02083    662 -------------------------------RARLFSRVEPSHKSKIVELLQSQGEItaMT---GDGVNDAPALKKAEIG 707

                   ....*...
gi 1489866104 1070 IGI-SGQE 1076
Cdd:cd02083    708 IAMgSGTA 715
P-type_ATPase_Mg cd02077
magnesium transporting ATPase (MgtA), similar to Escherichia coli MgtA and Salmonella ...
766-1070 7.51e-13

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: 73.44  E-value: 7.51e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  766 FDSVRKRMSVVVRHPlTGEIVVYTKGADSVIMDL----LEDPACVPDINMEKklRKIRARTQKhldlYARDGLRTLCIAK 841
Cdd:cd02077    385 FDFERRRMSVVVKDN-DGKHLLITKGAVEEILNVcthvEVNGEVVPLTDTLR--EKILAQVEE----LNREGLRVLAIAY 457
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  842 KVVSeedfrrwasfRREAEASLDNrdellmetaqhlENQLTLLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDKQET 921
Cdd:cd02077    458 KKLP----------APEGEYSVKD------------EKELILIGFLAFLDPPKESAAQAIKALKKNGVNVKILTGDNEIV 515
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  922 AVNIahsCRLLNqtdtvytINTENQETCESILNCALEELKqfRELQKpdrklfgfrlpsktpsitseavvpeaglvidgk 1001
Cdd:cd02077    516 TKAI---CKQVG-------LDINRVLTGSEIEALSDEELA--KIVEE--------------------------------- 550
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1489866104 1002 tlNAIFqGKLekkfleltqycrsvlccrsTPLQKSMIVKLVRDKLRVMTLsIGDGANDVSMIQAADIGI 1070
Cdd:cd02077    551 --TNIF-AKL-------------------SPLQKARIIQALKKNGHVVGF-MGDGINDAPALRQADVGI 596
P-type_ATPase_cation cd02080
P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, ...
722-1076 4.25e-12

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: 71.14  E-value: 4.25e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  722 PDEAALVHAAHAYSFTlvsrtPEQVTVRLPQgtcltfslLCTLGFDSVRKRMSVvvRHPLTGEIVVYTKGADSVIMDLle 801
Cdd:cd02080    342 PTEGALLVLAAKAGLD-----PDRLASSYPR--------VDKIPFDSAYRYMAT--LHRDDGQRVIYVKGAPERLLDM-- 404
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  802 dpaCVPDINMEKKLRKIRARTQKHLDLYARDGLRTLCIAKKVVSEEdfrrwasfrreaEASLDNRDellmetaqhLENQL 881
Cdd:cd02080    405 ---CDQELLDGGVSPLDRAYWEAEAEDLAKQGLRVLAFAYREVDSE------------VEEIDHAD---------LEGGL 460
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  882 TLLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDKQETAVNIAHSCRLLNQTDtvytintenqetcesilncaleelk 961
Cdd:cd02080    461 TFLGLQGMIDPPRPEAIAAVAECQSAGIRVKMITGDHAETARAIGAQLGLGDGKK------------------------- 515
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  962 qfrelqkpdrklfgfrlpsktpsitseavvpeaglVIDGKTLNAIFQGKLEKKFLEltqycRSVLcCRSTPLQKSMIVKL 1041
Cdd:cd02080    516 -----------------------------------VLTGAELDALDDEELAEAVDE-----VDVF-ARTSPEHKLRLVRA 554
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1489866104 1042 V--RDKLRVMTlsiGDGANDVSMIQAADIGI--GISGQE 1076
Cdd:cd02080    555 LqaRGEVVAMT---GDGVNDAPALKQADIGIamGIKGTE 590
PRK10517 PRK10517
magnesium-transporting P-type ATPase MgtA;
766-1074 8.22e-09

magnesium-transporting P-type ATPase MgtA;


