B2RZT0 (SYA_BORHD) 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:	BH0220

Organism

Borrelia hermsii (strain DAH) [Complete proteome] [HAMAP]

Taxonomic identifier

314723 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia

Protein attributes

Sequence length	593 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 By similarity HAMAP MF_00036_B.
Domain	Consists of two domains; the N-terminal catalytic domain (in this organism this is shorter than usual) and the editing domain; the C-terminal C-Ala domain found in most orthologs is missing. The editing domain removes incorrectly charged amino acids 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 – 593	593	Alanine--tRNA ligase HAMAP MF_00036_B		PRO_0000347511
Sites
	Metal binding	456	1	Zinc Potential
	Metal binding	460	1	Zinc Potential
	Metal binding	558	1	Zinc Potential
	Metal binding	562	1	Zinc Potential

Sequences

	Sequence		Length	Mass (Da)
	B2RZT0 [UniParc]. Last modified July 1, 2008. Version 1. Checksum: E1B2C81631B1473C	FASTA	593	67,598
	10 20 30 40 50 60 MKLDELRKKY IDFFKSKGHC EIAGKSLIPD NDSTVLFNTA GMQPLVPYLL GEMHPSGDML 70 80 90 100 110 120 VDVQKCLRTG DIDEVGDLSH LTFFEMLGNW SLGAYFKELS VKYSFEFLTS PNYLNISKDK 130 140 150 160 170 180 LYVSVFEGDE SIPRDTETAN VWESLGIPKD RIFYLSREHN FWGPVGNTGP CGPDTEIFVD 190 200 210 220 230 240 TGKEKCSVRC DITCSCGKYF EIWNNVFMQY KRDENGNYEE LKRKCVDTGM GIERTITFLQ 250 260 270 280 290 300 GKSSVYDTDA FKPIIDKIEK ISGKIYGQNL EDDRSIRIIA DHIKASCFIL ADNFAVLPSN 310 320 330 340 350 360 IGQGYVLRRI IRRAIRYAKK LGMESYVLAD LVDSVEEIYK SFYKELTEKK DFIKAELNVE 370 380 390 400 410 420 EEKFFKTLRH GEQEFIKLIQ QLSSKSIPGD ISFKLYDTYG FPYEITEELA TEYGFSIDKA 430 440 450 460 470 480 GFEEHFKKHQ EVSKKGGDKV FKGGLADCTY ETTKLHTATH LLHKALQLVL GEHVRQKGSN 490 500 510 520 530 540 ITAERLRFDF NHPYKMTDDE IKQVEDMVNL QIKNKLSVKR SVMNLDDALA KGAMALFGEK 550 560 570 580 590 YEDIVSVYEI DGFSIEVCGG PHVKNTGELG TFKIQKEQAS SSGVRRIRAI LID

References

[1]

"The genome sequence of Borrelia hermsii and Borrelia turicatae: comparative analysis of two agents of endemic N. America relapsing fever." Porcella S.F., Raffel S.J., Schrumpf M.E., Montgomery B., Smith T., Schwan T.G. Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DAH.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000048 Genomic DNA. Translation: AAX16736.1.
RefSeq	YP_001883656.1. NC_010673.1.
3D structure databases
ProteinModelPortal	B2RZT0.
ModBase	Search...
Protein-protein interaction databases
STRING	B2RZT0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBORT00000006559; EBBORP00000005983; EBBORG00000006559.
GeneID	6277031.
GenomeReviews	Gene locus BH0220 in contig CP000048_GR.
KEGG	bhr:BH0220.
PATRIC	20567760. VBIBorHer61105_0219.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000006849.
HOGENOM	HBG354397.
OMA	RKCVDTG.
ProtClustDB	PRK01584.
Enzyme and pathway databases
BioCyc	BHER314723:BH0220-MONOMER.
Family and domain databases
HAMAP	MF_00036_B. Ala_tRNA_synth_B. Divergent sequence. [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. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view]
KO	K01872.
PANTHER	PTHR11777:SF6. PTHR11777:SF6. 1 hit.
Pfam	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_BORHD

Accession

Primary (citable) accession number: B2RZT0

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	July 1, 2008
Last modified:	January 25, 2012
This is version 25 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program