A9KLZ5 (SYA2_CLOPH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alanine--tRNA ligase 2
EC=6.1.1.7

Alternative name(s):
Alanyl-tRNA synthetase 2
Short name=AlaRS 2

Gene names

Name:	alaS2
Ordered Locus Names:	Cphy_0956

Organism

Clostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) [Complete proteome] [HAMAP]

Taxonomic identifier

357809 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	591 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 Potential. 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 – 591	591	Alanine--tRNA ligase 2 HAMAP MF_00036_B		PRO_0000347572
Sites
	Metal binding	453	1	Zinc Potential
	Metal binding	457	1	Zinc Potential
	Metal binding	555	1	Zinc Potential
	Metal binding	559	1	Zinc Potential

Sequences

	Sequence		Length	Mass (Da)
	A9KLZ5 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: 8668C8B00DD6A5DB	FASTA	591	67,558
	10 20 30 40 50 60 MTANELRKMY VDYFKERGHQ EIASASLLPE NDPTVLFTTA GMHPLVPYLL GENHPKGTRL 70 80 90 100 110 120 VSVQKCVRTG DIDEVGDDTH LTFFEMLGNW SLGEYFKEES ISISYDFLTT CLNIPKEKLA 130 140 150 160 170 180 VTVFEGDELV PRDEEVSQTW KSKGLQDNQI FYYGREENWW GPAGQTGPCG TDTEIFYDMG 190 200 210 220 230 240 KPSCGVNCGP ACDCGKYVEI WNNVFMQYHK KPDGSYEEMK QKNVDTGMGF ERVLTILNGY 250 260 270 280 290 300 TNVYETELFL PVKNRLDEII EANEAKLSEK SKRIICEHIR AVTFLLGDPK MIVPSNSEQG 310 320 330 340 350 360 YILRRLIRRM IRHLKQVSIE NNVLCKLSKV IVEQYGSIYV ELRENELFIM EQLEKEYDLF 370 380 390 400 410 420 SKTLDRGLKN AKLYFDQVGE EKILNGELSF KLYDTFGFPI EFTIELASEM EITVDVEAYN 430 440 450 460 470 480 QKFAEHQKKS RQGAEVKFKG GLSDHGEQTT RLHTATHLLN GALRTVLGTD VFQRGSNITE 490 500 510 520 530 540 ERLRFDFSFH RKLTKEELEE VERIVNEAIR NQIDVLCEEM TVKEAKELGA VGIFEDKYGE 550 560 570 580 590 VVKVYMIPGY SKEICGGPHV KNTSELKSFR TVKEEASSAG VRRIKAVIGS N

References

[1]

"Complete genome sequence of Clostridium phytofermentans ISDg." Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L., LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C. , Han C., Kuske C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.A., Richardson P. Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700394 / DSM 18823 / ISDg.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000885 Genomic DNA. Translation: ABX41338.1.
RefSeq	YP_001558077.1. NC_010001.1.
3D structure databases
ProteinModelPortal	A9KLZ5.
ModBase	Search...
Protein-protein interaction databases
STRING	A9KLZ5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5743897.
GenomeReviews	Gene locus Cphy_0956 in contig CP000885_GR.
KEGG	cpy:Cphy_0956.
PATRIC	19501506. VBICloPhy16213_0993.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG354397.
OMA	RKCVDTG.
ProtClustDB	PRK01584.
Enzyme and pathway databases
BioCyc	CPHY357809:CPHY_0956-MONOMER.
Family and domain databases
HAMAP	MF_00036_B. Ala_tRNA_synth_B. Divergent sequence. [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. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view]
KO	K01872.
PANTHER	PTHR11777:SF6. PTHR11777:SF6. 1 hit.
Pfam	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.
PROSITE	PS50860. AA_TRNA_LIGASE_II_ALA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYA2_CLOPH

Accession

Primary (citable) accession number: A9KLZ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	February 5, 2008
Last modified:	January 25, 2012
This is version 28 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program