A3PY69 (A3PY69_MYCSJ) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Proline--tRNA ligase HAMAP MF_01569
EC=6.1.1.15 HAMAP MF_01569

Alternative name(s):
Prolyl-tRNA synthetase HAMAP MF_01569

Gene names

Name:	proS HAMAP MF_01569
Ordered Locus Names:	Mjls_2059

Organism

Mycobacterium sp. (strain JLS) [Complete proteome] [HAMAP]

Taxonomic identifier

164757 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length	584 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS By similarity. HAMAP MF_01569
Catalytic activity	ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). HAMAP MF_01569
Subunit structure	Homodimer By similarity. HAMAP MF_01569
Subcellular location	Cytoplasm By similarity HAMAP MF_01569.
Domain	Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain By similarity. HAMAP MF_01569
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 subfamily. HAMAP MF_01569

Ontologies

Keywords
Biological process	Protein biosynthesis HAMAP MF_01569
Cellular component	Cytoplasm HAMAP MF_01569
Ligand	ATP-binding HAMAP MF_01569 Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase HAMAP MF_01569 EMBL ABN97846.1 Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	prolyl-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 proline-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	A3PY69 [UniParc]. Last modified April 3, 2007. Version 1. Checksum: B32538BEBA5AB2C4	FASTA	584	63,945
	10 20 30 40 50 60 MITRMSELFL RTLRDDPADA EVPSHKLLIR AGYVRPVGPG LYTWLPLGLR VFRKIEQIVR 70 80 90 100 110 120 DEMTAIGGQE ILFPALLPRA PYETTNRWTE YGDTLFRLKD RRDNDYLLGP THEELFTLTV 130 140 150 160 170 180 KGEYSSYKDF PLILFQIQTK YRDEARPRAG ILRGREFVMK DSYSFDVDDD GLKTAYHLHR 190 200 210 220 230 240 EAYQRIFARL GVHYVIVSAV SGAMGGSASE EFLAESEVGE DTFVRCLQSG YAANVEAVLT 250 260 270 280 290 300 RVPEPLPIEG QPEAVVYDTP DAPTIATLVD WANGADLPNF AGRAVTAADT LKNVLVKVRE 310 320 330 340 350 360 PGGEWELLAV GVPGDREVDD KRLGAALEPA EYALLDEADF ARHPFLVKGY VGPKALLDNG 370 380 390 400 410 420 VRYLVDPRVV DGTAWITGAD APNKHVVGLV AGRDFVADGT IEAAEVRDGD PSPDGAGPLV 430 440 450 460 470 480 SARGIEIGHI FQLGRKYTEA FSADVLGEDG KPVRLTMGSY GIGVSRLVAV IAEQQHDELG 490 500 510 520 530 540 LRWPAAVAPF DVHVVIANKD DGARTGATEL AGELDRLGLE VLLDDRKSSP GVKFKDAELL 550 560 570 580 GVPWIVVVGR GWGDGVVELR DRFSGEKREI GVDDAATEIL ATVR

References

[1]

"Complete sequence of Mycobacterium sp. JLS." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J., Sims R.C., Richardson P. Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JLS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000580 Genomic DNA. Translation: ABN97846.1.
RefSeq	YP_001070337.1. NC_009077.1.
3D structure databases
ProteinModelPortal	A3PY69.
ModBase	Search...
Protein-protein interaction databases
STRING	A3PY69.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000047605; EBMYCP00000045886; EBMYCG00000047600.
GeneID	4877780.
GenomeReviews	Gene locus Mjls_2059 in contig CP000580_GR.
KEGG	mjl:Mjls_2059.
PATRIC	18090240. VBIMycSp51234_2060.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0442.
GeneTree	EBGT00050000016802.
HOGENOM	HBG403504.
OMA	IQPAELW.
PhylomeDB	A3PY69.
ProtClustDB	PRK09194.
Family and domain databases
HAMAP	MF_01569. Pro_tRNA_synth_type1. [Tree]
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-dom. IPR006195. aa-tRNA-synth_II. IPR004154. Anticodon-bd. IPR002316. Pro-tRNA-synth_IIa. IPR004500. Pro-tRNA-synth_IIa_bac-type. IPR023717. Pro-tRNA-Synthase_IIa_type1. IPR007214. YbaK/aa-tRNA-synth-assoc-dom. [Graphical view]
Gene3D	G3DSA:3.40.50.800. Anticodon_bd. 1 hit.
KO	K01881.
PANTHER	PTHR11451:SF3. PTHR11451:SF3. 1 hit.
Pfam	PF03129. HGTP_anticodon. 1 hit. PF00587. tRNA-synt_2b. 1 hit. PF04073. YbaK. 1 hit. [Graphical view]
PRINTS	PR01046. TRNASYNTHPRO.
SUPFAM	SSF52954. Anticodon_bd. 1 hit. SSF55826. YbaK/aa-tRNA-synth-assoc-reg. 1 hit.
TIGRFAMs	TIGR00409. ProS_fam_II. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

A3PY69_MYCSJ

Accession

Primary (citable) accession number: A3PY69

Entry history

Integrated into UniProtKB/TrEMBL:	April 3, 2007
Last sequence update:	April 3, 2007
Last modified:	January 25, 2012
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)