Alanine--tRNA ligase - Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

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Q57984 (SYA_METJA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 85. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	MJ0564

Organism

Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]

Taxonomic identifier

243232 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus ›

Protein attributes

Sequence length	892 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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) By similarity. Also functions in trans to edit the amino acid moiety from incorrectly charged Ser-tRNA(Ala), and maybe also from Gly-tRNA(Ala). Ref.2
Catalytic activity	ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP-Rule MF_00036_A
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_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 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 aminoacyl-tRNA editing activity Inferred from direct assay Ref.2. Source: UniProtKB 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-Rule MF_00036_A

PRO_0000075264

Sites

Metal binding

590

Zinc By similarity

Metal binding

594

Zinc By similarity

Metal binding

699

Zinc By similarity

Metal binding

703

Zinc By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q57984 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 409A542E72C8188B
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FASTA

892

102,851

        10         20         30         40         50         60 
MKHNYKVKLF DELGFVRKKC KKCGQWFWTL DEERETCGDA PCDIYSFIGK PITKKPYTYK 

        70         80         90        100        110        120 
EMVKEFINFF KEHGHEPIKR APVTARRWRD DILLTIASIA VFQPWITKGI VKPKANPLVI 

       130        140        150        160        170        180 
AQPCIRLNDI DNVGRTGRHL TCFTMGGHHA FNREDDFKYW QDETVELCFN FFKKLGIDEK 

       190        200        210        220        230        240 
SITFIESWWE GGGNAGPCYE VITHGVELAT LVFMQYEKVG DNYKEIPLKI VDTGYGIERF 

       250        260        270        280        290        300 
VWASTGEPTI YDAIFKNIVN KLKEDAGVKD IDKEILAKIT EVAGLMDVKD VGDLRKLREE 

       310        320        330        340        350        360 
VANKVNIPVE ELDKLISPYE DIYAIVDHTR ALAFMLGDGI VPSNVKDGYL VRMLIRKTLR 

       370        380        390        400        410        420 
HMDRLNLSTP ITEIVAMQLN ELKDLYPELL DMEDYIMEIL EIETNKYRQT IERGKGIVER 

       430        440        450        460        470        480 
LLKSKKEIDL ENLIELYDSH GLPPEIVKDV AKSLGKDVKI PDNFYTIVAE RHENKKEVKE 

       490        500        510        520        530        540 
KIKLPEVNVD KTELLFYEYP KMKEFEAKIL RIVDDYVILD RTAFYPEGGG QKADTGYIIK 

       550        560        570        580        590        600 
GDKKFRVVDV QKENNIVYHK IENLNDELKE GDIVKGVIDW KRRLSLMRNH TATHIINAAA 

       610        620        630        640        650        660 
QKVLGRHVWQ AGSDVDVDKA RLDITHYKRI SREELKDIER VANEIVLNNY NIKSIFMDRN 

       670        680        690        700        710        720 
EAEEKFGFRI YQGGVVPGNV LRIVIIEDEN GNIVDVQACG GTHCQNTGEV GFIKIIKTER 

       730        740        750        760        770        780 
VQDGVERLIY SSGLSALKAV QEMEDILEES AEILRCPTEE LPKVIKRFFE EWKEQRKKIE 

       790        800        810        820        830        840 
ELEKKIGELK KFELINKFET IGNYKVLVEK VEANPKEMLN IADNLATENA IVVLLNDKGN 

       850        860        870        880        890 
ILCKRGENVD IKMNELIRYI AKGGGREHLA QGKYEGDVEE IKKKVIEFIK NK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. Venter J.C. Science 273:1058-1073(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[2]	"Trans-editing of mischarged tRNAs." Ahel I., Korencic D., Ibba M., Soll D. Proc. Natl. Acad. Sci. U.S.A. 100:15422-15427(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN EDITING ACTIVITY ON MISCHARGED TRNA(ALA).

Cross-references

Sequence databases
EMBL GenBank DDBJ	L77117 Genomic DNA. Translation: AAB98556.1.
PIR	D64370.
RefSeq	NP_247543.1. NC_000909.1.
3D structure databases
ProteinModelPortal	Q57984.
ModBase	Search...
Protein-protein interaction databases
STRING	243232.MJ0564.
Protocols and materials databases
DNASU	1451429.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAB98556; AAB98556; MJ_0564.
GeneID	1451429.
KEGG	mja:MJ_0564.
Phylogenomic databases
eggNOG	COG0013.
KO	K01872.
OMA	ISQPSIR.
ProtClustDB	PRK13902.
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. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view]
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_METJA

Accession

Primary (citable) accession number: Q57984

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents