Q2GKS1 (SYS_ANAPZ) 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:	APH_0427

Organism

Anaplasma phagocytophilum (strain HZ) [Complete proteome] [HAMAP]

Taxonomic identifier

212042 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma › phagocytophilum group

Protein attributes

Sequence length	428 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 – 428	428	Serine--tRNA ligase HAMAP MF_00176		PRO_1000019609
Regions
	Nucleotide binding	259 – 261	3	ATP By similarity
	Nucleotide binding	346 – 349	4	ATP By similarity
	Region	228 – 230	3	Serine binding By similarity
Sites
	Binding site	282	1	Serine By similarity
	Binding site	384	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2GKS1 [UniParc]. Last modified March 21, 2006. Version 1. Checksum: 5AC1A7A4F94FC1DF	FASTA	428	48,221
	10 20 30 40 50 60 MHDIEFIKNN PELFDKAMLS RGLESQAAKI IELDLQKRKL LTELYALREQ RNAITKEVTV 70 80 90 100 110 120 LKQSGADCSS HVETSKKLAH EISELEERIK RDTGLSYLLC SLPNIPDDAV PFGKSADDNV 130 140 150 160 170 180 EVRSYGQKRS FSFEIKPHYV LGEMLNLMDF RRAAFLSGSR FSILSGQLAA LERGLASFML 190 200 210 220 230 240 EMHTKEFGYT EVFHPSLVND LAMFNVGQLP KFTHDSFQTT DAMRLVPTSE VVLTNLVANT 250 260 270 280 290 300 NLHRNSLPLR FTAYSQCFRS EAGSAGQDTR GMIRQHQFSK VELVSITDAS QSNVELERML 310 320 330 340 350 360 SVAEEVLKRL ELPYRVVLLC TGDMGFSASI SYDIEVWMPA QNKYREISSC SNCKDFQARR 370 380 390 400 410 420 MGAKCFYLEK QNKRSSFVHT LNGSALALGR TIAAIMENYQ NSDGTITIPD ALRKFMSADY IRPGTALP

References

[1]

"Comparative genomics of emerging human ehrlichiosis agents." Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N. , Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R., Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H. PLoS Genet. 2:208-222(2006) [PubMed: 16482227] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HZ.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000235 Genomic DNA. Translation: ABD44439.1.
RefSeq	YP_505030.1. NC_007797.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q2GKS1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3931299.
GenomeReviews	Gene locus APH_0427 in contig CP000235_GR.
KEGG	aph:APH_0427.
NMPDR	fig|212042.5.peg.414.
PATRIC	20949470. VBIAnaPha602_0454.
TIGR	APH_0427.
Phylogenomic databases
eggNOG	COG0172.
HOGENOM	HBG629391.
OMA	PKFADDM.
PhylomeDB	Q2GKS1.
ProtClustDB	PRK05431.
Enzyme and pathway databases
BioCyc	APHA212042:APH_0427-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_ANAPZ

Accession

Primary (citable) accession number: Q2GKS1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	March 21, 2006
Last modified:	January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program