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Conserved domains on  [gi|568916992|ref|XP_006499563|]
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probable phospholipid-transporting ATPase IM isoform X4 [Mus musculus]

Protein Classification

HAD family hydrolase( domain architecture ID 229399)

HAD (haloacid dehalogenase) family hydrolase; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

EC:  3.6.3.-
Gene Ontology:  GO:0005524|GO:0016887|GO:0005215

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
31-707 0e+00

Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.


The actual alignment was detected with superfamily member cd02073:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 836  Bit Score: 925.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  31 DNRIHTSKYNVLTFLPINLFEQLQRVANAYFLFLLILQLIPEISSLTWFTTIVPLVLVISMTAVKDATDDYFRHKSDNQV 110
Cdd:cd02073    1 DNRISTTKYTVFTFLPKNLFEQFRRVANLYFLFIAILQQIPGISPTGPYTTLLPLLFVLGVTAIKEGYEDIRRHKSDNEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 111 NNRQSKVLINSKLQNEKWMNVKVGDIIKLENNQFVAADLLLLSSSEPHGLCYVETAELDGETNLKVRQALPVTSELGaDI 190
Cdd:cd02073   81 NNRPVQVLRGGKFVKKKWKDIRVGDIVRVKNDEFVPADLLLLSSSEPDGLCYVETANLDGETNLKIRQALPETALLL-SE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 191 SSLAEFDGIVRCEAPNNKLDRFSGVLSWKDSK-HALSNQKIILRGCVLRNTSWCFGMVLFAGPDTKLMQNSGKTKFKRTS 269
Cdd:cd02073  160 EDLARFSGEIECEQPNNDLYTFNGTLELNGGReLPLSPDNLLLRGCTLRNTEWVYGVVVYTGHETKLMLNSGGTPLKRSS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 270 IDRLMNTLVLWIFGFLVCLGIILAVGSSILESEVGdqfRTPPFWREGEKSF-LFSGFLTFWSYVIILNTLVPISLYVSVE 348
Cdd:cd02073  240 IEKKMNRFIIAIFCILIVMCLISAIGKGIWLSKHG---RDLWYLLPKEERSpALEFFFDFLTFIILYNNLIPISLYVTIE 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 349 VIRLGHSYFINWDRKMYYASKAMPAEARTTTLNEELGQIEYIFSDKTGTLTQNIMTFKKCSINGRVYAgevlddpiqkke 428
Cdd:cd02073  317 VVKFLQSFFINWDLDMYDEETDTPAEARTSNLNEELGQVEYIFSDKTGTLTENIMEFKKCSINGVDYG------------ 384
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 429 itkekeatdfssksksektlhffdqslmesielgdpkvheFLRLLALCHTVM-SEENSAGQLVYQVQSPDEGALVTAARN 507
Cdd:cd02073  385 ----------------------------------------FFLALALCHTVVpEKDDHPGQLVYQASSPDEAALVEAARD 424
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 508 FGFIFKSRTPETITIEELGTPVTYQLLAFLDFNNIRKRMSVIVRNPEGRIKLYSKGADTILFEKLHPSNEDLQSLTSDHL 587
Cdd:cd02073  425 LGFVFLSRTPDTVTINALGEEEEYEILHILEFNSDRKRMSVIVRDPDGRILLYCKGADSVIFERLSPSSLELVEKTQEHL 504
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 588 SEFAGEGLRTLAIAYRELDDKYFKMWQKMLEDANSATLERDERISGLYEEIERDLMLLGATAVEDKLQEGVIETITSLSL 667
Cdd:cd02073  505 EDFASEGLRTLCLAYREISEEEYEEWNEKYDEASTALQNREELLDEVAEEIEKDLILLGATAIEDKLQDGVPETIEALQR 584
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|.
gi 568916992 668 ANIKIWILTGDKQETAINIGYACNVLTDAMDAL-FVITGNT 707
Cdd:cd02073  585 AGIKIWVLTGDKQETAINIGYSCRLLSEDMENLaLVIDGKT 625
 
Name Accession Description Interval E-value
P-type_ATPase_APLT_Dnf-like cd02073
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ...
31-707 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: 925.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  31 DNRIHTSKYNVLTFLPINLFEQLQRVANAYFLFLLILQLIPEISSLTWFTTIVPLVLVISMTAVKDATDDYFRHKSDNQV 110
Cdd:cd02073    1 DNRISTTKYTVFTFLPKNLFEQFRRVANLYFLFIAILQQIPGISPTGPYTTLLPLLFVLGVTAIKEGYEDIRRHKSDNEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 111 NNRQSKVLINSKLQNEKWMNVKVGDIIKLENNQFVAADLLLLSSSEPHGLCYVETAELDGETNLKVRQALPVTSELGaDI 190
Cdd:cd02073   81 NNRPVQVLRGGKFVKKKWKDIRVGDIVRVKNDEFVPADLLLLSSSEPDGLCYVETANLDGETNLKIRQALPETALLL-SE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 191 SSLAEFDGIVRCEAPNNKLDRFSGVLSWKDSK-HALSNQKIILRGCVLRNTSWCFGMVLFAGPDTKLMQNSGKTKFKRTS 269
Cdd:cd02073  160 EDLARFSGEIECEQPNNDLYTFNGTLELNGGReLPLSPDNLLLRGCTLRNTEWVYGVVVYTGHETKLMLNSGGTPLKRSS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 270 IDRLMNTLVLWIFGFLVCLGIILAVGSSILESEVGdqfRTPPFWREGEKSF-LFSGFLTFWSYVIILNTLVPISLYVSVE 348
Cdd:cd02073  240 IEKKMNRFIIAIFCILIVMCLISAIGKGIWLSKHG---RDLWYLLPKEERSpALEFFFDFLTFIILYNNLIPISLYVTIE 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 349 VIRLGHSYFINWDRKMYYASKAMPAEARTTTLNEELGQIEYIFSDKTGTLTQNIMTFKKCSINGRVYAgevlddpiqkke 428
Cdd:cd02073  317 VVKFLQSFFINWDLDMYDEETDTPAEARTSNLNEELGQVEYIFSDKTGTLTENIMEFKKCSINGVDYG------------ 384
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 429 itkekeatdfssksksektlhffdqslmesielgdpkvheFLRLLALCHTVM-SEENSAGQLVYQVQSPDEGALVTAARN 507
Cdd:cd02073  385 ----------------------------------------FFLALALCHTVVpEKDDHPGQLVYQASSPDEAALVEAARD 424
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 508 FGFIFKSRTPETITIEELGTPVTYQLLAFLDFNNIRKRMSVIVRNPEGRIKLYSKGADTILFEKLHPSNEDLQSLTSDHL 587
Cdd:cd02073  425 LGFVFLSRTPDTVTINALGEEEEYEILHILEFNSDRKRMSVIVRDPDGRILLYCKGADSVIFERLSPSSLELVEKTQEHL 504
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 588 SEFAGEGLRTLAIAYRELDDKYFKMWQKMLEDANSATLERDERISGLYEEIERDLMLLGATAVEDKLQEGVIETITSLSL 667
Cdd:cd02073  505 EDFASEGLRTLCLAYREISEEEYEEWNEKYDEASTALQNREELLDEVAEEIEKDLILLGATAIEDKLQDGVPETIEALQR 584
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|.
gi 568916992 668 ANIKIWILTGDKQETAINIGYACNVLTDAMDAL-FVITGNT 707
Cdd:cd02073  585 AGIKIWVLTGDKQETAINIGYSCRLLSEDMENLaLVIDGKT 625
ATPase-Plipid TIGR01652
phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase ...
29-713 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: 744.97  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992    29 YADNRIHTSKYNVLTFLPINLFEQLQRVANAYFLFLLILQLIPEISSLTWFTTIVPLVLVISMTAVKDATDDYFRHKSDN 108
Cdd:TIGR01652    1 FCSNKISTTKYTVLTFLPKNLFEQFKRFANLYFLVVALLQQVPILSPTYRGTSIVPLAFVLIVTAIKEAIEDIRRRRRDK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   109 QVNNRQSKVLINS-KLQNEKWMNVKVGDIIKLENNQFVAADLLLLSSSEPHGLCYVETAELDGETNLKVRQALPVTSELg 187
Cdd:TIGR01652   81 EVNNRLTEVLEGHgQFVEIPWKDLRVGDIVKVKKDERIPADLLLLSSSEPDGVCYVETANLDGETNLKLRQALEETQKM- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   188 ADISSLAEFDGIVRCEAPNNKLDRFSGVLSWKDSKH-ALSNQKIILRGCVLRNTSWCFGMVLFAGPDTKLMQNSGKTKFK 266
Cdd:TIGR01652  160 LDEDDIKNFSGEIECEQPNASLYSFQGNMTINGDRQyPLSPDNILLRGCTLRNTDWVIGVVVYTGHDTKLMRNATQAPSK 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   267 RTSIDRLMNTLVLWIFGFLVCLGIILAVGSSIleseVGDQFRTPPFWREGEKSF---LFSGFLTFWSYVIILNTLVPISL 343
Cdd:TIGR01652  240 RSRLEKELNFLIIILFCLLFVLCLISSVGAGI----WNDAHGKDLWYIRLDVSErnaAANGFFSFLTFLILFSSLIPISL 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   344 YVSVEVIRLGHSYFINWDRKMYYASKAMPAEARTTTLNEELGQIEYIFSDKTGTLTQNIMTFKKCSINGRVYAGEVLDDP 423
Cdd:TIGR01652  316 YVSLELVKSVQAYFINSDLQMYHEKTDTPASVRTSNLNEELGQVEYIFSDKTGTLTQNIMEFKKCSIAGVSYGDGFTEIK 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   424 IQKKEITKEKEATDFSSKSKSeKTLHFFDQSLMESIELGDPK---VHEFLRLLALCHTVMSE--ENSAGQLVYQVQSPDE 498
Cdd:TIGR01652  396 DGIRERLGSYVENENSMLVES-KGFTFVDPRLVDLLKTNKPNakrINEFFLALALCHTVVPEfnDDGPEEITYQAASPDE 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   499 GALVTAARNFGFIFKSRTPETIT--IEELGTPVTYQLLAFLDFNNIRKRMSVIVRNPEGRIKLYSKGADTILFEKLHPSN 576
Cdd:TIGR01652  475 AALVKAARDVGFVFFERTPKSISllIEMHGETKEYEILNVLEFNSDRKRMSVIVRNPDGRIKLLCKGADTVIFKRLSSGG 554
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   577 EDLQSLTSDHLSEFAGEGLRTLAIAYRELDDKYFKMWQKMLEDANSATLERDERISGLYEEIERDLMLLGATAVEDKLQE 656
Cdd:TIGR01652  555 NQVNEETKEHLENYASEGLRTLCIAYRELSEEEYEEWNEEYNEASTALTDREEKLDVVAESIEKDLILLGATAIEDKLQE 634
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568916992   657 GVIETITSLSLANIKIWILTGDKQETAINIGYACNVLTDAMdALFVITGNTAGEVRE 713
Cdd:TIGR01652  635 GVPETIELLRQAGIKIWVLTGDKVETAINIGYSCRLLSRNM-EQIVITSDSLDATRS 690
PLN03190 PLN03190
aminophospholipid translocase; Provisional
11-715 2.37e-163

