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Conserved domains on  [gi|20128937|ref|NP_570008|]
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vacuolar H[+] ATPase 36kD subunit 3, isoform B [Drosophila melanogaster]

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 ...
15-207 2.33e-70

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: 214.01  E-value: 2.33e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128937    15 AQTLMKSRLAGATKGHGLLKKKADALQMRFRLILGKIIETKTLMGQVMKEAAFSLAEVKFTTG--DINQIVLQNVtKAQI 92
Cdd:pfam01813   1 ELIRLKKRLKLAQRGHKLLKRKRDALIMEFRKILREIKELREELEEALKEAYFSLALAYALGGeeDVESLALESV-PSVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128937    93 KIRTKKDNVAGVTLPIFEPYTDGVDTYELAGLARGGQQLAKLKKNYQSAVRLLVQLASLQTSFVTLDDVIKVTNRRVNAI 172
Cdd:pfam01813  80 RVEVKTENIMGVKVPVFELVEDERFEIPLYGLLGTGAWLDEAREAFEELLELLIELAELETALRLLAEEIKKTNRRVNAL 159
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 20128937   173 EHVIIPRINRTIEYIISELDELEREEFYRLKKIQD 207
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 ...
15-207 2.33e-70

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: 214.01  E-value: 2.33e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128937    15 AQTLMKSRLAGATKGHGLLKKKADALQMRFRLILGKIIETKTLMGQVMKEAAFSLAEVKFTTG--DINQIVLQNVtKAQI 92
Cdd:pfam01813   1 ELIRLKKRLKLAQRGHKLLKRKRDALIMEFRKILREIKELREELEEALKEAYFSLALAYALGGeeDVESLALESV-PSVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128937    93 KIRTKKDNVAGVTLPIFEPYTDGVDTYELAGLARGGQQLAKLKKNYQSAVRLLVQLASLQTSFVTLDDVIKVTNRRVNAI 172
Cdd:pfam01813  80 RVEVKTENIMGVKVPVFELVEDERFEIPLYGLLGTGAWLDEAREAFEELLELLIELAELETALRLLAEEIKKTNRRVNAL 159
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 20128937   173 EHVIIPRINRTIEYIISELDELEREEFYRLKKIQD 207
Cdd:pfam01813 160 EKVVIPRLEETIKYIKSELDEREREEFFRLKKVKA 194
V_ATPase_subD TIGR00309
H(+)-transporting ATP synthase, vacuolar type, subunit D; Although this ATPase can run ...
9-209 1.76e-52

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: 169.23  E-value: 1.76e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128937     9 IFPSRGAQTLMKSRLAGATKGHGLLKKKADALQMRFRLILGKIIETKTLMGQVMKEAAFSLAEVKFTTGD-INQIVLQNV 87
Cdd:TIGR00309   4 VNPTRMELLKLKDKLKMAKRGYSLLKLKRDALIMEFRQILERAKDIKNKMEQKLKEAISDLIEAQSVMGPfAVWIAALSV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128937    88 TKAQIKIRTKKDNVAGVTLPIFEPY-TDGVDTYELAGLARGGQQLAKLKKNYQSAVRLLVQLASLQTSFVTLDDVIKVTN 166
Cdd:TIGR00309  84 VTARFEVDMKSKNIMGVVVPVFDSYeIRRKVHERGYGLLFTSYKVDEAAEIYEEAVELIVELAEIETTIRLLAEEIEITK 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 20128937   167 RRVNAIEHVIIPRINRTIEYIISELDELEREEFYRLKKIQDKK 209
Cdd:TIGR00309 164 RRVNALEHVIIPRLKNTIKYINMRLDEMDRENFVRLKKIKSSK 206
NtpD COG1394
Archaeal/vacuolar-type H+-ATPase subunit D/Vma8 [Energy production and conversion]; Archaeal ...
9-209 4.12e-35

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: 124.19  E-value: 4.12e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128937   9 IFPSRGAQTLMKSRLAGATKGHGLLKKKADALQMRFRLILGKIIETKTLMGQVMKEAAFSLAEVKFTTGDINQIVLQNVT 88
Cdd:COG1394   4 VKPTKMELLRLKRQLKLAKRGHKLLKDKRDALIREFLKLIDEAEELREELEELLEEAYEALALANARMGIEAVEELALSV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128937  89 KAQIKIRTKKDNVAGVTLPIFEPytDGVDTYELAGLARGGQQLAKLKKNYQSAVRLLVQLASLQTSFVTLDDVIKVTNRR 168
Cdd:COG1394  84 PRVLEVEVSTRNIMGVEVPVLES--EEFKEERPYGLLGTSAWLDEAIEALEELLELLLELAELETALRRLAEEIRKTQRR 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 20128937 169 VNAIEHVIIPRINRTIEYIISELDELEREEFYRLKKIQDKK 209
Cdd:COG1394 162 VNALEKVLIPRLEETIKYIRMKLEEREREEFVRLKKVKKKL 202
PRK00373 PRK00373
V-type ATP synthase subunit D; Reviewed
5-207 5.46e-29

V-type ATP synthase subunit D; Reviewed


Pssm-ID: 178991  Cd Length: 204  Bit Score: 108.37  E-value: 5.46e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128937    5 DRLPIFPSRGAQTLMKSRLAGATKGHGLLKKKADALQMRFRLILGKIIETKTLMGQVMKEAAFSLAEVKFTTGDINQIVL 84
Cdd:PRK00373   2 ARLNVKPTRMELINLKRRLKLAERGHKLLKDKRDELIMEFFDILDEAKKLREEVEEELEEAYKDFLMARAVEGSLAVEEA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128937   85 QNVTKAQIKIRTKKDNVAGVTLPIFEpYTDGVDTYELA-GLARGGQQLAKLKKNYQSAVRLLVQLASLQTSFVTLDDVIK 163
Cdd:PRK00373  82 AASPKESLEVDVSSKNIMGVVVPVIE-LSVKRTLPERGyGFLGTSAELDEAAEKFEELLEKILELAEVEKTIQLLADEIE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 20128937  164 VTNRRVNAIEHVIIPRINRTIEYIISELDELEREEFYRLKKIQD 207
Cdd:PRK00373 161 KTKRRVNALEYVIIPRLEETIKYIKMKLDEMERENFVRLKKIKS 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 ...
15-207 2.33e-70

