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Conserved domains on  [gi|672085173|ref|XP_008770818|]
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calcium-transporting ATPase type 2C member 2 isoform X1 [Rattus norvegicus]

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

 Zoom to residue level

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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 ...
1-680 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 cd02085:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 804  Bit Score: 1151.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   1 MGTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLVGWVQGKPLLSMFTIG 80
Cdd:cd02085  166 MGTLVRCGHGKGIVIGTGENSEFGEVFKMMQAEEAPKTPLQKSMDKLGKQLSLYSFIIIGVIMLIGWLQGKNLLEMFTIG 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  81 VSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVTsdgfhaevsgi 160
Cdd:cd02085  246 VSLAVAAIPEGLPIVVTVTLALGVMRMAKRRAIVKKLPIVETLGCVNVICSDKTGTLTKNEMTVTKIVT----------- 314
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 161 gysgegtvcllpskevikefsnvsvgklveaGCVANNAVVRKNAVMGQPTEGALVVLAMKMNLGSIKDSYIRKKEIPFSS 240
Cdd:cd02085  315 -------------------------------GCVCNNAVIRNNTLMGQPTEGALIALAMKMGLSDIRETYIRKQEIPFSS 363
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 241 EQKWMAVRCSLK-NEDEEDVYFMKGAFEEVIHHCSTYNNGGIP-LPLTPQQKSYCQQEEKKMGSLGLRVLALASGPELGR 318
Cdd:cd02085  364 EQKWMAVKCIPKyNSDNEEIYFMKGALEQVLDYCTTYNSSDGSaLPLTQQQRSEINEEEKEMGSKGLRVLALASGPELGD 443
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 319 LTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLCDEKLKAMSGEEVEGMEQDALAARVRQVS 398
Cdd:cd02085  444 LTFLGLVGINDPPRPGVREAIQILLESGVRVKMITGDAQETAIAIGSSLGLYSPSLQALSGEEVDQMSDSQLASVVRKVT 523
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 399 VFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGQTGTDVSKEAADMILVDDDFSAIMSAVEEGKGI 478
Cdd:cd02085  524 VFYRASPRHKLKIVKALQKSGAVVAMTGDGVNDAVALKSADIGIAMGRTGTDVCKEAADMILVDDDFSTILAAIEEGKGI 603
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 479 FYNIKNFVRFQLSTSIAALSLITLSTVCNLPNPLNAMQILWVNIIMDGPPAQSLGVEPVDRDALKRPPRSVKDTILNRAL 558
Cdd:cd02085  604 FYNIKNFVRFQLSTSIAALSLIALSTLFNLPNPLNAMQILWINIIMDGPPAQSLGVEPVDKDVIRQPPRNVKDPILTRSL 683
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 559 ILKILMSAAVILGGTLFIFWREIPENRTsTPRTTTMAFTCFVFFDLFNALSCRSQTKLIFEIGFFRNRMFLYSILGSLLG 638
Cdd:cd02085  684 ILNVLLSAAIIVSGTLWVFWKEMSDDNV-TPRDTTMTFTCFVFFDMFNALSCRSQTKSIFEIGFFSNRMFLYAVGGSLIG 762
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|..
gi 672085173 639 QLAVIYAPPLQKVFQTENLSALDLLLLTGLASSVFILSELLK 680
Cdd:cd02085  763 QLLVIYFPPLQRVFQTEALGLLDLLFLLGLTSSVFIVSELRK 804
 
Name Accession Description Interval E-value
P-type_ATPase_SPCA cd02085
golgi-associated secretory pathway Ca(2+) transport ATPases, similar to human ATPase secretory ...
1-680 0e+00

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: 1151.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   1 MGTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLVGWVQGKPLLSMFTIG 80
Cdd:cd02085  166 MGTLVRCGHGKGIVIGTGENSEFGEVFKMMQAEEAPKTPLQKSMDKLGKQLSLYSFIIIGVIMLIGWLQGKNLLEMFTIG 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  81 VSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVTsdgfhaevsgi 160
Cdd:cd02085  246 VSLAVAAIPEGLPIVVTVTLALGVMRMAKRRAIVKKLPIVETLGCVNVICSDKTGTLTKNEMTVTKIVT----------- 314
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 161 gysgegtvcllpskevikefsnvsvgklveaGCVANNAVVRKNAVMGQPTEGALVVLAMKMNLGSIKDSYIRKKEIPFSS 240
Cdd:cd02085  315 -------------------------------GCVCNNAVIRNNTLMGQPTEGALIALAMKMGLSDIRETYIRKQEIPFSS 363
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 241 EQKWMAVRCSLK-NEDEEDVYFMKGAFEEVIHHCSTYNNGGIP-LPLTPQQKSYCQQEEKKMGSLGLRVLALASGPELGR 318
Cdd:cd02085  364 EQKWMAVKCIPKyNSDNEEIYFMKGALEQVLDYCTTYNSSDGSaLPLTQQQRSEINEEEKEMGSKGLRVLALASGPELGD 443
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 319 LTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLCDEKLKAMSGEEVEGMEQDALAARVRQVS 398
Cdd:cd02085  444 LTFLGLVGINDPPRPGVREAIQILLESGVRVKMITGDAQETAIAIGSSLGLYSPSLQALSGEEVDQMSDSQLASVVRKVT 523
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 399 VFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGQTGTDVSKEAADMILVDDDFSAIMSAVEEGKGI 478
Cdd:cd02085  524 VFYRASPRHKLKIVKALQKSGAVVAMTGDGVNDAVALKSADIGIAMGRTGTDVCKEAADMILVDDDFSTILAAIEEGKGI 603
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 479 FYNIKNFVRFQLSTSIAALSLITLSTVCNLPNPLNAMQILWVNIIMDGPPAQSLGVEPVDRDALKRPPRSVKDTILNRAL 558
Cdd:cd02085  604 FYNIKNFVRFQLSTSIAALSLIALSTLFNLPNPLNAMQILWINIIMDGPPAQSLGVEPVDKDVIRQPPRNVKDPILTRSL 683
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 559 ILKILMSAAVILGGTLFIFWREIPENRTsTPRTTTMAFTCFVFFDLFNALSCRSQTKLIFEIGFFRNRMFLYSILGSLLG 638
Cdd:cd02085  684 ILNVLLSAAIIVSGTLWVFWKEMSDDNV-TPRDTTMTFTCFVFFDMFNALSCRSQTKSIFEIGFFSNRMFLYAVGGSLIG 762
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|..
gi 672085173 639 QLAVIYAPPLQKVFQTENLSALDLLLLTGLASSVFILSELLK 680
Cdd:cd02085  763 QLLVIYFPPLQRVFQTEALGLLDLLFLLGLTSSVFIVSELRK 804
ATPase-IIA2_Ca TIGR01522
golgi membrane calcium-translocating P-type ATPase; This model describes the P-type ATPase ...
1-684 0e+00

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: 950.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173    1 MGTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLVGWVQGKPLLSMFTIG 80
Cdd:TIGR01522 199 MGTLVRCGHGKGIVVGTGSNTEFGAVFKMMQAIEKPKTPLQKSMDLLGKQLSLVSFGVIGVICLVGWFQGKDWLEMFTIS 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   81 VSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVTSDGFHAEVSGI 160
Cdd:TIGR01522 279 VSLAVAAIPEGLPIIVTVTLALGVLRMSKKRAIVRKLPSVETLGSVNVICSDKTGTLTKNHMTVTKIWTSDGLHTMLNAV 358
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  161 GYSGEGTVclLPSKEVIKEFSNVSVGKLVEAGCVANNAVVRKNA--VMGQPTEGALVVLAMKMNLGSIKDSYIRKKEIPF 238
Cdd:TIGR01522 359 SLNQFGEV--IVDGDVLHGFYTVAVSRILEAGNLCNNAKFRNEAdtLLGNPTDVALIELLMKFGLDDLRETYIRVAEVPF 436
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  239 SSEQKWMAVRCsLKNEDEEDVYFMKGAFEEVIHHCSTY-NNGGIPLPLTPQQKSYCQQEEKKMGSLGLRVLALASGPELG 317
Cdd:TIGR01522 437 SSERKWMAVKC-VHRQDRSEMCFMKGAYEQVLKYCTYYqKKDGKTLTLTQQQRDVIQEEAAEMASAGLRVIAFASGPEKG 515
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  318 RLTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLCDEKLKAMSGEEVEGMEQDALAARVRQV 397
Cdd:TIGR01522 516 QLTFLGLVGINDPPRPGVKEAVTTLITGGVRIIMITGDSQETAVSIARRLGMPSKTSQSVSGEKLDAMDDQQLSQIVPKV 595
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  398 SVFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGQTGTDVSKEAADMILVDDDFSAIMSAVEEGKG 477
Cdd:TIGR01522 596 AVFARASPEHKMKIVKALQKRGDVVAMTGDGVNDAPALKLADIGVAMGQTGTDVAKEAADMILTDDDFATILSAIEEGKG 675
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  478 IFYNIKNFVRFQLSTSIAALSLITLSTVCNLPNPLNAMQILWVNIIMDGPPAQSLGVEPVDRDALKRPPRSVKDTILNRA 557
Cdd:TIGR01522 676 IFNNIKNFITFQLSTSVAALSLIALATLMGFPNPLNAMQILWINILMDGPPAQSLGVEPVDKDVMRKPPRPRNDKILTKD 755
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  558 LILKILMSAAVILGGTLFIFWREIPENRTsTPRTTTMAFTCFVFFDLFNALSCRSQTKLIFEIGFFRNRMFLYSILGSLL 637
Cdd:TIGR01522 756 LIKKILVSAIIIVVGTLFVFVREMQDGVI-TARDTTMTFTCFVFFDMFNALACRSQTKSVFEIGFFSNRMFNYAVGGSII 834
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*..
gi 672085173  638 GQLAVIYAPPLQKVFQTENLSALDLLLLTGLASSVFILSELLKLCEK 684
Cdd:TIGR01522 835 GQLLVIYFPPLQSVFQTEALSIKDLLFLLLITSSVCIVDEIRKKVER 881
MgtA COG0474
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism];
1-681 0e+00

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


Pssm-ID: 440242 [Multi-domain]  Cd Length: 874  Bit Score: 756.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   1 MGTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLVGWVQGKPLLSMFTIG 80
Cdd:COG0474  198 MGTLVTSGRGTAVVVATGMNTEFGKIAKLLQEAEEEKTPLQKQLDRLGKLLAIIALVLAALVFLIGLLRGGPLLEALLFA 277
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  81 VSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVTSDGFHaEVSGi 160
Cdd:COG0474  278 VALAVAAIPEGLPAVVTITLALGAQRMAKRNAIVRRLPAVETLGSVTVICTDKTGTLTQNKMTVERVYTGGGTY-EVTG- 355
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 161 gysgegtvcllpskevikeFSNVSVGKLVEAGCVANNAVVRKNAVMGQPTEGALVVLAMKMNLG--SIKDSYIRKKEIPF 238
Cdd:COG0474  356 -------------------EFDPALEELLRAAALCSDAQLEEETGLGDPTEGALLVAAAKAGLDveELRKEYPRVDEIPF 416
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 239 SSEQKWMAVRCslKNEDEEDVYFMKGAFEEVIHHCSTYNNGGIPLPLTPQQKSYCQQEEKKMGSLGLRVLALA-----SG 313
Cdd:COG0474  417 DSERKRMSTVH--EDPDGKRLLIVKGAPEVVLALCTRVLTGGGVVPLTEEDRAEILEAVEELAAQGLRVLAVAykelpAD 494
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 314 PELGR------LTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLCDEKLKAMSGEEVEGMEQ 387
Cdd:COG0474  495 PELDSeddesdLTFLGLVGMIDPPRPEAKEAIAECRRAGIRVKMITGDHPATARAIARQLGLGDDGDRVLTGAELDAMSD 574
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 388 DALAARVRQVSVFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGQTGTDVSKEAADMILVDDDFSA 467
Cdd:COG0474  575 EELAEAVEDVDVFARVSPEHKLRIVKALQANGHVVAMTGDGVNDAPALKAADIGIAMGITGTDVAKEAADIVLLDDNFAT 654
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 468 IMSAVEEGKGIFYNIKNFVRFQLSTSIAALSLITLSTVCNLPNPLNAMQILWVNIIMDGPPAQSLGVEPVDRDALKRPPR 547
Cdd:COG0474  655 IVAAVEEGRRIYDNIRKFIKYLLSSNFGEVLSVLLASLLGLPLPLTPIQILWINLVTDGLPALALGFEPVEPDVMKRPPR 734
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 548 SVKDTILNRALILKILMSAAVILGGTLFIFWREIPENRtSTPRTTTMAFTCFVFFDLFNALSCRSQTKLIFEIGFFRNRM 627
Cdd:COG0474  735 WPDEPILSRFLLLRILLLGLLIAIFTLLTFALALARGA-SLALARTMAFTTLVLSQLFNVFNCRSERRSFFKSGLFPNRP 813
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....
gi 672085173 628 FLYSILGSLLGQLAVIYAPPLQKVFQTENLSALDLLLLTGLASSVFILSELLKL 681
Cdd:COG0474  814 LLLAVLLSLLLQLLLIYVPPLQALFGTVPLPLSDWLLILGLALLYLLLVELVKL 867
PRK10517 PRK10517
magnesium-transporting P-type ATPase MgtA;
1-547 1.60e-66

magnesium-transporting P-type ATPase MgtA;


Pssm-ID: 236705 [Multi-domain]  Cd Length: 902  Bit Score: 235.73  E-value: 1.60e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   1 MGTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLV-GWVQGKpLLSMFTI 79
Cdd:PRK10517 246 MGTNVVSGTAQAVVIATGANTWFGQLAGRVSEQDSEPNAFQQGISRVSWLLIRFMLVMAPVVLLInGYTKGD-WWEAALF 324
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  80 GVSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQlvtsdgfHAEVSG 159
Cdd:PRK10517 325 ALSVAVGLTPEMLPMIVTSTLARGAVKLSKQKVIVKRLDAIQNFGAMDILCTDKTGTLTQDKIVLEN-------HTDISG 397
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 160 IgysgegtvcllPSKEVIKEF---SNVSVGklveagcvannavvRKN----AVMgqptEGalVVLAMKMNLGSikdSYIR 232
Cdd:PRK10517 398 K-----------TSERVLHSAwlnSHYQTG--------------LKNlldtAVL----EG--VDEESARSLAS---RWQK 443
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 233 KKEIPFSSEQKWMAVRCSlkneDEEDVYFM--KGAFEEVIHHCSTYNNGGIPLPLTPQQKSYCQQEEKKMGSLGLRVLAL 310
Cdd:PRK10517 444 IDEIPFDFERRRMSVVVA----ENTEHHQLicKGALEEILNVCSQVRHNGEIVPLDDIMLRRIKRVTDTLNRQGLRVVAV 519
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 311 ASGP------ELGR-----LTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLcdEKLKAMSG 379
Cdd:PRK10517 520 ATKYlparegDYQRadesdLILEGYIAFLDPPKETTAPALKALKASGVTVKILTGDSELVAAKVCHEVGL--DAGEVLIG 597
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 380 EEVEGMEQDALAARVRQVSVFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMgQTGTDVSKEAADMI 459
Cdd:PRK10517 598 SDIETLSDDELANLAERTTLFARLTPMHKERIVTLLKREGHVVGFMGDGINDAPALRAADIGISV-DGAVDIAREAADII 676
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 460 LVDDDFSAIMSAVEEGKGIFYNIKNFVRFQLSTSIA-ALSLITLSTVcnLPN-PLNAMQILWVNIIMDgpPAQ-SLGVEP 536
Cdd:PRK10517 677 LLEKSLMVLEEGVIEGRRTFANMLKYIKMTASSNFGnVFSVLVASAF--LPFlPMLPLHLLIQNLLYD--VSQvAIPFDN 752
                        570
                 ....*....|.
gi 672085173 537 VDRDALKRPPR 547
Cdd:PRK10517 753 VDDEQIQKPQR 763
Cation_ATPase_C pfam00689
Cation transporting ATPase, C-terminus; Members of this families are involved in Na+/K+, H+/K+, ...
509-681 1.55e-47

Cation transporting ATPase, C-terminus; Members of this families are involved in Na+/K+, H+/K+, Ca++ and Mg++ transport. This family represents 5 transmembrane helices.


