A4FM44 (A4FM44_SACEN) 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/ pro EMBL CAM05119.1
Synonyms:	proS HAMAP MF_01569
Ordered Locus Names:	SACE_5936

Organism

Saccharopolyspora erythraea (strain NRRL 23338) [Complete proteome] [HAMAP]

Taxonomic identifier

405948 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Pseudonocardineae › Pseudonocardiaceae › Saccharopolyspora

Protein attributes

Sequence length	574 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 CAM05119.1 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)
	A4FM44 [UniParc]. Last modified April 17, 2007. Version 1. Checksum: 0E872D8542D5D479	FASTA	574	62,926
	10 20 30 40 50 60 MFLRTLREDP ADAEVPSHRL LVRAGYVRRI GPGIYSWLPL GLRVLRNIEE IVRQEMDAIG 70 80 90 100 110 120 AQEIHFPALL PKEPYEATNR WTEYGPNLFR LKDRKGGDYL LGPTHEELFT LTVKGEYSSY 130 140 150 160 170 180 KDYPVILYQI QTKYRDEERP RAGILRGREF VMKDSYSFDL DDEGLTNSYR LHRDAYIRIF 190 200 210 220 230 240 DRVGLRYVIV AATSGAMGGS ASEEFLAEAP TGEDTFVRST SSGFAANVEA VVTPVPEPEP 250 260 270 280 290 300 IEDKPAAQVH HTPDTPTIET LVDFLNAHGD RKFTAADTLK NVLVKTRQPG AREWELLAVA 310 320 330 340 350 360 VPGDREVDLK RLEASLEPAE VALLEESDFA ANPFLVKGYI GPKALQDNGI RYLVDPRVVT 370 380 390 400 410 420 GTAWVTGADK PDHHVVDLVV GRDFTPDGTI EAAEVREGDP SPDGEGTLVA ARGIEIGHIF 430 440 450 460 470 480 QLGRKYADAF SLDALGQDGK PKRITMGSYG VGVSRMVAAI AEQSHDELGL VWPREVAPAD 490 500 510 520 530 540 VHVVIAGKDE SVREGAERLA ADLDAAGVRV LLDDRNASPG VKFADAELVG VPTILVVGKG 550 560 570 LAKGVVEVKD RRSGDREEVP VDGAVEHLVS TIRA

References

[1]

"Complete genome sequence of the erythromycin-producing bacterium Saccharopolyspora erythraea NRRL23338." Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S., Haydock S.F., Leadlay P.F. Nat. Biotechnol. 25:447-453(2007) [PubMed: 17369815] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM420293 Genomic DNA. Translation: CAM05119.1.
RefSeq	YP_001108044.1. NC_009142.1.
3D structure databases
ProteinModelPortal	A4FM44.
ModBase	Search...
Protein-protein interaction databases
STRING	A4FM44.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4945675.
GenomeReviews	Gene locus SACE_5936 in contig AM420293_GR.
KEGG	sen:SACE_5936.
PATRIC	23419226. VBISacEry28377_5903.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0442.
HOGENOM	HBG403504.
OMA	IQPAELW.
PhylomeDB	A4FM44.
ProtClustDB	PRK09194.
Enzyme and pathway databases
BioCyc	SERY405948:SACE_5936-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. G3DSA:3.90.960.10. YbaK/aa-tRNA-synth-assoc-reg. 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

A4FM44_SACEN

Accession

Primary (citable) accession number: A4FM44

Entry history

Integrated into UniProtKB/TrEMBL:	April 17, 2007
Last sequence update:	April 17, 2007
Last modified:	January 25, 2012
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)