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Conserved domains on  [gi|6457264|gb|AAF09444|]
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putative E1-E2 ATPase, partial [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PhoLip_ATPase_C pfam16212
Phospholipid-translocating P-type ATPase C-terminal; PhoLip_ATPase_C is found at the ...
1-251 8.48e-104

Phospholipid-translocating P-type ATPase C-terminal; PhoLip_ATPase_C is found at the C-terminus of a number of phospholipid-translocating ATPases. It is found in higher eukaryotes.


:

Pssm-ID: 465071 [Multi-domain]  Cd Length: 250  Bit Score: 305.20  E-value: 8.48e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6457264      1 DYSFSQFKFLQRLLLVHGRWSYLRMCKFLCYFFYKNFAFTMVHFWFGFFCGFSAQTVYDQYFITLYNIVYTSLPVLAMGV 80
Cdd:pfam16212   5 DYAIAQFRFLKRLLLVHGRWSYRRTSKLILYFFYKNIVFTLTQFWYQFYNGFSGQSLYESWYLTLYNLLFTSLPVIVLGI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6457264     81 FDQDVPEQRSMEYPKLYEPGQLNLLFNKREFFICIAQGIYTSVLMFLIPYGVFAEATRDDGtQLADYQSFAVTVATSLVI 160
Cdd:pfam16212  85 FDQDVSAETLLAYPELYKLGQKNKFFNLKTFLGWMLDGIYQSLIIFFIPYLAYGDSVFSGG-KDADLWAFGTTVFTALVL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6457264    161 VVSVQIGLDTGYWTAINHFFIWGSLAVYFAILFAMHSNGLFDMFPnqfrFVGNAQNTLAQPTVWLTIALTTAVCIMPVVA 240
Cdd:pfam16212 164 VVNLKLALETHYWTWITHLAIWGSILLYFLFTLIYSSIYPSSYSV----FYGVASRLFGSPSFWLTLLLIVVVALLPDFA 239
                         250
                  ....*....|.
gi 6457264    241 FRFLRLSLKPD 251
Cdd:pfam16212 240 YKALKRTFFPT 250
 
Name Accession Description Interval E-value
PhoLip_ATPase_C pfam16212
Phospholipid-translocating P-type ATPase C-terminal; PhoLip_ATPase_C is found at the ...
1-251 8.48e-104

Phospholipid-translocating P-type ATPase C-terminal; PhoLip_ATPase_C is found at the C-terminus of a number of phospholipid-translocating ATPases. It is found in higher eukaryotes.


Pssm-ID: 465071 [Multi-domain]  Cd Length: 250  Bit Score: 305.20  E-value: 8.48e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6457264      1 DYSFSQFKFLQRLLLVHGRWSYLRMCKFLCYFFYKNFAFTMVHFWFGFFCGFSAQTVYDQYFITLYNIVYTSLPVLAMGV 80
Cdd:pfam16212   5 DYAIAQFRFLKRLLLVHGRWSYRRTSKLILYFFYKNIVFTLTQFWYQFYNGFSGQSLYESWYLTLYNLLFTSLPVIVLGI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6457264     81 FDQDVPEQRSMEYPKLYEPGQLNLLFNKREFFICIAQGIYTSVLMFLIPYGVFAEATRDDGtQLADYQSFAVTVATSLVI 160
Cdd:pfam16212  85 FDQDVSAETLLAYPELYKLGQKNKFFNLKTFLGWMLDGIYQSLIIFFIPYLAYGDSVFSGG-KDADLWAFGTTVFTALVL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6457264    161 VVSVQIGLDTGYWTAINHFFIWGSLAVYFAILFAMHSNGLFDMFPnqfrFVGNAQNTLAQPTVWLTIALTTAVCIMPVVA 240
Cdd:pfam16212 164 VVNLKLALETHYWTWITHLAIWGSILLYFLFTLIYSSIYPSSYSV----FYGVASRLFGSPSFWLTLLLIVVVALLPDFA 239
                         250
                  ....*....|.
gi 6457264    241 FRFLRLSLKPD 251
Cdd:pfam16212 240 YKALKRTFFPT 250
P-type_ATPase_APLT_Dnf-like cd02073
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ...
1-129 6.20e-73

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: 241.69  E-value: 6.20e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6457264    1 DYSFSQFKFLQRLLLVHGRWSYLRMCKFLCYFFYKNFAFTMVHFWFGFFCGFSAQTVYDQYFITLYNIVYTSLPVLAMGV 80
Cdd:cd02073 708 DYAIAQFRFLRRLLLVHGRWSYQRLAKLILYFFYKNIAFYLTQFWYQFFNGFSGQTLYDSWYLTLYNVLFTSLPPLVIGI 787
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 6457264   81 FDQDVPEQRSMEYPKLYEPGQLNLLFNKREFFICIAQGIYTSVLMFLIP 129
Cdd:cd02073 788 FDQDVSAETLLRYPELYKPGQLNELFNWKVFLYWILDGIYQSLIIFFVP 836
ATPase-Plipid TIGR01652
phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase ...
1-257 5.42e-71

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: 238.82  E-value: 5.42e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6457264       1 DYSFSQFKFLQRLLLVHGRWSYLRMCKFLCYFFYKNFAFTMVHFWFGFFCGFSAQTVYDQYFITLYNIVYTSLPVLAMGV 80
Cdd:TIGR01652  806 DFAIGQFRFLTKLLLVHGRWSYKRISKMILYFFYKNLIFAIIQFWYSFYNGFSGQTLYEGWYMVLYNVFFTALPVISLGV 885
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6457264      81 FDQDVPEQRSMEYPKLYEPGQLNLLFNKREFFICIAQGIYTSVLMFLIPYGVFAEATRDDGTQLADYQSFAVTVATSLVI 160
Cdd:TIGR01652  886 FDQDVSASLSLRYPQLYREGQKGQGFSTKTFWGWMLDGIYQSLVIFFFPMFAYILGDFVSSGSVDDFSSVGVIVFTALVV 965
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6457264     161 VVSVQIGLDTGYWTAINHFFIWGSLAVYFAILFAmhsngLFDMFPNQfRFVGNAQNTLAQPTVWLTIALTTAVCIMPVVA 240
Cdd:TIGR01652  966 IVNLKIALEINRWNWISLITIWGSILVWLIFVIV-----YSSIFPSP-AFYKAAPRVMGTFGFWLVLLVIVLISLLPRFT 1039
                          250
                   ....*....|....*..
gi 6457264     241 FRFLRLSLKPDLSDTVR 257
Cdd:TIGR01652 1040 YKAIQRLFRPPDYDIVQ 1056
PLN03190 PLN03190
aminophospholipid translocase; Provisional
1-251 1.02e-37

aminophospholipid translocase; Provisional


Pssm-ID: 215623 [Multi-domain]  Cd Length: 1178  Bit Score: 143.89  E-value: 1.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6457264      1 DYSFSQFKFLQRLLLVHGRWSYLRMCKFLCYFFYKNFAFTMVHFWFGFFCGFSAQTVYDQYFITLYNIVYTSLPVLAMGV 80
Cdd:PLN03190  909 DFAMGQFRFLVPLLLVHGHWNYQRMGYMILYNFYRNAVFVLVLFWYVLFTCFTLTTAINEWSSVLYSVIYTALPTIVVGI 988
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6457264     81 FDQDVPEQRSMEYPKLYEPGQLNLLFNKREFFICIAQGIYTSVLMFLIPygVFAE-ATRDDGTQLADYQSFAVtvatslV 159
Cdd:PLN03190  989 LDKDLSRRTLLKYPQLYGAGQRQEAYNSKLFWLTMIDTLWQSAVVFFVP--LFAYwASTIDGSSIGDLWTLAV------V 1060
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6457264    160 IVVSVQIGLDTGYWTAINHFFIWGSLAVYFAILFAMHSnglFDMFPNQFRFVgnaqNTLAQPTVWLTIALTTAVCIMPVV 239
Cdd:PLN03190 1061 ILVNLHLAMDIIRWNWITHAAIWGSIVATFICVIVIDA---IPTLPGYWAIF----HIAKTGSFWLCLLAIVVAALLPRF 1133
                         250
                  ....*....|..
gi 6457264    240 AFRFLRLSLKPD 251
Cdd:PLN03190 1134 VVKVLYQYFTPC 1145
 
Name Accession Description Interval E-value
PhoLip_ATPase_C pfam16212
Phospholipid-translocating P-type ATPase C-terminal; PhoLip_ATPase_C is found at the ...
1-251 8.48e-104

Phospholipid-translocating P-type ATPase C-terminal; PhoLip_ATPase_C is found at the C-terminus of a number of phospholipid-translocating ATPases. It is found in higher eukaryotes.


Pssm-ID: 465071 [Multi-domain]  Cd Length: 250  Bit Score: 305.20  E-value: 8.48e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6457264      1 DYSFSQFKFLQRLLLVHGRWSYLRMCKFLCYFFYKNFAFTMVHFWFGFFCGFSAQTVYDQYFITLYNIVYTSLPVLAMGV 80
Cdd:pfam16212   5 DYAIAQFRFLKRLLLVHGRWSYRRTSKLILYFFYKNIVFTLTQFWYQFYNGFSGQSLYESWYLTLYNLLFTSLPVIVLGI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6457264     81 FDQDVPEQRSMEYPKLYEPGQLNLLFNKREFFICIAQGIYTSVLMFLIPYGVFAEATRDDGtQLADYQSFAVTVATSLVI 160
Cdd:pfam16212  85 FDQDVSAETLLAYPELYKLGQKNKFFNLKTFLGWMLDGIYQSLIIFFIPYLAYGDSVFSGG-KDADLWAFGTTVFTALVL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6457264    161 VVSVQIGLDTGYWTAINHFFIWGSLAVYFAILFAMHSNGLFDMFPnqfrFVGNAQNTLAQPTVWLTIALTTAVCIMPVVA 240
Cdd:pfam16212 164 VVNLKLALETHYWTWITHLAIWGSILLYFLFTLIYSSIYPSSYSV----FYGVASRLFGSPSFWLTLLLIVVVALLPDFA 239
                         250
                  ....*....|.
gi 6457264    241 FRFLRLSLKPD 251
Cdd:pfam16212 240 YKALKRTFFPT 250
P-type_ATPase_APLT_Dnf-like cd02073
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ...
1-129 6.20e-73

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: 241.69  E-value: 6.20e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6457264    1 DYSFSQFKFLQRLLLVHGRWSYLRMCKFLCYFFYKNFAFTMVHFWFGFFCGFSAQTVYDQYFITLYNIVYTSLPVLAMGV 80
Cdd:cd02073 708 DYAIAQFRFLRRLLLVHGRWSYQRLAKLILYFFYKNIAFYLTQFWYQFFNGFSGQTLYDSWYLTLYNVLFTSLPPLVIGI 787
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 6457264   81 FDQDVPEQRSMEYPKLYEPGQLNLLFNKREFFICIAQGIYTSVLMFLIP 129
Cdd:cd02073 788 FDQDVSAETLLRYPELYKPGQLNELFNWKVFLYWILDGIYQSLIIFFVP 836
ATPase-Plipid TIGR01652
phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase ...
1-257 5.42e-71

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: 238.82  E-value: 5.42e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6457264       1 DYSFSQFKFLQRLLLVHGRWSYLRMCKFLCYFFYKNFAFTMVHFWFGFFCGFSAQTVYDQYFITLYNIVYTSLPVLAMGV 80
Cdd:TIGR01652  806 DFAIGQFRFLTKLLLVHGRWSYKRISKMILYFFYKNLIFAIIQFWYSFYNGFSGQTLYEGWYMVLYNVFFTALPVISLGV 885
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6457264      81 FDQDVPEQRSMEYPKLYEPGQLNLLFNKREFFICIAQGIYTSVLMFLIPYGVFAEATRDDGTQLADYQSFAVTVATSLVI 160
Cdd:TIGR01652  886 FDQDVSASLSLRYPQLYREGQKGQGFSTKTFWGWMLDGIYQSLVIFFFPMFAYILGDFVSSGSVDDFSSVGVIVFTALVV 965
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6457264     161 VVSVQIGLDTGYWTAINHFFIWGSLAVYFAILFAmhsngLFDMFPNQfRFVGNAQNTLAQPTVWLTIALTTAVCIMPVVA 240
Cdd:TIGR01652  966 IVNLKIALEINRWNWISLITIWGSILVWLIFVIV-----YSSIFPSP-AFYKAAPRVMGTFGFWLVLLVIVLISLLPRFT 1039
                          250
                   ....*....|....*..
gi 6457264     241 FRFLRLSLKPDLSDTVR 257
Cdd:TIGR01652 1040 YKAIQRLFRPPDYDIVQ 1056
PLN03190 PLN03190
aminophospholipid translocase; Provisional
1-251 1.02e-37

