PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: histidyl-tRNA synthetase; COGs: COG0124 Histidyl-tRNA synthetase; HAMAP: Histidyl-tRNA synthetase, class IIa, subgroup; InterPro IPR015807:IPR002314:IPR004154; KEGG: npu:Npun_R5420 histidyl-tRNA synthetase; PFAM: Anticodon-binding; Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved domain; PRIAM: Histidine--tRNA ligase; SPTR: Histidyl-tRNA synthetase; TIGRFAM: Histidyl-tRNA synthetase, class IIa, subgroup.

alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.

ATP synthase F1 subcomplex delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.

GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP.

phenylalanyl-tRNA synthetase, alpha subunit; PFAM: tRNA synthetases class II core domain (F); Aminoacyl tRNA synthetase class II, N-terminal domain; TIGRFAM: phenylalanyl-tRNA synthetase, alpha subunit; COGs: COG0016 Phenylalanyl-tRNA synthetase alpha subunit; HAMAP: Phenylalanyl-tRNA synthetase alpha chain 1, bacterial; InterPro IPR022911:IPR004529:IPR004188:IPR002319; KEGG: npu:Npun_R0940 phenylalanyl-tRNA synthetase subunit alpha; PFAM: Phenylalanyl-tRNA synthetase; Phenylalanyl-tRNA synthetase, class II, N-terminal; SPTR: Phenylalanyl-tRNA synthetase alpha chain; TIGRFAM: Phenylala [...]

aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.

valyl-tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.

Isoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.

SSU ribosomal protein S7P; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA; Belongs to the universal ribosomal protein uS7 family.