B0JI84 (SYA_MICAN) Reviewed, UniProtKB/Swiss-Prot

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:	MAE_25600

Organism

Microcystis aeruginosa (strain NIES-843) [Complete proteome] [HAMAP]

Taxonomic identifier

449447 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Microcystis

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 MF_00036_B
Catalytic activity	ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP MF_00036_B
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_00036_B
Subcellular location	Cytoplasm By similarity HAMAP MF_00036_B.
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 MF_00036_B
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: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW alanine-tRNA ligase activity Inferred from electronic annotation. Source: EC 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 – 874	874	Alanine--tRNA ligase HAMAP MF_00036_B		PRO_0000347677
Sites
	Metal binding	559	1	Zinc Potential
	Metal binding	563	1	Zinc Potential
	Metal binding	661	1	Zinc Potential
	Metal binding	665	1	Zinc Potential

Sequences

	Sequence		Length	Mass (Da)
	B0JI84 [UniParc]. Last modified March 18, 2008. Version 1. Checksum: C6D94330DFC5EAF8	FASTA	874	96,037
	10 20 30 40 50 60 MSNHLSGSEI RQRFLDFFAA RNHKILPSAS LVPEDPTVLL TIAGMLPFKP IFLGQKTPEF 70 80 90 100 110 120 PRATTSQKCI RTNDIENVGR TARHHTFFEM LGNFSFGDYF KEQAIAWAWE LSTEVFNLPP 130 140 150 160 170 180 ERLVVSVFKE DEEAFAIWRD KIGIPAHRIQ KMGEEDNFWV SGPTGPCGPC SEIYYDFHPE 190 200 210 220 230 240 LGDKTIDLED DSRFIEFYNL VFMQYNRDAD GNLTPLANKN IDTGMGLERM AQILQKVANN 250 260 270 280 290 300 YETDLIFPIV AEAARLAAID YQKADEKTKV SLKVIGDHVR SVVHMIADGI SASNTDRGYV 310 320 330 340 350 360 LRRLIRRVVR HGRLIGIEGQ FITKVAEVAI ALSESVYGNV RERETVIKAE LEREEARFLE 370 380 390 400 410 420 TLERGEKLLE SILEKEKSQI SGVDAFTLYD TYGFPLELTQ EIAEEQGLSV DTAGFEQEMK 430 440 450 460 470 480 KQQQRSKAAH ETIDLTVQGS LDKLAEHIHP TEFLGYTDLQ ATATVTAVLV AGKTVESAAA 490 500 510 520 530 540 GTEVQVVLDR TPFYAESGGQ IGDKGYLTGD NLLIRIEDVQ KESGIFIHFG RIERGIVTTG 550 560 570 580 590 600 DTINAQIDRS CRRRAQANHT ATHLLQSALK KLVDGGISQA GSLVSFDRLR FDFNCPRPLT 610 620 630 640 650 660 SSELQQVEEQ INTWIAEAHD TQIAVMGLEE AKQKGAIAMF GEKYGSEVRV IDIPSVSMEL 670 680 690 700 710 720 CGGTHVKNTA EIGLFKIISE TGIAAGIRRI EAVAGPAVLA YLNERDQVVR ALCDRFKVKP 730 740 750 760 770 780 LEIPDRITAL QSELKGTQKQ LEAVKQELAL NKSDALLSQA ESIGEFKLLV ASLGDIDANA 790 800 810 820 830 840 LMAAAERLQQ KLGEGAVILA STPAADKVSL VAAFSPRVIK DKGLQAGKFI GAIAKICAGG 850 860 870 GGGRPNLAQA GGRDASKLSE ALAKAKSQLT SSLQ

References

[1]

"Complete genomic structure of the bloom-forming toxic cyanobacterium Microcystis aeruginosa NIES-843." Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M., Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A., Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M. , Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M. DNA Res. 14:247-256(2007) [PubMed: 18192279] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NIES-843.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP009552 Genomic DNA. Translation: BAG02382.1.
RefSeq	YP_001657574.1. NC_010296.1.
3D structure databases
ProteinModelPortal	B0JI84.
ModBase	Search...
Protein-protein interaction databases
STRING	B0JI84.
Proteomic databases
PRIDE	B0JI84.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5863372.
GenomeReviews	Gene locus MAE_25600 in contig AP009552_GR.
KEGG	mar:MAE_25600.
PATRIC	22630029. VBIMicAer59304_2341.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG354397.
OMA	GESKTDQ.
PhylomeDB	B0JI84.
ProtClustDB	PRK00252.
Enzyme and pathway databases
BioCyc	MAER449447:MAE_25600-MONOMER.
Family and domain databases
HAMAP	MF_00036_B. Ala_tRNA_synth_B. [Tree]
InterPro	IPR002318. Ala-tRNA-synth_IIc. IPR018162. Ala-tRNA-synth_IIc_anticod-bd. IPR018165. Ala-tRNA-synth_IIc_core. IPR018164. Ala-tRNA-synth_IIc_N. IPR023033. Ala_tRNA_synth_euk/bac. IPR003156. Pesterase_DHHA1. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view]
KO	K01872.
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_MICAN

Accession

Primary (citable) accession number: B0JI84

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	March 18, 2008
Last modified:	January 25, 2012
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program