NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15617197|ref|NP_077135|]
View 

V-type proton ATPase subunit G 1 [Mus musculus]

Protein Classification

V-type proton ATPase subunit G( domain architecture ID 10017661)

V-type proton ATPase subunit G is the catalytic subunit of the peripheral V1 complex of vacuolar ATPase that is responsible for acidifying a variety of intracellular compartments in eukaryotic cells

CATH:  1.20.5.620
Gene Ontology:  GO:0005524|GO:0046961|GO:0016471|GO:1902600
PubMed:  9872382
TCDB:  3.A.2

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
V_ATP_synt_G TIGR01147
vacuolar ATP synthase, subunit G; This model describes the vacuolar ATP synthase G subunit in ...
 1-113 5.96e-41

vacuolar ATP synthase, subunit G; This model describes the vacuolar ATP synthase G subunit in eukaryotes and includes members from diverse groups e.g., fungi, plants, parasites etc. V-ATPases are multi-subunit enzymes composed of two functional domains: A transmembrane Vo domain and a peripheral catalytic domain V1. The G subunit is one of the subunits of the catalytic domain. V-ATPases are responsible for the acidification of endosomes and lysosomes, which are part of the central vacuolar system. [Energy metabolism, ATP-proton motive force interconversion]


:

Pssm-ID: 130217 [Multi-domain]  Cd Length: 113  Bit Score: 131.49  E-value: 5.96e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15617197     1 MASQSQGIQQLLQAEKRAAEKVSEARKRKNRRLKQAKEEAQAEIEQYRLQREKEFKAKEAAALGSHGSCSSEVEKETREK 80
Cdd:TIGR01147   1 MASQTQGIQQLLQAEKRAAEKVSEARKRKTKRLKQAKEEAQKEVEKYKQQREKEFKEFEAKHLGGNGAAEEKAEAETQAK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 15617197    81 MTVLQNYFEQNRDEVLDNLLAFVCDIRPEIHEN 113
Cdd:TIGR01147  81 IREIKKAVQKNKDAVIKDLLHLVCDISPELHIN 113
 
Name Accession Description Interval E-value
V_ATP_synt_G TIGR01147
vacuolar ATP synthase, subunit G; This model describes the vacuolar ATP synthase G subunit in ...
 1-113 5.96e-41

vacuolar ATP synthase, subunit G; This model describes the vacuolar ATP synthase G subunit in eukaryotes and includes members from diverse groups e.g., fungi, plants, parasites etc. V-ATPases are multi-subunit enzymes composed of two functional domains: A transmembrane Vo domain and a peripheral catalytic domain V1. The G subunit is one of the subunits of the catalytic domain. V-ATPases are responsible for the acidification of endosomes and lysosomes, which are part of the central vacuolar system. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 130217 [Multi-domain]  Cd Length: 113  Bit Score: 131.49  E-value: 5.96e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15617197     1 MASQSQGIQQLLQAEKRAAEKVSEARKRKNRRLKQAKEEAQAEIEQYRLQREKEFKAKEAAALGSHGSCSSEVEKETREK 80
Cdd:TIGR01147   1 MASQTQGIQQLLQAEKRAAEKVSEARKRKTKRLKQAKEEAQKEVEKYKQQREKEFKEFEAKHLGGNGAAEEKAEAETQAK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 15617197    81 MTVLQNYFEQNRDEVLDNLLAFVCDIRPEIHEN 113
Cdd:TIGR01147  81 IREIKKAVQKNKDAVIKDLLHLVCDISPELHIN 113
V-ATPase_G pfam03179
Vacuolar (H+)-ATPase G subunit; This family represents the eukaryotic vacuolar (H+)-ATPase ...
 3-107 1.16e-35

Vacuolar (H+)-ATPase G subunit; This family represents the eukaryotic vacuolar (H+)-ATPase (V-ATPase) G subunit. V-ATPases generate an acidic environment in several intracellular compartments. Correspondingly, they are found as membrane-attached proteins in several organelles. They are also found in the plasma membranes of some specialized cells. V-ATPases consist of peripheral (V1) and membrane integral (V0) heteromultimeric complexes. The G subunit is part of the V1 subunit, but is also thought to be strongly attached to the V0 complex. It may be involved in the coupling of ATP degradation to H+ translocation.