aminophospholipid translocase; Provisional


Pssm-ID: 215623 [Multi-domain]  Cd Length: 1178  Bit Score: 502.89  E-value: 2.37e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   11 EVERVVKANDRD-YNEKFQYADNRIHTSKYNVLTFLPINLFEQLQRVANAYFLFLLILQLIPEISSLTWFTTIVPLVLVI 89
Cdd:PLN03190   68 EDARLVYLNDPEkSNERFEFAGNSIRTAKYSVFSFLPRNLFEQFHRVAYIYFLVIAVLNQLPQLAVFGRGASILPLAFVL 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   90 SMTAVKDATDDYFRHKSDNQVNNRQSKVLINSKLQNEKWMNVKVGDIIKLENNQFVAADLLLLSSSEPHGLCYVETAELD 169
Cdd:PLN03190  148 LVTAVKDAYEDWRRHRSDRIENNRLAWVLVDDQFQEKKWKDIRVGEIIKIQANDTLPCDMVLLSTSDPTGVAYVQTINLD 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  170 GETNLKVRQAlpvTSELGADISSLAEFDGIVRCEAPNNKLDRFSGVLSWKDSKHALSNQKIILRGCVLRNTSWCFGMVLF 249
Cdd:PLN03190  228 GESNLKTRYA---KQETLSKIPEKEKINGLIKCEKPNRNIYGFQANMEVDGKRLSLGPSNIILRGCELKNTAWAIGVAVY 304
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  250 AGPDTKLMQNSGKTKFKRTSIDRLMNTLVLWIFGFLVCLGIILAVGSSILESEVGDQFRTPPFWR------EGEKSFLFS 323
Cdd:PLN03190  305 CGRETKAMLNNSGAPSKRSRLETRMNLEIIILSLFLIALCTIVSVCAAVWLRRHRDELDTIPFYRrkdfseGGPKNYNYY 384
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  324 G-----FLTFWSYVIILNTLVPISLYVSVEVIRLGHSYFINWDRKMYYASKAMPAEARTTTLNEELGQIEYIFSDKTGTL 398
Cdd:PLN03190  385 GwgweiFFTFLMSVIVFQIMIPISLYISMELVRVGQAYFMIRDDQMYDEASNSRFQCRALNINEDLGQIKYVFSDKTGTL 464
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  399 TQNIMTFKKCSINGRVYAGEVLDDPIQKKEITKEKEATDFSSKSKSEKTLHFFDQSLMESIELGDPKVHEFLRLLALCHT 478
Cdd:PLN03190  465 TENKMEFQCASIWGVDYSDGRTPTQNDHAGYSVEVDGKILRPKMKVKVDPQLLELSKSGKDTEEAKHVHDFFLALAACNT 544
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  479 VM-----SEENSAGQLV-YQVQSPDEGALVTAARNFGFIFKSRTPETITIEELGTPVTYQLLAFLDFNNIRKRMSVIVRN 552
Cdd:PLN03190  545 IVpivvdDTSDPTVKLMdYQGESPDEQALVYAAAAYGFMLIERTSGHIVIDIHGERQRFNVLGLHEFDSDRKRMSVILGC 624
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  553 PEGRIKLYSKGADTILFEKLHPS-NEDLQSLTSDHLSEFAGEGLRTLAIAYRELDDKYFKMWQKMLEDANSATLERDERI 631
Cdd:PLN03190  625 PDKTVKVFVKGADTSMFSVIDRSlNMNVIRATEAHLHTYSSLGLRTLVVGMRELNDSEFEQWHFSFEAASTALIGRAALL 704
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  632 SGLYEEIERDLMLLGATAVEDKLQEGVIETITSLSLANIKIWILTGDKQETAINIGYACNVLTDAMDALfVITGNTAGEV 711
Cdd:PLN03190  705 RKVASNVENNLTILGASAIEDKLQQGVPEAIESLRTAGIKVWVLTGDKQETAISIGYSSKLLTNKMTQI-IINSNSKESC 783

                  ....
gi 568916992  712 REEL 715
Cdd:PLN03190  784 RKSL 787
MgtA COG0474
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism];
382-698 1.50e-30

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


Pssm-ID: 440242 [Multi-domain]  Cd Length: 874  Bit Score: 129.07  E-value: 1.50e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 382 EELGQIEYIFSDKTGTLTQNIMTFKKCSINGRVYagevlddpiqkkEITKEKeatdfssksksektlhffdqslmesiel 461
Cdd:COG0474  318 ETLGSVTVICTDKTGTLTQNKMTVERVYTGGGTY------------EVTGEF---------------------------- 357
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 462 gDPKVHEFLRLLALCHTVMSEENSAgqlvyqVQSPDEGALVTAARNFGfifksrtpetITIEELGTpvTYQLLAFLDFNN 541
Cdd:COG0474  358 -DPALEELLRAAALCSDAQLEEETG------LGDPTEGALLVAAAKAG----------LDVEELRK--EYPRVDEIPFDS 418
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 542 IRKRMSVIVRNPEGRIKLYSKGA-DTIL--------FEKLHPSNEDLQSLTSDHLSEFAGEGLRTLAIAYRELddkyfkm 612
Cdd:COG0474  419 ERKRMSTVHEDPDGKRLLIVKGApEVVLalctrvltGGGVVPLTEEDRAEILEAVEELAAQGLRVLAVAYKEL------- 491
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 613 wqkmledansatlerDERISGLYEEIERDLMLLGATAVEDKLQEGVIETITSLSLANIKIWILTGDKQETAINIG----- 687
Cdd:COG0474  492 ---------------PADPELDSEDDESDLTFLGLVGMIDPPRPEAKEAIAECRRAGIRVKMITGDHPATARAIArqlgl 556
                        330
                 ....*....|....*..
gi 568916992 688 --YACNVLT----DAMD 698
Cdd:COG0474  557 gdDGDRVLTgaelDAMS 573
PhoLip_ATPase_N pfam16209
Phospholipid-translocating ATPase N-terminal; PhoLip_ATPase_N is found at the N-terminus of a ...
16-82 4.83e-22

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: 90.23  E-value: 4.83e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568916992   16 VKANDRDYNEKFQYADNRIHTSKYNVLTFLPINLFEQLQRVANAYFLFLLILQLIPEISSLTWFTTI 82
Cdd:pfam16209   1 VYINDPEKNSEFKYPSNKISTSKYTLLTFLPKNLFEQFRRVANLYFLLIAILQLIPGISPTGPYTTI 67
 
Name Accession Description Interval E-value
P-type_ATPase_APLT_Dnf-like cd02073
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ...
31-707 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: 925.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  31 DNRIHTSKYNVLTFLPINLFEQLQRVANAYFLFLLILQLIPEISSLTWFTTIVPLVLVISMTAVKDATDDYFRHKSDNQV 110
Cdd:cd02073    1 DNRISTTKYTVFTFLPKNLFEQFRRVANLYFLFIAILQQIPGISPTGPYTTLLPLLFVLGVTAIKEGYEDIRRHKSDNEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 111 NNRQSKVLINSKLQNEKWMNVKVGDIIKLENNQFVAADLLLLSSSEPHGLCYVETAELDGETNLKVRQALPVTSELGaDI 190
Cdd:cd02073   81 NNRPVQVLRGGKFVKKKWKDIRVGDIVRVKNDEFVPADLLLLSSSEPDGLCYVETANLDGETNLKIRQALPETALLL-SE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 191 SSLAEFDGIVRCEAPNNKLDRFSGVLSWKDSK-HALSNQKIILRGCVLRNTSWCFGMVLFAGPDTKLMQNSGKTKFKRTS 269
Cdd:cd02073  160 EDLARFSGEIECEQPNNDLYTFNGTLELNGGReLPLSPDNLLLRGCTLRNTEWVYGVVVYTGHETKLMLNSGGTPLKRSS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 270 IDRLMNTLVLWIFGFLVCLGIILAVGSSILESEVGdqfRTPPFWREGEKSF-LFSGFLTFWSYVIILNTLVPISLYVSVE 348
Cdd:cd02073  240 IEKKMNRFIIAIFCILIVMCLISAIGKGIWLSKHG---RDLWYLLPKEERSpALEFFFDFLTFIILYNNLIPISLYVTIE 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 349 VIRLGHSYFINWDRKMYYASKAMPAEARTTTLNEELGQIEYIFSDKTGTLTQNIMTFKKCSINGRVYAgevlddpiqkke 428
Cdd:cd02073  317 VVKFLQSFFINWDLDMYDEETDTPAEARTSNLNEELGQVEYIFSDKTGTLTENIMEFKKCSINGVDYG------------ 384
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 429 itkekeatdfssksksektlhffdqslmesielgdpkvheFLRLLALCHTVM-SEENSAGQLVYQVQSPDEGALVTAARN 507
Cdd:cd02073  385 ----------------------------------------FFLALALCHTVVpEKDDHPGQLVYQASSPDEAALVEAARD 424
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 508 FGFIFKSRTPETITIEELGTPVTYQLLAFLDFNNIRKRMSVIVRNPEGRIKLYSKGADTILFEKLHPSNEDLQSLTSDHL 587
Cdd:cd02073  425 LGFVFLSRTPDTVTINALGEEEEYEILHILEFNSDRKRMSVIVRDPDGRILLYCKGADSVIFERLSPSSLELVEKTQEHL 504
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 588 SEFAGEGLRTLAIAYRELDDKYFKMWQKMLEDANSATLERDERISGLYEEIERDLMLLGATAVEDKLQEGVIETITSLSL 667
Cdd:cd02073  505 EDFASEGLRTLCLAYREISEEEYEEWNEKYDEASTALQNREELLDEVAEEIEKDLILLGATAIEDKLQDGVPETIEALQR 584
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|.
gi 568916992 668 ANIKIWILTGDKQETAINIGYACNVLTDAMDAL-FVITGNT 707
Cdd:cd02073  585 AGIKIWVLTGDKQETAINIGYSCRLLSEDMENLaLVIDGKT 625
ATPase-Plipid TIGR01652
phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase ...
29-713 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: 744.97  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992    29 YADNRIHTSKYNVLTFLPINLFEQLQRVANAYFLFLLILQLIPEISSLTWFTTIVPLVLVISMTAVKDATDDYFRHKSDN 108
Cdd:TIGR01652    1 FCSNKISTTKYTVLTFLPKNLFEQFKRFANLYFLVVALLQQVPILSPTYRGTSIVPLAFVLIVTAIKEAIEDIRRRRRDK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   109 QVNNRQSKVLINS-KLQNEKWMNVKVGDIIKLENNQFVAADLLLLSSSEPHGLCYVETAELDGETNLKVRQALPVTSELg 187
Cdd:TIGR01652   81 EVNNRLTEVLEGHgQFVEIPWKDLRVGDIVKVKKDERIPADLLLLSSSEPDGVCYVETANLDGETNLKLRQALEETQKM- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   188 ADISSLAEFDGIVRCEAPNNKLDRFSGVLSWKDSKH-ALSNQKIILRGCVLRNTSWCFGMVLFAGPDTKLMQNSGKTKFK 266
Cdd:TIGR01652  160 LDEDDIKNFSGEIECEQPNASLYSFQGNMTINGDRQyPLSPDNILLRGCTLRNTDWVIGVVVYTGHDTKLMRNATQAPSK 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   267 RTSIDRLMNTLVLWIFGFLVCLGIILAVGSSIleseVGDQFRTPPFWREGEKSF---LFSGFLTFWSYVIILNTLVPISL 343
Cdd:TIGR01652  240 RSRLEKELNFLIIILFCLLFVLCLISSVGAGI----WNDAHGKDLWYIRLDVSErnaAANGFFSFLTFLILFSSLIPISL 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   344 YVSVEVIRLGHSYFINWDRKMYYASKAMPAEARTTTLNEELGQIEYIFSDKTGTLTQNIMTFKKCSINGRVYAGEVLDDP 423
Cdd:TIGR01652  316 YVSLELVKSVQAYFINSDLQMYHEKTDTPASVRTSNLNEELGQVEYIFSDKTGTLTQNIMEFKKCSIAGVSYGDGFTEIK 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   424 IQKKEITKEKEATDFSSKSKSeKTLHFFDQSLMESIELGDPK---VHEFLRLLALCHTVMSE--ENSAGQLVYQVQSPDE 498
Cdd:TIGR01652  396 DGIRERLGSYVENENSMLVES-KGFTFVDPRLVDLLKTNKPNakrINEFFLALALCHTVVPEfnDDGPEEITYQAASPDE 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   499 GALVTAARNFGFIFKSRTPETIT--IEELGTPVTYQLLAFLDFNNIRKRMSVIVRNPEGRIKLYSKGADTILFEKLHPSN 576
Cdd:TIGR01652  475 AALVKAARDVGFVFFERTPKSISllIEMHGETKEYEILNVLEFNSDRKRMSVIVRNPDGRIKLLCKGADTVIFKRLSSGG 554
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   577 EDLQSLTSDHLSEFAGEGLRTLAIAYRELDDKYFKMWQKMLEDANSATLERDERISGLYEEIERDLMLLGATAVEDKLQE 656
Cdd:TIGR01652  555 NQVNEETKEHLENYASEGLRTLCIAYRELSEEEYEEWNEEYNEASTALTDREEKLDVVAESIEKDLILLGATAIEDKLQE 634
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568916992   657 GVIETITSLSLANIKIWILTGDKQETAINIGYACNVLTDAMdALFVITGNTAGEVRE 713
Cdd:TIGR01652  635 GVPETIELLRQAGIKIWVLTGDKVETAINIGYSCRLLSRNM-EQIVITSDSLDATRS 690
PLN03190 PLN03190
aminophospholipid translocase; Provisional
11-715 2.37e-163

aminophospholipid translocase; Provisional


Pssm-ID: 215623 [Multi-domain]  Cd Length: 1178  Bit Score: 502.89  E-value: 2.37e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   11 EVERVVKANDRD-YNEKFQYADNRIHTSKYNVLTFLPINLFEQLQRVANAYFLFLLILQLIPEISSLTWFTTIVPLVLVI 89
Cdd:PLN03190   68 EDARLVYLNDPEkSNERFEFAGNSIRTAKYSVFSFLPRNLFEQFHRVAYIYFLVIAVLNQLPQLAVFGRGASILPLAFVL 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   90 SMTAVKDATDDYFRHKSDNQVNNRQSKVLINSKLQNEKWMNVKVGDIIKLENNQFVAADLLLLSSSEPHGLCYVETAELD 169
Cdd:PLN03190  148 LVTAVKDAYEDWRRHRSDRIENNRLAWVLVDDQFQEKKWKDIRVGEIIKIQANDTLPCDMVLLSTSDPTGVAYVQTINLD 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  170 GETNLKVRQAlpvTSELGADISSLAEFDGIVRCEAPNNKLDRFSGVLSWKDSKHALSNQKIILRGCVLRNTSWCFGMVLF 249
Cdd:PLN03190  228 GESNLKTRYA---KQETLSKIPEKEKINGLIKCEKPNRNIYGFQANMEVDGKRLSLGPSNIILRGCELKNTAWAIGVAVY 304
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  250 AGPDTKLMQNSGKTKFKRTSIDRLMNTLVLWIFGFLVCLGIILAVGSSILESEVGDQFRTPPFWR------EGEKSFLFS 323
Cdd:PLN03190  305 CGRETKAMLNNSGAPSKRSRLETRMNLEIIILSLFLIALCTIVSVCAAVWLRRHRDELDTIPFYRrkdfseGGPKNYNYY 384
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  324 G-----FLTFWSYVIILNTLVPISLYVSVEVIRLGHSYFINWDRKMYYASKAMPAEARTTTLNEELGQIEYIFSDKTGTL 398
Cdd:PLN03190  385 GwgweiFFTFLMSVIVFQIMIPISLYISMELVRVGQAYFMIRDDQMYDEASNSRFQCRALNINEDLGQIKYVFSDKTGTL 464
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  399 TQNIMTFKKCSINGRVYAGEVLDDPIQKKEITKEKEATDFSSKSKSEKTLHFFDQSLMESIELGDPKVHEFLRLLALCHT 478
Cdd:PLN03190  465 TENKMEFQCASIWGVDYSDGRTPTQNDHAGYSVEVDGKILRPKMKVKVDPQLLELSKSGKDTEEAKHVHDFFLALAACNT 544
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  479 VM-----SEENSAGQLV-YQVQSPDEGALVTAARNFGFIFKSRTPETITIEELGTPVTYQLLAFLDFNNIRKRMSVIVRN 552
Cdd:PLN03190  545 IVpivvdDTSDPTVKLMdYQGESPDEQALVYAAAAYGFMLIERTSGHIVIDIHGERQRFNVLGLHEFDSDRKRMSVILGC 624
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  553 PEGRIKLYSKGADTILFEKLHPS-NEDLQSLTSDHLSEFAGEGLRTLAIAYRELDDKYFKMWQKMLEDANSATLERDERI 631
Cdd:PLN03190  625 PDKTVKVFVKGADTSMFSVIDRSlNMNVIRATEAHLHTYSSLGLRTLVVGMRELNDSEFEQWHFSFEAASTALIGRAALL 704
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  632 SGLYEEIERDLMLLGATAVEDKLQEGVIETITSLSLANIKIWILTGDKQETAINIGYACNVLTDAMDALfVITGNTAGEV 711
Cdd:PLN03190  705 RKVASNVENNLTILGASAIEDKLQQGVPEAIESLRTAGIKVWVLTGDKQETAISIGYSSKLLTNKMTQI-IINSNSKESC 783

                  ....
gi 568916992  712 REEL 715
Cdd:PLN03190  784 RKSL 787
P-type_ATPase_APLT cd07536
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ...
31-714 6.65e-162

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: 488.26  E-value: 6.65e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  31 DNRIHTSKYNVLTFLPINLFEQLQRVANAYFLFLLILQLIPEISSLTWFTTIVPLVLVISMTAVKDATDDYFRHKSDNQV 110
Cdd:cd07536    1 DNSISNQKYNVFTFLPGVLYEQFKRFLNLYFLVIACLQFVPALKPGYLYTTWAPLIFILAVTMTKEAIDDFRRFQRDKEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 111 NNRQSKVLINSKLQNEKWMNVKVGDIIKLENNQFVAADLLLLSSSEPHGLCYVETAELDGETNLKVRQALPVTSELGAdI 190
Cdd:cd07536   81 NKKQLYSKLTGRKVQIKSSDIQVGDIVIVEKNQRIPSDMVLLRTSEPQGSCYVETAQLDGETDLKLRVAVSCTQQLPA-L 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 191 SSLAEFDGIVRCEAPNNKLDRFSGVLSWKDSKH----ALSNQKIILRGCVLRNTSWCFGMVLFAGPDTKLMQNSGKTKFK 266
Cdd:cd07536  160 GDLMKISAYVECQKPQMDIHSFEGNFTLEDSDPpiheSLSIENTLLRASTLRNTGWVIGVVVYTGKETKLVMNTSNAKNK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 267 RTSIDRLMNTLVLWIFGFLVCLGIILAVGSSIleseVGDQFRTPPFWREGEKSFLFSGFLTFWSYVIILNTLVPISLYVS 346
Cdd:cd07536  240 VGLLDLELNRLTKALFLALVVLSLVMVTLQGF----WGPWYGEKNWYIKKMDTTSDNFGRNLLRFLLLFSYIIPISLRVN 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 347 VEVIRLGHSYFINWDRKMYYASKAMPAEARTTTLNEELGQIEYIFSDKTGTLTQNIMTFKKCSINGRVYAGEVLddpiqk 426
Cdd:cd07536  316 LDMVKAVYAWFIMWDENMYYIGNDTGTVARTSTIPEELGQVVYLLTDKTGTLTQNEMIFKRCHIGGVSYGGQVL------ 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 427 keitkekeatdfssksksektlhffdqslmesielgdpkvheflrllalchtvmseensagqlvyqvqspdegalvtaar 506
Cdd:cd07536      --------------------------------------------------------------------------------
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 507 nfgfifksrtpetitieelgtpvTYQLLAFLDFNNIRKRMSVIVRNPE-GRIKLYSKGADTILFEKLHPSNEDLQslTSD 585
Cdd:cd07536  390 -----------------------SFCILQLLEFTSDRKRMSVIVRDEStGEITLYMKGADVAISPIVSKDSYMEQ--YND 444
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 586 HLSEFAGEGLRTLAIAYRELDDKYFKMWQKMLEDANSATLERDERISGLYEEIERDLMLLGATAVEDKLQEGVIETITSL 665
Cdd:cd07536  445 WLEEECGEGLRTLCVAKKALTENEYQEWESRYTEASLSLHDRSLRVAEVVESLERELELLGLTAIEDRLQAGVPETIETL 524
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|
gi 568916992 666 SLANIKIWILTGDKQETAINIGYACNVLTDAMDA-LFVITGNTAGEVREE 714
Cdd:cd07536  525 RKAGIKIWMLTGDKQETAICIAKSCHLVSRTQDIhLLRQDTSRGERAAIT 574
P-type_ATPase_APLT_Neo1-like cd07541
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Neo1p and human ...
32-686 1.52e-86

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: 290.08  E-value: 1.52e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  32 NRIHTSKYNVLTFLPINLFEQLQRVANAYFLFLLILQLIPEISSLTWFTTIVPLVLVISMTAVKDATDDYFRHKSDNQVN 111
Cdd:cd07541    2 NEVRNQKYNIFTFLPKVLYEQFKFFYNLYFLVVALSQFVPALKIGYLYTYWAPLGFVLAVTMAKEAVDDIRRRRRDKEQN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 112 NRQSKVLINSKLQNEKwmNVKVGDIIKLENNQFVAADLLLLSSSEPHGLCYVETAELDGETNLKVRQALPVTSELGADIS 191
Cdd:cd07541   82 YEKLTVRGETVEIPSS--DIKVGDLIIVEKNQRIPADMVLLRTSEKSGSCFIRTDQLDGETDWKLRIAVPCTQKLPEEGI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 192 SLAEFdgIVRCEAPNNKLDRFSGVLSWKDskhalsnqKIILRGCVLRNTSW---------CFGMVLFAGPDTKLMQNSGK 262
Cdd:cd07541  160 LNSIS--AVYAEAPQKDIHSFYGTFTIND--------DPTSESLSVENTLWantvvasgtVIGVVVYTGKETRSVMNTSQ 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 263 TKFKRTSIDRLMNTLVLWIFGFLVCLGIILAvgssilesevgdqfrtppfwregeksfLFSGFLTFW-----SYVIILNT 337
Cdd:cd07541  230 PKNKVGLLDLEINFLTKILFCAVLALSIVMV---------------------------ALQGFQGPWyiylfRFLILFSS 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 338 LVPISLYVSVEVIRLGHSYFINWDrkmyyasKAMP-AEARTTTLNEELGQIEYIFSDKTGTLTQNIMTFKKcsingrvya 416
Cdd:cd07541  283 IIPISLRVNLDMAKIVYSWQIEHD-------KNIPgTVVRTSTIPEELGRIEYLLSDKTGTLTQNEMVFKK--------- 346
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 417 gevlddpiqkkeitkekeatdfssksksektLHFfdqslmesielgdpkvheflrllalchtvmseensaGQLVYQvqsp 496
Cdd:cd07541  347 -------------------------------LHL------------------------------------GTVSYG---- 355
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 497 degalvtaarnfgfifksrtpetitieelGTPVTYQLLAFLDFNNIRKRMSVIVRNPE-GRIKLYSKGADTILFEKLHPs 575
Cdd:cd07541  356 -----------------------------GQNLNYEILQIFPFTSESKRMGIIVREEKtGEITFYMKGADVVMSKIVQY- 405
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 576 nedlqsltSDHLSE----FAGEGLRTLAIAYRELDDKYFKMWQKMLEDANSATLERDERISGLYEEIERDLMLLGATAVE 651
Cdd:cd07541  406 --------NDWLEEecgnMAREGLRTLVVAKKKLSEEEYQAFEKRYNAAKLSIHDRDLKVAEVVESLERELELLCLTGVE 477
                        650       660       670
                 ....*....|....*....|....*....|....*
gi 568916992 652 DKLQEGVIETITSLSLANIKIWILTGDKQETAINI 686
Cdd:cd07541  478 DKLQEDVKPTLELLRNAGIKIWMLTGDKLETATCI 512
ATPase_P-type TIGR01494
ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large ...
79-690 6.63e-78

