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InterPro: IPR012947 Threonyl/alanyl tRNA synthetase, SAD

Protein matches Help

UniProtKB

Matches:

4650 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR012947 tRNA_SAD

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF07973	tRNA_SAD	4647
SMART	SM00863	tRNA_SAD	4598
Signatures in BioMart

InterPro Relationships Help

Found in

IPR002318 Alanyl-tRNA synthetase, class IIc
IPR002320 Threonyl-tRNA synthetase, class IIa
IPR018163 Threonyl/alanyl tRNA synthetase, class II-like, putative editing domain
IPR018165 Alanyl-tRNA synthetase, class IIc, core domain

GO Term annotation Help

Process

GO:0006412 translation
GO:0043039 tRNA aminoacylation

Function

GO:0005524 ATP binding
GO:0016876 ligase activity, forming aminoacyl-tRNA and related compounds

Component

GO:0005737 cytoplasm

InterPro annotation

Entry Details in BioMart

Abstract

The catalytically active form of threonyl/alanyl tRNA synthetase is a dimer. Within the tRNA synthetase class II dimer, the bound tRNA interacts with both monomers making specific interactions with the catalytic domain, the C-terminal domain, and this SAD domain (the second additional domain). The second additional domain is comprised of a pair of perpendicularly orientated antiparallel beta sheets, of four and three strands, respectively, that surround a central alpha helix that forms the core of the domain [1].

Structural links Help

PDB - click here

SCOP: d.67.1.1 , d.67.1.2

CATH: 3.30.54.20 , 3.30.980.10

Database links Help

Enzyme: EC:6.1.1

PANDIT: PF07973

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR012947

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O04630 Threonyl-tRNA synthetase, mitochondrial

P04801 Threonyl-tRNA synthetase, cytoplasmic

P26639 Threonyl-tRNA synthetase, cytoplasmic

P52709 Threonyl-tRNA synthetase, cytoplasmic

Q14CH7 Probable alanyl-tRNA synthetase, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR012947	Threonyl/alanyl tRNA synthetase, SAD
IPR002318	Alanyl-tRNA synthetase, class IIc
IPR002320	Threonyl-tRNA synthetase, class IIa
IPR004154	Anticodon-binding
IPR018158	Threonyl-tRNA synthetase, class IIa, conserved region
IPR004095	TGS
IPR002314	Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved region
IPR012676	TGS-like
IPR012675	Beta-grasp fold, ferredoxin-type
IPR018165	Alanyl-tRNA synthetase, class IIc, core domain
IPR006195	Aminoacyl-tRNA synthetase, class II, conserved region
IPR018162	Alanyl-tRNA synthetase, class IIc, anti-codon-binding domain
IPR018163	Threonyl/alanyl tRNA synthetase, class II-like, putative editing domain
IPR018164	Alanyl-tRNA synthetase, class IIc, N-terminal
	PDB Chain
	ModBase
	SWISS-MODEL

Publications Open in usermanual
1.	Sankaranarayanan R, Dock-Bregeon AC, Romby P, Caillet J, Springer M, Rees B, Ehresmann C, Ehresmann B, Moras D. The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site. Cell 97 371-81 1999 [PubMed: 10319817] http://dx.doi.org/10.1016/S0092-8674(00)80746-1

Additional Reading Open in usermanual
	Sokabe M, Okada A, Yao M, Nakashima T, Tanaka I. Molecular basis of alanine discrimination in editing site. Proc. Natl. Acad. Sci. U.S.A. 102 2005 11669-74 [PubMed: 16087889] http://dx.doi.org/10.1073/pnas.0502119102
	Torres-Larios A, Sankaranarayanan R, Rees B, Dock-Bregeon AC, Moras D. Conformational movements and cooperativity upon amino acid, ATP and tRNA binding in threonyl-tRNA synthetase. J. Mol. Biol. 331 2003 201-11 [PubMed: 12875846] http://dx.doi.org/10.1016/S0022-2836(03)00719-8
	Ishijima J, Uchida Y, Kuroishi C, Tuzuki C, Takahashi N, Okazaki N, Yutani K, Miyano M. Crystal structure of alanyl-tRNA synthetase editing-domain homolog (PH0574) from a hyperthermophile, Pyrococcus horikoshii OT3 at 1.45 A resolution. Proteins 62 2006 1133-7 [PubMed: 16374837] http://dx.doi.org/10.1002/prot.20760
	Dock-Bregeon AC, Rees B, Torres-Larios A, Bey G, Caillet J, Moras D. Achieving error-free translation; the mechanism of proofreading of threonyl-tRNA synthetase at atomic resolution. Mol. Cell 16 2004 375-86 [PubMed: 15525511] http://dx.doi.org/10.1016/j.molcel.2004.10.002
	Fukunaga R, Yokoyama S. Structure of the AlaX-M trans-editing enzyme from Pyrococcus horikoshii. Acta Crystallogr. D Biol. Crystallogr. 63 2007 390-400 [PubMed: 17327676] http://dx.doi.org/10.1107/S090744490605640X

InterPro 23.1