Reviewed, UniProtKB/Swiss-Prot Q0VML5 (SYC_ALCBS)

Names and origin

Protein names

Recommended name:
    Cysteinyl-tRNA synthetase
    EC=6.1.1.16
Alternative name(s):
    Cysteine--tRNA ligase
      Short name=CysRS

Gene names

Name:	cysS
Ordered Locus Names:	ABO_2135

Organism

Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]

Taxonomic identifier

393595 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Alcanivoracaceae › Alcanivorax

Protein attributes

Sequence length	460 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys). HAMAP MF_00041
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm. HAMAP MF_00041
Sequence similarities	Belongs to the class-I 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	cysteinyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP cysteine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 460	460	Cysteinyl-tRNA synthetase HAMAP MF_00041		PRO_1000006560
Regions
	Motif	31 – 41	11	"HIGH" region HAMAP MF_00041
	Motif	266 – 270	5	"KMSKS" region HAMAP MF_00041
Sites
	Metal binding	29	1	Zinc By similarity
	Metal binding	209	1	Zinc By similarity
	Metal binding	234	1	Zinc By similarity
	Metal binding	238	1	Zinc By similarity
	Binding site	269	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0VML5-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 156608ACA20EEFC3	FASTA	460	51,328
	10 20 30 40 50 60 MTLRLQNTLT GKKDDFIPLD PNRITLYVCG PTVYNFVHIG NARPVVVFDV LYRLLQRLYP 70 80 90 100 110 120 NVVYARNITD IDDKIIKAAA DNGEAISTLT ERFTQAFADD MASLNAKTPS IIPKATDHIP 130 140 150 160 170 180 EMIQMIAILV EKGHAYEADG QVLFAVESMP DYGKLSGRKL EDMLAGARVE VADYKRHPGD 190 200 210 220 230 240 FILWKPSTDE QPGWDSPWGR GRPGWHIECS AMIHKHLGDV IDIHGGGQDL IFPHHENEIA 250 260 270 280 290 300 QGCCAHGTDY VRYWLHNGYI NIDGEKMSKS LGNFRLVRDL LTQYHGETLR FALLSSHYRS 310 320 330 340 350 360 PLNFSADVLD NAEKGLDTLY YALLGRGETV APEAGYQLPD NHPVLDALKD DLNTSEAVSA 370 380 390 400 410 420 LHAIAGELNK AELDDKPKLK AELLAAADLL GLLTVEPTAW FQNKNVSEDG LSNDAIDALV 430 440 450 460 EERTQAKKDK NFARADEIRQ QLTKAGIQLE DTREGTRWSR

References

[1]

"Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium Alcanivorax borkumensis." Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B., McHardy A.C., Meyer F. , Nechitaylo T., Puehler A., Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N. Nat. Biotechnol. 24:997-1004(2006) [PubMed: 16878126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM286690 Genomic DNA. Translation: CAL17583.1.
RefSeq	YP_693855.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q0VML5.
Genome annotation databases
GeneID	4212582.
GenomeReviews	Gene locus ABO_2135 in contig AM286690_GR.
KEGG	abo:ABO_2135.
NMPDR	fig|393595.12.peg.2133.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0VML5.
OMA	NFVTIHD.
Enzyme and pathway databases
BioCyc	ABOR393595:ABO_2135-MON.
Family and domain databases
HAMAP	MF_00041. [Tree]
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR015804. Cys-tRNA-synt_Ia_C. IPR015273. Cys-tRNA-synt_Ia_DALR. IPR015803. Cys-tRNA-synt_Ia_N. IPR002308. Cys-tRNA-synth_1a. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHER	PTHR10890. Cys_tRNA-synt_1a. 1 hit.
Pfam	PF09190. DALR_2. 1 hit. PF01406. tRNA-synt_1e. 1 hit. [Graphical view]
PRINTS	PR00983. TRNASYNTHCYS.
TIGRFAMs	TIGR00435. cysS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYC_ALCBS

Accession

Primary (citable) accession number: Q0VML5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 5, 2006
Last modified:	November 3, 2009
This is version 28 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)