Pssm-ID: 236705 [Multi-domain]  Cd Length: 902  Bit Score: 60.47  E-value: 8.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  766 FDSVRKRMSVVVRHPLTGEIVVyTKGAD----SVIMDLLEDPACVP-DINMekkLRKIRARTQKhldlYARDGLRTLCIA 840
Cdd:PRK10517   449 FDFERRRMSVVVAENTEHHQLI-CKGALeeilNVCSQVRHNGEIVPlDDIM---LRRIKRVTDT----LNRQGLRVVAVA 520
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  841 KKVVSEedfrrwasfRREAEASLDnrdellmetaqhlENQLTLLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDKQE 920
Cdd:PRK10517   521 TKYLPA---------REGDYQRAD-------------ESDLILEGYIAFLDPPKETTAPALKALKASGVTVKILTGDSEL 578
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  921 TAvniAHSCRllnqtdtvytintenqetcesilncaleelkqfrelqkpdrklfgfrlpsktpsitseavvpEAGLVIDG 1000
Cdd:PRK10517   579 VA---AKVCH--------------------------------------------------------------EVGLDAGE 593
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1489866104 1001 KTLNAIFQGKLEKKFLELTQycRSVLCCRSTPLQKSMIVKLVRDKLRVMTLsIGDGANDVSMIQAADIGIGISG 1074
Cdd:PRK10517   594 VLIGSDIETLSDDELANLAE--RTTLFARLTPMHKERIVTLLKREGHVVGF-MGDGINDAPALRAADIGISVDG 664
Cation_ATPase pfam13246
Cation transport ATPase (P-type); This domain is found in cation transport ATPases, including ...
721-798 8.49e-09

Cation transport ATPase (P-type); This domain is found in cation transport ATPases, including phospholipid-transporting ATPases, calcium-transporting ATPases, and sodium-potassium ATPases.


Pssm-ID: 463817 [Multi-domain]  Cd Length: 91  Bit Score: 54.15  E-value: 8.49e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1489866104  721 SPDEAALVHAAHAYSFtLVSRTPEQvtvrlpqgtcltFSLLCTLGFDSVRKRMSVVVRHPLTGEIVVYTKGADSVIMD 798
Cdd:pfam13246   22 DPTESALLVFAEKMGI-DVEELRKD------------YPRVAEIPFNSDRKRMSTVHKLPDDGKYRLFVKGAPEIILD 86
P-type_ATPase_SPCA cd02085
golgi-associated secretory pathway Ca(2+) transport ATPases, similar to human ATPase secretory ...
766-1077 6.40e-08

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: 57.41  E-value: 6.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  766 FDSVRKRMSVVV--RHPLTGEIVVYTKGA-DSVI----MDLLEDPACVPdinMEKKLRKIRARTQKHLDlyaRDGLRTLC 838
Cdd:cd02085    361 FSSEQKWMAVKCipKYNSDNEEIYFMKGAlEQVLdyctTYNSSDGSALP---LTQQQRSEINEEEKEMG---SKGLRVLA 434
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  839 IAKKVVSEedfrrwasfrreaeasldnrdellmetaqhlenQLTLLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDK 918
Cdd:cd02085    435 LASGPELG---------------------------------DLTFLGLVGINDPPRPGVREAIQILLESGVRVKMITGDA 481
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  919 QETAVNIAHSCRLLNQTDTVYTintenqetcesilncaLEELKQFRELQkpdrklfgfrLPSKTPSITseavvpeaglvi 998
Cdd:cd02085    482 QETAIAIGSSLGLYSPSLQALS----------------GEEVDQMSDSQ----------LASVVRKVT------------ 523
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  999 dgktlnaIFQgklekkfleltqycrsvlccRSTPLQKSMIVKLVRDKLRV--MTlsiGDGANDVSMIQAADIGIGIsGQE 1076
Cdd:cd02085    524 -------VFY--------------------RASPRHKLKIVKALQKSGAVvaMT---GDGVNDAVALKSADIGIAM-GRT 572

                   .
gi 1489866104 1077 G 1077
Cdd:cd02085    573 G 573
P-type_ATPase cd07538
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ...
757-1075 1.24e-07

