Reviewed, UniProtKB/Swiss-Prot Q9JJL8 (SYSM_MOUSE)

Names and origin

Protein names

Recommended name:
    Seryl-tRNA synthetase, mitochondrial
    EC=6.1.1.11
Alternative name(s):
    Seryl-tRNA(Ser/Sec) synthetase
    Serine--tRNA ligase
    SerRSmt

Gene names

Name:	Sars2
Synonyms:	Sarsm

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	518 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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) By similarity.
Catalytic activity	ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec).
Pathway	Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
Subunit structure	Homodimer. The tRNA molecule binds across the dimer By similarity.
Subcellular location	Mitochondrion matrix 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	Mitochondrion
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	seryl-tRNA aminoacylation Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB serine-tRNA ligase activity Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 34	34	Mitochondrion By similarity
	Chain	35 – 518	484	Seryl-tRNA synthetase, mitochondrial		PRO_0000035823
Regions
	Nucleotide binding	330 – 332	3	ATP By similarity
	Nucleotide binding	418 – 421	4	ATP By similarity
	Region	299 – 301	3	Serine binding By similarity
Sites
	Binding site	345	1	ATP; via carbonyl oxygen and amide nitrogen By similarity
	Binding site	352	1	Serine By similarity
	Binding site	453	1	Serine By similarity
Amino acid modifications
	Modified residue	52	1	Phosphotyrosine By similarity
	Modified residue	110	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	237	1	V → L in BAB26981. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9JJL8-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 31DF15E444BB8061	FASTA	518	58,302
	10 20 30 40 50 60 MAASMARLWW PFLARQGLRS RGRCVCSQNP RRSFATEKRV RNLLYEHARE GYSELPYLDM 70 80 90 100 110 120 ESVCACPEKA ARSLELRKGE LRPADLPAII STWQELRQLR EQIRSLEAEK EAVAEAVRAL 130 140 150 160 170 180 LANQDSDQVQ KDPQYQGLRA RGREIRKQLT PLYPQETQLE EQLYQQALRL PNQTHPDTPV 190 200 210 220 230 240 GDESQARVVR VVGEKPAFSF QPRGHLEIGE KLDIIRQKRL SHVSGHRSYY LRGAGAVLQH 250 260 270 280 290 300 GLVNFTLSKL VSRGFTPMTV PDLLRGAVFE GCGMTPNANP SQIYNIDPSR FEDLNLAGTA 310 320 330 340 350 360 EVGLAGYFMD HSVAFRDLPV RMVCASTCYR AETDTGKEPW GLYRVHHFTK VEMFGVTGPG 370 380 390 400 410 420 LEQSSQLLDE FLSLQVEILT ELGLHFRVLD MPTQELGLPA YRKFDIEAWM PGRGRYGEVT 430 440 450 460 470 480 SASNCTDFQS RRLYIMFETE TGELQFAHTV NATACAVPRV LIALLESNQQ KDGSVLVPAA 490 500 510 LQPYLGTDRI TAPTHVPLQY IGPNQPQKPR LPGQSATR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization and tRNA recognition of mammalian mitochondrial seryl-tRNA synthetase." Yokogawa T., Shimada N., Takeuchi N., Benkowski L., Suzuki T., Omori A., Ueda T., Nishikawa K., Spremulli L.L., Watanabe K. J. Biol. Chem. 275:19913-19920(2000) [PubMed: 10764807] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Embryonic stem cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB029949 mRNA. Translation: BAA99558.1. AK010491 mRNA. Translation: BAB26981.1.
IPI	IPI00109354.
RefSeq	NP_076126.2.
UniGene	Mm.333725
3D structure databases
SMR	Q9JJL8. Positions 41-507.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9JJL8.
PTM databases
PhosphoSite	Q9JJL8.
Proteomic databases
PRIDE	Q9JJL8.
Genome annotation databases
Ensembl	ENSMUST00000094632; ENSMUSP00000092216; ENSMUSG00000070699; Mus musculus. [Genome view]
GeneID	71984.
KEGG	mmu:71984.
UCSC	uc009fzq.1. mouse.
Organism-specific databases
CTD	71984.
MGI	MGI:1919234. Sars2.
Phylogenomic databases
HOGENOM	HBG629391.
HOVERGEN	Q9JJL8.
InParanoid	Q9JJL8.
PhylomeDB	Q9JJL8.
Enzyme and pathway databases
BRENDA	6.1.1.11. 244.
Gene expression databases
ArrayExpress	Q9JJL8.
Bgee	Q9JJL8.
CleanEx	MM_SARS2.
Genevestigator	Q9JJL8.
GermOnline	ENSMUSG00000070699. Mus musculus.
Family and domain databases
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-dom. IPR006195. aa-tRNA-synth_II_cons-dom. IPR002317. Ser-tRNA-synth_IIa. IPR018156. Ser-tRNA-synth_IIa_C. IPR015866. Ser-tRNA-synth_IIa_N. IPR010978. tRNA_bd_arm. [Graphical view]
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...
Other Resources
NextBio	335130.
SOURCE	Search...

Entry information

Entry name

SYSM_MOUSE

Accession

Primary (citable) accession number: Q9JJL8
Secondary accession number(s): Q9CWP1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2002
Last sequence update:	October 1, 2000
Last modified:	February 9, 2010
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)