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Conserved domains on  [gi|767992219|ref|XP_011522194|]
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sarcoplasmic/endoplasmic reticulum calcium ATPase 3 isoform X10 [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 ...
5-518 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 cd02083:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 979  Bit Score: 1001.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   5 HLLPAADVLRHFSVTAEGGLSPAQVTGARERYGPNELPSEEGKSLWELVLEQFEDLLVRILLLAALVSFVLAWFEEGEET 84
Cdd:cd02083    1 HSKTVEEVLAYFGVDPTRGLSDEQVKRRREKYGPNELPAEEGKSLWELVLEQFDDLLVRILLLAAIISFVLALFEEGEEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  85 TTAFVEPLVIMLILVANAIVGVWQERNAESAIEALKEYEPEMGKVIRSDrKGVQRIRARDIVPGDIVEVAVGDKVPADLR 164
Cdd:cd02083   81 VTAFVEPFVILLILIANAVVGVWQERNAEKAIEALKEYEPEMAKVLRNG-KGVQRIRARELVPGDIVEVAVGDKVPADIR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 165 LIEIKSTTLRVDQSILTGESVSVTKHTEAIPDPRAVNQDKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMAAVEP 244
Cdd:cd02083  160 IIEIKSTTLRVDQSILTGESVSVIKHTDVVPDPRAVNQDKKNMLFSGTNVAAGKARGVVVGTGLNTEIGKIRDEMAETEE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 245 ERTPLQRKLDEFGRQLSHAISVICVAVWVINIGHFADPAHGGSWLRGAVYYFKIAVALAVAAIPEGLPAVITTCLALGTR 324
Cdd:cd02083  240 EKTPLQQKLDEFGEQLSKVISVICVAVWAINIGHFNDPAHGGSWIKGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTR 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 325 RMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFVVAEADAGsCLLHEFTISGTTYTPEGEVRQGDQPVRC 404
Cdd:cd02083  320 RMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVSRMFILDKVEDD-SSLNEFEVTGSTYAPEGEVFKNGKKVKA 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 405 GQFDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTDLQALSRVERAGACNTVIKQLMRKEFT 484
Cdd:cd02083  399 GQYDGLVELATICALCNDSSLDYNESKGVYEKVGEATETALTVLVEKMNVFNTDKSGLSKRERANACNDVIEQLWKKEFT 478
                        490       500       510
                 ....*....|....*....|....*....|....
gi 767992219 485 LEFSRDRKSMSVYCTPTRPhptGQGSKMFVKvGA 518
Cdd:cd02083  479 LEFSRDRKSMSVYCSPTKA---SGGNKLFVK-GA 508
 
Name Accession Description Interval E-value
P-type_ATPase_SERCA cd02083
sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; ...
5-518 0e+00

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: 1001.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   5 HLLPAADVLRHFSVTAEGGLSPAQVTGARERYGPNELPSEEGKSLWELVLEQFEDLLVRILLLAALVSFVLAWFEEGEET 84
Cdd:cd02083    1 HSKTVEEVLAYFGVDPTRGLSDEQVKRRREKYGPNELPAEEGKSLWELVLEQFDDLLVRILLLAAIISFVLALFEEGEEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  85 TTAFVEPLVIMLILVANAIVGVWQERNAESAIEALKEYEPEMGKVIRSDrKGVQRIRARDIVPGDIVEVAVGDKVPADLR 164
Cdd:cd02083   81 VTAFVEPFVILLILIANAVVGVWQERNAEKAIEALKEYEPEMAKVLRNG-KGVQRIRARELVPGDIVEVAVGDKVPADIR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 165 LIEIKSTTLRVDQSILTGESVSVTKHTEAIPDPRAVNQDKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMAAVEP 244
Cdd:cd02083  160 IIEIKSTTLRVDQSILTGESVSVIKHTDVVPDPRAVNQDKKNMLFSGTNVAAGKARGVVVGTGLNTEIGKIRDEMAETEE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 245 ERTPLQRKLDEFGRQLSHAISVICVAVWVINIGHFADPAHGGSWLRGAVYYFKIAVALAVAAIPEGLPAVITTCLALGTR 324
Cdd:cd02083  240 EKTPLQQKLDEFGEQLSKVISVICVAVWAINIGHFNDPAHGGSWIKGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTR 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 325 RMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFVVAEADAGsCLLHEFTISGTTYTPEGEVRQGDQPVRC 404
Cdd:cd02083  320 RMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVSRMFILDKVEDD-SSLNEFEVTGSTYAPEGEVFKNGKKVKA 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 405 GQFDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTDLQALSRVERAGACNTVIKQLMRKEFT 484
Cdd:cd02083  399 GQYDGLVELATICALCNDSSLDYNESKGVYEKVGEATETALTVLVEKMNVFNTDKSGLSKRERANACNDVIEQLWKKEFT 478
                        490       500       510
                 ....*....|....*....|....*....|....
gi 767992219 485 LEFSRDRKSMSVYCTPTRPhptGQGSKMFVKvGA 518
Cdd:cd02083  479 LEFSRDRKSMSVYCSPTKA---SGGNKLFVK-GA 508
ATPase-IIA1_Ca TIGR01116
sarco/endoplasmic reticulum calcium-translocating P-type ATPase; This model describes the ...
53-518 0e+00

sarco/endoplasmic reticulum calcium-translocating P-type ATPase; This model describes the P-type ATPase responsible for translocating calcium ions across the endoplasmic reticulum membrane of eukaryotes, and is of particular importance in the sarcoplasmic reticulum of skeletal and cardiac muscle in vertebrates. These pumps transfer Ca2+ from the cytoplasm to the lumen of the endoplasmic reticulum. In humans and mice, at least, there are multiple isoforms of the SERCA pump with overlapping but not redundant functions. Defects in SERCA isoforms are associated with diseases in humans. The calcium P-type ATPases have been characterized as Type IIA based on a phylogenetic analysis which distinguishes this group from the Type IIB PMCA calcium pump modelled by TIGR01517. A separate analysis divides Type IIA into sub-types, SERCA and PMR1, the latter of which is modelled by TIGR01522. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273452 [Multi-domain]  Cd Length: 917  Bit Score: 733.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   53 VLEQFEDLLVRILLLAALVSFVLAWFEEGEETTTAFVEPLVIMLILVANAIVGVWQERNAESAIEALKEYEPEMGKVIRS 132
Cdd:TIGR01116   1 VLEQFEDLLVRILLLAACVSFVLAWFEEGEETVTAFVEPFVILLILVANAIVGVWQERNAEKAIEALKEYESEHAKVLRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  133 DRKGVqrIRARDIVPGDIVEVAVGDKVPADLRLIEIKstTLRVDQSILTGESVSVTKHTEAIPDPRAVNQDKKNMLFSGT 212
Cdd:TIGR01116  81 GRWSV--IKAKDLVPGDIVELAVGDKVPADIRVLSLK--TLRVDQSILTGESVSVNKHTESVPDERAVNQDKKNMLFSGT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  213 NITSGKAVGVAVATGLHTELGKIRSQMAAVEPERTPLQRKLDEFGRQLSHAISVICVAVWVINIGHFADPAHGGSWLRGA 292
Cdd:TIGR01116 157 LVVAGKARGVVVRTGMSTEIGKIRDEMRAAEQEDTPLQKKLDEFGELLSKVIGLICILVWVINIGHFNDPALGGGWIQGA 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  293 VYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFVVaea 372
Cdd:TIGR01116 237 IYYFKIAVALAVAAIPEGLPAVITTCLALGTRKMAKKNAIVRKLPSVETLGCTTVICSDKTGTLTTNQMSVCKVVAL--- 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  373 DAGSCLLHEFTISGTTYTPEGEVRQGDQPVRCGQFDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKM 452
Cdd:TIGR01116 314 DPSSSSLNEFCVTGTTYAPEGGVIKDDGPVAGGQDAGLEELATIAALCNDSSLDFNERKGVYEKVGEATEAALKVLVEKM 393
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767992219  453 NVFDTDLQALSRVERAGACNTVIKQLMRKEFTLEFSRDRKSMSVYCTPTRphptgqGSKMFVKvGA 518
Cdd:TIGR01116 394 GLPATKNGVSSKRRPALGCNSVWNDKFKKLATLEFSRDRKSMSVLCKPST------GNKLFVK-GA 452
MgtA COG0474
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism];
1-518 1.28e-148

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


Pssm-ID: 440242 [Multi-domain]  Cd Length: 874  Bit Score: 448.40  E-value: 1.28e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   1 MEAAHLLPAADVLRHFSVTAEGgLSPAQVTGARERYGPNELPSEEGKSLWELVLEQFEDLLVRILLLAALVSFVLawfee 80
Cdd:COG0474    5 LKDWHALSAEEVLAELGTSEEG-LSSEEAARRLARYGPNELPEEKKRSLLRRFLEQFKNPLILILLAAAVISALL----- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  81 GEetttaFVEPLVIMLILVANAIVGVWQERNAESAIEALKEYEPEMGKVIRSDRkgVQRIRARDIVPGDIVEVAVGDKVP 160
Cdd:COG0474   79 GD-----WVDAIVILAVVLLNAIIGFVQEYRAEKALEALKKLLAPTARVLRDGK--WVEIPAEELVPGDIVLLEAGDRVP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 161 ADLRLIEIKSttLRVDQSILTGESVSVTKHTEAIPDPRAVnQDKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMA 240
Cdd:COG0474  152 ADLRLLEAKD--LQVDESALTGESVPVEKSADPLPEDAPL-GDRGNMVFMGTLVTSGRGTAVVVATGMNTEFGKIAKLLQ 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 241 AVEPERTPLQRKLDEFGRQLSHAISVICVAVWVINIghfadpAHGGSWLR----------GAVyyfkiavalavaaiPEG 310
Cdd:COG0474  229 EAEEEKTPLQKQLDRLGKLLAIIALVLAALVFLIGL------LRGGPLLEallfavalavAAI--------------PEG 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 311 LPAVITTCLALGTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFVvaeadagscllheftiSGTTYT 390
Cdd:COG0474  289 LPAVVTITLALGAQRMAKRNAIVRRLPAVETLGSVTVICTDKTGTLTQNKMTVERVYT----------------GGGTYE 352
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 391 PEGEVRqgdqpvrcgqfDGLVELATICALCNDSALDYNEAkgvyekVGEATETALTCLVEKMNVFDTDLQalsrveraga 470
Cdd:COG0474  353 VTGEFD-----------PALEELLRAAALCSDAQLEEETG------LGDPTEGALLVAAAKAGLDVEELR---------- 405
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 767992219 471 cntvikQLMRKEFTLEFSRDRKSMSVYCtptrpHPTGQGSKMFVKvGA 518
Cdd:COG0474  406 ------KEYPRVDEIPFDSERKRMSTVH-----EDPDGKRLLIVK-GA 441
E1-E2_ATPase pfam00122
E1-E2 ATPase;
121-329 1.32e-47

E1-E2 ATPase;


Pssm-ID: 425475 [Multi-domain]  Cd Length: 181  Bit Score: 163.51  E-value: 1.32e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  121 EYEPEMGKVIRSDrkGVQRIRARDIVPGDIVEVAVGDKVPADLRLIEiksTTLRVDQSILTGESVSVTKHteaipdprav 200
Cdd:pfam00122   1 SLLPPTATVLRDG--TEEEVPADELVPGDIVLLKPGERVPADGRIVE---GSASVDESLLTGESLPVEKK---------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  201 nqdKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMAAVEPERTPLQRKLDEFGRQLSHAISVICVAVWVINIghfa 280
Cdd:pfam00122  66 ---KGDMVYSGTVVVSGSAKAVVTATGEDTELGRIARLVEEAKSKKTPLQRLLDRLGKYFSPVVLLIALAVFLLWL---- 138
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 767992219  281 dpahggSWLRGAVYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMARK 329
Cdd:pfam00122 139 ------FVGGPPLRALLRALAVLVAACPCALPLATPLALAVGARRLAKK 181
PRK10517 PRK10517
magnesium-transporting P-type ATPase MgtA;
7-357 1.31e-43

magnesium-transporting P-type ATPase MgtA;


Pssm-ID: 236705 [Multi-domain]  Cd Length: 902  Bit Score: 166.01  E-value: 1.31e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   7 LPAADVLRHFSvTAEGGLSPAQVTGARERYGPNELPSEEG----KSLWELVLEQFeDLLVRILllaALVSFVLawfeegE 82
Cdd:PRK10517  52 MPEEELWKTFD-THPEGLNEAEVESAREQHGENELPAQKPlpwwVHLWVCYRNPF-NILLTIL---GAISYAT------E 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  83 ETTTAfvepLVIMLILVANAIVGVWQERNAESAIEALKEYEPEMGKVIRSD----RKGVQRIRARDIVPGDIVEVAVGDK 158
Cdd:PRK10517 121 DLFAA----GVIALMVAISTLLNFIQEARSTKAADALKAMVSNTATVLRVIndkgENGWLEIPIDQLVPGDIIKLAAGDM 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 159 VPADLRLIEIKSttLRVDQSILTGESVSVtkhtEAIPDPRAVNQ----DKKNMLFSGTNITSGKAVGVAVATGLHTELGK 234
Cdd:PRK10517 197 IPADLRILQARD--LFVAQASLTGESLPV----EKFATTRQPEHsnplECDTLCFMGTNVVSGTAQAVVIATGANTWFGQ 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 235 IRSQMAAVEPERTPLQRKLDEFGRQLSHAISVICVAVWVINighfadpahG---GSWLRGAVYyfkiAVALAVAAIPEGL 311
Cdd:PRK10517 271 LAGRVSEQDSEPNAFQQGISRVSWLLIRFMLVMAPVVLLIN---------GytkGDWWEAALF----ALSVAVGLTPEML 337
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 767992219 312 PAVITTCLALGTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLT 357
Cdd:PRK10517 338 PMIVTSTLARGAVKLSKQKVIVKRLDAIQNFGAMDILCTDKTGTLT 383
Cation_ATPase_N smart00831
Cation transporter/ATPase, N-terminus; This entry represents the conserved N-terminal region ...
5-75 1.69e-17

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


Pssm-ID: 214842 [Multi-domain]  Cd Length: 75  Bit Score: 76.85  E-value: 1.69e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767992219     5 HLLPAADVLRHFSVTAEGGLSPAQVTGARERYGPNELPSEEGKSLWELVLEQFEDLLVRILLLAALVSFVL 75
Cdd:smart00831   5 HALSLEEVLERLQTDLEKGLSSEEAARRLERYGPNELPPPKKTSPLLRFLRQFHNPLIYILLAAAVLSALL 75
 
Name Accession Description Interval E-value
P-type_ATPase_SERCA cd02083
sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; ...
5-518 0e+00

