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Conserved domains on  [gi|150421684|ref|NP_056020|]
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phospholipid-transporting ATPase IH isoform a [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, ...
47-983 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: 1269.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   47 DNRIVSSKYTFWNFIPKNLFEQFRRVANFYFLIIFLVQLI-IDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHKADNAM 125
Cdd:cd02073     1 DNRISTTKYTVFTFLPKNLFEQFRRVANLYFLFIAILQQIpGISPTGPYTTLLPLLFVLGVTAIKEGYEDIRRHKSDNEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  126 NQCPVHFIQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNRGDGTCHVTTASLDGESSHKTHYAVQDTKGFHTEE 205
Cdd:cd02073    81 NNRPVQVLRGGKFVKKKWKDIRVGDIVRVKNDEFVPADLLLLSSSEPDGLCYVETANLDGETNLKIRQALPETALLLSEE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  206 DIGGLHATIECEQPQPDLYKFVGRINvysdLNDPVVRPLGSENLLLRGATLKNTEKIFGVAIYTGMETKMALNYQSKSQK 285
Cdd:cd02073   161 DLARFSGEIECEQPNNDLYTFNGTLE----LNGGRELPLSPDNLLLRGCTLRNTEWVYGVVVYTGHETKLMLNSGGTPLK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  286 RSAVEKSMNAFLIVYLCILISKALINTVLKYMWQSEPFRDEPWYNQKTEserqRNLFLKAFTDFLAFMVLFNYIIPVSMY 365
Cdd:cd02073   237 RSSIEKKMNRFIIAIFCILIVMCLISAIGKGIWLSKHGRDLWYLLPKEE----RSPALEFFFDFLTFIILYNNLIPISLY 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  366 VTVEMQKFLGSYFITWDEDMFDEETGEGPLVNTSDLNEELGQVEYIFTDKTGTLTENNMEFKECCIEGHVYvphvicngq 445
Cdd:cd02073   313 VTIEVVKFLQSFFINWDLDMYDEETDTPAEARTSNLNEELGQVEYIFSDKTGTLTENIMEFKKCSINGVDY--------- 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  446 vlpessgidmidsspsvngrereeLFFRALCLCHTVQVKDDDSVDgprkspdggkSCVYISSSPDEVALVEGVQRLGFTY 525
Cdd:cd02073   384 ------------------------GFFLALALCHTVVPEKDDHPG----------QLVYQASSPDEAALVEAARDLGFVF 429
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  526 LRLKDNYMEIlNRENHIERFELLEILSFDSVRRRMSVIVKSATGEIYLFCKGADSSIFPRVIEGK---VDQIRARVERNA 602
Cdd:cd02073   430 LSRTPDTVTI-NALGEEEEYEILHILEFNSDRKRMSVIVRDPDGRILLYCKGADSVIFERLSPSSlelVEKTQEHLEDFA 508
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  603 VEGLRTLCVAYKRLIQEEYEGICKLLQAAKVALQDREKKLAEAYEQIEKDLTLLGATAVEDRLQEKAADTIEALQKAGIK 682
Cdd:cd02073   509 SEGLRTLCLAYREISEEEYEEWNEKYDEASTALQNREELLDEVAEEIEKDLILLGATAIEDKLQDGVPETIEALQRAGIK 588
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  683 VWVLTGDKMETAAATCYACKLFRRntqllelttkrieeqslhdvlfelsktvlrhsgsltrdnlsglsaDMQDYGLIIDG 762
Cdd:cd02073   589 IWVLTGDKQETAINIGYSCRLLSE---------------------------------------------DMENLALVIDG 623
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  763 AALSLIMKPREdgssgnyRELFLEICRSCSAVLCCRMAPLQKAQIVKLIKFSKEhPITLAIGDGANDVSMILEAHVGIGV 842
Cdd:cd02073   624 KTLTYALDPEL-------ERLFLELALKCKAVICCRVSPLQKALVVKLVKKSKK-AVTLAIGDGANDVSMIQEAHVGVGI 695
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  843 IGKEGRQAARNSDYAIPKFKHLKKMLLVHGHFYYIRISELVQYFFYKNVCFIFPQFLYQFFCGFSQQTLYDTAYLTLYNI 922
Cdd:cd02073   696 SGQEGMQAARASDYAIAQFRFLRRLLLVHGRWSYQRLAKLILYFFYKNIAFYLTQFWYQFFNGFSGQTLYDSWYLTLYNV 775
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150421684  923 SFTSLPILLYSLMEQHVGIDVLKRDPTLYRDVAKNALLRWRVFIYWTLLGLFDALVFFFGA 983
Cdd:cd02073   776 LFTSLPPLVIGIFDQDVSAETLLRYPELYKPGQLNELFNWKVFLYWILDGIYQSLIIFFVP 836
 
Name Accession Description Interval E-value
P-type_ATPase_APLT_Dnf-like cd02073
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ...
47-983 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: 1269.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   47 DNRIVSSKYTFWNFIPKNLFEQFRRVANFYFLIIFLVQLI-IDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHKADNAM 125
Cdd:cd02073     1 DNRISTTKYTVFTFLPKNLFEQFRRVANLYFLFIAILQQIpGISPTGPYTTLLPLLFVLGVTAIKEGYEDIRRHKSDNEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  126 NQCPVHFIQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNRGDGTCHVTTASLDGESSHKTHYAVQDTKGFHTEE 205
Cdd:cd02073    81 NNRPVQVLRGGKFVKKKWKDIRVGDIVRVKNDEFVPADLLLLSSSEPDGLCYVETANLDGETNLKIRQALPETALLLSEE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  206 DIGGLHATIECEQPQPDLYKFVGRINvysdLNDPVVRPLGSENLLLRGATLKNTEKIFGVAIYTGMETKMALNYQSKSQK 285
Cdd:cd02073   161 DLARFSGEIECEQPNNDLYTFNGTLE----LNGGRELPLSPDNLLLRGCTLRNTEWVYGVVVYTGHETKLMLNSGGTPLK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  286 RSAVEKSMNAFLIVYLCILISKALINTVLKYMWQSEPFRDEPWYNQKTEserqRNLFLKAFTDFLAFMVLFNYIIPVSMY 365
Cdd:cd02073   237 RSSIEKKMNRFIIAIFCILIVMCLISAIGKGIWLSKHGRDLWYLLPKEE----RSPALEFFFDFLTFIILYNNLIPISLY 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  366 VTVEMQKFLGSYFITWDEDMFDEETGEGPLVNTSDLNEELGQVEYIFTDKTGTLTENNMEFKECCIEGHVYvphvicngq 445
Cdd:cd02073   313 VTIEVVKFLQSFFINWDLDMYDEETDTPAEARTSNLNEELGQVEYIFSDKTGTLTENIMEFKKCSINGVDY--------- 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  446 vlpessgidmidsspsvngrereeLFFRALCLCHTVQVKDDDSVDgprkspdggkSCVYISSSPDEVALVEGVQRLGFTY 525
Cdd:cd02073   384 ------------------------GFFLALALCHTVVPEKDDHPG----------QLVYQASSPDEAALVEAARDLGFVF 429
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  526 LRLKDNYMEIlNRENHIERFELLEILSFDSVRRRMSVIVKSATGEIYLFCKGADSSIFPRVIEGK---VDQIRARVERNA 602
Cdd:cd02073   430 LSRTPDTVTI-NALGEEEEYEILHILEFNSDRKRMSVIVRDPDGRILLYCKGADSVIFERLSPSSlelVEKTQEHLEDFA 508
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  603 VEGLRTLCVAYKRLIQEEYEGICKLLQAAKVALQDREKKLAEAYEQIEKDLTLLGATAVEDRLQEKAADTIEALQKAGIK 682
Cdd:cd02073   509 SEGLRTLCLAYREISEEEYEEWNEKYDEASTALQNREELLDEVAEEIEKDLILLGATAIEDKLQDGVPETIEALQRAGIK 588
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  683 VWVLTGDKMETAAATCYACKLFRRntqllelttkrieeqslhdvlfelsktvlrhsgsltrdnlsglsaDMQDYGLIIDG 762
Cdd:cd02073   589 IWVLTGDKQETAINIGYSCRLLSE---------------------------------------------DMENLALVIDG 623
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  763 AALSLIMKPREdgssgnyRELFLEICRSCSAVLCCRMAPLQKAQIVKLIKFSKEhPITLAIGDGANDVSMILEAHVGIGV 842
Cdd:cd02073   624 KTLTYALDPEL-------ERLFLELALKCKAVICCRVSPLQKALVVKLVKKSKK-AVTLAIGDGANDVSMIQEAHVGVGI 695
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  843 IGKEGRQAARNSDYAIPKFKHLKKMLLVHGHFYYIRISELVQYFFYKNVCFIFPQFLYQFFCGFSQQTLYDTAYLTLYNI 922
Cdd:cd02073   696 SGQEGMQAARASDYAIAQFRFLRRLLLVHGRWSYQRLAKLILYFFYKNIAFYLTQFWYQFFNGFSGQTLYDSWYLTLYNV 775
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150421684  923 SFTSLPILLYSLMEQHVGIDVLKRDPTLYRDVAKNALLRWRVFIYWTLLGLFDALVFFFGA 983
Cdd:cd02073   776 LFTSLPPLVIGIFDQDVSAETLLRYPELYKPGQLNELFNWKVFLYWILDGIYQSLIIFFVP 836
ATPase-Plipid TIGR01652
phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase ...
45-1109 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: 1009.60  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684    45 YPDNRIVSSKYTFWNFIPKNLFEQFRRVANFYFLIIFLVQLI-IDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHKADN 123
Cdd:TIGR01652    1 FCSNKISTTKYTVLTFLPKNLFEQFKRFANLYFLVVALLQQVpILSPTYRGTSIVPLAFVLIVTAIKEAIEDIRRRRRDK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   124 AMNQCPVH-FIQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNRGDGTCHVTTASLDGESSHKTHYAVQDTKGFH 202
Cdd:TIGR01652   81 EVNNRLTEvLEGHGQFVEIPWKDLRVGDIVKVKKDERIPADLLLLSSSEPDGVCYVETANLDGETNLKLRQALEETQKML 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   203 TEEDIGGLHATIECEQPQPDLYKFVGriNVYsdLNDPVVRPLGSENLLLRGATLKNTEKIFGVAIYTGMETKMALNYQSK 282
Cdd:TIGR01652  161 DEDDIKNFSGEIECEQPNASLYSFQG--NMT--INGDRQYPLSPDNILLRGCTLRNTDWVIGVVVYTGHDTKLMRNATQA 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   283 SQKRSAVEKSMNAFLIVYLCILISKALINTVLKYMWqSEPFRDEPWYNQKTESERqrNLFLKAFTDFLAFMVLFNYIIPV 362
Cdd:TIGR01652  237 PSKRSRLEKELNFLIIILFCLLFVLCLISSVGAGIW-NDAHGKDLWYIRLDVSER--NAAANGFFSFLTFLILFSSLIPI 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   363 SMYVTVEMQKFLGSYFITWDEDMFDEETGEGPLVNTSDLNEELGQVEYIFTDKTGTLTENNMEFKECCIEGHVY------ 436
Cdd:TIGR01652  314 SLYVSLELVKSVQAYFINSDLQMYHEKTDTPASVRTSNLNEELGQVEYIFSDKTGTLTQNIMEFKKCSIAGVSYgdgfte 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   437 ---------VPHVICNGQVLPESSGIDMIDSSPSVNGREREEL------FFRALCLCHTVQvkdddsvdgPRKSPDGGKS 501
Cdd:TIGR01652  394 ikdgirerlGSYVENENSMLVESKGFTFVDPRLVDLLKTNKPNakrineFFLALALCHTVV---------PEFNDDGPEE 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   502 CVYISSSPDEVALVEGVQRLGFTYLRlKDNYMEILNRENHIE--RFELLEILSFDSVRRRMSVIVKSATGEIYLFCKGAD 579
Cdd:TIGR01652  465 ITYQAASPDEAALVKAARDVGFVFFE-RTPKSISLLIEMHGEtkEYEILNVLEFNSDRKRMSVIVRNPDGRIKLLCKGAD 543
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   580 SSIFPRVIEGKVDQIRA---RVERNAVEGLRTLCVAYKRLIQEEYEGICKLLQAAKVALQDREKKLAEAYEQIEKDLTLL 656
Cdd:TIGR01652  544 TVIFKRLSSGGNQVNEEtkeHLENYASEGLRTLCIAYRELSEEEYEEWNEEYNEASTALTDREEKLDVVAESIEKDLILL 623
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   657 GATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAATCYACKLFRRNTQLLELTTkriEEQSLHDVLFELSKTVLR 736
Cdd:TIGR01652  624 GATAIEDKLQEGVPETIELLRQAGIKIWVLTGDKVETAINIGYSCRLLSRNMEQIVITS---DSLDATRSVEAAIKFGLE 700
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   737 HSGSLTRDnlsglSADMQDYGLIIDGAALSLIMKPRedgssgnYRELFLEICRSCSAVLCCRMAPLQKAQIVKLIKfSKE 816
Cdd:TIGR01652  701 GTSEEFNN-----LGDSGNVALVIDGKSLGYALDEE-------LEKEFLQLALKCKAVICCRVSPSQKADVVRLVK-KST 767
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   817 HPITLAIGDGANDVSMILEAHVGIGVIGKEGRQAARNSDYAIPKFKHLKKMLLVHGHFYYIRISELVQYFFYKNVCFIFP 896
Cdd:TIGR01652  768 GKTTLAIGDGANDVSMIQEADVGVGISGKEGMQAVMASDFAIGQFRFLTKLLLVHGRWSYKRISKMILYFFYKNLIFAII 847
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   897 QFLYQFFCGFSQQTLYDTAYLTLYNISFTSLPILLYSLMEQHVGIDVLKRDPTLYRDVAKNALLRWRVFIYWTLLGLFDA 976
Cdd:TIGR01652  848 QFWYSFYNGFSGQTLYEGWYMVLYNVFFTALPVISLGVFDQDVSASLSLRYPQLYREGQKGQGFSTKTFWGWMLDGIYQS 927
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   977 LVFFFGAYFVFENTTVTSNGQIFGNWTFGTLVFTVMVFTVTLKLALDTHYWTWINHFVIWGSLLFYVVFSLLWGGvIWPF 1056
Cdd:TIGR01652  928 LVIFFFPMFAYILGDFVSSGSVDDFSSVGVIVFTALVVIVNLKIALEINRWNWISLITIWGSILVWLIFVIVYSS-IFPS 1006
                         1050      1060      1070      1080      1090
                   ....*....|....*....|....*....|....*....|....*....|...
gi 150421684  1057 LNYqrmYYVFIQMLSSGPAWLAIVLLVTISLLPDVLKKVLCRQLWPTATERVQ 1109
Cdd:TIGR01652 1007 PAF---YKAAPRVMGTFGFWLVLLVIVLISLLPRFTYKAIQRLFRPPDYDIVQ 1056
PLN03190 PLN03190
aminophospholipid translocase; Provisional
22-1102 0e+00