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: 260.33  E-value: 6.63e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   79 FTTIVPLVLVISMTAVKDATDDYFRHKSDNQVNNRQSKVLINSKLQNEKwMNVKVGDIIKLENNQFVAADLLLLSSSeph 158
Cdd:TIGR01494   1 FILFLVLLFVLLEVKQKLKAEDALRSLKDSLVNTATVLVLRNGWKEISS-KDLVPGDVVLVKSGDTVPADGVLLSGS--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  159 glCYVETAELDGETNLKVRQALPvtselgadisslaefdgivRCEAPNNKLDRFSGvlswkdskhalsNQKIILRGCVLR 238
Cdd:TIGR01494  77 --AFVDESSLTGESLPVLKTALP-------------------DGDAVFAGTINFGG------------TLIVKVTATGIL 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  239 NTSWCFGMVLFAGPDTKLMQNSGKTKFKRTSIdrlmntlvlWIFGFLVCLGIILAVGSSILESEvgdqfrtppfwregek 318
Cdd:TIGR01494 124 TTVGKIAVVVYTGFSTKTPLQSKADKFENFIF---------ILFLLLLALAVFLLLPIGGWDGN---------------- 178
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  319 sflfSGFLTFWSYVIILNTLVPISLYVSVEVIRLGHsyfinwDRKMYYAskamPAEARTTTLNEELGQIEYIFSDKTGTL 398
Cdd:TIGR01494 179 ----SIYKAILRALAVLVIAIPCALPLAVSVALAVG------DARMAKK----GILVKNLNALEELGKVDVICFDKTGTL 244
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  399 TQNIMTFKKCSINGRVYagevlddpiqkkeitkekeatdfsskskSEKTLHFfdqslmesielgdpkvheflrllalcht 478
Cdd:TIGR01494 245 TTNKMTLQKVIIIGGVE----------------------------EASLALA---------------------------- 268
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  479 vmseeNSAGQLVYQVQSPDEGALVTAARNfgfifksrtpetiTIEELGTPVTYQLLAFLDFNNIRKRMSVIVRNPEGRIK 558
Cdd:TIGR01494 269 -----LLAASLEYLSGHPLERAIVKSAEG-------------VIKSDEINVEYKILDVFPFSSVLKRMGVIVEGANGSDL 330
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  559 LYSKGADTILFEKLHPsnedlQSLTSDHLSEFAGEGLRTLAIAYRELDDkyfkmwqkmledansatlerderisglyeei 638
Cdd:TIGR01494 331 LFVKGAPEFVLERCNN-----ENDYDEKVDEYARQGLRVLAFASKKLPD------------------------------- 374
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568916992  639 erDLMLLGATAVEDKLQEGVIETITSLSLANIKIWILTGDKQETAINIGYAC 690
Cdd:TIGR01494 375 --DLEFLGLLTFEDPLRPDAKETIEALRKAGIKVVMLTGDNVLTAKAIAKEL 424
MgtA COG0474
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism];
382-698 1.50e-30

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


Pssm-ID: 440242 [Multi-domain]  Cd Length: 874  Bit Score: 129.07  E-value: 1.50e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 382 EELGQIEYIFSDKTGTLTQNIMTFKKCSINGRVYagevlddpiqkkEITKEKeatdfssksksektlhffdqslmesiel 461
Cdd:COG0474  318 ETLGSVTVICTDKTGTLTQNKMTVERVYTGGGTY------------EVTGEF---------------------------- 357
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 462 gDPKVHEFLRLLALCHTVMSEENSAgqlvyqVQSPDEGALVTAARNFGfifksrtpetITIEELGTpvTYQLLAFLDFNN 541
Cdd:COG0474  358 -DPALEELLRAAALCSDAQLEEETG------LGDPTEGALLVAAAKAG----------LDVEELRK--EYPRVDEIPFDS 418
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 542 IRKRMSVIVRNPEGRIKLYSKGA-DTIL--------FEKLHPSNEDLQSLTSDHLSEFAGEGLRTLAIAYRELddkyfkm 612
Cdd:COG0474  419 ERKRMSTVHEDPDGKRLLIVKGApEVVLalctrvltGGGVVPLTEEDRAEILEAVEELAAQGLRVLAVAYKEL------- 491
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 613 wqkmledansatlerDERISGLYEEIERDLMLLGATAVEDKLQEGVIETITSLSLANIKIWILTGDKQETAINIG----- 687
Cdd:COG0474  492 ---------------PADPELDSEDDESDLTFLGLVGMIDPPRPEAKEAIAECRRAGIRVKMITGDHPATARAIArqlgl 556
                        330
                 ....*....|....*..
gi 568916992 688 --YACNVLT----DAMD 698
Cdd:COG0474  557 gdDGDRVLTgaelDAMS 573
P-type_ATPase_Ca_PMCA-like cd02081
animal plasma membrane Ca2(+)-ATPases (PMCA), similar to human ATP2B1-4/PMCA1-4, and related ...
495-732 8.69e-26

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: 113.45  E-value: 8.69e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 495 SPDEGALVTAARNFG--FIFKSRTPETitieelgtpvtyQLLAFLDFNNIRKRMSVIVRNPEGRIKLYSKGADTILFEK- 571
Cdd:cd02081  340 NKTECALLGFVLELGgdYRYREKRPEE------------KVLKVYPFNSARKRMSTVVRLKDGGYRLYVKGASEIVLKKc 407
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 572 --LHPSNEDLQSLTSDH-------LSEFAGEGLRTLAIAYRELDDKyfkmwqkmledaNSATLERDERIsglYEEIERDL 642
Cdd:cd02081  408 syILNSDGEVVFLTSEKkeeikrvIEPMASDSLRTIGLAYRDFSPD------------EEPTAERDWDD---EEDIESDL 472
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 643 MLLGATAVEDKLQEGVIETITSLSLANIKIWILTGDKQETAINIGYACNVLTDAMDALfVITG----NTAGEVREELRPM 718
Cdd:cd02081  473 TFIGIVGIKDPLRPEVPEAVAKCQRAGITVRMVTGDNINTARAIARECGILTEGEDGL-VLEGkefrELIDEEVGEVCQE 551
                        250       260
                 ....*....|....*....|.
gi 568916992 719 P-------LKVMSRtifwSSP 732
Cdd:cd02081  552 KfdkiwpkLRVLAR----SSP 568
PhoLip_ATPase_N pfam16209
Phospholipid-translocating ATPase N-terminal; PhoLip_ATPase_N is found at the N-terminus of a ...
16-82 4.83e-22

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: 90.23  E-value: 4.83e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568916992   16 VKANDRDYNEKFQYADNRIHTSKYNVLTFLPINLFEQLQRVANAYFLFLLILQLIPEISSLTWFTTI 82
Cdd:pfam16209   1 VYINDPEKNSEFKYPSNKISTSKYTLLTFLPKNLFEQFRRVANLYFLLIAILQLIPGISPTGPYTTI 67
P-type_ATPases cd01431
ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, ...
519-726 4.31e-21

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: 94.83  E-value: 4.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 519 TITIEELgtPVTYQLLAFLDFNNIRKRMSVIVRNPeGRIKLYSKGADTILFE--KLHPSNEDLQSLTSDhLSEFAGEGLR 596
Cdd:cd01431    9 TLTKNGM--TVTKLFIEEIPFNSTRKRMSVVVRLP-GRYRAIVKGAPETILSrcSHALTEEDRNKIEKA-QEESAREGLR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 597 TLAIAYRELDDKYFKmwqkmledansatlerderisglyEEIERDLMLLGATAVEDKLQEGVIETITSLSLANIKIWILT 676
Cdd:cd01431   85 VLALAYREFDPETSK------------------------EAVELNLVFLGLIGLQDPPRPEVKEAIAKCRTAGIKVVMIT 140
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568916992 677 GDKQETAINIGYACNVLTDAMDALF-VITGNTAGEVREELRPmPLKVMSRT 726
Cdd:cd01431  141 GDNPLTAIAIAREIGIDTKASGVILgEEADEMSEEELLDLIA-KVAVFARV 190
ATPase-IIB_Ca TIGR01517
plasma-membrane calcium-translocating P-type ATPase; This model describes the P-type ATPase ...
382-732 2.01e-19