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: 56.30  E-value: 1.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  757 TFSLLCTLGFDSVRKRMSVVVRHPltGEIVVYTKGADSVIMDLledpaCvpDINMEKKlrkirARTQKHLDLYARDGLRT 836
Cdd:cd07538    319 LTSLVREYPLRPELRMMGQVWKRP--EGAFAAAKGSPEAIIRL-----C--RLNPDEK-----AAIEDAVSEMAGEGLRV 384
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  837 LCIAKKVVSEEdfrrwasfrreaeasldnrdellmETAQHLEN-QLTLLGATGIEDRLQEGVPDTIATLREAGIQLWVLT 915
Cdd:cd07538    385 LAVAACRIDES------------------------FLPDDLEDaVFIFVGLIGLADPLREDVPEAVRICCEAGIRVVMIT 440
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  916 GDKQETAVNIAHSCRLlnqtdtvytINTENQETCESILNCALEElkqfrelqkpdrklfgfrLPSKTPSITseavvpeag 995
Cdd:cd07538    441 GDNPATAKAIAKQIGL---------DNTDNVITGQELDAMSDEE------------------LAEKVRDVN--------- 484
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  996 lvidgktlnaIFQgklekkfleltqycrsvlccRSTPLQKSMIVKLVRDKLRVMTLSiGDGANDVSMIQAADIGIGISGQ 1075
Cdd:cd07538    485 ----------IFA--------------------RVVPEQKLRIVQAFKANGEIVAMT-GDGVNDAPALKAAHIGIAMGKR 533
P-type_ATPase_cation cd07543
P-type cation-transporting ATPases, similar to human cation-transporting ATPase type 13A1 ...
766-1070 1.78e-07

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: 55.85  E-value: 1.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  766 FDSVRKRMSVVVRH----PLTGEIVVYTKGADSVIMDLLEDpacVPDiNMEKKLRKirartqkhldlYARDGLRTLCIAK 841
Cdd:cd07543    411 FSSALKRMSVVASYkdpgSTDLKYIVAVKGAPETLKSMLSD---VPA-DYDEVYKE-----------YTRQGSRVLALGY 475
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  842 KVVSEEDFRRWASFRREaeasldnrdellmetaqHLENQLTLLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDKQET 921
Cdd:cd07543    476 KELGHLTKQQARDYKRE-----------------DVESDLTFAGFIVFSCPLKPDSKETIKELNNSSHRVVMITGDNPLT 538
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  922 AVNIAhscrllnqtdtvytintenqetcesilncalEELKqfrelqkpdrklfgfrlpsktpsITSEAVVpeaglvidgk 1001
Cdd:cd07543    539 ACHVA-------------------------------KELG-----------------------IVDKPVL---------- 554
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1489866104 1002 tlnaIFQGKLEKKFLELTQYCRSVLCCRSTPLQKSMIVKLVRDKLRVmTLSIGDGANDVSMIQAADIGI 1070
Cdd:cd07543    555 ----ILILSEEGKSNEWKLIPHVKVFARVAPKQKEFIITTLKELGYV-TLMCGDGTNDVGALKHAHVGV 618
P-type_ATPase cd02609
uncharacterized subfamily of P-type ATPase transporter, similar to uncharacterized ...
699-1180 2.22e-07

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: 55.36  E-value: 2.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  699 LEEALEAPATDLARpEFCYEAESPDEAALVHAAHaysftLVSRTPEQVTVRLPqgtcltfsllctlgFDSVRKRMSVVVR 778
Cdd:cd02609    310 LDEANEAEAAAALA-AFVAASEDNNATMQAIRAA-----FFGNNRFEVTSIIP--------------FSSARKWSAVEFR 369
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  779 hpltgEIVVYTKGADSVImdLLEDPACVPDINMEkklrkirartqkhldlYARDGLRTLCIAKkvvSEEDFrrwasfrre 858
Cdd:cd02609    370 -----DGGTWVLGAPEVL--LGDLPSEVLSRVNE----------------LAAQGYRVLLLAR---SAGAL--------- 414
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  859 aeasldnrdellmeTAQHLENQLTLLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDKQETAVNIAHSCRLLNQTDTV 938
Cdd:cd02609    415 --------------THEQLPVGLEPLALILLTDPIRPEAKETLAYFAEQGVAVKVISGDNPVTVSAIAKRAGLEGAESYI 480
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  939 YTINTENQETcesiLNCALEElkqfrelqkpdrklfgfrlpsktpsitseavvpeaglvidgktlNAIFQgklekkflel 1018
Cdd:cd02609    481 DASTLTTDEE----LAEAVEN--------------------------------------------YTVFG---------- 502
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1019 tqycrsvlccRSTPLQKSMIVKLVRDKLRV--MTlsiGDGANDVSMIQAADIGIGI-SGQEGMQAVmsSDFAI--TRFKH 1093
Cdd:cd02609    503 ----------RVTPEQKRQLVQALQALGHTvaMT---GDGVNDVLALKEADCSIAMaSGSDATRQV--AQVVLldSDFSA 567
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1094 LKKLLLvHGHWCYSRLARMVVYYLYKNVcYVNLLfwyQFFCGFSSS---------TMIDYWqMIFFNLFFTSLPPLVFGV 1164
Cdd:cd02609    568 LPDVVF-EGRRVVNNIERVASLFLVKTI-YSVLL---ALICVITALpfpflpiqiTLISLF-TIGIPSFFLALEPNKRRI 641
                          490
                   ....*....|....*.
gi 1489866104 1165 LDKDISAETLLALPEL 1180
Cdd:cd02609    642 EGGFLRRVLTKALPPL 657
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
883-926 1.35e-06