aminophospholipid translocase; Provisional


Pssm-ID: 215623 [Multi-domain]  Cd Length: 1178  Bit Score: 629.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   22 DSRTIYVGhrEPPPGAEAYipqRYPDNRIVSSKYTFWNFIPKNLFEQFRRVANFYFLIIF----LVQLIIDTPTSPVtsg 97
Cdd:PLN03190   69 DARLVYLN--DPEKSNERF---EFAGNSIRTAKYSVFSFLPRNLFEQFHRVAYIYFLVIAvlnqLPQLAVFGRGASI--- 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   98 LPLFFVITVTAIKQGYEDWLRHKADNAMNQCPVHFIQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNRGDGTCH 177
Cdd:PLN03190  141 LPLAFVLLVTAVKDAYEDWRRHRSDRIENNRLAWVLVDDQFQEKKWKDIRVGEIIKIQANDTLPCDMVLLSTSDPTGVAY 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  178 VTTASLDGESSHKTHYAVQDT-KGFHTEEDIGGLhatIECEQPQPDLYKFVGRINVysdlnDPVVRPLGSENLLLRGATL 256
Cdd:PLN03190  221 VQTINLDGESNLKTRYAKQETlSKIPEKEKINGL---IKCEKPNRNIYGFQANMEV-----DGKRLSLGPSNIILRGCEL 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  257 KNTEKIFGVAIYTGMETKMALNYQSKSQKRSAVEKSMNAFLIVYLCILISKALINTVLKYMWQSEpFRDE----PWYNQK 332
Cdd:PLN03190  293 KNTAWAIGVAVYCGRETKAMLNNSGAPSKRSRLETRMNLEIIILSLFLIALCTIVSVCAAVWLRR-HRDEldtiPFYRRK 371
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  333 TESERQRNLF------LKAFTDFLAFMVLFNYIIPVSMYVTVEMQKFLGSYFITWDEDMFDEETGEGPLVNTSDLNEELG 406
Cdd:PLN03190  372 DFSEGGPKNYnyygwgWEIFFTFLMSVIVFQIMIPISLYISMELVRVGQAYFMIRDDQMYDEASNSRFQCRALNINEDLG 451
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  407 QVEYIFTDKTGTLTENNMEFKECCIEGHVYVPHVICNGQVLPESSG-IDMIDSSP-------------SVNGREREEL-- 470
Cdd:PLN03190  452 QIKYVFSDKTGTLTENKMEFQCASIWGVDYSDGRTPTQNDHAGYSVeVDGKILRPkmkvkvdpqllelSKSGKDTEEAkh 531
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  471 ---FFRALCLCHT-VQVKDDDSVDGPRKSPDggkscvYISSSPDEVALVEGVQRLGFTYLRLKDNYMeILNRENHIERFE 546
Cdd:PLN03190  532 vhdFFLALAACNTiVPIVVDDTSDPTVKLMD------YQGESPDEQALVYAAAAYGFMLIERTSGHI-VIDIHGERQRFN 604
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  547 LLEILSFDSVRRRMSVIVKSATGEIYLFCKGADSSIFPrVIE-----GKVDQIRARVERNAVEGLRTLCVAYKRLIQEEY 621
Cdd:PLN03190  605 VLGLHEFDSDRKRMSVILGCPDKTVKVFVKGADTSMFS-VIDrslnmNVIRATEAHLHTYSSLGLRTLVVGMRELNDSEF 683
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  622 EGICKLLQAAKVALQDREKKLAEAYEQIEKDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAATCYAC 701
Cdd:PLN03190  684 EQWHFSFEAASTALIGRAALLRKVASNVENNLTILGASAIEDKLQQGVPEAIESLRTAGIKVWVLTGDKQETAISIGYSS 763
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  702 KLFRRN-TQL-LELTTKRIEEQSLHDVLFeLSKTVLRHSGslTRDNLSGLSADMQD-YGLIIDGAALSLIMkpredgsSG 778
Cdd:PLN03190  764 KLLTNKmTQIiINSNSKESCRKSLEDALV-MSKKLTTVSG--ISQNTGGSSAAASDpVALIIDGTSLVYVL-------DS 833
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  779 NYRELFLEICRSCSAVLCCRMAPLQKAQIVKLIKfSKEHPITLAIGDGANDVSMILEAHVGIGVIGKEGRQAARNSDYAI 858
Cdd:PLN03190  834 ELEEQLFQLASKCSVVLCCRVAPLQKAGIVALVK-NRTSDMTLAIGDGANDVSMIQMADVGVGISGQEGRQAVMASDFAM 912
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  859 PKFKHLKKMLLVHGHFYYIRISELVQYFFYKNVCFIFPQFLYQFFCGFSQQTLYDTAYLTLYNISFTSLPILLYSLMEQH 938
Cdd:PLN03190  913 GQFRFLVPLLLVHGHWNYQRMGYMILYNFYRNAVFVLVLFWYVLFTCFTLTTAINEWSSVLYSVIYTALPTIVVGILDKD 992
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  939 VGIDVLKRDPTLY----RDVAKNALLRWrvfiYWTLLGLFDALVFFFGAYFVFENTTVtsNGQIFGN-WTFGtlvftvMV 1013
Cdd:PLN03190  993 LSRRTLLKYPQLYgagqRQEAYNSKLFW----LTMIDTLWQSAVVFFVPLFAYWASTI--DGSSIGDlWTLA------VV 1060
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684 1014 FTVTLKLALDTHYWTWINHFVIWGSLLFYVVFSLLWGGViwPFLnyqRMYYVFIQMLSSGPAWLAIVLLVTISLLPDVLK 1093
Cdd:PLN03190 1061 ILVNLHLAMDIIRWNWITHAAIWGSIVATFICVIVIDAI--PTL---PGYWAIFHIAKTGSFWLCLLAIVVAALLPRFVV 1135

                  ....*....
gi 150421684 1094 KVLCRQLWP 1102
Cdd:PLN03190 1136 KVLYQYFTP 1144
PhoLip_ATPase_C pfam16212
Phospholipid-translocating P-type ATPase C-terminal; PhoLip_ATPase_C is found at the ...
851-1103 3.47e-100

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: 317.14  E-value: 3.47e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   851 ARNSDYAIPKFKHLKKMLLVHGHFYYIRISELVQYFFYKNVCFIFPQFLYQFFCGFSQQTLYDTAYLTLYNISFTSLPIL 930
Cdd:pfam16212    1 ARASDYAIAQFRFLKRLLLVHGRWSYRRTSKLILYFFYKNIVFTLTQFWYQFYNGFSGQSLYESWYLTLYNLLFTSLPVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   931 LYSLMEQHVGIDVLKRDPTLYRDVAKNALLRWRVFIYWTLLGLFDALVFFFGAYFVFENTTVtSNGQIFGNWTFGTLVFT 1010
Cdd:pfam16212   81 VLGIFDQDVSAETLLAYPELYKLGQKNKFFNLKTFLGWMLDGIYQSLIIFFIPYLAYGDSVF-SGGKDADLWAFGTTVFT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  1011 VMVFTVTLKLALDTHYWTWINHFVIWGSLLFYVVFSLLWGGVIWPFlnYQRMYYVFIQMLSSGPAWLAIVLLVTISLLPD 1090
Cdd:pfam16212  160 ALVLVVNLKLALETHYWTWITHLAIWGSILLYFLFTLIYSSIYPSS--YSVFYGVASRLFGSPSFWLTLLLIVVVALLPD 237
                          250
                   ....*....|...
gi 150421684  1091 VLKKVLCRQLWPT 1103
Cdd:pfam16212  238 FAYKALKRTFFPT 250
MgtA COG0474
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism];
43-1100 3.67e-38

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


Pssm-ID: 440242 [Multi-domain]  Cd Length: 874  Bit Score: 154.49  E-value: 3.67e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   43 QRYPDNRIVSSK-YTFWnfipKNLFEQFRrvaNFYFLIIF---LVQLIIDTPTSPVTsglpLFFVITVTAIkQGYedWLR 118
Cdd:COG0474    37 ARYGPNELPEEKkRSLL----RRFLEQFK---NPLILILLaaaVISALLGDWVDAIV----ILAVVLLNAI-IGF--VQE 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  119 HKADNAM--------NQCPVhfIQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNRgdgtCHVTTASLDGESshk 190
Cdd:COG0474   103 YRAEKALealkkllaPTARV--LRDGKWVEIPAEELVPGDIVLLEAGDRVPADLRLLEAKD----LQVDESALTGES--- 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  191 thYAVqdTKgfHTEedigglhaTIECEQPQPDlykfvgRIN-VYSdlndpvvrplGSenLLLRG-ATlkntekifGVAIY 268
Cdd:COG0474   174 --VPV--EK--SAD--------PLPEDAPLGD------RGNmVFM----------GT--LVTSGrGT--------AVVVA 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  269 TGMET---KMALNYQSKSQKRSAVEKSMNAF--LIVYLCILISkALIntVLKYMwqsepFRDEPWYNqkteserqrnLFL 343
Cdd:COG0474   214 TGMNTefgKIAKLLQEAEEEKTPLQKQLDRLgkLLAIIALVLA-ALV--FLIGL-----LRGGPLLE----------ALL 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  344 KAFTdfLAFMvlfnyIIPVS--MYVTV-------EMQKflgsyfitwdedmfdeetgEGPLVntSDLN--EELGQVEYIF 412
Cdd:COG0474   276 FAVA--LAVA-----AIPEGlpAVVTItlalgaqRMAK-------------------RNAIV--RRLPavETLGSVTVIC 327
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  413 TDKTGTLTENNMEFKECCIEGHVYvphvicngqvlpessgidmidsspSVNGREREEL--FFRALCLCHTVQVkDDDSVD 490
Cdd:COG0474   328 TDKTGTLTQNKMTVERVYTGGGTY------------------------EVTGEFDPALeeLLRAAALCSDAQL-EEETGL 382
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  491 GprkspdggkscvyissSPDEVALVEGVQRLGFTYLRLKDNYmeilnrenhierfELLEILSFDSVRRRMSVIVKSATGE 570
Cdd:COG0474   383 G----------------DPTEGALLVAAAKAGLDVEELRKEY-------------PRVDEIPFDSERKRMSTVHEDPDGK 433
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  571 IYLFCKGADSSIFPR----VIEGKV--------DQIRARVERNAVEGLRTLCVAYKRLiqeeyegickllqaakvalqdr 638
Cdd:COG0474   434 RLLIVKGAPEVVLALctrvLTGGGVvplteedrAEILEAVEELAAQGLRVLAVAYKEL---------------------- 491
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  639 EKKLAEAYEQIEKDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAATCyacklfrrntqllelttKRI 718
Cdd:COG0474   492 PADPELDSEDDESDLTFLGLVGMIDPPRPEAKEAIAECRRAGIRVKMITGDHPATARAIA-----------------RQL 554
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  719 eeqslhdvlfelsktvlrhsgsltrdnlsGLSadmQDYGLIIDGAALSLiMKPREdgssgnyrelFLEICRSCSavLCCR 798
Cdd:COG0474   555 -----------------------------GLG---DDGDRVLTGAELDA-MSDEE----------LAEAVEDVD--VFAR 589
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  799 MAPLQKAQIVKLIKfSKEHpiTLA-IGDGANDVSMILEAHVGIGViGKEGRQAARN-SDyaipkfkhlkkMLLVHGHFY- 875
Cdd:COG0474   590 VSPEHKLRIVKALQ-ANGH--VVAmTGDGVNDAPALKAADIGIAM-GITGTDVAKEaAD-----------IVLLDDNFAt 654
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  876 -----------YIRISELVQYFFYKNVCFIFPQFLyqffcgfsqqtlydtAYLTLYNISFTSLPILLYSL---------- 934
Cdd:COG0474   655 ivaaveegrriYDNIRKFIKYLLSSNFGEVLSVLL---------------ASLLGLPLPLTPIQILWINLvtdglpalal 719
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  935 -MEqHVGIDVLKRDPtlyRDvAKNALLRWRVFIYWTLLGLFdALVFFFGAYFVFENTTVTSNgqifgnwTFGTLVFTVMV 1013
Cdd:COG0474   720 gFE-PVEPDVMKRPP---RW-PDEPILSRFLLLRILLLGLL-IAIFTLLTFALALARGASLA-------LARTMAFTTLV 786
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684 1014 FTVTLK-LALDTHYWTWI------NHFVIWGSLLfyvVFSLLWGGVIWPFLNyqrmyyvfiQMLSSGP----AWLAIVLL 1082
Cdd:COG0474   787 LSQLFNvFNCRSERRSFFksglfpNRPLLLAVLL---SLLLQLLLIYVPPLQ---------ALFGTVPlplsDWLLILGL 854
                        1130
                  ....*....|....*...
gi 150421684 1083 VTISLLPDVLKKVLCRQL 1100
Cdd:COG0474   855 ALLYLLLVELVKLLRRRF 872
 
