2RHS

PheRS from Staphylococcus haemolyticus- rational protein engineering and inhibitor studies

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2rhsa_	Alpha and beta proteins (a+b)	Class II aaRS and biotin synthetases	Class II aaRS and biotin synthetases	automated matches	automated matches	(Staphylococcus haemolyticus ) [TaxId: 1283 ],	SCOPe (2.08)
C	d2rhsc1	Alpha and beta proteins (a+b)	Class II aaRS and biotin synthetases	Class II aaRS and biotin synthetases	automated matches	automated matches	(Staphylococcus haemolyticus ) [TaxId: 1283 ],	SCOPe (2.08)
C	d2rhsc2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Staphylococcus haemolyticus ) [TaxId: 1283 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Class II aaRS and biotin synthetases	8099502	3000058	SCOP2B (2022-06-29)
C	SCOP2 Family	Class II aminoacyl-tRNA synthetase (aaRS)-like catalytic domain	8099501	4001782	SCOP2 (2022-06-29)
C	SCOP2 Superfamily	Class II aaRS and biotin synthetases	8099502	3000058	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF01409	e2rhsA1	A: a+b three layers	X: Class II aaRS and biotin synthetases (From Topology)	H: Class II aaRS and biotin synthetases (From Topology)	T: Class II aaRS and biotin synthetases	F: PF01409	ECOD (1.6)
C	PF01409	e2rhsC1	A: a+b three layers	X: Class II aaRS and biotin synthetases (From Topology)	H: Class II aaRS and biotin synthetases (From Topology)	T: Class II aaRS and biotin synthetases	F: PF01409	ECOD (1.6)
B	PF01588	e2rhsB2	A: beta barrels	X: OB-fold	H: Nucleic acid-binding proteins (From Topology)	T: Nucleic acid-binding proteins	F: PF01588	ECOD (1.6)
B	PF03483	e2rhsB3	A: beta complex topology	X: PheT/TilS domain (From Topology)	H: PheT/TilS domain (From Topology)	T: PheT/TilS domain	F: PF03483	ECOD (1.6)
B	F_UNCLASSIFIED	e2rhsB1	A: alpha arrays	X: HTH	H: HTH	T: Putative DNA-binding domain	F: F_UNCLASSIFIED	ECOD (1.6)
B	PF03484	e2rhsB4	A: alpha arrays	X: HTH	H: HTH	T: Putative DNA-binding domain	F: PF03484	ECOD (1.6)
B	PF03147	e2rhsB6	A: a+b two layers	X: Alpha-beta plaits	H: Anticodon-binding domain of PheRS (From Topology)	T: Anticodon-binding domain of PheRS	F: PF03147	ECOD (1.6)
B	PF17759	e2rhsB5	A: a+b three layers	X: Class II aaRS and biotin synthetases (From Topology)	H: Class II aaRS and biotin synthetases (From Topology)	T: Class II aaRS and biotin synthetases	F: PF17759	ECOD (1.6)
D	PF01588	e2rhsD23	A: beta barrels	X: OB-fold	H: Nucleic acid-binding proteins (From Topology)	T: Nucleic acid-binding proteins	F: PF01588	ECOD (1.6)
D	PF03483	e2rhsD21	A: beta complex topology	X: PheT/TilS domain (From Topology)	H: PheT/TilS domain (From Topology)	T: PheT/TilS domain	F: PF03483	ECOD (1.6)
D	F_UNCLASSIFIED	e2rhsD19	A: alpha arrays	X: HTH	H: HTH	T: Putative DNA-binding domain	F: F_UNCLASSIFIED	ECOD (1.6)
D	PF03484	e2rhsD20	A: alpha arrays	X: HTH	H: HTH	T: Putative DNA-binding domain	F: PF03484	ECOD (1.6)
D	PF03147	e2rhsD24	A: a+b two layers	X: Alpha-beta plaits	H: Anticodon-binding domain of PheRS (From Topology)	T: Anticodon-binding domain of PheRS	F: PF03147	ECOD (1.6)
D	PF17759	e2rhsD22	A: a+b three layers	X: Class II aaRS and biotin synthetases (From Topology)	H: Class II aaRS and biotin synthetases (From Topology)	T: Class II aaRS and biotin synthetases	F: PF17759	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.930.10	Alpha Beta	2-Layer Sandwich	BirA Bifunctional Protein	domain 2	CATH (4.3.0)
C	3.30.930.10	Alpha Beta	2-Layer Sandwich	BirA Bifunctional Protein	domain 2	CATH (4.3.0)
B	3.30.56.10	Alpha Beta	2-Layer Sandwich	Phenylalanyl-tRNA Synthetase	Chain B, domain 1	CATH (4.3.0)
B	2.40.50.140	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)	Nucleic acid-binding proteins	CATH (4.3.0)
B	3.50.40.10	Alpha Beta	3-Layer(bba) Sandwich	Phenylalanyl-tRNA Synthetase	Chain B, domain 3	CATH (4.3.0)