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: 1001.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   5 HLLPAADVLRHFSVTAEGGLSPAQVTGARERYGPNELPSEEGKSLWELVLEQFEDLLVRILLLAALVSFVLAWFEEGEET 84
Cdd:cd02083    1 HSKTVEEVLAYFGVDPTRGLSDEQVKRRREKYGPNELPAEEGKSLWELVLEQFDDLLVRILLLAAIISFVLALFEEGEEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  85 TTAFVEPLVIMLILVANAIVGVWQERNAESAIEALKEYEPEMGKVIRSDrKGVQRIRARDIVPGDIVEVAVGDKVPADLR 164
Cdd:cd02083   81 VTAFVEPFVILLILIANAVVGVWQERNAEKAIEALKEYEPEMAKVLRNG-KGVQRIRARELVPGDIVEVAVGDKVPADIR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 165 LIEIKSTTLRVDQSILTGESVSVTKHTEAIPDPRAVNQDKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMAAVEP 244
Cdd:cd02083  160 IIEIKSTTLRVDQSILTGESVSVIKHTDVVPDPRAVNQDKKNMLFSGTNVAAGKARGVVVGTGLNTEIGKIRDEMAETEE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 245 ERTPLQRKLDEFGRQLSHAISVICVAVWVINIGHFADPAHGGSWLRGAVYYFKIAVALAVAAIPEGLPAVITTCLALGTR 324
Cdd:cd02083  240 EKTPLQQKLDEFGEQLSKVISVICVAVWAINIGHFNDPAHGGSWIKGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTR 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 325 RMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFVVAEADAGsCLLHEFTISGTTYTPEGEVRQGDQPVRC 404
Cdd:cd02083  320 RMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVSRMFILDKVEDD-SSLNEFEVTGSTYAPEGEVFKNGKKVKA 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 405 GQFDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTDLQALSRVERAGACNTVIKQLMRKEFT 484
Cdd:cd02083  399 GQYDGLVELATICALCNDSSLDYNESKGVYEKVGEATETALTVLVEKMNVFNTDKSGLSKRERANACNDVIEQLWKKEFT 478
                        490       500       510
                 ....*....|....*....|....*....|....
gi 767992219 485 LEFSRDRKSMSVYCTPTRPhptGQGSKMFVKvGA 518
Cdd:cd02083  479 LEFSRDRKSMSVYCSPTKA---SGGNKLFVK-GA 508
ATPase-IIA1_Ca TIGR01116
sarco/endoplasmic reticulum calcium-translocating P-type ATPase; This model describes the ...
53-518 0e+00

sarco/endoplasmic reticulum calcium-translocating P-type ATPase; This model describes the P-type ATPase responsible for translocating calcium ions across the endoplasmic reticulum membrane of eukaryotes, and is of particular importance in the sarcoplasmic reticulum of skeletal and cardiac muscle in vertebrates. These pumps transfer Ca2+ from the cytoplasm to the lumen of the endoplasmic reticulum. In humans and mice, at least, there are multiple isoforms of the SERCA pump with overlapping but not redundant functions. Defects in SERCA isoforms are associated with diseases in humans. The calcium P-type ATPases have been characterized as Type IIA based on a phylogenetic analysis which distinguishes this group from the Type IIB PMCA calcium pump modelled by TIGR01517. A separate analysis divides Type IIA into sub-types, SERCA and PMR1, the latter of which is modelled by TIGR01522. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273452 [Multi-domain]  Cd Length: 917  Bit Score: 733.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   53 VLEQFEDLLVRILLLAALVSFVLAWFEEGEETTTAFVEPLVIMLILVANAIVGVWQERNAESAIEALKEYEPEMGKVIRS 132
Cdd:TIGR01116   1 VLEQFEDLLVRILLLAACVSFVLAWFEEGEETVTAFVEPFVILLILVANAIVGVWQERNAEKAIEALKEYESEHAKVLRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  133 DRKGVqrIRARDIVPGDIVEVAVGDKVPADLRLIEIKstTLRVDQSILTGESVSVTKHTEAIPDPRAVNQDKKNMLFSGT 212
Cdd:TIGR01116  81 GRWSV--IKAKDLVPGDIVELAVGDKVPADIRVLSLK--TLRVDQSILTGESVSVNKHTESVPDERAVNQDKKNMLFSGT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  213 NITSGKAVGVAVATGLHTELGKIRSQMAAVEPERTPLQRKLDEFGRQLSHAISVICVAVWVINIGHFADPAHGGSWLRGA 292
Cdd:TIGR01116 157 LVVAGKARGVVVRTGMSTEIGKIRDEMRAAEQEDTPLQKKLDEFGELLSKVIGLICILVWVINIGHFNDPALGGGWIQGA 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  293 VYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFVVaea 372
Cdd:TIGR01116 237 IYYFKIAVALAVAAIPEGLPAVITTCLALGTRKMAKKNAIVRKLPSVETLGCTTVICSDKTGTLTTNQMSVCKVVAL--- 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  373 DAGSCLLHEFTISGTTYTPEGEVRQGDQPVRCGQFDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKM 452
Cdd:TIGR01116 314 DPSSSSLNEFCVTGTTYAPEGGVIKDDGPVAGGQDAGLEELATIAALCNDSSLDFNERKGVYEKVGEATEAALKVLVEKM 393
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767992219  453 NVFDTDLQALSRVERAGACNTVIKQLMRKEFTLEFSRDRKSMSVYCTPTRphptgqGSKMFVKvGA 518
Cdd:TIGR01116 394 GLPATKNGVSSKRRPALGCNSVWNDKFKKLATLEFSRDRKSMSVLCKPST------GNKLFVK-GA 452
MgtA COG0474
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism];
1-518 1.28e-148

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


Pssm-ID: 440242 [Multi-domain]  Cd Length: 874  Bit Score: 448.40  E-value: 1.28e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   1 MEAAHLLPAADVLRHFSVTAEGgLSPAQVTGARERYGPNELPSEEGKSLWELVLEQFEDLLVRILLLAALVSFVLawfee 80
Cdd:COG0474    5 LKDWHALSAEEVLAELGTSEEG-LSSEEAARRLARYGPNELPEEKKRSLLRRFLEQFKNPLILILLAAAVISALL----- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  81 GEetttaFVEPLVIMLILVANAIVGVWQERNAESAIEALKEYEPEMGKVIRSDRkgVQRIRARDIVPGDIVEVAVGDKVP 160
Cdd:COG0474   79 GD-----WVDAIVILAVVLLNAIIGFVQEYRAEKALEALKKLLAPTARVLRDGK--WVEIPAEELVPGDIVLLEAGDRVP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 161 ADLRLIEIKSttLRVDQSILTGESVSVTKHTEAIPDPRAVnQDKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMA 240
Cdd:COG0474  152 ADLRLLEAKD--LQVDESALTGESVPVEKSADPLPEDAPL-GDRGNMVFMGTLVTSGRGTAVVVATGMNTEFGKIAKLLQ 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 241 AVEPERTPLQRKLDEFGRQLSHAISVICVAVWVINIghfadpAHGGSWLR----------GAVyyfkiavalavaaiPEG 310
Cdd:COG0474  229 EAEEEKTPLQKQLDRLGKLLAIIALVLAALVFLIGL------LRGGPLLEallfavalavAAI--------------PEG 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 311 LPAVITTCLALGTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFVvaeadagscllheftiSGTTYT 390
Cdd:COG0474  289 LPAVVTITLALGAQRMAKRNAIVRRLPAVETLGSVTVICTDKTGTLTQNKMTVERVYT----------------GGGTYE 352
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 391 PEGEVRqgdqpvrcgqfDGLVELATICALCNDSALDYNEAkgvyekVGEATETALTCLVEKMNVFDTDLQalsrveraga 470
Cdd:COG0474  353 VTGEFD-----------PALEELLRAAALCSDAQLEEETG------LGDPTEGALLVAAAKAGLDVEELR---------- 405
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 767992219 471 cntvikQLMRKEFTLEFSRDRKSMSVYCtptrpHPTGQGSKMFVKvGA 518
Cdd:COG0474  406 ------KEYPRVDEIPFDSERKRMSTVH-----EDPDGKRLLIVK-GA 441
P-type_ATPase_Ca_prok cd02089
prokaryotic P-type Ca(2+)-ATPase similar to Synechococcus elongatus sp. strain PCC 7942 PacL ...
23-369 3.17e-120

prokaryotic P-type Ca(2+)-ATPase similar to Synechococcus elongatus sp. strain PCC 7942 PacL and Listeria monocytogenes LMCA1; Ca(2+) transport ATPase is a plasma membrane protein which pumps Ca(2+) ion out of the cytoplasm. This prokaryotic subfamily includes the Ca(2+)-ATPase Synechococcus elongatus PacL, Listeria monocytogenes Ca(2+)-ATPase 1 (LMCA1) which has a low Ca(2+) affinity and a high pH optimum (pH about 9) and may remove Ca(2+) from the microorganism in environmental conditions when e.g. stressed by high Ca(2+) and alkaline pH, and the Bacillus subtilis putative P-type Ca(2+)-transport ATPase encoded by the yloB gene, which is expressed during sporulation. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319781 [Multi-domain]  Cd Length: 674  Bit Score: 368.86  E-value: 3.17e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  23 GLSPAQVTGARERYGPNELPSEEGKSLWELVLEQFEDLLVRILLLAALVSFVLawfeeGEEtttafVEPLVIMLILVANA 102
Cdd:cd02089    1 GLSEEEAERRLAKYGPNELVEKKKRSPWKKFLEQFKDFMVIVLLAAAVISGVL-----GEY-----VDAIVIIAIVILNA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 103 IVGVWQERNAESAIEALKEYEPEMGKVIRSDRKgvQRIRARDIVPGDIVEVAVGDKVPADLRLIEikSTTLRVDQSILTG 182
Cdd:cd02089   71 VLGFVQEYKAEKALAALKKMSAPTAKVLRDGKK--QEIPARELVPGDIVLLEAGDYVPADGRLIE--SASLRVEESSLTG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 183 ESVSVTKHTEAIPDPRAVNQDKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMAAVEPERTPLQRKLDEFGRQLSH 262
Cdd:cd02089  147 ESEPVEKDADTLLEEDVPLGDRKNMVFSGTLVTYGRGRAVVTATGMNTEMGKIATLLEETEEEKTPLQKRLDQLGKRLAI 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 263 AISVICVAVWVINIGHFADPAhgGSWLRG---AVyyfkiavalavAAIPEGLPAVITTCLALGTRRMARKNAIVRSLPSV 339
Cdd:cd02089  227 AALIICALVFALGLLRGEDLL--DMLLTAvslAV-----------AAIPEGLPAIVTIVLALGVQRMAKRNAIIRKLPAV 293
                        330       340       350
                 ....*....|....*....|....*....|
gi 767992219 340 ETLGCTSVICSDKTGTLTTNQMSVCRMFVV 369
Cdd:cd02089  294 ETLGSVSVICSDKTGTLTQNKMTVEKIYTI 323
P-type_ATPase_cation cd02080
P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, ...
23-515 3.10e-115

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: 360.04  E-value: 3.10e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  23 GLSPAQVTGARERYGPNELPSEEGKSLWELVLEQFEDLLVRILLLAALVSFVLawfeeGEETTTAfveplVIMLILVANA 102
Cdd:cd02080    1 GLTSEEAAERLERYGPNRLPEKKTKSPLLRFLRQFNNPLIYILLAAAVVTAFL-----GHWVDAI-----VIFGVVLINA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 103 IVGVWQERNAESAIEALKEYEPEMGKVIRSDRKgvQRIRARDIVPGDIVEVAVGDKVPADLRLIEIKSttLRVDQSILTG 182
Cdd:cd02080   71 IIGYIQEGKAEKALAAIKNMLSPEATVLRDGKK--LTIDAEELVPGDIVLLEAGDKVPADLRLIEARN--LQIDESALTG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 183 ESVSVTKHTEAIPdPRAVNQDKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMAAVEPERTPLQRKLDEFGRQLSH 262
Cdd:cd02080  147 ESVPVEKQEGPLE-EDTPLGDRKNMAYSGTLVTAGSATGVVVATGADTEIGRINQLLAEVEQLATPLTRQIAKFSKALLI 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 263 AISVICVAVWVInighfadpahgGSWLRG--AVYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMARKNAIVRSLPSVE 340
Cdd:cd02080  226 VILVLAALTFVF-----------GLLRGDysLVELFMAVVALAVAAIPEGLPAVITITLAIGVQRMAKRNAIIRRLPAVE 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 341 TLGCTSVICSDKTGTLTTNQMSVCRMFvvaeadagscllheftisgttytpegevrqgdqpvrcgqfdglvelaticALC 420
Cdd:cd02080  295 TLGSVTVICSDKTGTLTRNEMTVQAIV--------------------------------------------------TLC 324
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 421 NDSALDYNEakGVYEKVGEATETALTCLVEKMNVFDTDLqaLSRVERAGacntvikqlmrkefTLEFSRDRKSMSvyctp 500
Cdd:cd02080  325 NDAQLHQED--GHWKITGDPTEGALLVLAAKAGLDPDRL--ASSYPRVD--------------KIPFDSAYRYMA----- 381
                        490
                 ....*....|....*
gi 767992219 501 TRpHPTGQGSKMFVK 515
Cdd:cd02080  382 TL-HRDDGQRVIYVK 395
ATPase-IIA2_Ca TIGR01522
golgi membrane calcium-translocating P-type ATPase; This model describes the P-type ATPase ...
7-515 4.71e-85

golgi membrane calcium-translocating P-type ATPase; This model describes the P-type ATPase responsible for translocating calcium ions across the golgi membrane of fungi and animals, and is of particular importance in the sarcoplasmic reticulum of skeletal and cardiac muscle in vertebrates. The calcium P-type ATPases have been characterized as Type IIA based on a phylogenetic analysis which distinguishes this group from the Type IIB PMCA calcium pump modelled by TIGR01517. A separate analysis divides Type IIA into sub-types, SERCA and PMR1, the former of which is modelled by TIGR01116.