Pssm-ID: 376368 [Multi-domain]  Cd Length: 175  Bit Score: 165.49  E-value: 1.55e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  509 PNPLNAMQILWVNIIMDGPPAQSLGVEPVDRDALKRPPRSVKDTILNRALILKILMSAAVILGGTLFIFW-----REIPE 583
Cdd:pfam00689   1 PLPLTPIQILWINLVTDGLPALALGFEPPEPDLMKRPPRKPKEPLFSRKMLRRILLQGLLIAILTLLVFFlgllgFGISE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  584 NRTstprTTTMAFTCFVFFDLFNALSCRSQTKLIFEIGFFRNRMFLYSILGSLLGQLAVIYAPPLQKVFQTENLSALDLL 663
Cdd:pfam00689  81 SQN----AQTMAFNTLVLSQLFNALNARSLRRSLFKIGLFSNKLLLLAILLSLLLQLLIIYVPPLQAVFGTTPLSLEQWL 156
                         170
                  ....*....|....*...
gi 672085173  664 LLTGLASSVFILSELLKL 681
Cdd:pfam00689 157 IVLLLALVVLLVVELRKL 174
 
Name Accession Description Interval E-value
P-type_ATPase_SPCA cd02085
golgi-associated secretory pathway Ca(2+) transport ATPases, similar to human ATPase secretory ...
1-680 0e+00

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: 1151.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   1 MGTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLVGWVQGKPLLSMFTIG 80
Cdd:cd02085  166 MGTLVRCGHGKGIVIGTGENSEFGEVFKMMQAEEAPKTPLQKSMDKLGKQLSLYSFIIIGVIMLIGWLQGKNLLEMFTIG 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  81 VSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVTsdgfhaevsgi 160
Cdd:cd02085  246 VSLAVAAIPEGLPIVVTVTLALGVMRMAKRRAIVKKLPIVETLGCVNVICSDKTGTLTKNEMTVTKIVT----------- 314
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 161 gysgegtvcllpskevikefsnvsvgklveaGCVANNAVVRKNAVMGQPTEGALVVLAMKMNLGSIKDSYIRKKEIPFSS 240
Cdd:cd02085  315 -------------------------------GCVCNNAVIRNNTLMGQPTEGALIALAMKMGLSDIRETYIRKQEIPFSS 363
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 241 EQKWMAVRCSLK-NEDEEDVYFMKGAFEEVIHHCSTYNNGGIP-LPLTPQQKSYCQQEEKKMGSLGLRVLALASGPELGR 318
Cdd:cd02085  364 EQKWMAVKCIPKyNSDNEEIYFMKGALEQVLDYCTTYNSSDGSaLPLTQQQRSEINEEEKEMGSKGLRVLALASGPELGD 443
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 319 LTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLCDEKLKAMSGEEVEGMEQDALAARVRQVS 398
Cdd:cd02085  444 LTFLGLVGINDPPRPGVREAIQILLESGVRVKMITGDAQETAIAIGSSLGLYSPSLQALSGEEVDQMSDSQLASVVRKVT 523
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 399 VFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGQTGTDVSKEAADMILVDDDFSAIMSAVEEGKGI 478
Cdd:cd02085  524 VFYRASPRHKLKIVKALQKSGAVVAMTGDGVNDAVALKSADIGIAMGRTGTDVCKEAADMILVDDDFSTILAAIEEGKGI 603
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 479 FYNIKNFVRFQLSTSIAALSLITLSTVCNLPNPLNAMQILWVNIIMDGPPAQSLGVEPVDRDALKRPPRSVKDTILNRAL 558
Cdd:cd02085  604 FYNIKNFVRFQLSTSIAALSLIALSTLFNLPNPLNAMQILWINIIMDGPPAQSLGVEPVDKDVIRQPPRNVKDPILTRSL 683
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 559 ILKILMSAAVILGGTLFIFWREIPENRTsTPRTTTMAFTCFVFFDLFNALSCRSQTKLIFEIGFFRNRMFLYSILGSLLG 638
Cdd:cd02085  684 ILNVLLSAAIIVSGTLWVFWKEMSDDNV-TPRDTTMTFTCFVFFDMFNALSCRSQTKSIFEIGFFSNRMFLYAVGGSLIG 762
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|..
gi 672085173 639 QLAVIYAPPLQKVFQTENLSALDLLLLTGLASSVFILSELLK 680
Cdd:cd02085  763 QLLVIYFPPLQRVFQTEALGLLDLLFLLGLTSSVFIVSELRK 804
ATPase-IIA2_Ca TIGR01522
golgi membrane calcium-translocating P-type ATPase; This model describes the P-type ATPase ...
1-684 0e+00

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: 950.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173    1 MGTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLVGWVQGKPLLSMFTIG 80
Cdd:TIGR01522 199 MGTLVRCGHGKGIVVGTGSNTEFGAVFKMMQAIEKPKTPLQKSMDLLGKQLSLVSFGVIGVICLVGWFQGKDWLEMFTIS 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   81 VSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVTSDGFHAEVSGI 160
Cdd:TIGR01522 279 VSLAVAAIPEGLPIIVTVTLALGVLRMSKKRAIVRKLPSVETLGSVNVICSDKTGTLTKNHMTVTKIWTSDGLHTMLNAV 358
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  161 GYSGEGTVclLPSKEVIKEFSNVSVGKLVEAGCVANNAVVRKNA--VMGQPTEGALVVLAMKMNLGSIKDSYIRKKEIPF 238
Cdd:TIGR01522 359 SLNQFGEV--IVDGDVLHGFYTVAVSRILEAGNLCNNAKFRNEAdtLLGNPTDVALIELLMKFGLDDLRETYIRVAEVPF 436
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  239 SSEQKWMAVRCsLKNEDEEDVYFMKGAFEEVIHHCSTY-NNGGIPLPLTPQQKSYCQQEEKKMGSLGLRVLALASGPELG 317
Cdd:TIGR01522 437 SSERKWMAVKC-VHRQDRSEMCFMKGAYEQVLKYCTYYqKKDGKTLTLTQQQRDVIQEEAAEMASAGLRVIAFASGPEKG 515
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  318 RLTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLCDEKLKAMSGEEVEGMEQDALAARVRQV 397
Cdd:TIGR01522 516 QLTFLGLVGINDPPRPGVKEAVTTLITGGVRIIMITGDSQETAVSIARRLGMPSKTSQSVSGEKLDAMDDQQLSQIVPKV 595
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  398 SVFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGQTGTDVSKEAADMILVDDDFSAIMSAVEEGKG 477
Cdd:TIGR01522 596 AVFARASPEHKMKIVKALQKRGDVVAMTGDGVNDAPALKLADIGVAMGQTGTDVAKEAADMILTDDDFATILSAIEEGKG 675
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  478 IFYNIKNFVRFQLSTSIAALSLITLSTVCNLPNPLNAMQILWVNIIMDGPPAQSLGVEPVDRDALKRPPRSVKDTILNRA 557
Cdd:TIGR01522 676 IFNNIKNFITFQLSTSVAALSLIALATLMGFPNPLNAMQILWINILMDGPPAQSLGVEPVDKDVMRKPPRPRNDKILTKD 755
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  558 LILKILMSAAVILGGTLFIFWREIPENRTsTPRTTTMAFTCFVFFDLFNALSCRSQTKLIFEIGFFRNRMFLYSILGSLL 637
Cdd:TIGR01522 756 LIKKILVSAIIIVVGTLFVFVREMQDGVI-TARDTTMTFTCFVFFDMFNALACRSQTKSVFEIGFFSNRMFNYAVGGSII 834
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*..
gi 672085173  638 GQLAVIYAPPLQKVFQTENLSALDLLLLTGLASSVFILSELLKLCEK 684
Cdd:TIGR01522 835 GQLLVIYFPPLQSVFQTEALSIKDLLFLLLITSSVCIVDEIRKKVER 881
MgtA COG0474
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism];
1-681 0e+00

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


Pssm-ID: 440242 [Multi-domain]  Cd Length: 874  Bit Score: 756.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   1 MGTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLVGWVQGKPLLSMFTIG 80
Cdd:COG0474  198 MGTLVTSGRGTAVVVATGMNTEFGKIAKLLQEAEEEKTPLQKQLDRLGKLLAIIALVLAALVFLIGLLRGGPLLEALLFA 277
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  81 VSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVTSDGFHaEVSGi 160
Cdd:COG0474  278 VALAVAAIPEGLPAVVTITLALGAQRMAKRNAIVRRLPAVETLGSVTVICTDKTGTLTQNKMTVERVYTGGGTY-EVTG- 355
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 161 gysgegtvcllpskevikeFSNVSVGKLVEAGCVANNAVVRKNAVMGQPTEGALVVLAMKMNLG--SIKDSYIRKKEIPF 238
Cdd:COG0474  356 -------------------EFDPALEELLRAAALCSDAQLEEETGLGDPTEGALLVAAAKAGLDveELRKEYPRVDEIPF 416
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 239 SSEQKWMAVRCslKNEDEEDVYFMKGAFEEVIHHCSTYNNGGIPLPLTPQQKSYCQQEEKKMGSLGLRVLALA-----SG 313
Cdd:COG0474  417 DSERKRMSTVH--EDPDGKRLLIVKGAPEVVLALCTRVLTGGGVVPLTEEDRAEILEAVEELAAQGLRVLAVAykelpAD 494
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 314 PELGR------LTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLCDEKLKAMSGEEVEGMEQ 387
Cdd:COG0474  495 PELDSeddesdLTFLGLVGMIDPPRPEAKEAIAECRRAGIRVKMITGDHPATARAIARQLGLGDDGDRVLTGAELDAMSD 574
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 388 DALAARVRQVSVFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGQTGTDVSKEAADMILVDDDFSA 467
Cdd:COG0474  575 EELAEAVEDVDVFARVSPEHKLRIVKALQANGHVVAMTGDGVNDAPALKAADIGIAMGITGTDVAKEAADIVLLDDNFAT 654
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 468 IMSAVEEGKGIFYNIKNFVRFQLSTSIAALSLITLSTVCNLPNPLNAMQILWVNIIMDGPPAQSLGVEPVDRDALKRPPR 547
Cdd:COG0474  655 IVAAVEEGRRIYDNIRKFIKYLLSSNFGEVLSVLLASLLGLPLPLTPIQILWINLVTDGLPALALGFEPVEPDVMKRPPR 734
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 548 SVKDTILNRALILKILMSAAVILGGTLFIFWREIPENRtSTPRTTTMAFTCFVFFDLFNALSCRSQTKLIFEIGFFRNRM 627
Cdd:COG0474  735 WPDEPILSRFLLLRILLLGLLIAIFTLLTFALALARGA-SLALARTMAFTTLVLSQLFNVFNCRSERRSFFKSGLFPNRP 813
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....
gi 672085173 628 FLYSILGSLLGQLAVIYAPPLQKVFQTENLSALDLLLLTGLASSVFILSELLKL 681
Cdd:COG0474  814 LLLAVLLSLLLQLLLIYVPPLQALFGTVPLPLSDWLLILGLALLYLLLVELVKL 867
P-type_ATPase_cation cd02080
P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, ...
1-680 0e+00

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: 569.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   1 MGTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLVG-WVQGKPLLSMFTI 79
Cdd:cd02080  173 SGTLVTAGSATGVVVATGADTEIGRINQLLAEVEQLATPLTRQIAKFSKALLIVILVLAALTFVFGlLRGDYSLVELFMA 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  80 GVSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVTsdgfhaevsg 159
Cdd:cd02080  253 VVALAVAAIPEGLPAVITITLAIGVQRMAKRNAIIRRLPAVETLGSVTVICSDKTGTLTRNEMTVQAIVT---------- 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 160 igysgegtvcllpskevikefsnvsvgklveagcVANNAVVRKN----AVMGQPTEGALVVLAMKMNL--GSIKDSYIRK 233
Cdd:cd02080  323 ----------------------------------LCNDAQLHQEdghwKITGDPTEGALLVLAAKAGLdpDRLASSYPRV 368
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 234 KEIPFSSEQKWMAVrcsLKNEDEEDVYFMKGAFEEVIHHCSTYNNGGIPLPLtpqQKSYCQQEEKKMGSLGLRVLALASG 313
Cdd:cd02080  369 DKIPFDSAYRYMAT---LHRDDGQRVIYVKGAPERLLDMCDQELLDGGVSPL---DRAYWEAEAEDLAKQGLRVLAFAYR 442
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 314 PE------------LGRLTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLCDEKlKAMSGEE 381
Cdd:cd02080  443 EVdseveeidhadlEGGLTFLGLQGMIDPPRPEAIAAVAECQSAGIRVKMITGDHAETARAIGAQLGLGDGK-KVLTGAE 521
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 382 VEGMEQDALAARVRQVSVFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGQTGTDVSKEAADMILV 461
Cdd:cd02080  522 LDALDDEELAEAVDEVDVFARTSPEHKLRLVRALQARGEVVAMTGDGVNDAPALKQADIGIAMGIKGTEVAKEAADMVLA 601
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 462 DDDFSAIMSAVEEGKGIFYNIKNFVRFQLSTSIAALSLITLSTVCNLPNPLNAMQILWVNIIMDGPPAQSLGVEPVDRDA 541
Cdd:cd02080  602 DDNFATIAAAVEEGRRVYDNLKKFILFTLPTNLGEGLVIIVAILFGVTLPLTPVQILWINMVTAITLGLALAFEPAEPGI 681
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 542 LKRPPRSVKDTILNRALILKILMSAAVILGGTLFIFWREIPeNRTSTPRTTTMAFTCFVFFDLFNALSCRSQTKLIFEIG 621
Cdd:cd02080  682 MKRPPRDPSEPLLSRELIWRILLVSLLMLGGAFGLFLWALD-RGYSLETARTMAVNTIVVAQIFYLFNCRSLHRSILKLG 760
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 672085173 622 FFRNRMFLYSILGSLLGQLAVIYAPPLQKVFQTENLSALDLLLLTGLASSVFILSELLK 680
Cdd:cd02080  761 VFSNKILFLGIGALILLQLAFTYLPFMNSLFGTAPIDLVDWAIILLVGIVVFIVVELEK 819
P-type_ATPase_Ca_prok cd02089
prokaryotic P-type Ca(2+)-ATPase similar to Synechococcus elongatus sp. strain PCC 7942 PacL ...
1-547 0e+00

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: 550.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   1 MGTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLVGWVQGKPLLSMFTIG 80
Cdd:cd02089  174 SGTLVTYGRGRAVVTATGMNTEMGKIATLLEETEEEKTPLQKRLDQLGKRLAIAALIICALVFALGLLRGEDLLDMLLTA 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  81 VSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVTsdgfhaevsgi 160
Cdd:cd02089  254 VSLAVAAIPEGLPAIVTIVLALGVQRMAKRNAIIRKLPAVETLGSVSVICSDKTGTLTQNKMTVEKIYT----------- 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 161 gysgegtvcllpskevikefsnvsvgklveagcvannavvrknavMGQPTEGALVVLAMKMNLG--SIKDSYIRKKEIPF 238
Cdd:cd02089  323 ---------------------------------------------IGDPTETALIRAARKAGLDkeELEKKYPRIAEIPF 357
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 239 SSEQKWMAVrcslKNEDEEDVY-FMKGAFEEVIHHCSTYNNGGIPLPLTPQQKSYCQQEEKKMGSLGLRVLALA------ 311
Cdd:cd02089  358 DSERKLMTT----VHKDAGKYIvFTKGAPDVLLPRCTYIYINGQVRPLTEEDRAKILAVNEEFSEEALRVLAVAykplde 433
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 312 ----SGPELGR-LTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLCDEKLKAMSGEEVEGME 386
Cdd:cd02089  434 dpteSSEDLENdLIFLGLVGMIDPPRPEVKDAVAECKKAGIKTVMITGDHKLTARAIAKELGILEDGDKALTGEELDKMS 513
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 387 QDALAARVRQVSVFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGQTGTDVSKEAADMILVDDDFS 466
Cdd:cd02089  514 DEELEKKVEQISVYARVSPEHKLRIVKALQRKGKIVAMTGDGVNDAPALKAADIGVAMGITGTDVAKEAADMILTDDNFA 593
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 467 AIMSAVEEGKGIFYNIKNFVRFQLSTSIAALSLITLSTVCNLPNPLNAMQILWVNIIMDGPPAQSLGVEPVDRDALKRPP 546
Cdd:cd02089  594 TIVAAVEEGRTIYDNIRKFIRYLLSGNVGEILTMLLAPLLGWPVPLLPIQLLWINLLTDGLPALALGVEPAEPDIMDRKP 673

                 .
gi 672085173 547 R 547
Cdd:cd02089  674 R 674
P-type_ATPase_SERCA cd02083
sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; ...
2-688 2.39e-167

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: 505.67  E-value: 2.39e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   2 GTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLV------------GWVQ 69
Cdd:cd02083  206 GTNVAAGKARGVVVGTGLNTEIGKIRDEMAETEEEKTPLQQKLDEFGEQLSKVISVICVAVWAInighfndpahggSWIK 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  70 GKplLSMFTIGVSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVT 149
Cdd:cd02083  286 GA--IYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVSRMFI 363
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 150 SDGFHA-------EVSGIGYSGEGTVCLLPSKEVIKEFSNVsvGKLVEAGCVANNAVVRKNAV------MGQPTEGALVV 216
Cdd:cd02083  364 LDKVEDdsslnefEVTGSTYAPEGEVFKNGKKVKAGQYDGL--VELATICALCNDSSLDYNESkgvyekVGEATETALTV 441
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 217 LAMKMNL-------GSIKD------SYIR---KKE--IPFSSEQKWMAVRCSLKNEDEEDVYFMKGAFEEVIHHCS-TYN 277
Cdd:cd02083  442 LVEKMNVfntdksgLSKREranacnDVIEqlwKKEftLEFSRDRKSMSVYCSPTKASGGNKLFVKGAPEGVLERCThVRV 521
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 278 NGGIPLPLTPQQKSYCQQEEKKMGSLGLRVLALASGPELGR------------------LTFLGLVGIIDPPRAGVKEAV 339
Cdd:cd02083  522 GGGKVVPLTAAIKILILKKVWGYGTDTLRCLALATKDTPPKpedmdledstkfykyetdLTFVGVVGMLDPPRPEVRDSI 601
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 340 QALSESDVSVKMVTGDALETALAIGRTIGL----CDEKLKAMSGEEVEGMEQDALAARVRQVSVFFRTSPKHKVKIIKAL 415
Cdd:cd02083  602 EKCRDAGIRVIVITGDNKGTAEAICRRIGIfgedEDTTGKSYTGREFDDLSPEEQREACRRARLFSRVEPSHKSKIVELL 681
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 416 QESGAIVAMTGDGVNDSVALKSADIGIAMGqTGTDVSKEAADMILVDDDFSAIMSAVEEGKGIFYNIKNFVRFQLSTSIA 495
Cdd:cd02083  682 QSQGEITAMTGDGVNDAPALKKAEIGIAMG-SGTAVAKSASDMVLADDNFATIVAAVEEGRAIYNNMKQFIRYLISSNIG 760
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 496 ALSLITLSTVCNLPNPLNAMQILWVNIIMDGPPAQSLGVEPVDRDALKRPPRSVKDTILN-----RALILKILMSAAVIL 570
Cdd:cd02083  761 EVVSIFLTAALGLPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMKKPPRKPDEPLISgwlffRYLAIGTYVGLATVG 840
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 571 G----------GTLFIFWR--------EIPENRT-------STPRTTTMAFTCFVFFDLFNALSCRSQTKLIFEIGFFRN 625
Cdd:cd02083  841 AfawwfmyyeeGPQVSFYQlthfmqcsSWEPNFEgvdceifEDPHPMTMALSVLVVIEMFNALNSLSENQSLLVMPPWSN 920
                        730       740       750       760       770       780
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672085173 626 RMFLYSILGSLLGQLAVIYAPPLQKVFQTENLSALDLLLLTGLASSVFILSELLklceKFCSR 688
Cdd:cd02083  921 PWLVGAIALSMALHFVILYVPPLATIFQITPLSFAEWIAVIKISLPVILLDELL----KFIAR 979
ATPase-IIA1_Ca TIGR01116
sarco/endoplasmic reticulum calcium-translocating P-type ATPase; This model describes the ...
2-681 3.57e-152

