ID A0A0G0RM83_9BACT Unreviewed; 419 AA.
AC A0A0G0RM83;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Proline--tRNA ligase {ECO:0000256|ARBA:ARBA00019110};
DE EC=6.1.1.15 {ECO:0000256|ARBA:ARBA00012831};
DE AltName: Full=Prolyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029731};
GN ORFNames=UT90_C0004G0049 {ECO:0000313|EMBL:KKR53864.1};
OS Parcubacteria group bacterium GW2011_GWA1_40_21.
OC Bacteria.
OX NCBI_TaxID=1618784 {ECO:0000313|EMBL:KKR53864.1, ECO:0000313|Proteomes:UP000034712};
RN [1] {ECO:0000313|EMBL:KKR53864.1, ECO:0000313|Proteomes:UP000034712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-
CC tRNA(Pro); Xref=Rhea:RHEA:14305, Rhea:RHEA-COMP:9700, Rhea:RHEA-
CC COMP:9702, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:60039,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78532, ChEBI:CHEBI:456215;
CC EC=6.1.1.15; Evidence={ECO:0000256|ARBA:ARBA00000857};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKR53864.1}.
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DR EMBL; LBYO01000004; KKR53864.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0RM83; -.
DR STRING; 1618784.UT90_C0004G0049; -.
DR PATRIC; fig|1618784.3.peg.236; -.
DR Proteomes; UP000034712; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00861; ProRS_anticodon_short; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR002316; Pro-tRNA-ligase_IIa.
DR InterPro; IPR044140; ProRS_anticodon_short.
DR PANTHER; PTHR42753; MITOCHONDRIAL RIBOSOME PROTEIN L39/PROLYL-TRNA LIGASE FAMILY MEMBER; 1.
DR PANTHER; PTHR42753:SF2; PROLINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01046; TRNASYNTHPRO.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KKR53864.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 5..317
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 419 AA; 47220 MW; BE57166460568F91 CRC64;
MRQSQLLSKT RKEAPKDEVS RNAELLIRAG FIHKEMAGVY SFLPLGLRVL NKVNGVIREE
MNAIGGQEIL LAALQDRELW EKTGRWDDAV VDNWFKTKLK SGAELGLGFT HEEPLTALMK
NHIRSFRDLP LYPYQIQTKF RNETRAKSGI MRGREFLMKD LYSFSRDEKE HSLFYEKAKL
AYMNVFDKVG IGETTYITSA SGGTFSKYSD EFQTITEAGE DTIYVCEGCK IAINDEVLES
KKACGNCQSS DLKKKKSVEV GNIFNLGVRF SEALNLAYLD EEGKEKFVVM GSYGLGPTRL
IGTIAEVLSD KEGLVWPKRV APFDIHLVEI GGESGEVRKV SERIYSALNS RGLEVLFDDR
DLRAGEKFKD SDLIGIPLRL IISKKTLDEG LFEIKERSGG KVSKVKEGGL RDFADDYLK
//
