1ULH

A short peptide insertion crucial for angiostatic activity of human tryptophanyl-tRNA synthetase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004830	molecular_function	tryptophan-tRNA ligase activity
A	0005524	molecular_function	ATP binding
A	0006418	biological_process	tRNA aminoacylation for protein translation
A	0006436	biological_process	tryptophanyl-tRNA aminoacylation
B	0000166	molecular_function	nucleotide binding
B	0004812	molecular_function	aminoacyl-tRNA ligase activity
B	0004830	molecular_function	tryptophan-tRNA ligase activity
B	0005524	molecular_function	ATP binding
B	0006418	biological_process	tRNA aminoacylation for protein translation
B	0006436	biological_process	tryptophanyl-tRNA aminoacylation

Functional Information from PROSITE/UniProt

site_id	PS00178
Number of Residues	11
Details	AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Ps.SEaMHVGHL

Chain	Residue	Details
A	PRO117-LEU127

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	Motif: {"description":"'HIGH' region","evidences":[{"source":"PubMed","id":"1373391","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P32921","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	4
Details	Motif: {"description":"'KMSKS' region","evidences":[{"source":"PubMed","id":"1373391","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1d2r

Chain	Residue	Details
B	LYS302
B	ALA305

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