Name Accession Description Interval E-value
P-type_ATPase_APLT_Dnf-like cd02073
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ...
47-983 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: 1269.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   47 DNRIVSSKYTFWNFIPKNLFEQFRRVANFYFLIIFLVQLI-IDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHKADNAM 125
Cdd:cd02073     1 DNRISTTKYTVFTFLPKNLFEQFRRVANLYFLFIAILQQIpGISPTGPYTTLLPLLFVLGVTAIKEGYEDIRRHKSDNEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  126 NQCPVHFIQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNRGDGTCHVTTASLDGESSHKTHYAVQDTKGFHTEE 205
Cdd:cd02073    81 NNRPVQVLRGGKFVKKKWKDIRVGDIVRVKNDEFVPADLLLLSSSEPDGLCYVETANLDGETNLKIRQALPETALLLSEE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  206 DIGGLHATIECEQPQPDLYKFVGRINvysdLNDPVVRPLGSENLLLRGATLKNTEKIFGVAIYTGMETKMALNYQSKSQK 285
Cdd:cd02073   161 DLARFSGEIECEQPNNDLYTFNGTLE----LNGGRELPLSPDNLLLRGCTLRNTEWVYGVVVYTGHETKLMLNSGGTPLK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  286 RSAVEKSMNAFLIVYLCILISKALINTVLKYMWQSEPFRDEPWYNQKTEserqRNLFLKAFTDFLAFMVLFNYIIPVSMY 365
Cdd:cd02073   237 RSSIEKKMNRFIIAIFCILIVMCLISAIGKGIWLSKHGRDLWYLLPKEE----RSPALEFFFDFLTFIILYNNLIPISLY 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  366 VTVEMQKFLGSYFITWDEDMFDEETGEGPLVNTSDLNEELGQVEYIFTDKTGTLTENNMEFKECCIEGHVYvphvicngq 445
Cdd:cd02073   313 VTIEVVKFLQSFFINWDLDMYDEETDTPAEARTSNLNEELGQVEYIFSDKTGTLTENIMEFKKCSINGVDY--------- 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  446 vlpessgidmidsspsvngrereeLFFRALCLCHTVQVKDDDSVDgprkspdggkSCVYISSSPDEVALVEGVQRLGFTY 525
Cdd:cd02073   384 ------------------------GFFLALALCHTVVPEKDDHPG----------QLVYQASSPDEAALVEAARDLGFVF 429
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  526 LRLKDNYMEIlNRENHIERFELLEILSFDSVRRRMSVIVKSATGEIYLFCKGADSSIFPRVIEGK---VDQIRARVERNA 602
Cdd:cd02073   430 LSRTPDTVTI-NALGEEEEYEILHILEFNSDRKRMSVIVRDPDGRILLYCKGADSVIFERLSPSSlelVEKTQEHLEDFA 508
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  603 VEGLRTLCVAYKRLIQEEYEGICKLLQAAKVALQDREKKLAEAYEQIEKDLTLLGATAVEDRLQEKAADTIEALQKAGIK 682
Cdd:cd02073   509 SEGLRTLCLAYREISEEEYEEWNEKYDEASTALQNREELLDEVAEEIEKDLILLGATAIEDKLQDGVPETIEALQRAGIK 588
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  683 VWVLTGDKMETAAATCYACKLFRRntqllelttkrieeqslhdvlfelsktvlrhsgsltrdnlsglsaDMQDYGLIIDG 762
Cdd:cd02073   589 IWVLTGDKQETAINIGYSCRLLSE---------------------------------------------DMENLALVIDG 623
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  763 AALSLIMKPREdgssgnyRELFLEICRSCSAVLCCRMAPLQKAQIVKLIKFSKEhPITLAIGDGANDVSMILEAHVGIGV 842
Cdd:cd02073   624 KTLTYALDPEL-------ERLFLELALKCKAVICCRVSPLQKALVVKLVKKSKK-AVTLAIGDGANDVSMIQEAHVGVGI 695
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  843 IGKEGRQAARNSDYAIPKFKHLKKMLLVHGHFYYIRISELVQYFFYKNVCFIFPQFLYQFFCGFSQQTLYDTAYLTLYNI 922
Cdd:cd02073   696 SGQEGMQAARASDYAIAQFRFLRRLLLVHGRWSYQRLAKLILYFFYKNIAFYLTQFWYQFFNGFSGQTLYDSWYLTLYNV 775
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150421684  923 SFTSLPILLYSLMEQHVGIDVLKRDPTLYRDVAKNALLRWRVFIYWTLLGLFDALVFFFGA 983
Cdd:cd02073   776 LFTSLPPLVIGIFDQDVSAETLLRYPELYKPGQLNELFNWKVFLYWILDGIYQSLIIFFVP 836
ATPase-Plipid TIGR01652
phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase ...
45-1109 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: 1009.60  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684    45 YPDNRIVSSKYTFWNFIPKNLFEQFRRVANFYFLIIFLVQLI-IDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHKADN 123
Cdd:TIGR01652    1 FCSNKISTTKYTVLTFLPKNLFEQFKRFANLYFLVVALLQQVpILSPTYRGTSIVPLAFVLIVTAIKEAIEDIRRRRRDK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   124 AMNQCPVH-FIQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNRGDGTCHVTTASLDGESSHKTHYAVQDTKGFH 202
Cdd:TIGR01652   81 EVNNRLTEvLEGHGQFVEIPWKDLRVGDIVKVKKDERIPADLLLLSSSEPDGVCYVETANLDGETNLKLRQALEETQKML 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   203 TEEDIGGLHATIECEQPQPDLYKFVGriNVYsdLNDPVVRPLGSENLLLRGATLKNTEKIFGVAIYTGMETKMALNYQSK 282
Cdd:TIGR01652  161 DEDDIKNFSGEIECEQPNASLYSFQG--NMT--INGDRQYPLSPDNILLRGCTLRNTDWVIGVVVYTGHDTKLMRNATQA 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   283 SQKRSAVEKSMNAFLIVYLCILISKALINTVLKYMWqSEPFRDEPWYNQKTESERqrNLFLKAFTDFLAFMVLFNYIIPV 362
Cdd:TIGR01652  237 PSKRSRLEKELNFLIIILFCLLFVLCLISSVGAGIW-NDAHGKDLWYIRLDVSER--NAAANGFFSFLTFLILFSSLIPI 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   363 SMYVTVEMQKFLGSYFITWDEDMFDEETGEGPLVNTSDLNEELGQVEYIFTDKTGTLTENNMEFKECCIEGHVY------ 436
Cdd:TIGR01652  314 SLYVSLELVKSVQAYFINSDLQMYHEKTDTPASVRTSNLNEELGQVEYIFSDKTGTLTQNIMEFKKCSIAGVSYgdgfte 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   437 ---------VPHVICNGQVLPESSGIDMIDSSPSVNGREREEL------FFRALCLCHTVQvkdddsvdgPRKSPDGGKS 501
Cdd:TIGR01652  394 ikdgirerlGSYVENENSMLVESKGFTFVDPRLVDLLKTNKPNakrineFFLALALCHTVV---------PEFNDDGPEE 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   502 CVYISSSPDEVALVEGVQRLGFTYLRlKDNYMEILNRENHIE--RFELLEILSFDSVRRRMSVIVKSATGEIYLFCKGAD 579
Cdd:TIGR01652  465 ITYQAASPDEAALVKAARDVGFVFFE-RTPKSISLLIEMHGEtkEYEILNVLEFNSDRKRMSVIVRNPDGRIKLLCKGAD 543
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   580 SSIFPRVIEGKVDQIRA---RVERNAVEGLRTLCVAYKRLIQEEYEGICKLLQAAKVALQDREKKLAEAYEQIEKDLTLL 656
Cdd:TIGR01652  544 TVIFKRLSSGGNQVNEEtkeHLENYASEGLRTLCIAYRELSEEEYEEWNEEYNEASTALTDREEKLDVVAESIEKDLILL 623
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   657 GATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAATCYACKLFRRNTQLLELTTkriEEQSLHDVLFELSKTVLR 736
Cdd:TIGR01652  624 GATAIEDKLQEGVPETIELLRQAGIKIWVLTGDKVETAINIGYSCRLLSRNMEQIVITS---DSLDATRSVEAAIKFGLE 700
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   737 HSGSLTRDnlsglSADMQDYGLIIDGAALSLIMKPRedgssgnYRELFLEICRSCSAVLCCRMAPLQKAQIVKLIKfSKE 816
Cdd:TIGR01652  701 GTSEEFNN-----LGDSGNVALVIDGKSLGYALDEE-------LEKEFLQLALKCKAVICCRVSPSQKADVVRLVK-KST 767
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   817 HPITLAIGDGANDVSMILEAHVGIGVIGKEGRQAARNSDYAIPKFKHLKKMLLVHGHFYYIRISELVQYFFYKNVCFIFP 896
Cdd:TIGR01652  768 GKTTLAIGDGANDVSMIQEADVGVGISGKEGMQAVMASDFAIGQFRFLTKLLLVHGRWSYKRISKMILYFFYKNLIFAII 847
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   897 QFLYQFFCGFSQQTLYDTAYLTLYNISFTSLPILLYSLMEQHVGIDVLKRDPTLYRDVAKNALLRWRVFIYWTLLGLFDA 976
Cdd:TIGR01652  848 QFWYSFYNGFSGQTLYEGWYMVLYNVFFTALPVISLGVFDQDVSASLSLRYPQLYREGQKGQGFSTKTFWGWMLDGIYQS 927
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   977 LVFFFGAYFVFENTTVTSNGQIFGNWTFGTLVFTVMVFTVTLKLALDTHYWTWINHFVIWGSLLFYVVFSLLWGGvIWPF 1056
Cdd:TIGR01652  928 LVIFFFPMFAYILGDFVSSGSVDDFSSVGVIVFTALVVIVNLKIALEINRWNWISLITIWGSILVWLIFVIVYSS-IFPS 1006
                         1050      1060      1070      1080      1090
                   ....*....|....*....|....*....|....*....|....*....|...
gi 150421684  1057 LNYqrmYYVFIQMLSSGPAWLAIVLLVTISLLPDVLKKVLCRQLWPTATERVQ 1109
Cdd:TIGR01652 1007 PAF---YKAAPRVMGTFGFWLVLLVIVLISLLPRFTYKAIQRLFRPPDYDIVQ 1056
P-type_ATPase_APLT cd07536
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ...
47-981 0e+00

