NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1907089376|ref|XP_036013525|]
View 

V-type proton ATPase subunit D isoform X2 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
1-184 3.69e-66

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: 202.84  E-value: 3.69e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089376   1 MKARLKGAQTGRNLLKKKSDALTLRFRQILKKIIETKMLMGEVMREAAFSLAEAKFTAG--DFSTTVIQNVNKaQVKIRA 78
Cdd:pfam01813   5 LKKRLKLAQRGHKLLKRKRDALIMEFRKILREIKELREELEEALKEAYFSLALAYALGGeeDVESLALESVPS-VVRVEV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089376  79 KKDNVAGVTLPVFEHYHEGTDSYELTGLARGGEQLAKLKRNYAKAVELLVELASLQTSFVTLDEAIKITNRRVNAIEHVI 158
Cdd:pfam01813  84 KTENIMGVKVPVFELVEDERFEIPLYGLLGTGAWLDEAREAFEELLELLIELAELETALRLLAEEIKKTNRRVNALEKVV 163
                         170       180
                  ....*....|....*....|....*.
gi 1907089376 159 IPRIERTLAYIITELDEREREEFYRL 184
Cdd:pfam01813 164 IPRLEETIKYIKSELDEREREEFFRL 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 ...
1-184 3.69e-66

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: 202.84  E-value: 3.69e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089376   1 MKARLKGAQTGRNLLKKKSDALTLRFRQILKKIIETKMLMGEVMREAAFSLAEAKFTAG--DFSTTVIQNVNKaQVKIRA 78
Cdd:pfam01813   5 LKKRLKLAQRGHKLLKRKRDALIMEFRKILREIKELREELEEALKEAYFSLALAYALGGeeDVESLALESVPS-VVRVEV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089376  79 KKDNVAGVTLPVFEHYHEGTDSYELTGLARGGEQLAKLKRNYAKAVELLVELASLQTSFVTLDEAIKITNRRVNAIEHVI 158
Cdd:pfam01813  84 KTENIMGVKVPVFELVEDERFEIPLYGLLGTGAWLDEAREAFEELLELLIELAELETALRLLAEEIKKTNRRVNALEKVV 163
                         170       180
                  ....*....|....*....|....*.
gi 1907089376 159 IPRIERTLAYIITELDEREREEFYRL 184
Cdd:pfam01813 164 IPRLEETIKYIKSELDEREREEFFRL 189
V_ATPase_subD TIGR00309
H(+)-transporting ATP synthase, vacuolar type, subunit D; Although this ATPase can run ...
1-184 2.40e-47

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: 155.37  E-value: 2.40e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089376   1 MKARLKGAQTGRNLLKKKSDALTLRFRQILKKIIETKMLMGEVMREAAFSLAEAKFTAGDFSTTVIQ-NVNKAQVKIRAK 79
Cdd:TIGR00309  14 LKDKLKMAKRGYSLLKLKRDALIMEFRQILERAKDIKNKMEQKLKEAISDLIEAQSVMGPFAVWIAAlSVVTARFEVDMK 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089376  80 KDNVAGVTLPVFEHYH-EGTDSYELTGLARGGEQLAKLKRNYAKAVELLVELASLQTSFVTLDEAIKITNRRVNAIEHVI 158
Cdd:TIGR00309  94 SKNIMGVVVPVFDSYEiRRKVHERGYGLLFTSYKVDEAAEIYEEAVELIVELAEIETTIRLLAEEIEITKRRVNALEHVI 173
                         170       180
                  ....*....|....*....|....*.
gi 1907089376 159 IPRIERTLAYIITELDEREREEFYRL 184
Cdd:TIGR00309 174 IPRLKNTIKYINMRLDEMDRENFVRL 199
NtpD COG1394
Archaeal/vacuolar-type H+-ATPase subunit D/Vma8 [Energy production and conversion]; Archaeal ...
2-184 1.41e-30

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: 111.86  E-value: 1.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089376   2 KARLKGAQTGRNLLKKKSDALTLRFRQILKKIIETKMLMGEVMREAAFSLAEAKFTAGDFSTTVIQNVNKAQVKIRAKKD 81
Cdd:COG1394    15 KRQLKLAKRGHKLLKDKRDALIREFLKLIDEAEELREELEELLEEAYEALALANARMGIEAVEELALSVPRVLEVEVSTR 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089376  82 NVAGVTLPVFEhYHEGTDSYELtGLARGGEQLAKLKRNYAKAVELLVELASLQTSFVTLDEAIKITNRRVNAIEHVIIPR 161
Cdd:COG1394    95 NIMGVEVPVLE-SEEFKEERPY-GLLGTSAWLDEAIEALEELLELLLELAELETALRRLAEEIRKTQRRVNALEKVLIPR 172
                         170       180
                  ....*....|....*....|...
gi 1907089376 162 IERTLAYIITELDEREREEFYRL 184
Cdd:COG1394   173 LEETIKYIRMKLEEREREEFVRL 195
PRK00373 PRK00373
V-type ATP synthase subunit D; Reviewed
1-184 2.64e-27

