Q7US70 (SYC_RHOBA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cysteine--tRNA ligase
EC=6.1.1.16

Alternative name(s):
Cysteinyl-tRNA synthetase
Short name=CysRS

Gene names

Name:	cysS
Ordered Locus Names:	RB4675

Organism

Rhodopirellula baltica (strain SH1)

Taxonomic identifier

243090 [NCBI]

Taxonomic lineage

Bacteria › Planctomycetes › Planctomycetacia › Planctomycetales › Planctomycetaceae › Rhodopirellula

Protein attributes

Sequence length	537 AA.
Sequence status	Complete.
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. HAMAP MF_00041
Subunit structure	Monomer By similarity. HAMAP MF_00041
Subcellular location	Cytoplasm HAMAP MF_00041.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.
Caution	The Arg residue that is thought to bind ATP in this protein is missing; it probably binds ATP elsewhere.
Sequence caution	The sequence CAD73927.1 differs from that shown. Reason: Erroneous initiation.

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	cysteinyl-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 cysteine-tRNA ligase activity Inferred from electronic annotation. Source: EC metal 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 – 537	537	Cysteine--tRNA ligase HAMAP MF_00041		PRO_0000159466
Regions
	Motif	48 – 58	11	"HIGH" region HAMAP MF_00041
Sites
	Metal binding	46	1	Zinc By similarity
	Metal binding	225	1	Zinc By similarity
	Metal binding	250	1	Zinc By similarity
	Metal binding	254	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7US70 [UniParc]. Last modified October 11, 2005. Version 2. Checksum: 8487F55CF6BFEA8C	FASTA	537	58,486
	10 20 30 40 50 60 MTAADPTASV ASPSSAQPAI RVYNTLSKTK EPFLPLRAPR VGMYLCGPTV YAESHIGHMV 70 80 90 100 110 120 GPVIFDTIKR YLTYSGYEVT WVVNITDVDD KLIGKSKERG IPMSQIAVEM TADYLANLRE 130 140 150 160 170 180 LGVNQIDHLP RATDHMPQII AFIGSLESKG FAYAIDGDVF FDVTKDPGYG QLSNRSVEDQ 190 200 210 220 230 240 QGEGGGAAAK KRNPGDFALW KSARPGEPFW DSPWGEGRPG WHIECSAMSH EILGETFDIH 250 260 270 280 290 300 GGGLDLMFPH HENERAQSTC CHGAPMVKYW MHNGLMRAGE KGKVGGKSDR ENAAAEAASV 310 320 330 340 350 360 EEQASGKISR SKGAGGLADL IRSQTGERIR FFLLRTQYRS TIVYNEETLA EAGTSLEAFY 370 380 390 400 410 420 RYFDRFAEIT GDSFYDLSAA TRRADGGFDP AGDALLTEIH AIREKFLAAM DDDFNTGAAI 430 440 450 460 470 480 SVLFDALRTL NRHIDANQLA AGADAKSPAV ESLVKATSVI AELSRVLGLF AKPPATSGGD 490 500 510 520 530 EADAELLDSV VHLLINLRKE ARERKDYATG DAIRDRLADL GVALLDKKEG TSWERKS

References

[1]

"Complete genome sequence of the marine planctomycete Pirellula sp. strain 1." Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W., Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R., Reinhardt R. Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003) [PubMed: 12835416] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SH1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX294140 Genomic DNA. Translation: CAD73927.1. Different initiation.
RefSeq	NP_866241.1. NC_005027.1.
3D structure databases
ProteinModelPortal	Q7US70.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1792243.
GenomeReviews	Gene locus RB4675 in contig BX119912_GR.
KEGG	rba:RB4675.
NMPDR	fig|243090.1.peg.2581.
PATRIC	23245829. VBIRhoBal59814_2196.
Phylogenomic databases
HOGENOM	HBG327651.
PhylomeDB	Q7US70.
ProtClustDB	CLSK2758886.
Enzyme and pathway databases
BioCyc	PSP117:RB4675-MONOMER.
Family and domain databases
HAMAP	MF_00041. Cys_tRNA_synth. [Tree]
InterPro	IPR015803. Cys-tRNA-synt. IPR015273. Cys-tRNA-synt_Ia_DALR. IPR024909. Cys-tRNA/MSH_ligase. IPR014729. Rossmann-like_a/b/a_fold. IPR009080. tRNAsynth_1a_anticodon-bd. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
KO	K01883.
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.
SMART	SM00840. DALR_2. 1 hit. [Graphical view]
SUPFAM	SSF47323. tRNAsyn_1a_bind. 1 hit.
TIGRFAMs	TIGR00435. CysS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYC_RHOBA

Accession

Primary (citable) accession number: Q7US70

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2005
Last sequence update:	October 11, 2005
Last modified:	January 25, 2012
This is version 58 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program