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Conserved domains on  [gi|12963559|ref|NP_075668|]
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V-type proton ATPase subunit G 2 isoform 1 [Mus musculus]

Protein Classification

V-type proton ATPase subunit G( domain architecture ID 10504972)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
V-ATPase_G pfam03179
Vacuolar (H+)-ATPase G subunit; This family represents the eukaryotic vacuolar (H+)-ATPase ...
 3-107 8.91e-31

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: 105.38  E-value: 8.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963559     3 SQTQGIQQLLQAEKRAAEKVADARKRKARRLKQAKEEAQMEVEQYRREREQEFQSKQQAAMGSQGNLSAEVEQATRRQVQ 82
Cdd:pfam03179   1 SQSQGIQQLLQAEKEAAEIVNEARKRKQKRLKQAKEEAEKEIEEYRAQREKEFKEFEAKHMGSREELEKKIEKETQEKIQ 80

                          90       100
                  ....*....|....*....|....*
gi 12963559    83 GMQSSQQRNRERVLAQLLGMVCEVR 107
Cdd:pfam03179  81 EIKDSVNKNKEAVVKMLLSAVTTVK 105
 
Name Accession Description Interval E-value
V-ATPase_G pfam03179
Vacuolar (H+)-ATPase G subunit; This family represents the eukaryotic vacuolar (H+)-ATPase ...
 3-107 8.91e-31

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: 105.38  E-value: 8.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963559     3 SQTQGIQQLLQAEKRAAEKVADARKRKARRLKQAKEEAQMEVEQYRREREQEFQSKQQAAMGSQGNLSAEVEQATRRQVQ 82
Cdd:pfam03179   1 SQSQGIQQLLQAEKEAAEIVNEARKRKQKRLKQAKEEAEKEIEEYRAQREKEFKEFEAKHMGSREELEKKIEKETQEKIQ 80

                          90       100
                  ....*....|....*....|....*
gi 12963559    83 GMQSSQQRNRERVLAQLLGMVCEVR 107
Cdd:pfam03179  81 EIKDSVNKNKEAVVKMLLSAVTTVK 105
V_ATP_synt_G TIGR01147
vacuolar ATP synthase, subunit G; This model describes the vacuolar ATP synthase G subunit in ...
 1-113 2.27e-26

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: 94.51  E-value: 2.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963559     1 MASQTQGIQQLLQAEKRAAEKVADARKRKARRLKQAKEEAQMEVEQYRREREQEFQSKQQAAMGSQGNLSAEVEQATRRQ 80
Cdd:TIGR01147   1 MASQTQGIQQLLQAEKRAAEKVSEARKRKTKRLKQAKEEAQKEVEKYKQQREKEFKEFEAKHLGGNGAAEEKAEAETQAK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 12963559    81 VQGMQSSQQRNRERVLAQLLGMVCEVRPQVHPN 113
Cdd:TIGR01147  81 IREIKKAVQKNKDAVIKDLLHLVCDISPELHIN 113
PRK12704 PRK12704
phosphodiesterase; Provisional
 9-80 5.13e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 37.84  E-value: 5.13e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12963559    9 QQLLQAEKRAAEKVADARKR----KARRLKQAKEEAQ---MEVEQYRREREQEFQSKQQAAMGSQGNLSAEVEQATRRQ 80
Cdd:PRK12704  31 AKIKEAEEEAKRILEEAKKEaeaiKKEALLEAKEEIHklrNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 2-87 1.24e-03

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 37.12  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963559     2 ASQTQGIQQLLQAEKRAAEKVADARKRKA------RRLKQAKEEAQMEVEQYRREREQE-FQSKQQAAMGSQGNLSAEVE 74
Cdd:NF012221 1696 AGVAQGEQNQANAEQDIDDAKADAEKRKDdalakqNEAQQAESDANAAANDAQSRGEQDaSAAENKANQAQADAKGAKQD 1775

                          90
                  ....*....|...
gi 12963559    75 QATRRQVQGMQSS 87
Cdd:NF012221 1776 ESDKPNRQGAAGS 1788
 
Name Accession Description Interval E-value
V-ATPase_G pfam03179
Vacuolar (H+)-ATPase G subunit; This family represents the eukaryotic vacuolar (H+)-ATPase ...
 3-107 8.91e-31

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: 105.38  E-value: 8.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963559     3 SQTQGIQQLLQAEKRAAEKVADARKRKARRLKQAKEEAQMEVEQYRREREQEFQSKQQAAMGSQGNLSAEVEQATRRQVQ 82
Cdd:pfam03179   1 SQSQGIQQLLQAEKEAAEIVNEARKRKQKRLKQAKEEAEKEIEEYRAQREKEFKEFEAKHMGSREELEKKIEKETQEKIQ 80

                          90       100
                  ....*....|....*....|....*
gi 12963559    83 GMQSSQQRNRERVLAQLLGMVCEVR 107
Cdd:pfam03179  81 EIKDSVNKNKEAVVKMLLSAVTTVK 105
V_ATP_synt_G TIGR01147
vacuolar ATP synthase, subunit G; This model describes the vacuolar ATP synthase G subunit in ...
 1-113 2.27e-26

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: 94.51  E-value: 2.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963559     1 MASQTQGIQQLLQAEKRAAEKVADARKRKARRLKQAKEEAQMEVEQYRREREQEFQSKQQAAMGSQGNLSAEVEQATRRQ 80
Cdd:TIGR01147   1 MASQTQGIQQLLQAEKRAAEKVSEARKRKTKRLKQAKEEAQKEVEKYKQQREKEFKEFEAKHLGGNGAAEEKAEAETQAK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 12963559    81 VQGMQSSQQRNRERVLAQLLGMVCEVRPQVHPN 113
Cdd:TIGR01147  81 IREIKKAVQKNKDAVIKDLLHLVCDISPELHIN 113
PRK12704 PRK12704
phosphodiesterase; Provisional
 9-80 5.13e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 37.84  E-value: 5.13e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12963559    9 QQLLQAEKRAAEKVADARKR----KARRLKQAKEEAQ---MEVEQYRREREQEFQSKQQAAMGSQGNLSAEVEQATRRQ 80
Cdd:PRK12704  31 AKIKEAEEEAKRILEEAKKEaeaiKKEALLEAKEEIHklrNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 2-87 1.24e-03

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 37.12  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963559     2 ASQTQGIQQLLQAEKRAAEKVADARKRKA------RRLKQAKEEAQMEVEQYRREREQE-FQSKQQAAMGSQGNLSAEVE 74
Cdd:NF012221 1696 AGVAQGEQNQANAEQDIDDAKADAEKRKDdalakqNEAQQAESDANAAANDAQSRGEQDaSAAENKANQAQADAKGAKQD 1775

                          90
                  ....*....|...
gi 12963559    75 QATRRQVQGMQSS 87
Cdd:NF012221 1776 ESDKPNRQGAAGS 1788
 
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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