P84178 (SY1_PHYPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Putative isoleucine--tRNA ligase EC=6.1.1.5 Alternative name(s): Isoleucyl-tRNA synthetase Short name=IleRS
Organism	Physarum polycephalum (Slime mold)
Taxonomic identifier	5791 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Amoebozoa › Mycetozoa › Myxogastria › Myxogastromycetidae › Physariida › Physaraceae › Physarum

Protein attributes

Sequence length	64 AA.
Sequence status	Fragments.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile).
Subunit structure	Member of a complex that includes annexin. Ref.1
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.
Caution	The order of the peptides shown is unknown. Ref.1

Ontologies

Keywords
Biological process	Protein biosynthesis
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	translation Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW isoleucine-tRNA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – ›64	›64	Putative isoleucine--tRNA ligase		PRO_0000098606
Experimental info
	Non-adjacent residues	10 – 11	2
	Non-adjacent residues	25 – 26	2
	Non-adjacent residues	36 – 37	2
	Non-adjacent residues	47 – 48	2
	Non-adjacent residues	56 – 57	2
	Non-terminal residue	1	1
	Non-terminal residue	64	1

Sequences

	Sequence		Length	Mass (Da)
	P84178 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: D4FEA4CFEB8C7ECE	FASTA	64	7,116
	10 20 30 40 50 60 LSGVRVTDLH AGVNPGDPVE VFYAVKYTPL FNYFLKVMPY STVLTTSLIN ILYXDNVALA FXXI

References

[1]	"Class-specific binding of two aminoacyl-tRNA synthetases to annexin, a Ca2+- and phospholipid-binding protein." Shirakawa T., Nakamura A., Kohama K., Hirakata M., Ogihara S. Cell Struct. Funct. 29:159-164(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE, SUBUNIT.

Cross-references

3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
PROSITE	PS00178. AA_TRNA_LIGASE_I. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SY1_PHYPO

Accession

Primary (citable) accession number: P84178

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	April 26, 2005
Last modified:	January 25, 2012
This is version 19 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)