C1F7U6 (C1F7U6_ACIC5) 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 EMBL ACO33434.1
Ordered Locus Names:	ACP_1828

Organism

Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / JCM 7670) [Complete proteome] [HAMAP]

Taxonomic identifier

240015 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Fibrobacteres/Acidobacteria group › Acidobacteria › Acidobacteriia › Acidobacteriales › Acidobacteriaceae › Acidobacterium › Acidobacterium capsulatum

Protein attributes

Sequence length	371 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 ACO33434.1 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	280	1	Magnesium By similarity HAMAP-Rule MF_00281

Sequences

	Sequence		Length	Mass (Da)
	C1F7U6 [UniParc]. Last modified May 26, 2009. Version 1. Checksum: 71D6E2FB88152FBE	FASTA	371	40,776
	10 20 30 40 50 60 MTMSDQPIPS LTGWTEAELD AAFAALMREV ESSAAALDAT SAEAVEAFRL HWLGRKQGRL 70 80 90 100 110 120 KAVSDAWLKA APVEAKKLLG QRFNALKAQV EARLDDASSA SSASALDAEA IDITLPGRAR 130 140 150 160 170 180 RLGAEHPLIK TLNEIVSIFQ RMGYSVGVGP EVETDYYNFE SLNFPPNHPA RDTQDTLVVA 190 200 210 220 230 240 QQERKPLRDR LLMRTHTSPV QIRTMEQQPP PVRIVIPGKV HRNDAADATH SPIFHQVEGL 250 260 270 280 290 300 CVDTNITFSD LKGTLDHAMK ELFGTSVKTR FFPSFFPFTE PSADVQISCP FCGGKGCRKC 310 320 330 340 350 360 KHSGWIELLG CGMVDPAVFG FVQQKQPGYD PKKISGFAFG MGVDRIAMMK YGISDIGLLY 370 GGDQRFLEQF G

References

[1]

"Three genomes from the phylum Acidobacteria provide insight into the lifestyles of these microorganisms in soils." Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C., Davidsen T.M. , DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R. Appl. Environ. Microbiol. 75:2046-2056(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51196 / DSM 11244 / JCM 7670.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001472 Genomic DNA. Translation: ACO33434.1.
RefSeq	YP_002754902.1. NC_012483.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	240015.ACP_1828.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACO33434; ACO33434; ACP_1828.
GeneID	7701045.
KEGG	aca:ACP_1828.
PATRIC	20666951. VBIAciCap40988_1762.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0016.
HOGENOM	HOG000242675.
KO	K01889.
OMA	LTHTPMF.
ProtClustDB	PRK00488.
Enzyme and pathway databases
BioCyc	ACAP240015:GI5H-2169-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

C1F7U6_ACIC5

Accession

Primary (citable) accession number: C1F7U6

Entry history

Integrated into UniProtKB/TrEMBL:	May 26, 2009
Last sequence update:	May 26, 2009
Last modified:	May 1, 2013
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)