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 52.84  E-value: 1.35e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1489866104  883 LLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDKQETAVNIA 926
Cdd:COG2217    532 LLGLIALADTLRPEAAEAIAALKALGIRVVMLTGDNERTAEAVA 575
P-type_ATPase_cation cd02082
P-type cation-transporting ATPases, similar to human ATPase type 13A1-A4 (ATP13A1-A4) proteins ...
766-1160 1.93e-06

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: 52.59  E-value: 1.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  766 FDSVRKRMSVVVRHPLTGE----IVVYTKGADSVIMDLLEdpACVPDInmekklrkirartQKHLDLYARDGLRTLCIAK 841
Cdd:cd02082    407 FHSALQRMSVVAKEVDMITkdfkHYAFIKGAPEKIQSLFS--HVPSDE-------------KAQLSTLINEGYRVLALGY 471
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  842 KVVSEEDFRRWASFRREAeasldnrdellmetaqhLENQLTLLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDKQET 921
Cdd:cd02082    472 KELPQSEIDAFLDLSREA-----------------QEANVQFLGFIIYKNNLKPDTQAVIKEFKEACYRIVMITGDNPLT 534
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  922 AVNIAHSCRLLNQTDTVytintenqetcesilncaleelkqfrelqkpdrklfgfrlpsktpsITSEAVVPEAGLVidgk 1001
Cdd:cd02082    535 ALKVAQELEIINRKNPT----------------------------------------------IIIHLLIPEIQKD---- 564
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1002 tlnaifqGKLEKKFLELTQycrsvLCCRSTPLQKSMIVKLVRDkLRVMTLSIGDGANDVSMIQAADIGIGISGQEGmqAV 1081
Cdd:cd02082    565 -------NSTQWILIIHTN-----VFARTAPEQKQTIIRLLKE-SDYIVCMCGDGANDCGALKEADVGISLAEADA--SF 629
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104 1082 MSSDFAITRFKHLKKLLLVHGHWCYSRLARMV-VYYLYKNVCYVNLLFWYQFFCGFSSSTMIDyWQMI--FFNLFFTSLP 1158
Cdd:cd02082    630 ASPFTSKSTSISCVKRVILEGRVNLSTSVEIFkGYALVALIRYLSFLTLYYFYSSYSSSGQMD-WQLLaaGYFLVYLRLG 708

                   ..
gi 1489866104 1159 PL 1160
Cdd:cd02082    709 CN 710
P-type_ATPase_HM cd02079
P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) ...
882-927 2.09e-06

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: 52.22  E-value: 2.09e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1489866104  882 TLLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDKQETAVNIAH 927
Cdd:cd02079    438 KLVGLFALEDQLRPEAKEVIAELKSGGIKVVMLTGDNEAAAQAVAK 483
ATPase-IID_K-Na TIGR01523
potassium and/or sodium efflux P-type ATPase, fungal-type; Initially described as a calcium ...
766-932 4.14e-06

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: 51.55  E-value: 4.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  766 FDSVRKRMSVVVRHPLTGEIVVYTKGADSVIMDLLEDPACVPDINMEKKLRKIRARTQKHLDLYARDGLRTLCIAKKVVS 845
Cdd:TIGR01523  533 FDSEIKRMASIYEDNHGETYNIYAKGAFERIIECCSSSNGKDGVKISPLEDCDRELIIANMESLAAEGLRVLAFASKSFD 612
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  846 EEDfrrwasfrreaeaslDNRDELLMETAQH--LENQLTLLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDKQETAV 923
Cdd:TIGR01523  613 KAD---------------NNDDQLKNETLNRatAESDLEFLGLIGIYDPPRNESAGAVEKCHQAGINVHMLTGDFPETAK 677