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: 464.64  E-value: 3.57e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173    2 GTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTvfsfGIIGLLMLVGWVQG----------- 70
Cdd:TIGR01116 155 GTLVVAGKARGVVVRTGMSTEIGKIRDEMRAAEQEDTPLQKKLDEFGELLS----KVIGLICILVWVINighfndpalgg 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   71 ---KPLLSMFTIGVSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQL 147
Cdd:TIGR01116 231 gwiQGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRKMAKKNAIVRKLPSVETLGCTTVICSDKTGTLTTNQMSVCKV 310
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  148 VTSDGFHAEVSGigYSGEGTVcLLPSKEVIKEFSNVSVGK---LVEAGCVA---NNAVV----RKNAV--MGQPTEGALV 215
Cdd:TIGR01116 311 VALDPSSSSLNE--FCVTGTT-YAPEGGVIKDDGPVAGGQdagLEELATIAalcNDSSLdfneRKGVYekVGEATEAALK 387
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  216 VLAMKMNLGS------------------IKDSYIRKKEIPFSSEQKWMAVRCSlknEDEEDVYFMKGAFEEVIHHCSTYN 277
Cdd:TIGR01116 388 VLVEKMGLPAtkngvsskrrpalgcnsvWNDKFKKLATLEFSRDRKSMSVLCK---PSTGNKLFVKGAPEGVLERCTHIL 464
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  278 NG-GIPLPLTPQQKSYCQQEEKKMGSL-GLRVLALASGPELGR------------------LTFLGLVGIIDPPRAGVKE 337
Cdd:TIGR01116 465 NGdGRAVPLTDKMKNTILSVIKEMGTTkALRCLALAFKDIPDPreedllsdpanfeaiesdLTFIGVVGMLDPPRPEVAD 544
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  338 AVQALSESDVSVKMVTGDALETALAIGRTIGL----CDEKLKAMSGEEVEGMEQDALAARVRQVSVFFRTSPKHKVKIIK 413
Cdd:TIGR01116 545 AIEKCRTAGIRVIMITGDNKETAEAICRRIGIfspdEDVTFKSFTGREFDEMGPAKQRAACRSAVLFSRVEPSHKSELVE 624
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  414 ALQESGAIVAMTGDGVNDSVALKSADIGIAMGqTGTDVSKEAADMILVDDDFSAIMSAVEEGKGIFYNIKNFVRFQLSTS 493
Cdd:TIGR01116 625 LLQEQGEIVAMTGDGVNDAPALKKADIGIAMG-SGTEVAKEASDMVLADDNFATIVAAVEEGRAIYNNMKQFIRYMISSN 703
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  494 IAALSLITLSTVCNLPNPLNAMQILWVNIIMDGPPAQSLGVEPVDRDALKRPPRSVKDTILN-----RALILKILMSAAV 568
Cdd:TIGR01116 704 IGEVVCIFLTAALGIPEGLIPVQLLWVNLVTDGLPATALGFNPPDKDIMWKPPRRPDEPLITgwlffRYLVVGVYVGLAT 783
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  569 ILGgtlFIFWREI--------PENRTSTP-------------RTTTMAFTCFVFFDLFNALSCRSQTKLIFEIGFFRNRM 627
Cdd:TIGR01116 784 VGG---FVWWYLLthftgcdeDSFTTCPDfedpdcyvfegkqPARTISLSVLVVIEMFNALNALSEDQSLLRMPPWVNKW 860
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....
gi 672085173  628 FLYSILGSLLGQLAVIYAPPLQKVFQTENLSALDLLLLTGLASSVFILSELLKL 681
Cdd:TIGR01116 861 LIGAICLSMALHFLILYVPFLSRIFGVTPLSLTDWLMVLKLSLPVILVDEVLKF 914
P-type_ATPase_Ca_PMCA-like cd02081
animal plasma membrane Ca2(+)-ATPases (PMCA), similar to human ATP2B1-4/PMCA1-4, and related ...
2-556 5.15e-119

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: 372.69  E-value: 5.15e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   2 GTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLV---------------- 65
Cdd:cd02081  174 GTKVLEGSGKMLVTAVGVNSQTGKIMTLLRAENEEKTPLQEKLTKLAVQIGKVGLIVAALTFIVliirfiidgfvndgks 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  66 -GWVQGKPLLSMFTIGVSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTA 144
Cdd:cd02081  254 fSAEDLQEFVNFFIIAVTIIVVAVPEGLPLAVTLSLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTQNRMTV 333
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 145 TQlvtsdgfhaevsgiGYsgegtvcllpskevikefsnvsvgklveagcvannavvrknavMGQPTEGALVVLAMKmnLG 224
Cdd:cd02081  334 VQ--------------GY-------------------------------------------IGNKTECALLGFVLE--LG 354
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 225 sIKDSYIRKKE-------IPFSSEQKWMAVrcSLKNEDEEDVYFMKGAFEEVIHHCSTY-NNGGIPLPLTPQQKSYCQQE 296
Cdd:cd02081  355 -GDYRYREKRPeekvlkvYPFNSARKRMST--VVRLKDGGYRLYVKGASEIVLKKCSYIlNSDGEVVFLTSEKKEEIKRV 431
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 297 EKKMGSLGLRVLALA------------------SGPELGRLTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALE 358
Cdd:cd02081  432 IEPMASDSLRTIGLAyrdfspdeeptaerdwddEEDIESDLTFIGIVGIKDPLRPEVPEAVAKCQRAGITVRMVTGDNIN 511
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 359 TALAIGRTIGLCDE----------KLKAMSGEEVEGMEQDALAARVRQVSVFFRTSPKHKVKIIKALQESGAIVAMTGDG 428
Cdd:cd02081  512 TARAIARECGILTEgedglvlegkEFRELIDEEVGEVCQEKFDKIWPKLRVLARSSPEDKYTLVKGLKDSGEVVAVTGDG 591
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 429 VNDSVALKSADIGIAMGQTGTDVSKEAADMILVDDDFSAIMSAVEEGKGIFYNIKNFVRFQLSTSIAALSLITLSTVCNL 508
Cdd:cd02081  592 TNDAPALKKADVGFAMGIAGTEVAKEASDIILLDDNFSSIVKAVMWGRNVYDSIRKFLQFQLTVNVVAVILAFIGAVVTK 671
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*...
gi 672085173 509 PNPLNAMQILWVNIIMDGPPAQSLGVEPVDRDALKRPPRSVKDTILNR 556
Cdd:cd02081  672 DSPLTAVQMLWVNLIMDTLAALALATEPPTEDLLKRKPYGRDKPLISR 719
P-type_ATPase_Na_ENA cd02086
fungal-type Na(+)-ATPase, similar to the plasma membrane sodium transporters Saccharomyces ...
2-652 4.44e-114

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: 365.24  E-value: 4.44e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   2 GTLVQCGKGQGVVIGTGEQSQFGEVFKMMRaEETPKTPLQKSMDKLGKQLTVFSFGIIGLLmlvGWVQGKPL---LSMFT 78
Cdd:cd02086  177 SSTVTKGRAKGIVVATGMNTEIGKIAKALR-GKGGLISRDRVKSWLYGTLIVTWDAVGRFL---GTNVGTPLqrkLSKLA 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  79 I----------------------------GVSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVIC 130
Cdd:cd02086  253 YllffiavilaiivfavnkfdvdneviiyAIALAISMIPESLVAVLTITMAVGAKRMVKRNVIVRKLDALEALGAVTDIC 332
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 131 SDKTGTLTANEMTATQlvtsdgfhaevsgigysgegtVCLLPSkevikefsnvsvgklveagcVANNAVVRKN------A 204
Cdd:cd02086  333 SDKTGTLTQGKMVVRQ---------------------VWIPAA--------------------LCNIATVFKDeetdcwK 371
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 205 VMGQPTEGALVVLAMKMNLG-SIKDSYIRKK-----EIPFSSEQKWMAVrCSLKNEDEEDVYFMKGAFEEVIHHCSTYNN 278
Cdd:cd02086  372 AHGDPTEIALQVFATKFDMGkNALTKGGSAQfqhvaEFPFDSTVKRMSV-VYYNNQAGDYYAYMKGAVERVLECCSSMYG 450
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 279 GGIPLPLT-PQQKSYCQQEEKkMGSLGLRVLALAS--------------GPELGR------LTFLGLVGIIDPPRAGVKE 337
Cdd:cd02086  451 KDGIIPLDdEFRKTIIKNVES-LASQGLRVLAFASrsftkaqfnddqlkNITLSRadaesdLTFLGLVGIYDPPRNESAG 529
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 338 AVQALSESDVSVKMVTGDALETALAIGRTIGLCD------------------EKLKAMSGEEVEGMEQDALaarvrqvsV 399
Cdd:cd02086  530 AVEKCHQAGITVHMLTGDHPGTAKAIAREVGILPpnsyhysqeimdsmvmtaSQFDGLSDEEVDALPVLPL--------V 601
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 400 FFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGQTGTDVSKEAADMILVDDDFSAIMSAVEEGKGIF 479
Cdd:cd02086  602 IARCSPQTKVRMIEALHRRKKFCAMTGDGVNDSPSLKMADVGIAMGLNGSDVAKDASDIVLTDDNFASIVNAIEEGRRMF 681
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 480 YNIKNFVRFQLSTSIAALSLITLSTVCNLPN-----PLNAMQILWVNIIMDGPPAQSLGVEPVDRDALKRPPRSVKDTIL 554
Cdd:cd02086  682 DNIQKFVLHLLAENVAQVILLLIGLAFKDEDglsvfPLSPVEILWINMVTSSFPAMGLGLEKASPDVMQRPPHDLKVGIF 761
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 555 NRALILKIL-----MSAAVILGGTLFIF-WRE----IPENRTSTP------RTTTMAFTCFVFFDLFNALSCRSQTKLIF 618
Cdd:cd02086  762 TRELIIDTFvygtfMGVLCLASFTLVIYgIGNgdlgSDCNESYNSscedvfRARAAVFATLTWCALILAWEVVDMRRSFF 841
                        730       740       750       760
                 ....*....|....*....|....*....|....*....|....*...
gi 672085173 619 EIG-------------FFRNRMFLYSILGSLLGQLAVIYAPPL-QKVF 652
Cdd:cd02086  842 NMHpdtdspvksffktLWKNKFLFWSVVLGFVSVFPTLYIPVInDDVF 889
ATPase-IIB_Ca TIGR01517
plasma-membrane calcium-translocating P-type ATPase; This model describes the P-type ATPase ...
2-640 1.33e-112

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: 362.17  E-value: 1.33e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173    2 GTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLV---------GWVQG-- 70
Cdd:TIGR01517 240 GTVVNEGSGRMLVTAVGVNSFGGKLMMELRQAGEEETPLQEKLSELAGLIGKFGMGSAVLLFLVlslryvfriIRGDGrf 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   71 -------KPLLSMFTIGVSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMT 143
Cdd:TIGR01517 320 edteedaQTFLDHFIIAVTIVVVAVPEGLPLAVTIALAYSMKKMMKDNNLVRHLAACETMGSATAICSDKTGTLTQNVMS 399
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  144 ATQlvtsdgfhaevsgiGYSGEGTVCLLPsKEVIKEFSNVSVGKLVEAGCVANNAVV-----RKNAVMGQPTEGALVVLA 218
Cdd:TIGR01517 400 VVQ--------------GYIGEQRFNVRD-EIVLRNLPAAVRNILVEGISLNSSSEEvvdrgGKRAFIGSKTECALLDFG 464
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  219 MKMNLGSIKDSYIRKKE-----IPFSSEQKWMAVrcSLKNEDEEDVYFMKGAFEEVIHHCSTY-NNGGIPLPLTPQQKSY 292
Cdd:TIGR01517 465 LLLLLQSRDVQEVRAEEkvvkiYPFNSERKFMSV--VVKHSGGKYREFRKGASEIVLKPCRKRlDSNGEATPISEDDKDR 542
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  293 CQQEEKKMGSLGLRVLALA-----------SGPELGRLTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETAL 361
Cdd:TIGR01517 543 CADVIEPLASDALRTICLAyrdfapeefprKDYPNKGLTLIGVVGIKDPLRPGVREAVQECQRAGITVRMVTGDNIDTAK 622
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  362 AIGRTIGLCDEKLKAMSGEEVEGMEQDALAARVRQVSVFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIG 441
Cdd:TIGR01517 623 AIARNCGILTFGGLAMEGKEFRSLVYEEMDPILPKLRVLARSSPLDKQLLVLMLKDMGEVVAVTGDGTNDAPALKLADVG 702
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  442 IAMGQTGTDVSKEAADMILVDDDFSAIMSAVEEGKGIFYNIKNFVRFQLSTSIAALSLITLSTVC--NLPNPLNAMQILW 519
Cdd:TIGR01517 703 FSMGISGTEVAKEASDIILLDDNFASIVRAVKWGRNVYDNIRKFLQFQLTVNVVAVILTFVGSCIssSHTSPLTAVQLLW 782
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  520 VNIIMDGPPAQSLGVEPVDRDALKRPPRSVKDTILNRALILKILMSAA---VILGGTLF----IFWREIPENRTSTPRT- 591
Cdd:TIGR01517 783 VNLIMDTLAALALATEPPTEALLDRKPIGRNAPLISRSMWKNILGQAGyqlVVTFILLFaggsIFDVSGPDEITSHQQGe 862
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|..
gi 672085173  592 -TTMAFTCFVFFDLFNALSCRSQTKLI--FEiGFFRNRMFLYSILGSLLGQL 640
Cdd:TIGR01517 863 lNTIVFNTFVLLQLFNEINARKLYEGMnvFE-GLFKNRIFVTIMGFTFGFQV 913
P-type_ATPase_Na-K_like cd02608
alpha-subunit of Na(+)/K(+)-ATPases and of gastric H(+)/K(+)-ATPase, similar to the human Na(+) ...
8-559 6.16e-104

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: 337.78  E-value: 6.16e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   8 GKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLT---VF---SFGIIGLLMLVGWVQGkpllSMFTIGV 81
Cdd:cd02608  191 GTARGIVINTGDRTVMGRIATLASGLEVGKTPIAREIEHFIHIITgvaVFlgvSFFILSLILGYTWLEA----VIFLIGI 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  82 slAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTAT------QLVTSD---- 151
Cdd:cd02608  267 --IVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAhmwfdnQIHEADtted 344
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 152 --GFHAEVSGIGYSGEGTVCLLPSKEVIKefsnvsvgklveAGcvANNAVVRKNAVMGQPTEGALVVLaMKMNLGSIKDs 229
Cdd:cd02608  345 qsGASFDKSSATWLALSRIAGLCNRAEFK------------AG--QENVPILKRDVNGDASESALLKC-IELSCGSVME- 408
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 230 yIRKK-----EIPFSSEQKWmavRCSL-KNEDEEDVYF---MKGAFEEVIHHCSTYNNGGIPLPLTPQQKSYCQQEEKKM 300
Cdd:cd02608  409 -MRERnpkvaEIPFNSTNKY---QLSIhENEDPGDPRYllvMKGAPERILDRCSTILINGKEQPLDEEMKEAFQNAYLEL 484
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 301 GSLGLRVLALA-------SGPE------------LGRLTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETAL 361
Cdd:cd02608  485 GGLGERVLGFChlylpddKFPEgfkfdtdevnfpTENLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAK 564
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 362 AIGRTIGLCdeklkamsgeevegmeqdalaarvrqvsVFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIG 441
Cdd:cd02608  565 AIAKGVGII----------------------------VFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIG 616
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 442 IAMGQTGTDVSKEAADMILVDDDFSAIMSAVEEGKGIFYNIKNFVRFQLSTSIAALSLITLSTVCNLPNPLNAMQILWVN 521
Cdd:cd02608  617 VAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIANIPLPLGTITILCID 696
                        570       580       590
                 ....*....|....*....|....*....|....*....
gi 672085173 522 IIMDGPPAQSLGVEPVDRDALKRPPRS-VKDTILNRALI 559
Cdd:cd02608  697 LGTDMVPAISLAYEKAESDIMKRQPRNpKTDKLVNERLI 735
P-type_ATPase cd07538
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ...
2-567 4.47e-103

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: 329.02  E-value: 4.47e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   2 GTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLVGWVQGKPLLSMFTIGV 81
Cdd:cd07538  174 GTLVVRGRGVAKVEATGSRTELGKIGKSLAEMDDEPTPLQKQTGRLVKLCALAALVFCALIVAVYGVTRGDWIQAILAGI 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  82 SLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVtsdgfhaevsgig 161
Cdd:cd07538  254 TLAMAMIPEEFPVILTVFMAMGAWRLAKKNVLVRRAAAVETLGSITVLCVDKTGTLTKNQMEVVELT------------- 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 162 ysgegtvcllpskevikefsnvsvgklveagcvannavvrknavmgqptegalvvlamkmnlgsikdSYIRkkEIPFSSE 241
Cdd:cd07538  321 -------------------------------------------------------------------SLVR--EYPLRPE 331
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 242 QKWMAvrcSLKNEDEEDVYFMKGAFEEVIHHCStynnggiplpLTPQQKSYCQQEEKKMGSLGLRVLALASG-------- 313
Cdd:cd07538  332 LRMMG---QVWKRPEGAFAAAKGSPEAIIRLCR----------LNPDEKAAIEDAVSEMAGEGLRVLAVAACridesflp 398
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 314 --PELGRLTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLcDEKLKAMSGEEVEGMEQDALA 391
Cdd:cd07538  399 ddLEDAVFIFVGLIGLADPLREDVPEAVRICCEAGIRVVMITGDNPATAKAIAKQIGL-DNTDNVITGQELDAMSDEELA 477
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 392 ARVRQVSVFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGQTGTDVSKEAADMILVDDDFSAIMSA 471
Cdd:cd07538  478 EKVRDVNIFARVVPEQKLRIVQAFKANGEIVAMTGDGVNDAPALKAAHIGIAMGKRGTDVAREASDIVLLDDNFSSIVST 557
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 472 VEEGKGIFYNIKN---FVrFQLSTSIAALSLITLstVCNLPNPLNAMQILWVNIIMDGPPAQSLGVEPVDRDALKRPPRS 548
Cdd:cd07538  558 IRLGRRIYDNLKKaitYV-FAIHVPIAGLALLPP--LLGLPPLLFPVHVVLLELIIDPTCSIVFEAEPAERDIMRRPPRP 634
                        570
                 ....*....|....*....
gi 672085173 549 VKDTILNRALILKILMSAA 567
Cdd:cd07538  635 PDEPLFGPRLVIKAILQGA 653
P-type_ATPase cd07539
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ...
1-535 1.82e-102

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: 326.68  E-value: 1.82e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   1 MGTLVQCGKGQGVVIGTGEQSQFGEVFKMMrAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLVGWVQGKPLLSMFTIG 80
Cdd:cd07539  175 EGTTVVSGQGRAVVVATGPHTEAGRAQSLV-APVETATGVQAQLRELTSQLLPLSLGGGAAVTGLGLLRGAPLRQAVADG 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  81 VSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVTsdgfhaevsgi 160
Cdd:cd07539  254 VSLAVAAVPEGLPLVATLAQLAAARRLSRRGVLVRSPRTVEALGRVDTICFDKTGTLTENRLRVVQVRP----------- 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 161 gysgegtvcllpskevikefsnvsvgklveagcvannavvrknavmgqPTEgalvvlamkmnlgsikdsyirkkEIPFSS 240
Cdd:cd07539  323 ------------------------------------------------PLA-----------------------ELPFES 331
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 241 EQKWMAVRCSLKNEDEEDVyfMKGAFEEVIHHCSTYNNGGIPLPLTPQQKSYCQQEEKKMGSLGLRVLALA-----SGPE 315
Cdd:cd07539  332 SRGYAAAIGRTGGGIPLLA--VKGAPEVVLPRCDRRMTGGQVVPLTEADRQAIEEVNELLAGQGLRVLAVAyrtldAGTT 409
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 316 L------GRLTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLcDEKLKAMSGEEVEGMEQDA 389
Cdd:cd07539  410 HaveavvDDLELLGLLGLADTARPGAAALIAALHDAGIDVVMITGDHPITARAIAKELGL-PRDAEVVTGAELDALDEEA 488
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 390 LAARVRQVSVFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGQTGTDVSKEAADMILVDDDFSAIM 469
Cdd:cd07539  489 LTGLVADIDVFARVSPEQKLQIVQALQAAGRVVAMTGDGANDAAAIRAADVGIGVGARGSDAAREAADLVLTDDDLETLL 568
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672085173 470 SAVEEGKGIFYNIKNFVRFQLSTSIAALSLITLSTVCNLPNPLNAMQILWVNIIMDGPPAQSLGVE 535
Cdd:cd07539  569 DAVVEGRTMWQNVRDAVHVLLGGNLGEVMFTLIGTAIGGGAPLNTRQLLLVNLLTDMFPALALAVE 634
ATPase-IIC_X-K TIGR01106
sodium or proton efflux -- potassium uptake antiporter, P-type ATPase, alpha subunit; This ...
8-559 2.11e-98

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: 324.82  E-value: 2.11e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173    8 GKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLT---VF---SFGIIGLLMLVGWVQGkpllSMFTIGV 81
Cdd:TIGR01106 226 GTARGIVVNTGDRTVMGRIASLASGLENGKTPIAIEIEHFIHIITgvaVFlgvSFFILSLILGYTWLEA----VIFLIGI 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   82 slAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTAT------QLVTSDGFHA 155
Cdd:TIGR01106 302 --IVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAhmwfdnQIHEADTTED 379
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  156 EvSGIGYSGEGTVCLLPSKevIKEFSNVSVGKlveAGcvANNAVVRKNAVMGQPTEGALVVLaMKMNLGSIKDsyIRKK- 234
Cdd:TIGR01106 380 Q-SGVSFDKSSATWLALSR--IAGLCNRAVFK---AG--QENVPILKRAVAGDASESALLKC-IELCLGSVME--MRERn 448
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  235 ----EIPFSSEQKWmavRCSL-KNEDEEDVYF---MKGAFEEVIHHCSTYNNGGIPLPLTPQQKSYCQQEEKKMGSLGLR 306
Cdd:TIGR01106 449 pkvvEIPFNSTNKY---QLSIhENEDPRDPRHllvMKGAPERILERCSSILIHGKEQPLDEELKEAFQNAYLELGGLGER 525
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  307 VL-----ALASG--PE------------LGRLTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTI 367
Cdd:TIGR01106 526 VLgfchlYLPDEqfPEgfqfdtddvnfpTDNLCFVGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGV 605
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  368 GLCDE------------------------KLKAMSGEEVEGMEQDAL--AARVRQVSVFFRTSPKHKVKIIKALQESGAI 421
Cdd:TIGR01106 606 GIISEgnetvediaarlnipvsqvnprdaKACVVHGSDLKDMTSEQLdeILKYHTEIVFARTSPQQKLIIVEGCQRQGAI 685
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  422 VAMTGDGVNDSVALKSADIGIAMGQTGTDVSKEAADMILVDDDFSAIMSAVEEGKGIFYNIKNFVRFQLSTSIAALSLIT 501
Cdd:TIGR01106 686 VAVTGDGVNDSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFL 765
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 672085173  502 LSTVCNLPNPLNAMQILWVNIIMDGPPAQSLGVEPVDRDALKRPPR-SVKDTILNRALI 559
Cdd:TIGR01106 766 IFIIANIPLPLGTITILCIDLGTDMVPAISLAYEKAESDIMKRQPRnPKTDKLVNERLI 824
P-type_ATPases cd01431
ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, ...
128-532 1.16e-96

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: 300.91  E-value: 1.16e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 128 VICSDKTGTLTANEMTATQLVTsdgfhaevsgigysgegtvcllpskevikefsnvsvgklveagcvannavvrknavmg 207
Cdd:cd01431    1 VICSDKTGTLTKNGMTVTKLFI---------------------------------------------------------- 22
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 208 qptegalvvlamkmnlgsikdsyirkKEIPFSSEQKWMAVRCSLkneDEEDVYFMKGAFEEVIHHCSTynnggiplPLTP 287
Cdd:cd01431   23 --------------------------EEIPFNSTRKRMSVVVRL---PGRYRAIVKGAPETILSRCSH--------ALTE 65
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 288 QQKSYCQQEEKKMGSLGLRVLALASGPELGR---------LTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALE 358
Cdd:cd01431   66 EDRNKIEKAQEESAREGLRVLALAYREFDPEtskeavelnLVFLGLIGLQDPPRPEVKEAIAKCRTAGIKVVMITGDNPL 145
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 359 TALAIGRTIGLCDEKLKAMSGEEVEGMEQDALAARVRQVSVFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSA 438
Cdd:cd01431  146 TAIAIAREIGIDTKASGVILGEEADEMSEEELLDLIAKVAVFARVTPEQKLRIVKALQARGEVVAMTGDGVNDAPALKQA 225
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 439 DIGIAMGQTGTDVSKEAADMILVDDDFSAIMSAVEEGKGIFYNIKNFVRFQLSTSIAALSLITLSTVCNLPNPLNAMQIL 518
Cdd:cd01431  226 DVGIAMGSTGTDVAKEAADIVLLDDNFATIVEAVEEGRAIYDNIKKNITYLLANNVAEVFAIALALFLGGPLPLLAFQIL 305
                        410
                 ....*....|....
gi 672085173 519 WVNIIMDGPPAQSL 532
Cdd:cd01431  306 WINLVTDLIPALAL 319
ATPase_P-type TIGR01494
ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large ...
2-518 3.33e-96

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: 307.71  E-value: 3.33e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173    2 GTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGL-LMLVGWVQGKPLLSMFTI- 79
Cdd:TIGR01494 105 GTINFGGTLIVKVTATGILTTVGKIAVVVYTGFSTKTPLQSKADKFENFIFILFLLLLALaVFLLLPIGGWDGNSIYKAi 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   80 --GVSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVTsDGFHAEV 157
Cdd:TIGR01494 185 lrALAVLVIAIPCALPLAVSVALAVGDARMAKKGILVKNLNALEELGKVDVICFDKTGTLTTNKMTLQKVII-IGGVEEA 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  158 SGIGYSgegtvcllpskevikefSNVSVGKLVeagcvannavvrknavmGQPTEGALVVLAMKMNLG-SIKDSYIRKKEI 236
Cdd:TIGR01494 264 SLALAL-----------------LAASLEYLS-----------------GHPLERAIVKSAEGVIKSdEINVEYKILDVF 309
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  237 PFSSEQKWMAVRCSLKNEDeeDVYFMKGAFEEVIHHCstynnggiplpltpQQKSYCQQEEKKMGSLGLRVLALASGPEL 316
Cdd:TIGR01494 310 PFSSVLKRMGVIVEGANGS--DLLFVKGAPEFVLERC--------------NNENDYDEKVDEYARQGLRVLAFASKKLP 373
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  317 GRLTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLcdeklkamsgeevegmeqdalaarvrq 396
Cdd:TIGR01494 374 DDLEFLGLLTFEDPLRPDAKETIEALRKAGIKVVMLTGDNVLTAKAIAKELGI--------------------------- 426
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  397 vSVFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGQtgTDVSKEAADMILVDDDFSAIMSAVEEGK 476
Cdd:TIGR01494 427 -DVFARVKPEEKAAIVEALQEKGRTVAMTGDGVNDAPALKKADVGIAMGS--GDVAKAAADIVLLDDDLSTIVEAVKEGR 503
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 672085173  477 GIFYNIKNFVRFQLSTSIAALSLITLSTVCNLPNPLNAMQIL 518
Cdd:TIGR01494 504 KTFSNIKKNIFWAIAYNLILIPLALLLIVIILLPPLLAALAL 545
ATPase-IID_K-Na TIGR01523
potassium and/or sodium efflux P-type ATPase, fungal-type; Initially described as a calcium ...
3-578 1.40e-88

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: 299.23  E-value: 1.40e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173     3 TLVQCGKGQGVVIGTGEQSQFGEVFKMMRAE---------ETPK--------------------------TPLQKSMDKL 47
Cdd:TIGR01523  203 SAVTKGRAKGICIATALNSEIGAIAAGLQGDgglfqrpekDDPNkrrklnkwilkvtkkvtgaflglnvgTPLHRKLSKL 282
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173    48 GKQLtvFSFGIIgLLMLVGWVQGKPLLSMFTI-GVSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCC 126
Cdd:TIGR01523  283 AVIL--FCIAII-FAIIVMAAHKFDVDKEVAIyAICLAISIIPESLIAVLSITMAMGAANMSKRNVIVRKLDALEALGAV 359
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   127 NVICSDKTGTLTANEMTATQL-VTSDGF-HAEVSGIGYS-GEGTVCLLPS-------------KEVIKEF---------- 180
Cdd:TIGR01523  360 NDICSDKTGTITQGKMIARQIwIPRFGTiSIDNSDDAFNpNEGNVSGIPRfspyeyshneaadQDILKEFkdelkeidlp 439
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   181 SNVSVG---KLVEAGCVANNAVVRKN------AVMGQPTEGALVVLAMKMNL---------------------------- 223
Cdd:TIGR01523  440 EDIDMDlfiKLLETAALANIATVFKDdatdcwKAHGDPTEIAIHVFAKKFDLphnaltgeedllksnendqsslsqhnek 519
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   224 -GSIKDSYIRkkEIPFSSEQKWMAVrCSLKNEDEEDVYFMKGAFEEVIHHCSTYnNGGIPLPLTPQQKSYCQQEEKKMGS 302
Cdd:TIGR01523  520 pGSAQFEFIA--EFPFDSEIKRMAS-IYEDNHGETYNIYAKGAFERIIECCSSS-NGKDGVKISPLEDCDRELIIANMES 595
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   303 L---GLRVLALAS--------------GPELGR------LTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALET 359
Cdd:TIGR01523  596 LaaeGLRVLAFASksfdkadnnddqlkNETLNRataesdLEFLGLIGIYDPPRNESAGAVEKCHQAGINVHMLTGDFPET 675
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   360 ALAIGRTIGLCDEKL----------KAMSGEEVEGMEQDALAARVRQVSVFFRTSPKHKVKIIKALQESGAIVAMTGDGV 429
Cdd:TIGR01523  676 AKAIAQEVGIIPPNFihdrdeimdsMVMTGSQFDALSDEEVDDLKALCLVIARCAPQTKVKMIEALHRRKAFCAMTGDGV 755
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   430 NDSVALKSADIGIAMGQTGTDVSKEAADMILVDDDFSAIMSAVEEGKGIFYNIKNFVRFQLSTSIAALSLITLSTVCNLP 509
Cdd:TIGR01523  756 NDSPSLKMANVGIAMGINGSDVAKDASDIVLSDDNFASILNAIEEGRRMFDNIMKFVLHLLAENVAEAILLIIGLAFRDE 835
                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672085173   510 N-----PLNAMQILWVNIIMDGPPAQSLGVEPVDRDALKRPPRSVKDTILNRALILKiLMSAAVILGGTLFIFW 578
Cdd:TIGR01523  836 NgksvfPLSPVEILWCIMITSCFPAMGLGLEKAAPDLMDRLPHDNEVGIFQKELIID-MFAYGFFLGGSCLASF 908
P-type_ATPase_Mg cd02077
magnesium transporting ATPase (MgtA), similar to Escherichia coli MgtA and Salmonella ...
1-547 1.34e-85

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: 285.68  E-value: 1.34e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   1 MGTLVQCGKGQGVVIGTGEQSQFGEVFKMMrAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLVGWVQGKPLLSMFTIG 80
Cdd:cd02077  183 MGTNVVSGSALAVVIATGNDTYFGSIAKSI-TEKRPETSFDKGINKVSKLLIRFMLVMVPVVFLINGLTKGDWLEALLFA 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  81 VSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTatqLVTSDGFHAEVSgi 160
Cdd:cd02077  262 LAVAVGLTPEMLPMIVTSNLAKGAVRMSKRKVIVKNLNAIQNFGAMDILCTDKTGTLTQDKIV---LERHLDVNGKES-- 336
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 161 gysgegtvcllpsKEVIKEF---SNVSVGklveagcvannavvRKNavmgqPTEGALVVLAMKMNLGSIKDSYIRKKEIP 237
Cdd:cd02077  337 -------------ERVLRLAylnSYFQTG--------------LKN-----LLDKAIIDHAEEANANGLIQDYTKIDEIP 384
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 238 FSSEQKWMAVrcSLKNEDEEDVYFMKGAFEEVIHHCSTYNNGGIPLPLTPQQKSYCQQEEKKMGSLGLRVLALA----SG 313
Cdd:cd02077  385 FDFERRRMSV--VVKDNDGKHLLITKGAVEEILNVCTHVEVNGEVVPLTDTLREKILAQVEELNREGLRVLAIAykklPA 462
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 314 PELG-------RLTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLCDEKLkaMSGEEVEGME 386
Cdd:cd02077  463 PEGEysvkdekELILIGFLAFLDPPKESAAQAIKALKKNGVNVKILTGDNEIVTKAICKQVGLDINRV--LTGSEIEALS 540
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 387 QDALAARVRQVSVFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMgQTGTDVSKEAADMILVDDDFS 466
Cdd:cd02077  541 DEELAKIVEETNIFAKLSPLQKARIIQALKKNGHVVGFMGDGINDAPALRQADVGISV-DSAVDIAKEAADIILLEKDLM 619
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 467 AIMSAVEEGKGIFYNIKNFVRFQLSTSIA-ALSLITLSTVcnLP-NPLNAMQILWVNIIMDgpPAQ-SLGVEPVDRDALK 543
Cdd:cd02077  620 VLEEGVIEGRKTFGNILKYIKMTASSNFGnVFSVLVASAF--LPfLPMLPIQLLLQNLLYD--FSQlAIPFDNVDEEFLK 695

                 ....
gi 672085173 544 RPPR 547
Cdd:cd02077  696 KPQK 699
ATPase-IIIA_H TIGR01647
plasma-membrane proton-efflux P-type ATPase; This model describes the plasma membrane proton ...
1-527 5.52e-68

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: 237.61  E-value: 5.52e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173    1 MGTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLVGWVQ-GKPLLSMFTI 79
Cdd:TIGR01647 160 SGSTVKQGEAEAVVTATGMNTFFGKAAALVQSTETGSGHLQKILSKIGLFLIVLIGVLVLIELVVLFFGrGESFREGLQF 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   80 GVSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATqlvtsdgfhaevsg 159
Cdd:TIGR01647 240 ALVLLVGGIPIAMPAVLSVTMAVGAAELAKKKAIVTRLTAIEELAGMDILCSDKTGTLTLNKLSID-------------- 305
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  160 igysgegtvcllpskEVIKEFSNVSVGKLVEAGCVANNavvrknavmgQPTEGAL--VVLAMKMNLGSIKDSYIRKKEIP 237
Cdd:TIGR01647 306 ---------------EILPFFNGFDKDDVLLYAALASR----------EEDQDAIdtAVLGSAKDLKEARDGYKVLEFVP 360
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  238 FSSEQKWMAVRCsLKNEDEEDVYFMKGAFEEVIHHCstYNNGGIPlpltpqqksycQQEEKKMGSL---GLRVLALASGP 314
Cdd:TIGR01647 361 FDPVDKRTEATV-EDPETGKRFKVTKGAPQVILDLC--DNKKEIE-----------EKVEEKVDELasrGYRALGVARTD 426
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  315 ELGRLTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDAL----ETA--LAIGRTIGLCDEKLKAMSGEEVEgmeqD 388
Cdd:TIGR01647 427 EEGRWHFLGLLPLFDPPRHDTKETIERARHLGVEVKMVTGDHLaiakETArrLGLGTNIYTADVLLKGDNRDDLP----S 502
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  389 ALAARVRQVSVFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMgQTGTDVSKEAADMILVDDDFSAI 468
Cdd:TIGR01647 503 GLGEMVEDADGFAEVFPEHKYEIVEILQKRGHLVGMTGDGVNDAPALKKADVGIAV-AGATDAARSAADIVLTEPGLSVI 581
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 672085173  469 MSAVEEGKGIFYNIKNFVRFQLSTSIAALSLITLSTVCnLPNPLNAMQILWVNIIMDGP 527
Cdd:TIGR01647 582 VDAILESRKIFQRMKSYVIYRIAETIRIVFFFGLLILI-LNFYFPPIMVVIIAILNDGT 639
PRK10517 PRK10517
magnesium-transporting P-type ATPase MgtA;
1-547 1.60e-66

magnesium-transporting P-type ATPase MgtA;


Pssm-ID: 236705 [Multi-domain]  Cd Length: 902  Bit Score: 235.73  E-value: 1.60e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   1 MGTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLV-GWVQGKpLLSMFTI 79
Cdd:PRK10517 246 MGTNVVSGTAQAVVIATGANTWFGQLAGRVSEQDSEPNAFQQGISRVSWLLIRFMLVMAPVVLLInGYTKGD-WWEAALF 324
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  80 GVSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQlvtsdgfHAEVSG 159
Cdd:PRK10517 325 ALSVAVGLTPEMLPMIVTSTLARGAVKLSKQKVIVKRLDAIQNFGAMDILCTDKTGTLTQDKIVLEN-------HTDISG 397
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 160 IgysgegtvcllPSKEVIKEF---SNVSVGklveagcvannavvRKN----AVMgqptEGalVVLAMKMNLGSikdSYIR 232
Cdd:PRK10517 398 K-----------TSERVLHSAwlnSHYQTG--------------LKNlldtAVL----EG--VDEESARSLAS---RWQK 443
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 233 KKEIPFSSEQKWMAVRCSlkneDEEDVYFM--KGAFEEVIHHCSTYNNGGIPLPLTPQQKSYCQQEEKKMGSLGLRVLAL 310
Cdd:PRK10517 444 IDEIPFDFERRRMSVVVA----ENTEHHQLicKGALEEILNVCSQVRHNGEIVPLDDIMLRRIKRVTDTLNRQGLRVVAV 519
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 311 ASGP------ELGR-----LTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLcdEKLKAMSG 379
Cdd:PRK10517 520 ATKYlparegDYQRadesdLILEGYIAFLDPPKETTAPALKALKASGVTVKILTGDSELVAAKVCHEVGL--DAGEVLIG 597
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 380 EEVEGMEQDALAARVRQVSVFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMgQTGTDVSKEAADMI 459
Cdd:PRK10517 598 SDIETLSDDELANLAERTTLFARLTPMHKERIVTLLKREGHVVGFMGDGINDAPALRAADIGISV-DGAVDIAREAADII 676
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 460 LVDDDFSAIMSAVEEGKGIFYNIKNFVRFQLSTSIA-ALSLITLSTVcnLPN-PLNAMQILWVNIIMDgpPAQ-SLGVEP 536
Cdd:PRK10517 677 LLEKSLMVLEEGVIEGRRTFANMLKYIKMTASSNFGnVFSVLVASAF--LPFlPMLPLHLLIQNLLYD--VSQvAIPFDN 752
                        570
                 ....*....|.
gi 672085173 537 VDRDALKRPPR 547
Cdd:PRK10517 753 VDDEQIQKPQR 763
P-type_ATPase_H cd02076
plant and fungal plasma membrane H(+)-ATPases, and related bacterial and archaeal putative H(+) ...
1-527 4.36e-66

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: 232.50  E-value: 4.36e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   1 MGTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEEtPKTPLQKSMDKLGKQLTVFSFGIIGLLMLVGWVQGKPLLSMFTIG 80
Cdd:cd02076  160 SGSIVKQGEMLAVVTATGSNTFFGKTAALVASAE-EQGHLQKVLNKIGNFLILLALILVLIIVIVALYRHDPFLEILQFV 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  81 VSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTatqlvtsdgFHAEVSGI 160
Cdd:cd02076  239 LVLLIASIPVAMPAVLTVTMAVGALELAKKKAIVSRLSAIEELAGVDILCSDKTGTLTLNKLS---------LDEPYSLE 309
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 161 GYsGEGTVCLLpskevikefsnvsvgklveagcvannavvrknAVMGQPTEGA----LVVLAMKMNLGSIKDSYIRKKEI 236
Cdd:cd02076  310 GD-GKDELLLL--------------------------------AALASDTENPdaidTAILNALDDYKPDLAGYKQLKFT 356
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 237 PFSSEQKW-MAVrcsLKNEDEEDVYFMKGAFEEVIHHCstynngGIPLPLTPQqksyCQQEEKKMGSLGLRVLALASGPE 315
Cdd:cd02076  357 PFDPVDKRtEAT---VEDPDGERFKVTKGAPQVILELV------GNDEAIRQA----VEEKIDELASRGYRSLGVARKED 423
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 316 LGRLTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLCDEKLKA---MSGEEVEGMEQDALAA 392
Cdd:cd02076  424 GGRWELLGLLPLFDPPRPDSKATIARAKELGVRVKMITGDQLAIAKETARQLGMGTNILSAerlKLGGGGGGMPGSELIE 503
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 393 RVRQVSVFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMgQTGTDVSKEAADMILVDDDFSAIMSAV 472
Cdd:cd02076  504 FIEDADGFAEVFPEHKYRIVEALQQRGHLVGMTGDGVNDAPALKKADVGIAV-SGATDAARAAADIVLTAPGLSVIIDAI 582
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 672085173 473 EEGKGIFYNIKNFVRFQLSTSIAALSLITLSTVCNLPNPLNAMQILWVNIIMDGP 527
Cdd:cd02076  583 KTSRQIFQRMKSYVIYRIAETLRILVFFTLGILILNFYPLPLIMIVLIAILNDGA 637
P-type_ATPase cd02609
uncharacterized subfamily of P-type ATPase transporter, similar to uncharacterized ...
37-539 8.34e-64

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: 224.08  E-value: 8.34e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  37 KTPLQKSMDKLGKQLTvFSFGIIGLLMLVG--WVQGKPLLSMFTIGVSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIV 114
Cdd:cd02609  196 NSELLNSINKILKFTS-FIIIPLGLLLFVEalFRRGGGWRQAVVSTVAALLGMIPEGLVLLTSVALAVGAIRLAKKKVLV 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 115 KKLPIVETLGCCNVICSDKTGTLTANEMTATQLVTSDGfhaevsgigySGEGTVCLLPSKEVIKEFSNVSVGKLVEAGCV 194
Cdd:cd02609  275 QELYSIETLARVDVLCLDKTGTITEGKMKVERVEPLDE----------ANEAEAAAALAAFVAASEDNNATMQAIRAAFF 344
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 195 ANNAvvrknavmgqptegalvvlamkmnlgsikdsYIRKKEIPFSSEQKWMAVRCslkneDEEDVYFMkGAFEEVIhhcs 274
Cdd:cd02609  345 GNNR-------------------------------FEVTSIIPFSSARKWSAVEF-----RDGGTWVL-GAPEVLL---- 383
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 275 tynnGGIPLPLTPQQKSYCQQeekkmgslGLRVLALASGPE-------LGRLTFLGLVGIIDPPRAGVKEAVQALSESDV 347
Cdd:cd02609  384 ----GDLPSEVLSRVNELAAQ--------GYRVLLLARSAGaltheqlPVGLEPLALILLTDPIRPEAKETLAYFAEQGV 451
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 348 SVKMVTGDALETALAIGRTIGLCDEKLkAMSGEEVEGMEqdALAARVRQVSVFFRTSPKHKVKIIKALQESGAIVAMTGD 427
Cdd:cd02609  452 AVKVISGDNPVTVSAIAKRAGLEGAES-YIDASTLTTDE--ELAEAVENYTVFGRVTPEQKRQLVQALQALGHTVAMTGD 528
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 428 GVNDSVALKSADIGIAMGqTGTDVSKEAADMILVDDDFSAIMSAVEEGKGIFYNIKNFVRFQLSTSI--AALSLITLSTv 505
Cdd:cd02609  529 GVNDVLALKEADCSIAMA-SGSDATRQVAQVVLLDSDFSALPDVVFEGRRVVNNIERVASLFLVKTIysVLLALICVIT- 606
                        490       500       510
                 ....*....|....*....|....*....|....
gi 672085173 506 cNLPNPLNAMQILWVNIIMDGPPAQSLGVEPVDR 539
Cdd:cd02609  607 -ALPFPFLPIQITLISLFTIGIPSFFLALEPNKR 639
PRK15122 PRK15122
magnesium-transporting ATPase; Provisional
1-545 4.18e-51

magnesium-transporting ATPase; Provisional


Pssm-ID: 237914 [Multi-domain]  Cd Length: 903  Bit Score: 191.39  E-value: 4.18e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   1 MGTLVQCGKGQGVVIGTGEQSQFGEVFKMMrAEETPKTPLQKSMDKLGKQLTVFSFGIIGL-LMLVGWVQGKpLLSMFTI 79
Cdd:PRK15122 245 MGTNVVSGTATAVVVATGSRTYFGSLAKSI-VGTRAQTAFDRGVNSVSWLLIRFMLVMVPVvLLINGFTKGD-WLEALLF 322
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  80 GVSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQlvtsdgfHAEVSG 159
Cdd:PRK15122 323 ALAVAVGLTPEMLPMIVSSNLAKGAIAMARRKVVVKRLNAIQNFGAMDVLCTDKTGTLTQDRIILEH-------HLDVSG 395
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 160 igysgegtvcllpskevikeFSNVSVGKLVEAGCVANNAVvrKNaVMGQptegalVVLAMKMNLGSI--KDSYIRKKEIP 237
Cdd:PRK15122 396 --------------------RKDERVLQLAWLNSFHQSGM--KN-LMDQ------AVVAFAEGNPEIvkPAGYRKVDELP 446
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 238 FSSEQKWMAVrcSLKNEDEEDVYFMKGAFEEVIHHCSTYNNGGIPLPLTPQQKSYCQQEEKKMGSLGLRVLALASgPELG 317
Cdd:PRK15122 447 FDFVRRRLSV--VVEDAQGQHLLICKGAVEEMLAVATHVRDGDTVRPLDEARRERLLALAEAYNADGFRVLLVAT-REIP 523
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 318 R--------------LTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLcdEKLKAMSGEEVE 383
Cdd:PRK15122 524 GgesraqystaderdLVIRGFLTFLDPPKESAAPAIAALRENGVAVKVLTGDNPIVTAKICREVGL--EPGEPLLGTEIE 601
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 384 GMEQDALAARVRQVSVFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMgQTGTDVSKEAADMILVDD 463
Cdd:PRK15122 602 AMDDAALAREVEERTVFAKLTPLQKSRVLKALQANGHTVGFLGDGINDAPALRDADVGISV-DSGADIAKESADIILLEK 680
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 464 DFSAIMSAVEEGKGIFYNIKNFVRFQLSTSIA-ALSLITLSTVcnLP-NPLNAMQILWVNIIMDgpPAQ-SLGVEPVDRD 540
Cdd:PRK15122 681 SLMVLEEGVIKGRETFGNIIKYLNMTASSNFGnVFSVLVASAF--IPfLPMLAIHLLLQNLMYD--ISQlSLPWDKMDKE 756

                 ....*
gi 672085173 541 ALKRP 545
Cdd:PRK15122 757 FLRKP 761
Cation_ATPase_C pfam00689
Cation transporting ATPase, C-terminus; Members of this families are involved in Na+/K+, H+/K+, ...
509-681 1.55e-47

Cation transporting ATPase, C-terminus; Members of this families are involved in Na+/K+, H+/K+, Ca++ and Mg++ transport. This family represents 5 transmembrane helices.


Pssm-ID: 376368 [Multi-domain]  Cd Length: 175  Bit Score: 165.49  E-value: 1.55e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  509 PNPLNAMQILWVNIIMDGPPAQSLGVEPVDRDALKRPPRSVKDTILNRALILKILMSAAVILGGTLFIFW-----REIPE 583
Cdd:pfam00689   1 PLPLTPIQILWINLVTDGLPALALGFEPPEPDLMKRPPRKPKEPLFSRKMLRRILLQGLLIAILTLLVFFlgllgFGISE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  584 NRTstprTTTMAFTCFVFFDLFNALSCRSQTKLIFEIGFFRNRMFLYSILGSLLGQLAVIYAPPLQKVFQTENLSALDLL 663
Cdd:pfam00689  81 SQN----AQTMAFNTLVLSQLFNALNARSLRRSLFKIGLFSNKLLLLAILLSLLLQLLIIYVPPLQAVFGTTPLSLEQWL 156
                         170
                  ....*....|....*...
gi 672085173  664 LLTGLASSVFILSELLKL 681
Cdd:pfam00689 157 IVLLLALVVLLVVELRKL 174
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
2-473 1.91e-44

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 169.94  E-value: 1.91e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   2 GTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLVGWVQGKPLLSMFTIGV 81
Cdd:COG2217  281 GTINLDGSLRVRVTKVGSDTTLARIIRLVEEAQSSKAPIQRLADRIARYFVPAVLAIAALTFLVWLLFGGDFSTALYRAV 360
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  82 SLAVAAIPEGL----PIVVMVtlvlGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVTSDGF---- 153
Cdd:COG2217  361 AVLVIACPCALglatPTAIMV----GTGRAARRGILIKGGEALERLAKVDTVVFDKTGTLTEGKPEVTDVVPLDGLdede 436
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 154 ----------------------HAEVSGIgysgegtvcllpSKEVIKEFSNVsVGKLVEAgcVANNAVVRknavmgqpte 211
Cdd:COG2217  437 llalaaaleqgsehplaraivaAAKERGL------------ELPEVEDFEAI-PGKGVEA--TVDGKRVL---------- 491
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 212 galvvlamkmnLGSikdsyirkkeipfsseQKWMAVRcslknedeedvyfmkgafeevihhcstynngGIPLPltpqqkS 291
Cdd:COG2217  492 -----------VGS----------------PRLLEEE-------------------------------GIDLP------E 507
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 292 YCQQEEKKMGSLGLRVLALASGpelGRLtfLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLcD 371
Cdd:COG2217  508 ALEERAEELEAEGKTVVYVAVD---GRL--LGLIALADTLRPEAAEAIAALKALGIRVVMLTGDNERTAEAVARELGI-D 581
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 372 EklkamsgeevegmeqdalaarvrqvsVFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGqTGTDV 451
Cdd:COG2217  582 E--------------------------VRAEVLPEDKAAAVRELQAQGKKVAMVGDGINDAPALAAADVGIAMG-SGTDV 634
                        490       500
                 ....*....|....*....|..
gi 672085173 452 SKEAADMILVDDDFSAIMSAVE 473
Cdd:COG2217  635 AIEAADIVLMRDDLRGVPDAIR 656
ATPase-IB_hvy TIGR01525
heavy metal translocating P-type ATPase; This model encompasses two equivalog models for the ...
13-486 1.30e-41

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: 159.72  E-value: 1.30e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   13 VVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLVGWVQGKPLLSMFTIGVSLAVAAIPEGL 92
Cdd:TIGR01525 135 RVTKLGEDSTLAQIVELVEEAQSSKAPIQRLADRIASYYVPAVLAIALLTFVVWLALGALWREALYRALTVLVVACPCAL 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   93 PIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVT-SDGFHAEVSGIGYSGEgtvclL 171
Cdd:TIGR01525 215 GLATPVAILVAIGAAARRGILIKGGDALEKLAKVKTVVFDKTGTLTTGKPTVVDIEPlDDASEEELLALAAALE-----Q 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  172 PSKEVIKEfsnvsvgklveagcvannAVVRknavmgqptegalvvlamkmnlgsikdsYIRKKEIPFSSEQkwmavrcsL 251
Cdd:TIGR01525 290 SSSHPLAR------------------AIVR----------------------------YAKERGLELPPED--------V 315
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  252 KNEDEEDVYFMKGAFEEVIHHCSTYnngGIPLPLTPQQKSYCQQEEKKMGSLGLRVLALASGPELgrltfLGLVGIIDPP 331
Cdd:TIGR01525 316 EEVPGKGVEATVDGGREVRIGNPRF---LGNRELAIEPISASPDLLNEGESQGKTVVFVAVDGEL-----LGVIALRDQL 387
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  332 RAGVKEAVQALSESDV-SVKMVTGDALETALAIGRTIGLCDEklkamsgeevegmeqdalaarvrqvsVFFRTSPKHKVK 410
Cdd:TIGR01525 388 RPEAKEAIAALKRAGGiKLVMLTGDNRSAAEAVAAELGIDDE--------------------------VHAELLPEDKLA 441
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672085173  411 IIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGqTGTDVSKEAADMILVDDDFSAIMSAVEEGKGIFYNIK-NFV 486
Cdd:TIGR01525 442 IVKKLQEEGGPVAMVGDGINDAPALAAADVGIAMG-SGSDVAIEAADIVLLNDDLRSLPTAIDLSRKTRRIIKqNLA 517
P-type_ATPase_HM cd02079
P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) ...
2-499 9.49e-40

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: 155.06  E-value: 9.49e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   2 GTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLVGWVQGKPLLSMFTIGV 81
Cdd:cd02079  193 GTINLNGPLTIEVTKTGEDTTLAKIIRLVEEAQSSKPPLQRLADRFARYFTPAVLVLAALVFLFWPLVGGPPSLALYRAL 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  82 SLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMtatqlvtsdgfhaEVSGIg 161
Cdd:cd02079  273 AVLVVACPCALGLATPTAIVAGIGRAARKGILIKGGDVLETLAKVDTVAFDKTGTLTEGKP-------------EVTEI- 338
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 162 ysgegtvcllpskEVIKEFSNVSVGKLveAGCVANNAvvrknavmGQPTEGALVVLAMKMNLGSIKDSYIRkkEIPfsse 241
Cdd:cd02079  339 -------------EPLEGFSEDELLAL--AAALEQHS--------EHPLARAIVEAAEEKGLPPLEVEDVE--EIP---- 389
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 242 qkwmavrcslknedeedvyfMKGAFEEVIHHcsTYNNGGIPLPLTPQQKSYCQQEEKkMGSLGLRVLALAsgpelGRLtf 321
Cdd:cd02079  390 --------------------GKGISGEVDGR--EVLIGSLSFAEEEGLVEAADALSD-AGKTSAVYVGRD-----GKL-- 439
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 322 LGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLcdeklkamsgeevegmeqdalaarvrqVSVFF 401
Cdd:cd02079  440 VGLFALEDQLRPEAKEVIAELKSGGIKVVMLTGDNEAAAQAVAKELGI---------------------------DEVHA 492
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 402 RTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGQtGTDVSKEAADMILVDDDFSAIMSAVEEGKGIFYN 481
Cdd:cd02079  493 GLLPEDKLAIVKALQAEGGPVAMVGDGINDAPALAQADVGIAMGS-GTDVAIETADIVLLSNDLSKLPDAIRLARRTRRI 571
                        490
                 ....*....|....*....
gi 672085173 482 IK-NFVrFQLSTSIAALSL 499
Cdd:cd02079  572 IKqNLA-WALGYNAIALPL 589
P-type_ATPase_Cu-like cd02094
P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A ...
2-486 7.82e-38

