ID A0A0G1LLG1_9BACT Unreviewed; 423 AA.
AC A0A0G1LLG1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=UW97_C0003G0002 {ECO:0000313|EMBL:KKT96741.1};
OS Parcubacteria group bacterium GW2011_GWA2_45_15.
OC Bacteria.
OX NCBI_TaxID=1618833 {ECO:0000313|EMBL:KKT96741.1, ECO:0000313|Proteomes:UP000034700};
RN [1] {ECO:0000313|EMBL:KKT96741.1, ECO:0000313|Proteomes:UP000034700}
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:KKT96741.1}.
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DR EMBL; LCKK01000003; KKT96741.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1LLG1; -.
DR PATRIC; fig|1618833.3.peg.58; -.
DR Proteomes; UP000034700; 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 ECO:0000313|EMBL:KKT96741.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 38..318
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 423 AA; 48046 MW; 809A063275484161 CRC64;
MRQSELFTKT RREAPKDEEA KNAKLLIRAG FINKEMAGVY AYLPLGLRVI EKIKNVVREE
MNTFGGQEII MTTLQRKELW QETDRWDDKK VDVWFKSQLK NGAEVGLGWS HEEPITEMMK
NYISSYRDLP VFVYQFQTKL RNELRAKSGI MRGREFMMKD MYSYVADETA HKRIYDTVTA
SYMNIFRRVG LGDRTFLTFA SGGAFTQFSH EFQTIIDTGE DTIYLNREKK VAVNKEVLNE
EVLKELGLVR GELEEVAAAE VGNIFSFGGS KSEQLGLFFK DEKGESRPVI LGSYGLGITR
LMGVIVEALS DEKGIVWPKE VAPFQIHLLA LSPSKGLSYA NEVYKTLISR GIEVLYDDRD
LRAGEKFADA DLIGIPTQVV IGEKALESKI LEVKDRATGK MKEMTIEHLI NELDPSTSLG
VNK
//