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: 676.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   47 DNRIVSSKYTFWNFIPKNLFEQFRRVANFYFLIIFLVQLIID-TPTSPVTSGLPLFFVITVTAIKQGYEDWLRHKADNAM 125
Cdd:cd07536     1 DNSISNQKYNVFTFLPGVLYEQFKRFLNLYFLVIACLQFVPAlKPGYLYTTWAPLIFILAVTMTKEAIDDFRRFQRDKEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  126 NQCPVHFIQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNRGDGTCHVTTASLDGESSHKTHYAVQDTKGFHTEE 205
Cdd:cd07536    81 NKKQLYSKLTGRKVQIKSSDIQVGDIVIVEKNQRIPSDMVLLRTSEPQGSCYVETAQLDGETDLKLRVAVSCTQQLPALG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  206 DIGGLHATIECEQPQPDLYKFVGRINVYsDLNDPVVRPLGSENLLLRGATLKNTEKIFGVAIYTGMETKMALNYQSKSQK 285
Cdd:cd07536   161 DLMKISAYVECQKPQMDIHSFEGNFTLE-DSDPPIHESLSIENTLLRASTLRNTGWVIGVVVYTGKETKLVMNTSNAKNK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  286 RSAVEKSMNAFLIVYLCILISKALINTVLKYMWQSEPFRDEpWYNQKTES---ERQRNLFlkaftdflAFMVLFNYIIPV 362
Cdd:cd07536   240 VGLLDLELNRLTKALFLALVVLSLVMVTLQGFWGPWYGEKN-WYIKKMDTtsdNFGRNLL--------RFLLLFSYIIPI 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  363 SMYVTVEMQKFLGSYFITWDEDMFDEETGEGPLVNTSDLNEELGQVEYIFTDKTGTLTENNMEFKECCIEGHVYvphvic 442
Cdd:cd07536   311 SLRVNLDMVKAVYAWFIMWDENMYYIGNDTGTVARTSTIPEELGQVVYLLTDKTGTLTQNEMIFKRCHIGGVSY------ 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  443 NGQVLpessgidmidsspsvngrereelffralclchtvqvkdddsvdgprkspdggkscvyissspdevalvegvqrlg 522
Cdd:cd07536   385 GGQVL--------------------------------------------------------------------------- 389
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  523 ftylrlkdnymeilnrenhieRFELLEILSFDSVRRRMSVIVKS-ATGEIYLFCKGADSSIFPRVIEGK-VDQIRARVER 600
Cdd:cd07536   390 ---------------------SFCILQLLEFTSDRKRMSVIVRDeSTGEITLYMKGADVAISPIVSKDSyMEQYNDWLEE 448
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  601 NAVEGLRTLCVAYKRLIQEEYEGICKLLQAAKVALQDREKKLAEAYEQIEKDLTLLGATAVEDRLQEKAADTIEALQKAG 680
Cdd:cd07536   449 ECGEGLRTLCVAKKALTENEYQEWESRYTEASLSLHDRSLRVAEVVESLERELELLGLTAIEDRLQAGVPETIETLRKAG 528
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  681 IKVWVLTGDKMETAAATCYACKLFRRNT--QLLELTTKRIEEQSLHDVLFELSKTVLRHsgsltrdnlsglsadmQDYGL 758
Cdd:cd07536   529 IKIWMLTGDKQETAICIAKSCHLVSRTQdiHLLRQDTSRGERAAITQHAHLELNAFRRK----------------HDVAL 592
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  759 IIDGAALSLIMKpredgssgNYRELFLEICRSCSAVLCCRMAPLQKAQIVKLIKfSKEHPITLAIGDGANDVSMILEAHV 838
Cdd:cd07536   593 VIDGDSLEVALK--------YYRHEFVELACQCPAVICCRVSPTQKARIVTLLK-QHTGRRTLAIGDGGNDVSMIQAADC 663
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  839 GIGVIGKEGRQAARNSDYAIPKFKHLKKMLLVHGHFYYIRISELVQYFFYKNVCFIFPQFLYQFFCGFSQQTLYDTAYLT 918
Cdd:cd07536   664 GVGISGKEGKQASLAADYSITQFRHLGRLLLVHGRNSYNRSAALGQYVFYKGLIISTIQAVFSFVFGFSGVPLFQGFLMV 743
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 150421684  919 LYNISFTSLPILLySLMEQHVGIDVLKRDPTLYRDVAKNALLRWRVFIYWTLLGLFDALVFFF 981
Cdd:cd07536   744 GYNVIYTMFPVFS-LVIDQDVKPESAMLYPQLYKDLQKGRSLNFKTFLGWVLISLYHGGILFY 805
PLN03190 PLN03190
aminophospholipid translocase; Provisional
22-1102 0e+00

aminophospholipid translocase; Provisional


Pssm-ID: 215623 [Multi-domain]  Cd Length: 1178  Bit Score: 629.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   22 DSRTIYVGhrEPPPGAEAYipqRYPDNRIVSSKYTFWNFIPKNLFEQFRRVANFYFLIIF----LVQLIIDTPTSPVtsg 97
Cdd:PLN03190   69 DARLVYLN--DPEKSNERF---EFAGNSIRTAKYSVFSFLPRNLFEQFHRVAYIYFLVIAvlnqLPQLAVFGRGASI--- 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   98 LPLFFVITVTAIKQGYEDWLRHKADNAMNQCPVHFIQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNRGDGTCH 177
Cdd:PLN03190  141 LPLAFVLLVTAVKDAYEDWRRHRSDRIENNRLAWVLVDDQFQEKKWKDIRVGEIIKIQANDTLPCDMVLLSTSDPTGVAY 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  178 VTTASLDGESSHKTHYAVQDT-KGFHTEEDIGGLhatIECEQPQPDLYKFVGRINVysdlnDPVVRPLGSENLLLRGATL 256
Cdd:PLN03190  221 VQTINLDGESNLKTRYAKQETlSKIPEKEKINGL---IKCEKPNRNIYGFQANMEV-----DGKRLSLGPSNIILRGCEL 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  257 KNTEKIFGVAIYTGMETKMALNYQSKSQKRSAVEKSMNAFLIVYLCILISKALINTVLKYMWQSEpFRDE----PWYNQK 332
Cdd:PLN03190  293 KNTAWAIGVAVYCGRETKAMLNNSGAPSKRSRLETRMNLEIIILSLFLIALCTIVSVCAAVWLRR-HRDEldtiPFYRRK 371
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  333 TESERQRNLF------LKAFTDFLAFMVLFNYIIPVSMYVTVEMQKFLGSYFITWDEDMFDEETGEGPLVNTSDLNEELG 406
Cdd:PLN03190  372 DFSEGGPKNYnyygwgWEIFFTFLMSVIVFQIMIPISLYISMELVRVGQAYFMIRDDQMYDEASNSRFQCRALNINEDLG 451
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  407 QVEYIFTDKTGTLTENNMEFKECCIEGHVYVPHVICNGQVLPESSG-IDMIDSSP-------------SVNGREREEL-- 470
Cdd:PLN03190  452 QIKYVFSDKTGTLTENKMEFQCASIWGVDYSDGRTPTQNDHAGYSVeVDGKILRPkmkvkvdpqllelSKSGKDTEEAkh 531
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  471 ---FFRALCLCHT-VQVKDDDSVDGPRKSPDggkscvYISSSPDEVALVEGVQRLGFTYLRLKDNYMeILNRENHIERFE 546
Cdd:PLN03190  532 vhdFFLALAACNTiVPIVVDDTSDPTVKLMD------YQGESPDEQALVYAAAAYGFMLIERTSGHI-VIDIHGERQRFN 604
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  547 LLEILSFDSVRRRMSVIVKSATGEIYLFCKGADSSIFPrVIE-----GKVDQIRARVERNAVEGLRTLCVAYKRLIQEEY 621
Cdd:PLN03190  605 VLGLHEFDSDRKRMSVILGCPDKTVKVFVKGADTSMFS-VIDrslnmNVIRATEAHLHTYSSLGLRTLVVGMRELNDSEF 683
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  622 EGICKLLQAAKVALQDREKKLAEAYEQIEKDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAATCYAC 701
Cdd:PLN03190  684 EQWHFSFEAASTALIGRAALLRKVASNVENNLTILGASAIEDKLQQGVPEAIESLRTAGIKVWVLTGDKQETAISIGYSS 763
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  702 KLFRRN-TQL-LELTTKRIEEQSLHDVLFeLSKTVLRHSGslTRDNLSGLSADMQD-YGLIIDGAALSLIMkpredgsSG 778
Cdd:PLN03190  764 KLLTNKmTQIiINSNSKESCRKSLEDALV-MSKKLTTVSG--ISQNTGGSSAAASDpVALIIDGTSLVYVL-------DS 833
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  779 NYRELFLEICRSCSAVLCCRMAPLQKAQIVKLIKfSKEHPITLAIGDGANDVSMILEAHVGIGVIGKEGRQAARNSDYAI 858
Cdd:PLN03190  834 ELEEQLFQLASKCSVVLCCRVAPLQKAGIVALVK-NRTSDMTLAIGDGANDVSMIQMADVGVGISGQEGRQAVMASDFAM 912
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  859 PKFKHLKKMLLVHGHFYYIRISELVQYFFYKNVCFIFPQFLYQFFCGFSQQTLYDTAYLTLYNISFTSLPILLYSLMEQH 938
Cdd:PLN03190  913 GQFRFLVPLLLVHGHWNYQRMGYMILYNFYRNAVFVLVLFWYVLFTCFTLTTAINEWSSVLYSVIYTALPTIVVGILDKD 992
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  939 VGIDVLKRDPTLY----RDVAKNALLRWrvfiYWTLLGLFDALVFFFGAYFVFENTTVtsNGQIFGN-WTFGtlvftvMV 1013
Cdd:PLN03190  993 LSRRTLLKYPQLYgagqRQEAYNSKLFW----LTMIDTLWQSAVVFFVPLFAYWASTI--DGSSIGDlWTLA------VV 1060
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684 1014 FTVTLKLALDTHYWTWINHFVIWGSLLFYVVFSLLWGGViwPFLnyqRMYYVFIQMLSSGPAWLAIVLLVTISLLPDVLK 1093
Cdd:PLN03190 1061 ILVNLHLAMDIIRWNWITHAAIWGSIVATFICVIVIDAI--PTL---PGYWAIFHIAKTGSFWLCLLAIVVAALLPRFVV 1135

                  ....*....
gi 150421684 1094 KVLCRQLWP 1102
Cdd:PLN03190 1136 KVLYQYFTP 1144
P-type_ATPase_APLT_Neo1-like cd07541
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Neo1p and human ...
48-988 3.23e-155

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: 482.29  E-value: 3.23e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   48 NRIVSSKYTFWNFIPKNLFEQFRRVANFYFLIIFLVQLIIDTPTS-PVTSGLPLFFVITVTAIKQGYEDWLRHKADNAMN 126
Cdd:cd07541     2 NEVRNQKYNIFTFLPKVLYEQFKFFYNLYFLVVALSQFVPALKIGyLYTYWAPLGFVLAVTMAKEAVDDIRRRRRDKEQN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  127 QCPVHfiQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNRGDGTCHVTTASLDGESSHKTHYAVQDTKGFHTEED 206
Cdd:cd07541    82 YEKLT--VRGETVEIPSSDIKVGDLIIVEKNQRIPADMVLLRTSEKSGSCFIRTDQLDGETDWKLRIAVPCTQKLPEEGI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  207 IGGLHAtIECEQPQPDLYKFVGRINVYSDlndPVVRPLGSENLLLrGATLKNTEKIFGVAIYTGMETKMALNYQSKSQKR 286
Cdd:cd07541   160 LNSISA-VYAEAPQKDIHSFYGTFTINDD---PTSESLSVENTLW-ANTVVASGTVIGVVVYTGKETRSVMNTSQPKNKV 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  287 SAVEKSMNAFLIVYLCILISKALINTVLKYmwqsepFRDePWYnqkteserqRNLFlkaftdflAFMVLFNYIIPVSMYV 366
Cdd:cd07541   235 GLLDLEINFLTKILFCAVLALSIVMVALQG------FQG-PWY---------IYLF--------RFLILFSSIIPISLRV 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  367 TVEMQKFLGSYFITWDEDMfdeetgEGPLVNTSDLNEELGQVEYIFTDKTGTLTENNMEFKECCIEGHVYvphvicngqv 446
Cdd:cd07541   291 NLDMAKIVYSWQIEHDKNI------PGTVVRTSTIPEELGRIEYLLSDKTGTLTQNEMVFKKLHLGTVSY---------- 354
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  447 lpessgidmidsspsvngrereelffralclchtvqvkdddsvdgprkspdGGKSCVYissspdevalvegvqrlgftyl 526
Cdd:cd07541   355 ---------------------------------------------------GGQNLNY---------------------- 361
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  527 rlkdnymeilnrenhierfELLEILSFDSVRRRMSVIVKS-ATGEIYLFCKGADSsIFPRVIEgKVDQIRARVERNAVEG 605
Cdd:cd07541   362 -------------------EILQIFPFTSESKRMGIIVREeKTGEITFYMKGADV-VMSKIVQ-YNDWLEEECGNMAREG 420
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  606 LRTLCVAYKRLIQEEYEGICKLLQAAKVALQDREKKLAEAYEQIEKDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWV 685
Cdd:cd07541   421 LRTLVVAKKKLSEEEYQAFEKRYNAAKLSIHDRDLKVAEVVESLERELELLCLTGVEDKLQEDVKPTLELLRNAGIKIWM 500
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  686 LTGDKMETAAATCYACKLFRRNtqllelttkrieeQSLHdVLFELSKtvlRHSGSLTRDNLSglsaDMQDYGLIIDGAAL 765
Cdd:cd07541   501 LTGDKLETATCIAKSSKLVSRG-------------QYIH-VFRKVTT---REEAHLELNNLR----RKHDCALVIDGESL 559
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  766 SLIMKpredgssgNYRELFLEICRSCSAVLCCRMAPLQKAQIVKLIKfSKEHPITLAIGDGANDVSMILEAHVGIGVIGK 845
Cdd:cd07541   560 EVCLK--------YYEHEFIELACQLPAVVCCRCSPTQKAQIVRLIQ-KHTGKRTCAIGDGGNDVSMIQAADVGVGIEGK 630
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  846 EGRQAARNSDYAIPKFKHLKKMLLVHGHFYYIRISELVQYFFYKNVCFIFPQFLYQFFCGFSQQTLYDTAYLTLYNISFT 925
Cdd:cd07541   631 EGKQASLAADFSITQFSHIGRLLLWHGRNSYKRSAKLAQFVMHRGLIISIMQAVFSSVFYFAPIALYQGFLMVGYSTIYT 710
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150421684  926 SLPIllYSL-MEQHVGIDVLKRDPTLYRDVAKNALLRWRVFIYWTLLGLFDALVFFFGAYFVFE 988
Cdd:cd07541   711 MAPV--FSLvLDQDVSEELAMLYPELYKELTKGRSLSYKTFFIWVLISIYQGGIIMYGALLLFD 772
ATPase_P-type TIGR01494
ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large ...
94-900 8.88e-122