Pssm-ID: 130585 [Multi-domain]  Cd Length: 884  Bit Score: 281.72  E-value: 4.71e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219    7 LPAADVLRHFSVTAEGGLSPAQ-VTGARERYGPNELPSEEGKSLWELVLEQF-EDLLVRILLLAALVSFVLAWFEEGEET 84
Cdd:TIGR01522   7 LSVEETCSKLQTDLQNGLNSSQeASHRRAFHGWNEFDVEEDESLWKKFLSQFvKNPLILLLIASAVISVFMGNIDDAVSI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   85 TTAfveplviMLILVAnaiVGVWQERNAESAIEALKEYEPEMGKVIRSDRKgvQRIRARDIVPGDIVEVAVGDKVPADLR 164
Cdd:TIGR01522  87 TLA-------ILIVVT---VGFVQEYRSEKSLEALNKLVPPECHLIREGKL--EHVLASTLVPGDLVCLSVGDRVPADLR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  165 LIEikSTTLRVDQSILTGESVSVTKHTEAIPDPRAVN-QDKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMAAVE 243
Cdd:TIGR01522 155 IVE--AVDLSIDESNLTGETTPVSKVTAPIPAATNGDlAERSNIAFMGTLVRCGHGKGIVVGTGSNTEFGAVFKMMQAIE 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  244 PERTPLQRKLDEFGRQLShAISVICVAVWVInIGHFadpaHGGSWLRgavyYFKIAVALAVAAIPEGLPAVITTCLALGT 323
Cdd:TIGR01522 233 KPKTPLQKSMDLLGKQLS-LVSFGVIGVICL-VGWF----QGKDWLE----MFTISVSLAVAAIPEGLPIIVTVTLALGV 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  324 RRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFVVaeaDAGSCLLheftiSGTTYTPEGEVRQGDQPVR 403
Cdd:TIGR01522 303 LRMSKKRAIVRKLPSVETLGSVNVICSDKTGTLTKNHMTVTKIWTS---DGLHTML-----NAVSLNQFGEVIVDGDVLH 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  404 CGQFDGLVELATICALCNDSALDyNEAKGVyekVGEATETALTCLVEKMNVFDTDlQALSRVERagacntvikqlmrkef 483
Cdd:TIGR01522 375 GFYTVAVSRILEAGNLCNNAKFR-NEADTL---LGNPTDVALIELLMKFGLDDLR-ETYIRVAE---------------- 433
                         490       500       510
                  ....*....|....*....|....*....|..
gi 767992219  484 tLEFSRDRKSMSVYCTptrpHPTGQGSKMFVK 515
Cdd:TIGR01522 434 -VPFSSERKWMAVKCV----HRQDRSEMCFMK 460
P-type_ATPase_SPCA cd02085
golgi-associated secretory pathway Ca(2+) transport ATPases, similar to human ATPase secretory ...
33-518 2.98e-81

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: 270.04  E-value: 2.98e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  33 RERYGPNELPSEEGKSLWELVLEQFEDLLVRILLLAALVSFVLAWFEEGEETTTAfveplviMLILVANAIVgvwQERNA 112
Cdd:cd02085    2 RKLHGPNEFKVEDEEPLWKKYLEQFKNPLILLLLGSAVVSVVMKQYDDAVSITVA-------ILIVVTVAFV---QEYRS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 113 ESAIEALKEYEPEMGKVIRSDRkgVQRIRARDIVPGDIVEVAVGDKVPADLRLIEikSTTLRVDQSILTGESVSVTKHTE 192
Cdd:cd02085   72 EKSLEALNKLVPPECHCLRDGK--LEHFLARELVPGDLVCLSIGDRIPADLRLFE--ATDLSIDESSLTGETEPCSKTTE 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 193 AIPDPRAVN-QDKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMAAVEPERTPLQRKLDEFGRQLShAISVICVAV 271
Cdd:cd02085  148 VIPKASNGDlTTRSNIAFMGTLVRCGHGKGIVIGTGENSEFGEVFKMMQAEEAPKTPLQKSMDKLGKQLS-LYSFIIIGV 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 272 WVInIGHFadpaHGGSWLRgavyYFKIAVALAVAAIPEGLPAVITTCLALGTRRMARKNAIVRSLPSVETLGCTSVICSD 351
Cdd:cd02085  227 IML-IGWL----QGKNLLE----MFTIGVSLAVAAIPEGLPIVVTVTLALGVMRMAKRRAIVKKLPIVETLGCVNVICSD 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 352 KTGTLTTNQMSVCRMFvvaeadagscllheftisgttytpegevrqgdqpvrCGqfdglvelaticALCNDSALDYNEAk 431
Cdd:cd02085  298 KTGTLTKNEMTVTKIV------------------------------------TG------------CVCNNAVIRNNTL- 328
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 432 gvyekVGEATETALTCLVEKMNVFDTDlqalsrveragacNTVIkqlmRKEFtLEFSRDRKSMSVYCtptRPHPTGQGSK 511
Cdd:cd02085  329 -----MGQPTEGALIALAMKMGLSDIR-------------ETYI----RKQE-IPFSSEQKWMAVKC---IPKYNSDNEE 382

                 ....*..
gi 767992219 512 MFVKVGA 518
Cdd:cd02085  383 IYFMKGA 389
ATPase_P-type TIGR01494
ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large ...
93-515 7.42e-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: 254.93  E-value: 7.42e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   93 VIMLILVANAIVGVWQERNAESAIEALKEYEpEMGKVIRSDRKGVQRIRARDIVPGDIVEVAVGDKVPADLRLIeikSTT 172
Cdd:TIGR01494   1 FILFLVLLFVLLEVKQKLKAEDALRSLKDSL-VNTATVLVLRNGWKEISSKDLVPGDVVLVKSGDTVPADGVLL---SGS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  173 LRVDQSILTGESVSVTKHTEaipdpravnqDKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMAAVEPERTPLQRK 252
Cdd:TIGR01494  77 AFVDESSLTGESLPVLKTAL----------PDGDAVFAGTINFGGTLIVKVTATGILTTVGKIAVVVYTGFSTKTPLQSK 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  253 LDEFGRQL-SHAISVICVAVWVINIGHFADPAHGGSWLRGAVYYFKIAValavaaiPEGLPAVITTCLALGTRRMARKNA 331
Cdd:TIGR01494 147 ADKFENFIfILFLLLLALAVFLLLPIGGWDGNSIYKAILRALAVLVIAI-------PCALPLAVSVALAVGDARMAKKGI 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  332 IVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFVvaeadagscllheftisgttytpegevrqgdqpvrcgqfDGLV 411
Cdd:TIGR01494 220 LVKNLNALEELGKVDVICFDKTGTLTTNKMTLQKVII---------------------------------------IGGV 260
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  412 ELATIcalcndsaLDYNEAKGVYEKVGEATETALTCLVEKMNVFDtdlqalsrveragacntVIKQLMRKEFTLEFSRDR 491
Cdd:TIGR01494 261 EEASL--------ALALLAASLEYLSGHPLERAIVKSAEGVIKSD-----------------EINVEYKILDVFPFSSVL 315
                         410       420
                  ....*....|....*....|....
gi 767992219  492 KSMSVYCtptrpHPTGQGSKMFVK 515
Cdd:TIGR01494 316 KRMGVIV-----EGANGSDLLFVK 334
P-type_ATPase_Ca_PMCA-like cd02081
animal plasma membrane Ca2(+)-ATPases (PMCA), similar to human ATP2B1-4/PMCA1-4, and related ...
33-368 6.18e-71

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: 240.57  E-value: 6.18e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  33 RERYGPNELPSEEGKSLWELVLEQFEDLLVRILLLAALVSFVLAWFEE--GEETTTAFVEPLVIMLILVANAIVGVWQER 110
Cdd:cd02081    5 REVYGKNEIPPKPPKSFLQLVWEALQDPTLIILLIAAIVSLGLGFYTPfgEGEGKTGWIEGVAILVAVILVVLVTAGNDY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 111 NAESAIEAL-KEYEPEMGKVIRSDRkgVQRIRARDIVPGDIVEVAVGDKVPADLRLIEikSTTLRVDQSILTGESVSVTK 189
Cdd:cd02081   85 QKEKQFRKLnSKKEDQKVTVIRDGE--VIQISVFDIVVGDIVQLKYGDLIPADGLLIE--GNDLKIDESSLTGESDPIKK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 190 HTEaipdpravNQDKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMAAVEPERTPLQRKLDEFGRQLSHAISVICV 269
Cdd:cd02081  161 TPD--------NQIPDPFLLSGTKVLEGSGKMLVTAVGVNSQTGKIMTLLRAENEEKTPLQEKLTKLAVQIGKVGLIVAA 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 270 AVWVINIGHFA-DPAHGGSWLRGAVY------YFKIAVALAVAAIPEGLPAVITTCLALGTRRMARKNAIVRSLPSVETL 342
Cdd:cd02081  233 LTFIVLIIRFIiDGFVNDGKSFSAEDlqefvnFFIIAVTIIVVAVPEGLPLAVTLSLAYSVKKMMKDNNLVRHLDACETM 312
                        330       340
                 ....*....|....*....|....*.
gi 767992219 343 GCTSVICSDKTGTLTTNQMSVCRMFV 368
Cdd:cd02081  313 GNATAICSDKTGTLTQNRMTVVQGYI 338
P-type_ATPase_Na_ENA cd02086
fungal-type Na(+)-ATPase, similar to the plasma membrane sodium transporters Saccharomyces ...
23-496 1.90e-70

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: 242.75  E-value: 1.90e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  23 GLSPAQVTGARERYGPNELPSEEGKSLWELVLEQFEDLLVRILLLAALVSF-VLAWFEEGeetttafveplVIMLILVAN 101
Cdd:cd02086    1 GLTNDEAERRLKEYGENELEGDTGVSAWKILLRQVANAMTLVLIIAMALSFaVKDWIEGG-----------VIAAVIALN 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 102 AIVGVWQERNAESAIEALKEYEPEMGKVIRSDRkgVQRIRARDIVPGDIVEVAVGDKVPADLRLIEIKSttLRVDQSILT 181
Cdd:cd02086   70 VIVGFIQEYKAEKTMDSLRNLSSPNAHVIRSGK--TETISSKDVVPGDIVLLKVGDTVPADLRLIETKN--FETDEALLT 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 182 GESVSVTKHTEAI--PDPRAVNQDKKNMLFSGTNITSGKAVGVAVATGLHTELGKI----RSQMAAVEPER--------- 246
Cdd:cd02086  146 GESLPVIKDAELVfgKEEDVSVGDRLNLAYSSSTVTKGRAKGIVVATGMNTEIGKIakalRGKGGLISRDRvkswlygtl 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 247 ----------------TPLQRKLDEFGRQLsHAISVIC-VAVWVINIGHFADpahggswlRGAVYyfkiAVALAVAAIPE 309
Cdd:cd02086  226 ivtwdavgrflgtnvgTPLQRKLSKLAYLL-FFIAVILaIIVFAVNKFDVDN--------EVIIY----AIALAISMIPE 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 310 GLPAVITTCLALGTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSvcrmfvvaeadagscllheftisgtty 389
Cdd:cd02086  293 SLVAVLTITMAVGAKRMVKRNVIVRKLDALEALGAVTDICSDKTGTLTQGKMV--------------------------- 345
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 390 tpegeVRQGDQPvrcgqfdglvelatiCALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMnvfdtDLQALSRVERAG 469
Cdd:cd02086  346 -----VRQVWIP---------------AALCNIATVFKDEETDCWKAHGDPTEIALQVFATKF-----DMGKNALTKGGS 400
                        490       500
                 ....*....|....*....|....*..
gi 767992219 470 ACNTVIkqlmrKEFTleFSRDRKSMSV 496
Cdd:cd02086  401 AQFQHV-----AEFP--FDSTVKRMSV 420
P-type_ATPase cd07539
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ...
35-371 4.20e-67

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: 228.45  E-value: 4.20e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  35 RYGPNELPSEEGKSLWELVLEQFEDLLVRILLLAALVSFVlawfeegeetTTAFVEPLVIMLILVANAIVGVWQERNAES 114
Cdd:cd07539   14 LPARNLALETATRSGILAVAAQLELPPVALLGLAAGASAS----------TGGGVDAVLIVGVLTVNAVIGGVQRLRAER 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 115 AIEALKEYEPEMGKVIRSDRKGVQRIRARDIVPGDIVEVAVGDKVPADLRLIEikSTTLRVDQSILTGESVSVTKHTEAI 194
Cdd:cd07539   84 ALAALLAQQQQPARVVRAPAGRTQTVPAESLVPGDVIELRAGEVVPADARLLE--ADDLEVDESALTGESLPVDKQVAPT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 195 PdpRAVNQDKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMAAVEPErTPLQRKLDEFGRQLSHAISVICVAVWvi 274
Cdd:cd07539  162 P--GAPLADRACMLYEGTTVVSGQGRAVVVATGPHTEAGRAQSLVAPVETA-TGVQAQLRELTSQLLPLSLGGGAAVT-- 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 275 nighfadpahGGSWLRGA--VYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMARKNAIVRSLPSVETLGCTSVICSDK 352
Cdd:cd07539  237 ----------GLGLLRGAplRQAVADGVSLAVAAVPEGLPLVATLAQLAAARRLSRRGVLVRSPRTVEALGRVDTICFDK 306
                        330
                 ....*....|....*....
gi 767992219 353 TGTLTTNQMSVCRMFVVAE 371
Cdd:cd07539  307 TGTLTENRLRVVQVRPPLA 325
P-type_ATPase cd07538
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ...
23-368 1.82e-63

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


Pssm-ID: 319839 [Multi-domain]  Cd Length: 653  Bit Score: 219.24  E-value: 1.82e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  23 GLSPAQVTGARERYGPNELPSEEGKSLWELVLEQFEDLLVRILLLAALVSFVLAWFEEGeetttafveplVIMLILVANA 102
Cdd:cd07538    1 GLTEAEARRRLESGGKNELPQPKKRTLLASILDVLREPMFLLLLAAALIYFVLGDPREG-----------LILLIFVVVI 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 103 IV-GVWQERNAESAIEALKEYEPEMGKVIRSDRKgvQRIRARDIVPGDIVEVAVGDKVPADLRLIEikSTTLRVDQSILT 181
Cdd:cd07538   70 IAiEVVQEWRTERALEALKNLSSPRATVIRDGRE--RRIPSRELVPGDLLILGEGERIPADGRLLE--NDDLGVDESTLT 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 182 GESVSVTKhTEAIPDPRAVNQDKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMAAVEPERTPLQRKLDEFGRQLS 261
Cdd:cd07538  146 GESVPVWK-RIDGKAMSAPGGWDKNFCYAGTLVVRGRGVAKVEATGSRTELGKIGKSLAEMDDEPTPLQKQTGRLVKLCA 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 262 HAISVIC---VAVWVINIGHFADPAHGGSWLRGAVyyfkiavalavaaIPEGLPAVITTCLALGTRRMARKNAIVRSLPS 338
Cdd:cd07538  225 LAALVFCaliVAVYGVTRGDWIQAILAGITLAMAM-------------IPEEFPVILTVFMAMGAWRLAKKNVLVRRAAA 291
                        330       340       350
                 ....*....|....*....|....*....|
gi 767992219 339 VETLGCTSVICSDKTGTLTTNQMSVCRMFV 368
Cdd:cd07538  292 VETLGSITVLCVDKTGTLTKNQMEVVELTS 321
P-type_ATPase_H cd02076
plant and fungal plasma membrane H(+)-ATPases, and related bacterial and archaeal putative H(+) ...
23-380 7.86e-62

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: 217.10  E-value: 7.86e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  23 GLSPAQVTGARERYGPNELPSEEgKSLWELVLEQFEDLLVRILLLAALVSFVLA-WfeegeetttafVEPLVIMLILVAN 101
Cdd:cd02076    1 GLTSEEAAKRLKEYGPNELPEKK-ENPILKFLSFFWGPIPWMLEAAAILAAALGdW-----------VDFAIILLLLLIN 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 102 AIVGVWQERNAESAIEALKEYEPEMGKVIRSDRkgVQRIRARDIVPGDIVEVAVGDKVPADLRLIEIKstTLRVDQSILT 181
Cdd:cd02076   69 AGIGFIEERQAGNAVAALKKSLAPKARVLRDGQ--WQEIDAKELVPGDIVSLKIGDIVPADARLLTGD--ALQVDQSALT 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 182 GESVSVTKHTEAipdpravnqdkknMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMAAVEPeRTPLQRKLDEFGRQLS 261
Cdd:cd02076  145 GESLPVTKHPGD-------------EAYSGSIVKQGEMLAVVTATGSNTFFGKTAALVASAEE-QGHLQKVLNKIGNFLI 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 262 HAISVICVAVWVINIGHFADPAHGgswLRGAVYYFkiavalaVAAIPEGLPAVITTCLALGTRRMARKNAIVRSLPSVET 341
Cdd:cd02076  211 LLALILVLIIVIVALYRHDPFLEI---LQFVLVLL-------IASIPVAMPAVLTVTMAVGALELAKKKAIVSRLSAIEE 280
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 767992219 342 LGCTSVICSDKTGTLTTNQMSVCRMFVVAEADAGSCLLH 380
Cdd:cd02076  281 LAGVDILCSDKTGTLTLNKLSLDEPYSLEGDGKDELLLL 319
P-type_ATPase_Mg cd02077
magnesium transporting ATPase (MgtA), similar to Escherichia coli MgtA and Salmonella ...
23-361 9.74e-61