B	3.30.930.10	Alpha Beta	2-Layer Sandwich	BirA Bifunctional Protein	domain 2	CATH (4.3.0)
B	3.30.70.380	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Ferrodoxin-fold anticodon-binding domain	CATH (4.3.0)
D	3.30.56.10	Alpha Beta	2-Layer Sandwich	Phenylalanyl-tRNA Synthetase	Chain B, domain 1	CATH (4.3.0)
D	2.40.50.140	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)	Nucleic acid-binding proteins	CATH (4.3.0)
D	3.50.40.10	Alpha Beta	3-Layer(bba) Sandwich	Phenylalanyl-tRNA Synthetase	Chain B, domain 3	CATH (4.3.0)
D	3.30.930.10	Alpha Beta	2-Layer Sandwich	BirA Bifunctional Protein	domain 2	CATH (4.3.0)
D	3.30.70.380	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Ferrodoxin-fold anticodon-binding domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, C	PF02912	Aminoacyl tRNA synthetase class II, N-terminal domain (Phe_tRNA-synt_N)	Aminoacyl tRNA synthetase class II, N-terminal domain	-	Domain
A, C	PF01409	tRNA synthetases class II core domain (F) (tRNA-synt_2d)	tRNA synthetases class II core domain (F)	Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only phenylalanyl-tRNA synthetases. This is the core catalytic domain.	Domain
B, D	PF03483	B3/4 domain (B3_4)	B3/4 domain	This domain is found in tRNA synthetase beta subunits as well as in some non tRNA synthetase proteins.	Domain
B, D	PF03484	tRNA synthetase B5 domain (B5)	tRNA synthetase B5 domain	This domain is found in phenylalanine-tRNA synthetase beta subunits.	Domain
B, D	PF03147	Ferredoxin-fold anticodon binding domain (FDX-ACB)	Ferredoxin-fold anticodon binding domain	This is the anticodon binding domain found in some phenylalanyl tRNA synthetases. The domain has a ferredoxin fold [1,2].	Domain
B, D	PF17759	Phenylalanyl tRNA synthetase beta chain CLM domain (tRNA_synthFbeta)	Phenylalanyl tRNA synthetase beta chain CLM domain	This domain corresponds to the catalytic like domain (CLM) in the beta chain of phe tRNA synthetase [1].	Domain
B, D	PF01588	Putative tRNA binding domain (tRNA_bind)	Putative tRNA binding domain	This domain is found in prokaryotic methionyl-tRNA synthetases, prokaryotic phenylalanyl tRNA synthetases the yeast GU4 nucleic-binding protein (G4p1 or p42, ARC1) [2], human tyrosyl-tRNA synthetase [1], and endothelial-monocyte activating polypept ...	This domain is found in prokaryotic methionyl-tRNA synthetases, prokaryotic phenylalanyl tRNA synthetases the yeast GU4 nucleic-binding protein (G4p1 or p42, ARC1) [2], human tyrosyl-tRNA synthetase [1], and endothelial-monocyte activating polypeptide II. G4p1 binds specifically to tRNA form a complex with methionyl-tRNA synthetases [2]. In human tyrosyl-tRNA synthetase this domain may direct tRNA to the active site of the enzyme [2]. This domain may perform a common function in tRNA aminoacylation [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, C	Phenylalanyl-tRNA synthetase alpha chain	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding ligase activity, forming carbon-oxygen bonds aminoacyl-tRNA ligase activity catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid phenylalanine-tRNA ligase activity catalytic activity, acting on a tRNA catalytic activity ligase activity RNA binding tRNA binding nucleic acid binding transferase activity	amino acid activation tRNA aminoacylation cellular biosynthetic process organonitrogen compound biosynthetic process RNA metabolic process amino acid metabolic process nucleobase-containing compound metabolic process organic substance metabolic process organic substance biosynthetic process protein metabolic process organonitrogen compound metabolic process cellular metabolic process primary metabolic process translation amino acid activation tRNA aminoacylation cellular biosynthetic process organonitrogen compound biosynthetic process RNA