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: 385.90  E-value: 8.88e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684    94 VTSGLPLFFVITVTAIKQGYEDWLRHKADNAMNQCPVHFIQHGKlVRKQSRKLRVGDIVMVKEDETFPCDLIFLSsnrgd 173
Cdd:TIGR01494    1 FILFLVLLFVLLEVKQKLKAEDALRSLKDSLVNTATVLVLRNGW-KEISSKDLVPGDVVLVKSGDTVPADGVLLS----- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   174 GTCHVTTASLDGESSHKTHYAVQdtkgfhteedigglhatiECEQPQPDLYKFVGRINVysdlndpVVRPLGSENlllrg 253
Cdd:TIGR01494   75 GSAFVDESSLTGESLPVLKTALP------------------DGDAVFAGTINFGGTLIV-------KVTATGILT----- 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   254 atlknTEKIFGVAIYTGMETKMALnyqskSQKRSAVEKsmnaFLIVYLCILISKALINTVLKYMWQSEPFrdepwynqkt 333
Cdd:TIGR01494  125 -----TVGKIAVVVYTGFSTKTPL-----QSKADKFEN----FIFILFLLLLALAVFLLLPIGGWDGNSI---------- 180
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   334 eserqrnlflkaFTDFLAFMVLFNYIIPVSMYVTVEMQKFLGsyfitwDEDMFDEetgeGPLVNTSDLNEELGQVEYIFT 413
Cdd:TIGR01494  181 ------------YKAILRALAVLVIAIPCALPLAVSVALAVG------DARMAKK----GILVKNLNALEELGKVDVICF 238
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   414 DKTGTLTENNMEFKECCIEGhvyvphvicngqvlpessgidmidsspsVNGREREELFFRAlclchtvqvkdddsvdgpr 493
Cdd:TIGR01494  239 DKTGTLTTNKMTLQKVIIIG----------------------------GVEEASLALALLA------------------- 271
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   494 kspdggKSCVYISSSPDEVALVEGVQRLGFTYLRlkdnymeilnrenhIERFELLEILSFDSVRRRMSVIVKSATGEIYL 573
Cdd:TIGR01494  272 ------ASLEYLSGHPLERAIVKSAEGVIKSDEI--------------NVEYKILDVFPFSSVLKRMGVIVEGANGSDLL 331
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   574 FCKGADSSIFPRVIegKVDQIRARVERNAVEGLRTLCVAYKRLiqeeyegickllqaakvalqdrekklaeayeqiEKDL 653
Cdd:TIGR01494  332 FVKGAPEFVLERCN--NENDYDEKVDEYARQGLRVLAFASKKL---------------------------------PDDL 376
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   654 TLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAATCYACKLFrrntqllelttkrieeqslhdvlfelskt 733
Cdd:TIGR01494  377 EFLGLLTFEDPLRPDAKETIEALRKAGIKVVMLTGDNVLTAKAIAKELGID----------------------------- 427
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   734 vlrhsgsltrdnlsglsadmqdygliidgaalslimkpredgssgnyrelfleicrscsavLCCRMAPLQKAQIVKliKF 813
Cdd:TIGR01494  428 -------------------------------------------------------------VFARVKPEEKAAIVE--AL 444
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   814 SKEHPITLAIGDGANDVSMILEAHVGIGVIGKEGRQAArnSDYAIPKFK-HLKKMLLVHGHFYYIRISELVQYFFYKNVC 892
Cdd:TIGR01494  445 QEKGRTVAMTGDGVNDAPALKKADVGIAMGSGDVAKAA--ADIVLLDDDlSTIVEAVKEGRKTFSNIKKNIFWAIAYNLI 522

                   ....*...
gi 150421684   893 FIFPQFLY 900
Cdd:TIGR01494  523 LIPLALLL 530
PhoLip_ATPase_C pfam16212
Phospholipid-translocating P-type ATPase C-terminal; PhoLip_ATPase_C is found at the ...
851-1103 3.47e-100

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: 317.14  E-value: 3.47e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   851 ARNSDYAIPKFKHLKKMLLVHGHFYYIRISELVQYFFYKNVCFIFPQFLYQFFCGFSQQTLYDTAYLTLYNISFTSLPIL 930
Cdd:pfam16212    1 ARASDYAIAQFRFLKRLLLVHGRWSYRRTSKLILYFFYKNIVFTLTQFWYQFYNGFSGQSLYESWYLTLYNLLFTSLPVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   931 LYSLMEQHVGIDVLKRDPTLYRDVAKNALLRWRVFIYWTLLGLFDALVFFFGAYFVFENTTVtSNGQIFGNWTFGTLVFT 1010
Cdd:pfam16212   81 VLGIFDQDVSAETLLAYPELYKLGQKNKFFNLKTFLGWMLDGIYQSLIIFFIPYLAYGDSVF-SGGKDADLWAFGTTVFT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  1011 VMVFTVTLKLALDTHYWTWINHFVIWGSLLFYVVFSLLWGGVIWPFlnYQRMYYVFIQMLSSGPAWLAIVLLVTISLLPD 1090
Cdd:pfam16212  160 ALVLVVNLKLALETHYWTWITHLAIWGSILLYFLFTLIYSSIYPSS--YSVFYGVASRLFGSPSFWLTLLLIVVVALLPD 237
                          250
                   ....*....|...
gi 150421684  1091 VLKKVLCRQLWPT 1103
Cdd:pfam16212  238 FAYKALKRTFFPT 250
MgtA COG0474
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism];
43-1100 3.67e-38

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


Pssm-ID: 440242 [Multi-domain]  Cd Length: 874  Bit Score: 154.49  E-value: 3.67e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   43 QRYPDNRIVSSK-YTFWnfipKNLFEQFRrvaNFYFLIIF---LVQLIIDTPTSPVTsglpLFFVITVTAIkQGYedWLR 118
Cdd:COG0474    37 ARYGPNELPEEKkRSLL----RRFLEQFK---NPLILILLaaaVISALLGDWVDAIV----ILAVVLLNAI-IGF--VQE 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  119 HKADNAM--------NQCPVhfIQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNRgdgtCHVTTASLDGESshk 190
Cdd:COG0474   103 YRAEKALealkkllaPTARV--LRDGKWVEIPAEELVPGDIVLLEAGDRVPADLRLLEAKD----LQVDESALTGES--- 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  191 thYAVqdTKgfHTEedigglhaTIECEQPQPDlykfvgRIN-VYSdlndpvvrplGSenLLLRG-ATlkntekifGVAIY 268
Cdd:COG0474   174 --VPV--EK--SAD--------PLPEDAPLGD------RGNmVFM----------GT--LVTSGrGT--------AVVVA 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  269 TGMET---KMALNYQSKSQKRSAVEKSMNAF--LIVYLCILISkALIntVLKYMwqsepFRDEPWYNqkteserqrnLFL 343
Cdd:COG0474   214 TGMNTefgKIAKLLQEAEEEKTPLQKQLDRLgkLLAIIALVLA-ALV--FLIGL-----LRGGPLLE----------ALL 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  344 KAFTdfLAFMvlfnyIIPVS--MYVTV-------EMQKflgsyfitwdedmfdeetgEGPLVntSDLN--EELGQVEYIF 412
Cdd:COG0474   276 FAVA--LAVA-----AIPEGlpAVVTItlalgaqRMAK-------------------RNAIV--RRLPavETLGSVTVIC 327
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  413 TDKTGTLTENNMEFKECCIEGHVYvphvicngqvlpessgidmidsspSVNGREREEL--FFRALCLCHTVQVkDDDSVD 490
Cdd:COG0474   328 TDKTGTLTQNKMTVERVYTGGGTY------------------------EVTGEFDPALeeLLRAAALCSDAQL-EEETGL 382
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  491 GprkspdggkscvyissSPDEVALVEGVQRLGFTYLRLKDNYmeilnrenhierfELLEILSFDSVRRRMSVIVKSATGE 570
Cdd:COG0474   383 G----------------DPTEGALLVAAAKAGLDVEELRKEY-------------PRVDEIPFDSERKRMSTVHEDPDGK 433
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  571 IYLFCKGADSSIFPR----VIEGKV--------DQIRARVERNAVEGLRTLCVAYKRLiqeeyegickllqaakvalqdr 638
Cdd:COG0474   434 RLLIVKGAPEVVLALctrvLTGGGVvplteedrAEILEAVEELAAQGLRVLAVAYKEL---------------------- 491
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  639 EKKLAEAYEQIEKDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAATCyacklfrrntqllelttKRI 718
Cdd:COG0474   492 PADPELDSEDDESDLTFLGLVGMIDPPRPEAKEAIAECRRAGIRVKMITGDHPATARAIA-----------------RQL 554
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  719 eeqslhdvlfelsktvlrhsgsltrdnlsGLSadmQDYGLIIDGAALSLiMKPREdgssgnyrelFLEICRSCSavLCCR 798
Cdd:COG0474   555 -----------------------------GLG---DDGDRVLTGAELDA-MSDEE----------LAEAVEDVD--VFAR 589
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  799 MAPLQKAQIVKLIKfSKEHpiTLA-IGDGANDVSMILEAHVGIGViGKEGRQAARN-SDyaipkfkhlkkMLLVHGHFY- 875
Cdd:COG0474   590 VSPEHKLRIVKALQ-ANGH--VVAmTGDGVNDAPALKAADIGIAM-GITGTDVAKEaAD-----------IVLLDDNFAt 654
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  876 -----------YIRISELVQYFFYKNVCFIFPQFLyqffcgfsqqtlydtAYLTLYNISFTSLPILLYSL---------- 934
Cdd:COG0474   655 ivaaveegrriYDNIRKFIKYLLSSNFGEVLSVLL---------------ASLLGLPLPLTPIQILWINLvtdglpalal 719
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  935 -MEqHVGIDVLKRDPtlyRDvAKNALLRWRVFIYWTLLGLFdALVFFFGAYFVFENTTVTSNgqifgnwTFGTLVFTVMV 1013
Cdd:COG0474   720 gFE-PVEPDVMKRPP---RW-PDEPILSRFLLLRILLLGLL-IAIFTLLTFALALARGASLA-------LARTMAFTTLV 786
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684 1014 FTVTLK-LALDTHYWTWI------NHFVIWGSLLfyvVFSLLWGGVIWPFLNyqrmyyvfiQMLSSGP----AWLAIVLL 1082
Cdd:COG0474   787 LSQLFNvFNCRSERRSFFksglfpNRPLLLAVLL---SLLLQLLLIYVPPLQ---------ALFGTVPlplsDWLLILGL 854
                        1130
                  ....*....|....*...
gi 150421684 1083 VTISLLPDVLKKVLCRQL 1100
Cdd:COG0474   855 ALLYLLLVELVKLLRRRF 872
P-type_ATPases cd01431
ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, ...
551-907 1.82e-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: 123.33  E-value: 1.82e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  551 LSFDSVRRRMSVIVKSATGEIyLFCKGADSSIFPRVIEGKVDQIRARVER----NAVEGLRTLCVAYKRLIQEEYEgick 626
Cdd:cd01431    25 IPFNSTRKRMSVVVRLPGRYR-AIVKGAPETILSRCSHALTEEDRNKIEKaqeeSAREGLRVLALAYREFDPETSK---- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  627 llqaakvalqdrekklaeayEQIEKDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAATCYACKLFRR 706
Cdd:cd01431   100 --------------------EAVELNLVFLGLIGLQDPPRPEVKEAIAKCRTAGIKVVMITGDNPLTAIAIAREIGIDTK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  707 NTQLLELTTKRIEEQSLHDVLfelsktvlrhsgsltrdnlsglsadmqdygliidgaalslimkpredgssgnyrelfle 786
Cdd:cd01431   160 ASGVILGEEADEMSEEELLDL----------------------------------------------------------- 180
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  787 icrSCSAVLCCRMAPLQKAQIVKLIKFSKEhpITLAIGDGANDVSMILEAHVGIGvIGKEGRQAARNSDYAIPKFKHLKK 866
Cdd:cd01431   181 ---IAKVAVFARVTPEQKLRIVKALQARGE--VVAMTGDGVNDAPALKQADVGIA-MGSTGTDVAKEAADIVLLDDNFAT 254
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 150421684  867 ML--LVHGHFYYIRISELVQYFFYKNVCFIFPQFLYQFFCGFS 907
Cdd:cd01431   255 IVeaVEEGRAIYDNIKKNITYLLANNVAEVFAIALALFLGGPL 297
P-ATPase-V TIGR01657
P-type ATPase of unknown pump specificity (type V); These P-type ATPases form a distinct clade ...
406-851 1.33e-26

