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Conserved domains on  [gi|21749067|dbj|BAC03528|]
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unnamed protein product [Homo sapiens]

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 ...
 68-455 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: 569.50  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067  68 GNRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITMLPLAIVLFVIMIKDGMEDFKRHRFDKAI 147
Cdd:cd02073   1 DNRISTTKYTVFTFLPKNLFEQFRRVANLYFLFIAILQQIPGISPTGPYTTLLPLLFVLGVTAIKEGYEDIRRHKSDNEV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067 148 NCSNIRIYERKEqtYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVKGFSQQEV 227
Cdd:cd02073  81 NNRPVQVLRGGK--FVKKKWKDIRVGDIVRVKNDEFVPADLLLLSSSEPDGLCYVETANLDGETNLKIRQALPETALLLS 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067 228 QFEPELSHNTIVCEKPNNHLNKFKGYMEHPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKAMLNNSGPRYKRS 307
Cdd:cd02073 159 EEDLARFSGEIECEQPNNDLYTFNGTLELNGGRELPLSPDNLLLRGCTLRNTEWVYGVVVYTGHETKLMLNSGGTPLKRS 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067 308 KIERRMNIDIFFCIGILILMCLIGAVGHSIWNGTFEEHPPFDVPDANGSflpSALGGFYMFLTMIILLQVLIPISLYVSI 387
Cdd:cd02073 239 SIEKKMNRFIIAIFCILIVMCLISAIGKGIWLSKHGRDLWYLLPKEERS---PALEFFFDFLTFIILYNNLIPISLYVTI 315

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21749067 388 ELVKLGQVFFLSNDLDLYDEETDLSIQCRALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEY 455
Cdd:cd02073 316 EVVKFLQSFFINWDLDMYDEETDTPAEARTSNLNEELGQVEYIFSDKTGTLTENIMEFKKCSINGVDY 383
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
 429-495 9.90e-04

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 cd01431:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 319  Bit Score: 41.28  E-value: 9.90e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21749067 429 YIFSDKTGTLTENKMVFRRC-----------TIMGSEYSHQENGIEAPKGSIPLSKRKYPALLRNEEIKDILLALLEA 495
Cdd:cd01431   1 VICSDKTGTLTKNGMTVTKLfieeipfnstrKRMSVVVRLPGRYRAIVKGAPETILSRCSHALTEEDRNKIEKAQEES 78
 
Name Accession Description Interval E-value
P-type_ATPase_APLT_Dnf-like cd02073
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ...
 68-455 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: 569.50  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067  68 GNRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITMLPLAIVLFVIMIKDGMEDFKRHRFDKAI 147
Cdd:cd02073   1 DNRISTTKYTVFTFLPKNLFEQFRRVANLYFLFIAILQQIPGISPTGPYTTLLPLLFVLGVTAIKEGYEDIRRHKSDNEV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067 148 NCSNIRIYERKEqtYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVKGFSQQEV 227
Cdd:cd02073  81 NNRPVQVLRGGK--FVKKKWKDIRVGDIVRVKNDEFVPADLLLLSSSEPDGLCYVETANLDGETNLKIRQALPETALLLS 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067 228 QFEPELSHNTIVCEKPNNHLNKFKGYMEHPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKAMLNNSGPRYKRS 307
Cdd:cd02073 159 EEDLARFSGEIECEQPNNDLYTFNGTLELNGGRELPLSPDNLLLRGCTLRNTEWVYGVVVYTGHETKLMLNSGGTPLKRS 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067 308 KIERRMNIDIFFCIGILILMCLIGAVGHSIWNGTFEEHPPFDVPDANGSflpSALGGFYMFLTMIILLQVLIPISLYVSI 387
Cdd:cd02073 239 SIEKKMNRFIIAIFCILIVMCLISAIGKGIWLSKHGRDLWYLLPKEERS---PALEFFFDFLTFIILYNNLIPISLYVTI 315

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21749067 388 ELVKLGQVFFLSNDLDLYDEETDLSIQCRALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEY 455
Cdd:cd02073 316 EVVKFLQSFFINWDLDMYDEETDTPAEARTSNLNEELGQVEYIFSDKTGTLTENIMEFKKCSINGVDY 383
ATPase-Plipid TIGR01652
phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase ...
 66-464 1.20e-144

