Q2GKF4 (SYC_ANAPZ) 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:	APH_0555

Organism

Anaplasma phagocytophilum (strain HZ) [Complete proteome] [HAMAP]

Taxonomic identifier

212042 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma › phagocytophilum group

Protein attributes

Sequence length	462 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 – 462	462	Cysteine--tRNA ligase HAMAP MF_00041		PRO_0000240888
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)
	Q2GKF4 [UniParc]. Last modified March 21, 2006. Version 1. Checksum: E015BBC0EEA9D2DD	FASTA	462	51,808
	10 20 30 40 50 60 MKLYDTFSAA KRVFDPIDSA CVKIYACGPT VYDLAHIGNA RSAVVYDVLF RLLRELYPEV 70 80 90 100 110 120 IYVRNITDVD DKIINAAAET GQNIGDFTER YIRYFHEDMD ALNCLSPTVE PRATAEIDTM 130 140 150 160 170 180 LQLISRLVES GHAYVKGGSV YFSISSHRHY GRLSGRKIDE MISGNRVSID AEKLHPGDFV 190 200 210 220 230 240 LWKPATEQDI KLGAAWESPW GGGRPGWHIE CSAMSYRYLG ESFDIHGGGA DLMFPHHENE 250 260 270 280 290 300 LAQNMCAFSG SEYARYWVHN GFLTVNAGEK MSKSLGNVIT VRGLRNSGIE GAVIRYVFLC 310 320 330 340 350 360 THYRKPLDWN EKAIFDAQSA LSKMRRSCEE FTSEELNSDI EAVGVHNMLL EALKDDMNTP 370 380 390 400 410 420 MAIAALHALV GEINKTTDFK ERLKLARVLN RSAKLMGITD GFAGKSAEEA VDVDKIQELL 430 440 450 460 ERRREARNGG NYSLADEIRD QLHSMGIVIK DDKDGVTRWS RA

References

[1]

"Comparative genomics of emerging human ehrlichiosis agents." Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N. , Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R., Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H. PLoS Genet. 2:208-222(2006) [PubMed: 16482227] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HZ.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000235 Genomic DNA. Translation: ABD43506.1.
RefSeq	YP_505147.1. NC_007797.1.
3D structure databases
ProteinModelPortal	Q2GKF4.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2GKF4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3930041.
GenomeReviews	Gene locus APH_0555 in contig CP000235_GR.
KEGG	aph:APH_0555.
NMPDR	fig|212042.5.peg.547.
PATRIC	20949776. VBIAnaPha602_0604.
TIGR	APH_0555.
Phylogenomic databases
eggNOG	COG0215.
HOGENOM	HBG327651.
OMA	DFDALNM.
PhylomeDB	Q2GKF4.
ProtClustDB	PRK00260.
Enzyme and pathway databases
BioCyc	APHA212042:APH_0555-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_ANAPZ

Accession

Primary (citable) accession number: Q2GKF4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2006
Last sequence update:	March 21, 2006
Last modified:	January 25, 2012
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program