metabolic process amino acid metabolic process nucleobase-containing compound metabolic process organic substance metabolic process organic substance biosynthetic process protein metabolic process organonitrogen compound metabolic process cellular metabolic process primary metabolic process translation gene expression tRNA aminoacylation for protein translation macromolecule biosynthetic process nucleic acid metabolic process tRNA metabolic process organic cyclic compound metabolic process biosynthetic process ncRNA metabolic process metabolic process cellular process macromolecule metabolic process phenylalanyl-tRNA aminoacylation	intracellular anatomical structure cytoplasm cellular anatomical entity
B, D	Phenylalanyl-tRNA synthetase beta chain	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding ligase activity, forming carbon-oxygen bonds aminoacyl-tRNA ligase activity catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid phenylalanine-tRNA ligase activity catalytic activity, acting on a tRNA catalytic activity ligase activity RNA binding tRNA binding nucleic acid binding transferase activity	amino acid activation tRNA aminoacylation cellular biosynthetic process organonitrogen compound biosynthetic process RNA metabolic process amino acid metabolic process nucleobase-containing compound metabolic process organic substance metabolic process organic substance biosynthetic process protein metabolic process organonitrogen compound metabolic process cellular metabolic process primary metabolic process translation amino acid activation tRNA aminoacylation cellular biosynthetic process organonitrogen compound biosynthetic process RNA metabolic process amino acid metabolic process nucleobase-containing compound metabolic process organic substance metabolic process organic substance biosynthetic process protein metabolic process organonitrogen compound metabolic process cellular metabolic process primary metabolic process translation gene expression tRNA aminoacylation for protein translation macromolecule biosynthetic process nucleic acid metabolic process tRNA metabolic process organic cyclic compound metabolic process biosynthetic process ncRNA metabolic process metabolic process cellular process macromolecule metabolic process phenylalanyl-tRNA aminoacylation	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, C	IPR045864	Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)	Homologous Superfamily
A, C	IPR002319	Phenylalanyl-tRNA synthetase	Domain
A, C	IPR004188	Phenylalanine-tRNA ligase, class II, N-terminal	Domain
A, C	IPR004529	Phenylalanyl-tRNA synthetase, class IIc, alpha subunit	Family
A, C	IPR022911	Phenylalanine-tRNA ligase alpha chain 1, bacterial	Family
A, C	IPR006195	Aminoacyl-tRNA synthetase, class II	Domain
A, C	IPR010978	Class I and II aminoacyl-tRNA synthetase, tRNA-binding arm	Homologous Superfamily
B, D	IPR009061	Putative DNA-binding domain superfamily	Homologous Superfamily
B, D	IPR045060	Phenylalanine-tRNA ligase, class IIc, beta subunit	Family
B, D	IPR020825	Phenylalanyl-tRNA synthetase-like, B3/B4	Homologous Superfamily
B, D	IPR045864	Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)	Homologous Superfamily
B, D	IPR002547	tRNA-binding domain	Domain
B, D	IPR005147	tRNA synthetase, B5-domain	Domain
B, D	IPR005146	B3/B4 tRNA-binding domain	Domain
B, D	IPR041616	Phenylalanyl tRNA synthetase beta chain, core domain	Domain
B, D	IPR033714	Phenylalanly tRNA synthetase, tRNA-binding-domain	Domain
B, D	IPR005121	Ferrodoxin-fold anticodon-binding domain	Domain
B, D	IPR012340	Nucleic acid-binding, OB-fold	Homologous Superfamily
B, D	IPR036690	Ferrodoxin-fold anticodon-binding domain superfamily	Homologous Superfamily
B, D	IPR004532	Phenylalanine-tRNA ligase, class IIc, beta subunit, bacterial type	Family