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: 149.94  E-value: 7.82e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   2 GTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKqltVFSFGIIGL--LMLVGWV---QGKPLLSM 76
Cdd:cd02094  207 GTINGNGSLLVRATRVGADTTLAQIIRLVEEAQGSKAPIQRLADRVSG---VFVPVVIAIaiLTFLVWLllgPEPALTFA 283
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  77 FTIGVSLAVAAIPEGL----PIVVMVtlvlGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVTSDG 152
Cdd:cd02094  284 LVAAVAVLVIACPCALglatPTAIMV----GTGRAAELGILIKGGEALERAHKVDTVVFDKTGTLTEGKPEVTDVVPLPG 359
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 153 F-HAEVSGIGYSGEGTvcllpskevikefSNVSVGKLVEAGCVANNAVVRK----NAVMGQPTEGalVVLAMKMNLGSik 227
Cdd:cd02094  360 DdEDELLRLAASLEQG-------------SEHPLAKAIVAAAKEKGLELPEvedfEAIPGKGVRG--TVDGRRVLVGN-- 422
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 228 dsyirkkeipfsseQKWMAvrcslknedeedvyfmkgafeevihhcstynNGGIPLPLTPQQKSYCQQEekkmgslGLRV 307
Cdd:cd02094  423 --------------RRLME-------------------------------ENGIDLSALEAEALALEEE-------GKTV 450
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 308 LALASGPELgrltfLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLcDEklkamsgeevegmeq 387
Cdd:cd02094  451 VLVAVDGEL-----AGLIAVADPLKPDAAEAIEALKKMGIKVVMLTGDNRRTARAIAKELGI-DE--------------- 509
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 388 dalaarvrqvsVFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGqTGTDVSKEAADMILVDDDFSA 467
Cdd:cd02094  510 -----------VIAEVLPEDKAEKVKKLQAQGKKVAMVGDGINDAPALAQADVGIAIG-SGTDVAIESADIVLMRGDLRG 577
                        490       500
                 ....*....|....*....|
gi 672085173 468 IMSAVEEGKGIFYNIK-NFV 486
Cdd:cd02094  578 VVTAIDLSRATMRNIKqNLF 597
ATPase-IB2_Cd TIGR01512
heavy metal-(Cd/Co/Hg/Pb/Zn)-translocating P-type ATPase; This model describes the P-type ...
13-509 3.94e-36

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: 143.62  E-value: 3.94e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   13 VVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLVGWVQGK-PLLSMFTIGVSLAVAAIPEG 91
Cdd:TIGR01512 134 EVTKLPADSTIAKIVNLVEEAQSRKAPTQRFIDRFARYYTPAVLAIALAAALVPPLLGAgPFLEWIYRALVLLVVASPCA 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   92 LPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVTSDGFHAEVsgigysgegtvcll 171
Cdd:TIGR01512 214 LVISAPAAYLSAISAAARHGILIKGGAALEALAKIKTVAFDKTGTLTTGKPKVTDVHPADGHSESE-------------- 279
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  172 pskevikefsnvsvgklveagcvannaVVRKNAVMGQPTEGALVVlamkmnlgSIKDsYIRKKEIPFSSEQKWMAVRCSL 251
Cdd:TIGR01512 280 ---------------------------VLRLAAAAEQGSTHPLAR--------AIVD-YARARELAPPVEDVEEVPGEGV 323
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  252 KNEDEEDVYFM--KGAFEEvihhcstynnggIPLPLTPQQKSYCQQEekkmgslglrVLALASGpelgrlTFLGLVGIID 329
Cdd:TIGR01512 324 RAVVDGGEVRIgnPRSLSE------------AVGASIAVPESAGKTI----------VLVARDG------TLLGYIALSD 375
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  330 PPRAGVKEAVQALSESDVS-VKMVTGDALETALAIGRTIGlCDEklkamsgeevegmeqdalaarvrqvsVFFRTSPKHK 408
Cdd:TIGR01512 376 ELRPDAAEAIAELKALGIKrLVMLTGDRRAVAEAVARELG-IDE--------------------------VHAELLPEDK 428
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  409 VKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGQTGTDVSKEAADMILVDDDFSAIMSAVEEGKGIFYNIKNFVRF 488
Cdd:TIGR01512 429 LEIVKELREKAGPVAMVGDGINDAPALAAADVGIAMGASGSDVALETADVVLLNDDLSRLPQAIRLARRTRRIIKQNVVI 508
                         490       500
                  ....*....|....*....|.
gi 672085173  489 QLsTSIAALSLITLSTVCNLP 509
Cdd:TIGR01512 509 AL-GIILVLILLALFGVLPLW 528
ATPase-IB1_Cu TIGR01511
copper-(or silver)-translocating P-type ATPase; This model describes the P-type ATPase ...
2-486 7.00e-35

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: 140.10  E-value: 7.00e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173    2 GTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLtVFSFGIIGLLMLVGWVQGkpllsmFTIGV 81
Cdd:TIGR01511 160 GTVNGTGSLVVRATATGEDTTLAQIVRLVRQAQQSKAPIQRLADKVAGYF-VPVVIAIALITFVIWLFA------LEFAV 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   82 SLAVAAIPEGL----PIVVMVtlvlGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQlvtsdgfhaev 157
Cdd:TIGR01511 233 TVLIIACPCALglatPTVIAV----ATGLAAKNGVLIKDGDALERAANIDTVVFDKTGTLTQGKPTVTD----------- 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  158 sgigysgegtvcllpskevIKEFSNVSVGKLVeagcvannavvrknAVMGQPTEGALVVLAMkmnlgSIKdSYIRKKEIP 237
Cdd:TIGR01511 298 -------------------VHVFGDRDRTELL--------------ALAAALEAGSEHPLAK-----AIV-SYAKEKGIT 338
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  238 FSSEQKWMAVR-CSLKNEDEEDVYfmkgafeeVIHHCSTYNNGGIPLPLTPQQKSycqqeekkmgslgLRVLALASGpEL 316
Cdd:TIGR01511 339 LVTVSDFKAIPgIGVEGTVEGTKI--------QLGNEKLLGENAIKIDGKAGQGS-------------TVVLVAVNG-EL 396
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  317 grltfLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLcdeklkamsgeevegmeqdalaarvrq 396
Cdd:TIGR01511 397 -----AGVFALEDQLRPEAKEVIQALKRRGIEPVMLTGDNRKTAKAVAKELGI--------------------------- 444
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  397 vSVFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGqTGTDVSKEAADMILVDDDFSAIMSAVEEGK 476
Cdd:TIGR01511 445 -DVRAEVLPDDKAALIKKLQEKGPVVAMVGDGINDAPALAQADVGIAIG-AGTDVAIEAADVVLLRNDLNDVATAIDLSR 522
                         490
                  ....*....|.
gi 672085173  477 GIFYNIK-NFV 486
Cdd:TIGR01511 523 KTLRRIKqNLL 533
P-type_ATPase_HM cd07550
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
2-486 6.95e-31

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: 128.16  E-value: 6.95e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   2 GTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLV--GWVQG-KPLLSMFT 78
Cdd:cd07550  168 STVVEEGQLVIRAERVGRETRAARIAELIEQSPSLKARIQNYAERLADRLVPPTLGLAGLVYALtgDISRAaAVLLVDFS 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  79 IGVSLAVAaipeglpivvmvTLVLGVLRMA-KKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVTSDGfhaev 157
Cdd:cd07550  248 CGIRLSTP------------VAVLSALNHAaRHGILVKGGRALELLAKVDTVVFDKTGTLTEGEPEVTAIITFDG----- 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 158 sgiGYSGEGTVCLLPSKEvikEFSNVSVGklveagcvanNAVVRKNAVMGQPTEGALVVlamKMNLGSIKDSYIRKKEIP 237
Cdd:cd07550  311 ---RLSEEDLLYLAASAE---EHFPHPVA----------RAIVREAEERGIEHPEHEEV---EYIVGHGIASTVDGKRIR 371
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 238 FSSEQkwmavrcslknedeedvyFMkgaFEEVIHHCSTYNNGGIPLPLtpQQKSycqqeekkmgslglrVLALASGPELg 317
Cdd:cd07550  372 VGSRH------------------FM---EEEEIILIPEVDELIEDLHA--EGKS---------------LLYVAIDGRL- 412
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 318 rltfLGLVGIIDPPRAGVKEAVQALSESDV-SVKMVTGDALETALAIGRTIGLcdeklkamsgeevegmeqDALAARVrq 396
Cdd:cd07550  413 ----IGVIGLSDPLRPEAAEVIARLRALGGkRIIMLTGDHEQRARALAEQLGI------------------DRYHAEA-- 468
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 397 vsvffrtSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGQtGTDVSKEAADMILVDDDFSAIMSAVEEGK 476
Cdd:cd07550  469 -------LPEDKAEIVEKLQAEGRTVAFVGDGINDSPALSYADVGISMRG-GTDIARETADVVLLEDDLRGLAEAIELAR 540
                        490
                 ....*....|.
gi 672085173 477 GIFYNIK-NFV 486
Cdd:cd07550  541 ETMALIKrNIA 551
P-ATPase-V TIGR01657
P-type ATPase of unknown pump specificity (type V); These P-type ATPases form a distinct clade ...
13-581 2.40e-30

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: 128.25  E-value: 2.40e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173    13 VVIGTG-EQSQFGEVFKMMRAEETPKTPLQKSMdKLGKQLTVFSFGIIGLLMLVGWVQGKPLLSMFTIGVSLAVAAIPEG 91
Cdd:TIGR01657  335 IVVRTGfSTSKGQLVRSILYPKPRVFKFYKDSF-KFILFLAVLALIGFIYTIIELIKDGRPLGKIILRSLDIITIVVPPA 413
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173    92 LPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMtatqlvtsdgfhaEVSGI-GYSGEGT--- 167
Cdd:TIGR01657  414 LPAELSIGINNSLARLKKKGIFCTSPFRINFAGKIDVCCFDKTGTLTEDGL-------------DLRGVqGLSGNQEflk 480
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   168 ----VCLLPSKEVIKEFS---------NVSVGKLVEAGCV-ANNAVVRKNAVMGQPTEGALVVlamKMNLGSIKDSYIRK 233
Cdd:TIGR01657  481 ivteDSSLKPSITHKALAtchsltkleGKLVGDPLDKKMFeATGWTLEEDDESAEPTSILAVV---RTDDPPQELSIIRR 557
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   234 keIPFSSEQKWMAVRCSLKNEDEEDVyFMKGAfEEVIHhcSTYNNGGIPLPLTPQQKSYCQQeekkmgslGLRVLALASG 313
Cdd:TIGR01657  558 --FQFSSALQRMSVIVSTNDERSPDA-FVKGA-PETIQ--SLCSPETVPSDYQEVLKSYTRE--------GYRVLALAYK 623
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   314 P----------ELGR------LTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGL-------- 369
Cdd:TIGR01657  624 ElpkltlqkaqDLSRdavesnLTFLGFIVFENPLKPDTKEVIKELKRASIRTVMITGDNPLTAVHVARECGIvnpsntli 703
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   370 ----------------------------------------CDEKLK-----AMSG---EEVEGMEQDALAARVRQVSVFF 401
Cdd:TIGR01657  704 laeaeppesgkpnqikfevidsipfastqveipyplgqdsVEDLLAsryhlAMSGkafAVLQAHSPELLLRLLSHTTVFA 783
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   402 RTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGQTGTDV-----SKEAadmilvddDFSAIMSAVEEGk 476
Cdd:TIGR01657  784 RMAPDQKETLVELLQKLDYTVGMCGDGANDCGALKQADVGISLSEAEASVaapftSKLA--------SISCVPNVIREG- 854
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   477 gifyniknfvRFQLSTSI---------AALSLITLSTVCNLPNPLNAMQILWVN---------IIMDGPPAQSLGVEpvd 538
Cdd:TIGR01657  855 ----------RCALVTSFqmfkymalySLIQFYSVSILYLIGSNLGDGQFLTIDlllifpvalLMSRNKPLKKLSKE--- 921
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|...
gi 672085173   539 rdalkRPPrsvkDTILNRALILKILMSAAVILgGTLFIFWREI 581
Cdd:TIGR01657  922 -----RPP----SNLFSVYILTSVLIQFVLHI-LSQVYLVFEL 954
P-type_ATPase_Cu-like cd07552
P-type heavy metal-transporting ATPase, similar to Archaeoglobus fulgidus CopB, a Cu(2+) ...
14-516 1.60e-29

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: 124.34  E-value: 1.60e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  14 VIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIiGLLMLVGWVQGKPLLSMFTIGVSLAVAAIPEGL- 92
Cdd:cd07552  211 VTKTGEDSYLSQVMELVAQAQASKSRAENLADKVAGWLFYIALGV-GIIAFIIWLILGDLAFALERAVTVLVIACPHALg 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  93 ---PIVVMVTLVLGvlrmAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVTSDGFHAEvsgigysgegtvc 169
Cdd:cd07552  290 laiPLVVARSTSIA----AKNGLLIRNREALERARDIDVVLFDKTGTLTEGKFGVTDVITFDEYDED------------- 352
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 170 llpskEVIKEFSNVsvgklvEAGCvannavvrknavmGQPTEGALVvlamkmnlgsikdSYIRKKEIPFSSEQkwmavrc 249
Cdd:cd07552  353 -----EILSLAAAL------EAGS-------------EHPLAQAIV-------------SAAKEKGIRPVEVE------- 388
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 250 slknedeeDVYFMKGAFEEVIHHCSTYNNGGiPLPLTPQQKSYCQQEEKKMGSLGLRVLALASGPELgrltfLGLVGIID 329
Cdd:cd07552  389 --------NFENIPGVGVEGTVNGKRYQVVS-PKYLKELGLKYDEELVKRLAQQGNTVSFLIQDGEV-----IGAIALGD 454
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 330 PPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLCDeklkamsgeevegmeqdalaarvrqvsVFFRTSPKHKV 409
Cdd:cd07552  455 EIKPESKEAIRALKAQGITPVMLTGDNEEVAQAVAEELGIDE---------------------------YFAEVLPEDKA 507
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 410 KIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGqTGTDVSKEAADMILVDDDFSAIMSAVEEGK------------G 477
Cdd:cd07552  508 KKVKELQAEGKKVAMVGDGVNDAPALAQADVGIAIG-AGTDVAIESADVVLVKSDPRDIVDFLELAKatyrkmkqnlwwG 586
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 672085173 478 IFYN---------IKNFVRFQLSTSIAALsLITLSTVCnlpNPLNAMQ 516
Cdd:cd07552  587 AGYNviaiplaagVLAPIGIILSPAVGAV-LMSLSTVI---VAINAMT 630
P-type_ATPase_HM_ZosA_PfeT-like cd07551
P-type heavy metal-transporting ATPase, similar to Bacillus subtilis ZosA/PfeT which ...
19-509 3.58e-29

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: 123.13  E-value: 3.58e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  19 EQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLVG-WVQGKPLLSMFTIGVSLAVAAIPEGLPIVVM 97
Cdd:cd07551  198 SDTVFAKIVQLVEEAQSEKSPTQSFIERFERIYVKGVLLAVLLLLLLPpFLLGWTWADSFYRAMVFLVVASPCALVASTP 277
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  98 VTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVTSDGFHAEvsgigysgegtvcllpskEVI 177
Cdd:cd07551  278 PATLSAIANAARQGVLFKGGVHLENLGSVKAIAFDKTGTLTEGKPRVTDVIPAEGVDEE------------------ELL 339
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 178 kefsnvsvgklveagcvanNAVVRKNAVMGQPTEGALVvlamkmnlgsikdSYIRKKEIPFSSEQKWMAVR-CSLKNEDE 256
Cdd:cd07551  340 -------------------QVAAAAESQSEHPLAQAIV-------------RYAEERGIPRLPAIEVEAVTgKGVTATVD 387
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 257 EDVYFM--KGAFEEVihhcstynngGIPLPLtpqqksycQQEEKKMGSLGLRVLALASGPelgrlTFLGLVGIIDPPRAG 334
Cdd:cd07551  388 GQTYRIgkPGFFGEV----------GIPSEA--------AALAAELESEGKTVVYVARDD-----QVVGLIALMDTPRPE 444
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 335 VKEAVQALSESDVSVKMVTGDALETALAIGRTIGLcDEklkamsgeevegmeqdalaarvrqvsVFFRTSPKHKVKIIKA 414
Cdd:cd07551  445 AKEAIAALRLGGIKTIMLTGDNERTAEAVAKELGI-DE--------------------------VVANLLPEDKVAIIRE 497
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 415 LQESGAIVAMTGDGVNDSVALKSADIGIAMGqTGTDVSKEAADMILVDDDFSAIMSAVEEGKGIFYNIKNFVRFQLsTSI 494
Cdd:cd07551  498 LQQEYGTVAMVGDGINDAPALANADVGIAMG-AGTDVALETADVVLMKDDLSKLPYAIRLSRKMRRIIKQNLIFAL-AVI 575
                        490
                 ....*....|....*
gi 672085173 495 AALSLITLSTVCNLP 509
Cdd:cd07551  576 ALLIVANLFGLLNLP 590
P-type_ATPase_Cd-like cd07545
P-type heavy metal-transporting ATPase, similar to Staphylococcus aureus plasmid pI258 CadA, a ...
2-500 1.32e-27

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: 118.29  E-value: 1.32e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   2 GTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLVgwvqgKPLL---SMFT 78
Cdd:cd07545  164 GTLNGEGALEVRVTKPAEDSTIARIIHLVEEAQAERAPTQAFVDRFARYYTPVVMAIAALVAIV-----PPLFfggAWFT 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  79 I---GVSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQL-VTSDGFH 154
Cdd:cd07545  239 WiyrGLALLVVACPCALVISTPVSIVSAIGNAARKGVLIKGGVYLEELGRLKTVAFDKTGTLTKGKPVVTDVvVLGGQTE 318
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 155 AEVSGIGYSGEgtvcllpsKEVIKEFSNVSVGKLVEAGCvANNAVVRKNAVMGQPTEGalVVLAMKMNLGSIKdsyirkk 234
Cdd:cd07545  319 KELLAIAAALE--------YRSEHPLASAIVKKAEQRGL-TLSAVEEFTALTGRGVRG--VVNGTTYYIGSPR------- 380
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 235 eipfsseqkwmavrcslknedeedvyfmkgAFEEVIHHcstynnggiplpltpqqKSYCQQEE-KKMGSLGLRVLALASG 313
Cdd:cd07545  381 ------------------------------LFEELNLS-----------------ESPALEAKlDALQNQGKTVMILGDG 413
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 314 PelgrlTFLGLVGIIDPPRAGVKEAVQALSESDVS-VKMVTGDALETALAIGRTIGLCDEKLKAMsgeevegmeqdalaa 392
Cdd:cd07545  414 E-----RILGVIAVADQVRPSSRNAIAALHQLGIKqTVMLTGDNPQTAQAIAAQVGVSDIRAELL--------------- 473
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 393 rvrqvsvffrtsPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGQTGTDVSKEAADMILVDDDFSAIMSAV 472
Cdd:cd07545  474 ------------PQDKLDAIEALQAEGGRVAMVGDGVNDAPALAAADVGIAMGAAGTDTALETADIALMGDDLRKLPFAV 541
                        490       500
                 ....*....|....*....|....*...
gi 672085173 473 EEGKGIFYNIKNFVRFQLSTSIAALSLI 500
Cdd:cd07545  542 RLSRKTLAIIKQNIAFALGIKLIALLLV 569
E1-E2_ATPase pfam00122
E1-E2 ATPase;
1-110 7.76e-27

