[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 456-490. TISSUE=Posterior silk gland; PubMed=1701172 [NCBI, ExPASy, EBI, Israel, Japan] Chang P.K., Dignam J.D.; "Primary structure of alanyl-tRNA synthetase and the regulation of its mRNA levels in Bombyx mori."; J. Biol. Chem. 265:20898-20906(1990).
[2]	PROTEIN SEQUENCE OF 456-488. TISSUE=Posterior silk gland; PubMed=2040280 [NCBI, ExPASy, EBI, Israel, Japan] Dignam J.D., Dignam S.S., Brumley L.L.; "Alanyl-tRNA synthetase from Escherichia coli, Bombyx mori and Ratus ratus. Existence of common structural features."; Eur. J. Biochem. 198:201-210(1991).

Comments

CATALYTIC ACTIVITY: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala).
SUBUNIT: Monomer.
PTM: The N-terminus is blocked.
SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family [view classification].

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

M55993; AAA27821.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A38327; SYMTAT.

NP_001037452.1; -.

3D structure databases

ModBase

P21894.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0004813;	Molecular function: alanine-tRNA ligase activity (inferred from electronic annotation from InterPro).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0003676;	Molecular function: nucleic acid binding (inferred from electronic annotation from InterPro).
GO:0006419;	Biological process: alanyl-tRNA aminoacylation (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR002318; Ala-tRNA-synth_IIc.
IPR003156; Pesterase_DHHA1.
IPR012947; tRNA_SAD.
Graphical view of domain structure.

Pfam

PF02272; DHHA1; 1.
PF01411; tRNA-synt_2c; 1.
PF07973; tRNA_SAD; 1.
Pfam graphical view of domain structure.

PRINTS

PR00980; TRNASYNTHALA.

TIGRFAMs

TIGR00344; alaS; 1.

PROSITE

PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P21894.

Genome annotation databases

GeneID

693023; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Aminoacyl-tRNA synthetase; ATP-binding; Direct protein sequencing; Ligase; Nucleotide-binding; Protein biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 967`	`967`	`Alanyl-tRNA synthetase, cytoplasmic.`	`PRO_0000075285`
`REGION`	`1 500`	`500`	`Catalytic (By similarity).`

Sequence information

Length: 967 AA [This is the length of the unprocessed precursor]

Molecular weight: 108178 Da [This is the MW of the unprocessed precursor]

CRC64: 54CBF135153DA5D5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDTSMTGNEI RKTFIDFFIK KGHKYVHSSS TIPLDDPTLL FANAGMNQFK PIFLGSVDPN 

        70         80         90        100        110        120 
SDMAQYIRVV NTQKCIRAGG KHNDLDDVGK DVYHHTFFEM MGNWSFGDYF KKEICAWAWE 

       130        140        150        160        170        180 
LLTDVFKLSR ERLYVTYFEG DPSSGLEPDL ECRNIWLNLG VPEAHILPGS MKDNFWEMGE 

       190        200        210        220        230        240 
TGPCGPCSEL HYDRIGDREA AHLVNMDDPD VLEIWNLVFI QFNRETDGSL KLLPTKHIDC 

       250        260        270        280        290        300 
GLGLERLVSV IQNKRANYDT DFFMPIFKAI ENATGVRPYS GKVGVDDVDG IDMAYRVLAD 

       310        320        330        340        350        360 
HARTLTIALS DGGCPDNTGR GYVLRRILRR AVRYASEKLN AKPGFFGSLV YTVVELLGDV 

       370        380        390        400        410        420 
FPEIKKDPDS IVHVINEEEV QFLKTLLRGR NLLYRTIEKL NNSKTLPGDV AWRLYDTYGF 

       430        440        450        460        470        480 
PIDLTQLMCE EKGLNVDMEG YEKSRKESQL VSQGKAAGQE DLIALDVHAI SHLQDTGIPA 

       490        500        510        520        530        540 
TDDSPKYNYL PSSTDKDALY TFAPCTAKIV ALRKNKEFVS EISSGQECGV ILDRTSFYAE 

       550        560        570        580        590        600 
QGGQIFDEGY MVKIDDETVE FTVKNVQVKG GYVLHAGKVE GILKVGDTLS LHIDTERRRL 

       610        620        630        640        650        660 
VMNNHTGTHV LNNVLRKVLG NDSDQRGSLV MPDRLRFDFT NKGPMTIKQI KDTENEIKEI 

       670        680        690        700        710        720 
IAKNKTVYAN YTSLSEAKKI NGLRAMFDEH YPDPVRVVSV GVPVEDLIKN PDAPTGFETS 

       730        740        750        760        770        780 
VEFCGGSHLH RTSHIGEYVI VSEEGIAKGI RRIVAVTGPE AIKAINKLSV LENEVNNVAN 

       790        800        810        820        830        840 
FIKEQNESIS HKEVSKKIVD LTNEISQAQI SYWKKDELRN MLKNLKKQLD DKERAEKAII 

       850        860        870        880        890        900 
ITQVTEKAKE LCLERKESKY IVSELKAFGN TKALDGALKQ VKQFCPNSAA MFFSVDKDAD 

       910        920        930        940        950        960 
KIYCLAAVPK SDVEKGLLAS EWVQSVVDII GGKGGGKAES AQASGNNPNS LNEAIQIANE 


YAKSKLN

P21894 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools