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Conserved domains on  [gi|1039767634|ref|XP_017175683|]
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V-type proton ATPase subunit d 2 isoform X1 [Mus musculus]

Protein Classification

V-type ATPase subunit (domain architecture ID 10488051)

V-type ATPase subunit such as Enterococcus hirae V-type sodium ATPase subunit C that is involved in ATP-driven sodium extrusion, and eukaryotic V-type proton ATPase subunit d that is part of the integral membrane V0 proton pore complex of vacuolar ATPase, which is responsible for acidifying a variety of intracellular compartments in cells and providing the energy required for transport in the vacuolar system

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
vATP-synt_AC39 pfam01992
ATP synthase (C/AC39) subunit; This family includes the AC39 subunit from vacuolar ATP ...
1-234 1.30e-63

ATP synthase (C/AC39) subunit; This family includes the AC39 subunit from vacuolar ATP synthase, and the C subunit from archaebacterial ATP synthase. The family also includes subunit C from the Sodium transporting ATP synthase from Enterococcus hirae.


:

Pssm-ID: 396538  Cd Length: 333  Bit Score: 201.35  E-value: 1.30e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767634   1 MIDNIILLMNGALQKKSVKEVLAKCHPLGRFT--EMEAVNIAETPSDLFKAVLvETPLAPFFQDCMsENTLDELNIELLR 78
Cdd:pfam01992  90 DIHNLKLLLRGKLSGLDLEELLEFLIPLGTLSalDLDKLIEAKDVEELPEALL-GTPYAEALEEAL-DELEETGDLQLIE 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767634  79 NKLYKSYLEAFYKFCKDHGDVTADVMCPILEFEADRRALIITLNSFG-TELSKEDRETLFPTCGRLYPEGLRLLAQAEDF 157
Cdd:pfam01992 168 NALDKAYYEDLYKFCKKLGGKTAEILREYLGFEIDLRNIKIILRSKKyGKLSPEEIYKLLIPGGSLSPEELKALAEAEDV 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767634 158 EQMKRVADNYGvYKPLFDAVGGSGG---KTLEDVFYEREVQMNV-LAFNRQFHYGVFYAYVKLKEQEMRNIVWIAECISQ 233
Cdd:pfam01992 248 EEVLAALEGTP-YGELLSEALEELTgslSALERALDRYLLELAKkLARYQPFSIGPILAYLKLKEQEIRNLRIIAEGKRY 326

                  .
gi 1039767634 234 R 234
Cdd:pfam01992 327 G 327
 
Name Accession Description Interval E-value
vATP-synt_AC39 pfam01992
ATP synthase (C/AC39) subunit; This family includes the AC39 subunit from vacuolar ATP ...
1-234 1.30e-63

ATP synthase (C/AC39) subunit; This family includes the AC39 subunit from vacuolar ATP synthase, and the C subunit from archaebacterial ATP synthase. The family also includes subunit C from the Sodium transporting ATP synthase from Enterococcus hirae.


Pssm-ID: 396538  Cd Length: 333  Bit Score: 201.35  E-value: 1.30e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767634   1 MIDNIILLMNGALQKKSVKEVLAKCHPLGRFT--EMEAVNIAETPSDLFKAVLvETPLAPFFQDCMsENTLDELNIELLR 78
Cdd:pfam01992  90 DIHNLKLLLRGKLSGLDLEELLEFLIPLGTLSalDLDKLIEAKDVEELPEALL-GTPYAEALEEAL-DELEETGDLQLIE 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767634  79 NKLYKSYLEAFYKFCKDHGDVTADVMCPILEFEADRRALIITLNSFG-TELSKEDRETLFPTCGRLYPEGLRLLAQAEDF 157
Cdd:pfam01992 168 NALDKAYYEDLYKFCKKLGGKTAEILREYLGFEIDLRNIKIILRSKKyGKLSPEEIYKLLIPGGSLSPEELKALAEAEDV 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767634 158 EQMKRVADNYGvYKPLFDAVGGSGG---KTLEDVFYEREVQMNV-LAFNRQFHYGVFYAYVKLKEQEMRNIVWIAECISQ 233
Cdd:pfam01992 248 EEVLAALEGTP-YGELLSEALEELTgslSALERALDRYLLELAKkLARYQPFSIGPILAYLKLKEQEIRNLRIIAEGKRY 326

                  .
gi 1039767634 234 R 234
Cdd:pfam01992 327 G 327
NtpC COG1527
Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 [Energy production and conversion];
1-246 2.29e-39

Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 [Energy production and conversion];


Pssm-ID: 224444  Cd Length: 346  Bit Score: 139.02  E-value: 2.29e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767634   1 MIDNIILLMNGALQKKSvKEVLAKCHPLGRFTEMEAVNIAETPSDLFKAVLVETPLAPFFQDCMSEntLDELNIELLRNK 80
Cdd:COG1527   100 DIENIKTLLRAKLAGDP-EEISDLLIPLGDFETLLTLAEAKTMEEVVETLEGTTYLAPLEEALRDY--EDTGDIEPLENA 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767634  81 LYKSYLEAFYKFCKDHGDvtADVMCPILEFEADRRALIITLNSFGTELSKEDRETLFPTCGRLYPEGLRLLAQAEDFEQM 160
Cdd:COG1527   177 LDKAYYEDLLRSVNSEKG--DELLREFLRLEIDRRNIKTALRGKASELSEELMESLIPDGGSLDASALRDLAEAEDILDV 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767634 161 KRVADNYGVYKPLFDAVGG---SGGKTLEDVFYEREVQMNVLAFNRQFHYGVF--YAYVKLKEQEMRNIVWIAECISQ-R 234
Cdd:COG1527   255 LEALEGTSYGDALSEYREEyeeGGSIAVFEEALRKALLKRAKEFAQYYPLSVGpvLAYLLRKEIEVKNLRWIAEGKANgL 334
                         250
                  ....*....|..
gi 1039767634 235 HRTKINSYIPIL 246
Cdd:COG1527   335 PREEIKELLVPL 346
AhaC TIGR02923
ATP synthase A1, C subunit; The A1/A0 ATP synthase is homologous to the V-type (V1/V0, ...
4-228 3.55e-08

ATP synthase A1, C subunit; The A1/A0 ATP synthase is homologous to the V-type (V1/V0, vacuolar) ATPase, but functions in the ATP synthetic direction as does the F1/F0 ATPase of bacteria. The C subunit is part of the hydrophilic A1 "stalk" complex (AhaABCDEFG), which is the site of ATP generation and is coupled to the membrane-embedded proton translocating A0 complex.


Pssm-ID: 274352  Cd Length: 343  Bit Score: 53.22  E-value: 3.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767634   4 NIILLMNGALQKKSVKEVLAKCHPLGRFTE--MEAVNIAETPSDLFKAvLVETPLAPFFQDCMSENTldelNIELLRNKL 81
Cdd:TIGR02923 101 NIKTLIRAKYANASAEEVEDLLIPAGEFLEkrIKELAEAKTIEEIVEA-LEGTPYYGPLQEALAGNG----DLSPIENEL 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767634  82 YKSYLEAFYKFCKDHGDVTADVMCPILEFEADRRALIITLNSFGTELS-KEDRETLFPTCGRLYPEGLRLLAQAEDFEQM 160
Cdd:TIGR02923 176 DRMYYEKLLKYVGSPSDDETKLFTEFIKTEVDIRNLKTLLRLKAAGLSpDEIMPYTIPGGYELDEEKLAPLAHIESIDEV 255
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039767634 161 KRVADNYGvYKPLFDAVGGSGGK---TLEDVFYEREVQM-NVLAFNRQFHYGVFYAYVKLKEQEMRNIVWIA 228
Cdd:TIGR02923 256 VSALDGTK-YGEDISEVLSEEEKsvaVFERALDEYLIKMaTKLSLRYPLSVGPVLGYILKKEREVRNLRAIA 326
 
Name Accession Description Interval E-value
vATP-synt_AC39 pfam01992
ATP synthase (C/AC39) subunit; This family includes the AC39 subunit from vacuolar ATP ...
1-234 1.30e-63

ATP synthase (C/AC39) subunit; This family includes the AC39 subunit from vacuolar ATP synthase, and the C subunit from archaebacterial ATP synthase. The family also includes subunit C from the Sodium transporting ATP synthase from Enterococcus hirae.