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: 214.01  E-value: 2.33e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128937    15 AQTLMKSRLAGATKGHGLLKKKADALQMRFRLILGKIIETKTLMGQVMKEAAFSLAEVKFTTG--DINQIVLQNVtKAQI 92
Cdd:pfam01813   1 ELIRLKKRLKLAQRGHKLLKRKRDALIMEFRKILREIKELREELEEALKEAYFSLALAYALGGeeDVESLALESV-PSVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128937    93 KIRTKKDNVAGVTLPIFEPYTDGVDTYELAGLARGGQQLAKLKKNYQSAVRLLVQLASLQTSFVTLDDVIKVTNRRVNAI 172
Cdd:pfam01813  80 RVEVKTENIMGVKVPVFELVEDERFEIPLYGLLGTGAWLDEAREAFEELLELLIELAELETALRLLAEEIKKTNRRVNAL 159
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 20128937   173 EHVIIPRINRTIEYIISELDELEREEFYRLKKIQD 207
Cdd:pfam01813 160 EKVVIPRLEETIKYIKSELDEREREEFFRLKKVKA 194
V_ATPase_subD TIGR00309
H(+)-transporting ATP synthase, vacuolar type, subunit D; Although this ATPase can run ...
9-209 1.76e-52

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: 169.23  E-value: 1.76e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128937     9 IFPSRGAQTLMKSRLAGATKGHGLLKKKADALQMRFRLILGKIIETKTLMGQVMKEAAFSLAEVKFTTGD-INQIVLQNV 87
Cdd:TIGR00309   4 VNPTRMELLKLKDKLKMAKRGYSLLKLKRDALIMEFRQILERAKDIKNKMEQKLKEAISDLIEAQSVMGPfAVWIAALSV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128937    88 TKAQIKIRTKKDNVAGVTLPIFEPY-TDGVDTYELAGLARGGQQLAKLKKNYQSAVRLLVQLASLQTSFVTLDDVIKVTN 166
Cdd:TIGR00309  84 VTARFEVDMKSKNIMGVVVPVFDSYeIRRKVHERGYGLLFTSYKVDEAAEIYEEAVELIVELAEIETTIRLLAEEIEITK 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 20128937   167 RRVNAIEHVIIPRINRTIEYIISELDELEREEFYRLKKIQDKK 209
Cdd:TIGR00309 164 RRVNALEHVIIPRLKNTIKYINMRLDEMDRENFVRLKKIKSSK 206
NtpD COG1394
Archaeal/vacuolar-type H+-ATPase subunit D/Vma8 [Energy production and conversion]; Archaeal ...
9-209 4.12e-35

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: 124.19  E-value: 4.12e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128937   9 IFPSRGAQTLMKSRLAGATKGHGLLKKKADALQMRFRLILGKIIETKTLMGQVMKEAAFSLAEVKFTTGDINQIVLQNVT 88
Cdd:COG1394   4 VKPTKMELLRLKRQLKLAKRGHKLLKDKRDALIREFLKLIDEAEELREELEELLEEAYEALALANARMGIEAVEELALSV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128937  89 KAQIKIRTKKDNVAGVTLPIFEPytDGVDTYELAGLARGGQQLAKLKKNYQSAVRLLVQLASLQTSFVTLDDVIKVTNRR 168
Cdd:COG1394  84 PRVLEVEVSTRNIMGVEVPVLES--EEFKEERPYGLLGTSAWLDEAIEALEELLELLLELAELETALRRLAEEIRKTQRR 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 20128937 169 VNAIEHVIIPRINRTIEYIISELDELEREEFYRLKKIQDKK 209
Cdd:COG1394 162 VNALEKVLIPRLEETIKYIRMKLEEREREEFVRLKKVKKKL 202
PRK00373 PRK00373
V-type ATP synthase subunit D; Reviewed
5-207 5.46e-29

V-type ATP synthase subunit D; Reviewed


Pssm-ID: 178991  Cd Length: 204  Bit Score: 108.37  E-value: 5.46e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128937    5 DRLPIFPSRGAQTLMKSRLAGATKGHGLLKKKADALQMRFRLILGKIIETKTLMGQVMKEAAFSLAEVKFTTGDINQIVL 84
Cdd:PRK00373   2 ARLNVKPTRMELINLKRRLKLAERGHKLLKDKRDELIMEFFDILDEAKKLREEVEEELEEAYKDFLMARAVEGSLAVEEA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128937   85 QNVTKAQIKIRTKKDNVAGVTLPIFEpYTDGVDTYELA-GLARGGQQLAKLKKNYQSAVRLLVQLASLQTSFVTLDDVIK 163
Cdd:PRK00373  82 AASPKESLEVDVSSKNIMGVVVPVIE-LSVKRTLPERGyGFLGTSAELDEAAEKFEELLEKILELAEVEKTIQLLADEIE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 20128937  164 VTNRRVNAIEHVIIPRINRTIEYIISELDELEREEFYRLKKIQD 207
Cdd:PRK00373 161 KTKRRVNALEYVIIPRLEETIKYIKMKLDEMERENFVRLKKIKS 204
 
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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