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N-terminal domain of alpha and beta subunits of F1 ATP synthase superfamily

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   All beta proteins [ 48724] (174)
Fold:   Domain of alpha and beta subunits of F1 ATP synthase-like [ 50614] (3)
Superfamily:   N-terminal domain of alpha and beta subunits of F1 ATP synthase [ 50615]
Families:   N-terminal domain of alpha and beta subunits of F1 ATP synthase [ 50616] (2)


Superfamily statistics
Genomes (3,122) Uniprot 2018_03 genome PDB chains (SCOP 1.75)
Domains 7,684 72,137 12
Proteins 7,679 72,119 12


Functional annotation
General category Processes_IC
Detailed category Transport

Document:
Function annotation of SCOP domain superfamilies

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEO levelAnnotation (direct or inherited)
Enzyme Commission (EC)Acting on acid anhydrides0Least InformativeDirect
Enzyme Commission (EC)Acting on acid anhydrides; catalyzing transmembran0InformativeDirect
Enzyme Commission (EC)H(+)-transporting two-sector ATPase0Highly InformativeDirect

Document: EC annotation of SCOP domains

Worm Phenotype (WP)

(show details)
WP termFDR (all)SDWP levelAnnotation (direct or inherited)
Worm Phenotype (WP)cell physiology variant0Least InformativeDirect
Worm Phenotype (WP)organism metabolism processing variant0Least InformativeDirect
Worm Phenotype (WP)retarded heterochronic variations0Least InformativeDirect
Worm Phenotype (WP)larval growth variant0Least InformativeDirect
Worm Phenotype (WP)larval development variant0Least InformativeDirect
Worm Phenotype (WP)organ system morphology variant0Least InformativeDirect
Worm Phenotype (WP)organism environmental stimulus response variant0Least InformativeDirect
Worm Phenotype (WP)cell morphology variant0Least InformativeDirect
Worm Phenotype (WP)cell development variant0Least InformativeDirect
Worm Phenotype (WP)organism behavior variant0Least InformativeDirect
Worm Phenotype (WP)general pace of development variant0Least InformativeDirect
Worm Phenotype (WP)germ cell morphology variant0Moderately InformativeDirect
Worm Phenotype (WP)germ cell differentiation variant0Moderately InformativeDirect
Worm Phenotype (WP)pattern of transgene expression variant0Moderately InformativeDirect
Worm Phenotype (WP)protein interaction variant0Moderately InformativeDirect
Worm Phenotype (WP)apoptosis variant0Moderately InformativeDirect
Worm Phenotype (WP)cell organization biogenesis variant0Moderately InformativeDirect
Worm Phenotype (WP)cell division variant0Moderately InformativeDirect
Worm Phenotype (WP)germ cell development variant0Moderately InformativeDirect
Worm Phenotype (WP)cell cycle variant0Moderately InformativeDirect
Worm Phenotype (WP)reproductive system development variant0Moderately InformativeDirect
Worm Phenotype (WP)reproductive system morphology variant0Moderately InformativeDirect
Worm Phenotype (WP)vesicle organization variant0InformativeDirect
Worm Phenotype (WP)oocyte morphology variant0InformativeDirect
Worm Phenotype (WP)diplotene progression during oogenesis variant0InformativeDirect
Worm Phenotype (WP)somatic gonad development variant0InformativeDirect
Worm Phenotype (WP)lysosome-related organelle morphology variant0Highly InformativeDirect
Worm Phenotype (WP)cell membrane organization biogenesis variant0Highly InformativeDirect
Worm Phenotype (WP)oocyte septum formation variant0Highly InformativeDirect

Document: WP annotation of SCOP domains

Yeast Phenotype (YP)

(show details)
YP termFDR (all)SDYP levelAnnotation (direct or inherited)
Yeast Phenotype (YP)resistance to chemicals0Least InformativeDirect
Yeast Phenotype (YP)metabolism and growth0Least InformativeDirect
Yeast Phenotype (YP)morphology0Moderately InformativeDirect
Yeast Phenotype (YP)nutrient utilization0Moderately InformativeDirect
Yeast Phenotype (YP)lifespan0InformativeDirect
Yeast Phenotype (YP)chemical compound accumulation0InformativeDirect
Yeast Phenotype (YP)respiratory metabolism0InformativeDirect
Yeast Phenotype (YP)vegetative growth0InformativeDirect
Yeast Phenotype (YP)subcellular morphology0.2558InformativeInherited
Yeast Phenotype (YP)respiratory growth0Highly InformativeDirect
Yeast Phenotype (YP)chronological lifespan0Highly InformativeDirect
Yeast Phenotype (YP)desiccation resistance0Highly InformativeDirect
Yeast Phenotype (YP)alkaline pH resistance0.00000371Highly InformativeDirect
Yeast Phenotype (YP)mitochondrial morphology0.00002675Highly InformativeDirect

Document: YP annotation of SCOP domains

Fly Phenotype (FP)

(show details)
FP termFDR (all)SDFP levelAnnotation (direct or inherited)
Fly Phenotype (FP)viable0Least InformativeDirect
Fly Phenotype (FP)increased mortality0Least InformativeDirect
Fly Phenotype (FP)sterile0InformativeDirect
Fly Phenotype (FP)short lived0Highly InformativeDirect

Document: FP annotation of SCOP domains

Arabidopsis Plant Ontology (AP)

(show details)
AP termFDR (all)SDAP levelAnnotation (direct or inherited)
Plant ANatomical entity (PAN)whole plant0Least InformativeDirect
Plant ANatomical entity (PAN)guard cell0Least InformativeDirect
Plant ANatomical entity (PAN)microsporophyll0Least InformativeDirect
Plant ANatomical entity (PAN)sporangium0Least InformativeDirect
Plant ANatomical entity (PAN)pollen0Moderately InformativeDirect
Plant structure DEvelopment stage (PDE)seed development stage0InformativeDirect

Document: AP annotation of SCOP domains

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEC levelAnnotation (direct or inherited)
Enzyme Commission (EC)Catalysing the translocation of hydrons0InformativeDirect
Enzyme Commission (EC)Hydron translocation linked to the hydrolysis of a nucleoside triphosphate0Highly InformativeDirect
Enzyme Commission (EC)Linked to the hydrolysis of a nucleoside triphosphate0.213Highly InformativeInherited

Document: EC annotation of SCOP domains

InterPro annotation
Cross references IPR004100 SSF50615 Protein matches
Abstract

This entry represents the alpha and beta subunits found in the F1, V1, and A1 complexes of F-, V- and A-ATPases, respectively (sometimes called the A and B subunits in V- and A-ATPases). The F-ATPases (or F1F0-ATPases), V-ATPases (or V1V0-ATPases) and A-ATPases (or A1A0-ATPases) are composed of two linked complexes: the F1, V1 or A1 complex contains the catalytic core that synthesizes/hydrolyses ATP, and the F0, V0 or A0 complex that forms the membrane-spanning pore. The F-, V- and A-ATPases all contain rotary motors, one that drives proton translocation across the membrane and one that drives ATP synthesis/hydrolysis [PubMed11309608, PubMed15629643].

In F-ATPases, there are three copies each of the alpha and beta subunits that form the catalytic core of the F1 complex, while the remaining F1 subunits (gamma, delta, epsilon) form part of the stalks. There is a substrate-binding site on each of the alpha and beta subunits, those on the beta subunits being catalytic, while those on the alpha subunits are regulatory. The alpha and beta subunits form a cylinder that is attached to the central stalk. The alpha/beta subunits undergo a sequence of conformational changes leading to the formation of ATP from ADP, which are induced by the rotation of the gamma subunit, itself is driven by the movement of protons through the F0 complex C subunit [PubMed12745923].

In V- and A-ATPases, the alpha/A and beta/B subunits of the V1 or A1 complex are homologous to the alpha and beta subunits in the F1 complex of F-ATPases, except that the alpha subunit is catalytic and the beta subunit is regulatory.

The alpha/A and beta/B subunits can each be divided into three regions, or domains, centred around the ATP-binding pocket, and based on structure and function, where the central region is the nucleotide-binding domain [PubMed12885621]. This entry represents the N-terminal domain of the alpha/A/beta/B subunits, which forms a closed beta-barrel with Greek-key topology.

More information about this protein can be found at Protein of the Month: ATP Synthases.


InterPro database


PDBeMotif information about ligands, sequence and structure motifs
Cross references PDB entries
Ligand binding statistics
Nucleic-acid binding statistics
Occurrence of secondary structure elements
Occurrence of small 3D structural motifs

PDBeMotif resource

Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Enzyme Commission (EC) · Worm Phenotype (WP) · Yeast Phenotype (YP) · Fly Phenotype (FP) · Arabidopsis Plant Ontology (AP) · Enzyme Commission (EC) ]

Internal database links

Browse genome assignments for this superfamily. The SUPERFAMILY hidden Markov model library has been used to carry out SCOP domain assignments to all genomes at the superfamily level.


Alignments of sequences to 20 models in this superfamily are available by clicking on the 'Alignments' icon above. PDB sequences less than 40% identical are shown by default, but any other sequence(s) may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own sequences.


Browse and view proteins in genomes which have different domain combinations including a N-terminal domain of alpha and beta subunits of F1 ATP synthase domain.


Examine the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.


Explore domain occurrence network where nodes represent genomes and edges are domain architectures (shared between genomes) containing the superfamily of interest.

There are 20 hidden Markov models representing the N-terminal domain of alpha and beta subunits of F1 ATP synthase superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be inspected.


Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Enzyme Commission (EC) · Worm Phenotype (WP) · Yeast Phenotype (YP) · Fly Phenotype (FP) · Arabidopsis Plant Ontology (AP) · Enzyme Commission (EC) · Internal database links ]