C1AIU0 (SYS_MYCBT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine--tRNA ligase
EC=6.1.1.11

Alternative name(s):
Seryl-tRNA synthetase
Short name=SerRS
Seryl-tRNA(Ser/Sec) synthetase

Gene names

Name:	serS
Ordered Locus Names:	JTY_3899

Organism

Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019) [Complete proteome] [HAMAP]

Taxonomic identifier

561275 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › Mycobacterium bovis › Mycobacterium bovis BCG

Protein attributes

Sequence length	419 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) By similarity. HAMAP-Rule MF_00176
Catalytic activity	ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). HAMAP-Rule MF_00176 ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). HAMAP-Rule MF_00176
Pathway	Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. HAMAP-Rule MF_00176
Subunit structure	Homodimer. The tRNA molecule binds across the dimer By similarity.
Subcellular location	Cytoplasm By similarity.
Domain	Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding By similarity. HAMAP-Rule MF_00176
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	selenocysteine biosynthetic process Inferred from electronic annotation. Source: HAMAP selenocysteinyl-tRNA(Sec) biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway seryl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP serine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 419	419	Serine--tRNA ligase HAMAP-Rule MF_00176		PRO_1000199494
Regions
	Nucleotide binding	257 – 259	3	ATP By similarity
	Nucleotide binding	344 – 347	4	ATP By similarity
	Region	226 – 228	3	Serine binding By similarity
Sites
	Binding site	273	1	ATP; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	280	1	Serine By similarity
	Binding site	379	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	C1AIU0 [UniParc]. Last modified May 26, 2009. Version 1. Checksum: BC01C9FC2FF34FB5	FASTA	419	45,324
	10 20 30 40 50 60 MIDLKLLREN PDAVRRSQLS RGEDPALVDA LLTADAARRA VISTADSLRA EQKAASKSVG 70 80 90 100 110 120 GASPEERPPL LRRAKELAEQ VKAAEADEVE AEAAFTAAHL AISNVIVDGV PAGGEDDYAV 130 140 150 160 170 180 LDVVGEPSYL ENPKDHLELG ESLGLIDMQR GAKVSGSRFY FLTGRGALLQ LGLLQLALKL 190 200 210 220 230 240 AVDNGFVPTI PPVLVRPEVM VGTGFLGAHA EEVYRVEGDG LYLVGTSEVP LAGYHSGEIL 250 260 270 280 290 300 DLSRGPLRYA GWSSCFRREA GSHGKDTRGI IRVHQFDKVE GFVYCTPADA EHEHERLLGW 310 320 330 340 350 360 QRQMLARIEV PYRVIDVAAG DLGSSAARKF DCEAWIPTQG AYRELTSTSN CTTFQARRLA 370 380 390 400 410 TRYRDASGKP QIAATLNGTL ATTRWLVAIL ENHQRPDGSV RVPDALVPFV GVEVLEPVA

References

[1]

"Whole genome sequence analysis of Mycobacterium bovis bacillus Calmette-Guerin (BCG) Tokyo 172: a comparative study of BCG vaccine substrains." Seki M., Honda I., Fujita I., Yano I., Yamamoto S., Koyama A. Vaccine 27:1710-1716(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: BCG / Tokyo 172 / ATCC 35737 / TMC 1019.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP010918 Genomic DNA. Translation: BAH28169.1.
RefSeq	YP_002646937.1. NC_012207.1.
3D structure databases
ProteinModelPortal	C1AIU0.
SMR	C1AIU0. Positions 1-417.
ModBase	Search...
Protein-protein interaction databases
STRING	561275.JTY_3899.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAH28169; BAH28169; JTY_3899.
GeneID	7564261.
KEGG	mbt:JTY_3899.
PATRIC	18027775. VBIMycBov85238_4241.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0172.
HOGENOM	HOG000035937.
KO	K01875.
OMA	GPIRYAG.
ProtClustDB	PRK05431.
Enzyme and pathway databases
BioCyc	MBOV561275:GHDN-3860-MONOMER.
UniPathway	UPA00906; UER00895.
Family and domain databases
Gene3D	1.10.287.40. 1 hit.
HAMAP	MF_00176. Ser_tRNA_synth_type1.
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-dom. IPR006195. aa-tRNA-synth_II. IPR002317. Ser-tRNA-ligase_type_1. IPR015866. Ser-tRNA-synth_1_N. IPR010978. tRNA-bd_arm. [Graphical view]
PANTHER	PTHR11778. PTHR11778. 1 hit.
Pfam	PF02403. Seryl_tRNA_N. 1 hit. PF00587. tRNA-synt_2b. 1 hit. [Graphical view]
PIRSF	PIRSF001529. Ser-tRNA-synth_IIa. 1 hit.
PRINTS	PR00981. TRNASYNTHSER.
SUPFAM	SSF46589. tRNA_binding_arm. 1 hit.
TIGRFAMs	TIGR00414. serS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYS_MYCBT

Accession

Primary (citable) accession number: C1AIU0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	May 26, 2009
Last modified:	May 1, 2013
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program