                   ....*....
gi 1489866104  924 NIAHSCRLL 932
Cdd:TIGR01523  678 AIAQEVGII 686
MgtA COG0474
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism];
416-456 1.77e-05

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


Pssm-ID: 440242 [Multi-domain]  Cd Length: 874  Bit Score: 49.33  E-value: 1.77e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1489866104  416 RALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYS 456
Cdd:COG0474    312 RRLPAVETLGSVTVICTDKTGTLTQNKMTVERVYTGGGTYE 352
P-type_ATPase_Cu-like cd02094
P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A ...
883-926 1.79e-05

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: 49.40  E-value: 1.79e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1489866104  883 LLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDKQETAVNIA 926
Cdd:cd02094    459 LAGLIAVADPLKPDAAEAIEALKKMGIKVVMLTGDNRRTARAIA 502
COG4087 COG4087
Soluble P-type ATPase [General function prediction only];
1050-1099 4.22e-05

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


Pssm-ID: 443263 [Multi-domain]  Cd Length: 156  Bit Score: 45.15  E-value: 4.22e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1489866104 1050 TLSIGDGANDVSMIQAADIGIGISGQEGM--QAVMSSDFAITRFKHLKKLLL 1099
Cdd:COG4087     94 TVAIGNGRNDVLMLKEAALGIAVIGPEGAsvKALLAADIVVKSILDALDLLL 145
P-type_ATPase_FixI-like cd02092
Rhizobium meliloti FixI and related proteins; belongs to P-type heavy metal-transporting ...
768-928 1.09e-04

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: 46.58  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  768 SVRKRMSVVVRHPLTGEIVVYTKGADSVIMDLLEDPAcvpdinmekklRKIRARTQkhlDLYARDGLRTLCIAKKVVSEE 847
Cdd:cd02092    349 ALAAALAQASRHPLSRALAAAAGARPVELDDAREVPG-----------RGVEGRID---GARVRLGRPAWLGASAGVSTA 414
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  848 DFRrWASFRREAEASLdnrdellmetaqhlenqltllgatGIEDRLQEGVPDTIATLREAGIQLWVLTGDKQETAVNIAH 927
Cdd:cd02092    415 SEL-ALSKGGEEAARF------------------------PFEDRPRPDAREAISALRALGLSVEILSGDREPAVRALAR 469

                   .
gi 1489866104  928 S 928
Cdd:cd02092    470 A 470
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
882-1072 3.59e-04

HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273651 [Multi-domain]  Cd Length: 207  Bit Score: 43.52  E-value: 3.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  882 TLLGATGIEdrLQEGVPDTIATLREAGIQLWVLTGDKQETAVNIA------------HSCRLLNQTDTVYTINTENQETC 949
Cdd:TIGR01484    9 TLLDPNAHE--LSPETIEALERLREAGVKVVIVTGRSLAEIKELLkqlnlplpliaeNGALIFYPGEILYIEPSDVFEEI 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  950 ESI----LNCALEELK-QFRELQKPDRKLfgfrlpsktpSITSEAVVPEAGLVIDGK---TLNAIFQGKLEKKFLELTQY 1021
Cdd:TIGR01484   87 LGIkfeeIGAELKSLSeHYVGTFIEDKAI----------AVAIHYVGAELGQELDSKmreRLEKIGRNDLELEAIYSGKT 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1489866104 1022 CRSVLccrstPL--QKSMIVKLVRDKL---RVMTLSIGDGANDVSMIQAADIGIGI 1072
Cdd:TIGR01484  157 DLEVL-----PAgvNKGSALQALLQELngkKDEILAFGDSGNDEEMFEVAGLAVAV 207
YedP COG3769
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ...
1043-1077 5.88e-04

Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 442983 [Multi-domain]  Cd Length: 268  Bit Score: 43.28  E-value: 5.88e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1489866104 1043 RDKLRVMTLSIGDGANDVSMIQAADIGIGISGQEG 1077
Cdd:COG3769    203 RFGKNVVTIALGDSPNDIPMLEAADIAVVIRSPHG 237
ATPase-IIB_Ca TIGR01517
plasma-membrane calcium-translocating P-type ATPase; This model describes the P-type ATPase ...
169-473 7.70e-04

