O27718 (SYA_METTH) 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:	MTH_1683

Organism

Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum) [Reference proteome] [HAMAP]

Taxonomic identifier

187420 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter › Methanobacterium thermoformicicum

Protein attributes

Sequence length	898 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-Rule MF_00036
Catalytic activity	ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP-Rule MF_00036
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subcellular location	Cytoplasm By similarity.
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-Rule MF_00036
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 Reference proteome
Gene Ontology (GO)
Biological_process	alanyl-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 alanine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP 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 – 898	898	Alanine--tRNA ligase HAMAP-Rule MF_00036		PRO_0000075268
Sites
	Metal binding	589	1	Zinc By similarity
	Metal binding	593	1	Zinc By similarity
	Metal binding	693	1	Zinc By similarity
	Metal binding	697	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	O27718 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 46FDEE31106CC69D	FASTA	898	100,963
	10 20 30 40 50 60 MITMSHQLEK LGYRKYECRS CGNTFWSMKE RATCGDAPCD EYGFIGNPAT DRSYDLYEIQ 70 80 90 100 110 120 DKFMEFFAER GHEPIRRYPV LAKRWRDDVF LVGASIYNFQ PWVTSGLVKP PANPLVVAQP 130 140 150 160 170 180 SIRLNDVDNV GRTGRHLTCF TMGGHHAFNS EDNTVYWEEE TIKYCHDFLT HIGIDPSEIT 190 200 210 220 230 240 FIESWWQGGG NEGPCYEVCV RGVELATLVF IQYRTLPDGG REEIPLKIVD TGYGLERFAW 250 260 270 280 290 300 ISQGTPTAYD ACLGPVIEKL VELTGVKIDE EILAENAQVA GMMDIETYAD LRELRKRVAD 310 320 330 340 350 360 KLGISVEELE RAAAPMESVY AIADHTRCLA FMLADGVIPS NVKEGYLARL IIRRTLRLMK 370 380 390 400 410 420 DLGMKESLKD IMNIQVEFLE GHYPEIRSHH EHILNIIDLE EHRYARTVKR GRRIVEKTIK 430 440 450 460 470 480 YLKRDGKAEM PLEILIKLYD SHGIPPETIG EIAEESGFQV KIPDNFYTLV AERNETETEM 490 500 510 520 530 540 PEEDVHLDYP ATELLFYDEP DDLEFQAEVI GIHENGLILD RTLFYPEGGG QPSDTGYITA 550 560 570 580 590 600 EGCRLRIKHA EKIGAVVVHR TDDEICIEPG TTIRGFIDSD RRLQLTRNHT ATHLIVSAAR 610 620 630 640 650 660 KVLGDHIWQA GAQKGVKSSR LDLSHYRRIT LEELQEIERL ANEYVMMNVP LKVRWMDRDL 670 680 690 700 710 720 AERKYGFILY QGGVVPGSRI RVVEIPGVDV QACAGTHVHR TGDIGLIRIN RTERIQDGVE 730 740 750 760 770 780 RIEFSAGSAA IEIMQKTGDI LRESSDIFKV TPSQLPGTCE RFFTEWKALR NEVSRLKEKV 790 800 810 820 830 840 ASLKILEMKD RAERINDLTV IIDTVDADMD EMKNMALELS ATVDAVVLAN PEGKIVGAAS 850 860 870 880 890 EDAVKAGLRI NEVISQAAAV LGGGGGGRPH LAQGAGPATD KVDEALEEAR AALSTVRN

References

[1]

"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics." Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N. J. Bacteriol. 179:7135-7155(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000666 Genomic DNA. Translation: AAB86155.1.
PIR	A69092.
RefSeq	NP_276794.1. NC_000916.1.
3D structure databases
ProteinModelPortal	O27718.
ModBase	Search...
Protein-protein interaction databases
STRING	187420.MTH1683.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAB86155; AAB86155; MTH_1683.
GeneID	1470768.
KEGG	mth:MTH1683.
Phylogenomic databases
eggNOG	COG0013.
KO	K01872.
OMA	ISQPSIR.
ProtClustDB	PRK13902.
Enzyme and pathway databases
BioCyc	MTHE187420:GJNM-1685-MONOMER.
Family and domain databases
HAMAP	MF_00036_A. Ala_tRNA_synth_A.
InterPro	IPR002318. Ala-tRNA-lgiase_IIc. IPR018162. Ala-tRNA-ligase_IIc_anticod-bd. IPR018165. Ala-tRNA-synth_IIc_core. IPR018164. Ala-tRNA-synth_IIc_N. IPR022429. Ala-tRNA_lgiase_arc. IPR003156. Pesterase_DHHA1. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view]
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	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_METTH

Accession

Primary (citable) accession number: O27718

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program