Q0S235 (SYP1_RHOSR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proline--tRNA ligase 1
EC=6.1.1.15

Alternative name(s):
Prolyl-tRNA synthetase 1
Short name=ProRS 1

Gene names

Name:	proS1
Ordered Locus Names:	RHA1_ro06628

Organism

Rhodococcus sp. (strain RHA1) [Complete proteome] [HAMAP]

Taxonomic identifier

101510 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus

Protein attributes

Sequence length	581 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.

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	prolyl-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 proline-tRNA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 581	581	Proline--tRNA ligase 1 HAMAP MF_01569		PRO_0000288371

Sequences

	Sequence		Length	Mass (Da)
	Q0S235 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 7CCFE9BC03BEF4AD	FASTA	581	63,191
	10 20 30 40 50 60 MITRLSHLFL RTLRDDPADA EVPSHKLLVR AGYVRRIAPG VYSWLPLGLR VLREVERVVR 70 80 90 100 110 120 EEMNGIGAQE ISLPALLPRE PYEASNRWTE YGDGLFRLKD RKGGDYLLGP THEELFALTV 130 140 150 160 170 180 KGEYNSYKDF PVTLYQVQTK YRDEERPRAG ILRGREFVMK DSYSFDLTDE GLTASYRAHR 190 200 210 220 230 240 DAYERIFSRL GVKYVIVSAT SGAMGGSASE EFLAESEIGE DTYVRCLESG YAANVEAVKT 250 260 270 280 290 300 LAPEAVPFDG LPAAKVHDTP DTPTIATLVD WANGADLGWT VTAADTLKNI LVKTRQPGGK 310 320 330 340 350 360 WELLGIGVPG DREVDDKRLG ASLEPAEFEL LTEADFAANP FLVKGYIGPK ALQANGVRYL 370 380 390 400 410 420 VDPRIVDGTS WITGADEPGK HVVGLVAGRD FTPDGTIEAA EVRDGDPSPD GAGALVAARG 430 440 450 460 470 480 IEIGHVFQLG RKYTDVFSVD VLGENGKPVR PTMGSYGVGV SRLVAVIAEQ HHDEKGLRWP 490 500 510 520 530 540 AEVSPADVHV VIANKDETAR EGAEGLAAEL DKAGLEVILD DRKASPGVKF KDSELLGVPL 550 560 570 580 VVVVGRGWGE GKVEVRDRFT GESREVAAES ALSEIVKAVR G

References

[1]

"The complete genome of Rhodococcus sp. RHA1 provides insights into a catabolic powerhouse." McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H. , Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W., Eltis L.D. Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006) [PubMed: 17030794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RHA1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000431 Genomic DNA. Translation: ABG98401.1.
RefSeq	YP_706559.1. NC_008268.1.
3D structure databases
ProteinModelPortal	Q0S235.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0S235.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4224179.
GenomeReviews	Gene locus RHA1_ro06628 in contig CP000431_GR.
KEGG	rha:RHA1_ro06628.
PATRIC	23212229. VBIRhoJos26306_6686.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0442.
HOGENOM	HBG403504.
OMA	IQPAELW.
PhylomeDB	Q0S235.
ProtClustDB	PRK09194.
Enzyme and pathway databases
BioCyc	RSP101510:RHA1_RO06628-MONOMER.
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

SYP1_RHOSR

Accession

Primary (citable) accession number: Q0S235

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	September 5, 2006
Last modified:	January 25, 2012
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program