V-type ATP synthase subunit D; Reviewed


Pssm-ID: 178991  Cd Length: 204  Bit Score: 103.36  E-value: 2.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089376   1 MKARLKGAQTGRNLLKKKSDALTLRFRQILKKIIETKMLMGEVMREAAFSLAEAKFTAGDFSTTVIQNVNKAQVKIRAKK 80
Cdd:PRK00373   16 LKRRLKLAERGHKLLKDKRDELIMEFFDILDEAKKLREEVEEELEEAYKDFLMARAVEGSLAVEEAAASPKESLEVDVSS 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089376  81 DNVAGVTLPVFEHYHEGTDSYELTGLARGGEQLAKLKRNYAKAVELLVELASLQTSFVTLDEAIKITNRRVNAIEHVIIP 160
Cdd:PRK00373   96 KNIMGVVVPVIELSVKRTLPERGYGFLGTSAELDEAAEKFEELLEKILELAEVEKTIQLLADEIEKTKRRVNALEYVIIP 175
                         170       180
                  ....*....|....*....|....
gi 1907089376 161 RIERTLAYIITELDEREREEFYRL 184
Cdd:PRK00373  176 RLEETIKYIKMKLDEMERENFVRL 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 ...
1-184 3.69e-66

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: 202.84  E-value: 3.69e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089376   1 MKARLKGAQTGRNLLKKKSDALTLRFRQILKKIIETKMLMGEVMREAAFSLAEAKFTAG--DFSTTVIQNVNKaQVKIRA 78
Cdd:pfam01813   5 LKKRLKLAQRGHKLLKRKRDALIMEFRKILREIKELREELEEALKEAYFSLALAYALGGeeDVESLALESVPS-VVRVEV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089376  79 KKDNVAGVTLPVFEHYHEGTDSYELTGLARGGEQLAKLKRNYAKAVELLVELASLQTSFVTLDEAIKITNRRVNAIEHVI 158
Cdd:pfam01813  84 KTENIMGVKVPVFELVEDERFEIPLYGLLGTGAWLDEAREAFEELLELLIELAELETALRLLAEEIKKTNRRVNALEKVV 163
                         170       180
                  ....*....|....*....|....*.
gi 1907089376 159 IPRIERTLAYIITELDEREREEFYRL 184
Cdd:pfam01813 164 IPRLEETIKYIKSELDEREREEFFRL 189
V_ATPase_subD TIGR00309
H(+)-transporting ATP synthase, vacuolar type, subunit D; Although this ATPase can run ...
1-184 2.40e-47

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: 155.37  E-value: 2.40e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089376   1 MKARLKGAQTGRNLLKKKSDALTLRFRQILKKIIETKMLMGEVMREAAFSLAEAKFTAGDFSTTVIQ-NVNKAQVKIRAK 79
Cdd:TIGR00309  14 LKDKLKMAKRGYSLLKLKRDALIMEFRQILERAKDIKNKMEQKLKEAISDLIEAQSVMGPFAVWIAAlSVVTARFEVDMK 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089376  80 KDNVAGVTLPVFEHYH-EGTDSYELTGLARGGEQLAKLKRNYAKAVELLVELASLQTSFVTLDEAIKITNRRVNAIEHVI 158
Cdd:TIGR00309  94 SKNIMGVVVPVFDSYEiRRKVHERGYGLLFTSYKVDEAAEIYEEAVELIVELAEIETTIRLLAEEIEITKRRVNALEHVI 173
                         170       180
                  ....*....|....*....|....*.
gi 1907089376 159 IPRIERTLAYIITELDEREREEFYRL 184
Cdd:TIGR00309 174 IPRLKNTIKYINMRLDEMDRENFVRL 199
NtpD COG1394
Archaeal/vacuolar-type H+-ATPase subunit D/Vma8 [Energy production and conversion]; Archaeal ...
2-184 1.41e-30

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: 111.86  E-value: 1.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089376   2 KARLKGAQTGRNLLKKKSDALTLRFRQILKKIIETKMLMGEVMREAAFSLAEAKFTAGDFSTTVIQNVNKAQVKIRAKKD 81
Cdd:COG1394    15 KRQLKLAKRGHKLLKDKRDALIREFLKLIDEAEELREELEELLEEAYEALALANARMGIEAVEELALSVPRVLEVEVSTR 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089376  82 NVAGVTLPVFEhYHEGTDSYELtGLARGGEQLAKLKRNYAKAVELLVELASLQTSFVTLDEAIKITNRRVNAIEHVIIPR 161
Cdd:COG1394    95 NIMGVEVPVLE-SEEFKEERPY-GLLGTSAWLDEAIEALEELLELLLELAELETALRRLAEEIRKTQRRVNALEKVLIPR 172
                         170       180
                  ....*....|....*....|...
gi 1907089376 162 IERTLAYIITELDEREREEFYRL 184
Cdd:COG1394   173 LEETIKYIRMKLEEREREEFVRL 195
PRK00373 PRK00373
V-type ATP synthase subunit D; Reviewed
1-184 2.64e-27

V-type ATP synthase subunit D; Reviewed


Pssm-ID: 178991  Cd Length: 204  Bit Score: 103.36  E-value: 2.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089376   1 MKARLKGAQTGRNLLKKKSDALTLRFRQILKKIIETKMLMGEVMREAAFSLAEAKFTAGDFSTTVIQNVNKAQVKIRAKK 80
Cdd:PRK00373   16 LKRRLKLAERGHKLLKDKRDELIMEFFDILDEAKKLREEVEEELEEAYKDFLMARAVEGSLAVEEAAASPKESLEVDVSS 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089376  81 DNVAGVTLPVFEHYHEGTDSYELTGLARGGEQLAKLKRNYAKAVELLVELASLQTSFVTLDEAIKITNRRVNAIEHVIIP 160
Cdd:PRK00373   96 KNIMGVVVPVIELSVKRTLPERGYGFLGTSAELDEAAEKFEELLEKILELAEVEKTIQLLADEIEKTKRRVNALEYVIIP 175
                         170       180
                  ....*....|....*....|....
gi 1907089376 161 RIERTLAYIITELDEREREEFYRL 184
Cdd:PRK00373  176 RLEETIKYIKMKLDEMERENFVRL 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH