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UniProtKB/Swiss-Prot entry B2HWK7


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SYA_ACIBC
Primary accession number B2HWK7
Secondary accession numbers None
Integrated into Swiss-Prot on September 2, 2008
Sequence was last modified on September 2, 2008 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 6)
Name and origin of the protein
Protein name Alanyl-tRNA synthetase
Synonyms EC 6.1.1.7
Alanine--tRNA ligase
AlaRS
Gene name
Name: alaS
OrderedLocusNames: ACICU_01154
From
Acinetobacter baumannii (strain ACICU) [TaxID: 405416] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Moraxellaceae; Acinetobacter.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/AAC.01643-07; PubMed=18411315 [NCBI, ExPASy, EBI, Israel, Japan]
Iacono M., Villa L., Fortini D., Bordoni R., Imperi F., Bonnal R.J., Sicheritz-Ponten T., De Bellis G., Visca P., Cassone A., Carattoli A.;
"Whole-genome pyrosequencing of an epidemic multidrug-resistant Acinetobacter baumannii strain belonging to the European clone II group.";
Antimicrob. Agents Chemother. 52:2616-2625(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CP000863; ACC56466.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001845813.1; -.
3D structure databases
ModBase B2HWK7.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004813; Molecular function: alanine-tRNA ligase activity (inferred from electronic annotation from HAMAP).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0003676; Molecular function: nucleic acid binding (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006419; Biological process: alanyl-tRNA aminoacylation (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00036; -; 1.
PBIL [Tree]
PROSITE PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 6235611; -.
GenomeReviews CP000863_GR; ACICU_01154.
KEGG abc:ACICU_01154; -.
CMR B2HWK7; ACICU_01154.
Other
ProtoNet B2HWK7.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   878  878     Alanyl-tRNA synthetase. PRO_0000347473
ZN_FING   177   190  14     C2H2-type. 
Sequence information
Length: 878 AA [This is the length of the unprocessed precursor] Molecular weight: 96528 Da [This is the MW of the unprocessed precursor] CRC64: 48DC937CBAF0C6F6 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTSAEIREAF LRYFETQGHT RVASSSLVPA NDPTLLFTNA GMNQFKDCFL GLEKRDYVRA 

        70         80         90        100        110        120 
TTSQKCVRAG GKHNDLDNVG YTARHHTFFE MLGNFSFGDY FKRDALKFAW EFLTSEQWLA 

       130        140        150        160        170        180 
LPKDKLYVTV YHTDDEAYDI WNKEIGLAPE RIIRIGDNKG EKYASDNFWA MGDTGPCGPC 

       190        200        210        220        230        240 
SEIFFDHGEH IWGGLPGSPE EDGDRFIEIW NNVFMQFNRT ADGVLHPLPA PSVDTGMGLE 

       250        260        270        280        290        300 
RISAVLQHVN SNYDIDLFQH LLKAAANIIG IEDEGQPSLR VVADHARSCC FLIADGVNPS 

       310        320        330        340        350        360 
NEGRGYVLRR IIRRAVRHGN KLGATGTFFY KMLQPLIEVM GQAYPELEAR REVIEATLIR 

       370        380        390        400        410        420 
EEEQFAKTLE QGLKLLEGEL AQLKDKTIPG ATVFKLYDTY GFPTDLTADI ARERGFIIDE 

       430        440        450        460        470        480 
AGFEVEMAAQ RQRARDAGKF AVDYNNIVKV EGETQFDGYT NTTGQGQIVA IYKDGVQVDE 

       490        500        510        520        530        540 
VSEGDEALIV LNQTPFYAES GGQIGDTGIF KNETGIFEVQ DTKKSGGAFV HQGIVTVGNL 

       550        560        570        580        590        600 
KTSQNVEAIV KADIREATAR NHSATHLLHA ALRQILGSHV QQKGSLVASD ILRFDFANDQ 

       610        620        630        640        650        660 
PVSFEQLQQV ERLVNAEIIA NTAVTTELLD IETAKAKGAM MLFGEKYGDE VRVLSMGSVI 

       670        680        690        700        710        720 
DEKNFSIELC GGIHVKRTGD IGLFKITSEG GVAAGVRRIE AVTGTKALEV VQKADHDIQH 

       730        740        750        760        770        780 
INSLLKAQKD QTVERVQANV ELVSALQKQI EQLNQKLANF QAADLIDQVQ TIAGRQTLIT 

       790        800        810        820        830        840 
TVQGVDAKAL RNLHDSVKSK LENAVIVLAG VEGDKVSLLA SVASQYTANL KAGDIIKHLA 

       850        860        870 
TELGGKGGGK PDLAQGGAPL NEKFGQVMAA LPAWLEQK 

B2HWK7 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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