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: 213.65  E-value: 9.74e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  23 GLSPAQVTGARERYGPNELPSEEGKSLWELVLEQFEDLLVRILLLAALVSFVLAWFEEGEETTtaFVEPLVIMLILVANA 102
Cdd:cd02077    1 GLTNEEAEERLEKYGPNEISHEKFPSWFKLLLKAFINPFNIVLLVLALVSFFTDVLLAPGEFD--LVGALIILLMVLISG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 103 IVGVWQERNAESAIEALKEYEPEMGKVIRsDRKGVQRIRARDIVPGDIVEVAVGDKVPADLRLIEikSTTLRVDQSILTG 182
Cdd:cd02077   79 LLDFIQEIRSLKAAEKLKKMVKNTATVIR-DGSKYMEIPIDELVPGDIVYLSAGDMIPADVRIIQ--SKDLFVSQSSLTG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 183 ESVSVTKHTEAIPDPRAVNQDKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMAAVEPErTPLQRKLDEFGRQLSH 262
Cdd:cd02077  156 ESEPVEKHATAKKTKDESILELENICFMGTNVVSGSALAVVIATGNDTYFGSIAKSITEKRPE-TSFDKGINKVSKLLIR 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 263 AISVICVAVWVINIghfadpAHGGSWLRGAVYyfkiAVALAVAAIPEGLPAVITTCLALGTRRMARKNAIVRSLPSVETL 342
Cdd:cd02077  235 FMLVMVPVVFLING------LTKGDWLEALLF----ALAVAVGLTPEMLPMIVTSNLAKGAVRMSKRKVIVKNLNAIQNF 304
                        330
                 ....*....|....*....
gi 767992219 343 GCTSVICSDKTGTLTTNQM 361
Cdd:cd02077  305 GAMDILCTDKTGTLTQDKI 323
ATPase-IIIA_H TIGR01647
plasma-membrane proton-efflux P-type ATPase; This model describes the plasma membrane proton ...
23-380 1.30e-59

plasma-membrane proton-efflux P-type ATPase; This model describes the plasma membrane proton efflux P-type ATPase found in plants, fungi, protozoa, slime molds and archaea. The best studied representative is from yeast.


Pssm-ID: 273731 [Multi-domain]  Cd Length: 754  Bit Score: 210.26  E-value: 1.30e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   23 GLSPAQVTGARERYGPNELPsEEGKSLWELVLEQFEDLLVRILLLAALVSFVLAWFEEGeetttafvepLVIMLILVANA 102
Cdd:TIGR01647   1 GLTSAEAKKRLAKYGPNELP-EKKVSPLLKFLGFFWNPLSWVMEAAAIIAIALENWVDF----------VIILGLLLLNA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  103 IVGVWQERNAESAIEALKEYEPEMGKVIRsDRKGVQrIRARDIVPGDIVEVAVGDKVPADLRLIEikSTTLRVDQSILTG 182
Cdd:TIGR01647  70 TIGFIEENKAGNAVEALKQSLAPKARVLR-DGKWQE-IPASELVPGDVVRLKIGDIVPADCRLFE--GDYIQVDQAALTG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  183 ESVSVTKHTEAIPdpravnqdkknmlFSGTNITSGKAVGVAVATGLHTELGKIRSQMAAVEPERTPLQRKLDEFGRQLSH 262
Cdd:TIGR01647 146 ESLPVTKKTGDIA-------------YSGSTVKQGEAEAVVTATGMNTFFGKAAALVQSTETGSGHLQKILSKIGLFLIV 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  263 AISVICVAVWVINIGHFadpahGGSWLRGAVYyfkiAVALAVAAIPEGLPAVITTCLALGTRRMARKNAIVRSLPSVETL 342
Cdd:TIGR01647 213 LIGVLVLIELVVLFFGR-----GESFREGLQF----ALVLLVGGIPIAMPAVLSVTMAVGAAELAKKKAIVTRLTAIEEL 283
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 767992219  343 GCTSVICSDKTGTLTTNQMSVCR-MFVVAEADAGSCLLH 380
Cdd:TIGR01647 284 AGMDILCSDKTGTLTLNKLSIDEiLPFFNGFDKDDVLLY 322
ATPase-IIB_Ca TIGR01517
plasma-membrane calcium-translocating P-type ATPase; This model describes the P-type ATPase ...
24-526 1.05e-58

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: 210.02  E-value: 1.05e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   24 LSPAQVTGARERYGPNELPSEEGKSLWELVLEQFEDLLVRILLLAALVSFVLAWF-----EEGEETTTAFVEPLVIML-I 97
Cdd:TIGR01517  62 LSSSTLERREKVYGKNELPEKPPKSFLQIVWAALSDQTLILLSVAAVVSLVLGLYvpsvgEDKADTETGWIEGVAILVsV 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   98 LVANAIVGVWQERNAESAIEALKEYEPEMGKVIRSDRkgVQRIRARDIVPGDIVEVAVGDKVPADLrlIEIKSTTLRVDQ 177
Cdd:TIGR01517 142 ILVVLVTAVNDYKKELQFRQLNREKSAQKIAVIRGGQ--EQQISIHDIVVGDIVSLSTGDVVPADG--VFISGLSLEIDE 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  178 SILTGESvsvtkhteaipDPRAVNQDKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMAAVEPERTPLQRKLDEFG 257
Cdd:TIGR01517 218 SSITGES-----------DPIKKGPVQDPFLLSGTVVNEGSGRMLVTAVGVNSFGGKLMMELRQAGEEETPLQEKLSELA 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  258 RQLSHA---ISVICVAV----WVINI----GHFADPAHGGSWLrgaVYYFKIAVALAVAAIPEGLPAVITTCLALGTRRM 326
Cdd:TIGR01517 287 GLIGKFgmgSAVLLFLVlslrYVFRIirgdGRFEDTEEDAQTF---LDHFIIAVTIVVVAVPEGLPLAVTIALAYSMKKM 363
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  327 ARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFvvaeadagscllheftISGTTYTPEGEVRQGDQPvrcgq 406
Cdd:TIGR01517 364 MKDNNLVRHLAACETMGSATAICSDKTGTLTQNVMSVVQGY----------------IGEQRFNVRDEIVLRNLP----- 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  407 fDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTDLQALSRVERagacntVIKqlmrkefTLE 486
Cdd:TIGR01517 423 -AAVRNILVEGISLNSSSEEVVDRGGKRAFIGSKTECALLDFGLLLLLQSRDVQEVRAEEK------VVK-------IYP 488
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 767992219  487 FSRDRKSMSVYCTptrpHPtgQGSKMFVKVGACLAGLGPC 526
Cdd:TIGR01517 489 FNSERKFMSVVVK----HS--GGKYREFRKGASEIVLKPC 522
ATPase-IIC_X-K TIGR01106
sodium or proton efflux -- potassium uptake antiporter, P-type ATPase, alpha subunit; This ...
5-450 8.41e-57

sodium or proton efflux -- potassium uptake antiporter, P-type ATPase, alpha subunit; This model describes the P-type ATPases responsible for the exchange of either protons or sodium ions for potassium ions across the plasma membranes of eukaryotes. Unlike most other P-type ATPases, members of this subfamily require a beta subunit for activity. This model encompasses eukaryotes and consists of two functional types, a Na/K antiporter found widely distributed in eukaryotes and a H/K antiporter found only in vertebrates. The Na+ or H+/K+ antiporter P-type ATPases have been characterized as Type IIC based on a published phylogenetic analysis. Sequences from Blastocladiella emersonii (GP|6636502, GP|6636502 and PIR|T43025), C. elegans (GP|2315419, GP|6671808 and PIR|T31763) and Drosophila melanogaster (GP|7291424) score below trusted cutoff, apparently due to long branch length (excessive divergence from the last common ancestor) as evidenced by a phylogenetic tree. Experimental evidence is needed to determine whether these sequences represent ATPases with conserved function. Aside from fragments, other sequences between trusted and noise appear to be bacterial ATPases of unclear lineage, but most likely calcium pumps. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 273445 [Multi-domain]  Cd Length: 997  Bit Score: 205.03  E-value: 8.41e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219    5 HLLPAADVLRHFSVTAEGGLSPAQVTGARERYGPNELPSEEGKSLWELVLEQFEDLLVRILLLAALVSFVLAWFEEGEET 84
Cdd:TIGR01106  18 HKLSLDELERKYGTDLSKGLSAARAAEILARDGPNALTPPPTTPEWVKFCRQLFGGFSMLLWIGAILCFLAYGIQASTEE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   85 TTAFVE---PLVIMLILVANAIVGVWQERNAESAIEALKEYEPEMGKVIRSDRKgvQRIRARDIVPGDIVEVAVGDKVPA 161
Cdd:TIGR01106  98 EPQNDNlylGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRDGEK--MSINAEQVVVGDLVEVKGGDRIPA 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  162 DLRLIEIKSttLRVDQSILTGESVsvtkhteaiPDPRAVN------QDKKNMLFSGTNITSGKAVGVAVATGLHTELGKI 235
Cdd:TIGR01106 176 DLRIISAQG--CKVDNSSLTGESE---------PQTRSPEfthenpLETRNIAFFSTNCVEGTARGIVVNTGDRTVMGRI 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  236 RSQMAAVEPERTPLQRKLDEFGRQLSHAISVICVAVWVINIghfadpAHGGSWLRGAVYYFkiavALAVAAIPEGLPAVI 315
Cdd:TIGR01106 245 ASLASGLENGKTPIAIEIEHFIHIITGVAVFLGVSFFILSL------ILGYTWLEAVIFLI----GIIVANVPEGLLATV 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  316 TTCLALGTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFV---VAEADAGScllhefTISGTTYtpe 392
Cdd:TIGR01106 315 TVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFdnqIHEADTTE------DQSGVSF--- 385
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767992219  393 gevrqgDQPVRcgqfdGLVELATICALCNDSALDYN-EAKGVYEK--VGEATETALTCLVE 450
Cdd:TIGR01106 386 ------DKSSA-----TWLALSRIAGLCNRAVFKAGqENVPILKRavAGDASESALLKCIE 435
P-type_ATPase_Na-K_like cd02608
alpha-subunit of Na(+)/K(+)-ATPases and of gastric H(+)/K(+)-ATPase, similar to the human Na(+) ...
23-450 3.68e-56

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: 202.58  E-value: 3.68e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  23 GLSPAQVTGARERYGPNELPSEEGKSLWELVLEQFEDLLVRILLLAALVSFVLAWFEEGEETttafvEP--------LVI 94
Cdd:cd02608    1 GLTSARAAEILARDGPNALTPPPTTPEWVKFCKQLFGGFSMLLWIGAILCFLAYGIQAATEE-----EPsndnlylgIVL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  95 MLILVANAIVGVWQERNAESAIEALKEYEPEMGKVIRSDRKgvQRIRARDIVPGDIVEVAVGDKVPADLRLIEIKSttLR 174
Cdd:cd02608   76 AAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVIRDGEK--MQINAEELVVGDLVEVKGGDRIPADIRIISAHG--CK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 175 VDQSILTGESVSVTKHTEAIPDpravNQ-DKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMAAVEPERTPLQRKL 253
Cdd:cd02608  152 VDNSSLTGESEPQTRSPEFTHE----NPlETKNIAFFSTNCVEGTARGIVINTGDRTVMGRIATLASGLEVGKTPIAREI 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 254 DEFgrqlSHAISVicVAVWvINIGHFA-DPAHGGSWLRGAVYYFkiavALAVAAIPEGLPAVITTCLALGTRRMARKNAI 332
Cdd:cd02608  228 EHF----IHIITG--VAVF-LGVSFFIlSLILGYTWLEAVIFLI----GIIVANVPEGLLATVTVCLTLTAKRMARKNCL 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 333 VRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFV---VAEADAGScllhefTISGTTYTPEGevrqgdqpvrcgqfDG 409
Cdd:cd02608  297 VKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFdnqIHEADTTE------DQSGASFDKSS--------------AT 356
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 767992219 410 LVELATICALCNDSALDYNEAKGVYEK---VGEATETALTCLVE 450
Cdd:cd02608  357 WLALSRIAGLCNRAEFKAGQENVPILKrdvNGDASESALLKCIE 400
ATPase-IID_K-Na TIGR01523
potassium and/or sodium efflux P-type ATPase, fungal-type; Initially described as a calcium ...
10-453 3.28e-52

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: 191.76  E-value: 3.28e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219    10 ADVLRHFSVTA-EGGLSPAQVTGARERYGPNELPSEEGKSLWELVLEQFEDLLVRILLLAALVSFvlawfeegeeTTTAF 88
Cdd:TIGR01523   12 ADEAAEFIGTSiPEGLTHDEAQHRLKEVGENRLEADSGIDAKAMLLHQVCNAMCMVLIIAAAISF----------AMHDW 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219    89 VEPLVIMLILVANAIVGVWQERNAESAIEALKEYEPEMGKVIRSDRKgvQRIRARDIVPGDIVEVAVGDKVPADLRLIEI 168
Cdd:TIGR01523   82 IEGGVISAIIALNILIGFIQEYKAEKTMDSLKNLASPMAHVIRNGKS--DAIDSHDLVPGDICLLKTGDTIPADLRLIET 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   169 KSttLRVDQSILTGESVSVTKHTEAI--PDPRAVNQDKKNMLFSGTNITSGKAVGVAVATGLHTELGKIR---------- 236
Cdd:TIGR01523  160 KN--FDTDEALLTGESLPVIKDAHATfgKEEDTPIGDRINLAFSSSAVTKGRAKGICIATALNSEIGAIAaglqgdgglf 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   237 SQMAAVEPER-------------------------TPLQRKLDEFgrqlshAISVICVAVWVINIGHFADPAHGGSwlRG 291
Cdd:TIGR01523  238 QRPEKDDPNKrrklnkwilkvtkkvtgaflglnvgTPLHRKLSKL------AVILFCIAIIFAIIVMAAHKFDVDK--EV 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   292 AVYyfkiAVALAVAAIPEGLPAVITTCLALGTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFV--- 368
Cdd:TIGR01523  310 AIY----AICLAISIIPESLIAVLSITMAMGAANMSKRNVIVRKLDALEALGAVNDICSDKTGTITQGKMIARQIWIprf 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   369 ----VAEAD-------AGSCLLHEFTISGTTYTPEG----------EVRQGDQP--VRCGQFDGLVElatICALCNDSAL 425
Cdd:TIGR01523  386 gtisIDNSDdafnpneGNVSGIPRFSPYEYSHNEAAdqdilkefkdELKEIDLPedIDMDLFIKLLE---TAALANIATV 462
                          490       500
                   ....*....|....*....|....*...
gi 767992219   426 DYNEAKGVYEKVGEATETALTCLVEKMN 453
Cdd:TIGR01523  463 FKDDATDCWKAHGDPTEIAIHVFAKKFD 490
E1-E2_ATPase pfam00122
E1-E2 ATPase;
121-329 1.32e-47

E1-E2 ATPase;


Pssm-ID: 425475 [Multi-domain]  Cd Length: 181  Bit Score: 163.51  E-value: 1.32e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  121 EYEPEMGKVIRSDrkGVQRIRARDIVPGDIVEVAVGDKVPADLRLIEiksTTLRVDQSILTGESVSVTKHteaipdprav 200
Cdd:pfam00122   1 SLLPPTATVLRDG--TEEEVPADELVPGDIVLLKPGERVPADGRIVE---GSASVDESLLTGESLPVEKK---------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  201 nqdKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMAAVEPERTPLQRKLDEFGRQLSHAISVICVAVWVINIghfa 280
Cdd:pfam00122  66 ---KGDMVYSGTVVVSGSAKAVVTATGEDTELGRIARLVEEAKSKKTPLQRLLDRLGKYFSPVVLLIALAVFLLWL---- 138
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 767992219  281 dpahggSWLRGAVYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMARK 329
Cdd:pfam00122 139 ------FVGGPPLRALLRALAVLVAACPCALPLATPLALAVGARRLAKK 181
ATPase-IIIB_Mg TIGR01524
magnesium-translocating P-type ATPase; This model describes the magnesium translocating P-type ...
1-361 3.71e-47

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


Pssm-ID: 130587 [Multi-domain]  Cd Length: 867  Bit Score: 176.21  E-value: 3.71e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219    1 MEAAHLlPAADVLRHFSVTAEGgLSPAQVTGARERYGPNELPSEEGKSLWELVLEQFEDLLVRILLLAALVSFVlawfee 80
Cdd:TIGR01524  13 LKESQM-GKETLLRKLGVHETG-LTNVEVTERLAEFGPNQTVEEKKVPNLRLLIRAFNNPFIYILAMLMGVSYL------ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   81 geetTTAFVEPLVIMLILVANAIVGVWQERNAESAIEALKEYEPEMGKVIR---SDRKGVQRIRARD-IVPGDIVEVAVG 156
Cdd:TIGR01524  85 ----TDDLEATVIIALMVLASGLLGFIQESRAERAAYALKNMVKNTATVLRvinENGNGSMDEVPIDaLVPGDLIELAAG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  157 DKVPADLRLIEikSTTLRVDQSILTGESVSVTKHTEaIPDPRAVNQ-DKKNMLFSGTNITSGKAVGVAVATGLHTELGKI 235
Cdd:TIGR01524 161 DIIPADARVIS--ARDLFINQSALTGESLPVEKFVE-DKRARDPEIlERENLCFMGTNVLSGHAQAVVLATGSSTWFGSL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  236 rSQMAAVEPERTPLQRKLDEFGRQLSHAISVICVAVWVINiGHFAdpahgGSWLRGAVYyfkiAVALAVAAIPEGLPAVI 315
Cdd:TIGR01524 238 -AIAATERRGQTAFDKGVKSVSKLLIRFMLVMVPVVLMIN-GLMK-----GDWLEAFLF----ALAVAVGLTPEMLPMIV 306
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 767992219  316 TTCLALGTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQM 361
Cdd:TIGR01524 307 SSNLAKGAINMSKKKVIVKELSAIQNFGAMDILCTDKTGTLTQDKI 352
PRK10517 PRK10517
magnesium-transporting P-type ATPase MgtA;
7-357 1.31e-43

magnesium-transporting P-type ATPase MgtA;


Pssm-ID: 236705 [Multi-domain]  Cd Length: 902  Bit Score: 166.01  E-value: 1.31e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   7 LPAADVLRHFSvTAEGGLSPAQVTGARERYGPNELPSEEG----KSLWELVLEQFeDLLVRILllaALVSFVLawfeegE 82
Cdd:PRK10517  52 MPEEELWKTFD-THPEGLNEAEVESAREQHGENELPAQKPlpwwVHLWVCYRNPF-NILLTIL---GAISYAT------E 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  83 ETTTAfvepLVIMLILVANAIVGVWQERNAESAIEALKEYEPEMGKVIRSD----RKGVQRIRARDIVPGDIVEVAVGDK 158
Cdd:PRK10517 121 DLFAA----GVIALMVAISTLLNFIQEARSTKAADALKAMVSNTATVLRVIndkgENGWLEIPIDQLVPGDIIKLAAGDM 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 159 VPADLRLIEIKSttLRVDQSILTGESVSVtkhtEAIPDPRAVNQ----DKKNMLFSGTNITSGKAVGVAVATGLHTELGK 234
Cdd:PRK10517 197 IPADLRILQARD--LFVAQASLTGESLPV----EKFATTRQPEHsnplECDTLCFMGTNVVSGTAQAVVIATGANTWFGQ 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 235 IRSQMAAVEPERTPLQRKLDEFGRQLSHAISVICVAVWVINighfadpahG---GSWLRGAVYyfkiAVALAVAAIPEGL 311
Cdd:PRK10517 271 LAGRVSEQDSEPNAFQQGISRVSWLLIRFMLVMAPVVLLIN---------GytkGDWWEAALF----ALSVAVGLTPEML 337
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 767992219 312 PAVITTCLALGTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLT 357
Cdd:PRK10517 338 PMIVTSTLARGAVKLSKQKVIVKRLDAIQNFGAMDILCTDKTGTLT 383
PRK15122 PRK15122
magnesium-transporting ATPase; Provisional
19-357 3.79e-41

magnesium-transporting ATPase; Provisional


Pssm-ID: 237914 [Multi-domain]  Cd Length: 903  Bit Score: 158.65  E-value: 3.79e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  19 TAEGGLSPAQVTGARERYGPNELPSEEGKSLWELVLEQFEDLLVRILLLAALVSFVL-AWF--EEGEETTTAFVEPLVIM 95
Cdd:PRK15122  41 THRQGLTEEDAAERLQRYGPNEVAHEKPPHALVQLLQAFNNPFIYVLMVLAAISFFTdYWLplRRGEETDLTGVIIILTM 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  96 LILvaNAIVGVWQERNAESAIEALKEYEPEMGKVIR---SDRKGVQR-IRARDIVPGDIVEVAVGDKVPADLRLIEikST 171
Cdd:PRK15122 121 VLL--SGLLRFWQEFRSNKAAEALKAMVRTTATVLRrghAGAEPVRReIPMRELVPGDIVHLSAGDMIPADVRLIE--SR 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 172 TLRVDQSILTGESVSVTK-------HTEAIPDPRAVNQ---DKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMAA 241
Cdd:PRK15122 197 DLFISQAVLTGEALPVEKydtlgavAGKSADALADDEGsllDLPNICFMGTNVVSGTATAVVVATGSRTYFGSLAKSIVG 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 242 VEPErTPLQRKLDEFGRQLSHAISVICVAVWVINighfadpahG---GSWLRGAVYyfkiAVALAVAAIPEGLPAVITTC 318
Cdd:PRK15122 277 TRAQ-TAFDRGVNSVSWLLIRFMLVMVPVVLLIN---------GftkGDWLEALLF----ALAVAVGLTPEMLPMIVSSN 342
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 767992219 319 LALGTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLT 357
Cdd:PRK15122 343 LAKGAIAMARRKVVVKRLNAIQNFGAMDVLCTDKTGTLT 381
P-type_ATPase cd02609
uncharacterized subfamily of P-type ATPase transporter, similar to uncharacterized ...
23-375 1.75e-40

uncharacterized subfamily of P-type ATPase transporter, similar to uncharacterized Streptococcus pneumoniae exported protein 7, Exp7; This subfamily contains P-type ATPase transporters of unknown function, similar to Streptococcus pneumoniae Exp7. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids. They are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd(2+), and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine.


Pssm-ID: 319795 [Multi-domain]  Cd Length: 661  Bit Score: 155.52  E-value: 1.75e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  23 GLSPAQVTGARERYGPNELPSEEGKSLWELVleqFEDLLVRI----LLLAALVSFVLAWfeegeetttafvEPLVIMLIL 98
Cdd:cd02609    1 GLTTKEVEERQAEGKVNDQVEPVSRSVWQIV---RENVFTLFnlinFVIAVLLILVGSY------------SNLAFLGVI 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  99 VANAIVGVWQERNAESAIEALKEYEPEMGKVIRsDRKgVQRIRARDIVPGDIVEVAVGDKVPADLRLIEikSTTLRVDQS 178
Cdd:cd02609   66 IVNTVIGIVQEIRAKRQLDKLSILNAPKVTVIR-DGQ-EVKIPPEELVLDDILILKPGEQIPADGEVVE--GGGLEVDES 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 179 ILTGESVSVTKhteaipdpravnqDKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMAAVEPERTPLQRKLDEFGR 258
Cdd:cd02609  142 LLTGESDLIPK-------------KAGDKLLSGSFVVSGAAYARVTAVGAESYAAKLTLEAKKHKLINSELLNSINKILK 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 259 QLSHAISVICVAVWVINIghfadPAHGGSWLRGAVyyfkIAVALAVAAIPEGLPAVITTCLALGTRRMARKNAIVRSLPS 338
Cdd:cd02609  209 FTSFIIIPLGLLLFVEAL-----FRRGGGWRQAVV----STVAALLGMIPEGLVLLTSVALAVGAIRLAKKKVLVQELYS 279
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 767992219 339 VETLGCTSVICSDKTGTLTTNQMSVCRMFVVAEADAG 375
Cdd:cd02609  280 IETLARVDVLCLDKTGTITEGKMKVERVEPLDEANEA 316
ATPase-IB_hvy TIGR01525
heavy metal translocating P-type ATPase; This model encompasses two equivalog models for the ...
59-380 2.32e-28

heavy metal translocating P-type ATPase; This model encompasses two equivalog models for the copper and cadmium-type heavy metal transporting P-type ATPases (TIGR01511 and TIGR01512) as well as those species which score ambiguously between both models. For more comments and references, see the files on TIGR01511 and 01512.


Pssm-ID: 273669 [Multi-domain]  Cd Length: 558  Bit Score: 118.89  E-value: 2.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   59 DLLVrilLLAALVSFVLAWFEEGeetttafvepLVIMLILVANAIVGVWQERNAESAIEALKEYEPEMGKVIRSDRKgVQ 138
Cdd:TIGR01525   2 DTLM---ALAAIAAYAMGLVLEG----------ALLLFLFLLGETLEERAKSRASDALSALLALAPSTARVLQGDGS-EE 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  139 RIRARDIVPGDIVEVAVGDKVPADLRLIEIKSTtlrVDQSILTGESVSVTKHTeaipdpravnQDKknmLFSGTNITSGK 218
Cdd:TIGR01525  68 EVPVEELQVGDIVIVRPGERIPVDGVVISGESE---VDESALTGESMPVEKKE----------GDE---VFAGTINGDGS 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  219 AVGVAVATGLHTELGKIRSQMAAVEPERTPLQRKLDEFGRQLSHAISVICVAVWVInighfadPAHGGSWLRGAVYYFki 298
Cdd:TIGR01525 132 LTIRVTKLGEDSTLAQIVELVEEAQSSKAPIQRLADRIASYYVPAVLAIALLTFVV-------WLALGALWREALYRA-- 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  299 aVALAVAAIPEGLPAVITTCLALGTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRmFVVAEADAGSCL 378
Cdd:TIGR01525 203 -LTVLVVACPCALGLATPVAILVAIGAAARRGILIKGGDALEKLAKVKTVVFDKTGTLTTGKPTVVD-IEPLDDASEEEL 280

                  ..
gi 767992219  379 LH 380
Cdd:TIGR01525 281 LA 282
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
59-378 9.92e-27

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 114.85  E-value: 9.92e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  59 DLLVrilLLAALVSFVLAWFEEGEETTTAFVEPLVIMLILVAnaiVGVWQE----RNAESAIEALKEYEPEMGKVIRSDR 134
Cdd:COG2217  149 DVLV---ALGTLAAFLYSLYATLFGAGHVYFEAAAMIIFLLL---LGRYLEarakGRARAAIRALLSLQPKTARVLRDGE 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 135 kgVQRIRARDIVPGDIVEVAVGDKVPADLRLIEIKSTtlrVDQSILTGESVSVTKHTEAIpdpravnqdkknmLFSGTNI 214
Cdd:COG2217  223 --EVEVPVEELRVGDRVLVRPGERIPVDGVVLEGESS---VDESMLTGESLPVEKTPGDE-------------VFAGTIN 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 215 TSGKAVGVAVATGLHTELGKIRSQMAAVEPERTPLQRKLDEFGRQL---SHAISVICVAVWVINIGHFADpahggsWLRG 291
Cdd:COG2217  285 LDGSLRVRVTKVGSDTTLARIIRLVEEAQSSKAPIQRLADRIARYFvpaVLAIAALTFLVWLLFGGDFST------ALYR 358
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 292 AVyyfkiavalavaaipeglpAV-ITTC---LAL--------GTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTN 359
Cdd:COG2217  359 AV-------------------AVlVIACpcaLGLatptaimvGTGRAARRGILIKGGEALERLAKVDTVVFDKTGTLTEG 419
                        330
                 ....*....|....*....
gi 767992219 360 QMSVCRMFVVAEADAGSCL 378
Cdd:COG2217  420 KPEVTDVVPLDGLDEDELL 438
ATPase-IB2_Cd TIGR01512
heavy metal-(Cd/Co/Hg/Pb/Zn)-translocating P-type ATPase; This model describes the P-type ...
58-363 3.53e-24

heavy metal-(Cd/Co/Hg/Pb/Zn)-translocating P-type ATPase; This model describes the P-type ATPase primarily responsible for translocating cadmium ions (and other closely-related divalent heavy metals such as cobalt, mercury, lead and zinc) across biological membranes. These transporters are found in prokaryotes and plants. Experimentally characterized members of the seed alignment include: SP|P37617 from E. coli, SP|Q10866 from Mycobacterium tuberculosis and SP|Q59998 from Synechocystis PCC6803. The cadmium P-type ATPases have been characterized as Type IB based on a phylogenetic analysis which combines the copper-translocating ATPases with the cadmium-translocating species. This model and that describing the copper-ATPases (TIGR01511) are well separated, and thus we further type the copper-ATPases as IB1 and the cadmium-ATPases as IB2. Several sequences which have not been characterized experimentally fall just below trusted cutoff for both of these models (SP|Q9CCL1 from Mycobacterium leprae, GP|13816263 from Sulfolobus solfataricus, OMNI|NTL01CJ01098 from Campylobacter jejuni, OMNI|NTL01HS01687 from Halobacterium sp., GP|6899169 from Ureaplasma urealyticum and OMNI|HP1503 from Helicobacter pylori). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273665 [Multi-domain]  Cd Length: 550  Bit Score: 106.25  E-value: 3.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   58 EDLLVRILLLAALvsFVLAWFEEgeetttafvepLVIMLILVANAIVGVWQERNAESAIEALKEYEPEMGKVIRSDrkGV 137
Cdd:TIGR01512   1 VDLLMALAALGAV--AIGEYLEG-----------ALLLLLFSIGETLEEYASGRARRALKALMELAPDTARRLQGD--SL 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  138 QRIRARDIVPGDIVEVAVGDKVPADLRLIEIKSTtlrVDQSILTGESVSVTKHTEaipdpravnqDKknmLFSGTNITSG 217
Cdd:TIGR01512  66 EEVAVEELKVGDVVVVKPGERVPVDGEVLSGTSS---VDESALTGESVPVEKAPG----------DE---VFAGAINLDG 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  218 KAVGVAVATGLHTELGKIRSQMAAVEPERTPLQRKLDEFGRQLSHAISVICVAVWVINighfadPAHGGSWLRGAVYYFk 297
Cdd:TIGR01512 130 VLTIEVTKLPADSTIAKIVNLVEEAQSRKAPTQRFIDRFARYYTPAVLAIALAAALVP------PLLGAGPFLEWIYRA- 202
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767992219  298 iaVALAVAAIPEGLpaVITTCLAL--GTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSV 363
Cdd:TIGR01512 203 --LVLLVVASPCAL--VISAPAAYlsAISAAARHGILIKGGAALEALAKIKTVAFDKTGTLTTGKPKV 266
ATPase-IB1_Cu TIGR01511
copper-(or silver)-translocating P-type ATPase; This model describes the P-type ATPase ...
66-363 1.45e-21