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: 44.00  E-value: 7.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  169 DVRVGDFIQMKCNEIVPADILLLFSSDpngiCHLETASLDGETNLKQRCVVKgfsqqevqfEPELFHNTIVCEkpnnhln 248
Cdd:TIGR01517  186 DIVVGDIVSLSTGDVVPADGVFISGLS----LEIDESSITGESDPIKKGPVQ---------DPFLLSGTVVNE------- 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  249 kfkgymehpdqtrtGFGceslllrgctiRNTEMAVGIVIYAGhETKAMLNNSGPryKRSKIERRMN-----IDIFFCIG- 322
Cdd:TIGR01517  246 --------------GSG-----------RMLVTAVGVNSFGG-KLMMELRQAGE--EETPLQEKLSelaglIGKFGMGSa 297
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  323 -ILILMCLIGAVGHSIWNGTFEEHPPFDVPdangSFLPsalggfyMFLTMIILLQVLIP--ISLYVSIELVKLGQVFFLS 399
Cdd:TIGR01517  298 vLLFLVLSLRYVFRIIRGDGRFEDTEEDAQ----TFLD-------HFIIAVTIVVVAVPegLPLAVTIALAYSMKKMMKD 366
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1489866104  400 NDLdlydeetdlsiqCRALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYSHQENAKRLETPKELDSD 473
Cdd:TIGR01517  367 NNL------------VRHLAACETMGSATAICSDKTGTLTQNVMSVVQGYIGEQRFNVRDEIVLRNLPAAVRNI 428
P-type_ATPase_Ca_prok cd02089
prokaryotic P-type Ca(2+)-ATPase similar to Synechococcus elongatus sp. strain PCC 7942 PacL ...
416-452 8.02e-04

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: 44.14  E-value: 8.02e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1489866104  416 RALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMG 452
Cdd:cd02089    288 RKLPAVETLGSVSVICSDKTGTLTQNKMTVEKIYTIG 324
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
1050-1098 1.07e-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: 42.34  E-value: 1.07e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1489866104 1050 TLSIGDGANDVSMIQAADIGIGISGQEGMQAVmsSDFAItRFKHLKKLL 1098
Cdd:TIGR00338  171 TVAVGDGANDLSMIKAAGLGIAFNAKPKLQQK--ADICI-NKKDLTDIL 216
P-type_ATPase_cation cd02082
P-type cation-transporting ATPases, similar to human ATPase type 13A1-A4 (ATP13A1-A4) proteins ...
86-446 1.12e-03

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: 43.73  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104   86 LFEQFHRWANLYFLFLVILnWMPSmEVFHREITMLPLAIVLFVIMIKDGMEDFKRHRfdKAINCSNIRIYERKEQTYVQK 165
Cdd:cd02082     25 MWREFKKPFNFFQYFGVIL-WGID-EYVYYAITVVFMTTINSLSCIYIRGVMQKELK--DACLNNTSVIVQRHGYQEITI 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  166 CWKDVRVGDFIQMKCNE-IVPADILLLfssdpNGICHLETASLDGETNLKQRCVVKGFSQQEVQFEPE------LFHNTI 238
Cdd:cd02082    101 ASNMIVPGDIVLIKRREvTLPCDCVLL-----EGSCIVTEAMLTGESVPIGKCQIPTDSHDDVLFKYEsskshtLFQGTQ 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  239 VcekpnnhlnkfkgyMEHpdQTRTGFGCESLLLRgctirntemaVGIVIYAGHETKAMLnnsgprYKRsKIERRMNIDIF 318
Cdd:cd02082    176 V--------------MQI--IPPEDDILKAIVVR----------TGFGTSKGQLIRAIL------YPK-PFNKKFQQQAV 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  319 FCIGILILMCLIGAVgHSIWNGTFEEHPPfdvpdangsflpsalgGFYMFLTMIILLQVLIP-----ISLYVSIELVKLG 393
Cdd:cd02082    223 KFTLLLATLALIGFL-YTLIRLLDIELPP----------------LFIAFEFLDILTYSVPPglpmlIAITNFVGLKRLK 285
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1489866104  394 QvfflsndldlydeetdLSIQCRALNIAEDLGQIQYIFSDKTGTLTENKMVFR 446
Cdd:cd02082    286 K----------------NQILCQDPNRISQAGRIQTLCFDKTGTLTEDKLDLI 322
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
1050-1071 2.13e-03

