Q827S4 (SYA_STRAW) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alanine--tRNA ligase
EC=6.1.1.7

Alternative name(s):
Alanyl-tRNA synthetase
Short name=AlaRS

Gene names

Name:	alaS
Ordered Locus Names:	SAV_6850

Organism

Streptomyces avermitilis [Complete proteome] [HAMAP]

Taxonomic identifier

33903 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	890 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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 By similarity. HAMAP MF_00036_B
Catalytic activity	ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP MF_00036_B
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_00036_B
Subcellular location	Cytoplasm HAMAP MF_00036_B.
Domain	Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs By similarity. HAMAP MF_00036_B
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding RNA-binding Zinc tRNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	alanyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW alanine-tRNA ligase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW tRNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 890	890	Alanine--tRNA ligase HAMAP MF_00036_B		PRO_0000075223
Sites
	Metal binding	573	1	Zinc Potential
	Metal binding	577	1	Zinc Potential
	Metal binding	675	1	Zinc Potential
	Metal binding	679	1	Zinc Potential

Sequences

	Sequence		Length	Mass (Da)
	Q827S4 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 9E5F2A4B281B07DF	FASTA	890	96,256
	10 20 30 40 50 60 MESAEIRRRW LSFYEERGHT VVPSASLIAD DPTLLLVPAG MVPFKPYFLG EVKPPWPRAT 70 80 90 100 110 120 SVQKCVRTPD IEEVGKTTRH GTFFQMCGNF SFGDYFKEGA ITYAWELLTT PQDKGGYGLD 130 140 150 160 170 180 PERLWITVYL DDDEAETIWR DKIGVPAERI QRLGKKDNYW SMGVPGPCGP CSEINYDRGP 190 200 210 220 230 240 EFGVEGGPAV NDERYVEIWN LVFMQYERGE GTSKDDFEIL GDLPQKNIDT GLGMERLAMI 250 260 270 280 290 300 LQGVQNMYEI DTSMAVIQKA TELTGVEYGA AHGSDVSLRV VTDHMRTSVM LIGDGVTPGN 310 320 330 340 350 360 EGRGYVLRRI MRRAIRNMRL LGATGPVVKD LVDVVIAMMG QQYPELISDR QRIETVALAE 370 380 390 400 410 420 EAAFLKTLKA GTNILDTAVT ETKASGGQVL PGDKAFLLHD TWGFPIDLTL EMAAEQGLSV 430 440 450 460 470 480 DEDGFRRLMK EQRERAKADA QSKKTGHADL GAYREIADAA GETDFIGYTQ TEGESTIVGI 490 500 510 520 530 540 LVDGVSSPAA TEGDEVEIVL DRTPFYAEGG GQIGDTGRIK VESGAIIEVR DCQKPVPGVY 550 560 570 580 590 600 VHKGVVQVGE VTVGAKAQVS IDVRRRKAIA RAHSATHLTH QALRDALGPT AAQAGSENQP 610 620 630 640 650 660 GRFRFDFGSP SAVPTTVMTD VEQQINEVLA RDLDVQAEVM SIDEAKKQGA IAEFGEKYGE 670 680 690 700 710 720 RVRVVTIGDF SKELCGGTHV HNTAQLGLVK LLGESSIGSG VRRIEALVGV DAYNFLAREH 730 740 750 760 770 780 TVVAQIQELV KGRPEELPEK VSAMLGKLKD AEKEIERFRA EKVLQAAAGL VDSAKDVRGI 790 800 810 820 830 840 ALVTGQVPDG TTADDLRRLV LDVRGRIQGG RPAVVALFTT VGGKPLTVIA TNEAARERGL 850 860 870 880 890 KAGDLVRAAA KTLGGGGGGK PDVAQGGGQN PAAIGEAIDA VERLVTETAK

References

[1]

"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites." Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M. Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed: 11572948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

[2]

"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis." Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S. Nat. Biotechnol. 21:526-531(2003) [PubMed: 12692562] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000030 Genomic DNA. Translation: BAC74561.1.
RefSeq	NP_828026.1. NC_003155.4.
3D structure databases
ProteinModelPortal	Q827S4.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1211591.
GenomeReviews	Gene locus SAV_6850 in contig BA000030_GR.
KEGG	sma:SAV_6850.
NMPDR	fig|227882.1.peg.6852.
PATRIC	23727834. VBIStrAve112782_7259.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG354397.
OMA	GESKTDQ.
ProtClustDB	PRK00252.
Enzyme and pathway databases
BioCyc	SAVE227882:SAV6850-MONOMER.
Family and domain databases
HAMAP	MF_00036_B. Ala_tRNA_synth_B. [Tree]
InterPro	IPR002318. Ala-tRNA-synth_IIc. IPR018162. Ala-tRNA-synth_IIc_anticod-bd. IPR018165. Ala-tRNA-synth_IIc_core. IPR018164. Ala-tRNA-synth_IIc_N. IPR023033. Ala_tRNA_synth_euk/bac. IPR003156. Pesterase_DHHA1. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view]
KO	K01872.
PANTHER	PTHR11777:SF6. PTHR11777:SF6. 1 hit.
Pfam	PF02272. DHHA1. 1 hit. PF01411. tRNA-synt_2c. 1 hit. PF07973. tRNA_SAD. 1 hit. [Graphical view]
PRINTS	PR00980. TRNASYNTHALA.
SMART	SM00863. tRNA_SAD. 1 hit. [Graphical view]
SUPFAM	SSF101353. Ala-tRNA-synth_IIc_anticod-bd. 1 hit. SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit.
TIGRFAMs	TIGR00344. AlaS. 1 hit.
PROSITE	PS50860. AA_TRNA_LIGASE_II_ALA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYA_STRAW

Accession

Primary (citable) accession number: Q827S4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program