copper-(or silver)-translocating P-type ATPase; This model describes the P-type ATPase primarily responsible for translocating copper ions accross biological membranes. These transporters are found in prokaryotes and eukaryotes. This model encompasses those species which pump copper ions out of cells or organelles (efflux pumps such as CopA of Escherichia coli) as well as those which pump the ion into cells or organelles either for the purpose of supporting life in extremely low-copper environments (for example CopA of Enterococcus hirae) or for the specific delivery of copper to a biological complex for which it is a necessary component (for example FixI of Bradyrhizobium japonicum, or CtaA and PacS of Synechocystis). The substrate specificity of these transporters may, to a varying degree, include silver ions (for example, CopA from Archaeoglobus fulgidus). Copper transporters from this family are well known as the genes which are mutated in two human disorders of copper metabolism, Wilson's and Menkes' diseases. The sequences contributing to the seed of this model are all experimentally characterized. The copper P-type ATPases have been characterized as Type IB based on a phylogenetic analysis which combines the copper-translocating ATPases with the cadmium-translocating species. This model and that describing the cadmium-ATPases (TIGR01512) are well separated, and thus we further type the copper-ATPases as IB1 (and the cadmium-ATPases as IB2). Several sequences which have not been characterized experimentally fall just below the cutoffs for both of these models (SP|Q9CCL1 from Mycobacterium leprae, GP|13816263 from Sulfolobus solfataricus, OMNI|NTL01CJ01098 from Campylobacter jejuni, OMNI|NTL01HS01687 from Halobacterium sp., GP|6899169 from Ureaplasma urealyticum and OMNI|HP1503 from Helicobacter pylori). Accession PIR|A29576 from Enterococcus faecalis scores very high against this model, but yet is annotated as an "H+/K+ exchanging ATPase". BLAST of this sequence does not hit anything else annotated in this way. This error may come from the characterization paper published in 1987. Accession GP|7415611 from Saccharomyces cerevisiae appears to be mis-annotated as a cadmium resistance protein. Accession OMNI|NTL01HS00542 from Halobacterium which scores above trusted for this model is annotated as "molybdenum-binding protein" although no evidence can be found for this classification. [Cellular processes, Detoxification, Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273664 [Multi-domain]  Cd Length: 562  Bit Score: 98.12  E-value: 1.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   66 LLAALVSFVLAWFEEGEETTTAFVEPLVIMLILvanaIVGVWQERNAES----AIEALKEYEPEMGKVIRSDrKGVQRIR 141
Cdd:TIGR01511  32 YGYSLVALLANQVLTGLHVHTFFDASAMLITFI----LLGRWLEMLAKGrasdALSKLAKLQPSTATLLTKD-GSIEEVP 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  142 ARDIVPGDIVEVAVGDKVPADLRLIEIKSTtlrVDQSILTGESVSVTKHTeaipdpravnQDKknmLFSGTNITSGKAVG 221
Cdd:TIGR01511 107 VALLQPGDIVKVLPGEKIPVDGTVIEGESE---VDESLVTGESLPVPKKV----------GDP---VIAGTVNGTGSLVV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  222 VAVATGLHTELGKIRSQMAAVEPERTPLQRKLDEFGRQLS---HAISVICVAVWVinighFAdpahggswLRGAVYYFki 298
Cdd:TIGR01511 171 RATATGEDTTLAQIVRLVRQAQQSKAPIQRLADKVAGYFVpvvIAIALITFVIWL-----FA--------LEFAVTVL-- 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767992219  299 avalaVAAIPEGLPAVITTCLALGTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSV 363
Cdd:TIGR01511 236 -----IIACPCALGLATPTVIAVATGLAAKNGVLIKDGDALERAANIDTVVFDKTGTLTQGKPTV 295
P-type_ATPase_HM cd02079
P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) ...
59-378 4.34e-21

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: 96.90  E-value: 4.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  59 DLLVrilLLAALVSFVLAWFEEGEETTTAFVEPLVIMLILVANAIVGVWQERNAESAIEALKEYEPEmgKVIRSDRKGVQ 138
Cdd:cd02079   62 DVLV---SLAAIGAFVASLLTPLLGGIGYFEEAAMLLFLFLLGRYLEERARSRARSALKALLSLAPE--TATVLEDGSTE 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 139 RIRARDIVPGDIVEVAVGDKVPADLRLIEIKSTtlrVDQSILTGESVSVTKHTEAipdprAVnqdkknmlFSGTNITSGK 218
Cdd:cd02079  137 EVPVDDLKVGDVVLVKPGERIPVDGVVVSGESS---VDESSLTGESLPVEKGAGD-----TV--------FAGTINLNGP 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 219 AVGVAVATGLHTELGKIRSQMAAVEPERTPLQRKLDEFGRQLSHAISVICVAVWVINIGHFADPAHggsWLRGAVyyfki 298
Cdd:cd02079  201 LTIEVTKTGEDTTLAKIIRLVEEAQSSKPPLQRLADRFARYFTPAVLVLAALVFLFWPLVGGPPSL---ALYRAL----- 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 299 avalavaaipeglpAV-ITTC---LAL--------GTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRM 366
Cdd:cd02079  273 --------------AVlVVACpcaLGLatptaivaGIGRAARKGILIKGGDVLETLAKVDTVAFDKTGTLTEGKPEVTEI 338
                        330
                 ....*....|..
gi 767992219 367 FVVAEADAGSCL 378
Cdd:cd02079  339 EPLEGFSEDELL 350
Cation_ATPase pfam13246
Cation transport ATPase (P-type); This domain is found in cation transport ATPases, including ...
418-518 7.00e-20

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: 84.19  E-value: 7.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  418 ALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMnvfdtdlqalsrveraGACNTVIKQLMRKEFTLEFSRDRKSMSVY 497
Cdd:pfam13246   1 ALCNSAAFDENEEKGKWEIVGDPTESALLVFAEKM----------------GIDVEELRKDYPRVAEIPFNSDRKRMSTV 64
                          90       100
                  ....*....|....*....|.
gi 767992219  498 CTPtrphPTGQGSKMFVKvGA 518
Cdd:pfam13246  65 HKL----PDDGKYRLFVK-GA 80
Cation_ATPase_N pfam00690
Cation transporter/ATPase, N-terminus; Members of this families are involved in Na+/K+, H+/K+, ...
4-71 1.49e-19

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


Pssm-ID: 459907 [Multi-domain]  Cd Length: 68  Bit Score: 82.61  E-value: 1.49e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767992219    4 AHLLPAADVLRHFSVTAEGGLSPAQVTGARERYGPNELPSEEGKSLWELVLEQFEDLLVRILLLAALV 71
Cdd:pfam00690   1 WHALSVEEVLKKLGTDLEKGLTEAEAEKRLKKYGPNELPEKKPKSLWKLFLRQFKDPLIIILLIAAIV 68
P-type_ATPase_cation cd07542
P-type cation-transporting ATPases, similar to human ATPase type 13A2 (ATP13A2) protein and ...
33-359 1.67e-19

P-type cation-transporting ATPases, similar to human ATPase type 13A2 (ATP13A2) protein and Saccharomyces cerevisiae Ypk9p; Saccharomyces cerevisiae Yph9p localizes to the yeast vacuole and may play a role in sequestering heavy metal ions, its deletion confers sensitivity for growth for cadmium, manganese, nickel or selenium. Human ATP13A2 (PARK9/CLN12) is a lysosomal transporter with zinc as the possible substrate. Mutation in the ATP13A2 gene has been linked to Parkinson's disease and Kufor-Rakeb syndrome, and to neuronal ceroid lipofuscinoses. ATP13A3/AFURS1 is a candidate gene for oculo auriculo vertebral spectrum (OAVS), being one of nine genes included in a 3q29 microduplication in a patient with OAVS. Mutation in the human ATP13A4 may be involved in a speech-language disorder. This subfamily also includes zebrafish ATP13A2 a lysosome-specific transmembrane ATPase protein of unknown function which plays a crucial role during embryonic development, its deletion is lethal. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319842 [Multi-domain]  Cd Length: 760  Bit Score: 92.31  E-value: 1.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  33 RERYGPNELPSEEgKSLWEL----VLEQFedllvrilLLAALVSfVLAWFEEGeetttaFVE-PLVIMLILVANAIVGVW 107
Cdd:cd07542    7 RLIYGPNEIDVPL-KSILKLlfkeVLNPF--------YVFQLFS-VILWSSDD------YYYyAACIVIISVISIFLSLY 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 108 QERNAESAIEALKEYePEMGKVIRsdRKGVQRIRARDIVPGDIVEVAVGDKV-PADLRLIeikSTTLRVDQSILTGESVS 186
Cdd:cd07542   71 ETRKQSKRLREMVHF-TCPVRVIR--DGEWQTISSSELVPGDILVIPDNGTLlPCDAILL---SGSCIVNESMLTGESVP 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 187 VTK-----HTEAIPDPRAVNQD-KKNMLFSGTNI------TSGKAVGVAVATGLHTELGK-IRSQMAavePERTPLQRKL 253
Cdd:cd07542  145 VTKtplpdESNDSLWSIYSIEDhSKHTLFCGTKViqtrayEGKPVLAVVVRTGFNTTKGQlVRSILY---PKPVDFKFYR 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 254 DefgrqlshAISVICVAVWVINIGHFADpahggswlrgAVYYFKIAVALAVA----------AIPEGLPAVITTCLALGT 323
Cdd:cd07542  222 D--------SMKFILFLAIIALIGFIYT----------LIILILNGESLGEIiiraldiitiVVPPALPAALTVGIIYAQ 283
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 767992219 324 RRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTN 359
Cdd:cd07542  284 SRLKKKGIFCISPQRINICGKINLVCFDKTGTLTED 319
P-type_ATPase_Pb_Zn_Cd2-like cd07546
P-type heavy metal-transporting ATPase, similar to Escherichia coli ZntA which is selective ...
92-379 1.09e-18

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


Pssm-ID: 319846 [Multi-domain]  Cd Length: 597  Bit Score: 89.39  E-value: 1.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  92 LVIMLILVANAIVGVWQERnAESAIEALKEYEPEMGKVIRSDrkGVQRIRARDIVPGDIVEVAVGDKVPADLRLIEIKST 171
Cdd:cd07546   67 MVLLLFLVGELLEGYAASR-ARSGVKALMALVPETALREENG--ERREVPADSLRPGDVIEVAPGGRLPADGELLSGFAS 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 172 tlrVDQSILTGESVSVTKhteaipdpravnqDKKNMLFSGTNITSGKA-VGVAVATGLHTeLGKIRSQMAAVEPERTPLQ 250
Cdd:cd07546  144 ---FDESALTGESIPVEK-------------AAGDKVFAGSINVDGVLrIRVTSAPGDNA-IDRILHLIEEAEERRAPIE 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 251 RKLDEFGRQLSHAISVICVAVWVInighfadP--AHGGSW----LRGavyyfkiaVALAVAAIPEGL----PAVITTCLA 320
Cdd:cd07546  207 RFIDRFSRWYTPAIMAVALLVIVV-------PplLFGADWqtwiYRG--------LALLLIGCPCALvistPAAITSGLA 271
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767992219 321 LGTRRmarkNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFVVAEADAGSCLL 379
Cdd:cd07546  272 AAARR----GALIKGGAALEQLGRVTTVAFDKTGTLTRGKPVVTDVVPLTGISEAELLA 326
P-ATPase-V TIGR01657
P-type ATPase of unknown pump specificity (type V); These P-type ATPases form a distinct clade ...
23-363 1.41e-18

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: 89.73  E-value: 1.41e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219    23 GLSPAQVTGARERYGPNEL----PSEEgKSLWELVLEQFEDLLVRILLLAALVSFvlaWFeegeetTTAFveplvIMLIL 98
Cdd:TIGR01657  139 GLTTGDIAQRKAKYGKNEIeipvPSFL-ELLKEEVLHPFYVFQVFSVILWLLDEY---YY------YSLC-----IVFMS 203
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219    99 VANAIVGVWQERNAESAIEALKeYEPEMGKVIRSDRKgvQRIRARDIVPGDIVEVAV--GDKVPADLRLIeikSTTLRVD 176
Cdd:TIGR01657  204 STSISLSVYQIRKQMQRLRDMV-HKPQSVIVIRNGKW--VTIASDELVPGDIVSIPRpeEKTMPCDSVLL---SGSCIVN 277
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   177 QSILTGESVSVTKhtEAIPDPRAVNQD-------KKNMLFSGTNI-------TSGKAVGVAVATGLHTELGKIRSQMaaV 242
Cdd:TIGR01657  278 ESMLTGESVPVLK--FPIPDNGDDDEDlflyetsKKHVLFGGTKIlqirpypGDTGCLAIVVRTGFSTSKGQLVRSI--L 353
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   243 EPERTPLQRKLDEFGRQLSHAISVICVAVWVINIGHfadpahggswLRGAVYYFKIAVALA--VAAIPEGLPAVITTCLA 320
Cdd:TIGR01657  354 YPKPRVFKFYKDSFKFILFLAVLALIGFIYTIIELI----------KDGRPLGKIILRSLDiiTIVVPPALPAELSIGIN 423
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 767992219   321 LGTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSV 363
Cdd:TIGR01657  424 NSLARLKKKGIFCTSPFRINFAGKIDVCCFDKTGTLTEDGLDL 466
Cation_ATPase_N smart00831
Cation transporter/ATPase, N-terminus; This entry represents the conserved N-terminal region ...
5-75 1.69e-17

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


Pssm-ID: 214842 [Multi-domain]  Cd Length: 75  Bit Score: 76.85  E-value: 1.69e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767992219     5 HLLPAADVLRHFSVTAEGGLSPAQVTGARERYGPNELPSEEGKSLWELVLEQFEDLLVRILLLAALVSFVL 75
Cdd:smart00831   5 HALSLEEVLERLQTDLEKGLSSEEAARRLERYGPNELPPPKKTSPLLRFLRQFHNPLIYILLAAAVLSALL 75
P-type_ATPase_HM_ZosA_PfeT-like cd07551
P-type heavy metal-transporting ATPase, similar to Bacillus subtilis ZosA/PfeT which ...
50-364 1.51e-16

P-type heavy metal-transporting ATPase, similar to Bacillus subtilis ZosA/PfeT which transports copper, and perhaps zinc under oxidative stress, and perhaps ferrous iron; Bacillus subtilis ZosA/PfeT (previously known as YkvW) transports copper, it may also transport zinc under oxidative stress and may also be involved in ferrous iron efflux. ZosA/PfeT is expressed under the regulation of the peroxide-sensing repressor PerR. It is involved in competence development. Disruption of the zosA/pfeT gene results in low transformability. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319849 [Multi-domain]  Cd Length: 611  Bit Score: 82.68  E-value: 1.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  50 WELVLEQFEDLL------VRIL-LLAALVSFVLAWFEEGeetttafvePLVIMLILVANAIVGVWQERnAESAIEALKEY 122
Cdd:cd07551   40 YASAKEGIEATLrkktlnVDLLmILAAIGAAAIGYWAEG---------ALLIFIFSLSHALEDYAMGR-SKRAITALMQL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 123 EPEMGKVIRSDrKGVQRIRARDIVPGDIVEVAVGDKVPADLRLIEIKSTtlrVDQSILTGESVSVTKHteaIPDPravnq 202
Cdd:cd07551  110 APETARRIQRD-GEIEEVPVEELQIGDRVQVRPGERVPADGVILSGSSS---IDEASITGESIPVEKT---PGDE----- 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 203 dkknmLFSGTnITSGKAVGVAVaTGLHTE--LGKIRSQMAAVEPERTPLQRKLDEFGRQlsHAISVICVAVWVINIGHFA 280
Cdd:cd07551  178 -----VFAGT-INGSGALTVRV-TKLSSDtvFAKIVQLVEEAQSEKSPTQSFIERFERI--YVKGVLLAVLLLLLLPPFL 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 281 DpahGGSW----LRGAVYyfkiavalAVAAIPEGLPAVITTCLALGTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTL 356
Cdd:cd07551  249 L---GWTWadsfYRAMVF--------LVVASPCALVASTPPATLSAIANAARQGVLFKGGVHLENLGSVKAIAFDKTGTL 317

                 ....*...
gi 767992219 357 TTNQMSVC 364
Cdd:cd07551  318 TEGKPRVT 325
P-type_ATPase_Cd-like cd07545
P-type heavy metal-transporting ATPase, similar to Staphylococcus aureus plasmid pI258 CadA, a ...
92-378 7.67e-15

P-type heavy metal-transporting ATPase, similar to Staphylococcus aureus plasmid pI258 CadA, a cadmium-efflux ATPase; CadA from gram-positive Staphylococcus aureus plasmid pI258 is required for full Cd(2+) and Zn(2+) resistance. This subfamily also includes CadA, from the gram-negative bacilli, Stenotrophomonas maltophilia D457R, which is a cadmium efflux pump acquired as part of a cluster of antibiotic and heavy metal resistance genes from gram-positive bacteria. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319845 [Multi-domain]  Cd Length: 599  Bit Score: 77.46  E-value: 7.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  92 LVIMLILVANAIVGVWQERnAESAIEALKEYEPEMGKVIRSDRKgvQRIRARDIVPGDIVEVAVGDKVPADLRLIEIKST 171
Cdd:cd07545   64 MVVFLFAISEALEAYSMDR-ARRSIRSLMDIAPKTALVRRDGQE--REVPVAEVAVGDRMIVRPGERIAMDGIIVRGESS 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 172 tlrVDQSILTGESVSVTKhteaipdpravnqDKKNMLFSGTNITSGkAVGVAV-ATGLHTELGKIRSQMAAVEPERTPLQ 250
Cdd:cd07545  141 ---VNQAAITGESLPVEK-------------GVGDEVFAGTLNGEG-ALEVRVtKPAEDSTIARIIHLVEEAQAERAPTQ 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 251 RKLDEFGRQLSHAISVICVAVWVINIGHFadpahGGSWLrGAVYyfkIAVALAVAAIPEGLpaVITTCL----ALGTrrM 326
Cdd:cd07545  204 AFVDRFARYYTPVVMAIAALVAIVPPLFF-----GGAWF-TWIY---RGLALLVVACPCAL--VISTPVsivsAIGN--A 270
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767992219 327 ARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFVVAEADAGSCL 378
Cdd:cd07545  271 ARKGVLIKGGVYLEELGRLKTVAFDKTGTLTKGKPVVTDVVVLGGQTEKELL 322
P-type_ATPase_FixI-like cd02092
Rhizobium meliloti FixI and related proteins; belongs to P-type heavy metal-transporting ...
110-357 1.91e-14

Rhizobium meliloti FixI and related proteins; belongs to P-type heavy metal-transporting ATPase subfamily; FixI may be a pump of a specific cation involved in symbiotic nitrogen fixation. The Rhizobium fixI gene is part of an operon conserved among rhizobia, fixGHIS. FixG, FixH, FixI, and FixS may participate in a membrane-bound complex coupling the FixI cation pump with a redox process catalyzed by FixG, an iron-sulfur protein. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319782 [Multi-domain]  Cd Length: 605  Bit Score: 76.24  E-value: 1.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 110 RNAESAIEALKEYEPEMGKVIRSDrkGVQR-IRARDIVPGDIVEVAVGDKVPADLRLIeikSTTLRVDQSILTGESVSVT 188
Cdd:cd02092  111 GRARSAAEELAALEARGAQRLQAD--GSREyVPVAEIRPGDRVLVAAGERIPVDGTVV---SGTSELDRSLLTGESAPVT 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 189 KHTEAipdpravnqdkknMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMAAVEPERTPLQRKLDEFGRQLS---HAIS 265
Cdd:cd02092  186 VAPGD-------------LVQAGAMNLSGPLRLRATAAGDDTLLAEIARLMEAAEQGRSRYVRLADRAARLYApvvHLLA 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 266 VICVAVWVInighfadpaHGGSWlRGAVyyfkiavalavaaipegLPAV---ITTC-LALG----------TRRMARKNA 331
Cdd:cd02092  253 LLTFVGWVA---------AGGDW-RHAL-----------------LIAVavlIITCpCALGlavpavqvvaSGRLFRRGV 305
                        250       260
                 ....*....|....*....|....*.
gi 767992219 332 IVRSLPSVETLGCTSVICSDKTGTLT 357
Cdd:cd02092  306 LVKDGTALERLAEVDTVVFDKTGTLT 331
P-type_ATPase_Cu-like cd02094
P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A ...
92-363 6.21e-14

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: 74.44  E-value: 6.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  92 LVIMLILVanaivGVWQE----RNAESAIEALKEYEPEMGKVIRSDrkGVQRIRARDIVPGDIVEVAVGDKVPADLRLIE 167
Cdd:cd02094  107 VIITFILL-----GKYLEarakGKTSEAIKKLLGLQPKTARVIRDG--KEVEVPIEEVQVGDIVRVRPGEKIPVDGVVVE 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 168 IKSTtlrVDQSILTGESVSVTKHTEaipdpravnqDKknmLFSGTNITSGKAVGVAVATGLHTELGKIrsqMAAVEpE-- 245
Cdd:cd02094  180 GESS---VDESMLTGESLPVEKKPG----------DK---VIGGTINGNGSLLVRATRVGADTTLAQI---IRLVE-Eaq 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 246 --RTPLQRKLDefgrQLS-------HAISVICVAVWVInIGHFADPAHGgswLRGAVyyfkiavalavaaipeglpAV-I 315
Cdd:cd02094  240 gsKAPIQRLAD----RVSgvfvpvvIAIAILTFLVWLL-LGPEPALTFA---LVAAV-------------------AVlV 292
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767992219 316 TTC---LAL--------GTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSV 363
Cdd:cd02094  293 IACpcaLGLatptaimvGTGRAAELGILIKGGEALERAHKVDTVVFDKTGTLTEGKPEV 351
P-type_ATPase_cation cd02082
P-type cation-transporting ATPases, similar to human ATPase type 13A1-A4 (ATP13A1-A4) proteins ...
92-363 1.05e-13

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: 74.16  E-value: 1.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  92 LVIMLILVANAIVGVWQERNAESAIEALKeYEPEMGKVIRSDRKgVQRIRARDIVPGDIVEVAV-GDKVPADLRLIEiks 170
Cdd:cd02082   54 ITVVFMTTINSLSCIYIRGVMQKELKDAC-LNNTSVIVQRHGYQ-EITIASNMIVPGDIVLIKRrEVTLPCDCVLLE--- 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 171 TTLRVDQSILTGESVSVTKhtEAIPDP----RAVNQD--KKNMLFSGTNI------TSGKAVGVAVATGLHTELGKIRsq 238
Cdd:cd02082  129 GSCIVTEAMLTGESVPIGK--CQIPTDshddVLFKYEssKSHTLFQGTQVmqiippEDDILKAIVVRTGFGTSKGQLI-- 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 239 maavepeRTPLQRKLDEFGRQLSHAISVICVAVwvinighFADPAHGGSWLRG------AVYYFKIAVALAVAAIPEGLP 312
Cdd:cd02082  205 -------RAILYPKPFNKKFQQQAVKFTLLLAT-------LALIGFLYTLIRLldielpPLFIAFEFLDILTYSVPPGLP 270
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767992219 313 AVITTCLALGTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSV 363
Cdd:cd02082  271 MLIAITNFVGLKRLKKNQILCQDPNRISQAGRIQTLCFDKTGTLTEDKLDL 321
zntA PRK11033
zinc/cadmium/mercury/lead-transporting ATPase; Provisional
92-379 6.79e-13

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


Pssm-ID: 236827 [Multi-domain]  Cd Length: 741  Bit Score: 71.18  E-value: 6.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  92 LVIMLILVANAIVGvWQERNAESAIEALKEYEPEMGKVIRSDRKgvQRIRARDIVPGDIVEVAVGDKVPADLRLIeikST 171
Cdd:PRK11033 211 MVLLLFLIGERLEG-YAASRARRGVSALMALVPETATRLRDGER--EEVAIADLRPGDVIEVAAGGRLPADGKLL---SP 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 172 TLRVDQSILTGESVSVTKHT-EAIPdPRAVNQDKKNMLfsgtNITSGKAvgvavatglHTELGKIRSQMAAVEPERTPLQ 250
Cdd:PRK11033 285 FASFDESALTGESIPVERATgEKVP-AGATSVDRLVTL----EVLSEPG---------ASAIDRILHLIEEAEERRAPIE 350
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 251 RKLDEFGRQLSHAISVICVAVWVINIGHFADPahggsWLrGAVYyfkiavalavaaipEGL---------------PAVI 315
Cdd:PRK11033 351 RFIDRFSRIYTPAIMLVALLVILVPPLLFAAP-----WQ-EWIY--------------RGLtllligcpcalvistPAAI 410
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767992219 316 TTCLALGTRRmarkNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFVVAEADAGSCLL 379
Cdd:PRK11033 411 TSGLAAAARR----GALIKGGAALEQLGRVTTVAFDKTGTLTEGKPQVTDIHPATGISESELLA 470
P-type_ATPase_HM cd07553
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
67-362 3.66e-11

P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily of the heavy metal-transporting ATPases (Type IB ATPases) which transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319851 [Multi-domain]  Cd Length: 610  Bit Score: 65.61  E-value: 3.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  67 LAALVSFVLAWFEEGEETTTAFVEPL--VIMLILVANAIVGVWQERNAEsaiEALKEYEPEMGKVIRSDRKGVQRIRARD 144
Cdd:cd07553   69 LGIVIGFVVSWYGLIKGDGLVYFDSLsvLVFLMLVGRWLQVVTQERNRN---RLADSRLEAPITEIETGSGSRIKTRADQ 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 145 IVPGDIVEVAVGDKVPADLRLIeikSTTLRVDQSILTGESVSVTKHteaipdpravnqdKKNMLFSGTNITSGKAVGVAV 224
Cdd:cd07553  146 IKSGDVYLVASGQRVPVDGKLL---SEQASIDMSWLTGESLPRIVE-------------RGDKVPAGTSLENQAFEIRVE 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 225 ATGLHTELGKIRSQMAAVEPERTPLqrklDEFGRQLSHAISVICVAVWVinighfadpAHGGSWLR-GAVYYFKIAVALA 303
Cdd:cd07553  210 HSLAESWSGSILQKVEAQEARKTPR----DLLADKIIHYFTVIALLIAV---------AGFGVWLAiDLSIALKVFTSVL 276
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767992219 304 VAAIPEGLPAVITTCLALGTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMS 362
Cdd:cd07553  277 IVACPCALALATPFTDEIALARLKKKGVLIKNASSLERLSRVRTIVFDKTGTLTRGKSS 335
P-type_ATPase_cation cd07543
P-type cation-transporting ATPases, similar to human cation-transporting ATPase type 13A1 ...
124-243 5.63e-10

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: 62.02  E-value: 5.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 124 PEMGKVIRsDRKGVQrIRARDIVPGDIVEV---AVGDKVPADLRLIeikSTTLRVDQSILTGESVSVTKHT-EAIPDPRA 199
Cdd:cd07543   85 PYTIQVYR-DGKWVP-ISSDELLPGDLVSIgrsAEDNLVPCDLLLL---RGSCIVNEAMLTGESVPLMKEPiEDRDPEDV 159
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767992219 200 V---NQDKKNMLFSGTNI-------------TSGKAVGVAVATGLHTELGK-IRSQMAAVE 243
Cdd:cd07543  160 LdddGDDKLHVLFGGTKVvqhtppgkgglkpPDGGCLAYVLRTGFETSQGKlLRTILFSTE 220
P-type_ATPase_HM cd07550
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
84-363 9.30e-10

P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily of the heavy metal-transporting ATPases (Type IB ATPases) which transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319848 [Multi-domain]  Cd Length: 592  Bit Score: 61.14  E-value: 9.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  84 TTTAFVEPLVIMLILVANAIVGVWQERNAESAIEALKEYEPEMGKVIRSDRkgVQRIRARDIVPGDIVEVAVGDKVPADL 163
Cdd:cd07550   59 LTGDYLAANTIAFLLELGELLEDYTARKSEKALLDLLSPQERTVWVERDGV--EVEVPADEVQPGDTVVVGAGDVIPVDG 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 164 RLIEIKSTtlrVDQSILTGESVSVTKhteaipdpravnqDKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMAAVE 243
Cdd:cd07550  137 TVLSGEAL---IDQASLTGESLPVEK-------------REGDLVFASTVVEEGQLVIRAERVGRETRAARIAELIEQSP 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 244 PERTPLQRKLDEFGRQLSHAISVICVAVWVINighfadpahgGSWLRGAVYYFKIAVALAVAAIPEGLPAVITTClalgt 323
Cdd:cd07550  201 SLKARIQNYAERLADRLVPPTLGLAGLVYALT----------GDISRAAAVLLVDFSCGIRLSTPVAVLSALNHA----- 265
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 767992219 324 rrmARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSV 363
Cdd:cd07550  266 ---ARHGILVKGGRALELLAKVDTVVFDKTGTLTEGEPEV 302
P-type_ATPase_Cu-like cd07552
P-type heavy metal-transporting ATPase, similar to Archaeoglobus fulgidus CopB, a Cu(2+) ...
93-363 3.74e-09