E1-E2 ATPase;


Pssm-ID: 425475 [Multi-domain]  Cd Length: 181  Bit Score: 107.66  E-value: 7.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173    1 MGTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLVGWVQGKPLLSMFTIG 80
Cdd:pfam00122  72 SGTVVVSGSAKAVVTATGEDTELGRIARLVEEAKSKKTPLQRLLDRLGKYFSPVVLLIALAVFLLWLFVGGPPLRALLRA 151
                          90       100       110
                  ....*....|....*....|....*....|
gi 672085173   81 VSLAVAAIPEGLPIVVMVTLVLGVLRMAKK 110
Cdd:pfam00122 152 LAVLVAACPCALPLATPLALAVGARRLAKK 181
P-type_ATPase_HM cd07544
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
21-473 8.12e-27

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: 115.88  E-value: 8.12e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  21 SQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGllmlVGW-VQGKPllsmfTIGVSLAVAAIPEGLPIVVMVT 99
Cdd:cd07544  197 SQYAGIVRLVKEAQANPAPFVRLADRYAVPFTLLALAIAG----VAWaVSGDP-----VRFAAVLVVATPCPLILAAPVA 267
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 100 LVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVTSDGFHA-EVSGIGYSGEGTvcllpSKEVIK 178
Cdd:cd07544  268 IVSGMSRSSRRGILVKDGGVLEKLARAKTVAFDKTGTLTYGQPKVVDVVPAPGVDAdEVLRLAASVEQY-----SSHVLA 342
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 179 EfsnvsvgKLVEAgcvANNAVVRKNAVM------GQPTEGalVVLAMKMNLGSIKdsyirkkeipFSSEQKWMAvrcslk 252
Cdd:cd07544  343 R-------AIVAA---ARERELQLSAVTeltevpGAGVTG--TVDGHEVKVGKLK----------FVLARGAWA------ 394
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 253 nedeedvyfmkgafeevihhcstynnggiplpltpqqksycqQEEKKMGSLGLRVLALASGPELGRLTFlglvgiIDPPR 332
Cdd:cd07544  395 ------------------------------------------PDIRNRPLGGTAVYVSVDGKYAGAITL------RDEVR 426
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 333 AGVKEAVQALSESDVS-VKMVTGDALETALAIGRTIGLcdeklkamsgEEVEGmEQdalaarvrqvsvffrtSPKHKVKI 411
Cdd:cd07544  427 PEAKETLAHLRKAGVErLVMLTGDRRSVAEYIASEVGI----------DEVRA-EL----------------LPEDKLAA 479
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672085173 412 IKALQESGaIVAMTGDGVNDSVALKSADIGIAMGQTGTDVSKEAADMILVDDDFSAIMSAVE 473
Cdd:cd07544  480 VKEAPKAG-PTIMVGDGVNDAPALAAADVGIAMGARGSTAASEAADVVILVDDLDRVVDAVA 540
P-type_ATPase_cation cd07543
P-type cation-transporting ATPases, similar to human cation-transporting ATPase type 13A1 ...
124-444 2.79e-26

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: 114.79  E-value: 2.79e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 124 GCCNVICSDKTGTLTANEMtatqlvtsdgfhaEVSGIGYSGEGTVCLLPSKEVIKEFSNVSvgklveAGCvanNAVVR-- 201
Cdd:cd07543  309 GKVDICCFDKTGTLTSDDL-------------VVEGVAGLNDGKEVIPVSSIEPVETILVL------ASC---HSLVKld 366
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 202 KNAVMGQPTEGALVVlAMKMNL---GSIKDSYIRKKEI------PFSSEQKWMAVRCSLK---NEDEEDVYFMKGAfEEV 269
Cdd:cd07543  367 DGKLVGDPLEKATLE-AVDWTLtkdEKVFPRSKKTKGLkiiqrfHFSSALKRMSVVASYKdpgSTDLKYIVAVKGA-PET 444
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 270 IHhcSTYNNggIPlpltpqqKSYcQQEEKKMGSLGLRVLALASGP----------ELGR------LTFLGLVGIIDPPRA 333
Cdd:cd07543  445 LK--SMLSD--VP-------ADY-DEVYKEYTRQGSRVLALGYKElghltkqqarDYKRedvesdLTFAGFIVFSCPLKP 512
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 334 GVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLCD-EKLKAMSGEEVEGMEQDALaarvRQVSVFFRTSPKHKVKII 412
Cdd:cd07543  513 DSKETIKELNNSSHRVVMITGDNPLTACHVAKELGIVDkPVLILILSEEGKSNEWKLI----PHVKVFARVAPKQKEFII 588
                        330       340       350
                 ....*....|....*....|....*....|..
gi 672085173 413 KALQESGAIVAMTGDGVNDSVALKSADIGIAM 444
Cdd:cd07543  589 TTLKELGYVTLMCGDGTNDVGALKHAHVGVAL 620
P-type_ATPase_cation cd07542
P-type cation-transporting ATPases, similar to human ATPase type 13A2 (ATP13A2) protein and ...
87-582 1.62e-25

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: 112.34  E-value: 1.62e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  87 AIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVTSDGfhaevSGIGysgeg 166
Cdd:cd07542  266 VVPPALPAALTVGIIYAQSRLKKKGIFCISPQRINICGKINLVCFDKTGTLTEDGLDLWGVRPVSG-----NNFG----- 335
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 167 tvcLLPSKEVIKEF-SNVSVGKLVEAGCVANNAVVRKNAVMGQPtegalvvLAMKMnLGSIKDSYIRKKEIPFSSEQKWM 245
Cdd:cd07542  336 ---DLEVFSLDLDLdSSLPNGPLLRAMATCHSLTLIDGELVGDP-------LDLKM-FEFTGWSLEILRQFPFSSALQRM 404
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 246 AVRCSLKNEDEEDVYfMKGAFEEVIHHCSTYNnggIPLPLTPQQKSYCQQeekkmgslGLRVLALASGP---------EL 316
Cdd:cd07542  405 SVIVKTPGDDSMMAF-TKGAPEMIASLCKPET---VPSNFQEVLNEYTKQ--------GFRVIALAYKAlesktwllqKL 472
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 317 GR------LTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLCDEKLKAMSGEEVEgMEQDAL 390
Cdd:cd07542  473 SReevesdLEFLGLIVMENRLKPETAPVINELNRANIRTVMVTGDNLLTAISVARECGMISPSKKVILIEAVK-PEDDDS 551
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 391 AAR----VRQVSVFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGQTGTDVskeAADMILVDDDFS 466
Cdd:cd07542  552 ASLtwtlLLKGTVFARMSPDQKSELVEELQKLDYTVGMCGDGANDCGALKAADVGISLSEAEASV---AAPFTSKVPDIS 628
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 467 AIMSAVEEGkgifyniknfvRFQLSTS------IAALSLITLSTVCNL---PNPLNAMQILWVNIIMDGPPAQSLG-VEP 536
Cdd:cd07542  629 CVPTVIKEG-----------RAALVTSfscfkyMALYSLIQFISVLILysiNSNLGDFQFLFIDLVIITPIAVFMSrTGA 697
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 672085173 537 VDRDALKRPPRSvkdtILNRALILKILMSAAVILG--GTLFIFWREIP 582
Cdd:cd07542  698 YPKLSSKRPPAS----LVSPPVLVSLLGQIVLILLfqVIGFLIVRQQP 741
P-type_ATPase_cation cd02082
P-type cation-transporting ATPases, similar to human ATPase type 13A1-A4 (ATP13A1-A4) proteins ...
13-444 1.87e-25

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: 112.30  E-value: 1.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  13 VVIGTGEQSQFGevfKMMRAEETPKtPLQKSMDKLGKQLTVFSFGIIGLLMLVGWVQG----KPLLSMFTIGVSLAVAAI 88
Cdd:cd02082  190 IVVRTGFGTSKG---QLIRAILYPK-PFNKKFQQQAVKFTLLLATLALIGFLYTLIRLldieLPPLFIAFEFLDILTYSV 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  89 PEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTanemtatqlvtSDGfhaeVSGIGYSGEGTv 168
Cdd:cd02082  266 PPGLPMLIAITNFVGLKRLKKNQILCQDPNRISQAGRIQTLCFDKTGTLT-----------EDK----LDLIGYQLKGQ- 329
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 169 cllpSKEVIKEFSNVSVGKLVEAGCVANNAVVRK--NAVMGQPTEgalvvLAMKMNLGSIKD---------SYIRKKEI- 236
Cdd:cd02082  330 ----NQTFDPIQCQDPNNISIEHKLFAICHSLTKinGKLLGDPLD-----VKMAEASTWDLDydheakqhySKSGTKRFy 400
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 237 -----PFSSEQKWMAVRCS---LKNEDEEDVYFMKGAFEEVIHHCSTynnggIPLPLTPQQKSYCQQeekkmgslGLRVL 308
Cdd:cd02082  401 iiqvfQFHSALQRMSVVAKevdMITKDFKHYAFIKGAPEKIQSLFSH-----VPSDEKAQLSTLINE--------GYRVL 467
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 309 ALASgPELGRLT-----------------FLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLCD 371
Cdd:cd02082  468 ALGY-KELPQSEidafldlsreaqeanvqFLGFIIYKNNLKPDTQAVIKEFKEACYRIVMITGDNPLTALKVAQELEIIN 546
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672085173 372 EKLKAMSGEEVEGMEQDALAARVR---QVSVFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAM 444
Cdd:cd02082  547 RKNPTIIIHLLIPEIQKDNSTQWIliiHTNVFARTAPEQKQTIIRLLKESDYIVCMCGDGANDCGALKEADVGISL 622
P-type_ATPase_K cd02078
potassium-transporting ATPase ATP-binding subunit, KdpB, a subunit of the prokaryotic ...
73-478 1.10e-23

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: 106.19  E-value: 1.10e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  73 LLSMFTIGVSLAVAAIP-------EGLPIVVMVTL-----------------VLGVLRMAKKRVIVKKLPIVETLGCCNV 128
Cdd:cd02078  212 LLVGLTLIFLIVVATLPpfaeysgAPVSVTVLVALlvclipttiggllsaigIAGMDRLLRFNVIAKSGRAVEAAGDVDT 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 129 ICSDKTGTLTANEMTATQLVTSDGfhaevsgigysgegtvcllpskevikefsnVSVGKLVEAGCVAnnavvrknAVMGQ 208
Cdd:cd02078  292 LLLDKTGTITLGNRQATEFIPVGG------------------------------VDEKELADAAQLA--------SLADE 333
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 209 PTEG-ALVVLAMKMNLGSIKDSYIRKKEIPFSSEqkwmaVRCSLKNEDEEDvYFMKGAFEEVIHHCSTyNNGGIPlpltp 287
Cdd:cd02078  334 TPEGrSIVILAKQLGGTERDLDLSGAEFIPFSAE-----TRMSGVDLPDGT-EIRKGAVDAIRKYVRS-LGGSIP----- 401
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 288 qqkSYCQQEEKKMGSLGLRVLALASGPELgrltfLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTI 367
Cdd:cd02078  402 ---EELEAIVEEISKQGGTPLVVAEDDRV-----LGVIYLKDIIKPGIKERFAELRKMGIKTVMITGDNPLTAAAIAAEA 473
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 368 GLcdeklkamsgeevegmeQDALAarvrqvsvffRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMgQT 447
Cdd:cd02078  474 GV-----------------DDFLA----------EAKPEDKLELIRKEQAKGKLVAMTGDGTNDAPALAQADVGVAM-NS 525
                        410       420       430
                 ....*....|....*....|....*....|.
gi 672085173 448 GTDVSKEAADMILVDDDFSAIMSAVEEGKGI 478
Cdd:cd02078  526 GTQAAKEAGNMVDLDSDPTKLIEVVEIGKQL 556
P-type_ATPase_Pb_Zn_Cd2-like cd07546
P-type heavy metal-transporting ATPase, similar to Escherichia coli ZntA which is selective ...
26-525 2.28e-20

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: 95.55  E-value: 2.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  26 VFKMMRAEETPKTPLQKSMDKLGKQLTVfsfGIIGLLMLVGWVQ----GKPLLSMFTIGVSLAVAAIPEGLPIVVMVTLV 101
Cdd:cd07546  191 ILHLIEEAEERRAPIERFIDRFSRWYTP---AIMAVALLVIVVPpllfGADWQTWIYRGLALLLIGCPCALVISTPAAIT 267
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 102 LGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVTSDGfhaevsgigySGEGTVCLLPSKevikefs 181
Cdd:cd07546  268 SGLAAAARRGALIKGGAALEQLGRVTTVAFDKTGTLTRGKPVVTDVVPLTG----------ISEAELLALAAA------- 330
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 182 nvsvgklVEAGCvannavvrknavmGQPTEGALVVLAMKMNLgsikdsyirkkEIPFSSEQKWMAVRCSLKNEDEEDVYF 261
Cdd:cd07546  331 -------VEMGS-------------SHPLAQAIVARAQAAGL-----------TIPPAEEARALVGRGIEGQVDGERVLI 379
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 262 MKGAFEEvihhcstynngGIPLPLTPQQKSYCQQEEKKMgslglrVLALASGpelgrlTFLGLVGIIDPPRAGVKEAVQA 341
Cdd:cd07546  380 GAPKFAA-----------DRGTLEVQGRIAALEQAGKTV------VVVLANG------RVLGLIALRDELRPDAAEAVAE 436
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 342 LSESDVSVKMVTGDALETALAIGRTIGLcdeklkamsgeevegmeqDALAARVrqvsvffrtsPKHKVKIIKALQESGAi 421
Cdd:cd07546  437 LNALGIKALMLTGDNPRAAAAIAAELGL------------------DFRAGLL----------PEDKVKAVRELAQHGP- 487
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 422 VAMTGDGVNDSVALKSADIGIAMGqTGTDVSKEAADMILVDDDFSAIMSAVEEGKGIFYNIKNFVRFQLstSIAALSLIT 501
Cdd:cd07546  488 VAMVGDGINDAPAMKAASIGIAMG-SGTDVALETADAALTHNRLGGVAAMIELSRATLANIRQNITIAL--GLKAVFLVT 564
                        490       500
                 ....*....|....*....|....
gi 672085173 502 lsTVCNLPNplnamqiLWVNIIMD 525
Cdd:cd07546  565 --TLLGITG-------LWLAVLAD 579
P-type_ATPase_HM cd07553
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
14-499 6.98e-20

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: 94.12  E-value: 6.98e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  14 VIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLVGWVQGkpLLSMFTIGVSLAVAAIPEGLP 93
Cdd:cd07553  208 VEHSLAESWSGSILQKVEAQEARKTPRDLLADKIIHYFTVIALLIAVAGFGVWLAID--LSIALKVFTSVLIVACPCALA 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  94 IVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANemtatqlvtsdgfhaevsgigysgegtvcllps 173
Cdd:cd07553  286 LATPFTDEIALARLKKKGVLIKNASSLERLSRVRTIVFDKTGTLTRG--------------------------------- 332
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 174 kevikefsnvsvgklveagcvannavvRKNAVMGQPTEGALVVLAMKMNLgsikdsyIRKKEIPFSSE-QKWMAVRCSLK 252
Cdd:cd07553  333 ---------------------------KSSFVMVNPEGIDRLALRAISAI-------EAHSRHPISRAiREHLMAKGLIK 378
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 253 NEDEEdvyfmkgaFEEVIhhcstynNGGIPLpltpqqksYCQQEEKKMGSLGLRVLALASGPELGRLTFLGLVGII-DPP 331
Cdd:cd07553  379 AGASE--------LVEIV-------GKGVSG--------NSSGSLWKLGSAPDACGIQESGVVIARDGRQLLDLSFnDLL 435
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 332 RAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLCDEKLkamsgeevegmeqdalaarvrqvsvFFRTSPKHKVKI 411
Cdd:cd07553  436 RPDSNREIEELKKGGLSIAILSGDNEEKVRLVGDSLGLDPRQL-------------------------FGNLSPEEKLAW 490
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 412 IKALQESGAIvaMTGDGVNDSVALKSADIGIAMgQTGTDVSKEAADMILVDDDFSAIMSAVEEGKGIFYNIKNFVRFQLS 491
Cdd:cd07553  491 IESHSPENTL--MVGDGANDALALASAFVGIAV-AGEVGVSLEAADIYYAGNGIGGIRDLLTLSKQTIKAIKGLFAFSLL 567

                 ....*...
gi 672085173 492 TSIAALSL 499
Cdd:cd07553  568 YNLVAIGL 575
Cation_ATPase pfam13246
Cation transport ATPase (P-type); This domain is found in cation transport ATPases, including ...
193-276 1.47e-17

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: 78.03  E-value: 1.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  193 CVANNAVVRKNA------VMGQPTEGALVVLAMKM--NLGSIKDSYIRKKEIPFSSEQKWMAVRCSLKNEDEEdVYFMKG 264
Cdd:pfam13246   1 ALCNSAAFDENEekgkweIVGDPTESALLVFAEKMgiDVEELRKDYPRVAEIPFNSDRKRMSTVHKLPDDGKY-RLFVKG 79
                          90
                  ....*....|..
gi 672085173  265 AFEEVIHHCSTY 276
Cdd:pfam13246  80 APEIILDRCTTI 91
copA PRK10671
copper-exporting P-type ATPase CopA;
324-496 4.74e-17

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 85.56  E-value: 4.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 324 LVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLcdeklkamsgeevegmeqDALAARVRqvsvffrt 403
Cdd:PRK10671 644 LLAIRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGI------------------DEVIAGVL-------- 697
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 404 sPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGqTGTDVSKEAADMILVDDDFSAIMSAVEEGKGIFYNIK 483
Cdd:PRK10671 698 -PDGKAEAIKRLQSQGRQVAMVGDGINDAPALAQADVGIAMG-GGSDVAIETAAITLMRHSLMGVADALAISRATLRNMK 775
                        170
                 ....*....|....*...
gi 672085173 484 N-----FVRFQLSTSIAA 496
Cdd:PRK10671 776 QnllgaFIYNSLGIPIAA 793
P-type_ATPase-Cd_Zn_Co_like cd07548
P-type heavy metal-transporting ATPase, similar to Bacillus subtilis CadA which appears to ...
320-476 2.04e-15

