Q7NYC6 (SYT_CHRVO) 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:	CV_1348

Organism

Chromobacterium violaceum [Complete proteome] [HAMAP]

Taxonomic identifier

536 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Chromobacterium

Protein attributes

Sequence length	633 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 – 633	633	Threonine--tRNA ligase HAMAP MF_00184		PRO_0000100964
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)
	Q7NYC6 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: 6C993E7DA9E73B5D	FASTA	633	72,082
	10 20 30 40 50 60 MPDIRLPDGS VRSFDKPVTV HEVAASIGAG LARAALAGRV DGQLVDTSYL IDRNADLAIV 70 80 90 100 110 120 TDKDADGLSV IRHSTAHLLA YAVKELFPEA QVTIGPEIEN GFYYDFAYKR PFTPEDLAAI 130 140 150 160 170 180 EKKMAELAKK DIPVERYELP RDEAIAYFKS IGEAYKAEII ESIPQGEVLS LYREGEFTDL 190 200 210 220 230 240 CRGPHVPSTG KLKVFKLMKV AGAYWRGDSK NEMLQRVYGT AWAKKEDLDA YLYMLEEAEK 250 260 270 280 290 300 RDHRKLGVQL DLFHLQDEAP GMVFWHPKGW QLWQNVEQYM RAKLNHEGYK EVRTPMMMDA 310 320 330 340 350 360 NLWERSGHAA NYRENMFITE SEKRDYAVKP MNCPGHVQIF NSGLRSYRDL PLRYAEFGSC 370 380 390 400 410 420 HRNEPSGALH GIMRVRGFVQ DDGHIFCTED QINQEAKDFH RLVMEVYDRF GFDKVAIKLA 430 440 450 460 470 480 LRPEKRIGEE STWDKAEEGM REALRACGVE WEELPGEGAF YGPKIEYHIK DALGRSWQCG 490 500 510 520 530 540 TLQLDFMLPE RLDAEYVADD NSRKRPVMLH RAALGSLERF LGILIENHAG AFPLWLAPVQ 550 560 570 580 590 600 MVVMNITEAQ AEYAAEIAKE LEKQGFRVEL DLRNEKIGYK IREHSLQKLP YQIIVGDKEK 610 620 630 ADGLVAVRAR GEDLGQLTLE AFAARLKAEM PEA

References

[1]

"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability." Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G. Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed: 14500782] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016825 Genomic DNA. Translation: AAQ59023.1.
RefSeq	NP_901018.1. NC_005085.1.
3D structure databases
ProteinModelPortal	Q7NYC6.
SMR	Q7NYC6. Positions 241-630.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2548723.
GenomeReviews	Gene locus CV_1348 in contig AE016825_GR.
KEGG	cvi:CV_1348.
NMPDR	fig|243365.1.peg.1348.
PATRIC	21437498. VBIChrVio67196_1322.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG352811.
OMA	VGSDALW.
PhylomeDB	Q7NYC6.
ProtClustDB	PRK00413.
Enzyme and pathway databases
BioCyc	CVIO243365:CV_1348-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_CHRVO

Accession

Primary (citable) accession number: Q7NYC6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	December 15, 2003
Last modified:	January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program