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Conserved domains on  [gi|17553636|ref|NP_499094|]
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V-type proton ATPase subunit D [Caenorhabditis elegans]

Protein Classification

V-type ATP synthase subunit D( domain architecture ID 10485349)

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
ATP-synt_D pfam01813
ATP synthase subunit D; This is a family of subunit D form various ATP synthases including ...
17-209 1.60e-74

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: 225.18  E-value: 1.60e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553636    17 AQTLMKTRLKGAQKGHSLLKKKADALNLRFRDILRKIVENKVLMGEVMKEAAFSLAEAKFTAG--DFSHTVIQNVSQaQY 94
Cdd:pfam01813   1 ELIRLKKRLKLAQRGHKLLKRKRDALIMEFRKILREIKELREELEEALKEAYFSLALAYALGGeeDVESLALESVPS-VV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553636    95 RVRMKKENVVGVFLPVFDAYQDGPDAYDLTGLGKGGANIARLKKNYNKAIELLVELATLQTCFITLDEAIKVTNRRVNAI 174
Cdd:pfam01813  80 RVEVKTENIMGVKVPVFELVEDERFEIPLYGLLGTGAWLDEAREAFEELLELLIELAELETALRLLAEEIKKTNRRVNAL 159
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 17553636   175 EHVIIPRIENTLTYIVTELDEMEREEFFRMKKIQA 209
Cdd:pfam01813 160 EKVVIPRLEETIKYIKSELDEREREEFFRLKKVKA 194
 
Name Accession Description Interval E-value
ATP-synt_D pfam01813
ATP synthase subunit D; This is a family of subunit D form various ATP synthases including ...
17-209 1.60e-74

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: 225.18  E-value: 1.60e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553636    17 AQTLMKTRLKGAQKGHSLLKKKADALNLRFRDILRKIVENKVLMGEVMKEAAFSLAEAKFTAG--DFSHTVIQNVSQaQY 94
Cdd:pfam01813   1 ELIRLKKRLKLAQRGHKLLKRKRDALIMEFRKILREIKELREELEEALKEAYFSLALAYALGGeeDVESLALESVPS-VV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553636    95 RVRMKKENVVGVFLPVFDAYQDGPDAYDLTGLGKGGANIARLKKNYNKAIELLVELATLQTCFITLDEAIKVTNRRVNAI 174
Cdd:pfam01813  80 RVEVKTENIMGVKVPVFELVEDERFEIPLYGLLGTGAWLDEAREAFEELLELLIELAELETALRLLAEEIKKTNRRVNAL 159
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 17553636   175 EHVIIPRIENTLTYIVTELDEMEREEFFRMKKIQA 209
Cdd:pfam01813 160 EKVVIPRLEETIKYIKSELDEREREEFFRLKKVKA 194
V_ATPase_subD TIGR00309
H(+)-transporting ATP synthase, vacuolar type, subunit D; Although this ATPase can run ...
11-213 4.47e-62

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: 193.89  E-value: 4.47e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553636    11 VFPSRMAQTLMKTRLKGAQKGHSLLKKKADALNLRFRDILRKIVENKVLMGEVMKEAAFSLAEAKFTAGDF-SHTVIQNV 89
Cdd:TIGR00309   4 VNPTRMELLKLKDKLKMAKRGYSLLKLKRDALIMEFRQILERAKDIKNKMEQKLKEAISDLIEAQSVMGPFaVWIAALSV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553636    90 SQAQYRVRMKKENVVGVFLPVFDAYQDGPDAYD-LTGLGKGGANIARLKKNYNKAIELLVELATLQTCFITLDEAIKVTN 168
Cdd:TIGR00309  84 VTARFEVDMKSKNIMGVVVPVFDSYEIRRKVHErGYGLLFTSYKVDEAAEIYEEAVELIVELAEIETTIRLLAEEIEITK 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 17553636   169 RRVNAIEHVIIPRIENTLTYIVTELDEMEREEFFRMKKIQANKKK 213
Cdd:TIGR00309 164 RRVNALEHVIIPRLKNTIKYINMRLDEMDRENFVRLKKIKSSKEK 208
NtpD COG1394
Archaeal/vacuolar-type H+-ATPase subunit D/Vma8 [Energy production and conversion]; Archaeal ...
11-211 3.80e-38