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: 442.59  E-value: 1.20e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067     66 YPGNRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITMLPLAIVLFVIMIKDGMEDFKRHRFDK 145
Cdd:TIGR01652    1 FCSNKISTTKYTVLTFLPKNLFEQFKRFANLYFLVVALLQQVPILSPTYRGTSIVPLAFVLIVTAIKEAIEDIRRRRRDK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067    146 AINCSNIRIYERKeQTYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGETNLKQR---CVVKGF 222
Cdd:TIGR01652   81 EVNNRLTEVLEGH-GQFVEIPWKDLRVGDIVKVKKDERIPADLLLLSSSEPDGVCYVETANLDGETNLKLRqalEETQKM 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067    223 SQQEV----QFEpelshntIVCEKPNNHLNKFKGYMEHPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKAMLN 298
Cdd:TIGR01652  160 LDEDDiknfSGE-------IECEQPNASLYSFQGNMTINGDRQYPLSPDNILLRGCTLRNTDWVIGVVVYTGHDTKLMRN 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067    299 NSGPRYKRSKIERRMNIDIFFCIGILILMCLIGAVGHSIWNGTFEEHPPFDVPDanGSFLPSALGGFYMFLTMIILLQVL 378
Cdd:TIGR01652  233 ATQAPSKRSRLEKELNFLIIILFCLLFVLCLISSVGAGIWNDAHGKDLWYIRLD--VSERNAAANGFFSFLTFLILFSSL 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067    379 IPISLYVSIELVKLGQVFFLSNDLDLYDEETDLSIQCRALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYSHQ 458
Cdd:TIGR01652  311 IPISLYVSLELVKSVQAYFINSDLQMYHEKTDTPASVRTSNLNEELGQVEYIFSDKTGTLTQNIMEFKKCSIAGVSYGDG 390


                   ....*.
gi 21749067    459 ENGIEA 464
Cdd:TIGR01652  391 FTEIKD 396
PLN03190 PLN03190
aminophospholipid translocase; Provisional
 54-456 2.10e-121

aminophospholipid translocase; Provisional


Pssm-ID: 215623 [Multi-domain]  Cd Length: 1178  Bit Score: 384.25  E-value: 2.10e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067    54 IFHQDWEEVSRRY--PGNRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITMLPLAIVLFVIMI 131
Cdd:PLN03190   73 VYLNDPEKSNERFefAGNSIRTAKYSVFSFLPRNLFEQFHRVAYIYFLVIAVLNQLPQLAVFGRGASILPLAFVLLVTAV 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067   132 KDGMEDFKRHRFDKAINCSNIRIYERKEqtYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGET 211
Cdd:PLN03190  153 KDAYEDWRRHRSDRIENNRLAWVLVDDQ--FQEKKWKDIRVGEIIKIQANDTLPCDMVLLSTSDPTGVAYVQTINLDGES 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067   212 NLKQRcvvkgFSQQEVQF---EPELSHNTIVCEKPNNHLNKFKGYMEhPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIY 288
Cdd:PLN03190  231 NLKTR-----YAKQETLSkipEKEKINGLIKCEKPNRNIYGFQANME-VDGKRLSLGPSNIILRGCELKNTAWAIGVAVY 304

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067   289 AGHETKAMLNNSGPRYKRSKIERRMNIDIFFCIGILILMCLIGAVGHSIWNGT---------FEEHPPFDVPDA-NGSFL 358
Cdd:PLN03190  305 CGRETKAMLNNSGAPSKRSRLETRMNLEIIILSLFLIALCTIVSVCAAVWLRRhrdeldtipFYRRKDFSEGGPkNYNYY 384

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067   359 PSALGGFYMFLTMIILLQVLIPISLYVSIELVKLGQVFFLSNDLDLYDEETDLSIQCRALNIAEDLGQIQYIFSDKTGTL 438
Cdd:PLN03190  385 GWGWEIFFTFLMSVIVFQIMIPISLYISMELVRVGQAYFMIRDDQMYDEASNSRFQCRALNINEDLGQIKYVFSDKTGTL 464

                         410
                  ....*....|....*...
gi 21749067   439 TENKMVFRRCTIMGSEYS 456
Cdd:PLN03190  465 TENKMEFQCASIWGVDYS 482
PhoLip_ATPase_N pfam16209
Phospholipid-translocating ATPase N-terminal; PhoLip_ATPase_N is found at the N-terminus of a ...
 48-119 1.04e-23

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: 94.08  E-value: 1.04e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21749067    48 VFPNNSIFHQDweevsRRYPGNRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITM 119
Cdd:pfam16209   1 VYINDPEKNSE-----FKYPSNKISTSKYTLLTFLPKNLFEQFRRVANLYFLLIAILQLIPGISPTGPYTTI 67
MgtA COG0474
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism];
416-456 4.68e-06

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


Pssm-ID: 440242 [Multi-domain]  Cd Length: 874  Bit Score: 49.33  E-value: 4.68e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 21749067 416 RALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYS 456
Cdd:COG0474 312 RRLPAVETLGSVTVICTDKTGTLTQNKMTVERVYTGGGTYE 352
P-type_ATPases cd01431
ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, ...
 429-495 9.90e-04

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


Pssm-ID: 319764 [Multi-domain]  Cd Length: 319  Bit Score: 41.28  E-value: 9.90e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21749067 429 YIFSDKTGTLTENKMVFRRC-----------TIMGSEYSHQENGIEAPKGSIPLSKRKYPALLRNEEIKDILLALLEA 495
Cdd:cd01431   1 VICSDKTGTLTKNGMTVTKLfieeipfnstrKRMSVVVRLPGRYRAIVKGAPETILSRCSHALTEEDRNKIEKAQEES 78
 
Name Accession Description Interval E-value
P-type_ATPase_APLT_Dnf-like cd02073
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ...
 68-455 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: 569.50  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067  68 GNRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITMLPLAIVLFVIMIKDGMEDFKRHRFDKAI 147
Cdd:cd02073   1 DNRISTTKYTVFTFLPKNLFEQFRRVANLYFLFIAILQQIPGISPTGPYTTLLPLLFVLGVTAIKEGYEDIRRHKSDNEV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067 148 NCSNIRIYERKEqtYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVKGFSQQEV 227
Cdd:cd02073  81 NNRPVQVLRGGK--FVKKKWKDIRVGDIVRVKNDEFVPADLLLLSSSEPDGLCYVETANLDGETNLKIRQALPETALLLS 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067 228 QFEPELSHNTIVCEKPNNHLNKFKGYMEHPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKAMLNNSGPRYKRS 307
Cdd:cd02073 159 EEDLARFSGEIECEQPNNDLYTFNGTLELNGGRELPLSPDNLLLRGCTLRNTEWVYGVVVYTGHETKLMLNSGGTPLKRS 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067 308 KIERRMNIDIFFCIGILILMCLIGAVGHSIWNGTFEEHPPFDVPDANGSflpSALGGFYMFLTMIILLQVLIPISLYVSI 387
Cdd:cd02073 239 SIEKKMNRFIIAIFCILIVMCLISAIGKGIWLSKHGRDLWYLLPKEERS---PALEFFFDFLTFIILYNNLIPISLYVTI 315

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21749067 388 ELVKLGQVFFLSNDLDLYDEETDLSIQCRALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEY 455
Cdd:cd02073 316 EVVKFLQSFFINWDLDMYDEETDTPAEARTSNLNEELGQVEYIFSDKTGTLTENIMEFKKCSINGVDY 383
ATPase-Plipid TIGR01652
phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase ...
 66-464 1.20e-144

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: 442.59  E-value: 1.20e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067     66 YPGNRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITMLPLAIVLFVIMIKDGMEDFKRHRFDK 145
Cdd:TIGR01652    1 FCSNKISTTKYTVLTFLPKNLFEQFKRFANLYFLVVALLQQVPILSPTYRGTSIVPLAFVLIVTAIKEAIEDIRRRRRDK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067    146 AINCSNIRIYERKeQTYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGETNLKQR---CVVKGF 222
Cdd:TIGR01652   81 EVNNRLTEVLEGH-GQFVEIPWKDLRVGDIVKVKKDERIPADLLLLSSSEPDGVCYVETANLDGETNLKLRqalEETQKM 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067    223 SQQEV----QFEpelshntIVCEKPNNHLNKFKGYMEHPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKAMLN 298
Cdd:TIGR01652  160 LDEDDiknfSGE-------IECEQPNASLYSFQGNMTINGDRQYPLSPDNILLRGCTLRNTDWVIGVVVYTGHDTKLMRN 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067    299 NSGPRYKRSKIERRMNIDIFFCIGILILMCLIGAVGHSIWNGTFEEHPPFDVPDanGSFLPSALGGFYMFLTMIILLQVL 378
Cdd:TIGR01652  233 ATQAPSKRSRLEKELNFLIIILFCLLFVLCLISSVGAGIWNDAHGKDLWYIRLD--VSERNAAANGFFSFLTFLILFSSL 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067    379 IPISLYVSIELVKLGQVFFLSNDLDLYDEETDLSIQCRALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYSHQ 458
Cdd:TIGR01652  311 IPISLYVSLELVKSVQAYFINSDLQMYHEKTDTPASVRTSNLNEELGQVEYIFSDKTGTLTQNIMEFKKCSIAGVSYGDG 390


                   ....*.
gi 21749067    459 ENGIEA 464
Cdd:TIGR01652  391 FTEIKD 396
PLN03190 PLN03190
aminophospholipid translocase; Provisional
 54-456 2.10e-121

aminophospholipid translocase; Provisional


Pssm-ID: 215623 [Multi-domain]  Cd Length: 1178  Bit Score: 384.25  E-value: 2.10e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067    54 IFHQDWEEVSRRY--PGNRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITMLPLAIVLFVIMI 131
Cdd:PLN03190   73 VYLNDPEKSNERFefAGNSIRTAKYSVFSFLPRNLFEQFHRVAYIYFLVIAVLNQLPQLAVFGRGASILPLAFVLLVTAV 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067   132 KDGMEDFKRHRFDKAINCSNIRIYERKEqtYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGET 211
Cdd:PLN03190  153 KDAYEDWRRHRSDRIENNRLAWVLVDDQ--FQEKKWKDIRVGEIIKIQANDTLPCDMVLLSTSDPTGVAYVQTINLDGES 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067   212 NLKQRcvvkgFSQQEVQF---EPELSHNTIVCEKPNNHLNKFKGYMEhPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIY 288
Cdd:PLN03190  231 NLKTR-----YAKQETLSkipEKEKINGLIKCEKPNRNIYGFQANME-VDGKRLSLGPSNIILRGCELKNTAWAIGVAVY 304

