Q5PB14 (SYC_ANAMM) 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:	AM481

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	466 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.

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: 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 – 466	466	Cysteine--tRNA ligase HAMAP MF_00041		PRO_0000159338
Regions
	Motif	29 – 39	11	"HIGH" region HAMAP MF_00041
	Motif	270 – 274	5	"KMSKS" region HAMAP MF_00041
Sites
	Metal binding	27	1	Zinc By similarity
	Metal binding	211	1	Zinc By similarity
	Metal binding	236	1	Zinc By similarity
	Metal binding	240	1	Zinc By similarity
	Binding site	273	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5PB14 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 5B7DA92E58E08885	FASTA	466	51,995
	10 20 30 40 50 60 MRLHDTLHAA KRVFSPKNSE RVGVYVCGPT VYDLAHIGNA RSVVVYDVLF RLLKALYPEV 70 80 90 100 110 120 IYVRNITDVD DKIINATESE NKSIAELTAH YTKLFHEDIE ALNCLSPTFE PRATEEIETM 130 140 150 160 170 180 LHIIGRLIQA GHAYVRGGTV YFSVESYKHY GALSGRKLGD MISGSRVEVV AEKLHPGDFV 190 200 210 220 230 240 LWKPATDLDM KLGACWPSPW GVGRPGWHVE CSAMSYRYLG DSFDIHGGGA DLMFPHHENE 250 260 270 280 290 300 ISQSCCAFPG SEYARYWVHN GFLTVNGGEK MSKSLGNVIT VRGLLSNGVD GEVIRYVFLS 310 320 330 340 350 360 THYRKPLDWG DKAVLDAKEA LNKIYRSCEG FSAQLLSTGL EDVGVHDAVM ASLRDDMNTP 370 380 390 400 410 420 AAIAALHELV KEINKTNNAG EKLRLARVLN KSAMLMGMFR NFPERKLLDM RGLVDEGEIN 430 440 450 460 RLIEKRVEAK KCGDFKLADE IRESLSNMGI GISDGKDGST RWHRKN

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: AAV86516.1.
RefSeq	YP_153771.1. NC_004842.2.
3D structure databases
ProteinModelPortal	Q5PB14.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5PB14.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3171872.
GenomeReviews	Gene locus AM481 in contig CP000030_GR.
KEGG	ama:AM481.
PATRIC	20946975. VBIAnaMar46146_0413.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0215.
HOGENOM	HBG327651.
OMA	ALRPTHE.
PhylomeDB	Q5PB14.
ProtClustDB	PRK00260.
Enzyme and pathway databases
BioCyc	AMAR234826:AM481-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_ANAMM

Accession

Primary (citable) accession number: Q5PB14

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	January 4, 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