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


Pssm-ID: 273668 [Multi-domain]  Cd Length: 956  Bit Score: 93.69  E-value: 2.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  382 EELGQIEYIFSDKTGTLTQNIMTFKKCSINGRVYAgevLDDPIQKKEItkekeatdfsskSKSEKTLhffdqsLMESIEL 461
Cdd:TIGR01517 377 ETMGSATAICSDKTGTLTQNVMSVVQGYIGEQRFN---VRDEIVLRNL------------PAAVRNI------LVEGISL 435
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  462 gdpkvheflrllalcHTVMSEENSAGQLVYQVQSPDEGALVTAARNFGfiFKSRTPETITIEElgtpvtyQLLAFLDFNN 541
Cdd:TIGR01517 436 ---------------NSSSEEVVDRGGKRAFIGSKTECALLDFGLLLL--LQSRDVQEVRAEE-------KVVKIYPFNS 491
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  542 IRKRMSVIVRNPEGRIKLYSKGADTILFEKLH----------PSNEDLQSLTSDHLSEFAGEGLRTLAIAYRELDDKYFK 611
Cdd:TIGR01517 492 ERKFMSVVVKHSGGKYREFRKGASEIVLKPCRkrldsngeatPISEDDKDRCADVIEPLASDALRTICLAYRDFAPEEFP 571
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  612 MWqkmledansatlerderisglyEEIERDLMLLGATAVEDKLQEGVIETITSLSLANIKIWILTGDKQETAINIGYACN 691
Cdd:TIGR01517 572 RK----------------------DYPNKGLTLIGVVGIKDPLRPGVREAVQECQRAGITVRMVTGDNIDTAKAIARNCG 629
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 568916992  692 VLTdamdalFVITGNTAGE----VREELRPM--PLKVMSRtifwSSP 732
Cdd:TIGR01517 630 ILT------FGGLAMEGKEfrslVYEEMDPIlpKLRVLAR----SSP 666
P-type_ATPase_Ca_prok cd02089
prokaryotic P-type Ca(2+)-ATPase similar to Synechococcus elongatus sp. strain PCC 7942 PacL ...
382-719 8.19e-19

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: 91.14  E-value: 8.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 382 EELGQIEYIFSDKTGTLTQNIMTFKKcsingrVYAgevlddpiqkkeitkekeatdfssksksektlhffdqslmesieL 461
Cdd:cd02089  294 ETLGSVSVICSDKTGTLTQNKMTVEK------IYT--------------------------------------------I 323
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 462 GDPKvheflrllalchtvmseensagqlvyqvqspdEGALVTAARNFGFIFKSRTPETITIEELgtPvtyqllafldFNN 541
Cdd:cd02089  324 GDPT--------------------------------ETALIRAARKAGLDKEELEKKYPRIAEI--P----------FDS 359
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 542 IRKRMSVIVRNPEGRIkLYSKGADTILFEK----------LHPSNEDLQSLTSDHlSEFAGEGLRTLAIAYRELDDKYFK 611
Cdd:cd02089  360 ERKLMTTVHKDAGKYI-VFTKGAPDVLLPRctyiyingqvRPLTEEDRAKILAVN-EEFSEEALRVLAVAYKPLDEDPTE 437
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 612 MWqkmledansatlerderisglyEEIERDLMLLGATAVEDKLQEGVIETITSLSLANIKIWILTGDKQETAINIGYACN 691
Cdd:cd02089  438 SS----------------------EDLENDLIFLGLVGMIDPPRPEVKDAVAECKKAGIKTVMITGDHKLTARAIAKELG 495
                        330       340
                 ....*....|....*....|....*...
gi 568916992 692 VLTDAMDAlfvITGntagevrEELRPMP 719
Cdd:cd02089  496 ILEDGDKA---LTG-------EELDKMS 513
P-ATPase-V TIGR01657
P-type ATPase of unknown pump specificity (type V); These P-type ATPases form a distinct clade ...
385-690 4.64e-17

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: 85.88  E-value: 4.64e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   385 GQIEYIFSDKTGTLTQNIMTFKKCSI--NGRVYAGEVLDDPiqkkeitkekeatdfssksksektlhffdqslmesielg 462
Cdd:TIGR01657  446 GKIDVCCFDKTGTLTEDGLDLRGVQGlsGNQEFLKIVTEDS--------------------------------------- 486
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   463 DPKVHEFLRLLALCHTVMSEENSAgqlvyqVQSPDEGALVTAarnFGFIFK----SRTPETI--TIEELGTPVTYQLLAF 536
Cdd:TIGR01657  487 SLKPSITHKALATCHSLTKLEGKL------VGDPLDKKMFEA---TGWTLEeddeSAEPTSIlaVVRTDDPPQELSIIRR 557
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   537 LDFNNIRKRMSVIVRNP-EGRIKLYSKGADTILFEKLHPsnEDLQSLTSDHLSEFAGEGLRTLAIAYRELDDKyfkMWQK 615
Cdd:TIGR01657  558 FQFSSALQRMSVIVSTNdERSPDAFVKGAPETIQSLCSP--ETVPSDYQEVLKSYTREGYRVLALAYKELPKL---TLQK 632
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568916992   616 MLEdansatLERDErisglyeeIERDLMLLGATAVEDKLQEGVIETITSLSLANIKIWILTGDKQETAINIGYAC 690
Cdd:TIGR01657  633 AQD------LSRDA--------VESNLTFLGFIVFENPLKPDTKEVIKELKRASIRTVMITGDNPLTAVHVAREC 693
P-type_ATPase_SERCA cd02083
sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; ...
382-686 1.13e-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: 84.65  E-value: 1.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 382 EELGQIEYIFSDKTGTLTQNIMTFKK-CSINGRVYAGEVLDDPIQKKEITKEKEATDFSSKSKSEktlhffdqslmesie 460
Cdd:cd02083  335 ETLGCTSVICSDKTGTLTTNQMSVSRmFILDKVEDDSSLNEFEVTGSTYAPEGEVFKNGKKVKAG--------------- 399
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 461 lGDPKVHEFLRLLALCHTVMSEENSAGQLVYQVQSPDEGALVTAARNFGFIFKSRTPetITIEELGTPVT------YQLL 534
Cdd:cd02083  400 -QYDGLVELATICALCNDSSLDYNESKGVYEKVGEATETALTVLVEKMNVFNTDKSG--LSKRERANACNdvieqlWKKE 476
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 535 AFLDFNNIRKRMSVIVR--NPEGRIKLYSKGADTILFE----------KLHPSNEDLQSLTSDHLSEFAGEGLRTLAIAY 602
Cdd:cd02083  477 FTLEFSRDRKSMSVYCSptKASGGNKLFVKGAPEGVLErcthvrvgggKVVPLTAAIKILILKKVWGYGTDTLRCLALAT 556
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 603 RELDDKYFKMwqkMLEDANSatlerderisglYEEIERDLMLLGATAVEDKLQEGVIETITSLSLANIKIWILTGDKQET 682
Cdd:cd02083  557 KDTPPKPEDM---DLEDSTK------------FYKYETDLTFVGVVGMLDPPRPEVRDSIEKCRDAGIRVIVITGDNKGT 621

                 ....
gi 568916992 683 AINI 686
Cdd:cd02083  622 AEAI 625
P-type_ATPase_cation cd07542
P-type cation-transporting ATPases, similar to human ATPase type 13A2 (ATP13A2) protein and ...
537-690 3.28e-12

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: 69.97  E-value: 3.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 537 LDFNNIRKRMSVIVRNP-EGRIKLYSKGADTILFEKLHPsnEDLQSLTSDHLSEFAGEGLRTLAIAYRELDdkyfkmwqk 615
Cdd:cd07542  395 FPFSSALQRMSVIVKTPgDDSMMAFTKGAPEMIASLCKP--ETVPSNFQEVLNEYTKQGFRVIALAYKALE--------- 463
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568916992 616 mLEDANSATLERDErisglyeeIERDLMLLGATAVEDKLQEGVIETITSLSLANIKIWILTGDKQETAINIGYAC 690
Cdd:cd07542  464 -SKTWLLQKLSREE--------VESDLEFLGLIVMENRLKPETAPVINELNRANIRTVMVTGDNLLTAISVAREC 529
P-type_ATPase_Na_ENA cd02086
fungal-type Na(+)-ATPase, similar to the plasma membrane sodium transporters Saccharomyces ...
382-692 3.66e-12

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: 70.18  E-value: 3.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 382 EELGQIEYIFSDKTGTLTQNIMTFKKCSIngrvyagevlddpiqkkeitkekeatdfssksksektlhffdqslmesiel 461
Cdd:cd02086  323 EALGAVTDICSDKTGTLTQGKMVVRQVWI--------------------------------------------------- 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 462 gdpkvheflrLLALCHTVMSEENSAGQLVYQVQSPDEGALVTAARNFGFifkSRTPETItieelGTPVTYQLLAFLDFNN 541
Cdd:cd02086  352 ----------PAALCNIATVFKDEETDCWKAHGDPTEIALQVFATKFDM---GKNALTK-----GGSAQFQHVAEFPFDS 413
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 542 IRKRMSVI-VRNPEGRIKLYSKGADTILFEKLHPSNEDLQSLTSD---------HLSEFAGEGLRTLAIAYRELDDKYFK 611
Cdd:cd02086  414 TVKRMSVVyYNNQAGDYYAYMKGAVERVLECCSSMYGKDGIIPLDdefrktiikNVESLASQGLRVLAFASRSFTKAQFN 493
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 612 mwqkmLEDANSATLERderisglyEEIERDLMLLGATAVEDKLQegvIETITSLSL---ANIKIWILTGDKQETAINIgy 688
Cdd:cd02086  494 -----DDQLKNITLSR--------ADAESDLTFLGLVGIYDPPR---NESAGAVEKchqAGITVHMLTGDHPGTAKAI-- 555

                 ....
gi 568916992 689 ACNV 692
Cdd:cd02086  556 AREV 559
Cation_ATPase pfam13246
Cation transport ATPase (P-type); This domain is found in cation transport ATPases, including ...
474-571 6.66e-11

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: 59.15  E-value: 6.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992  474 ALCHTVMSEENSAGQLVYQVQSPDEGALVTAARNFGfifksrtPETITIEElgtpvTYQLLAFLDFNNIRKRMSVIVRNP 553
Cdd:pfam13246   1 ALCNSAAFDENEEKGKWEIVGDPTESALLVFAEKMG-------IDVEELRK-----DYPRVAEIPFNSDRKRMSTVHKLP 68
                          90
                  ....*....|....*....
gi 568916992  554 -EGRIKLYSKGADTILFEK 571
Cdd:pfam13246  69 dDGKYRLFVKGAPEIILDR 87
P-type_ATPase_cation cd02080
P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, ...
382-698 5.65e-10

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: 63.05  E-value: 5.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 382 EELGQIEYIFSDKTGTLTQNIMTFKkcsingrvyagevlddpiqkkeitkekeatdfssksksektlhffdqslmesiel 461
Cdd:cd02080  294 ETLGSVTVICSDKTGTLTRNEMTVQ------------------------------------------------------- 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 462 gdpkvheflRLLALCHTVMSEENSAGqlvYQVQ-SPDEGALVTAARNFGFIFksrtpetitiEELGTPVTYqlLAFLDFN 540
Cdd:cd02080  319 ---------AIVTLCNDAQLHQEDGH---WKITgDPTEGALLVLAAKAGLDP----------DRLASSYPR--VDKIPFD 374
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 541 NIRKRMSVIVRNPEGRIkLYSKGA-DTIL----FEKLHPSNEDLQSLT-SDHLSEFAGEGLRTLAIAYRELDDKyfkmwq 614
Cdd:cd02080  375 SAYRYMATLHRDDGQRV-IYVKGApERLLdmcdQELLDGGVSPLDRAYwEAEAEDLAKQGLRVLAFAYREVDSE------ 447
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 615 kmledanSATLERDERISGLyeeierdlMLLGATAVEDKLQEGVIETITSLSLANIKIWILTGDKQETA------INIGY 688
Cdd:cd02080  448 -------VEEIDHADLEGGL--------TFLGLQGMIDPPRPEAIAAVAECQSAGIRVKMITGDHAETAraigaqLGLGD 512
                        330
                 ....*....|....
gi 568916992 689 ACNVLT----DAMD 698
Cdd:cd02080  513 GKKVLTgaelDALD 526
P-type_ATPase_cation cd07543
P-type cation-transporting ATPases, similar to human cation-transporting ATPase type 13A1 ...
123-686 1.37e-08

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: 58.55  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 123 LQNEKWMNVKV-----GDIIKL---ENNQFVAADLLLLSssephGLCYVETAELDGETnlkvrqaLPVTSElgaDISSLa 194
Cdd:cd07543   91 YRDGKWVPISSdellpGDLVSIgrsAEDNLVPCDLLLLR-----GSCIVNEAMLTGES-------VPLMKE---PIEDR- 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 195 efdgivrcEAPNNKLDRfsgvlswKDSKHAlsnqkiilrgcvlrntswcfgmVLFAGpdTKLMQNSGKTKFKRTSIDRlm 274
Cdd:cd07543  155 --------DPEDVLDDD-------GDDKLH----------------------VLFGG--TKVVQHTPPGKGGLKPPDG-- 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 275 ntlvlwifgflVCLGIILAVGssiLESEVGDQFRTPPFWRE-----GEKSFLFSGFLT---------------------- 327
Cdd:cd07543  194 -----------GCLAYVLRTG---FETSQGKLLRTILFSTErvtanNLETFIFILFLLvfaiaaaayvwiegtkdgrsry 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 328 --FWSYVIILNTLVP------ISLYVSVEVIRLGHSY-FINWDRKMYYAskampaeartttlneelGQIEYIFSDKTGTL 398
Cdd:cd07543  260 klFLECTLILTSVVPpelpmeLSLAVNTSLIALAKLYiFCTEPFRIPFA-----------------GKVDICCFDKTGTL 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 399 TQNIMTFkkcsingRVYAGEvlddpiqkkeitkekeatdfssKSKSEKTLHFFDQSlmesielgdpkvHEFLRLLALCHT 478
Cdd:cd07543  323 TSDDLVV-------EGVAGL----------------------NDGKEVIPVSSIEP------------VETILVLASCHS 361
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 479 VMSEENsaGQLVyqvQSPDEGALVTAARNFGFIFKSRTPETITIEELGTPVTYQllafldFNNIRKRMSVIVrnpeGRIK 558
Cdd:cd07543  362 LVKLDD--GKLV---GDPLEKATLEAVDWTLTKDEKVFPRSKKTKGLKIIQRFH------FSSALKRMSVVA----SYKD 426
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 559 LYSKGADTILFEKLHPsnEDLQSLTSDHLS-------EFAGEGLRTLAIAYRELDDkyfkmwqkmLEDANSATLERDEri 631
Cdd:cd07543  427 PGSTDLKYIVAVKGAP--ETLKSMLSDVPAdydevykEYTRQGSRVLALGYKELGH---------LTKQQARDYKRED-- 493
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568916992 632 sglyeeIERDLMLLGATAVEDKLQEGVIETITSLSLANIKIWILTGDKQETAINI 686
Cdd:cd07543  494 ------VESDLTFAGFIVFSCPLKPDSKETIKELNNSSHRVVMITGDNPLTACHV 542
ATPase-IID_K-Na TIGR01523
potassium and/or sodium efflux P-type ATPase, fungal-type; Initially described as a calcium ...
382-748 1.41e-08

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: 58.48  E-value: 1.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   382 EELGQIEYIFSDKTGTLTQNIMTFKKCSINGRVYAG-EVLDDPIQKKE-----ITKEKEATDFSSKSKSEKTLHFFDQSL 455
Cdd:TIGR01523  354 EALGAVNDICSDKTGTITQGKMIARQIWIPRFGTISiDNSDDAFNPNEgnvsgIPRFSPYEYSHNEAADQDILKEFKDEL 433
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   456 MESIELGDPKVHEFLRLL---ALCH-TVMSEENSAGQLVYQvQSPDEGALVTAARNFGFIFKSRTPETITIE-------- 523
Cdd:TIGR01523  434 KEIDLPEDIDMDLFIKLLetaALANiATVFKDDATDCWKAH-GDPTEIAIHVFAKKFDLPHNALTGEEDLLKsnendqss 512
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   524 -----ELGTPVTYQLLAFLDFNNIRKRMSVIVRNPEGRI-KLYSKGADTILFE-----------KLHPSNEDLQSLTSDH 586
Cdd:TIGR01523  513 lsqhnEKPGSAQFEFIAEFPFDSEIKRMASIYEDNHGETyNIYAKGAFERIIEccsssngkdgvKISPLEDCDRELIIAN 592
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   587 LSEFAGEGLRTLAIAYRELDDKyfKMWQKMLEDansATLERDerisglyeEIERDLMLLGATAVEDKLQEGVIETITSLS 666
Cdd:TIGR01523  593 MESLAAEGLRVLAFASKSFDKA--DNNDDQLKN---ETLNRA--------TAESDLEFLGLIGIYDPPRNESAGAVEKCH 659
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992   667 LANIKIWILTGDKQETAINIGYACNVL-------TDAMDALFVITGNTAGEVREE----LRPMPLkVMSRTifwSSPVCV 735
Cdd:TIGR01523  660 QAGINVHMLTGDFPETAKAIAQEVGIIppnfihdRDEIMDSMVMTGSQFDALSDEevddLKALCL-VIARC---APQTKV 735
                          410
                   ....*....|...
gi 568916992   736 RLwfaAESPHSRK 748
Cdd:TIGR01523  736 KM---IEALHRRK 745
P-type_ATPase_Mg cd02077
magnesium transporting ATPase (MgtA), similar to Escherichia coli MgtA and Salmonella ...
538-678 1.50e-08

