ID A0A1J4W675_9BACT Unreviewed; 412 AA.
AC A0A1J4W675;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=AUJ25_03265 {ECO:0000313|EMBL:OIO44860.1};
OS Parcubacteria group bacterium CG1_02_37_13.
OC Bacteria.
OX NCBI_TaxID=1805302 {ECO:0000313|EMBL:OIO44860.1, ECO:0000313|Proteomes:UP000182656};
RN [1] {ECO:0000313|EMBL:OIO44860.1, ECO:0000313|Proteomes:UP000182656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_37_13 {ECO:0000313|EMBL:OIO44860.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(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:OIO44860.1}.
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DR EMBL; MNWC01000049; OIO44860.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4W675; -.
DR STRING; 1805302.AUJ25_03265; -.
DR Proteomes; UP000182656; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 38..314
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 412 AA; 47201 MW; A89C2F7411850F1A CRC64;
MLQKELFTKT EKQSPKGEES KNAILLQRAG YIAKEMAGVY TFLPLGFLVL KKIEQIIREE
MLKLGAFEIF MPSLTSESSW EKTKRAEMDV LFHLEGRDKS RLVLNPTHEE VITPLMKKYI
SSYKDLPIST FQFQNKFRNE PRAKSGILRT REFMMKDLYS FHQNENDLEN FYEKVKENYF
NIFERVGLKE QTVLTFASGG AFSKYSHEFQ TICQAGEDII HLCEKCGIAI NSEIITEQRT
CPQCGNSSLE VKKAVEVGNI FKLRTKFSES FALKFRTKEG QDDLVEMGCY GIGLGRLMGV
IVEIYADEQG LVWPKEVAPF KAHLLCLGGD QERVMADKLY KELLAKNQEV LYDARDVSSG
EKFADADLIG LPLRVILSEK TLSQDNVEIK ERLSEKGELV KIKDLPKVLE EF
//
