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Conserved domains on  [gi|1104469668|ref|NP_001334280|]
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V-type proton ATPase subunit G 2 isoform 2 [Mus musculus]

Protein Classification

V-type proton ATPase subunit G( domain architecture ID 627)

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

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List of domain hits

 Name Accession Description Interval E-value
V-ATPase_G super family cl47797
Vacuolar (H+)-ATPase G subunit; This family represents the eukaryotic vacuolar (H+)-ATPase ...
 1-66 1.46e-14

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.


The actual alignment was detected with superfamily member pfam03179:

Pssm-ID: 460836 [Multi-domain]  Cd Length: 105  Bit Score: 62.62  E-value: 1.46e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1104469668   1 MEVEQYRREREQEFQSKQQAAMGSQGNLSAEVEQATRRQVQGMQSSQQRNRERVLAQLLGMVCEVR 66
Cdd:pfam03179  40 KEIEEYRAQREKEFKEFEAKHMGSREELEKKIEKETQEKIQEIKDSVNKNKEAVVKMLLSAVTTVK 105
 
Name Accession Description Interval E-value
V-ATPase_G pfam03179
Vacuolar (H+)-ATPase G subunit; This family represents the eukaryotic vacuolar (H+)-ATPase ...
 1-66 1.46e-14

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: 62.62  E-value: 1.46e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1104469668   1 MEVEQYRREREQEFQSKQQAAMGSQGNLSAEVEQATRRQVQGMQSSQQRNRERVLAQLLGMVCEVR 66
Cdd:pfam03179  40 KEIEEYRAQREKEFKEFEAKHMGSREELEKKIEKETQEKIQEIKDSVNKNKEAVVKMLLSAVTTVK 105
V_ATP_synt_G TIGR01147
vacuolar ATP synthase, subunit G; This model describes the vacuolar ATP synthase G subunit in ...
 2-72 7.68e-12

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: 55.99  E-value: 7.68e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1104469668   2 EVEQYRREREQEFQSKQQAAMGSQGNLSAEVEQATRRQVQGMQSSQQRNRERVLAQLLGMVCEVRPQVHPN 72
Cdd:TIGR01147  43 EVEKYKQQREKEFKEFEAKHLGGNGAAEEKAEAETQAKIREIKKAVQKNKDAVIKDLLHLVCDISPELHIN 113
 
Name Accession Description Interval E-value
V-ATPase_G pfam03179
Vacuolar (H+)-ATPase G subunit; This family represents the eukaryotic vacuolar (H+)-ATPase ...
 1-66 1.46e-14

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: 62.62  E-value: 1.46e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1104469668   1 MEVEQYRREREQEFQSKQQAAMGSQGNLSAEVEQATRRQVQGMQSSQQRNRERVLAQLLGMVCEVR 66
Cdd:pfam03179  40 KEIEEYRAQREKEFKEFEAKHMGSREELEKKIEKETQEKIQEIKDSVNKNKEAVVKMLLSAVTTVK 105
V_ATP_synt_G TIGR01147
vacuolar ATP synthase, subunit G; This model describes the vacuolar ATP synthase G subunit in ...
 2-72 7.68e-12

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: 55.99  E-value: 7.68e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1104469668   2 EVEQYRREREQEFQSKQQAAMGSQGNLSAEVEQATRRQVQGMQSSQQRNRERVLAQLLGMVCEVRPQVHPN 72
Cdd:TIGR01147  43 EVEKYKQQREKEFKEFEAKHLGGNGAAEEKAEAETQAKIREIKKAVQKNKDAVIKDLLHLVCDISPELHIN 113
 
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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