Reviewed, UniProtKB/Swiss-Prot O28244 (SYS_ARCFU)

Names and origin

Protein names

Recommended name:
    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:	AF_2035

Organism

Archaeoglobus fulgidus [Complete proteome] [HAMAP]

Taxonomic identifier

2234 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus

Protein attributes

Sequence length	453 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). HAMAP MF_00176 ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). HAMAP MF_00176
Pathway	Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. HAMAP 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.
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 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 – 453	453	Seryl-tRNA synthetase HAMAP MF_00176		PRO_0000122170
Regions
	Nucleotide binding	280 – 282	3	ATP By similarity
	Nucleotide binding	367 – 370	4	ATP By similarity
	Region	249 – 251	3	Serine binding By similarity
Sites
	Binding site	296	1	ATP; via carbonyl oxygen and amide nitrogen By similarity
	Binding site	303	1	Serine By similarity
	Binding site	404	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	O28244-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 4BFCE9EB4F606D90	FASTA	453	52,455
	10 20 30 40 50 60 MWSILKAVRE NPEILYESQR RRGLSVDIVD RAIELDRKWR EELKRVNQLR KRRNELARAV 70 80 90 100 110 120 KEAKGEERAK VIEEAKAVSE EVKRAEEELK RLEAELEEVL LSIPNIIHES VPVGKDDSEN 130 140 150 160 170 180 VPIKYWGKAK VYFEDVDAFV EMTQGMAEYE VTDVKPIGHA DAVEIFGWAD LERAAKVAGA 190 200 210 220 230 240 RFYYLLNDLV WLDFALTMYA LDFLRKEDFT IVSPPYMMRR EAYSGVTAFS DFEEVIYKVE 250 260 270 280 290 300 DEDLYLIATS EHPIAAMHMR EVLEERELPL LYAGVSPCFR KEAGAHGKDT KGIFRVHQFN 310 320 330 340 350 360 KVEQFVFCLP EQSWEWHEKL IENVEKLWQG LGIPYRIVNI CTGDLGIVAA KKYDLEAWMP 370 380 390 400 410 420 AQAKYREMVS CSNCTDWQSY RLDIRFAEER GKPSKGFVHT LNSTAIATTR AITAIIENFQ 430 440 450 LEDGRVEIPR VLRKYLEPIE SAPKDFIMPA KSQ

References

[1]

"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus." Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G. , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Nature 390:364-370(1997) [PubMed: 9389475] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE000782 Genomic DNA. Translation: AAB89219.1.
PIR	B69504.
RefSeq	NP_070859.1.
3D structure databases
HSSP	HSSP built from PDB template 1SES based on UniProtKB P34945.
ModBase	Search...
Genome annotation databases
GeneID	1485261.
GenomeReviews	Gene locus AF_2035 in contig AE000782_GR.
KEGG	afu:AF2035.
NMPDR	fig|224325.1.peg.2020.
TIGR	AF_2035.
Phylogenomic databases
HOGENOM	O28244.
OMA	YAGVSPC.
Enzyme and pathway databases
BioCyc	AFUL224325:AF_2035-MON.
BRENDA	6.1.1.11. 7576.
Family and domain databases
HAMAP	MF_00176. [Tree]
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-reg. IPR006195. aa-tRNA-synth_II_cons-reg. IPR002317. Ser-tRNA-synth_IIa. IPR018156. Ser-tRNA-synth_IIa_C. IPR015866. Ser-tRNA-synth_IIa_N. [Graphical view]
Gene3D	G3DSA:1.10.287.40. Ser-tRNA-synth_IIa_N. 1 hit.
PANTHER	PTHR11778. tRNA-synt_ser. 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.
TIGRFAMs	TIGR00414. serS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYS_ARCFU

Accession

Primary (citable) accession number: O28244

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	November 3, 2009
This is version 61 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)