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


Pssm-ID: 319850 [Multi-domain]  Cd Length: 632  Bit Score: 59.24  E-value: 3.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  93 VIMLIlvanaivGVWQERN----AESAIEALKEYEPEMGKVIRSDrkGVQRIRARDIVPGDIVEVAVGDKVPADLRLIEI 168
Cdd:cd07552  102 VIMLL-------GHWIEMKavmgAGDALKKLAELLPKTAHLVTDG--SIEDVPVSELKVGDVVLVRAGEKIPADGTILEG 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 169 KSttlRVDQSILTGESvsvtkhteaipdpRAVNQDKKNMLFSGTnITSGKAVGVAV-ATGLHTELGKIRSQMAAVEPERT 247
Cdd:cd07552  173 ES---SVNESMVTGES-------------KPVEKKPGDEVIGGS-VNGNGTLEVKVtKTGEDSYLSQVMELVAQAQASKS 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 248 PLQRKLDEFGRQLSHA---ISVICVAVWVInIGHFADPahggswLRGAVYYFkiavalaVAAIPEGLPAVITTCLALGTR 324
Cdd:cd07552  236 RAENLADKVAGWLFYIalgVGIIAFIIWLI-LGDLAFA------LERAVTVL-------VIACPHALGLAIPLVVARSTS 301
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 767992219 325 RMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSV 363
Cdd:cd07552  302 IAAKNGLLIRNREALERARDIDVVLFDKTGTLTEGKFGV 340
P-type_ATPase_HM cd07544
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
110-363 5.01e-09

P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily of the heavy metal-transporting ATPases (Type IB ATPases) which transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319844 [Multi-domain]  Cd Length: 596  Bit Score: 58.87  E-value: 5.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 110 RNAESAIEALKEYEPEMGKVIRSDrkGVQRIRARDIVPGDIVEVAVGDKVPADLRLIeikSTTLRVDQSILTGESVSVTK 189
Cdd:cd07544   95 RRASRELTALLDRAPRIAHRLVGG--QLEEVPVEEVTVGDRLLVRPGEVVPVDGEVV---SGTATLDESSLTGESKPVSK 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 190 HteaipdpravnqdkknmlfSGTNITSGKAVG------VAVATGLHTELGKIRSQMAAVEPERTPLQRKLDEFGRQLSHA 263
Cdd:cd07544  170 R-------------------PGDRVMSGAVNGdsaltmVATKLAADSQYAGIVRLVKEAQANPAPFVRLADRYAVPFTLL 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 264 ISVICVAVWVINighfADPAHGGSWLRGAvyyfkiavalavaaIPegLPAVITTCLAL--GTRRMARKNAIVRSLPSVET 341
Cdd:cd07544  231 ALAIAGVAWAVS----GDPVRFAAVLVVA--------------TP--CPLILAAPVAIvsGMSRSSRRGILVKDGGVLEK 290
                        250       260
                 ....*....|....*....|..
gi 767992219 342 LGCTSVICSDKTGTLTTNQMSV 363
Cdd:cd07544  291 LARAKTVAFDKTGTLTYGQPKV 312
P-type_ATPase-Cd_Zn_Co_like cd07548
P-type heavy metal-transporting ATPase, similar to Bacillus subtilis CadA which appears to ...
115-363 7.35e-08

P-type heavy metal-transporting ATPase, similar to Bacillus subtilis CadA which appears to transport cadmium, zinc and cobalt but not copper out of the cell; Bacillus subtilis CadA/YvgW appears to transport cadmium, zinc and cobalt but not copper, out of the cell. Functions in metal ion resistance and cellular metal ion homeostasis. CadA/YvgW is also important for sporulation in B. subtilis, the significant specific expression of the cadA/yvgW gene during the late stage of sporulation, is controlled by forespore-specific sigma factor, sigma G, and mother cell-specific sigma factor, sigma E. This subfamily also includes Helicobacter pylori CadA an essential resistance pump with ion specificity towards Cd(2+), Zn(2+) and Co(2+), and Zn-transporting ATPase, ZiaA(N) in Synechocystis PCC 6803. Transcription of ziaA is induced by Zn under the control of the Zn responsive repressor ZiaR. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319847 [Multi-domain]  Cd Length: 604  Bit Score: 54.93  E-value: 7.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 115 AIEALKEYEPEMGKVIRSDrkGVQRIRARDIVPGDIVEVAVGDKVPADLRLIEIKSTtlrVDQSILTGESVsvtkhteai 194
Cdd:cd07548   99 SIKALLDIRPDYANLKRNN--ELKDVKPEEVQIGDIIVVKPGEKIPLDGVVLKGESF---LDTSALTGESV--------- 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 195 pdPRAVNQDKKnmLFSGTNITSGkAVGVAVATGL-HTELGKIRSQMAAVEPERTPLQRKLDEFGRQLSHAISVICVAVWV 273
Cdd:cd07548  165 --PVEVKEGSS--VLAGFINLNG-VLEIKVTKPFkDSAVAKILELVENASARKAPTEKFITKFARYYTPIVVFLALLLAV 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 274 I-----NIGHFADpahggsWL-RGAVYyfkiavalAVAAIPEGLpaVITTCLAL--GTRRMARKNAIVRSLPSVETLGCT 345
Cdd:cd07548  240 IpplfsPDGSFSD------WIyRALVF--------LVISCPCAL--VISIPLGYfgGIGAASRKGILIKGSNYLEALSQV 303
                        250
                 ....*....|....*...
gi 767992219 346 SVICSDKTGTLTTNQMSV 363
Cdd:cd07548  304 KTVVFDKTGTLTKGVFKV 321
P-type_ATPase_K cd02078
potassium-transporting ATPase ATP-binding subunit, KdpB, a subunit of the prokaryotic ...
117-363 2.59e-07

potassium-transporting ATPase ATP-binding subunit, KdpB, a subunit of the prokaryotic high-affinity potassium uptake system KdpFABC; similar to Escherichia coli KdpB; KdpFABC is a prokaryotic high-affinity potassium uptake system. It is expressed under K(+) limiting conditions when the other potassium transport systems are not able to provide a sufficient flow of K(+) into the bacteria. The KdpB subunit represents the catalytic subunit performing ATP hydrolysis. KdpB is comprised of four domains: the transmembrane domain, the nucleotide-binding domain, the phosphorylation domain, and the actuator domain. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319773 [Multi-domain]  Cd Length: 667  Bit Score: 53.42  E-value: 2.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 117 EALKEYEPE-MGKVIRSDRKgVQRIRARDIVPGDIVEVAVGDKVPADLRLIE-IKSttlrVDQSILTGESVSVTKhtEAI 194
Cdd:cd02078   86 DSLRKTKTEtQAKRLRNDGK-IEKVPATDLKKGDIVLVEAGDIIPADGEVIEgVAS----VDESAITGESAPVIR--ESG 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 195 PDPRAVNqdkknmlfSGTNITSGKAVGVAVATGLHTELGKIRSQMAAVEPERTPLQRKLDEFGRQLSHAISVICVAVWVI 274
Cdd:cd02078  159 GDRSSVT--------GGTKVLSDRIKVRITANPGETFLDRMIALVEGASRQKTPNEIALTILLVGLTLIFLIVVATLPPF 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 275 nighfadpahggswlrgAVYYfkiavalavaaipeGLPAVITTCLAL-------------------GTRRMARKNAIVRS 335
Cdd:cd02078  231 -----------------AEYS--------------GAPVSVTVLVALlvclipttiggllsaigiaGMDRLLRFNVIAKS 279
                        250       260
                 ....*....|....*....|....*....
gi 767992219 336 LPSVETLGCTSVICSDKTGTLTT-NQMSV 363
Cdd:cd02078  280 GRAVEAAGDVDTLLLDKTGTITLgNRQAT 308
P-type_ATPase_APLT_Dnf-like cd02073
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ...
128-496 2.43e-06

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: 50.25  E-value: 2.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 128 KVIRSDRKGVQRIRARDIVPGDIVEVAVGDKVPADLRL-----------IEIKS----TTLRVDQSILTGESVSVTKHTE 192
Cdd:cd02073   84 PVQVLRGGKFVKKKWKDIRVGDIVRVKNDEFVPADLLLlsssepdglcyVETANldgeTNLKIRQALPETALLLSEEDLA 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 193 A----------------------IPDPRAVNQDKKNMLFSGTNI-TSGKAVGVAVATGLHTEL----GKIRSQmaavepe 245
Cdd:cd02073  164 RfsgeieceqpnndlytfngtleLNGGRELPLSPDNLLLRGCTLrNTEWVYGVVVYTGHETKLmlnsGGTPLK------- 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 246 RTPLQRKLDE-----FGRQLSHA-ISVICVAVWVINIGHFA---DPAHGGSWLRGAVYYFKIAVALAVAAIPEGLPAVIT 316
Cdd:cd02073  237 RSSIEKKMNRfiiaiFCILIVMClISAIGKGIWLSKHGRDLwylLPKEERSPALEFFFDFLTFIILYNNLIPISLYVTIE 316
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 317 TCLALGTRRMA----------RKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSvcrmFVvaeadagscllhEFTISG 386
Cdd:cd02073  317 VVKFLQSFFINwdldmydeetDTPAEARTSNLNEELGQVEYIFSDKTGTLTENIME----FK------------KCSING 380
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 387 TTYtpegevrqgdqpvrcgQFdgLVELaticALCNdsaldyneakgvyekvgeatetalTCLVEKMNVFDTDL-QALSRV 465
Cdd:cd02073  381 VDY----------------GF--FLAL----ALCH------------------------TVVPEKDDHPGQLVyQASSPD 414
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767992219 466 ERA---GACN-----------TVIKQLM--RKEF----TLEFSRDRKSMSV 496
Cdd:cd02073  415 EAAlveAARDlgfvflsrtpdTVTINALgeEEEYeilhILEFNSDRKRMSV 465
PRK14010 PRK14010
K(+)-transporting ATPase subunit B;
92-393 3.45e-06

K(+)-transporting ATPase subunit B;


Pssm-ID: 184448 [Multi-domain]  Cd Length: 673  Bit Score: 49.70  E-value: 3.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219  92 LVIMLILVANAIVGVWQERNAESAIEALKEYEPEM-GKVIRSDrKGVQRIRARDIVPGDIVEVAVGDKVPADLRLIEIKS 170
Cdd:PRK14010  70 IILLLTLVFANFSEALAEGRGKAQANALRQTQTEMkARRIKQD-GSYEMIDASDLKKGHIVRVATGEQIPNDGKVIKGLA 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 171 TtlrVDQSILTGESVSVTKHTEAipdpravnqdKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMAAVEPERTPLQ 250
Cdd:PRK14010 149 T---VDESAITGESAPVIKESGG----------DFDNVIGGTSVASDWLEVEITSEPGHSFLDKMIGLVEGATRKKTPNE 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 251 RKLdeFGRQLSHAISVICVAVWVINIGHFadpahggswlrgavYYFKIAVALAVAAIPEGLPAVITTCLAL----GTRRM 326
Cdd:PRK14010 216 IAL--FTLLMTLTIIFLVVILTMYPLAKF--------------LNFNLSIAMLIALAVCLIPTTIGGLLSAigiaGMDRV 279
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767992219 327 ARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFVVAEADAGSCLLHEFTISGTTYTPEG 393
Cdd:PRK14010 280 TQFNILAKSGRSVETCGDVNVLILDKTGTITYGNRMADAFIPVKSSSFERLVKAAYESSIADDTPEG 346
P-type_ATPases cd01431
ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, ...
347-368 1.31e-05

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: 47.45  E-value: 1.31e-05
                         10        20
                 ....*....|....*....|..
gi 767992219 347 VICSDKTGTLTTNQMSVCRMFV 368
Cdd:cd01431    1 VICSDKTGTLTKNGMTVTKLFI 22
copA PRK10671
copper-exporting P-type ATPase CopA;
114-357 6.82e-05

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 45.89  E-value: 6.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 114 SAIEALKEYEPEMGKVIRSDrkGVQRIRARDIVPGDIVEVAVGDKVPADLrliEIKSTTLRVDQSILTGesvsvtkhtEA 193
Cdd:PRK10671 312 KALEKLLDLTPPTARVVTDE--GEKSVPLADVQPGMLLRLTTGDRVPVDG---EITQGEAWLDEAMLTG---------EP 377
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 194 IPDPRAVNqdkkNMLFSGTNITSGKAVGVAVATGLHTELGKI---RSQMAAVEPERTPLQRKLDEFGRQLSHAISVICVA 270
Cdd:PRK10671 378 IPQQKGEG----DSVHAGTVVQDGSVLFRASAVGSHTTLSRIirmVRQAQSSKPEIGQLADKISAVFVPVVVVIALVSAA 453
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219 271 VWvinigHFADPAhggswlRGAVYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMARKNAIVRSLPSVETLGCTSVICS 350
Cdd:PRK10671 454 IW-----YFFGPA------PQIVYTLVIATTVLIIACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTLVF 522

                 ....*..
gi 767992219 351 DKTGTLT 357
Cdd:PRK10671 523 DKTGTLT 529
ATPase-Plipid TIGR01652
phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase ...
47-498 4.99e-04

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: 43.14  E-value: 4.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219    47 KSLWElvleQFEDLLVRILLLAALVSFVLAWFEEGEETTTAfvePLVIMLILVAnaivgvwqernAESAIEALK------ 120
Cdd:TIGR01652   19 KNLFE----QFKRFANLYFLVVALLQQVPILSPTYRGTSIV---PLAFVLIVTA-----------IKEAIEDIRrrrrdk 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   121 EYEPEMGKVIRSDRKGVqRIRARDIVPGDIVEVAVGDKVPADLRL-----------IEIKS----TTLRVDQSI------ 179
Cdd:TIGR01652   81 EVNNRLTEVLEGHGQFV-EIPWKDLRVGDIVKVKKDERIPADLLLlsssepdgvcyVETANldgeTNLKLRQALeetqkm 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   180 --------LTGESVSVTKH--------TEAIPDPRAVNQDKKNMLFSGTNITSGK-AVGVAVATGLHTELGKIRSQmaav 242
Cdd:TIGR01652  160 ldeddiknFSGEIECEQPNaslysfqgNMTINGDRQYPLSPDNILLRGCTLRNTDwVIGVVVYTGHDTKLMRNATQ---- 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   243 eperTPLQRKLDEfgRQLSHAISVICVAVWVINI-----GHFADPAHGGSwlrgaVYYFKIAVALAVAAIPEGLPavITT 317
Cdd:TIGR01652  236 ----APSKRSRLE--KELNFLIIILFCLLFVLCLissvgAGIWNDAHGKD-----LWYIRLDVSERNAAANGFFS--FLT 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   318 CLAL-------------------------GTRRMARKN----AIVRSLPSVETLGCTSVICSDKTGTLTTNQMSvcrmFV 368
Cdd:TIGR01652  303 FLILfsslipislyvslelvksvqayfinSDLQMYHEKtdtpASVRTSNLNEELGQVEYIFSDKTGTLTQNIME----FK 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   369 VAeadagscllhefTISGTTYTpEGEVRQGDQPVRCGQFDGLVELATICALCNDSALDYNEAKGVY--EKVGEATETALT 446
Cdd:TIGR01652  379 KC------------SIAGVSYG-DGFTEIKDGIRERLGSYVENENSMLVESKGFTFVDPRLVDLLKtnKPNAKRINEFFL 445
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992219   447 CL---------VEKMNVFDTDLQALSRVERA-------------GACNTVIKQLMR-----KEF----TLEFSRDRKSMS 495
Cdd:TIGR01652  446 ALalchtvvpeFNDDGPEEITYQAASPDEAAlvkaardvgfvffERTPKSISLLIEmhgetKEYeilnVLEFNSDRKRMS 525

                   ...
gi 767992219   496 VYC 498
Cdd:TIGR01652  526 VIV 528
 
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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