Q5P9F6 (SYT_ANAMM) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Threonine--tRNA ligase
EC=6.1.1.3

Alternative name(s):
Threonyl-tRNA synthetase
Short name=ThrRS

Gene names

Name:	thrS
Ordered Locus Names:	AM1273

Organism

Anaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]

Taxonomic identifier

234826 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma

Protein attributes

Sequence length	636 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr). HAMAP MF_00184
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_00184
Subunit structure	Homodimer By similarity. HAMAP MF_00184
Subcellular location	Cytoplasm HAMAP MF_00184.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

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
Gene Ontology (GO)
Biological process	threonyl-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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW threonine-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 – 636	636	Threonine--tRNA ligase HAMAP MF_00184		PRO_0000100932
Regions
	Region	244 – 535	292	Catalytic HAMAP MF_00184
Sites
	Metal binding	335	1	Zinc; catalytic By similarity
	Metal binding	386	1	Zinc; catalytic By similarity
	Metal binding	512	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5P9F6 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 324C52B0D42DC794	FASTA	636	72,773
	10 20 30 40 50 60 MINITTSFPN KTAAAFHKHV TGSEVASAMF PEIAESIVAL FVDGNLQDLA TPISKDGSVD 70 80 90 100 110 120 PVTIESNTGM DIIRHDAAHI MARAVREIFP DTKLAIGPTI ENGFYYDFDL SHSLSEKDFE 130 140 150 160 170 180 AIERKMADII AKDERFVREV WPRERAIKFF EDLGEHYKLE ILSKVPLGEE ITVYKHGEFV 190 200 210 220 230 240 DLCRGPHAPS ARYVKAFKLT KISGAYWLGD QKNKMLQRVY GTAWHSSEAL ASYIHNMQEA 250 260 270 280 290 300 EKRDHRKIAK DLGWFHIQNE ALGQVFWHDK GWVIYRIIEE YIRCKLKKHG YHEVKTPIML 310 320 330 340 350 360 DRKLWEKSGH WEKFKENMFV VEDDKKELAI KPMNCPCHVQ IFKSKIRSYK ELPIRMAEFG 370 380 390 400 410 420 MCHRNEPSGS LYGLMRVRGF TQDDAHIFCT HEQVRDEVLR FYELLMEVYK DFGFDSVTVK 430 440 450 460 470 480 LSDRPENRIG SDEIWDRSEQ SLMEPMNALG VQYTINKGEG AFYGPKLEFT LKDSIGREWQ 490 500 510 520 530 540 CGTVQLDFVL PDRLGAYYIG EDGKKHIPVI IHRAILGTIE RFIGILIEHY AGNIPAWLAP 550 560 570 580 590 600 VQLEILTVSG EVAEYARDLA EMASQENVRV ELNAAEENIS HKIRKAIFNK VPIVWVVGKS 610 620 630 EAGDRGVSVR RYGSGETCRM AAGKALKTLL TCVSMR

References

[1]

"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins." Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr. Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: St. Maries.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000030 Genomic DNA. Translation: AAV87074.1.
RefSeq	YP_154329.1. NC_004842.2.
3D structure databases
ProteinModelPortal	Q5P9F6.
SMR	Q5P9F6. Positions 243-629.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5P9F6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3171409.
GenomeReviews	Gene locus AM1273 in contig CP000030_GR.
KEGG	ama:AM1273.
PATRIC	20948385. VBIAnaMar46146_1102.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0441.
HOGENOM	HBG352811.
OMA	MIIRNIL.
PhylomeDB	Q5P9F6.
ProtClustDB	PRK00413.
Enzyme and pathway databases
BioCyc	AMAR234826:AM1273-MONOMER.
Family and domain databases
HAMAP	MF_00184. Thr_tRNA_synth. [Tree]
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-dom. IPR006195. aa-tRNA-synth_II. IPR004154. Anticodon-bd. IPR012675. Beta-grasp_ferredoxin-type. IPR012676. TGS-like. IPR002320. Thr-tRNA-synth_IIa. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view]
Gene3D	G3DSA:3.40.50.800. Anticodon_bd. 1 hit. G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
KO	K01868.
Pfam	PF03129. HGTP_anticodon. 1 hit. PF00587. tRNA-synt_2b. 1 hit. PF07973. tRNA_SAD. 1 hit. [Graphical view]
PRINTS	PR01047. TRNASYNTHTHR.
SMART	SM00863. tRNA_SAD. 1 hit. [Graphical view]
SUPFAM	SSF52954. Anticodon_bd. 1 hit. SSF81271. TGS-like. 1 hit. SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit.
TIGRFAMs	TIGR00418. ThrS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYT_ANAMM

Accession

Primary (citable) accession number: Q5P9F6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	January 4, 2005
Last modified:	January 25, 2012
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program