Alanine--tRNA ligase - Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)

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Q9JTG4 (SYA_NEIMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 75. History...

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

Documents (2) |

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:	NMA1788

Organism

Neisseria meningitidis serogroup A / serotype 4A (strain Z2491) [Complete proteome] [HAMAP]

Taxonomic identifier

122587 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria ›

Protein attributes

Sequence length	874 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. HAMAP-Rule MF_00036
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00036.
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
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 tRNA binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 874

874

Alanine--tRNA ligase HAMAP-Rule MF_00036

PRO_0000075160

Sites

Metal binding

562

Zinc Potential

Metal binding

566

Zinc Potential

Metal binding

664

Zinc Potential

Metal binding

668

Zinc Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q9JTG4 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 17EE6A14668211EA
Show »

FASTA

874

96,032

        10         20         30         40         50         60 
MKTSELRQKF LKFFETKGHT VVRSSSLVPH DDPTLLFTNA GMNQFKDVFL GFDKRPYSRA 

        70         80         90        100        110        120 
TTAQKCVRAG GKHNDLENVG YTARHHTFFE MMGNFSFGDY FKRDAIHFAW EFLTSPEWLN 

       130        140        150        160        170        180 
IPKDKLLATV YAEDDEAYNI WLNEIGMPSE RIVRIGDNKG AKYVSDNFWQ MGDTGPCGPC 

       190        200        210        220        230        240 
SEIFYDHGEE IWGGIPGSPE EDGDRWIEIW NCVFMQFNRD EQGNMNPLPK PSVDTGMGLE 

       250        260        270        280        290        300 
RMAAVMQHVH SNYEIDLFQD LLKAVARETG AAFSMDEPSL KVIADHIRSC SFLIADGVLP 

       310        320        330        340        350        360 
SNEGRGYVLR RIIRRAVRHG YKLGQSKPFF HKLVADLVKE MGGAYPELKE KQAQIEEALK 

       370        380        390        400        410        420 
NEESRFAQTL ETGMALLENA LAKGGKTLDG EIIFKLYDTY GFPYDLTADI CRERNIELDE 

       430        440        450        460        470        480 
AGFEREMEAQ RARARAAQSF KANAQLPYDG QDTEFKGYSE RQTESKVLAL YKDGEQVNEL 

       490        500        510        520        530        540 
NEGDSGAVVI DFTPFYAESG GQVGDVGYIF SSENRFEVRD TQKIKAAVFG QFGVQTSGRL 

       550        560        570        580        590        600 
KVGDSVTAKV DDEIRNANMR NHSATHLMHK ALRDVLGGHV EQKGSLVTAE STRFDISHPQ 

       610        620        630        640        650        660 
AVTAEEIAEV ERRVNEAVLA NVAVNAAIMS MEDAQKTGAM MLFGEKYGEE VRVLQMGGFS 

       670        680        690        700        710        720 
TELCGGTHVS RTGDIGLFKI ISEGGIAAGV RRIEAITGLN ALKWAQEQER LVKDIIAETK 

       730        740        750        760        770        780 
AQTEKDVLAK IQAGAAHAKA LEKELARAKA ELAVHAGAKL LDDAKDLGAA KLVAAQIEAD 

       790        800        810        820        830        840 
AAALREIVTD LTGKSDNAVI LLAAVNDGKV SLCAGVSKPL TGKVKAGDLV KFAAEQVGGK 

       850        860        870 
GGGRPDLAQA GGTDAGKLPE MLVSVESWLC QKLS

« Hide

References

[1]

"Complete DNA sequence of a serogroup A strain of Neisseria meningitidis Z2491."
Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M., Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M., Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K., Leather S.

Barrell B.G.
Nature 404:502-506(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Z2491.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL157959 Genomic DNA. Translation: CAM08912.1.
PIR	C81804.
RefSeq	YP_002343076.1. NC_003116.1.
3D structure databases
ProteinModelPortal	Q9JTG4.
SMR	Q9JTG4. Positions 1-460.
ModBase	Search...
Protein-protein interaction databases
STRING	122587.NMA1788.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAM08912; CAM08912; NMA1788.
GeneID	907637.
KEGG	nma:NMA1788.
PATRIC	20364887. VBINeiMen132687_2139.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0013.
HOGENOM	HOG000156964.
KO	K01872.
OMA	ISQPSIR.
ProtClustDB	PRK00252.
Enzyme and pathway databases
BioCyc	NMEN122587:GI3Q-1636-MONOMER.
Family and domain databases
HAMAP	MF_00036_B. Ala_tRNA_synth_B.
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. IPR023033. Ala_tRNA_ligase_euk/bac. 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	TIGR00344. alaS. 1 hit.
PROSITE	PS50860. AA_TRNA_LIGASE_II_ALA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYA_NEIMA

Accession

Primary (citable) accession number: Q9JTG4
Secondary accession number(s): A1IT00

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2002
Last sequence update:	October 1, 2000
Last modified:	May 29, 2013
This is version 75 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

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

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents