Reviewed, UniProtKB/Swiss-Prot O27194 (SYS2_METTH)

Names and origin

Protein names

Recommended name:
    Type-2 seryl-tRNA synthetase
    EC=6.1.1.11
Alternative name(s):
    Seryl-tRNA(Ser/Sec) synthetase
    Serine--tRNA ligase
      Short name=SerRS

Gene names

Name:	serS
Ordered Locus Names:	MTH_1122

Organism

Methanobacterium thermoautotrophicum [Complete proteome] [HAMAP]

Taxonomic identifier

187420 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter

Protein attributes

Sequence length	513 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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). Ref.1
Catalytic activity	ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). HAMAP MF_01278 ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). HAMAP MF_01278
Cofactor	Binds 1 Zn2+ ion per subunit. This ion is coordinated with 2 cysteines, 1 glutamate and a water molecule that dissociates from the zinc ion to allow the coordination of the amino group of the serine substrate, which is essential for catalysis By similarity.
Pathway	Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. HAMAP MF_01278
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Domain	Consists of two distinct domains, a catalytic core and a N-terminal extension that is presumably involved in tRNA binding By similarity.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. Type-2 seryl-tRNA synthetase subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	selenocysteine biosynthetic process Inferred from electronic annotation. Source: HAMAP 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 zinc ion 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 – 513	513	Type-2 seryl-tRNA synthetase HAMAP MF_01278		PRO_0000122177
Regions
	Nucleotide binding	344 – 346	3	ATP By similarity
	Nucleotide binding	355 – 356	2	ATP By similarity
	Region	361 – 363	3	Serine binding By similarity
Sites
	Metal binding	314	1	Zinc; catalytic By similarity
	Metal binding	363	1	Zinc; catalytic By similarity
	Metal binding	467	1	Zinc; catalytic By similarity
	Binding site	312	1	Serine; via carbonyl oxygen By similarity
	Binding site	344	1	Serine By similarity
	Binding site	474	1	ATP By similarity
Experimental info
	Sequence conflict	150	1	F → V in AAB87409. Ref.2
	Sequence conflict	187	1	D → E in AAB87409. Ref.2
	Sequence conflict	230	1	F → L in AAB87409. Ref.2
	Sequence conflict	242	1	E → R in AAB87409. Ref.2
	Sequence conflict	358	1	E → D in AAB87409. Ref.2
	Sequence conflict	501	1	V → VV in AAB87409. Ref.2
	Sequence conflict	503 – 504	2	NP → KG in AAB87409. Ref.2
	Sequence conflict	513	1	D → T in AAB87409. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O27194-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 213B65D10773AA2A	FASTA	513	58,808
	10 20 30 40 50 60 MKFKLKGIIK LSKEVPGIED DLEKFFTEAE SDILRRGVPE GQEHEAAHIK SWRLEGDTLH 70 80 90 100 110 120 IEMESGRRVR AHDGLLRLKK PLGQLLGPKY RVGVRGISVT DYTMEMKAPG VSGIPSLAEL 130 140 150 160 170 180 PFVEDAAITD GTIMVRFQPL EESDLRKHVF DRVVKHARTL VESSDDLTVQ VTRATPGEII 190 200 210 220 230 240 ARSRSRDFFF EGDPTEEAMR LGWVKKFPGR GQWFYGPKIT ALHRALEEFF IERIVKPLGF 250 260 270 280 290 300 VECLFPKLIP LDIMNKMRYL EGLPEGMYYC SAPSRDPETF EEFKNELIIN REVPMDLLKR 310 320 330 340 350 360 GIKDPGYVIA PAQCEPFYQF LSHEVVSAED LPVKFFDRSG WTYRWEAGGS KGLDRVHEFQ 370 380 390 400 410 420 RVELVWLAEP GETEEIRDRT VELSHDAADE LELEWYTEVG DDPFYLEGRK VEERGIEFPD 430 440 450 460 470 480 VPKYEMRLSL PGREKGVAVV SANVHGTHFI EGFSIREARN LNIWTGCTGI GLSRWIYGFL 490 500 510 AQKGFETGNW PDFIGERVEG VENPRIITWP RQD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence divergence of seryl-tRNA synthetases in archaea." Kim H.-S., Vothknecht U.C., Hedderich R., Celic I., Soell D. J. Bacteriol. 180:6446-6449(1998) [PubMed: 9851985] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-13, FUNCTION. Strain: Delta H.
[2]	"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics." Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N. J. Bacteriol. 179:7135-7155(1997) [PubMed: 9371463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Delta H.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF009823 Genomic DNA. Translation: AAB87409.1. AE000666 Genomic DNA. Translation: AAB85611.1.
PIR	D69016.
RefSeq	NP_276250.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	O27194.
Genome annotation databases
GeneID	1471530.
GenomeReviews	Gene locus MTH_1122 in contig AE000666_GR.
KEGG	mth:MTH1122.
NMPDR	fig|187420.1.peg.1105.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	O27194.
OMA	PAQCEPF.
Enzyme and pathway databases
BioCyc	MTHE187420:MTH1122-MON.
BRENDA	6.1.1.11. 270.
Family and domain databases
HAMAP	MF_01278. [Tree]
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-reg. IPR004503. Ser-tRNA-synth_IIa_arc. IPR018156. Ser-tRNA-synth_IIa_C. [Graphical view]
PANTHER	PTHR11778. tRNA-synt_ser. 1 hit.
Pfam	PF00587. tRNA-synt_2b. 1 hit. [Graphical view]
TIGRFAMs	TIGR00415. serS_MJ. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYS2_METTH

Accession

Primary (citable) accession number: O27194
Secondary accession number(s): O30521

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	November 3, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)