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: 132.28  E-value: 3.80e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553636  11 VFPSRMAQTLMKTRLKGAQKGHSLLKKKADALNLRFRDILRKIVENKVLMGEVMKEAAFSLAEAKFTAGDFSHTVIQNVS 90
Cdd:COG1394   4 VKPTKMELLRLKRQLKLAKRGHKLLKDKRDALIREFLKLIDEAEELREELEELLEEAYEALALANARMGIEAVEELALSV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553636  91 QAQYRVRMKKENVVGVFLPVFDAYQDGPDA-YDLTGLGkggANIARLKKNYNKAIELLVELATLQTCFITLDEAIKVTNR 169
Cdd:COG1394  84 PRVLEVEVSTRNIMGVEVPVLESEEFKEERpYGLLGTS---AWLDEAIEALEELLELLLELAELETALRRLAEEIRKTQR 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 17553636 170 RVNAIEHVIIPRIENTLTYIVTELDEMEREEFFRMKKIQANK 211
Cdd:COG1394 161 RVNALEKVLIPRLEETIKYIRMKLEEREREEFVRLKKVKKKL 202
PRK00373 PRK00373
V-type ATP synthase subunit D; Reviewed
11-209 3.35e-36

V-type ATP synthase subunit D; Reviewed


Pssm-ID: 178991  Cd Length: 204  Bit Score: 127.25  E-value: 3.35e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553636   11 VFPSRMAQTLMKTRLKGAQKGHSLLKKKADALNLRFRDILRkivENKVLMGEV---MKEAAFSLAEAKFTAGDFSHTVIQ 87
Cdd:PRK00373   6 VKPTRMELINLKRRLKLAERGHKLLKDKRDELIMEFFDILD---EAKKLREEVeeeLEEAYKDFLMARAVEGSLAVEEAA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553636   88 NVSQAQYRVRMKKENVVGVFLPVFDAYQDGPDAYDLTGLGKGGANIARLKKNYNKAIELLVELATLQ-TCFITLDEaIKV 166
Cdd:PRK00373  83 ASPKESLEVDVSSKNIMGVVVPVIELSVKRTLPERGYGFLGTSAELDEAAEKFEELLEKILELAEVEkTIQLLADE-IEK 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 17553636  167 TNRRVNAIEHVIIPRIENTLTYIVTELDEMEREEFFRMKKIQA 209
Cdd:PRK00373 162 TKRRVNALEYVIIPRLEETIKYIKMKLDEMERENFVRLKKIKS 204
 
Name Accession Description Interval E-value
ATP-synt_D pfam01813
ATP synthase subunit D; This is a family of subunit D form various ATP synthases including ...
17-209 1.60e-74

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: 225.18  E-value: 1.60e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553636    17 AQTLMKTRLKGAQKGHSLLKKKADALNLRFRDILRKIVENKVLMGEVMKEAAFSLAEAKFTAG--DFSHTVIQNVSQaQY 94
Cdd:pfam01813   1 ELIRLKKRLKLAQRGHKLLKRKRDALIMEFRKILREIKELREELEEALKEAYFSLALAYALGGeeDVESLALESVPS-VV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553636    95 RVRMKKENVVGVFLPVFDAYQDGPDAYDLTGLGKGGANIARLKKNYNKAIELLVELATLQTCFITLDEAIKVTNRRVNAI 174
Cdd:pfam01813  80 RVEVKTENIMGVKVPVFELVEDERFEIPLYGLLGTGAWLDEAREAFEELLELLIELAELETALRLLAEEIKKTNRRVNAL 159
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 17553636   175 EHVIIPRIENTLTYIVTELDEMEREEFFRMKKIQA 209
Cdd:pfam01813 160 EKVVIPRLEETIKYIKSELDEREREEFFRLKKVKA 194
V_ATPase_subD TIGR00309
H(+)-transporting ATP synthase, vacuolar type, subunit D; Although this ATPase can run ...
11-213 4.47e-62