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


Pssm-ID: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 40.61  E-value: 2.13e-03
                           10        20
                   ....*....|....*....|..
gi 1489866104 1050 TLSIGDGANDVSMIQAADIGIG 1071
Cdd:cd07500    156 TVAVGDGANDLPMLKAAGLGIA 177
P-type_ATPase_H cd02076
plant and fungal plasma membrane H(+)-ATPases, and related bacterial and archaeal putative H(+) ...
422-485 2.36e-03

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: 42.60  E-value: 2.36e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1489866104  422 EDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYSHQ-----------ENAKRLETP--KELDSDGEEWTQYQCLSF 485
Cdd:cd02076    279 EELAGVDILCSDKTGTLTLNKLSLDEPYSLEGDGKDEllllaalasdtENPDAIDTAilNALDDYKPDLAGYKQLKF 355
P-type_ATPase_Mg cd02077
magnesium transporting ATPase (MgtA), similar to Escherichia coli MgtA and Salmonella ...
56-211 3.23e-03

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: 41.85  E-value: 3.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104   56 HQDWEEVSRRYPGNRTCTTKYTLFTflpRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITMLPLAIVLFVIMIKDGM 135
Cdd:cd02077      4 NEEAEERLEKYGPNEISHEKFPSWF---KLLLKAFINPFNIVLLVLALVSFFTDVLLAPGEFDLVGALIILLMVLISGLL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866104  136 ---EDFKRHRFDKAI-----NCSNIRiyeRKEQTYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDpngiCHLETASL 207
Cdd:cd02077     81 dfiQEIRSLKAAEKLkkmvkNTATVI---RDGSKYMEIPIDELVPGDIVYLSAGDMIPADVRIIQSKD----LFVSQSSL 153

                   ....
gi 1489866104  208 DGET 211
Cdd:cd02077    154 TGES 157
P-type_ATPases cd01431
ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, ...
429-456 4.02e-03

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: 41.28  E-value: 4.02e-03
                           10        20
                   ....*....|....*....|....*...
gi 1489866104  429 YIFSDKTGTLTENKMVFRRCTIMGSEYS 456
Cdd:cd01431      1 VICSDKTGTLTKNGMTVTKLFIEEIPFN 28
P-type_ATPase_Na_ENA cd02086
fungal-type Na(+)-ATPase, similar to the plasma membrane sodium transporters Saccharomyces ...
416-447 4.46e-03

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: 41.67  E-value: 4.46e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1489866104  416 RALNIAEDLGQIQYIFSDKTGTLTENKMVFRR 447
Cdd:cd02086    317 RKLDALEALGAVTDICSDKTGTLTQGKMVVRQ 348
serB PRK11133
phosphoserine phosphatase; Provisional
1050-1070 6.04e-03

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 40.70  E-value: 6.04e-03
                           10        20
                   ....*....|....*....|.
gi 1489866104 1050 TLSIGDGANDVSMIQAADIGI 1070
Cdd:PRK11133   267 TVAIGDGANDLPMIKAAGLGI 287
P-type_ATPase cd07539
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ...
416-443 6.52e-03

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: 40.86  E-value: 6.52e-03
                           10        20
                   ....*....|....*....|....*...
gi 1489866104  416 RALNIAEDLGQIQYIFSDKTGTLTENKM 443
Cdd:cd07539    288 RSPRTVEALGRVDTICFDKTGTLTENRL 315
P-type_ATPase_cation cd02080
P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, ...
416-447 8.47e-03

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: 40.71  E-value: 8.47e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1489866104  416 RALNIAEDLGQIQYIFSDKTGTLTENKMVFRR 447
Cdd:cd02080    288 RRLPAVETLGSVTVICSDKTGTLTRNEMTVQA 319
P-type_ATPase_HM cd07550
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
883-926 9.89e-03

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: 40.34  E-value: 9.89e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1489866104  883 LLGATGIEDRLQEGVPDTIATLREAG-IQLWVLTGDKQETAVNIA 926
Cdd:cd07550    412 LIGVIGLSDPLRPEAAEVIARLRALGgKRIIMLTGDHEQRARALA 456
 
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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