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: 58.03  E-value: 1.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 538 DFNniRKRMSVIVRNPEGRIKLYSKGA--------DTILFE-KLHPSNEDLQSLTSDHLSEFAGEGLRTLAIAYRELDDK 608
Cdd:cd02077  386 DFE--RRRMSVVVKDNDGKHLLITKGAveeilnvcTHVEVNgEVVPLTDTLREKILAQVEELNREGLRVLAIAYKKLPAP 463
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 609 YFKMWQKmleDansatlerderisglyeeiERDLMLLGATAVEDKLQEGVIETITSLSLANIKIWILTGD 678
Cdd:cd02077  464 EGEYSVK---D-------------------EKELILIGFLAFLDPPKESAAQAIKALKKNGVNVKILTGD 511
P-type_ATPase cd07539
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ...
534-727 1.85e-07

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


Pssm-ID: 319840 [Multi-domain]  Cd Length: 634  Bit Score: 54.73  E-value: 1.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 534 LAFLDFNNIRKRMSVIVRNPEGRIKLYSKGA-DTIL--------FEKLHPSNEDLQSLTSDHLSEFAGEGLRTLAIAYRE 604
Cdd:cd07539  324 LAELPFESSRGYAAAIGRTGGGIPLLAVKGApEVVLprcdrrmtGGQVVPLTEADRQAIEEVNELLAGQGLRVLAVAYRT 403
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 605 LDdkyfkmwqkmleDANSATLERDerisglyeeiERDLMLLGATAVEDKLQEGVIETITSLSLANIKIWILTGDKQETAI 684
Cdd:cd07539  404 LD------------AGTTHAVEAV----------VDDLELLGLLGLADTARPGAAALIAALHDAGIDVVMITGDHPITAR 461
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 568916992 685 NIGYACNVLTDAMdalfVITGNTAgevrEELRPMPLKVMSRTI 727
Cdd:cd07539  462 AIAKELGLPRDAE----VVTGAEL----DALDEEALTGLVADI 496
P-type_ATPase_H cd02076
plant and fungal plasma membrane H(+)-ATPases, and related bacterial and archaeal putative H(+) ...
114-612 9.21e-06

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


Pssm-ID: 319771 [Multi-domain]  Cd Length: 781  Bit Score: 49.15  E-value: 9.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 114 QSKVLINSKLQNEKWMNVKVGDIIKLENNQFVAADLLLLSSSEPHglcyVETAELDGETnlkvrqaLPVTSELGADIssl 193
Cdd:cd02076   93 KARVLRDGQWQEIDAKELVPGDIVSLKIGDIVPADARLLTGDALQ----VDQSALTGES-------LPVTKHPGDEA--- 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 194 aefdgivrceapnnkldrFSGvlswkdskhalsnqKIILRG---CVLRNTswcfGMVLFAGPDTKLMQNSGKTKFKRTSI 270
Cdd:cd02076  159 ------------------YSG--------------SIVKQGemlAVVTAT----GSNTFFGKTAALVASAEEQGHLQKVL 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 271 DRLMNTLVLWIFgflVCLGIILAVGSsilesevgdqfrtppfwregeksFLFSGFLTFWSYVIILNTL-VPISLYVSVEV 349
Cdd:cd02076  203 NKIGNFLILLAL---ILVLIIVIVAL-----------------------YRHDPFLEILQFVLVLLIAsIPVAMPAVLTV 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 350 IrlghsyfinwdrkMYYASKAMPAE----ARTTTLnEELGQIEYIFSDKTGTLTQNIMTFKKCSIngrvyagevlddpiq 425
Cdd:cd02076  257 T-------------MAVGALELAKKkaivSRLSAI-EELAGVDILCSDKTGTLTLNKLSLDEPYS--------------- 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 426 kkeitkekeatdfssksksektlhffdqslmesieLGDPKVHEFLRLLALChtvMSEENsagqlvyqvQSPDEGALVTAA 505
Cdd:cd02076  308 -----------------------------------LEGDGKDELLLLAALA---SDTEN---------PDAIDTAILNAL 340
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 506 RNfgfifksrTPETITIeelgtpvtYQLLAFLDFNNIRKRMSVIVRNPEGRIKLYSKGADTILFEKLHPSNEDLQSLtSD 585
Cdd:cd02076  341 DD--------YKPDLAG--------YKQLKFTPFDPVDKRTEATVEDPDGERFKVTKGAPQVILELVGNDEAIRQAV-EE 403
                        490       500
                 ....*....|....*....|....*..
gi 568916992 586 HLSEFAGEGLRTLAIAyRELDDKYFKM 612
Cdd:cd02076  404 KIDELASRGYRSLGVA-RKEDGGRWEL 429
PRK10517 PRK10517
magnesium-transporting P-type ATPase MgtA;
538-678 3.60e-05

magnesium-transporting P-type ATPase MgtA;


Pssm-ID: 236705 [Multi-domain]  Cd Length: 902  Bit Score: 47.37  E-value: 3.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 538 DFNniRKRMSVIVRNPEGRIKLYSKGAdtiLFEKLHPS-----NEDLQSLTSDHLS-------EFAGEGLRTLAIAYREL 605
Cdd:PRK10517 450 DFE--RRRMSVVVAENTEHHQLICKGA---LEEILNVCsqvrhNGEIVPLDDIMLRrikrvtdTLNRQGLRVVAVATKYL 524
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568916992 606 ddkyfkmwqkmledanSATLERDERISglyeeiERDLMLLGATAVEDKLQEGVIETITSLSLANIKIWILTGD 678
Cdd:PRK10517 525 ----------------PAREGDYQRAD------ESDLILEGYIAFLDPPKETTAPALKALKASGVTVKILTGD 575
P-type_ATPase_Cu-like cd02094
P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A ...
614-686 3.88e-05

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


Pssm-ID: 319783 [Multi-domain]  Cd Length: 647  Bit Score: 47.09  E-value: 3.88e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568916992 614 QKMLEDANSATLERDERISGLYEE------IERDLMLLGATAVEDKLQEGVIETITSLSLANIKIWILTGDKQETAINI 686
Cdd:cd02094  423 RRLMEENGIDLSALEAEALALEEEgktvvlVAVDGELAGLIAVADPLKPDAAEAIEALKKMGIKVVMLTGDNRRTARAI 501
P-type_ATPase_HM cd02079
P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) ...
578-687 7.58e-05

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: 46.05  E-value: 7.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916992 578 DLQSLTSDHLSEFAGEGLRTlaiayrELDDKYF-----KMWQKMLEDANSATLERDERISGLYeeIERDLMLLGATAVED 652
Cdd:cd02079  376 GLPPLEVEDVEEIPGKGISG------EVDGREVligslSFAEEEGLVEAADALSDAGKTSAVY--VGRDGKLVGLFALED 447
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568916992 653 KLQEGVIETITSLSLANIKIWILTGDKQETAINIG 687
Cdd:cd02079  448 QLRPEAKEVIAELKSGGIKVVMLTGDNEAAAQAVA 482
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
644-687 1.04e-03

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 42.44  E-value: 1.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 568916992 644 LLGATAVEDKLQEGVIETITSLSLANIKIWILTGDKQETAINIG 687
Cdd:COG2217  532 LLGLIALADTLRPEAAEAIAALKALGIRVVMLTGDNERTAEAVA 575
P-type_ATPase_Na-K_like cd02608
alpha-subunit of Na(+)/K(+)-ATPases and of gastric H(+)/K(+)-ATPase, similar to the human Na(+) ...
382-404 5.60e-03

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


Pssm-ID: 319794 [Multi-domain]  Cd Length: 905  Bit Score: 40.03  E-value: 5.60e-03
                         10        20
                 ....*....|....*....|...
gi 568916992 382 EELGQIEYIFSDKTGTLTQNIMT 404
Cdd:cd02608  304 ETLGSTSTICSDKTGTLTQNRMT 326
 
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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