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Conserved domains on  [gi|12963799|ref|NP_076210|]
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V-type proton ATPase subunit D [Mus musculus]

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 ...
15-202 8.97e-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: 8.97e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963799    15 AQTIMKARLKGAQTGRNLLKKKSDALTLRFRQILKKIIETKMLMGEVMREAAFSLAEAKFTAG--DFSTTVIQNVNKaQV 92
Cdd:pfam01813   1 ELIRLKKRLKLAQRGHKLLKRKRDALIMEFRKILREIKELREELEEALKEAYFSLALAYALGGeeDVESLALESVPS-VV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963799    93 KIRAKKDNVAGVTLPVFEHYHEGTDSYELTGLARGGEQLAKLKRNYAKAVELLVELASLQTSFVTLDEAIKITNRRVNAI 172
Cdd:pfam01813  80 RVEVKTENIMGVKVPVFELVEDERFEIPLYGLLGTGAWLDEAREAFEELLELLIELAELETALRLLAEEIKKTNRRVNAL 159
                         170       180       190
                  ....*....|....*....|....*....|
gi 12963799   173 EHVIIPRIERTLAYIITELDEREREEFYRL 202
Cdd:pfam01813 160 EKVVIPRLEETIKYIKSELDEREREEFFRL 189
 
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 ...
15-202 8.97e-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: 8.97e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963799    15 AQTIMKARLKGAQTGRNLLKKKSDALTLRFRQILKKIIETKMLMGEVMREAAFSLAEAKFTAG--DFSTTVIQNVNKaQV 92
Cdd:pfam01813   1 ELIRLKKRLKLAQRGHKLLKRKRDALIMEFRKILREIKELREELEEALKEAYFSLALAYALGGeeDVESLALESVPS-VV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963799    93 KIRAKKDNVAGVTLPVFEHYHEGTDSYELTGLARGGEQLAKLKRNYAKAVELLVELASLQTSFVTLDEAIKITNRRVNAI 172
Cdd:pfam01813  80 RVEVKTENIMGVKVPVFELVEDERFEIPLYGLLGTGAWLDEAREAFEELLELLIELAELETALRLLAEEIKKTNRRVNAL 159
                         170       180       190
                  ....*....|....*....|....*....|
gi 12963799   173 EHVIIPRIERTLAYIITELDEREREEFYRL 202
Cdd:pfam01813 160 EKVVIPRLEETIKYIKSELDEREREEFFRL 189
V_ATPase_subD TIGR00309
H(+)-transporting ATP synthase, vacuolar type, subunit D; Although this ATPase can run ...
8-202 3.22e-50

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: 163.46  E-value: 3.22e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963799     8 EIFPSRMAQTIMKARLKGAQTGRNLLKKKSDALTLRFRQILKKIIETKMLMGEVMREAAFSLAEAKFTAGDFSTTVIQ-N 86
Cdd:TIGR00309   3 KVNPTRMELLKLKDKLKMAKRGYSLLKLKRDALIMEFRQILERAKDIKNKMEQKLKEAISDLIEAQSVMGPFAVWIAAlS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963799    87 VNKAQVKIRAKKDNVAGVTLPVFEHYH-EGTDSYELTGLARGGEQLAKLKRNYAKAVELLVELASLQTSFVTLDEAIKIT 165
Cdd:TIGR00309  83 VVTARFEVDMKSKNIMGVVVPVFDSYEiRRKVHERGYGLLFTSYKVDEAAEIYEEAVELIVELAEIETTIRLLAEEIEIT 162
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 12963799   166 NRRVNAIEHVIIPRIERTLAYIITELDEREREEFYRL 202
Cdd:TIGR00309 163 KRRVNALEHVIIPRLKNTIKYINMRLDEMDRENFVRL 199
NtpD COG1394
Archaeal/vacuolar-type H+-ATPase subunit D/Vma8 [Energy production and conversion]; Archaeal ...
7-202 1.51e-32

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: 117.64  E-value: 1.51e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963799   7 IEIFPSRMAQTIMKARLKGAQTGRNLLKKKSDALTLRFRQILKKIIETKMLMGEVMREAAFSLAEAKFTAGDFSTTVIQN 86
Cdd:COG1394   2 AKVKPTKMELLRLKRQLKLAKRGHKLLKDKRDALIREFLKLIDEAEELREELEELLEEAYEALALANARMGIEAVEELAL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963799  87 VNKAQVKIRAKKDNVAGVTLPVFEhYHEGTDSYELtGLARGGEQLAKLKRNYAKAVELLVELASLQTSFVTLDEAIKITN 166
Cdd:COG1394  82 SVPRVLEVEVSTRNIMGVEVPVLE-SEEFKEERPY-GLLGTSAWLDEAIEALEELLELLLELAELETALRRLAEEIRKTQ 159
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 12963799 167 RRVNAIEHVIIPRIERTLAYIITELDEREREEFYRL 202
Cdd:COG1394 160 RRVNALEKVLIPRLEETIKYIRMKLEEREREEFVRL 195
PRK00373 PRK00373
V-type ATP synthase subunit D; Reviewed
5-202 5.83e-29

V-type ATP synthase subunit D; Reviewed


Pssm-ID: 178991  Cd Length: 204  Bit Score: 108.37  E-value: 5.83e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963799    5 DRIEIFPSRMAQTIMKARLKGAQTGRNLLKKKSDALTLRFRQILKKIIETKMLMGEVMREAAFSLAEAKFTAGDFSTTVI 84
Cdd:PRK00373   2 ARLNVKPTRMELINLKRRLKLAERGHKLLKDKRDELIMEFFDILDEAKKLREEVEEELEEAYKDFLMARAVEGSLAVEEA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963799   85 QNVNKAQVKIRAKKDNVAGVTLPVFEHYHEGTDSYELTGLARGGEQLAKLKRNYAKAVELLVELASLQTSFVTLDEAIKI 164
Cdd:PRK00373  82 AASPKESLEVDVSSKNIMGVVVPVIELSVKRTLPERGYGFLGTSAELDEAAEKFEELLEKILELAEVEKTIQLLADEIEK 161
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 12963799  165 TNRRVNAIEHVIIPRIERTLAYIITELDEREREEFYRL 202
Cdd:PRK00373 162 TKRRVNALEYVIIPRLEETIKYIKMKLDEMERENFVRL 199
 
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 ...
15-202 8.97e-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: 8.97e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963799    15 AQTIMKARLKGAQTGRNLLKKKSDALTLRFRQILKKIIETKMLMGEVMREAAFSLAEAKFTAG--DFSTTVIQNVNKaQV 92
Cdd:pfam01813   1 ELIRLKKRLKLAQRGHKLLKRKRDALIMEFRKILREIKELREELEEALKEAYFSLALAYALGGeeDVESLALESVPS-VV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963799    93 KIRAKKDNVAGVTLPVFEHYHEGTDSYELTGLARGGEQLAKLKRNYAKAVELLVELASLQTSFVTLDEAIKITNRRVNAI 172
Cdd:pfam01813  80 RVEVKTENIMGVKVPVFELVEDERFEIPLYGLLGTGAWLDEAREAFEELLELLIELAELETALRLLAEEIKKTNRRVNAL 159
                         170       180       190
                  ....*....|....*....|....*....|
gi 12963799   173 EHVIIPRIERTLAYIITELDEREREEFYRL 202
Cdd:pfam01813 160 EKVVIPRLEETIKYIKSELDEREREEFFRL 189
V_ATPase_subD TIGR00309
H(+)-transporting ATP synthase, vacuolar type, subunit D; Although this ATPase can run ...
8-202 3.22e-50

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: 163.46  E-value: 3.22e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963799     8 EIFPSRMAQTIMKARLKGAQTGRNLLKKKSDALTLRFRQILKKIIETKMLMGEVMREAAFSLAEAKFTAGDFSTTVIQ-N 86
Cdd:TIGR00309   3 KVNPTRMELLKLKDKLKMAKRGYSLLKLKRDALIMEFRQILERAKDIKNKMEQKLKEAISDLIEAQSVMGPFAVWIAAlS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963799    87 VNKAQVKIRAKKDNVAGVTLPVFEHYH-EGTDSYELTGLARGGEQLAKLKRNYAKAVELLVELASLQTSFVTLDEAIKIT 165
Cdd:TIGR00309  83 VVTARFEVDMKSKNIMGVVVPVFDSYEiRRKVHERGYGLLFTSYKVDEAAEIYEEAVELIVELAEIETTIRLLAEEIEIT 162
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 12963799   166 NRRVNAIEHVIIPRIERTLAYIITELDEREREEFYRL 202
Cdd:TIGR00309 163 KRRVNALEHVIIPRLKNTIKYINMRLDEMDRENFVRL 199
NtpD COG1394
Archaeal/vacuolar-type H+-ATPase subunit D/Vma8 [Energy production and conversion]; Archaeal ...
7-202 1.51e-32

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: 117.64  E-value: 1.51e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963799   7 IEIFPSRMAQTIMKARLKGAQTGRNLLKKKSDALTLRFRQILKKIIETKMLMGEVMREAAFSLAEAKFTAGDFSTTVIQN 86
Cdd:COG1394   2 AKVKPTKMELLRLKRQLKLAKRGHKLLKDKRDALIREFLKLIDEAEELREELEELLEEAYEALALANARMGIEAVEELAL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963799  87 VNKAQVKIRAKKDNVAGVTLPVFEhYHEGTDSYELtGLARGGEQLAKLKRNYAKAVELLVELASLQTSFVTLDEAIKITN 166
Cdd:COG1394  82 SVPRVLEVEVSTRNIMGVEVPVLE-SEEFKEERPY-GLLGTSAWLDEAIEALEELLELLLELAELETALRRLAEEIRKTQ 159
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 12963799 167 RRVNAIEHVIIPRIERTLAYIITELDEREREEFYRL 202
Cdd:COG1394 160 RRVNALEKVLIPRLEETIKYIRMKLEEREREEFVRL 195
PRK00373 PRK00373
V-type ATP synthase subunit D; Reviewed
5-202 5.83e-29

V-type ATP synthase subunit D; Reviewed


Pssm-ID: 178991  Cd Length: 204  Bit Score: 108.37  E-value: 5.83e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963799    5 DRIEIFPSRMAQTIMKARLKGAQTGRNLLKKKSDALTLRFRQILKKIIETKMLMGEVMREAAFSLAEAKFTAGDFSTTVI 84
Cdd:PRK00373   2 ARLNVKPTRMELINLKRRLKLAERGHKLLKDKRDELIMEFFDILDEAKKLREEVEEELEEAYKDFLMARAVEGSLAVEEA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963799   85 QNVNKAQVKIRAKKDNVAGVTLPVFEHYHEGTDSYELTGLARGGEQLAKLKRNYAKAVELLVELASLQTSFVTLDEAIKI 164
Cdd:PRK00373  82 AASPKESLEVDVSSKNIMGVVVPVIELSVKRTLPERGYGFLGTSAELDEAAEKFEELLEKILELAEVEKTIQLLADEIEK 161
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 12963799  165 TNRRVNAIEHVIIPRIERTLAYIITELDEREREEFYRL 202
Cdd:PRK00373 162 TKRRVNALEYVIIPRLEETIKYIKMKLDEMERENFVRL 199
 
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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