A9WR21 (A9WR21_RENSM) 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:	RSal33209_0648

Organism

Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235) [Complete proteome] [HAMAP] EMBL ABY22395.1

Taxonomic identifier

288705 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Renibacterium

Protein attributes

Sequence length	619 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 ABY22395.1 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)
	A9WR21 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: FB55DC3FDBD92A43	FASTA	619	66,783
	10 20 30 40 50 60 MLCSADPQKG ATRVVLRLST LFLRTLREDP VDAEIASHKL MVRAGYIRRA APGIYSWLPL 70 80 90 100 110 120 GLRVLGKVEA IIREEMAAIG SQEVHFPALL PCEPYEATNR WTEYGDGIFR LKDRKGNDYL 130 140 150 160 170 180 LAPTHEEMFT LLVKDLYGSY KDLPVSLFQI QNKYRDEARP RAGLMRGREF IMKDSYSFDI 190 200 210 220 230 240 DDAGLDISYE AHRAAYFKIF ERLSLEVVAV KATAGAMGGS KSEEFLHPTP VGEDTYVRSA 250 260 270 280 290 300 GGYAANVEAV STVVPADIDF ADLADAMVHD TPNTPTIETL VAAANSMVPR ADAPWTAADT 310 320 330 340 350 360 LKNVVLAVDL PAVGDKKAER RLVVIGVPGD RGVDLKRIEA NISTHLGIGG EVEIEPANDE 370 380 390 400 410 420 DLKKNQLLVK GYIGPGLSLD AAVLGLESSS KLLYLVDPRV VSGTSWITGA NEHGKHVFGL 430 440 450 460 470 480 VAGRDFAWDG VIEAVEIREG DEAPDGSGPL EIARGIETGH VFQLGRKYAE IFDLKVLDQN 490 500 510 520 530 540 GKQVVVTMGS YGVGVTRAVA AIAEGNNDDR GLVWPIAVAP ADVHVVAVGR DSEVFETAEK 550 560 570 580 590 600 LAADLEAAGL DVILDDRQKV SPGVKFGDAE LIGVPMVLAV GRGLVDGVVE LKNRRTGEPN 610 NVPVADTVAE VLALRETLS

References

[1]

"Genome sequence of the fish pathogen Renibacterium salmoninarum suggests reductive evolution away from an environmental Arthrobacter ancestor." Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S., Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H., Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S. J. Bacteriol. 190:6970-6982(2008) [PubMed: 18723615] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000910 Genomic DNA. Translation: ABY22395.1.
RefSeq	YP_001623809.1. NC_010168.1.
3D structure databases
ProteinModelPortal	A9WR21.
ModBase	Search...
Protein-protein interaction databases
STRING	A9WR21.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5823639.
GenomeReviews	Gene locus RSal33209_0648 in contig CP000910_GR.
KEGG	rsa:RSal33209_0648.
PATRIC	23074464. VBIRenSal21953_0662.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG403504.
OMA	IQPAELW.
ProtClustDB	PRK09194.
Enzyme and pathway databases
BioCyc	RSAL288705:RSAL33209_0648-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.
TIGRFAMs	TIGR00409. ProS_fam_II. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

A9WR21_RENSM

Accession

Primary (citable) accession number: A9WR21

Entry history

Integrated into UniProtKB/TrEMBL:	February 5, 2008
Last sequence update:	February 5, 2008
Last modified:	January 25, 2012
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)