Pssm-ID: 460836 [Multi-domain]  Cd Length: 105  Bit Score: 117.70  E-value: 1.16e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15617197     3 SQSQGIQQLLQAEKRAAEKVSEARKRKNRRLKQAKEEAQAEIEQYRLQREKEFKAKEAAALGSHGSCSSEVEKETREKMT 82
Cdd:pfam03179   1 SQSQGIQQLLQAEKEAAEIVNEARKRKQKRLKQAKEEAEKEIEEYRAQREKEFKEFEAKHMGSREELEKKIEKETQEKIQ 80

                          90       100
                  ....*....|....*....|....*
gi 15617197    83 VLQNYFEQNRDEVLDNLLAFVCDIR 107
Cdd:pfam03179  81 EIKDSVNKNKEAVVKMLLSAVTTVK 105
PRK12704 PRK12704
phosphodiesterase; Provisional
 9-59 1.56e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.38  E-value: 1.56e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15617197    9 QQLLQAEKRAAEKVSEARKRKNRRLKQAKEEAQAEIEQYRLQREKEFKAKE 59
Cdd:PRK12704  31 AKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERR 81
 
Name Accession Description Interval E-value
V_ATP_synt_G TIGR01147
vacuolar ATP synthase, subunit G; This model describes the vacuolar ATP synthase G subunit in ...
 1-113 5.96e-41

vacuolar ATP synthase, subunit G; This model describes the vacuolar ATP synthase G subunit in eukaryotes and includes members from diverse groups e.g., fungi, plants, parasites etc. V-ATPases are multi-subunit enzymes composed of two functional domains: A transmembrane Vo domain and a peripheral catalytic domain V1. The G subunit is one of the subunits of the catalytic domain. V-ATPases are responsible for the acidification of endosomes and lysosomes, which are part of the central vacuolar system. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 130217 [Multi-domain]  Cd Length: 113  Bit Score: 131.49  E-value: 5.96e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15617197     1 MASQSQGIQQLLQAEKRAAEKVSEARKRKNRRLKQAKEEAQAEIEQYRLQREKEFKAKEAAALGSHGSCSSEVEKETREK 80
Cdd:TIGR01147   1 MASQTQGIQQLLQAEKRAAEKVSEARKRKTKRLKQAKEEAQKEVEKYKQQREKEFKEFEAKHLGGNGAAEEKAEAETQAK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 15617197    81 MTVLQNYFEQNRDEVLDNLLAFVCDIRPEIHEN 113
Cdd:TIGR01147  81 IREIKKAVQKNKDAVIKDLLHLVCDISPELHIN 113
V-ATPase_G pfam03179
Vacuolar (H+)-ATPase G subunit; This family represents the eukaryotic vacuolar (H+)-ATPase ...
 3-107 1.16e-35

Vacuolar (H+)-ATPase G subunit; This family represents the eukaryotic vacuolar (H+)-ATPase (V-ATPase) G subunit. V-ATPases generate an acidic environment in several intracellular compartments. Correspondingly, they are found as membrane-attached proteins in several organelles. They are also found in the plasma membranes of some specialized cells. V-ATPases consist of peripheral (V1) and membrane integral (V0) heteromultimeric complexes. The G subunit is part of the V1 subunit, but is also thought to be strongly attached to the V0 complex. It may be involved in the coupling of ATP degradation to H+ translocation.


Pssm-ID: 460836 [Multi-domain]  Cd Length: 105  Bit Score: 117.70  E-value: 1.16e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15617197     3 SQSQGIQQLLQAEKRAAEKVSEARKRKNRRLKQAKEEAQAEIEQYRLQREKEFKAKEAAALGSHGSCSSEVEKETREKMT 82
Cdd:pfam03179   1 SQSQGIQQLLQAEKEAAEIVNEARKRKQKRLKQAKEEAEKEIEEYRAQREKEFKEFEAKHMGSREELEKKIEKETQEKIQ 80

                          90       100
                  ....*....|....*....|....*
gi 15617197    83 VLQNYFEQNRDEVLDNLLAFVCDIR 107
Cdd:pfam03179  81 EIKDSVNKNKEAVVKMLLSAVTTVK 105
PRK12704 PRK12704
phosphodiesterase; Provisional
 9-59 1.56e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.38  E-value: 1.56e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15617197    9 QQLLQAEKRAAEKVSEARKRKNRRLKQAKEEAQAEIEQYRLQREKEFKAKE 59
Cdd:PRK12704  31 AKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERR 81
 
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