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Conserved domains on  [gi|1333615743|ref|XP_023484509|]
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V-type proton ATPase subunit G 1 [Equus caballus]

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

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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 3.60e-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: 131.88  E-value: 3.60e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333615743   1 MASQSQGIQQLLQAEKRAAEKVSEARKRKNRRLKQAKEEAQAEIEQYRLQREKEFKAKEAAALGSHGSCSSEVEKETQQK 80
Cdd:TIGR01147   1 MASQTQGIQQLLQAEKRAAEKVSEARKRKTKRLKQAKEEAQKEVEKYKQQREKEFKEFEAKHLGGNGAAEEKAEAETQAK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1333615743  81 MSILQTYFRQNRDEVLDDLLAFVCDIRPEIHEN 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 3.60e-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: 131.88  E-value: 3.60e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333615743   1 MASQSQGIQQLLQAEKRAAEKVSEARKRKNRRLKQAKEEAQAEIEQYRLQREKEFKAKEAAALGSHGSCSSEVEKETQQK 80
Cdd:TIGR01147   1 MASQTQGIQQLLQAEKRAAEKVSEARKRKTKRLKQAKEEAQKEVEKYKQQREKEFKEFEAKHLGGNGAAEEKAEAETQAK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1333615743  81 MSILQTYFRQNRDEVLDDLLAFVCDIRPEIHEN 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 3.47e-36

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: 119.24  E-value: 3.47e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333615743   3 SQSQGIQQLLQAEKRAAEKVSEARKRKNRRLKQAKEEAQAEIEQYRLQREKEFKAKEAAALGSHGSCSSEVEKETQQKMS 82
Cdd:pfam03179   1 SQSQGIQQLLQAEKEAAEIVNEARKRKQKRLKQAKEEAEKEIEEYRAQREKEFKEFEAKHMGSREELEKKIEKETQEKIQ 80

                          90       100
                  ....*....|....*....|....*
gi 1333615743  83 ILQTYFRQNRDEVLDDLLAFVCDIR 107
Cdd:pfam03179  81 EIKDSVNKNKEAVVKMLLSAVTTVK 105
PRK12704 PRK12704
phosphodiesterase; Provisional
 9-59 1.12e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 1.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1333615743   9 QQLLQAEKRAAEKVSEARKRKNRRLKQAKEEAQAEIEQYRLQREKEFKAKE 59
Cdd:PRK12704   31 AKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERR 81
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 9-63 9.33e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 33.57  E-value: 9.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1333615743   9 QQLLQAEKRAAEKVSEARKRKNRRLKQAKEEAQAEIEQYRLQREKEFKAKEAAAL 63
Cdd:cd06503    58 EKLAEARAEAQEIIEEARKEAEKIKEEILAEAKEEAERILEQAKAEIEQEKEKAL 112
 
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 3.60e-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: 131.88  E-value: 3.60e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333615743   1 MASQSQGIQQLLQAEKRAAEKVSEARKRKNRRLKQAKEEAQAEIEQYRLQREKEFKAKEAAALGSHGSCSSEVEKETQQK 80
Cdd:TIGR01147   1 MASQTQGIQQLLQAEKRAAEKVSEARKRKTKRLKQAKEEAQKEVEKYKQQREKEFKEFEAKHLGGNGAAEEKAEAETQAK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1333615743  81 MSILQTYFRQNRDEVLDDLLAFVCDIRPEIHEN 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 3.47e-36

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: 119.24  E-value: 3.47e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333615743   3 SQSQGIQQLLQAEKRAAEKVSEARKRKNRRLKQAKEEAQAEIEQYRLQREKEFKAKEAAALGSHGSCSSEVEKETQQKMS 82
Cdd:pfam03179   1 SQSQGIQQLLQAEKEAAEIVNEARKRKQKRLKQAKEEAEKEIEEYRAQREKEFKEFEAKHMGSREELEKKIEKETQEKIQ 80

                          90       100
                  ....*....|....*....|....*
gi 1333615743  83 ILQTYFRQNRDEVLDDLLAFVCDIR 107
Cdd:pfam03179  81 EIKDSVNKNKEAVVKMLLSAVTTVK 105
PRK12704 PRK12704
phosphodiesterase; Provisional
 9-59 1.12e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 1.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1333615743   9 QQLLQAEKRAAEKVSEARKRKNRRLKQAKEEAQAEIEQYRLQREKEFKAKE 59
Cdd:PRK12704   31 AKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERR 81
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 9-63 9.33e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 33.57  E-value: 9.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1333615743   9 QQLLQAEKRAAEKVSEARKRKNRRLKQAKEEAQAEIEQYRLQREKEFKAKEAAAL 63
Cdd:cd06503    58 EKLAEARAEAQEIIEEARKEAEKIKEEILAEAKEEAERILEQAKAEIEQEKEKAL 112
 
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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