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067   289 AGHETKAMLNNSGPRYKRSKIERRMNIDIFFCIGILILMCLIGAVGHSIWNGT---------FEEHPPFDVPDA-NGSFL 358
Cdd:PLN03190  305 CGRETKAMLNNSGAPSKRSRLETRMNLEIIILSLFLIALCTIVSVCAAVWLRRhrdeldtipFYRRKDFSEGGPkNYNYY 384

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067   359 PSALGGFYMFLTMIILLQVLIPISLYVSIELVKLGQVFFLSNDLDLYDEETDLSIQCRALNIAEDLGQIQYIFSDKTGTL 438
Cdd:PLN03190  385 GWGWEIFFTFLMSVIVFQIMIPISLYISMELVRVGQAYFMIRDDQMYDEASNSRFQCRALNINEDLGQIKYVFSDKTGTL 464

                         410
                  ....*....|....*...
gi 21749067   439 TENKMVFRRCTIMGSEYS 456
Cdd:PLN03190  465 TENKMEFQCASIWGVDYS 482
P-type_ATPase_APLT cd07536
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ...
 69-459 1.02e-99

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: 318.78  E-value: 1.02e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067  69 NRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITMLPLAIVLFVIMIKDGMEDFKRHRFDKAIN 148
Cdd:cd07536   2 NSISNQKYNVFTFLPGVLYEQFKRFLNLYFLVIACLQFVPALKPGYLYTTWAPLIFILAVTMTKEAIDDFRRFQRDKEVN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067 149 CSniRIYERKEQTYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVkgfsqQEVQ 228
Cdd:cd07536  82 KK--QLYSKLTGRKVQIKSSDIQVGDIVIVEKNQRIPSDMVLLRTSEPQGSCYVETAQLDGETDLKLRVAV-----SCTQ 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067 229 FEPELSH-----NTIVCEKPNNHLNKFKGYM--EHPD-QTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKAMLNNS 300
Cdd:cd07536 155 QLPALGDlmkisAYVECQKPQMDIHSFEGNFtlEDSDpPIHESLSIENTLLRASTLRNTGWVIGVVVYTGKETKLVMNTS 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067 301 GPRYKRSKIERRMNIDIFFCIGILILMCLIGAVGHSIWNGTFEEHPPFDVPDANGSFlpsalGGFYMFLTMIILLQVLIP 380
Cdd:cd07536 235 NAKNKVGLLDLELNRLTKALFLALVVLSLVMVTLQGFWGPWYGEKNWYIKKMDTTSD-----NFGRNLLRFLLLFSYIIP 309

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21749067 381 ISLYVSIELVKLGQVFFLSNDLDLYDEETDLSIQCRALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYSHQE 459
Cdd:cd07536 310 ISLRVNLDMVKAVYAWFIMWDENMYYIGNDTGTVARTSTIPEELGQVVYLLTDKTGTLTQNEMIFKRCHIGGVSYGGQV 388
P-type_ATPase_APLT_Neo1-like cd07541
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Neo1p and human ...
 69-447 1.69e-56

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: 201.87  E-value: 1.69e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067  69 NRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITMLPLAIVLFVIMIKDGMEDFKRHRFDKAIN 148
Cdd:cd07541   2 NEVRNQKYNIFTFLPKVLYEQFKFFYNLYFLVVALSQFVPALKIGYLYTYWAPLGFVLAVTMAKEAVDDIRRRRRDKEQN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067 149 csniriYERKEQ--TYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVKGFSQQE 226
Cdd:cd07541  82 ------YEKLTVrgETVEIPSSDIKVGDLIIVEKNQRIPADMVLLRTSEKSGSCFIRTDQLDGETDWKLRIAVPCTQKLP 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067 227 VQFEPeLSHNTIVCEKPNNHLNKFKG-YMEHPDQTRTGFGCESLLLrGCTIRNTEMAVGIVIYAGHETKAMLNNSGPRYK 305
Cdd:cd07541 156 EEGIL-NSISAVYAEAPQKDIHSFYGtFTINDDPTSESLSVENTLW-ANTVVASGTVIGVVVYTGKETRSVMNTSQPKNK 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067 306 RSKIERRMN--IDIFFC--IGILILMCLIGAVGHSiWngtfeehppfdvpdangsflpsalggfYMFLT-MIILLQVLIP 380
Cdd:cd07541 234 VGLLDLEINflTKILFCavLALSIVMVALQGFQGP-W---------------------------YIYLFrFLILFSSIIP 285

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21749067 381 ISLYVSIELVKLGQVFFLSNDLDLydEETDLsiqcRALNIAEDLGQIQYIFSDKTGTLTENKMVFRR 447
Cdd:cd07541 286 ISLRVNLDMAKIVYSWQIEHDKNI--PGTVV----RTSTIPEELGRIEYLLSDKTGTLTQNEMVFKK 346
ATPase_P-type TIGR01494
ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large ...
 117-456 3.13e-48

ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large family of trans-membrane transporters acting on charged substances. The distinguishing feature of the family is the formation of a phosphorylated intermediate (aspartyl-phosphate) during the course of the reaction. Another common name for these enzymes is the E1-E2 ATPases based on the two isolable conformations: E1 (unphosphorylated) and E2 (phosphorylated). Generally, P-type ATPases consist of only a single subunit encompassing the ATPase and ion translocation pathway, however, in the case of the potassium (TIGR01497) and sodium/potassium (TIGR01106) varieties, these functions are split between two subunits. Additional small regulatory or stabilizing subunits may also exist in some forms. P-type ATPases are nearly ubiquitous in life and are found in numerous copies in higher organisms (at least 45 in Arabidopsis thaliana, for instance). Phylogenetic analyses have revealed that the P-type ATPase subfamily is divided up into groups based on substrate specificities and this is represented in the various subfamily and equivalog models that have been made: IA (K+) TIGR01497, IB (heavy metals) TIGR01525, IIA1 (SERCA-type Ca++) TIGR01116, IIA2 (PMR1-type Ca++) TIGR01522, IIB (PMCA-type Ca++) TIGR01517, IIC (Na+/K+, H+/K+ antiporters) TIGR01106, IID (fungal-type Na+ and K+) TIGR01523, IIIA (H+) TIGR01647, IIIB (Mg++) TIGR01524, IV (phospholipid, flippase) TIGR01652 and V (unknown specificity) TIGR01657. The crystal structure of one calcium-pumping ATPase and an analysis of the fold of the catalytic domain of the P-type ATPases have been published. These reveal that the catalytic core of these enzymes is a haloacid dehalogenase(HAD)-type aspartate-nucleophile hydrolase. The location of the ATP-binding loop in between the first and second HAD conserved catalytic motifs defines these enzymes as members of subfamily I of the HAD superfamily (see also TIGR01493, TIGR01509, TIGR01549, TIGR01544 and TIGR01545). Based on these classifications, the P-type ATPase _superfamily_ corresponds to the IC subfamily of the HAD superfamily.


Pssm-ID: 273656 [Multi-domain]  Cd Length: 545  Bit Score: 175.20  E-value: 3.13e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067   117 ITMLPLAIVLFVIMIKDGMEDFKRHRFDKAINCSNIRIYeRKEQTYVQKcwKDVRVGDFIQMKCNEIVPADILLLFSSdp 196
Cdd:TIGR01494   2 ILFLVLLFVLLEVKQKLKAEDALRSLKDSLVNTATVLVL-RNGWKEISS--KDLVPGDVVLVKSGDTVPADGVLLSGS-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067   197 ngiCHLETASLDGETNLKQRCVVKGfsqqevqfepelshntivCEKPNNHLNKFKGYMEHpdQTRTGFGCeslllrgcti 276
Cdd:TIGR01494  77 ---AFVDESSLTGESLPVLKTALPD------------------GDAVFAGTINFGGTLIV--KVTATGIL---------- 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067   277 rNTEMAVGIVIYAGHETKAMLNNsgpryKRSKIERrmniDIFFCIGILILMCLIGAVGHSIWNGTfeehppfdvpdangs 356
Cdd:TIGR01494 124 -TTVGKIAVVVYTGFSTKTPLQS-----KADKFEN----FIFILFLLLLALAVFLLLPIGGWDGN--------------- 178

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067   357 flpsalGGFYMFLTMIILLQVLIPISLYVSIELVKLGQvfflsnDLDLYDEetdlSIQCRALNIAEDLGQIQYIFSDKTG 436
Cdd:TIGR01494 179 ------SIYKAILRALAVLVIAIPCALPLAVSVALAVG------DARMAKK----GILVKNLNALEELGKVDVICFDKTG 242

                         330       340
                  ....*....|....*....|
gi 21749067   437 TLTENKMVFRRCTIMGSEYS 456
Cdd:TIGR01494 243 TLTTNKMTLQKVIIIGGVEE 262
PhoLip_ATPase_N pfam16209
Phospholipid-translocating ATPase N-terminal; PhoLip_ATPase_N is found at the N-terminus of a ...
 48-119 1.04e-23

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: 94.08  E-value: 1.04e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21749067    48 VFPNNSIFHQDweevsRRYPGNRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITM 119
Cdd:pfam16209   1 VYINDPEKNSE-----FKYPSNKISTSKYTLLTFLPKNLFEQFRRVANLYFLLIAILQLIPGISPTGPYTTI 67
MgtA COG0474
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism];
416-456 4.68e-06

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


Pssm-ID: 440242 [Multi-domain]  Cd Length: 874  Bit Score: 49.33  E-value: 4.68e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 21749067 416 RALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYS 456
Cdd:COG0474 312 RRLPAVETLGSVTVICTDKTGTLTQNKMTVERVYTGGGTYE 352
P-type_ATPase_Ca_prok cd02089
prokaryotic P-type Ca(2+)-ATPase similar to Synechococcus elongatus sp. strain PCC 7942 PacL ...
 416-475 6.08e-05

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: 45.68  E-value: 6.08e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21749067 416 RALNIAEDLGQIQYIFSDKTGTLTENKMVFRR-CTI----------MGSEYSHQENGIEA--PK-GSIPL-SKRK 475
Cdd:cd02089 288 RKLPAVETLGSVSVICSDKTGTLTQNKMTVEKiYTIgdptetalirAARKAGLDKEELEKkyPRiAEIPFdSERK 362
P-type_ATPase_cation cd02082
P-type cation-transporting ATPases, similar to human ATPase type 13A1-A4 (ATP13A1-A4) proteins ...
 86-446 3.04e-04

P-type cation-transporting ATPases, similar to human ATPase type 13A1-A4 (ATP13A1-A4) proteins and Saccharomyces cerevisiae Ypk9p and Spf1p; Saccharomyces cerevisiae Yph9p localizes to the yeast vacuole and may play a role in sequestering heavy metal ions, its deletion confers sensitivity for growth for cadmium, manganese, nickel or selenium. Saccharomyces 1 Spf1p may mediate manganese transport into the endoplasmic reticulum. Human ATP13A2 (PARK9/CLN12) is a lysosomal transporter with zinc as the possible substrate. Mutation in the ATP13A2 gene has been linked to Parkinson's disease and Kufor-Rakeb syndrome, and to neuronal ceroid lipofuscinoses. ATP13A3/AFURS1 is a candidate gene for oculo auriculo vertebral spectrum (OAVS), being one of nine genes included in a 3q29 microduplication in a patient with OAVS. Mutation in the human ATP13A4 may be involved in a speech-language disorder. The expression of ATP13A1 has been followed during mouse development, ATP13A1 transcript expression showed an increase as development progressed, with the highest expression at the peak of neurogenesis. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319777 [Multi-domain]  Cd Length: 786  Bit Score: 43.73  E-value: 3.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067  86 LFEQFHRWANLYFLFLVILnWMPSmEVFHREITMLPLAIVLFVIMIKDGMEDFKRHRfdKAINCSNIRIYERKEQTYVQK 165
Cdd:cd02082  25 MWREFKKPFNFFQYFGVIL-WGID-EYVYYAITVVFMTTINSLSCIYIRGVMQKELK--DACLNNTSVIVQRHGYQEITI 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067 166 CWKDVRVGDFIQMKCNE-IVPADILLLfssdpNGICHLETASLDGETNLKQRCVVKGFSQQEVQFEPELSHNTIVcekpn 244
Cdd:cd02082 101 ASNMIVPGDIVLIKRREvTLPCDCVLL-----EGSCIVTEAMLTGESVPIGKCQIPTDSHDDVLFKYESSKSHTL----- 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067 245 nhlnkFKGYMEHPDQTRTGFGCESLLLRgctirntemaVGIVIYAGHETKAMLnnsgprYKRsKIERRMNIDIFFCIGIL 324
Cdd:cd02082 171 -----FQGTQVMQIIPPEDDILKAIVVR----------TGFGTSKGQLIRAIL------YPK-PFNKKFQQQAVKFTLLL 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067 325 ILMCLIGAVgHSIWNGTFEEHPPfdvpdangsflpsalgGFYMFLTMIILLQVLIP-----ISLYVSIELVKLGQvffls 399
Cdd:cd02082 229 ATLALIGFL-YTLIRLLDIELPP----------------LFIAFEFLDILTYSVPPglpmlIAITNFVGLKRLKK----- 286

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 21749067 400 ndldlydeetdLSIQCRALNIAEDLGQIQYIFSDKTGTLTENKMVFR 446
Cdd:cd02082 287 -----------NQILCQDPNRISQAGRIQTLCFDKTGTLTEDKLDLI 322
ATPase-IIB_Ca TIGR01517
plasma-membrane calcium-translocating P-type ATPase; This model describes the P-type ATPase ...
 169-490 4.20e-04

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


Pssm-ID: 273668 [Multi-domain]  Cd Length: 956  Bit Score: 43.23  E-value: 4.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067   169 DVRVGDFIQMKCNEIVPADILLLFSSDpngiCHLETASLDGETNLKQRCVVKgfsqqevqfEPELSHNTIVCEkpnnhln 248
Cdd:TIGR01517 186 DIVVGDIVSLSTGDVVPADGVFISGLS----LEIDESSITGESDPIKKGPVQ---------DPFLLSGTVVNE------- 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067   249 kfkgymehpdqtrtGFGceslllrgctiRNTEMAVGIVIYAGhETKAMLNNSGPryKRSKIERRMN-----IDIFFCIG- 322
Cdd:TIGR01517 246 --------------GSG-----------RMLVTAVGVNSFGG-KLMMELRQAGE--EETPLQEKLSelaglIGKFGMGSa 297

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067   323 -ILILMCLIGAVGHSIWNGTFEEHPPFDVPdangSFLPsalggfyMFLTMIILLQVLIP--ISLYVSIELVKLGQVFFLS 399
Cdd:TIGR01517 298 vLLFLVLSLRYVFRIIRGDGRFEDTEEDAQ----TFLD-------HFIIAVTIVVVAVPegLPLAVTIALAYSMKKMMKD 366

