ID A0A1G1WVY5_9BACT Unreviewed; 416 AA.
AC A0A1G1WVY5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=A3A61_03050 {ECO:0000313|EMBL:OGY31863.1};
OS Candidatus Woykebacteria bacterium RIFCSPLOWO2_01_FULL_43_14.
OC Bacteria; Candidatus Woykebacteria.
OX NCBI_TaxID=1802605 {ECO:0000313|EMBL:OGY31863.1, ECO:0000313|Proteomes:UP000177718};
RN [1] {ECO:0000313|EMBL:OGY31863.1, ECO:0000313|Proteomes:UP000177718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGY31863.1}.
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DR EMBL; MHDB01000022; OGY31863.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1WVY5; -.
DR STRING; 1802605.A3A61_03050; -.
DR Proteomes; UP000177718; 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 CDD; cd00779; ProRS_core_prok; 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 InterPro; IPR033730; ProRS_core_prok.
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 33..321
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 416 AA; 46626 MW; F0EEB831D143A52F CRC64;
MRYSELFGKT LREAPRDEES KNAQLLARGG YVNKLMSGVY TFLPLGTRVL TKIENIVREE
MAAIGGQEIL MPTMQPKENW VATGRWDDFD VLYKVKSPDG REVALGPTHE EVVAPLAKQY
VQSYKDLPLY LYQIQTKFRD ELRAKNGLLR GREFRMKDLY SFHSSVEDLE AYYEKAKQAY
AKIFDRVGLK ALLTEASGGT FSKYSHEFQV QVESGEDVLY HCSKCSFCQN KEIVSADLDK
LKVGEAGVCP KCGENLEVVS ATEVGNIFQL KNKYSDPFKL TFLDSDGQTQ TVMMGCYGIG
TSRLMGTIAE VLSDEKGLRW PEEVAPYKVH LVSLGKSMPF ANEVYHKLVS AGVEVLYDER
DCSAGVKLGD ADLVGLPLRV VVSDKTAAEN KVELKARNSE EVRVISIDET LEILVK
//
