Q9YAG3 (SYS_AERPE) 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:	APE_1976.1

Organism

Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) [Complete proteome] [HAMAP]

Taxonomic identifier

272557 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Aeropyrum

Protein attributes

Sequence length	460 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 MF_00176
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 HAMAP MF_00176.
Domain	Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding By similarity. HAMAP 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	seryl-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 serine-tRNA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 460	460	Serine--tRNA ligase HAMAP MF_00176		PRO_0000122169
Regions
	Nucleotide binding	286 – 288	3	ATP By similarity
	Nucleotide binding	373 – 376	4	ATP By similarity
	Region	255 – 257	3	Serine binding By similarity
Sites
	Binding site	302	1	ATP; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	309	1	Serine By similarity
	Binding site	409	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9YAG3 [UniParc]. Last modified July 10, 2007. Version 2. Checksum: A7F93E9BECA06173	FASTA	460	53,178
	10 20 30 40 50 60 MAGWSILELL RSNPEALKEH VRKRLMDPAI VDRAYRLDVE WRRLLTMVNE VRRRHNEITR 70 80 90 100 110 120 MIAKAGSREE RERLIAEAKR LLREREDLEE KLKKVERERE EALLGLPNIV APDVPVGDES 130 140 150 160 170 180 ATRPIEFWGK PKVWKGHVDA FREQTEAYGF KVDHEVIEWR PRGHADMMEE VLKLGDTLRA 190 200 210 220 230 240 ARVAGSRFYY LFEDLVFLDL ALLMYAIDFM TSKGYVLVLP PYMLRYNVMS RVIDLETFKD 250 260 270 280 290 300 AIYEIAGEDL YLIATAEHPL AALYYNSEIY DEDLPLKLVG VSPCFRKEAG AGNRDLKGIF 310 320 330 340 350 360 RVHQFHKVEQ FVYSLPEESS KLHEELISNA KEIFKGLEIP FRVVNIASGD LGACAVKKYD 370 380 390 400 410 420 LEAWMPAQGK YREMVSASNC TDWQAYRLGI RLVRRKGMER GYVHTLNATA VASTRTITAI 430 440 450 460 LENFQDEEGV VAIPRALRRY LEVFKRAPTD AIHPRRRPPA

References

[1]

"Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1." Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S. , Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H. DNA Res. 6:83-101(1999) [PubMed: 10382966] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000002 Genomic DNA. Translation: BAA80986.2.
PIR	B72500.
RefSeq	NP_148300.2. NC_000854.2.
3D structure databases
ProteinModelPortal	Q9YAG3.
SMR	Q9YAG3. Positions 7-443.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1446383.
GenomeReviews	Gene locus APE_1976.1 in contig BA000002_GR.
KEGG	ape:APE_1976.1.
NMPDR	fig|272557.1.peg.1408.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG629391.
ProtClustDB	PRK05431.
Enzyme and pathway databases
BioCyc	APER272557:APE1976-MONOMER.
Family and domain databases
HAMAP	MF_00176. Ser_tRNA_synth_type1. [Tree]
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-dom. IPR006195. aa-tRNA-synth_II. IPR002317. Ser-tRNA-synth_IIa. IPR015866. Ser-tRNA-synth_IIa_N. IPR010978. tRNA-bd_arm. [Graphical view]
Gene3D	G3DSA:1.10.287.40. Ser-tRNA-synth_IIa_N. 1 hit.
KO	K01875.
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.
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_AERPE

Accession

Primary (citable) accession number: Q9YAG3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	July 10, 2007
Last modified:	January 25, 2012
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program