Reviewed, UniProtKB/Swiss-Prot P21894 (SYAC_BOMMO)

Names and origin

Protein names	Recommended name:     Alanyl-tRNA synthetase, cytoplasmic     EC=6.1.1.7 Alternative name(s):     Alanine--tRNA ligase       Short name=AlaRS
Organism	Bombyx mori (Silk moth)
Taxonomic identifier	7091 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Lepidoptera › Glossata › Ditrysia › Bombycoidea › Bombycidae › Bombycinae › Bombyx

Protein attributes

Sequence length	967 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala).
Subunit structure	Monomer.
Domain	The C-terminal 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 Potential.
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Ligand	ATP-binding Nucleotide-binding RNA-binding tRNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	alanyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW alanine-tRNA ligase activity Inferred from electronic annotation. Source: EC nucleic acid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 967	967	Alanyl-tRNA synthetase, cytoplasmic		PRO_0000075285
Regions
	Region	1 – 500	500	Catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	P21894-1 [UniParc]. Last modified May 1, 1991. Version 1. Checksum: 54CBF135153DA5D5	FASTA	967	108,178
	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

References

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

Cross-references

Sequence databases
EMBLGenBankDDBJ	M55993 mRNA. Translation: AAA27821.1.
PIR	SYMTAT. A38327.
RefSeq	NP_001037452.1.
UniGene	Bmo.450
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	693023.
Enzyme and pathway databases
BRENDA	6.1.1.7. 252.
Family and domain databases
InterPro	IPR002318. Ala-tRNA-synth_IIc. IPR018165. Ala-tRNA-synth_IIc_cons-reg. IPR018164. Ala-tRNA-synth_IIc_N. IPR003156. Pesterase_DHHA1. IPR012947. tRNA_SAD. [Graphical view]
Pfam	PF02272. DHHA1. 1 hit. PF01411. tRNA-synt_2c. 1 hit. PF07973. tRNA_SAD. 1 hit. [Graphical view]
PRINTS	PR00980. TRNASYNTHALA.
TIGRFAMs	TIGR00344. alaS. 1 hit.
PROSITE	PS50860. AA_TRNA_LIGASE_II_ALA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYAC_BOMMO

Accession

Primary (citable) accession number: P21894

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	May 1, 1991
Last modified:	November 3, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)