E4TJZ0 (E4TJZ0_CALNY) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Phenylalanine--tRNA ligase alpha subunit HAMAP-Rule MF_00281
EC=6.1.1.20 HAMAP-Rule MF_00281

Alternative name(s):
Phenylalanyl-tRNA synthetase alpha subunit HAMAP-Rule MF_00281

Gene names

Name:	pheS HAMAP-Rule MF_00281
Ordered Locus Names:	Calni_0328 EMBL ADR18241.1

Organism

Calditerrivibrio nitroreducens (strain DSM 19672 / NBRC 101217 / Yu37-1) [Complete proteome] [HAMAP] EMBL ADR18241.1

Taxonomic identifier

768670 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Deferribacteres › Deferribacteres › Deferribacterales › Deferribacteraceae › Calditerrivibrio › Calditerrivibrio nitroreducens

Protein attributes

Sequence length	336 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe). HAMAP-Rule MF_00281 SAAS SAAS004529
Cofactor	Binds 2 magnesium ions per tetramer By similarity. HAMAP-Rule MF_00281 SAAS SAAS004529
Subunit structure	Tetramer of two alpha and two beta subunits By similarity. HAMAP-Rule MF_00281 SAAS SAAS004529
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00281 SAAS SAAS004529.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. HAMAP-Rule MF_00281

Ontologies

Keywords
Biological process	Protein biosynthesis HAMAP-Rule MF_00281 SAAS SAAS004529
Cellular component	Cytoplasm HAMAP-Rule MF_00281 SAAS SAAS004529
Ligand	ATP-binding HAMAP-Rule MF_00281 SAAS SAAS004529 Magnesium HAMAP-Rule MF_00281 SAAS SAAS004529 Metal-binding HAMAP-Rule MF_00281 SAAS SAAS004529 Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase HAMAP-Rule MF_00281 SAAS SAAS004529 EMBL ADR18241.1 Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	phenylalanyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP phenylalanine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP tRNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Metal binding	251	1	Magnesium By similarity HAMAP-Rule MF_00281

Sequences

	Sequence		Length	Mass (Da)
	E4TJZ0 [UniParc]. Last modified February 8, 2011. Version 1. Checksum: 30CC7D83E19F2C75	FASTA	336	38,852
	10 20 30 40 50 60 MEISKEIYEY KKEIVDAENL EQLYQVWVKY LGKKGLISLL NKELKNVPEE KRSEFGRIIV 70 80 90 100 110 120 GLREDFEKLY QEREIELKKA EINDKIEKER IDVTLPAFPL NYGGLHPITQ VYFEIVDIFK 130 140 150 160 170 180 SMGYELATGP EIELDFYNFE ALNIPKEHPA RDMQDTFYID DEVLLRTHTS PVQIRTMEMK 190 200 210 220 230 240 EPPIKIIAPG KVYRCDSDVT HTPMFHQVEG LLIDTDTTFG DLKGALITFI HRLFGKDIPV 250 260 270 280 290 300 RFRPSFFPFT EPSAEVDMGC VICGGKGCRV CKGTGWLEIL GSGMVHPKVL ESVGYDSEKY 310 320 330 RGFAFGMGIE RITMLKFGID DLRLFFDNNI KFLRQF

References

[1]

"The complete genome of chromosome of Calditerrivibrio nitroreducens DSM 19672." US DOE Joint Genome Institute (JGI-PGF) Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Zeytun A., Brettin T., Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V. , Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A. Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 19672.

[2]

"Complete genome sequence of Calditerrivibrio nitroreducens type strain (Yu37-1)." Pitluck S., Sikorski J., Zeytun A., Lapidus A., Nolan M., Lucas S., Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A., Chen A. , Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Brambilla E., Djao O.D., Rohde M., Spring S., Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Land M. Stand. Genomic Sci. 4:54-62(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 19672 / NBRC 101217 / Yu37-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP002347 Genomic DNA. Translation: ADR18241.1.
RefSeq	YP_004050404.1. NC_014758.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ADR18241; ADR18241; Calni_0328.
GeneID	10008330.
KEGG	cni:Calni_0328.
PATRIC	45188341. VBICalNit163602_0394.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000242675.
KO	K01889.
OMA	LTHTPMF.
Enzyme and pathway databases
BioCyc	CNIT768670:GHD1-332-MONOMER.
Family and domain databases
HAMAP	MF_00281. Phe_tRNA_synth_alpha1.
InterPro	IPR006195. aa-tRNA-synth_II. IPR004529. Phe-tRNA-synth_IIc_asu. IPR004188. Phe-tRNA_ligase_II_N. IPR022911. Phe_tRNA_ligase_alpha1_bac. IPR002319. Phenylalanyl-tRNA_Synthase. IPR010978. tRNA-bd_arm. [Graphical view]
Pfam	PF02912. Phe_tRNA-synt_N. 1 hit. PF01409. tRNA-synt_2d. 1 hit. [Graphical view]
SUPFAM	SSF46589. tRNA_binding_arm. 1 hit.
TIGRFAMs	TIGR00468. pheS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

E4TJZ0_CALNY

Accession

Primary (citable) accession number: E4TJZ0

Entry history

Integrated into UniProtKB/TrEMBL:	February 8, 2011
Last sequence update:	February 8, 2011
Last modified:	May 1, 2013
This is version 19 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)