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: 193.89  E-value: 4.47e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553636    11 VFPSRMAQTLMKTRLKGAQKGHSLLKKKADALNLRFRDILRKIVENKVLMGEVMKEAAFSLAEAKFTAGDF-SHTVIQNV 89
Cdd:TIGR00309   4 VNPTRMELLKLKDKLKMAKRGYSLLKLKRDALIMEFRQILERAKDIKNKMEQKLKEAISDLIEAQSVMGPFaVWIAALSV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553636    90 SQAQYRVRMKKENVVGVFLPVFDAYQDGPDAYD-LTGLGKGGANIARLKKNYNKAIELLVELATLQTCFITLDEAIKVTN 168
Cdd:TIGR00309  84 VTARFEVDMKSKNIMGVVVPVFDSYEIRRKVHErGYGLLFTSYKVDEAAEIYEEAVELIVELAEIETTIRLLAEEIEITK 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 17553636   169 RRVNAIEHVIIPRIENTLTYIVTELDEMEREEFFRMKKIQANKKK 213
Cdd:TIGR00309 164 RRVNALEHVIIPRLKNTIKYINMRLDEMDRENFVRLKKIKSSKEK 208
NtpD COG1394
Archaeal/vacuolar-type H+-ATPase subunit D/Vma8 [Energy production and conversion]; Archaeal ...
11-211 3.80e-38

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: 132.28  E-value: 3.80e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553636  11 VFPSRMAQTLMKTRLKGAQKGHSLLKKKADALNLRFRDILRKIVENKVLMGEVMKEAAFSLAEAKFTAGDFSHTVIQNVS 90
Cdd:COG1394   4 VKPTKMELLRLKRQLKLAKRGHKLLKDKRDALIREFLKLIDEAEELREELEELLEEAYEALALANARMGIEAVEELALSV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553636  91 QAQYRVRMKKENVVGVFLPVFDAYQDGPDA-YDLTGLGkggANIARLKKNYNKAIELLVELATLQTCFITLDEAIKVTNR 169
Cdd:COG1394  84 PRVLEVEVSTRNIMGVEVPVLESEEFKEERpYGLLGTS---AWLDEAIEALEELLELLLELAELETALRRLAEEIRKTQR 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 17553636 170 RVNAIEHVIIPRIENTLTYIVTELDEMEREEFFRMKKIQANK 211
Cdd:COG1394 161 RVNALEKVLIPRLEETIKYIRMKLEEREREEFVRLKKVKKKL 202
PRK00373 PRK00373
V-type ATP synthase subunit D; Reviewed
11-209 3.35e-36

V-type ATP synthase subunit D; Reviewed


Pssm-ID: 178991  Cd Length: 204  Bit Score: 127.25  E-value: 3.35e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553636   11 VFPSRMAQTLMKTRLKGAQKGHSLLKKKADALNLRFRDILRkivENKVLMGEV---MKEAAFSLAEAKFTAGDFSHTVIQ 87
Cdd:PRK00373   6 VKPTRMELINLKRRLKLAERGHKLLKDKRDELIMEFFDILD---EAKKLREEVeeeLEEAYKDFLMARAVEGSLAVEEAA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553636   88 NVSQAQYRVRMKKENVVGVFLPVFDAYQDGPDAYDLTGLGKGGANIARLKKNYNKAIELLVELATLQ-TCFITLDEaIKV 166
Cdd:PRK00373  83 ASPKESLEVDVSSKNIMGVVVPVIELSVKRTLPERGYGFLGTSAELDEAAEKFEELLEKILELAEVEkTIQLLADE-IEK 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 17553636  167 TNRRVNAIEHVIIPRIENTLTYIVTELDEMEREEFFRMKKIQA 209
Cdd:PRK00373 162 TKRRVNALEYVIIPRLEETIKYIKMKLDEMERENFVRLKKIKS 204
PRK02195 PRK02195
V-type ATP synthase subunit D; Provisional
95-212 4.48e-03

V-type ATP synthase subunit D; Provisional


Pssm-ID: 179382  Cd Length: 201  Bit Score: 37.22  E-value: 4.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553636   95 RVRMKKENVVGVFLPVFDA--YQDGPdaYDLTG----LGKGganIARLKKnynkAIELLVELATLQTCFITLDEAIKVTN 168
Cdd:PRK02195  83 KVEKDYENIAGVEVPILDSieFEIIE--YSLLNtpiwVDTG---IELLKE----LVQLKIEAEVLQERLLLLEEELRKTT 153
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 17553636  169 RRVNAIEHVIIPRIENTLTYIVTELDEMEREEFFRMK----KIQANKK 212
Cdd:PRK02195 154 QRVNLFEKVLIPETKANIKKIKIFLGDQETAAVVRQKiakkKIEKRKE 201
 
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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