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Conserved domains on  [gi|24649228|ref|NP_651128|]
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vacuolar H[+] ATPase AC39 subunit 2 [Drosophila melanogaster]

Protein Classification

V0D/AC39 family V-type ATPase subunit( domain architecture ID 10488051)

V0D/AC39 family V-type ATPase subunit such as Deinococcus radiodurans V-type ATPase subunit C, 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 ...
12-341 3.91e-82

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: 426553  Cd Length: 333  Bit Score: 252.96  E-value: 3.91e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228    12 LEALTRGFKNGMLKHSDYLNLTQCESLEDVMISIQGTDYGLIFGGEQSAPSVEVIERCLRDRLLQQYYYIRSHSTEPLTT 91
Cdd:pfam01992   1 LNARVRAMESKLLTEEDYERLLQCESLEEAVRYLKETGYGDFLADEESPLHRGDIEKALRRELAKTFEKLRRFAPGLSRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228    92 FMEFIRYPFMIDNVALLVAGLNNHRSMKRLLRMCHPLGEFDQ--LGAIEVASNSAELFDAVLiDTPIARFVPRDLPmESL 169
Cdd:pfam01992  81 FLDLYLYRYDIHNLKLLLRGKLSGLDLEELLEFLIPLGTLSAldLDKLIEAKDVEELVEALL-GTPYAEALEEALD-ELE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228   170 RYLDVEIVRAHLYRAYLEKFYAYCSQLGGNTANVMTNLLSFEADRRTITIAVNAIGS-DIIPKERLKMFPTCGYLPKIAL 248
Cdd:pfam01992 159 ETGDLQLIENALDKAYYEDLYKFCKKLGGKTAEILREYLGFEIDLRNIKIILRSKKYgKLSPEDIYKLLIPGGSLSPEEL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228   249 ASMSTLNDTDKIRDVCNvFDGYGKMFDN-LERDSDGMITLEDRFLMMEAKKNVQT-FLQQYHFGIFYSFIKLKQLEVRNI 326
Cdd:pfam01992 239 KALAEAEDVEEVLAALE-GTPYGELLSEaLEELTGSLSALERALDNYLLELAKKLaRYQPFSIGPVLAYLKLKEQEIRNL 317
                         330
                  ....*....|....*.
gi 24649228   327 VWISECIAQR-QTDRI 341
Cdd:pfam01992 318 RIIAEGKRYGlPPEEI 333
 
Name Accession Description Interval E-value
vATP-synt_AC39 pfam01992
ATP synthase (C/AC39) subunit; This family includes the AC39 subunit from vacuolar ATP ...
12-341 3.91e-82

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: 426553  Cd Length: 333  Bit Score: 252.96  E-value: 3.91e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228    12 LEALTRGFKNGMLKHSDYLNLTQCESLEDVMISIQGTDYGLIFGGEQSAPSVEVIERCLRDRLLQQYYYIRSHSTEPLTT 91
Cdd:pfam01992   1 LNARVRAMESKLLTEEDYERLLQCESLEEAVRYLKETGYGDFLADEESPLHRGDIEKALRRELAKTFEKLRRFAPGLSRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228    92 FMEFIRYPFMIDNVALLVAGLNNHRSMKRLLRMCHPLGEFDQ--LGAIEVASNSAELFDAVLiDTPIARFVPRDLPmESL 169
Cdd:pfam01992  81 FLDLYLYRYDIHNLKLLLRGKLSGLDLEELLEFLIPLGTLSAldLDKLIEAKDVEELVEALL-GTPYAEALEEALD-ELE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228   170 RYLDVEIVRAHLYRAYLEKFYAYCSQLGGNTANVMTNLLSFEADRRTITIAVNAIGS-DIIPKERLKMFPTCGYLPKIAL 248
Cdd:pfam01992 159 ETGDLQLIENALDKAYYEDLYKFCKKLGGKTAEILREYLGFEIDLRNIKIILRSKKYgKLSPEDIYKLLIPGGSLSPEEL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228   249 ASMSTLNDTDKIRDVCNvFDGYGKMFDN-LERDSDGMITLEDRFLMMEAKKNVQT-FLQQYHFGIFYSFIKLKQLEVRNI 326
Cdd:pfam01992 239 KALAEAEDVEEVLAALE-GTPYGELLSEaLEELTGSLSALERALDNYLLELAKKLaRYQPFSIGPVLAYLKLKEQEIRNL 317
                         330
                  ....*....|....*.
gi 24649228   327 VWISECIAQR-QTDRI 341
Cdd:pfam01992 318 RIIAEGKRYGlPPEEI 333
NtpC COG1527
Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 [Energy production and conversion]; Archaeal ...
3-334 2.28e-20

Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441136  Cd Length: 348  Bit Score: 90.40  E-value: 2.28e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228   3 MIFNTEYGYLEALTRGFKNGMLKHSDYLNLTQCESLEDVMISIQGTDYGLIFGGEQSAPS-VEVIERCLRDRLLQQYYYI 81
Cdd:COG1527   1 MASVTNYAYINARIRAMESKLLKEEDYERLLEAESLEEIARFLKETGYGEELDELAERESgRDLLEKALNRNLAKTYRKL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228  82 RSHSTEPLTTFMEFIRYPFMIDNVALLVAGLNNHRSMKRLLRMCHPLGEFDQLGAIE-VASNSAELFDAVLIDTPIARFV 160
Cdd:COG1527  81 LEFAPGELKEFVKLYLLRYDIHNLKVILRGKYSGEDLEEIRELLIPAGELSEEDLKKlLEAKSVEELVEALEGTPYYEAL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228 161 PRDLPM--ESLRYLDVEIVrahLYRAYLEKFYAYCSQLGGNTAnVMTNLLSFEADRRTITIAVNAIGSDIIPKERLKMFP 238
Cdd:COG1527 161 EEALEEyeETGDLFPIENA---LDRAYYENLLELAKKKGKDRK-LLLEYLGTEIDLLNLRTILRLKRYGLSPEEIEAYLI 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228 239 TCGY-LPKIALASMSTLNDTDKIRDVCNvFDGYGKMFDNLE--RDSDGMITLE---DRFLMMEAKKnvqtFLQQYHFGI- 311
Cdd:COG1527 237 PGGYrISEKELKELAEAEDVEELLEALE-GTPYGKLLSELEelEETGSLSEFEralDRYLLEYAKK----LSKYYPFSIg 311
                       330       340
                ....*....|....*....|....
gi 24649228 312 -FYSFIKLKQLEVRNIVWISECIA 334
Cdd:COG1527 312 pVLAYLLAKENEVKNLRIIAEGKR 335
AhaC TIGR02923
ATP synthase A1, C subunit; The A1/A0 ATP synthase is homologous to the V-type (V1/V0, ...
7-326 2.57e-11

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: 64.00  E-value: 2.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228     7 TEYGYLEALTRGFKNGMLKHSDYLNLTQCESLEDVMISIQGTDYGLI---FGGEQSapSVEVIERCLrDRLLQQYYYIRS 83
Cdd:TIGR02923   3 SPYAYPNARVRAMESRLLKEEDFNELLEMRGTDEIVRFLEETDYKKEldeLGSKSY--GVDLIEHAL-DANLAKTYEKLF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228    84 HSTEplttfmEFIRYPFM-------IDNVALLVAGLNNHRSMKRLLRMCHPLGEFDQLgAIEVASNSAELFDAV--LIDT 154
Cdd:TIGR02923  80 RISP------GASRDLIRlylkkwdVWNIKTLIRAKYANASAEEVEDLLIPAGEFLEK-RIKELAEAKTIEEIVeaLEGT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228   155 PIARfVPRDLPMESLRYLDVEivrAHLYRAYLEKFYAYCSQLGGNTANVMTNLLSFEADRRTITIAVNAIGSDIIPKERL 234
Cdd:TIGR02923 153 PYYG-PLQEALAGNGDLSPIE---NELDRMYYEKLLKYVGSPSDDETKLFTEFIKTEVDIRNLKTLLRLKAAGLSPDEIM 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228   235 KMFPTCGYLpkIALASMSTLNDTDKIRDVCNVFDG--YGKMFD-NLERDSDGMITLE---DRFLMMEAKKnvqtFLQQYH 308
Cdd:TIGR02923 229 PYTIPGGYE--LDEEKLAPLAHIESIDEVVSALDGtkYGEDISeVLSEEEKSVAVFEralDEYLIKMATK----LSLRYP 302
                         330       340
                  ....*....|....*....|
gi 24649228   309 FGI--FYSFIKLKQLEVRNI 326
Cdd:TIGR02923 303 LSVgpVLGYILKKEREVRNL 322
 
Name Accession Description Interval E-value
vATP-synt_AC39 pfam01992
ATP synthase (C/AC39) subunit; This family includes the AC39 subunit from vacuolar ATP ...
12-341 3.91e-82

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: 426553  Cd Length: 333  Bit Score: 252.96  E-value: 3.91e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228    12 LEALTRGFKNGMLKHSDYLNLTQCESLEDVMISIQGTDYGLIFGGEQSAPSVEVIERCLRDRLLQQYYYIRSHSTEPLTT 91
Cdd:pfam01992   1 LNARVRAMESKLLTEEDYERLLQCESLEEAVRYLKETGYGDFLADEESPLHRGDIEKALRRELAKTFEKLRRFAPGLSRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228    92 FMEFIRYPFMIDNVALLVAGLNNHRSMKRLLRMCHPLGEFDQ--LGAIEVASNSAELFDAVLiDTPIARFVPRDLPmESL 169
Cdd:pfam01992  81 FLDLYLYRYDIHNLKLLLRGKLSGLDLEELLEFLIPLGTLSAldLDKLIEAKDVEELVEALL-GTPYAEALEEALD-ELE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228   170 RYLDVEIVRAHLYRAYLEKFYAYCSQLGGNTANVMTNLLSFEADRRTITIAVNAIGS-DIIPKERLKMFPTCGYLPKIAL 248
Cdd:pfam01992 159 ETGDLQLIENALDKAYYEDLYKFCKKLGGKTAEILREYLGFEIDLRNIKIILRSKKYgKLSPEDIYKLLIPGGSLSPEEL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228   249 ASMSTLNDTDKIRDVCNvFDGYGKMFDN-LERDSDGMITLEDRFLMMEAKKNVQT-FLQQYHFGIFYSFIKLKQLEVRNI 326
Cdd:pfam01992 239 KALAEAEDVEEVLAALE-GTPYGELLSEaLEELTGSLSALERALDNYLLELAKKLaRYQPFSIGPVLAYLKLKEQEIRNL 317
                         330
                  ....*....|....*.
gi 24649228   327 VWISECIAQR-QTDRI 341
Cdd:pfam01992 318 RIIAEGKRYGlPPEEI 333
NtpC COG1527
Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 [Energy production and conversion]; Archaeal ...
3-334 2.28e-20

Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441136  Cd Length: 348  Bit Score: 90.40  E-value: 2.28e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228   3 MIFNTEYGYLEALTRGFKNGMLKHSDYLNLTQCESLEDVMISIQGTDYGLIFGGEQSAPS-VEVIERCLRDRLLQQYYYI 81
Cdd:COG1527   1 MASVTNYAYINARIRAMESKLLKEEDYERLLEAESLEEIARFLKETGYGEELDELAERESgRDLLEKALNRNLAKTYRKL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228  82 RSHSTEPLTTFMEFIRYPFMIDNVALLVAGLNNHRSMKRLLRMCHPLGEFDQLGAIE-VASNSAELFDAVLIDTPIARFV 160
Cdd:COG1527  81 LEFAPGELKEFVKLYLLRYDIHNLKVILRGKYSGEDLEEIRELLIPAGELSEEDLKKlLEAKSVEELVEALEGTPYYEAL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228 161 PRDLPM--ESLRYLDVEIVrahLYRAYLEKFYAYCSQLGGNTAnVMTNLLSFEADRRTITIAVNAIGSDIIPKERLKMFP 238
Cdd:COG1527 161 EEALEEyeETGDLFPIENA---LDRAYYENLLELAKKKGKDRK-LLLEYLGTEIDLLNLRTILRLKRYGLSPEEIEAYLI 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228 239 TCGY-LPKIALASMSTLNDTDKIRDVCNvFDGYGKMFDNLE--RDSDGMITLE---DRFLMMEAKKnvqtFLQQYHFGI- 311
Cdd:COG1527 237 PGGYrISEKELKELAEAEDVEELLEALE-GTPYGKLLSELEelEETGSLSEFEralDRYLLEYAKK----LSKYYPFSIg 311
                       330       340
                ....*....|....*....|....
gi 24649228 312 -FYSFIKLKQLEVRNIVWISECIA 334
Cdd:COG1527 312 pVLAYLLAKENEVKNLRIIAEGKR 335
AhaC TIGR02923
ATP synthase A1, C subunit; The A1/A0 ATP synthase is homologous to the V-type (V1/V0, ...
7-326 2.57e-11

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: 64.00  E-value: 2.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228     7 TEYGYLEALTRGFKNGMLKHSDYLNLTQCESLEDVMISIQGTDYGLI---FGGEQSapSVEVIERCLrDRLLQQYYYIRS 83
Cdd:TIGR02923   3 SPYAYPNARVRAMESRLLKEEDFNELLEMRGTDEIVRFLEETDYKKEldeLGSKSY--GVDLIEHAL-DANLAKTYEKLF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228    84 HSTEplttfmEFIRYPFM-------IDNVALLVAGLNNHRSMKRLLRMCHPLGEFDQLgAIEVASNSAELFDAV--LIDT 154
Cdd:TIGR02923  80 RISP------GASRDLIRlylkkwdVWNIKTLIRAKYANASAEEVEDLLIPAGEFLEK-RIKELAEAKTIEEIVeaLEGT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228   155 PIARfVPRDLPMESLRYLDVEivrAHLYRAYLEKFYAYCSQLGGNTANVMTNLLSFEADRRTITIAVNAIGSDIIPKERL 234
Cdd:TIGR02923 153 PYYG-PLQEALAGNGDLSPIE---NELDRMYYEKLLKYVGSPSDDETKLFTEFIKTEVDIRNLKTLLRLKAAGLSPDEIM 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649228   235 KMFPTCGYLpkIALASMSTLNDTDKIRDVCNVFDG--YGKMFD-NLERDSDGMITLE---DRFLMMEAKKnvqtFLQQYH 308
Cdd:TIGR02923 229 PYTIPGGYE--LDEEKLAPLAHIESIDEVVSALDGtkYGEDISeVLSEEEKSVAVFEralDEYLIKMATK----LSLRYP 302
                         330       340
                  ....*....|....*....|
gi 24649228   309 FGI--FYSFIKLKQLEVRNI 326
Cdd:TIGR02923 303 LSVgpVLGYILKKEREVRNL 322
 
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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