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067   400 NDLdlydeetdlsiqCRALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYSHQEngieapkgsiPLSKRKYPAL 479
Cdd:TIGR01517 367 NNL------------VRHLAACETMGSATAICSDKTGTLTQNVMSVVQGYIGEQRFNVRD----------EIVLRNLPAA 424

                         330
                  ....*....|.
gi 21749067   480 LRNEEIKDILL 490
Cdd:TIGR01517 425 VRNILVEGISL 435
P-type_ATPase_HM cd02079
P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) ...
 123-448 8.20e-04

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: 42.20  E-value: 8.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067 123 AIVLFVIMIKDGMEDFKRHRFDKAI----NCSNIRIYERKEQTYVQKCWKDVRVGDFIQMKCNEIVPAD-ILLlfssdpN 197
Cdd:cd02079  92 AMLLFLFLLGRYLEERARSRARSALkallSLAPETATVLEDGSTEEVPVDDLKVGDVVLVKPGERIPVDgVVV------S 165

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067 198 GICHLETASLDGETnlkqrcvvkgfsqqevqfepelshntivceKPnnhLNKFKGymehpDQTRTGfgceslllrgcTIr 277
Cdd:cd02079 166 GESSVDESSLTGES------------------------------LP---VEKGAG-----DTVFAG-----------TI- 195

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067 278 NTEMAVGI-VIYAGHETK-----AMLNNSgpRYKRSKIERRmnIDIF---FCIGILILMCLIGAVGHSIwngtfeehppf 348
Cdd:cd02079 196 NLNGPLTIeVTKTGEDTTlakiiRLVEEA--QSSKPPLQRL--ADRFaryFTPAVLVLAALVFLFWPLV----------- 260

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067 349 dvpdangsfLPSALGGFYMFLTMIIL-----LQVLIPISLYVSIE-------LVKLGQVFflsndldlydeetdlsiqcr 416
Cdd:cd02079 261 ---------GGPPSLALYRALAVLVVacpcaLGLATPTAIVAGIGraarkgiLIKGGDVL-------------------- 311

                       330       340       350
                ....*....|....*....|....*....|..
gi 21749067 417 alniaEDLGQIQYIFSDKTGTLTENKMVFRRC 448
Cdd:cd02079 312 -----ETLAKVDTVAFDKTGTLTEGKPEVTEI 338
P-type_ATPases cd01431
ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, ...
 429-495 9.90e-04

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


Pssm-ID: 319764 [Multi-domain]  Cd Length: 319  Bit Score: 41.28  E-value: 9.90e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21749067 429 YIFSDKTGTLTENKMVFRRC-----------TIMGSEYSHQENGIEAPKGSIPLSKRKYPALLRNEEIKDILLALLEA 495
Cdd:cd01431   1 VICSDKTGTLTKNGMTVTKLfieeipfnstrKRMSVVVRLPGRYRAIVKGAPETILSRCSHALTEEDRNKIEKAQEES 78
P-type_ATPase_Na_ENA cd02086
fungal-type Na(+)-ATPase, similar to the plasma membrane sodium transporters Saccharomyces ...
 416-447 1.28e-03

fungal-type Na(+)-ATPase, similar to the plasma membrane sodium transporters Saccharomyces cerevisiae Ena1p, Ena2p and Ustilago maydis Ena1, and the endoplasmic reticulum sodium transporter Ustilago maydis Ena2; Fungal-type Na(+)-ATPase (also called ENA ATPases). This subfamily includes the Saccharomyces cerevisiae plasma membrane transporters: Na(+)/Li(+)-exporting ATPase Ena1p which may also extrudes K(+), and Na(+)-exporting P-type ATPase Ena2p. It also includes Ustilago maydis plasma membrane Ena1, an K(+)/Na(+)-ATPase whose chief role is to pump Na(+) and K(+) out of the cytoplasm, especially at high pH values, and endoplasmic reticulum Ena2 ATPase which mediates Na(+) or K(+) fluxes in the ER or in other endomembranes. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319780 [Multi-domain]  Cd Length: 920  Bit Score: 41.67  E-value: 1.28e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 21749067 416 RALNIAEDLGQIQYIFSDKTGTLTENKMVFRR 447
Cdd:cd02086 317 RKLDALEALGAVTDICSDKTGTLTQGKMVVRQ 348
P-type_ATPase_Mg cd02077
magnesium transporting ATPase (MgtA), similar to Escherichia coli MgtA and Salmonella ...
 56-211 1.30e-03