aminophospholipid translocase; Provisional


Pssm-ID: 215623 [Multi-domain]  Cd Length: 1178  Bit Score: 143.89  E-value: 1.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6457264      1 DYSFSQFKFLQRLLLVHGRWSYLRMCKFLCYFFYKNFAFTMVHFWFGFFCGFSAQTVYDQYFITLYNIVYTSLPVLAMGV 80
Cdd:PLN03190  909 DFAMGQFRFLVPLLLVHGHWNYQRMGYMILYNFYRNAVFVLVLFWYVLFTCFTLTTAINEWSSVLYSVIYTALPTIVVGI 988
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6457264     81 FDQDVPEQRSMEYPKLYEPGQLNLLFNKREFFICIAQGIYTSVLMFLIPygVFAE-ATRDDGTQLADYQSFAVtvatslV 159
Cdd:PLN03190  989 LDKDLSRRTLLKYPQLYGAGQRQEAYNSKLFWLTMIDTLWQSAVVFFVP--LFAYwASTIDGSSIGDLWTLAV------V 1060
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6457264    160 IVVSVQIGLDTGYWTAINHFFIWGSLAVYFAILFAMHSnglFDMFPNQFRFVgnaqNTLAQPTVWLTIALTTAVCIMPVV 239
Cdd:PLN03190 1061 ILVNLHLAMDIIRWNWITHAAIWGSIVATFICVIVIDA---IPTLPGYWAIF----HIAKTGSFWLCLLAIVVAALLPRF 1133
                         250
                  ....*....|..
gi 6457264    240 AFRFLRLSLKPD 251
Cdd:PLN03190 1134 VVKVLYQYFTPC 1145
P-type_ATPase_APLT cd07536
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ...
1-126 6.69e-29

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: 117.70  E-value: 6.69e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6457264    1 DYSFSQFKFLQRLLLVHGRWSYLRMCKFLCYFFYKNFAFTMVHFWFGFFCGFSAQTVYDQYFITLYNIVYTSLPVLAMGV 80
Cdd:cd07536 680 DYSITQFRHLGRLLLVHGRNSYNRSAALGQYVFYKGLIISTIQAVFSFVFGFSGVPLFQGFLMVGYNVIYTMFPVFSLVI 759
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 6457264   81 fDQDVPEQRSMEYPKLYEPGQLNLLFNKREFFICIAQGIYTSVLMF 126
Cdd:cd07536 760 -DQDVKPESAMLYPQLYKDLQKGRSLNFKTFLGWVLISLYHGGILF 804
P-type_ATPase_APLT_Neo1-like cd07541
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Neo1p and human ...
1-127 1.57e-15

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: 77.83  E-value: 1.57e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6457264    1 DYSFSQFKFLQRLLLVHGRWSYLRMCKFLCYFFYKNFAFTMVHFWFGFFCGFSAQTVYDQYFITLYNIVYTSLPVLAMgV 80
Cdd:cd07541 640 DFSITQFSHIGRLLLWHGRNSYKRSAKLAQFVMHRGLIISIMQAVFSSVFYFAPIALYQGFLMVGYSTIYTMAPVFSL-V 718
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 6457264   81 FDQDVPEQRSMEYPKLYEPGQLNLLFNKREFFICIAQGIYT-SVLMFL 127
Cdd:cd07541 719 LDQDVSEELAMLYPELYKELTKGRSLSYKTFFIWVLISIYQgGIIMYG 766
 
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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