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Conserved domains on  [gi|501225778|ref|WP_012268796|]
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MULTISPECIES: V-type ATP synthase subunit D [Thermoanaerobacter]

Protein Classification

V-type ATP synthase subunit D( domain architecture ID 10011399)

V-type ATP synthase subunit D is part of the catalytic core (V1) of the vacuolar (V)-type ATP synthase complex (V0/V1) that catalyzes the production of ATP from ADP in the presence of a proton gradient across the membrane

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK00373 PRK00373
V-type ATP synthase subunit D; Reviewed
1-204 1.75e-92

V-type ATP synthase subunit D; Reviewed


:

Pssm-ID: 178991  Cd Length: 204  Bit Score: 269.00  E-value: 1.75e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501225778   1 MTMIHVNPTRMELTSLKKRLVTAKRGHKLLKDKQDELVKKFLDMVKQNRALREEVEAELIGAFKSFTMARSQMSANVVEE 80
Cdd:PRK00373   1 MARLNVKPTRMELINLKRRLKLAERGHKLLKDKRDELIMEFFDILDEAKKLREEVEEELEEAYKDFLMARAVEGSLAVEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501225778  81 SLMIPSAKVSINVKKENIMSVNVPKLEILQEESKNLYPYGFANTSAEMDAAIRTLATMLPKMLKLAELEKACQLMADEIE 160
Cdd:PRK00373  81 AAASPKESLEVDVSSKNIMGVVVPVIELSVKRTLPERGYGFLGTSAELDEAAEKFEELLEKILELAEVEKTIQLLADEIE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 501225778 161 KTRRRVNALEYVLIPQLENTIKYITMKLDENERSSRTRLMKIKE 204
Cdd:PRK00373 161 KTKRRVNALEYVIIPRLEETIKYIKMKLDEMERENFVRLKKIKS 204
 
Name Accession Description Interval E-value
PRK00373 PRK00373
V-type ATP synthase subunit D; Reviewed
1-204 1.75e-92

V-type ATP synthase subunit D; Reviewed


Pssm-ID: 178991  Cd Length: 204  Bit Score: 269.00  E-value: 1.75e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501225778   1 MTMIHVNPTRMELTSLKKRLVTAKRGHKLLKDKQDELVKKFLDMVKQNRALREEVEAELIGAFKSFTMARSQMSANVVEE 80
Cdd:PRK00373   1 MARLNVKPTRMELINLKRRLKLAERGHKLLKDKRDELIMEFFDILDEAKKLREEVEEELEEAYKDFLMARAVEGSLAVEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501225778  81 SLMIPSAKVSINVKKENIMSVNVPKLEILQEESKNLYPYGFANTSAEMDAAIRTLATMLPKMLKLAELEKACQLMADEIE 160
Cdd:PRK00373  81 AAASPKESLEVDVSSKNIMGVVVPVIELSVKRTLPERGYGFLGTSAELDEAAEKFEELLEKILELAEVEKTIQLLADEIE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 501225778 161 KTRRRVNALEYVLIPQLENTIKYITMKLDENERSSRTRLMKIKE 204
Cdd:PRK00373 161 KTKRRVNALEYVIIPRLEETIKYIKMKLDEMERENFVRLKKIKS 204
NtpD COG1394
Archaeal/vacuolar-type H+-ATPase subunit D/Vma8 [Energy production and conversion]; Archaeal ...
3-205 2.64e-75

Archaeal/vacuolar-type H+-ATPase subunit D/Vma8 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit D/Vma8 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441004  Cd Length: 202  Bit Score: 225.50  E-value: 2.64e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501225778   3 MIHVNPTRMELTSLKKRLVTAKRGHKLLKDKQDELVKKFLDMVKQNRALREEVEAELIGAFKSFTMARSQMSANVVEESL 82
Cdd:COG1394    1 AAKVKPTKMELLRLKRQLKLAKRGHKLLKDKRDALIREFLKLIDEAEELREELEELLEEAYEALALANARMGIEAVEELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501225778  83 MIPSAKVSINVKKENIMSVNVPKLEIlqEESKNLYPYGFANTSAEMDAAIRTLATMLPKMLKLAELEKACQLMADEIEKT 162
Cdd:COG1394   81 LSVPRVLEVEVSTRNIMGVEVPVLES--EEFKEERPYGLLGTSAWLDEAIEALEELLELLLELAELETALRRLAEEIRKT 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 501225778 163 RRRVNALEYVLIPQLENTIKYITMKLDENERSSRTRLMKIKEM 205
Cdd:COG1394  159 QRRVNALEKVLIPRLEETIKYIRMKLEEREREEFVRLKKVKKK 201
ATP-synt_D pfam01813
ATP synthase subunit D; This is a family of subunit D form various ATP synthases including ...
12-204 2.13e-67

ATP synthase subunit D; This is a family of subunit D form various ATP synthases including V-type H+ transporting and Na+ dependent. Subunit D is suggested to be an integral part of the catalytic sector of the V-ATPase.


Pssm-ID: 460343  Cd Length: 194  Bit Score: 205.15  E-value: 2.13e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501225778   12 ELTSLKKRLVTAKRGHKLLKDKQDELVKKFLDMVKQNRALREEVEAELIGAFKSFTMARSQMSANVVEE-SLMIPSAKVS 90
Cdd:pfam01813   1 ELIRLKKRLKLAQRGHKLLKRKRDALIMEFRKILREIKELREELEEALKEAYFSLALAYALGGEEDVESlALESVPSVVR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501225778   91 INVKKENIMSVNVPKLEILQEESKNLYPYGFANTSAEMDAAIRTLATMLPKMLKLAELEKACQLMADEIEKTRRRVNALE 170
Cdd:pfam01813  81 VEVKTENIMGVKVPVFELVEDERFEIPLYGLLGTGAWLDEAREAFEELLELLIELAELETALRLLAEEIKKTNRRVNALE 160
                         170       180       190
                  ....*....|....*....|....*....|....
gi 501225778  171 YVLIPQLENTIKYITMKLDENERSSRTRLMKIKE 204
Cdd:pfam01813 161 KVVIPRLEETIKYIKSELDEREREEFFRLKKVKA 194
V_ATPase_subD TIGR00309
H(+)-transporting ATP synthase, vacuolar type, subunit D; Although this ATPase can run ...
3-208 3.99e-40

H(+)-transporting ATP synthase, vacuolar type, subunit D; Although this ATPase can run backwards, using a proton gradient to synthesize ATP, the primary biological role is to acidify some compartment, such as yeast vacuole (a lysosomal homolog) or the interior of a prokaryote. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 129409  Cd Length: 209  Bit Score: 136.11  E-value: 3.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501225778    3 MIHVNPTRMELTSLKKRLVTAKRGHKLLKDKQDELVKKFLDMVKQNRALREEVEAELIGAFKSFTMARSQMSANVVEESL 82
Cdd:TIGR00309   1 MEKVNPTRMELLKLKDKLKMAKRGYSLLKLKRDALIMEFRQILERAKDIKNKMEQKLKEAISDLIEAQSVMGPFAVWIAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501225778   83 M-IPSAKVSINVKKENIMSVNVPKLEILQEESK-NLYPYGFANTSAEMDAAIRTLATMLPKMLKLAELEKACQLMADEIE 160
Cdd:TIGR00309  81 LsVVTARFEVDMKSKNIMGVVVPVFDSYEIRRKvHERGYGLLFTSYKVDEAAEIYEEAVELIVELAEIETTIRLLAEEIE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 501225778  161 KTRRRVNALEYVLIPQLENTIKYITMKLDENERSSRTRLMKIKEMVMK 208
Cdd:TIGR00309 161 ITKRRVNALEHVIIPRLKNTIKYINMRLDEMDRENFVRLKKIKSSKEK 208
 
Name Accession Description Interval E-value
PRK00373 PRK00373
V-type ATP synthase subunit D; Reviewed
1-204 1.75e-92

V-type ATP synthase subunit D; Reviewed


Pssm-ID: 178991  Cd Length: 204  Bit Score: 269.00  E-value: 1.75e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501225778   1 MTMIHVNPTRMELTSLKKRLVTAKRGHKLLKDKQDELVKKFLDMVKQNRALREEVEAELIGAFKSFTMARSQMSANVVEE 80
Cdd:PRK00373   1 MARLNVKPTRMELINLKRRLKLAERGHKLLKDKRDELIMEFFDILDEAKKLREEVEEELEEAYKDFLMARAVEGSLAVEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501225778  81 SLMIPSAKVSINVKKENIMSVNVPKLEILQEESKNLYPYGFANTSAEMDAAIRTLATMLPKMLKLAELEKACQLMADEIE 160
Cdd:PRK00373  81 AAASPKESLEVDVSSKNIMGVVVPVIELSVKRTLPERGYGFLGTSAELDEAAEKFEELLEKILELAEVEKTIQLLADEIE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 501225778 161 KTRRRVNALEYVLIPQLENTIKYITMKLDENERSSRTRLMKIKE 204
Cdd:PRK00373 161 KTKRRVNALEYVIIPRLEETIKYIKMKLDEMERENFVRLKKIKS 204
NtpD COG1394
Archaeal/vacuolar-type H+-ATPase subunit D/Vma8 [Energy production and conversion]; Archaeal ...
3-205 2.64e-75

Archaeal/vacuolar-type H+-ATPase subunit D/Vma8 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit D/Vma8 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441004  Cd Length: 202  Bit Score: 225.50  E-value: 2.64e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501225778   3 MIHVNPTRMELTSLKKRLVTAKRGHKLLKDKQDELVKKFLDMVKQNRALREEVEAELIGAFKSFTMARSQMSANVVEESL 82
Cdd:COG1394    1 AAKVKPTKMELLRLKRQLKLAKRGHKLLKDKRDALIREFLKLIDEAEELREELEELLEEAYEALALANARMGIEAVEELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501225778  83 MIPSAKVSINVKKENIMSVNVPKLEIlqEESKNLYPYGFANTSAEMDAAIRTLATMLPKMLKLAELEKACQLMADEIEKT 162
Cdd:COG1394   81 LSVPRVLEVEVSTRNIMGVEVPVLES--EEFKEERPYGLLGTSAWLDEAIEALEELLELLLELAELETALRRLAEEIRKT 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 501225778 163 RRRVNALEYVLIPQLENTIKYITMKLDENERSSRTRLMKIKEM 205
Cdd:COG1394  159 QRRVNALEKVLIPRLEETIKYIRMKLEEREREEFVRLKKVKKK 201
ATP-synt_D pfam01813
ATP synthase subunit D; This is a family of subunit D form various ATP synthases including ...
12-204 2.13e-67

ATP synthase subunit D; This is a family of subunit D form various ATP synthases including V-type H+ transporting and Na+ dependent. Subunit D is suggested to be an integral part of the catalytic sector of the V-ATPase.


Pssm-ID: 460343  Cd Length: 194  Bit Score: 205.15  E-value: 2.13e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501225778   12 ELTSLKKRLVTAKRGHKLLKDKQDELVKKFLDMVKQNRALREEVEAELIGAFKSFTMARSQMSANVVEE-SLMIPSAKVS 90
Cdd:pfam01813   1 ELIRLKKRLKLAQRGHKLLKRKRDALIMEFRKILREIKELREELEEALKEAYFSLALAYALGGEEDVESlALESVPSVVR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501225778   91 INVKKENIMSVNVPKLEILQEESKNLYPYGFANTSAEMDAAIRTLATMLPKMLKLAELEKACQLMADEIEKTRRRVNALE 170
Cdd:pfam01813  81 VEVKTENIMGVKVPVFELVEDERFEIPLYGLLGTGAWLDEAREAFEELLELLIELAELETALRLLAEEIKKTNRRVNALE 160
                         170       180       190
                  ....*....|....*....|....*....|....
gi 501225778  171 YVLIPQLENTIKYITMKLDENERSSRTRLMKIKE 204
Cdd:pfam01813 161 KVVIPRLEETIKYIKSELDEREREEFFRLKKVKA 194
V_ATPase_subD TIGR00309
H(+)-transporting ATP synthase, vacuolar type, subunit D; Although this ATPase can run ...
3-208 3.99e-40

H(+)-transporting ATP synthase, vacuolar type, subunit D; Although this ATPase can run backwards, using a proton gradient to synthesize ATP, the primary biological role is to acidify some compartment, such as yeast vacuole (a lysosomal homolog) or the interior of a prokaryote. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 129409  Cd Length: 209  Bit Score: 136.11  E-value: 3.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501225778    3 MIHVNPTRMELTSLKKRLVTAKRGHKLLKDKQDELVKKFLDMVKQNRALREEVEAELIGAFKSFTMARSQMSANVVEESL 82
Cdd:TIGR00309   1 MEKVNPTRMELLKLKDKLKMAKRGYSLLKLKRDALIMEFRQILERAKDIKNKMEQKLKEAISDLIEAQSVMGPFAVWIAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501225778   83 M-IPSAKVSINVKKENIMSVNVPKLEILQEESK-NLYPYGFANTSAEMDAAIRTLATMLPKMLKLAELEKACQLMADEIE 160
Cdd:TIGR00309  81 LsVVTARFEVDMKSKNIMGVVVPVFDSYEIRRKvHERGYGLLFTSYKVDEAAEIYEEAVELIVELAEIETTIRLLAEEIE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 501225778  161 KTRRRVNALEYVLIPQLENTIKYITMKLDENERSSRTRLMKIKEMVMK 208
Cdd:TIGR00309 161 ITKRRVNALEHVIIPRLKNTIKYINMRLDEMDRENFVRLKKIKSSKEK 208
PRK02195 PRK02195
V-type ATP synthase subunit D; Provisional
3-202 2.78e-07

V-type ATP synthase subunit D; Provisional


Pssm-ID: 179382  Cd Length: 201  Bit Score: 48.78  E-value: 2.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501225778   3 MIHVNPTRMELTSLKKRLVTAKRGHKLLKDKqdelvKKFLDMVKQN-RALREEVEAELIGAFKSFtmarsQMSANVVEES 81
Cdd:PRK02195   2 MSKIKLTKNSLKKQKKQLKMLERYLPTLKLK-----KAQLQAEVRRaKAEAAELEQEYQKLRQAI-----EAWISLFSEP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501225778  82 LMIPSAKVSI-NVKK--ENIMSVNVPKLEILQEESKnlyPYGFANTSAEMDAAIRTLATMLPKMLKLAELEKACQLMADE 158
Cdd:PRK02195  72 LYFDEDLIKVkKVEKdyENIAGVEVPILDSIEFEII---EYSLLNTPIWVDTGIELLKELVQLKIEAEVLQERLLLLEEE 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 501225778 159 IEKTRRRVNALEYVLIPQLENTIKYITMKLDENERSSRTRlMKI 202
Cdd:PRK02195 149 LRKTTQRVNLFEKVLIPETKANIKKIKIFLGDQETAAVVR-QKI 191
 
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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