magnesium transporting ATPase (MgtA), similar to Escherichia coli MgtA and Salmonella typhimurium MgtA; MgtA is a membrane protein which actively transports Mg(2+) into the cytosol with its electro-chemical gradient rather than against the gradient as other cation transporters do. It may act both as a transporter and as a sensor for Mg(2+). In Salmonella typhimurium and Escherichia coli, the two-component system PhoQ/PhoP regulates the transcription of the mgtA gene by sensing Mg(2+) concentrations in the periplasm. MgtA is activated by cardiolipin and it highly sensitive to free magnesium in vitro. It consists of a transmembrane domain and three cytosolic domains: nucleotide-binding domain, phosphorylation domain and actuator domain, and belongs to the P-type ATPase type III subfamily. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319772 [Multi-domain]  Cd Length: 768  Bit Score: 41.46  E-value: 1.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067  56 HQDWEEVSRRYPGNRTCTTKYTLFTflpRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITMLPLAIVLFVIMIKDGM 135
Cdd:cd02077   4 NEEAEERLEKYGPNEISHEKFPSWF---KLLLKAFINPFNIVLLVLALVSFFTDVLLAPGEFDLVGALIILLMVLISGLL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21749067 136 ---EDFKRHRFDKAI-----NCSNIRiyeRKEQTYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDpngiCHLETASL 207
Cdd:cd02077  81 dfiQEIRSLKAAEKLkkmvkNTATVI---RDGSKYMEIPIDELVPGDIVYLSAGDMIPADVRIIQSKD----LFVSQSSL 153


                ....
gi 21749067 208 DGET 211
Cdd:cd02077 154 TGES 157
P-type_ATPase cd07539
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ...
 416-443 1.89e-03

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


Pssm-ID: 319840 [Multi-domain]  Cd Length: 634  Bit Score: 40.86  E-value: 1.89e-03
                        10        20
                ....*....|....*....|....*...
gi 21749067 416 RALNIAEDLGQIQYIFSDKTGTLTENKM 443
Cdd:cd07539 288 RSPRTVEALGRVDTICFDKTGTLTENRL 315
P-type_ATPase_cation cd02080
P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, ...
 416-447 2.44e-03

P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, and Synechocystis sp. PCC 6803 PMA1, a putative Ca(2+)-ATPase; This subfamily includes the P-type Na(+)-ATPase of an alkaliphilic bacterium Exiguobacterium aurantiacum Mna and cyanobacterium Synechocystis sp. PCC 6803 PMA1, a cation-transporting ATPase which may translocate calcium. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319775 [Multi-domain]  Cd Length: 819  Bit Score: 40.71  E-value: 2.44e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 21749067 416 RALNIAEDLGQIQYIFSDKTGTLTENKMVFRR 447
Cdd:cd02080 288 RRLPAVETLGSVTVICSDKTGTLTRNEMTVQA 319
P-type_ATPase_SERCA cd02083
sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; ...
 416-479 2.70e-03

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: 40.74  E-value: 2.70e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21749067 416 RALNIAEDLGQIQYIFSDKTGTLTENKM-VFRRCTIMGSEYSHQENGIE------APKGSIPLSKRK-----YPAL 479
Cdd:cd02083 329 RSLPSVETLGCTSVICSDKTGTLTTNQMsVSRMFILDKVEDDSSLNEFEvtgstyAPEGEVFKNGKKvkagqYDGL 404
P-type_ATPase_SPCA cd02085
golgi-associated secretory pathway Ca(2+) transport ATPases, similar to human ATPase secretory ...
 416-452 5.64e-03

golgi-associated secretory pathway Ca(2+) transport ATPases, similar to human ATPase secretory pathway Ca(2+) transporting 1/hSPCA1 and Saccharomyces cerevisiae Ca(2+)/Mn(2+)-transporting P-type ATPase, Pmr1p; SPCAs are Ca(2+) pumps important for the golgi-associated secretion pathway, in addition some function as Mn(2+) pumps in Mn(2+) detoxification. Saccharomyces cerevisiae Pmr1p is a high affinity Ca(2+)/Mn(2+) ATPase which transports Ca(2+) and Mn(2+) from the cytoplasm into the Golgi. Pmr1p also contributes to Cd(2+) detoxification. This subfamily includes human SPCA1 and SPCA2, encoded by the ATP2C1 and ATP2C2 genes; autosomal dominant Hailey-Hailey disease is caused by mutations in the human ATP2C1 gene. It also includes Strongylocentrotus purpuratus testis secretory pathway calcium transporting ATPase SPCA which plays an important role in fertilization. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319779 [Multi-domain]  Cd Length: 804  Bit Score: 39.69  E-value: 5.64e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 21749067 416 RALNIAEDLGQIQYIFSDKTGTLTENKM--------------VFRRCTIMG 452
Cdd:cd02085 280 KKLPIVETLGCVNVICSDKTGTLTKNEMtvtkivtgcvcnnaVIRNNTLMG 330
P-type_ATPase_Ca_PMCA-like cd02081
animal plasma membrane Ca2(+)-ATPases (PMCA), similar to human ATP2B1-4/PMCA1-4, and related ...
 416-450 5.94e-03

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: 39.49  E-value: 5.94e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 21749067 416 RALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTI 450
Cdd:cd02081 304 RHLDACETMGNATAICSDKTGTLTQNRMTVVQGYI 338
 
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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