Pssm-ID: 396538  Cd Length: 333  Bit Score: 201.35  E-value: 1.30e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767634   1 MIDNIILLMNGALQKKSVKEVLAKCHPLGRFT--EMEAVNIAETPSDLFKAVLvETPLAPFFQDCMsENTLDELNIELLR 78
Cdd:pfam01992  90 DIHNLKLLLRGKLSGLDLEELLEFLIPLGTLSalDLDKLIEAKDVEELPEALL-GTPYAEALEEAL-DELEETGDLQLIE 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767634  79 NKLYKSYLEAFYKFCKDHGDVTADVMCPILEFEADRRALIITLNSFG-TELSKEDRETLFPTCGRLYPEGLRLLAQAEDF 157
Cdd:pfam01992 168 NALDKAYYEDLYKFCKKLGGKTAEILREYLGFEIDLRNIKIILRSKKyGKLSPEEIYKLLIPGGSLSPEELKALAEAEDV 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767634 158 EQMKRVADNYGvYKPLFDAVGGSGG---KTLEDVFYEREVQMNV-LAFNRQFHYGVFYAYVKLKEQEMRNIVWIAECISQ 233
Cdd:pfam01992 248 EEVLAALEGTP-YGELLSEALEELTgslSALERALDRYLLELAKkLARYQPFSIGPILAYLKLKEQEIRNLRIIAEGKRY 326

                  .
gi 1039767634 234 R 234
Cdd:pfam01992 327 G 327
NtpC COG1527
Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 [Energy production and conversion];
1-246 2.29e-39

Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 [Energy production and conversion];


Pssm-ID: 224444  Cd Length: 346  Bit Score: 139.02  E-value: 2.29e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767634   1 MIDNIILLMNGALQKKSvKEVLAKCHPLGRFTEMEAVNIAETPSDLFKAVLVETPLAPFFQDCMSEntLDELNIELLRNK 80
Cdd:COG1527   100 DIENIKTLLRAKLAGDP-EEISDLLIPLGDFETLLTLAEAKTMEEVVETLEGTTYLAPLEEALRDY--EDTGDIEPLENA 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767634  81 LYKSYLEAFYKFCKDHGDvtADVMCPILEFEADRRALIITLNSFGTELSKEDRETLFPTCGRLYPEGLRLLAQAEDFEQM 160
Cdd:COG1527   177 LDKAYYEDLLRSVNSEKG--DELLREFLRLEIDRRNIKTALRGKASELSEELMESLIPDGGSLDASALRDLAEAEDILDV 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767634 161 KRVADNYGVYKPLFDAVGG---SGGKTLEDVFYEREVQMNVLAFNRQFHYGVF--YAYVKLKEQEMRNIVWIAECISQ-R 234
Cdd:COG1527   255 LEALEGTSYGDALSEYREEyeeGGSIAVFEEALRKALLKRAKEFAQYYPLSVGpvLAYLLRKEIEVKNLRWIAEGKANgL 334
                         250
                  ....*....|..
gi 1039767634 235 HRTKINSYIPIL 246
Cdd:COG1527   335 PREEIKELLVPL 346
AhaC TIGR02923
ATP synthase A1, C subunit; The A1/A0 ATP synthase is homologous to the V-type (V1/V0, ...
4-228 3.55e-08

ATP synthase A1, C subunit; The A1/A0 ATP synthase is homologous to the V-type (V1/V0, vacuolar) ATPase, but functions in the ATP synthetic direction as does the F1/F0 ATPase of bacteria. The C subunit is part of the hydrophilic A1 "stalk" complex (AhaABCDEFG), which is the site of ATP generation and is coupled to the membrane-embedded proton translocating A0 complex.


Pssm-ID: 274352  Cd Length: 343  Bit Score: 53.22  E-value: 3.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767634   4 NIILLMNGALQKKSVKEVLAKCHPLGRFTE--MEAVNIAETPSDLFKAvLVETPLAPFFQDCMSENTldelNIELLRNKL 81
Cdd:TIGR02923 101 NIKTLIRAKYANASAEEVEDLLIPAGEFLEkrIKELAEAKTIEEIVEA-LEGTPYYGPLQEALAGNG----DLSPIENEL 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767634  82 YKSYLEAFYKFCKDHGDVTADVMCPILEFEADRRALIITLNSFGTELS-KEDRETLFPTCGRLYPEGLRLLAQAEDFEQM 160
Cdd:TIGR02923 176 DRMYYEKLLKYVGSPSDDETKLFTEFIKTEVDIRNLKTLLRLKAAGLSpDEIMPYTIPGGYELDEEKLAPLAHIESIDEV 255
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039767634 161 KRVADNYGvYKPLFDAVGGSGGK---TLEDVFYEREVQM-NVLAFNRQFHYGVFYAYVKLKEQEMRNIVWIA 228
Cdd:TIGR02923 256 VSALDGTK-YGEDISEVLSEEEKsvaVFERALDEYLIKMaTKLSLRYPLSVGPVLGYILKKEREVRNLRAIA 326
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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