B1YDH4 (SYA_THENV) 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:	Tneu_0900

Organism

Thermoproteus neutrophilus (strain DSM 2338 / JCM 9278 / V24Sta) [Complete proteome] [HAMAP]

Taxonomic identifier

444157 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Thermoproteales › Thermoproteaceae › Thermoproteus

Protein attributes

Sequence length	892 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_A
Catalytic activity	ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP MF_00036_A
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_00036_A
Subcellular location	Cytoplasm By similarity HAMAP MF_00036_A.
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_A
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 – 892	892	Alanine--tRNA ligase HAMAP MF_00036_A		PRO_0000347893
Sites
	Metal binding	594	1	Zinc By similarity
	Metal binding	598	1	Zinc By similarity
	Metal binding	702	1	Zinc By similarity
	Metal binding	706	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	B1YDH4 [UniParc]. Last modified May 20, 2008. Version 1. Checksum: 18FE54A67E3CC487	FASTA	892	99,923
	10 20 30 40 50 60 MLSAKILQSS GFHRKQCPLC KSYFWTRRAD QIYCGDQPCV PYGFIGNPPA RASVESLADL 70 80 90 100 110 120 RERFLRFFER NSHVRIRRYP VVARWRDDVY LVGASIYDFQ PWVTSGAVPP PANPLAISQP 130 140 150 160 170 180 SIRLTDVDKV GRSGRHLTGF EMMAHHAFNY PDKYVYWIDE TTQYAYEFFT RELGIPPDEI 190 200 210 220 230 240 TFKESMWEGG GNAGECFEVL IRGLEVATLV FMHYEVKDGR YVELPLKIVD TGYGLERIYW 250 260 270 280 290 300 LLKGTPTVYD AVFGPYLAKA RQRLGVPEPP AEVMGKASVY FGQMDPEVIG LEKAYDIIAE 310 320 330 340 350 360 KIGVDPKWLR EVVRPQEALY VLADHSRTVS WMIADGVIPS NTGAGYLARL LIRRILKNLR 370 380 390 400 410 420 LAGVDAPLVE LFDMHLAELK REYPEVWEAR GLILELVDME ERRYREVLKS APAAVKKALE 430 440 450 460 470 480 EARRRGRAGL DADDLVALYD SQGIPPEVAA EVAKSLGTEV KVPDDFYAKL AARHVKREKK 490 500 510 520 530 540 PESSPVEMGK VADLPRTREL FYEDSYMRSF KARVLRVIDG RYVVLDQTAF YPEGGGQPAD 550 560 570 580 590 600 RGVLKFQGGE AKVVDVQRVG HVVVHVVEGQ PPPEGAEVVG EVDWERRYSL MKMHTGTHVL 610 620 630 640 650 660 IQSIRRVLGS HIWQAGAQKD IPSSRIDVTH HRLPTAEEVA RIEELANRAV QADLPVYAKI 670 680 690 700 710 720 MPRNEAEAKY GFVLYQGGVV PAREIRVLQI GPDEQPYDVQ ACGGTHLRST GEIGLIKIQK 730 740 750 760 770 780 VERIADGVVR FVFTTGMHAL AYVQELERRA AEAASIAGGS RDELVEAVRR LAQRAEEADR 790 800 810 820 830 840 RARRYAELYA AALAENLKAE QVGRHRLAVV ELDDEELARK IALAATSRDR DLVLVFVGGG 850 860 870 880 890 RATVYTGGVD VAPIVKALRE VGFRGGGSKT FAQGQYKGDI QTLKEAIRRA LA

References

[1]

"Complete sequence of Thermoproteus neutrophilus V24Sta." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. , Kyrpides N., Mikhailova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M., Saltikov C., House C.H., Richardson P. Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 2338 / JCM 9278 / V24Sta.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001014 Genomic DNA. Translation: ACB39837.1.
RefSeq	YP_001794283.1. NC_010525.1.
3D structure databases
ProteinModelPortal	B1YDH4.
ModBase	Search...
Protein-protein interaction databases
STRING	B1YDH4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6164315.
GenomeReviews	Gene locus Tneu_0900 in contig CP001014_GR.
KEGG	tne:Tneu_0900.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG392147.
OMA	MFTNSGM.
ProtClustDB	PRK13902.
Family and domain databases
HAMAP	MF_00036_A. Ala_tRNA_synth_A. [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. IPR022429. Ala-tRNA_synth_arc. 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	TIGR03683. A-tRNA_syn_arch. 1 hit. TIGR00344. AlaS. 1 hit.
PROSITE	PS50860. AA_TRNA_LIGASE_II_ALA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYA_THENV

Accession

Primary (citable) accession number: B1YDH4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	May 20, 2008
Last modified:	January 25, 2012
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program