SMART: small_GTPase domain annotation

small_GTPase Small GTPase of the Ras superfamily; ill-defined subfamily

SMART accession number:	SM00010
Description:	SMART predicts Ras-like small GTPases of the ARF, RAB, RAN, RAS, and SAR subfamilies. Others that could not be classified in this way are predicted to be members of the small GTPase superfamily without predictions of the subfamily.
Family alignment:	View or

There are 12 small_GTPase domains in 10 proteins in SMART's nrdb database.

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Evolution (species in which this domain is found)
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This tree shows only several representative species. The complete taxonomic breakdown of all proteins with small_GTPase domain is also avaliable.

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Go to specific node: Homo sapiens
Cellular role (predicted cellular role)
Binding / catalysis: GTP hydrolysis
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Bos JL
- Ras-like GTPases.
- Biochim Biophys Acta. 1997; 1333: 1931-1931
- Geyer M, Wittinghofer A
- GEFs, GAPs, GDIs and effectors: taking a closer (3D) look at the regulation of Ras-related GTP-binding proteins.
- Curr Opin Struct Biol. 1997; 7: 786-92
- Display abstract
- Cell biology depends on the interactions of macromolecules, such as protein-DNA, protein-protein or protein-nucleotide interactions. GTP-binding proteins are no exception to the rule. They regulate cellular processes as diverse as protein biosynthesis and intracellular membrane trafficking. Recently, a large number of genes encoding GTP-binding proteins and the proteins that interact with these molecular switches have been cloned and expressed. The 3D structures of some of these have also been elucidated.
- Sprang SR
- G proteins, effectors and GAPs: structure and mechanism.
- Curr Opin Struct Biol. 1997; 7: 849-56
- Display abstract
- G proteins from a diverse family of regulatory GTPases which, in the GTP-bound state, bind to and activate downstream effectors. Structures of Ras homologs bound to effector domains have revealed mechanisms by which G proteins couple GTP binding to effector activation and achieve specificity. Complexes between structurally unrelated GTPase-activating proteins with complementary G proteins suggest common mechanisms by which GTP hydrolysis is stimulated via direct interactions with conformationally labile switch regions of the G protein.
Metabolism (metabolic pathways involving proteins which contain this domain)

Structure (3D structures containing this domain)

3D Structures of small_GTPase domains in PDB

PDB code	Main view	Title
1byu		Canine gdp-ran
1e0s		Small g protein arf6-gdp
1fqj		Crystal structure of the heterotrimeric complex of the rgs domain of rgs9, the gamma subunit of phosphodiesterase and the gt/i1 chimera alpha subunit [(rgs9)-(pdegamma)- (gt/i1alpha)-(gdp)-(alf4-)-(mg2+)]
1fqk		Crystal structure of the heterodimeric complex of the rgs domain of rgs9, and the gt/i1 chimera alpha subunit [(rgs9)-(gt/i1alpha)-(gdp)-(alf4-)-(mg2+)]
1got		Heterotrimeric complex of a gt-alpha/gi-alpha chimera and the gt-beta-gamma subunits
1svk		Structure of the k180p mutant of gi alpha subunit bound to alf4 and gdp
1svs		Structure of the k180p mutant of gi alpha subunit bound to gppnhp.
1xzp		Structure of the gtp-binding protein trme from thermotoga maritima
1xzq		Structure of the gtp-binding protein trme from thermotoga maritima complexed with 5-formyl-thf
1yzg		Structure of human adp-ribosylation factor-like 8
1z6y		Structure of human adp-ribosylation factor-like 5
1zd9		Structure of human adp-ribosylation factor-like 10b
1zj6		Crystal structure of human arl5
2a5d		Structural basis for the activation of cholera toxin by human arf6-gtp
2a5f		Cholera toxin a1 subunit bound to its substrate, nad+, and its human protein activator, arf6
2a5g		Cholera toxin a1 subunit bound to arf6(q67l)
2al7		Structure of human adp-ribosylation factor-like 10c
2bmj		Gtpase like domain of centaurin gamma 1 (human)
2cjw		Crystal structure of the small gtpase gem (gemdndcam) in complex to mg.gdp
2dpx		Crystal structure of human rad gtpase
2fh5		The structure of the mammalian srp receptor
2g3y		Crystal structure of the human small gtpase gem
2gjs		The crystal structure of human rrad in complex with gdp
2go5		Structure of signal recognition particle receptor (sr) in complex with signal recognition particle (srp) and ribosome nascent chain complex
2h16		Structure of human adp-ribosylation factor-like 5 (arl5)
2h18		Structure of human adp-ribosylation factor-like 10b (arl10b)
2h57		Crystal structure of human adp-ribosylation factor-like 6
2ht6		Crystal structure of human gem g-domain bound to gdp
2hxs		Crystal structure of rab28a gtpase in the inactive (gdp-3'p- bound) form
2iwr		Gtpase like domain of centaurin gamma 1 (human)
2j5x		Structure of the small g protein arf6 in complex with gtpgammas
2nzj		The crystal structure of rem1 in complex with gdp
2zej		Structure of the roc domain from the parkinson's disease- associated leucine-rich repeat kinase 2 reveals a dimeric gtpase
3c5c		Crystal structure of human ras-like, family 12 protein in complex with gdp
3cbq		Crystal structure of the human rem2 gtpase with bound gdp
3d6t		Structure of the roc domain from the parkinson's disease- associated leucine-rich repeat kinase 2 reveals a dimeric gtpase
3dpu		Roccor domain tandem of rab family protein (roco)
3e5h		Crystal structure of rab28 gtpase in the active (gppnhp- bound) form
3gee		Crystal structure of mnme from chlorobium tepidum in complex with gdp and folinic acid
3geh		Crystal structure of mnme from nostoc in complex with gdp, folinic acid and zn
3gei		Crystal structure of mnme from chlorobium tepidum in complex with gcp
3gj0		Crystal structure of human rangdp
3gj3		Crystal structure of human rangdp-nup153znf2 complex
3gj4		Crystal structure of human rangdp-nup153znf3 complex
3gj5		Crystal structure of human rangdp-nup153znf4 complex
3gj6		Crystal structure of human rangdp-nup153znf1 complex
3gj7		Crystal structure of human rangdp-nup153znf12 complex
3gj8		Crystal structure of human rangdp-nup153znf34 complex
3ihw		Crystal structure of the ras-like domain of centg3