A4TCE7 (A4TCE7_MYCGI) 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:	Mflv_4045

Organism

Mycobacterium gilvum (strain PYR-GCK) (Mycobacterium flavescens (strain ATCC 700033 / PYR-GCK)) [Complete proteome] [HAMAP]

Taxonomic identifier

350054 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	588 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 ABP46515.1 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)
	A4TCE7 [UniParc]. Last modified May 15, 2007. Version 1. Checksum: CF5F32220B58A74C	FASTA	588	64,017
	10 20 30 40 50 60 MITRMSELFL RTLRDDPADA EVPSHKLLIR AGYVRPVGPG LYSWLPLGLK VLRKIEHIVR 70 80 90 100 110 120 SEMDAIGGQE ILFPALLPRA PYETTNRWTE YGDTLFRLQD RRDNDYLLGP THEEMFTLTV 130 140 150 160 170 180 KGEYSSYKDF PLRLYQIQNK YRDEARPRAG ILRGREFLMK DSYSFDVDDD GLKNAYHAHR 190 200 210 220 230 240 EAYQRIFDRL KVRYVIVSAV SGAMGGSASE EFLAESEVGE DTFVRCAQSG YAANVEAVVT 250 260 270 280 290 300 TAPDPIPLDG LPEAVVYDTP DTPTIATLVD WANTADLPSF AGRAVTAADT LKNVLLKVRE 310 320 330 340 350 360 PGGDWELLAI GVPGDREVDD KRLGAALDPA EYAMADDADF AAHPFLKKGY IGPKALLANG 370 380 390 400 410 420 VRYLVDPRVV DGTAWITGAD ETGRHVVDLV AGRDFTPDGT IEAAEVREGD PSPDGAGPLV 430 440 450 460 470 480 AARGIEIGHV FQLGRKYADA FNADVLGENG KPVRLTMGSY GIGVSRLVAV IAEQHHDELG 490 500 510 520 530 540 LRWPGSVAPF AVHVVIANKD AEARAGATEL ATALDRAGAD VLLDDRTASP GVKFKDAELL 550 560 570 580 GVPWIVVVGR GWADGVVELR DRFSGEKREI PVGPDTTAAE QILAAITG

References

[1]

"Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK." 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., Richardson P. Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PYR-GCK.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000656 Genomic DNA. Translation: ABP46515.1.
RefSeq	YP_001135303.1. NC_009338.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A4TCE7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000026804; EBMYCP00000026466; EBMYCG00000026799.
GeneID	4975359.
GenomeReviews	Gene locus Mflv_4045 in contig CP000656_GR.
KEGG	mgi:Mflv_4045.
PATRIC	18036297. VBIMycGil17082_4119.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0442.
GeneTree	EBGT00050000016802.
HOGENOM	HBG403504.
OMA	IQPAELW.
PhylomeDB	A4TCE7.
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

A4TCE7_MYCGI

Accession

Primary (citable) accession number: A4TCE7

Entry history

Integrated into UniProtKB/TrEMBL:	May 15, 2007
Last sequence update:	May 15, 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)