Q8DH56 (SYA_THEEB) 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:	tll2103

Organism

Thermosynechococcus elongatus (strain BP-1)

Taxonomic identifier

197221 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Thermosynechococcus

Protein attributes

Sequence length	882 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.
Sequence caution	The sequence BAC09655.1 differs from that shown. Reason: Erroneous initiation.

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 Reference 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 – 882	882	Alanine--tRNA ligase HAMAP MF_00036_B		PRO_0000075226
Sites
	Metal binding	567	1	Zinc Potential
	Metal binding	571	1	Zinc Potential
	Metal binding	669	1	Zinc Potential
	Metal binding	673	1	Zinc Potential

Sequences

	Sequence		Length	Mass (Da)
	Q8DH56 [UniParc]. Last modified August 22, 2003. Version 2. Checksum: A54A1ECCA6D3C611	FASTA	882	96,733
	10 20 30 40 50 60 MTALTGDQIR QKFLDFYAAK GHTILPSASL IPDDPTVLLT IAGMLPFKPI FLGQEAPKVP 70 80 90 100 110 120 RATTAQKCLR TNDIENVGRT ARHHTFFEML GNFSFGDYFK GEAIAWAWEL MTTVYGLPPE 130 140 150 160 170 180 RLLVSVFEND DEAYDIWHRQ VGLPKERIQR MGEESNFWTA GPTGPCGPCS EIYYDFYPEK 190 200 210 220 230 240 GLANVDLDDD GRFIELYNLV FMELNQDDQG HRTPLKAKNI DTGMGLERMA QVLQGVPNNY 250 260 270 280 290 300 ETDLIFPIIE AAAQRAGIQY QKANASTQTS LKVIGDHTRA VVHLIADGVT ASNVGRGYVL 310 320 330 340 350 360 RRLIRRIVRH SRLLGINGLV TPDLAQVAID LAANVYPNVR ERQAVILSEL QREEEQFLKT 370 380 390 400 410 420 LDRGEKLLAE MLSPLKKAKG KKRSQPQLAG RDAFVLFDTY GFPLELTQEI AAEQGIGVDV 430 440 450 460 470 480 AEFEACMAEQ RQRSQAAHET IDVTVQEGID SLGDQLHPTQ FRGYEELSLT TTVTAILVAG 490 500 510 520 530 540 HPATTATAGT EVQVILEATP FYAESGGQIG DRGYLASSDA LVHIHDVQKQ KELFVHYGKV 550 560 570 580 590 600 ERGSLKVGDR VSAQIDLSCR RRVQAHHTAT HLLQAALKKL IDENISQAGS LVAFDRLRFD 610 620 630 640 650 660 FNCPRPLTRE ELQQIEDQIN AWISESHTTH TYIMALSEAK AKGAIAMFGE KYGEQVRVLD 670 680 690 700 710 720 IPGVSMELCG GTHVHNTAEI GLFKIISESG VAAGIRRIEA IAGAAVRDYL QQRDSIVREL 730 740 750 760 770 780 CDRFKAKPEE ILDRISQLQA DLKAQQKALE HLKAELALAK TQALLEQAKP VGNSHVLIAS 790 800 810 820 830 840 LAGVDPQGLK TAAEWLLNKL GSGAVVLATQ PAADKVNLLV AASQDVVQRG VHAGQLVAAL 850 860 870 880 AQVCGGRGGG RPNFAQAGGS QPAKLAEALE LAHSRLKEIL ES

References

[1]

"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1." Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M. , Takeuchi C., Yamada M., Tabata S. DNA Res. 9:123-130(2002) [PubMed: 12240834] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: BP-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000039 Genomic DNA. Translation: BAC09655.1. Different initiation.
RefSeq	NP_682893.1. NC_004113.1.
3D structure databases
ProteinModelPortal	Q8DH56.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8DH56.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1011493.
GenomeReviews	Gene locus tll2103 in contig BA000039_GR.
KEGG	tel:tll2103.
NMPDR	fig|197221.1.peg.2102.
PATRIC	23929632. VBITheElo119873_2201.
Phylogenomic databases
eggNOG	COG0013.
HOGENOM	HBG354397.
OMA	GESKTDQ.
ProtClustDB	PRK00252.
Enzyme and pathway databases
BioCyc	TELO197221:TLL2103-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_THEEB

Accession

Primary (citable) accession number: Q8DH56

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 22, 2003
Last sequence update:	August 22, 2003
Last modified:	January 25, 2012
This is version 52 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program