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: 117.85  E-value: 1.33e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   406 GQVEYIFTDKTGTLTENNMEFkecciegHVYvphvicngQVLPESSGIDMIDSSPSVNGREReelFFRALCLCHTVQVKD 485
Cdd:TIGR01657  446 GKIDVCCFDKTGTLTEDGLDL-------RGV--------QGLSGNQEFLKIVTEDSSLKPSI---THKALATCHSLTKLE 507
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   486 DDsvdgprkspdggkscvyISSSPDEVALVEGVqrlGFTYLRLKD-NY----MEILNRENHIERFELLEILSFDSVRRRM 560
Cdd:TIGR01657  508 GK-----------------LVGDPLDKKMFEAT---GWTLEEDDEsAEptsiLAVVRTDDPPQELSIIRRFQFSSALQRM 567
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   561 SVIVKSATGEIY-LFCKGADSSIFPRVIEGKV-DQIRARVERNAVEGLRTLCVAYKRLIQEEYEGICKLlqaakvalqDR 638
Cdd:TIGR01657  568 SVIVSTNDERSPdAFVKGAPETIQSLCSPETVpSDYQEVLKSYTREGYRVLALAYKELPKLTLQKAQDL---------SR 638
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   639 EkklaeayeQIEKDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAATCYACKLFRRNTQLL---ELTT 715
Cdd:TIGR01657  639 D--------AVESNLTFLGFIVFENPLKPDTKEVIKELKRASIRTVMITGDNPLTAVHVARECGIVNPSNTLIlaeAEPP 710
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   716 KRIEEQSLH-DVLFELSKTVLRHSGSLTRDNLSGLSADMQDYGLIIDGAALSLIMKpredgssgNYRELFLEICRSCSaV 794
Cdd:TIGR01657  711 ESGKPNQIKfEVIDSIPFASTQVEIPYPLGQDSVEDLLASRYHLAMSGKAFAVLQA--------HSPELLLRLLSHTT-V 781
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 150421684   795 LcCRMAPLQKAQIVKLIKfsKEHPITLAIGDGANDVSMILEAHVGIGVIGKEGRQAA 851
Cdd:TIGR01657  782 F-ARMAPDQKETLVELLQ--KLDYTVGMCGDGANDCGALKQADVGISLSEAEASVAA 835
PhoLip_ATPase_N pfam16209
Phospholipid-translocating ATPase N-terminal; PhoLip_ATPase_N is found at the N-terminus of a ...
26-96 1.66e-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: 97.54  E-value: 1.66e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150421684    26 IYVGHREPPpgaeayIPQRYPDNRIVSSKYTFWNFIPKNLFEQFRRVANFYFLIIFLVQLIID-TPTSPVTS 96
Cdd:pfam16209    1 VYINDPEKN------SEFKYPSNKISTSKYTLLTFLPKNLFEQFRRVANLYFLLIAILQLIPGiSPTGPYTT 66
P-type_ATPase_Ca_PMCA-like cd02081
animal plasma membrane Ca2(+)-ATPases (PMCA), similar to human ATP2B1-4/PMCA1-4, and related ...
508-720 1.96e-23

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: 106.90  E-value: 1.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  508 SPDEVALVEGVQRLGFTYlrlkdNYMEILNREnhierfELLEILSFDSVRRRMSVIVKSATGEIYLFCKGA--------- 578
Cdd:cd02081   340 NKTECALLGFVLELGGDY-----RYREKRPEE------KVLKVYPFNSARKRMSTVVRLKDGGYRLYVKGAseivlkkcs 408
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  579 ----DSSIFPRVIEGKVDQIRARVERNAVEGLRTLCVAYKRLIQEEYegickllqaakvalqDREKKLAEAYEQIEKDLT 654
Cdd:cd02081   409 yilnSDGEVVFLTSEKKEEIKRVIEPMASDSLRTIGLAYRDFSPDEE---------------PTAERDWDDEEDIESDLT 473
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150421684  655 LLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAATCYACKLFRRNTQLLELTTKRIEE 720
Cdd:cd02081   474 FIGIVGIKDPLRPEVPEAVAKCQRAGITVRMVTGDNINTARAIARECGILTEGEDGLVLEGKEFRE 539
P-type_ATPase_Ca_prok cd02089
prokaryotic P-type Ca(2+)-ATPase similar to Synechococcus elongatus sp. strain PCC 7942 PacL ...
63-696 3.26e-22

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: 103.08  E-value: 3.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   63 KNLFEQFRRVanfyFLIIFLVQLIIDTPTSPVTSGLPLFFVITVTAIKQGYEDwlrHKADNA------MNQCPVHFIQHG 136
Cdd:cd02089    29 KKFLEQFKDF----MVIVLLAAAVISGVLGEYVDAIVIIAIVILNAVLGFVQE---YKAEKAlaalkkMSAPTAKVLRDG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  137 KLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNrgdgTCHVTTASLDGESShkthyAVQDTKGFHTEEDIgglhatiec 216
Cdd:cd02089   102 KKQEIPARELVPGDIVLLEAGDYVPADGRLIESA----SLRVEESSLTGESE-----PVEKDADTLLEEDV--------- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  217 eqpqpdlykfvgrinvysdlndpvvrPLGSE-NLLLRGaTLKNTEKIFGVAIYTGMETKM---ALNYQSKSQKRSAVEKS 292
Cdd:cd02089   164 --------------------------PLGDRkNMVFSG-TLVTYGRGRAVVTATGMNTEMgkiATLLEETEEEKTPLQKR 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  293 MN------AFLIVYLCILIskalintVLKYMWQSEPFRDEpwynqkteserqrnlflkaftdFLAFMVLFNYIIPVSMYV 366
Cdd:cd02089   217 LDqlgkrlAIAALIICALV-------FALGLLRGEDLLDM----------------------LLTAVSLAVAAIPEGLPA 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  367 TVEMQKFLGSyfitwdEDMFDEETgegpLVNTSDLNEELGQVEYIFTDKTGTLTENNMefkeccieghvyvphvicngqv 446
Cdd:cd02089   268 IVTIVLALGV------QRMAKRNA----IIRKLPAVETLGSVSVICSDKTGTLTQNKM---------------------- 315
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  447 lpessgidmidsspsvngrereelffralclchTVQVkdddsvdgprkspdggkscVYISSSPDEVALVEGVQRLGFTYL 526
Cdd:cd02089   316 ---------------------------------TVEK-------------------IYTIGDPTETALIRAARKAGLDKE 343
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  527 RLKDNYMEIlnrenhierFELleilSFDSVRRRMSVIVKSATGeIYLFCKGADSSIFPR------------VIEGKVDQI 594
Cdd:cd02089   344 ELEKKYPRI---------AEI----PFDSERKLMTTVHKDAGK-YIVFTKGAPDVLLPRctyiyingqvrpLTEEDRAKI 409
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  595 RARVERNAVEGLRTLCVAYKRLiqeeyegickllqaakvalqdrEKKLAEAYEQIEKDLTLLGATAVEDRLQEKAADTIE 674
Cdd:cd02089   410 LAVNEEFSEEALRVLAVAYKPL----------------------DEDPTESSEDLENDLIFLGLVGMIDPPRPEVKDAVA 467
                         650       660
                  ....*....|....*....|..
gi 150421684  675 ALQKAGIKVWVLTGDKMETAAA 696
Cdd:cd02089   468 ECKKAGIKTVMITGDHKLTARA 489
P-type_ATPase_Mg cd02077
magnesium transporting ATPase (MgtA), similar to Escherichia coli MgtA and Salmonella ...
542-846 2.76e-19

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: 93.85  E-value: 2.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  542 IERFELLEILSFDSVRRRMSVIVKSATGEIYLFCKGADSSIF---PRV-IEGKV--------DQIRARVERNAVEGLRTL 609
Cdd:cd02077   374 IQDYTKIDEIPFDFERRRMSVVVKDNDGKHLLITKGAVEEILnvcTHVeVNGEVvpltdtlrEKILAQVEELNREGLRVL 453
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  610 CVAYKRLIQEEYEgickllqaakvalqdrekklaeaYEQI-EKDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTG 688
Cdd:cd02077   454 AIAYKKLPAPEGE-----------------------YSVKdEKELILIGFLAFLDPPKESAAQAIKALKKNGVNVKILTG 510
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  689 DKmetaaatcyacklfrrntqllELTTKRIeeqsLHDVLFELSKTVLrhsgsltrdnlsglsadmqdyGLIIDgaALSli 768
Cdd:cd02077   511 DN---------------------EIVTKAI----CKQVGLDINRVLT---------------------GSEIE--ALS-- 540
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  769 mkpredgssgnyRELFLEICRSCSavLCCRMAPLQKAQIVKLIKfSKEHPITLaIGDGANDVSMILEAHVGIGV-----I 843
Cdd:cd02077   541 ------------DEELAKIVEETN--IFAKLSPLQKARIIQALK-KNGHVVGF-MGDGINDAPALRQADVGISVdsavdI 604

                  ...
gi 150421684  844 GKE 846
Cdd:cd02077   605 AKE 607
P-type_ATPase_cation cd07542
P-type cation-transporting ATPases, similar to human ATPase type 13A2 (ATP13A2) protein and ...
406-840 7.08e-19

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: 92.31  E-value: 7.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  406 GQVEYIFTDKTGTLTENNMEFkecciegHVYVPHVICNGQVLPESSGIDMIDSSPSVNgrereeLFFRALCLCHTVQVKD 485
Cdd:cd07542   303 GKINLVCFDKTGTLTEDGLDL-------WGVRPVSGNNFGDLEVFSLDLDLDSSLPNG------PLLRAMATCHSLTLID 369
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  486 DDsvdgprkspdggkscvyISSSPDEVALVEgvqrlgFTylrlkdNY-MEILnrenhiERFElleilsFDSVRRRMSVIV 564
Cdd:cd07542   370 GE-----------------LVGDPLDLKMFE------FT------GWsLEIL------RQFP------FSSALQRMSVIV 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  565 KSATGEIY-LFCKGADSSIF----PRVIEGKVDQIrarVERNAVEGLRTLCVAYKRLIQeeyegickllqaaKVALQDRE 639
Cdd:cd07542   409 KTPGDDSMmAFTKGAPEMIAslckPETVPSNFQEV---LNEYTKQGFRVIALAYKALES-------------KTWLLQKL 472
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  640 KKlaeayEQIEKDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAatcyacklfrrntqllelttkrie 719
Cdd:cd07542   473 SR-----EEVESDLEFLGLIVMENRLKPETAPVINELNRANIRTVMVTGDNLLTAI------------------------ 523
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  720 eqslhdvlfelskTVLRHSGSLTRDNLSglsadmqdyglIIDGAAlslimkPREDGSSGNyreLFLEICRSCSaVLcCRM 799
Cdd:cd07542   524 -------------SVARECGMISPSKKV-----------ILIEAV------KPEDDDSAS---LTWTLLLKGT-VF-ARM 568
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 150421684  800 APLQKAQIVKLIkfsKEHPITLAI-GDGANDVSMILEAHVGI 840
Cdd:cd07542   569 SPDQKSELVEEL---QKLDYTVGMcGDGANDCGALKAADVGI 607
P-type_ATPase_SERCA cd02083
sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; ...
403-840 1.10e-16

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: 85.81  E-value: 1.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  403 EELGQVEYIFTDKTGTLTENNM---------------EFKECCIEGHVYVPhvicngqvlpessgIDMIDSSPSVNGRER 467
Cdd:cd02083   335 ETLGCTSVICSDKTGTLTTNQMsvsrmfildkveddsSLNEFEVTGSTYAP--------------EGEVFKNGKKVKAGQ 400
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  468 EELFFRALCLChtvQVKDDDSVDgprksPDGGKSCVYISSSPDEVALVEGVQRLGFTYLRLKDNYMEIL-NRENHI--ER 544
Cdd:cd02083   401 YDGLVELATIC---ALCNDSSLD-----YNESKGVYEKVGEATETALTVLVEKMNVFNTDKSGLSKRERaNACNDVieQL 472
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  545 FELLEILSFDSVRRRMSVIVKSATGEI--YLFCKGADSSI-----FPRVIEGKV--------DQIRARVERNAVEGLRTL 609
Cdd:cd02083   473 WKKEFTLEFSRDRKSMSVYCSPTKASGgnKLFVKGAPEGVlerctHVRVGGGKVvpltaaikILILKKVWGYGTDTLRCL 552
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  610 CVAYKRliqeeyegickllqaAKVALQDREKKLAEAYEQIEKDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGD 689
Cdd:cd02083   553 ALATKD---------------TPPKPEDMDLEDSTKFYKYETDLTFVGVVGMLDPPRPEVRDSIEKCRDAGIRVIVITGD 617
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  690 KMETAAATCYACKLFRRNTQlleLTTKrieeqslhdvlfelsktvlrhsgSLTRDNLSGLSADMQdygliidgaalslim 769
Cdd:cd02083   618 NKGTAEAICRRIGIFGEDED---TTGK-----------------------SYTGREFDDLSPEEQ--------------- 656
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150421684  770 kpredgssgnyrelfLEICRscSAVLCCRMAPLQKAQIVKLIKFSKEhpITLAIGDGANDVSMILEAHVGI 840
Cdd:cd02083   657 ---------------REACR--RARLFSRVEPSHKSKIVELLQSQGE--ITAMTGDGVNDAPALKKAEIGI 708
P-type_ATPase_cation cd07543
P-type cation-transporting ATPases, similar to human cation-transporting ATPase type 13A1 ...
406-843 1.38e-16

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: 85.13  E-value: 1.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  406 GQVEYIFTDKTGTLTENNMEFkecciEGhvyVPHVICNGQVLPESSgidmIDSSPSVngrereelffRALCLCHTVQVKD 485
Cdd:cd07543   309 GKVDICCFDKTGTLTSDDLVV-----EG---VAGLNDGKEVIPVSS----IEPVETI----------LVLASCHSLVKLD 366
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  486 DDSVDGprkspdggkscvyissSPDEVALVEGVqrlGFTYLRLKDNYMEILNRENH--IERFelleilSFDSVRRRMSVI 563
Cdd:cd07543   367 DGKLVG----------------DPLEKATLEAV---DWTLTKDEKVFPRSKKTKGLkiIQRF------HFSSALKRMSVV 421
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  564 V-----KSATGEIYLFCKGAdssifPRVIEGKVDQIRARVE----RNAVEGLRTLCVAYKRLiqeeyegicKLLQAAKVA 634
Cdd:cd07543   422 AsykdpGSTDLKYIVAVKGA-----PETLKSMLSDVPADYDevykEYTRQGSRVLALGYKEL---------GHLTKQQAR 487
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  635 LQDREkklaeayeQIEKDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAaatCYACKlfrrntqllELT 714
Cdd:cd07543   488 DYKRE--------DVESDLTFAGFIVFSCPLKPDSKETIKELNNSSHRVVMITGDNPLTA---CHVAK---------ELG 547
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  715 tkrieeqslhdvlfelsktvlrhsgsltrdnlsglsadmqdyglIIDGAALSLImkPREDGSSGNYRELFleicrscSAV 794
Cdd:cd07543   548 --------------------------------------------IVDKPVLILI--LSEEGKSNEWKLIP-------HVK 574
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 150421684  795 LCCRMAPLQKAQIVKLIKfsKEHPITLAIGDGANDVSMILEAHVGIGVI 843
Cdd:cd07543   575 VFARVAPKQKEFIITTLK--ELGYVTLMCGDGTNDVGALKHAHVGVALL 621
P-type_ATPase_Na_ENA cd02086
fungal-type Na(+)-ATPase, similar to the plasma membrane sodium transporters Saccharomyces ...
403-696 4.49e-16

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: 83.66  E-value: 4.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  403 EELGQVEYIFTDKTGTLTENNMefkeccIEGHVYVPHVICNgqvlpessgidmidsSPSVNGREREelffralclcHTVQ 482
Cdd:cd02086   323 EALGAVTDICSDKTGTLTQGKM------VVRQVWIPAALCN---------------IATVFKDEET----------DCWK 371
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  483 VKDDdsvdgprkspdggkscvyisssPDEVALVEGVQRLGFTYLRLKDNymeiLNREN-HIERFelleilSFDSVRRRMS 561
Cdd:cd02086   372 AHGD----------------------PTEIALQVFATKFDMGKNALTKG----GSAQFqHVAEF------PFDSTVKRMS 419
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  562 VIVKS-ATGEIYLFCKGADSSIFPR------------VIEGKVDQIRARVERNAVEGLRTLCVAYKRLiqeeyegickll 628
Cdd:cd02086   420 VVYYNnQAGDYYAYMKGAVERVLECcssmygkdgiipLDDEFRKTIIKNVESLASQGLRVLAFASRSF------------ 487
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150421684  629 qaAKVALQDREKKLAE-AYEQIEKDLTLLGATAVED--RLQEKAAdtIEALQKAGIKVWVLTGDKMETAAA 696
Cdd:cd02086   488 --TKAQFNDDQLKNITlSRADAESDLTFLGLVGIYDppRNESAGA--VEKCHQAGITVHMLTGDHPGTAKA 554
P-type_ATPase cd07539
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ...
548-853 4.27e-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: 80.15  E-value: 4.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  548 LEILSFDSVRRRMSVIVKSATGEIYLFCKGADSSIFPR--------VIEGKVDQIRARVERN----AVEGLRTLCVAYKR 615
Cdd:cd07539   324 LAELPFESSRGYAAAIGRTGGGIPLLAVKGAPEVVLPRcdrrmtggQVVPLTEADRQAIEEVnellAGQGLRVLAVAYRT 403
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  616 LiqeeyegickllqaakvalQDREKKLAEAyeqIEKDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAA 695
Cdd:cd07539   404 L-------------------DAGTTHAVEA---VVDDLELLGLLGLADTARPGAAALIAALHDAGIDVVMITGDHPITAR 461
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  696 AtcYACKLfrrntqllelttkrieeqslhdvlfelsktvlrhsgsltrdnlsGLSADMQdyglIIDGAALS-LIMKPRED 774
Cdd:cd07539   462 A--IAKEL--------------------------------------------GLPRDAE----VVTGAELDaLDEEALTG 491
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150421684  775 GSSGnyrelfleicrscsAVLCCRMAPLQKAQIVKLIKFSKEhpITLAIGDGANDVSMILEAHVGIGViGKEGRQAARN 853
Cdd:cd07539   492 LVAD--------------IDVFARVSPEQKLQIVQALQAAGR--VVAMTGDGANDAAAIRAADVGIGV-GARGSDAARE 553
P-type_ATPase_cation cd02082
P-type cation-transporting ATPases, similar to human ATPase type 13A1-A4 (ATP13A1-A4) proteins ...
406-851 2.98e-14

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: 77.63  E-value: 2.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  406 GQVEYIFTDKTGTLTENNMEFKECCIEGhvyvphvicNGQVLPESSGIDMIDSSpsvngrereeLFFRALCLCHTVqVKD 485
Cdd:cd02082   301 GRIQTLCFDKTGTLTEDKLDLIGYQLKG---------QNQTFDPIQCQDPNNIS----------IEHKLFAICHSL-TKI 360
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  486 DDSVDGprkspdggkscvyissSPDEVALVEGVqrlgfTYLRLKDNYMEILNRENHIERFELLEILSFDSVRRRMSVI-- 563
Cdd:cd02082   361 NGKLLG----------------DPLDVKMAEAS-----TWDLDYDHEAKQHYSKSGTKRFYIIQVFQFHSALQRMSVVak 419
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  564 -VKSATGEI--YLFCKGAdssifPRVIEGKVDQI----RARVERNAVEGLRTLCVAYKRLIQEEYEgickllqaakvalq 636
Cdd:cd02082   420 eVDMITKDFkhYAFIKGA-----PEKIQSLFSHVpsdeKAQLSTLINEGYRVLALGYKELPQSEID-------------- 480
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  637 dreKKLAEAYEQIEKDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETaaatcyACKLfrrntqllelttk 716
Cdd:cd02082   481 ---AFLDLSREAQEANVQFLGFIIYKNNLKPDTQAVIKEFKEACYRIVMITGDNPLT------ALKV------------- 538
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  717 rieEQSLHDVLfELSKTVLRHsgsltrdnlsglsadmqdygliidgaalsLIMKPREDGSSGNYRELFleicrscSAVLC 796
Cdd:cd02082   539 ---AQELEIIN-RKNPTIIIH-----------------------------LLIPEIQKDNSTQWILII-------HTNVF 578
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 150421684  797 CRMAPLQKAQIVKLIKFSKEhpITLAIGDGANDVSMILEAHVGIGVIGKEGRQAA 851
Cdd:cd02082   579 ARTAPEQKQTIIRLLKESDY--IVCMCGDGANDCGALKEADVGISLAEADASFAS 631
P-type_ATPase_cation cd02080
P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, ...
403-696 1.33e-13

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: 75.38  E-value: 1.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  403 EELGQVEYIFTDKTGTLTENNMEFKeccieghvyvphvicngqvlpessgidmidsspsvngrereelffRALCLCHTVQ 482
Cdd:cd02080   294 ETLGSVTVICSDKTGTLTRNEMTVQ---------------------------------------------AIVTLCNDAQ 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  483 VKDDDSVDGprkspdggkscvyISSSPDEVALVEGVQRLGftylrlkdnymeiLNRENHIERFELLEILSFDSVRRRMSV 562
Cdd:cd02080   329 LHQEDGHWK-------------ITGDPTEGALLVLAAKAG-------------LDPDRLASSYPRVDKIPFDSAYRYMAT 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  563 IVKSATGEIyLFCKGADSSIFPR---------VIEGKVDQIRARVERNAVEGLRTLCVAYKrliqeeyegickllqaakv 633
Cdd:cd02080   383 LHRDDGQRV-IYVKGAPERLLDMcdqelldggVSPLDRAYWEAEAEDLAKQGLRVLAFAYR------------------- 442
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 150421684  634 ALQDREKKLAEAyeQIEKDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAA 696
Cdd:cd02080   443 EVDSEVEEIDHA--DLEGGLTFLGLQGMIDPPRPEAIAAVAECQSAGIRVKMITGDHAETARA 503
PRK10517 PRK10517
magnesium-transporting P-type ATPase MgtA;
543-846 3.06e-13

magnesium-transporting P-type ATPase MgtA;


Pssm-ID: 236705 [Multi-domain]  Cd Length: 902  Bit Score: 74.34  E-value: 3.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  543 ERFELLEILSFDSVRRRMSVIVKSATGEIYLFCKGADS---SIFPRV-IEGKV----DQIRARVER-----NAvEGLRTL 609
Cdd:PRK10517  439 SRWQKIDEIPFDFERRRMSVVVAENTEHHQLICKGALEeilNVCSQVrHNGEIvpldDIMLRRIKRvtdtlNR-QGLRVV 517
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  610 CVAYKRLIQEEyegickllqaakvalqdrekklaEAYEQI-EKDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTG 688
Cdd:PRK10517  518 AVATKYLPARE-----------------------GDYQRAdESDLILEGYIAFLDPPKETTAPALKALKASGVTVKILTG 574
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  689 DKMETAAATCYACKLFRRNTqlleLTTKRIEEQSlhDVlfELSKTVLRHSgsltrdnlsglsadmqdygliidgaalsli 768
Cdd:PRK10517  575 DSELVAAKVCHEVGLDAGEV----LIGSDIETLS--DD--ELANLAERTT------------------------------ 616
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  769 mkpredgssgnyreLFleicrscsavlcCRMAPLQKAQIVKLIKfsKEHPITLAIGDGANDVSMILEAHVGIGV-----I 843
Cdd:PRK10517  617 --------------LF------------ARLTPMHKERIVTLLK--REGHVVGFMGDGINDAPALRAADIGISVdgavdI 668

                  ...
gi 150421684  844 GKE 846
Cdd:PRK10517  669 ARE 671
ATPase-IID_K-Na TIGR01523
potassium and/or sodium efflux P-type ATPase, fungal-type; Initially described as a calcium ...
395-696 6.41e-13

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


Pssm-ID: 130586 [Multi-domain]  Cd Length: 1053  Bit Score: 73.51  E-value: 6.41e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   395 LVNTSDLNEELGQVEYIFTDKTGTLTENNMEFKECCI------------------EGHVY-VPHVICNGQVLPESSGIDM 455
Cdd:TIGR01523  346 IVRKLDALEALGAVNDICSDKTGTITQGKMIARQIWIprfgtisidnsddafnpnEGNVSgIPRFSPYEYSHNEAADQDI 425
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   456 IDS---------SPSVNGREREELFFRALCLCHTVQVKDDDSVDgprkspdggksCVYISSSPDEVALVEGVQRLGFTYL 526
Cdd:TIGR01523  426 LKEfkdelkeidLPEDIDMDLFIKLLETAALANIATVFKDDATD-----------CWKAHGDPTEIAIHVFAKKFDLPHN 494
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   527 RL-------KDNYMEILNRENHIER-----FELLEILSFDSVRRRMSVIVKSATGEIY-LFCKGADSSIFPR-------- 585
Cdd:TIGR01523  495 ALtgeedllKSNENDQSSLSQHNEKpgsaqFEFIAEFPFDSEIKRMASIYEDNHGETYnIYAKGAFERIIECcsssngkd 574
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   586 ------VIEGKVDQIRARVERNAVEGLRTLCVAYKRLIQEEYEgickllqaakvalQDREKKLAEAYEQIEKDLTLLGAT 659
Cdd:TIGR01523  575 gvkispLEDCDRELIIANMESLAAEGLRVLAFASKSFDKADNN-------------DDQLKNETLNRATAESDLEFLGLI 641
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 150421684   660 AVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAA 696
Cdd:TIGR01523  642 GIYDPPRNESAGAVEKCHQAGINVHMLTGDFPETAKA 678
Cation_ATPase pfam13246
Cation transport ATPase (P-type); This domain is found in cation transport ATPases, including ...
476-585 2.68e-12