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: 79.97  E-value: 2.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 320 TFLGLVGIIDPPRAGVKEAVQALSESDVS-VKMVTGDALETALAIGRTIGLCDeklkamsgeevegmeqdalaarvrqvs 398
Cdd:cd07548  419 KYVGYIVISDEIKEDAKEAIKGLKELGIKnLVMLTGDRKSVAEKVAKKLGIDE--------------------------- 471
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672085173 399 VFFRTSPKHKVKIIKALQ-ESGAIVAMTGDGVNDSVALKSADIGIAMGQTGTDVSKEAADMILVDDDFSAIMSAVEEGK 476
Cdd:cd07548  472 VYAELLPEDKVEKVEELKaESKGKVAFVGDGINDAPVLARADVGIAMGGLGSDAAIEAADVVLMNDEPSKVAEAIKIAR 550
zntA PRK11033
zinc/cadmium/mercury/lead-transporting ATPase; Provisional
320-460 5.88e-15

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


Pssm-ID: 236827 [Multi-domain]  Cd Length: 741  Bit Score: 78.50  E-value: 5.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 320 TFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLcdeklkamsgeevegmeqDalaarvrqvsv 399
Cdd:PRK11033 558 DVLGLIALQDTLRADARQAISELKALGIKGVMLTGDNPRAAAAIAGELGI------------------D----------- 608
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672085173 400 fFRTS--PKHKVKIIKALQESgAIVAMTGDGVNDSVALKSADIGIAMGqTGTDVSKEAADMIL 460
Cdd:PRK11033 609 -FRAGllPEDKVKAVTELNQH-APLAMVGDGINDAPAMKAASIGIAMG-SGTDVALETADAAL 668
PRK14010 PRK14010
K(+)-transporting ATPase subunit B;
20-517 2.48e-14

K(+)-transporting ATPase subunit B;


Pssm-ID: 184448 [Multi-domain]  Cd Length: 673  Bit Score: 76.66  E-value: 2.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  20 QSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLT-VFSFGIIGLLMLVGWVQGKPLLSMFtigVSLAVAAIPEGLPIVVMV 98
Cdd:PRK14010 194 HSFLDKMIGLVEGATRKKTPNEIALFTLLMTLTiIFLVVILTMYPLAKFLNFNLSIAML---IALAVCLIPTTIGGLLSA 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  99 TLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVTsdgfhaevsgigysgegtvcllpskevik 178
Cdd:PRK14010 271 IGIAGMDRVTQFNILAKSGRSVETCGDVNVLILDKTGTITYGNRMADAFIP----------------------------- 321
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 179 eFSNVSVGKLVEAG--CVANNAVvrknavmgqPTEGALVVLAMKMNLGSIKDsyiRKKEIPFSSEQKWMAVRCSlknedE 256
Cdd:PRK14010 322 -VKSSSFERLVKAAyeSSIADDT---------PEGRSIVKLAYKQHIDLPQE---VGEYIPFTAETRMSGVKFT-----T 383
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 257 EDVYfmKGAFEEVIHHCSTyNNGGIPLPLtpqqKSYCQQEEKKMGSlglRVLALASGpelgrlTFLGLVGIIDPPRAGVK 336
Cdd:PRK14010 384 REVY--KGAPNSMVKRVKE-AGGHIPVDL----DALVKGVSKKGGT---PLVVLEDN------EILGVIYLKDVIKDGLV 447
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 337 EAVQALSESDVSVKMVTGDALETALAIGRTIGLcdeklkamsgeevegmeqDALAARVRqvsvffrtsPKHKVKIIKALQ 416
Cdd:PRK14010 448 ERFRELREMGIETVMCTGDNELTAATIAKEAGV------------------DRFVAECK---------PEDKINVIREEQ 500
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 417 ESGAIVAMTGDGVNDSVALKSADIGIAMgQTGTDVSKEAADMILVDDDFSAIMSAVEEGKGIFYNIKNFVRFQLSTSIAA 496
Cdd:PRK14010 501 AKGHIVAMTGDGTNDAPALAEANVGLAM-NSGTMSAKEAANLIDLDSNPTKLMEVVLIGKQLLMTRGSLTTFSIANDIAK 579
                        490       500
                 ....*....|....*....|....
gi 672085173 497 -LSLITLSTVCNLP--NPLNAMQI 517
Cdd:PRK14010 580 yFAILPAMFMAAMPamNHLNIMHL 603
P-type_ATPase_FixI-like cd02092
Rhizobium meliloti FixI and related proteins; belongs to P-type heavy metal-transporting ...
329-473 4.04e-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: 75.86  E-value: 4.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 329 DPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLcdeklkamsgeevegmeqDALAARVRqvsvffrtsPKHK 408
Cdd:cd02092  433 DRPRPDAREAISALRALGLSVEILSGDREPAVRALARALGI------------------EDWRAGLT---------PAEK 485
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672085173 409 VKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGqTGTDVSKEAADMILVDDDFSAIMSAVE 473
Cdd:cd02092  486 VARIEELKAQGRRVLMVGDGLNDAPALAAAHVSMAPA-SAVDASRSAADIVFLGDSLAPVPEAIE 549
P-type_ATPase_APLT_Dnf-like cd02073
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ...
119-448 1.44e-13

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: 74.51  E-value: 1.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 119 IVETLGCCNVICSDKTGTLTANEMtatqlvtsdgfhaevsgigysgegtvcllpskevikEFSNVSVG----KLVEAGCV 194
Cdd:cd02073  348 LNEELGQVEYIFSDKTGTLTENIM------------------------------------EFKKCSINgvdyGFFLALAL 391
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 195 ANNAVVRKNAVMGQ-------PTEGALVVLAMkmNLG--------SIKDSYIRKKE--------IPFSSEQKWMAVRCsl 251
Cdd:cd02073  392 CHTVVPEKDDHPGQlvyqassPDEAALVEAAR--DLGfvflsrtpDTVTINALGEEeeyeilhiLEFNSDRKRMSVIV-- 467
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 252 KNEDEEDVYFMKGA----FEEVIHHcstynnggiplplTPQQKSYCQQEEKKMGSLGLRVLALA----SGPEL------- 316
Cdd:cd02073  468 RDPDGRILLYCKGAdsviFERLSPS-------------SLELVEKTQEHLEDFASEGLRTLCLAyreiSEEEYeewneky 534
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 317 --------GR--------------LTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLCDEKL 374
Cdd:cd02073  535 deastalqNReelldevaeeiekdLILLGATAIEDKLQDGVPETIEALQRAGIKIWVLTGDKQETAINIGYSCRLLSEDM 614
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 375 KAMS------------GEEVEGMEQDaLAARVRQVsVFFRTSPKHKVKIIKALQES-GAIVAMTGDGVNDSVALKSADIG 441
Cdd:cd02073  615 ENLAlvidgktltyalDPELERLFLE-LALKCKAV-ICCRVSPLQKALVVKLVKKSkKAVTLAIGDGANDVSMIQEAHVG 692

                 ....*...
gi 672085173 442 IA-MGQTG 448
Cdd:cd02073  693 VGiSGQEG 700
P-type_ATPase_APLT_Neo1-like cd07541
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Neo1p and human ...
3-457 8.61e-11

Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Neo1p and human putative APLT, ATP9B; Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as a flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. The yeast Neo1 gene is an essential gene; Neo1p localizes to the endoplasmic reticulum and the Golgi complex and plays a role in membrane trafficking within the endomembrane system. Also included in this sub family is human putative ATPase phospholipid transporting 9B, ATP9B, which localizes to the trans-golgi network in a CDC50 protein-independent manner. Levels of ATP9B, along with levels of other ATPase genes, may contribute to expressivity of and atypical presentations of Hailey-Hailey disease (HHD), and the ATP9B gene has recently been identified as a putative Alzheimer's disease loci. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319841 [Multi-domain]  Cd Length: 792  Bit Score: 65.51  E-value: 8.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   3 TLVQCGKGQGVVIGTGEQSqfgevfKMMRAEETPKTP---LQKSMDKLGKQLTVFSFGI-IGLLMLVGwVQGKPLLSMFT 78
Cdd:cd07541  203 TVVASGTVIGVVVYTGKET------RSVMNTSQPKNKvglLDLEINFLTKILFCAVLALsIVMVALQG-FQGPWYIYLFR 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  79 IgVSLAVAAIPEGLPIVV-MVTLVLGVLRMAKKRV---IVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLvtsdgfh 154
Cdd:cd07541  276 F-LILFSSIIPISLRVNLdMAKIVYSWQIEHDKNIpgtVVRTSTIPEELGRIEYLLSDKTGTLTQNEMVFKKL------- 347
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 155 aEVSGIGYSGegtvcllpskeVIKEFSNVSVgklveagcvannavvrknavmgqptegalvvlamkmnlgsikdsyirkk 234
Cdd:cd07541  348 -HLGTVSYGG-----------QNLNYEILQI------------------------------------------------- 366
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 235 eIPFSSEQKWMAVrcSLKNEDEEDVYF-MKGAfEEVIHHCSTYNNggiplpltpqqksYCQQEEKKMGSLGLRVLALA-- 311
Cdd:cd07541  367 -FPFTSESKRMGI--IVREEKTGEITFyMKGA-DVVMSKIVQYND-------------WLEEECGNMAREGLRTLVVAkk 429
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 312 --------------SGPELGR-----------------LTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETA 360
Cdd:cd07541  430 klseeeyqafekryNAAKLSIhdrdlkvaevveslereLELLCLTGVEDKLQEDVKPTLELLRNAGIKIWMLTGDKLETA 509
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 361 LAIGRTIGLCD-----------------------EKLK-----AMSGEEVEGM------EQDALAARVRQVsVFFRTSPK 406
Cdd:cd07541  510 TCIAKSSKLVSrgqyihvfrkvttreeahlelnnLRRKhdcalVIDGESLEVClkyyehEFIELACQLPAV-VCCRCSPT 588
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 672085173 407 HKVKIIKALQES-GAIVAMTGDGVNDSVALKSADIGIAM-GQTGTDVSKeAAD 457
Cdd:cd07541  589 QKAQIVRLIQKHtGKRTCAIGDGGNDVSMIQAADVGVGIeGKEGKQASL-AAD 640
ATPase-Plipid TIGR01652
phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase ...
113-457 1.23e-10

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: 65.09  E-value: 1.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   113 IVKKLPIVETLGCCNVICSDKTGTLTANEMT----ATQLVTSDGFHAEVSGIGYSGEG--TVCLLPSKEVIKEFSNVS-- 184
Cdd:TIGR01652  346 SVRTSNLNEELGQVEYIFSDKTGTLTQNIMEfkkcSIAGVSYGDGFTEIKDGIRERLGsyVENENSMLVESKGFTFVDpr 425
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   185 --------------VGKLVEAGCVANNAVVRKNAVMGQ--------PTEGALVVLAMKMNLGSI----KDSYIRKKE--- 235
Cdd:TIGR01652  426 lvdllktnkpnakrINEFFLALALCHTVVPEFNDDGPEeityqaasPDEAALVKAARDVGFVFFertpKSISLLIEMhge 505
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   236 ---------IPFSSEQKWMAVRCslKNEDEEDVYFMKGA----FEEVIHHCSTYNnggiplpltpqQKSYCQQEekKMGS 302
Cdd:TIGR01652  506 tkeyeilnvLEFNSDRKRMSVIV--RNPDGRIKLLCKGAdtviFKRLSSGGNQVN-----------EETKEHLE--NYAS 570
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   303 LGLRVLAL-------------------ASGPELGR--------------LTFLGLVGIIDPPRAGVKEAVQALSESDVSV 349
Cdd:TIGR01652  571 EGLRTLCIayrelseeeyeewneeyneASTALTDReekldvvaesiekdLILLGATAIEDKLQEGVPETIELLRQAGIKI 650
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   350 KMVTGDALETALAIGRTIGLCDEKLK-----------------AMSGEEVEGMEQDALAARVRQVS-------------- 398
Cdd:TIGR01652  651 WVLTGDKVETAINIGYSCRLLSRNMEqivitsdsldatrsveaAIKFGLEGTSEEFNNLGDSGNVAlvidgkslgyalde 730
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672085173   399 ----VFF------------RTSPKHKVKIIKALQES-GAIVAMTGDGVNDSVALKSADIGIAM-GQTGTDVSKeAAD 457
Cdd:TIGR01652  731 elekEFLqlalkckaviccRVSPSQKADVVRLVKKStGKTTLAIGDGANDVSMIQEADVGVGIsGKEGMQAVM-ASD 806
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
329-439 2.19e-09

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


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 57.60  E-value: 2.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  329 DPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLCDEKLKAMSGEEVEgmeqdalaarvrqvsvFFRTSPKHK 408
Cdd:pfam00702  97 LKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVG----------------VGKPKPEIY 160
                          90       100       110
                  ....*....|....*....|....*....|.
gi 672085173  409 VKIIKALQESGAIVAMTGDGVNDSVALKSAD 439
Cdd:pfam00702 161 LAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
P-type_ATPase_APLT cd07536
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ...
3-457 4.00e-09

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


Pssm-ID: 319838 [Multi-domain]  Cd Length: 805  Bit Score: 59.92  E-value: 4.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173   3 TLVQCGKGQGVVIGTGEQSQFGevfkMMRAEETPKTPLqksMDKLGKQLTVFSFGIIGLLMLV---------------GW 67
Cdd:cd07536  209 TLRNTGWVIGVVVYTGKETKLV----MNTSNAKNKVGL---LDLELNRLTKALFLALVVLSLVmvtlqgfwgpwygekNW 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  68 VQGKPLLSMFTIGVSLAVAAI--PEGLPIVVMVTLVLGVLRMAK--------------KRVIVKKLPIVETLGCCNVICS 131
Cdd:cd07536  282 YIKKMDTTSDNFGRNLLRFLLlfSYIIPISLRVNLDMVKAVYAWfimwdenmyyigndTGTVARTSTIPEELGQVVYLLT 361
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 132 DKTGTLTANEMTATQLvtsdgfhaEVSGIGYSG-EGTVCLLPSKEVIKEFSNVSVgklveagcvannaVVR--KNAVMGQ 208
Cdd:cd07536  362 DKTGTLTQNEMIFKRC--------HIGGVSYGGqVLSFCILQLLEFTSDRKRMSV-------------IVRdeSTGEITL 420
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 209 PTEGALVVLAMKMNLGSIKDSYIRKKEiPFSSEQkwMAVRCSLKNEDEEDVYFmkgAFEEVIHHCSTYnnggiplpltpq 288
Cdd:cd07536  421 YMKGADVAISPIVSKDSYMEQYNDWLE-EECGEG--LRTLCVAKKALTENEYQ---EWESRYTEASLS------------ 482
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 289 qksycqqeekkMGSLGLRVLALASGPElGRLTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIG 368
Cdd:cd07536  483 -----------LHDRSLRVAEVVESLE-RELELLGLTAIEDRLQAGVPETIETLRKAGIKIWMLTGDKQETAICIAKSCH 550
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 369 LCDEKLKAMSGEEVEGMEQDALAARV---------RQVSVFF-------------------------------RTSPKHK 408
Cdd:cd07536  551 LVSRTQDIHLLRQDTSRGERAAITQHahlelnafrRKHDVALvidgdslevalkyyrhefvelacqcpaviccRVSPTQK 630
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 672085173 409 VKIIKALQE-SGAIVAMTGDGVNDSVALKSADIGIAM-GQTGTDVSKeAAD 457
Cdd:cd07536  631 ARIVTLLKQhTGRRTLAIGDGGNDVSMIQAADCGVGIsGKEGKQASL-AAD 680
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
426-474 2.67e-04

phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate phosphatase; belongs to the haloacid dehalogenase-like superfamily; Bacteroides thetaiotaomicron VPI-5482 BT4131 is a phosphatase with preference for hexose phosphates. In addition this family includes uncharacterized Bacillus subtilis YkrA, a putative phosphatase and uncharacterized Streptococcus pyogenes MGAS10394 a putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319819 [Multi-domain]  Cd Length: 213  Bit Score: 42.98  E-value: 2.67e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 672085173 426 GDGVNDSVALKSADIGIAMGQTGTDVsKEAADMILVDDDFSAIMSAVEE 474
Cdd:cd07517  164 GDGLNDIEMLEAVGIGIAMGNAHEEL-KEIADYVTKDVDEDGILKALKH 211
PLN03190 PLN03190
aminophospholipid translocase; Provisional
318-448 7.16e-04

aminophospholipid translocase; Provisional


Pssm-ID: 215623 [Multi-domain]  Cd Length: 1178  Bit Score: 42.96  E-value: 7.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  318 RLTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLCDEKLKAM-----SGEEVEGMEQDAL-- 390
Cdd:PLN03190  714 NLTILGASAIEDKLQQGVPEAIESLRTAGIKVWVLTGDKQETAISIGYSSKLLTNKMTQIiinsnSKESCRKSLEDALvm 793
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  391 ------------------AARVRQVS------------------VFFRTSPKHKVKI---IKALQESGaIVA-------- 423
Cdd:PLN03190  794 skklttvsgisqntggssAAASDPVAliidgtslvyvldseleeQLFQLASKCSVVLccrVAPLQKAG-IVAlvknrtsd 872
                         170       180
                  ....*....|....*....|....*....
gi 672085173  424 MT---GDGVNDSVALKSADIGIAM-GQTG 448
Cdd:PLN03190  873 MTlaiGDGANDVSMIQMADVGVGIsGQEG 901
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
320-474 1.48e-03

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 40.12  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 320 TFLGLVGIIDPpraGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGL--------------CDEKL---KAMSGEEV 382
Cdd:COG0561   12 TLLNDDGEISP---RTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLddplitsngaliydPDGEVlyeRPLDPEDV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173 383 EGMEQDALAARVRqVSVFFRTSPK---------HKVKIIKALQES-----GAIVAMtGDGVNDSVALKSADIGIAMGQTG 448
Cdd:COG0561   89 REILELLREHGLH-LQVVVRSGPGfleilpkgvSKGSALKKLAERlgippEEVIAF-GDSGNDLEMLEAAGLGVAMGNAP 166
                        170       180
                 ....*....|....*....|....*.
gi 672085173 449 TDVsKEAADMILVDDDFSAIMSAVEE 474
Cdd:COG0561  167 PEV-KAAADYVTGSNDEDGVAEALEK 191
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
410-468 3.68e-03

haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like hydrolase enzymes.


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 39.91  E-value: 3.68e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085173  410 KIIKALQESGA-IVAMtGDGVNDSVALKSADIGIAMGQtGTDVSKEAADMILVDDDFSAI 468
Cdd:pfam08282 194 ALAKHLNISLEeVIAF-GDGENDIEMLEAAGLGVAMGN-ASPEVKAAADYVTDSNNEDGV 251
 
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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