Reviewed, UniProtKB/Swiss-Prot Q2GLD8 (SYD_ANAPZ)

Names and origin

Protein names

Recommended name:
    Aspartyl-tRNA synthetase
    EC=6.1.1.12
Alternative name(s):
    Aspartate--tRNA ligase
      Short name=AspRS

Gene names

Name:	aspS
Ordered Locus Names:	APH_0190

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	598 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp). HAMAP MF_00044
Subunit structure	Homodimer By similarity. HAMAP MF_00044
Subcellular location	Cytoplasm By similarity HAMAP MF_00044.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	aspartyl-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 aspartate-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP nucleic acid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 598	598	Aspartyl-tRNA synthetase HAMAP MF_00044		PRO_1000006632

Sequences

	Sequence		Length	Mass (Da)
	Q2GLD8-1 [UniParc]. Last modified March 21, 2006. Version 1. Checksum: FDC3C3C7BE94D9F3	FASTA	598	66,205
	10 20 30 40 50 60 MNMYRTHLCN ALNLSHVGEE VTLSGWIFRK RDHGGILFID LRDFYGITQL VLNESSDQEL 70 80 90 100 110 120 FNYARSIGLE SVITVKGTVA ARSEDTINTS LSTGHVEVAV HTLVTESAAD ALPIHVPTST 130 140 150 160 170 180 NHPEDLRLKY RFLDLRCDKV KSNMLLRSAV ISEMRKAMES RGFIEVQTPI LTASSPEGAR 190 200 210 220 230 240 DYLVPSRVHA GKFYALPQAP QIFKQLLMAS GFDKYFQIAP CFRDEDARAD RSPGEFYQLD 250 260 270 280 290 300 VEMSFVTQED VFSVMEPVLR DIFTKFAGNR SVSPTFPRIT YKDAMLRYGT DKPDLRNPII 310 320 330 340 350 360 IADVSEVFLR SNFKTFQEGV ARGMVVRAIP APKTSEHPRS FFDSKVEYAK KIGARGLGYI 370 380 390 400 410 420 TFSTDNTVKG PVAKFLSDTE LANIQTLAGV GPGDSVFFVS DAADKAAELS GSVRELLGTE 430 440 450 460 470 480 LNLIEKDTFK FCWIVDFPYF QYENGKLAFS HNPFSMPQGG LDALSSSNPL DIVAYQYDIV 490 500 510 520 530 540 CNGIEISSGA IRNHKLDILY KAFSMVGYSP EAVDAEFGAL TRAFRFGVPP HGGIAPGVDR 550 560 570 580 590 IVMLLADVPN IREIIYFPLT QMGEDLLMGA PSEVNQSHLK ELSLALNITP KAAGKTSS

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].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000235 Genomic DNA. Translation: ABD43428.1.
RefSeq	YP_504813.1.
3D structure databases
HSSP	HSSP built from PDB template 1X56 based on UniProtKB O57980.
SMR	Q2GLD8. Positions 3-586.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2GLD8.
Genome annotation databases
GeneID	3930308.
GenomeReviews	Gene locus APH_0190 in contig CP000235_GR.
KEGG	aph:APH_0190.
NMPDR	fig|212042.5.peg.183.
TIGR	APH_0190.
Phylogenomic databases
eggNOG	COG0173.
HOGENOM	HBG396032.
OMA	YQLDVEM.
Enzyme and pathway databases
BioCyc	APHA212042:APH_0190-MONOMER.
Family and domain databases
HAMAP	MF_00044_B. Asp_tRNA_synth_B. [Tree]
InterPro	IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II_cons-dom. IPR002312. Asp-tRNA-synth_IIb. IPR020564. Asp-tRNA-synth_IIb_bac-type. IPR004524. Asp-tRNA-synth_IIb_bac/mt. IPR018153. Asp-tRNA-synth_IIb_C_bac/mt. IPR004115. GAD_dom. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR004365. NA_bd_OB_tRNA-helicase. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
PANTHER	PTHR22594. aa-tRNA-synt_II. 1 hit. PTHR22594:SF5. AspS_bac. 1 hit.
Pfam	PF02938. GAD. 1 hit. PF00152. tRNA-synt_2. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view]
PRINTS	PR01042. TRNASYNTHASP.
TIGRFAMs	TIGR00459. aspS_bact. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYD_ANAPZ

Accession

Primary (citable) accession number: Q2GLD8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	March 21, 2006
Last modified:	February 9, 2010
This is version 37 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)