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: 63.78  E-value: 2.68e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   476 CLCHTVQVKDDDSVDGprkspdggkscVYISSSPDEVALVEGVQRLGFtylrlkdNYMEILnrenhiERFELLEILSFDS 555
Cdd:pfam13246    1 ALCNSAAFDENEEKGK-----------WEIVGDPTESALLVFAEKMGI-------DVEELR------KDYPRVAEIPFNS 56
                           90       100       110
                   ....*....|....*....|....*....|.
gi 150421684   556 VRRRMSVIVK-SATGEIYLFCKGADSSIFPR 585
Cdd:pfam13246   57 DRKRMSTVHKlPDDGKYRLFVKGAPEIILDR 87
PRK15122 PRK15122
magnesium-transporting ATPase; Provisional
551-846 3.61e-12

magnesium-transporting ATPase; Provisional


Pssm-ID: 237914 [Multi-domain]  Cd Length: 903  Bit Score: 70.82  E-value: 3.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  551 LSFDSVRRRMSVIVKSATGEIYLFCKGADS---SIFPRVIEGKV-----DQIRARVERNAVE----GLRTLCVAYKRLIQ 618
Cdd:PRK15122  445 LPFDFVRRRLSVVVEDAQGQHLLICKGAVEemlAVATHVRDGDTvrpldEARRERLLALAEAynadGFRVLLVATREIPG 524
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  619 EEyegICKLLQAAKvalqdrekklaeayeqiEKDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDkmeTAAATC 698
Cdd:PRK15122  525 GE---SRAQYSTAD-----------------ERDLVIRGFLTFLDPPKESAAPAIAALRENGVAVKVLTGD---NPIVTA 581
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  699 YACklfrRNTQL---LELTTKRIEEqsLHDVlfELSKTVLRhsgsltrdnlsglsadmqdygliidgaalslimkpredg 775
Cdd:PRK15122  582 KIC----REVGLepgEPLLGTEIEA--MDDA--ALAREVEE--------------------------------------- 614
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150421684  776 ssgnyRELFleicrscsavlcCRMAPLQKAQIVKLIKfSKEHPITLaIGDGANDVSMILEAHVGIGV-----IGKE 846
Cdd:PRK15122  615 -----RTVF------------AKLTPLQKSRVLKALQ-ANGHTVGF-LGDGINDAPALRDADVGISVdsgadIAKE 671
ATPase-IIIB_Mg TIGR01524
magnesium-translocating P-type ATPase; This model describes the magnesium translocating P-type ...
544-842 2.38e-10

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


Pssm-ID: 130587 [Multi-domain]  Cd Length: 867  Bit Score: 64.89  E-value: 2.38e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   544 RFELLEILSFDSVRRRMSVIVKSATGEIYLFCKGADSSIFP---------RVI---EGKVDQIRARVERNAVEGLRTLCV 611
Cdd:TIGR01524  405 RWKKVDEIPFDFDRRRLSVVVENRAEVTRLICKGAVEEMLTvcthkrfggAVVtlsESEKSELQDMTAEMNRQGIRVIAV 484
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   612 AYKRLIQEEyegickllqaAKVALQDrekklaeayeqiEKDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKm 691
Cdd:TIGR01524  485 ATKTLKVGE----------ADFTKTD------------EEQLIIEGFLGFLDPPKESTKEAIAALFKNGINVKVLTGDN- 541
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   692 etaaatcyacklfrrntqllELTTKRIeeqsLHDVlfelsktVLRHSGSLTRDNLSGLSadmqdygliiDGAALSLIMKp 771
Cdd:TIGR01524  542 --------------------EIVTARI----CQEV-------GIDANDFLLGADIEELS----------DEELARELRK- 579
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150421684   772 redgssgnyRELFleicrscsavlcCRMAPLQKAQIVKLIKfsKEHPITLAIGDGANDVSMILEAHVGIGV 842
Cdd:TIGR01524  580 ---------YHIF------------ARLTPMQKSRIIGLLK--KAGHTVGFLGDGINDAPALRKADVGISV 627
P-type_ATPase_Cu-like cd02094
P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A ...
626-696 1.53e-08

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: 59.03  E-value: 1.53e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150421684  626 KLLQAAKVALQDREKKLAEAYEQ------IEKDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAA 696
Cdd:cd02094   424 RLMEENGIDLSALEAEALALEEEgktvvlVAVDGELAGLIAVADPLKPDAAEAIEALKKMGIKVVMLTGDNRRTARA 500
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
626-696 6.68e-08

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 56.69  E-value: 6.68e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 150421684  626 KLLQAAKVALQDREKKLAEAYEQIEK-------DLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAA 696
Cdd:COG2217   496 RLLEEEGIDLPEALEERAEELEAEGKtvvyvavDGRLLGLIALADTLRPEAAEAIAALKALGIRVVMLTGDNERTAEA 573
P-type_ATPase cd02609
uncharacterized subfamily of P-type ATPase transporter, similar to uncharacterized ...
403-904 3.50e-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: 54.59  E-value: 3.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  403 EELGQVEYIFTDKTGTLTENNMEFKEccieghvyvphvicngqVLPessgidmidsspsVNGREREELFFRALCLCHTvq 482
Cdd:cd02609   281 ETLARVDVLCLDKTGTITEGKMKVER-----------------VEP-------------LDEANEAEAAAALAAFVAA-- 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  483 vkdddsvdgprkspdggkscvyiSSSPDEVAlvegvqrlgftylrlkdnyMEILNRENHIERFELLEILSFDSVRRrMSV 562
Cdd:cd02609   329 -----------------------SEDNNATM-------------------QAIRAAFFGNNRFEVTSIIPFSSARK-WSA 365
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  563 IVKSATGEIYLfckGAdssifPRVIEGKVD-QIRARVERNAVEGLRTLCVAYkrliqeeyegickllqaAKVALQDrekk 641
Cdd:cd02609   366 VEFRDGGTWVL---GA-----PEVLLGDLPsEVLSRVNELAAQGYRVLLLAR-----------------SAGALTH---- 416
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  642 laeayEQIEKDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAAtcyacklfrrntqllelttkrIEEQ 721
Cdd:cd02609   417 -----EQLPVGLEPLALILLTDPIRPEAKETLAYFAEQGVAVKVISGDNPVTVSA---------------------IAKR 470
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  722 slhdvlfelsktvlrhsgsltrdnlsglsADMQDYGLIIDGAALslimKPREDgssgnYRELfLEicrscSAVLCCRMAP 801
Cdd:cd02609   471 -----------------------------AGLEGAESYIDASTL----TTDEE-----LAEA-VE-----NYTVFGRVTP 506
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  802 LQKAQIVKLIKfSKEHpiTLA-IGDGANDVSMILEAHVGIGVigKEGRQAAR--------NSDyaipkFKHLKKMLLvHG 872
Cdd:cd02609   507 EQKRQLVQALQ-ALGH--TVAmTGDGVNDVLALKEADCSIAM--ASGSDATRqvaqvvllDSD-----FSALPDVVF-EG 575
                         490       500       510
                  ....*....|....*....|....*....|..
gi 150421684  873 HFYYIRISELVQYFFYKNVCFIFPQFLYQFFC 904
Cdd:cd02609   576 RRVVNNIERVASLFLVKTIYSVLLALICVITA 607
COG4087 COG4087
Soluble P-type ATPase [General function prediction only];
802-859 2.01e-06

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


Pssm-ID: 443263 [Multi-domain]  Cd Length: 156  Bit Score: 48.62  E-value: 2.01e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  802 LQKAQIVKliKFSKEHpiTLAIGDGANDVSMILEAHVGIGVIGKEG--RQAARNSDYAIP 859
Cdd:COG4087    80 EEKLEFVE--KLGAET--TVAIGNGRNDVLMLKEAALGIAVIGPEGasVKALLAADIVVK 135
P-type_ATPase_HM cd02079
P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) ...
649-697 2.66e-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: 51.45  E-value: 2.66e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 150421684  649 IEKDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAAT 697
Cdd:cd02079   433 VGRDGKLVGLFALEDQLRPEAKEVIAELKSGGIKVVMLTGDNEAAAQAV 481
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
806-849 5.44e-05

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: 45.81  E-value: 5.44e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 150421684   806 QIVKLIKFSKEHpiTLAIGDGANDVSMILEAHVGIGVIGKEGRQ 849
Cdd:TIGR00338  159 ILLRKEGISPEN--TVAVGDGANDLSMIKAAGLGIAFNAKPKLQ 200
E1-E2_ATPase pfam00122
E1-E2 ATPase;
136-187 9.74e-04

E1-E2 ATPase;


Pssm-ID: 425475 [Multi-domain]  Cd Length: 181  Bit Score: 41.40  E-value: 9.74e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 150421684   136 GKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSsnrgdGTCHVTTASLDGES 187
Cdd:pfam00122   13 GTEEEVPADELVPGDIVLLKPGERVPADGRIVE-----GSASVDESLLTGES 59
R3H_PARN cd02637
R3H domain of Poly(A)-specific ribonuclease (PARN). PARN is a poly(A)-specific 3' exonuclease ...
639-695 9.82e-04

R3H domain of Poly(A)-specific ribonuclease (PARN). PARN is a poly(A)-specific 3' exonuclease from the RNase D family that, in Xenopus, deadenylates a specific class of maternal mRNAs which results in their translational repression. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA.


Pssm-ID: 100066 [Multi-domain]  Cd Length: 65  Bit Score: 38.46  E-value: 9.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 150421684  639 EKKLAEAYEQIEKDLTLLGATAVEDRLQEkaaDTIEALQKAGIKVWVLTGDKMETAA 695
Cdd:cd02637     5 IERIEAFLESEEDDLELEPCNGFQRKLIY---QTLEQKYPKGIHVETLETEKKERLI 58
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
603-837 1.35e-03

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


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 41.03  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   603 VEGLRTLCVAYKRLIQEEYEGICKLLQAAKVALQDREKKLAEAYEQIEKDLtlLGATAVEDRLQ--EKAADTIEALQKAG 680
Cdd:pfam00702   37 VAAAEDLPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEGLTVVLVEL--LGVIALADELKlyPGAAEALKALKERG 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   681 IKVWVLTGDKMETAAAtcyacklfrrntqllelttkrieeqslhdvlfelsktVLRHSGSLtrdnlsglsadmqDYGLII 760
Cdd:pfam00702  115 IKVAILTGDNPEAAEA-------------------------------------LLRLLGLD-------------DYFDVV 144
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150421684   761 DGAALSLIMKPredgssgnyrelfleicrscsavlccrmAPLQKAQIVKLIKFSKEHpiTLAIGDGANDVSMILEAH 837
Cdd:pfam00702  145 ISGDDVGVGKP----------------------------KPEIYLAALERLGVKPEE--VLMVGDGVNDIPAAKAAG 191
zntA PRK11033
zinc/cadmium/mercury/lead-transporting ATPase; Provisional
651-696 2.35e-03

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


Pssm-ID: 236827 [Multi-domain]  Cd Length: 741  Bit Score: 41.90  E-value: 2.35e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 150421684  651 KDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAA 696
Cdd:PRK11033  555 RNDDVLGLIALQDTLRADARQAISELKALGIKGVMLTGDNPRAAAA 600
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
820-841 2.80e-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: 39.84  E-value: 2.80e-03
                          10        20
                  ....*....|....*....|..
gi 150421684  820 TLAIGDGANDVSMILEAHVGIG 841
Cdd:cd07500   156 TVAVGDGANDLPMLKAAGLGIA 177
P-type_ATPase_Pb_Zn_Cd2-like cd07546
P-type heavy metal-transporting ATPase, similar to Escherichia coli ZntA which is selective ...
629-696 5.99e-03

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


Pssm-ID: 319846 [Multi-domain]  Cd Length: 597  Bit Score: 40.47  E-value: 5.99e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150421684  629 QAAKVALQDREKKLAEAYEQIEKDLTL-------LGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAA 696
Cdd:cd07546   383 KFAADRGTLEVQGRIAALEQAGKTVVVvlangrvLGLIALRDELRPDAAEAVAELNALGIKALMLTGDNPRAAAA 457
HAD pfam12710
haloacid dehalogenase-like hydrolase;
594-688 7.01e-03

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 39.05  E-value: 7.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684   594 IRARVERNAVEGLRTLCVAYKRLIqeeYEGICKLLQAAKVALQDREkkLAEAYEQIEKDLTLLGATAVEDRLQEKAADTI 673
Cdd:pfam12710   19 IRALLRRGGPDLWRALLVLLLLAL---LRLLGRLSRAGARELLRAL--LAGLPEEDAAELERFVAEVALPRLHPGALELL 93
                           90
                   ....*....|....*
gi 150421684   674 EALQKAGIKVWVLTG 688
Cdd:pfam12710   94 AAHRAAGDRVVVVTG 108
serB PRK11133
phosphoserine phosphatase; Provisional
804-840 7.96e-03

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 39.93  E-value: 7.96e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 150421684  804 KAQIvkLIKFSKEHPI----TLAIGDGANDVSMILEAHVGI 840
Cdd:PRK11133  249 KADT--LTRLAQEYEIplaqTVAIGDGANDLPMIKAAGLGI 287
P-type_ATPase_HM cd02079
P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) ...
100-187 9.08e-03

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: 39.89  E-value: 9.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150421684  100 LFFVitvtAIKQGYEDWLRHKADNAMNQ------CPVHFIQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSsnrgd 173
Cdd:cd02079    95 LFLF----LLGRYLEERARSRARSALKAllslapETATVLEDGSTEEVPVDDLKVGDVVLVKPGERIPVDGVVVS----- 165
                          90
                  ....*....|....
gi 150421684  174 GTCHVTTASLDGES 187
Cdd:cd02079   166 GESSVDESSLTGES 179
P-type_ATPase_Cu-like cd07552
P-type heavy metal-transporting ATPase, similar to Archaeoglobus fulgidus CopB, a Cu(2+) ...
651-696 9.28e-03

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


Pssm-ID: 319850 [Multi-domain]  Cd Length: 632  Bit Score: 39.98  E-value: 9.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 150421684  651 KDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAA 696
Cdd:cd07552   442 QDGEVIGAIALGDEIKPESKEAIRALKAQGITPVMLTGDNEEVAQA 487
 
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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