Q5F9U4 (SYT_NEIG1) 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:	NGO0295

Organism

Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)

Taxonomic identifier

242231 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length	637 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 Reference 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 – 637	637	Threonine--tRNA ligase HAMAP MF_00184		PRO_0000101014
Regions
	Region	242 – 533	292	Catalytic HAMAP MF_00184
Sites
	Metal binding	333	1	Zinc; catalytic By similarity
	Metal binding	384	1	Zinc; catalytic By similarity
	Metal binding	510	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5F9U4 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 0AD6BADF8ECF3046	FASTA	637	72,726
	10 20 30 40 50 60 MLNITLPDCS VRQYESPVTV AQIAASIGAG LAKAAVAGKV NGKLVDACDP IVEDSAVQII 70 80 90 100 110 120 TPKDQEGIEI IRHSCAHLVG HAVKQLYPNA KMVIGPVIEE GFYYDIATEK PFTPEDVAAI 130 140 150 160 170 180 EARMKELIAQ DYDVVKIMTP RAEAIKIFQE RGEEYKLRLI DDMPEVEAMG IYHHQEYVDM 190 200 210 220 230 240 CRGPHVPNTR FLKNFKLTKL AGAYWRGDSN NEMLQRIYGT AWATKDELKD YIQRIEEAEK 250 260 270 280 290 300 RDHRKLGKQL DLFHLQDEAP GMVFWHPKGW ALWQTIEQHM RKELNAAGYK EVKTPQIMDK 310 320 330 340 350 360 TFWEKSGHWD NYKDNMFVTS SEKREYAVKP MNCPGHVQIF NNGLRSYRDL PMRLAEFGSC 370 380 390 400 410 420 HRNEPSGALH GLMRVRGFVQ DDAHIFCTED QIVSEARAFN ELLVRIYKQF GFHDVSVRLS 430 440 450 460 470 480 LRPEKRAGSD DVWDKAEQGL REALTACGVE WGELPGEGAF YGPKIEYHVK DALGRSWQCG 490 500 510 520 530 540 TLQLDFVLPE RLDAEYVTEN NDRARPVMLH RAILGSLERF IGILIENHAG SFPLWLAPVQ 550 560 570 580 590 600 MVIMNITENQ ADYCREVAAK LQAAGFRAEL DLRNEKIGYK IRDNSQYRFP YQIVIGDKEK 610 620 630 QENKVAVRRK AEDLGSLDLD DFIAQLQQEI TDALVNH

References

[1]

"The complete genome sequence of Neisseria gonorrhoeae." Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H. , Qi S., Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W. Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700825 / FA 1090.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE004969 Genomic DNA. Translation: AAW89043.1.
RefSeq	YP_207455.1. NC_002946.2.
3D structure databases
ProteinModelPortal	Q5F9U4.
SMR	Q5F9U4. Positions 4-630.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5F9U4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBNEIT00000003818; EBNEIP00000003659; EBNEIG00000003818.
GeneID	3281668.
GenomeReviews	Gene locus NGO0295 in contig AE004969_GR.
KEGG	ngo:NGO0295.
NMPDR	fig|242231.4.peg.486.
PATRIC	20333573. VBINeiGon24812_0366.
Phylogenomic databases
eggNOG	COG0441.
GeneTree	EBGT00050000021120.
HOGENOM	HBG352811.
OMA	VGSDALW.
PhylomeDB	Q5F9U4.
ProtClustDB	PRK00413.
Enzyme and pathway databases
BioCyc	NGON242231:NGO0295-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. IPR004095. TGS. 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. PF02824. TGS. 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_NEIG1

Accession

Primary (citable) accession number: Q5F9U4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	March 15, 2005
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