ID A0A1F8FKA3_9BACT Unreviewed; 410 AA.
AC A0A1F8FKA3;
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=A3C71_02545 {ECO:0000313|EMBL:OGN13544.1};
OS Candidatus Yanofskybacteria bacterium RIFCSPHIGHO2_02_FULL_43_15c.
OC Bacteria; Candidatus Yanofskybacteria.
OX NCBI_TaxID=1802679 {ECO:0000313|EMBL:OGN13544.1, ECO:0000313|Proteomes:UP000178197};
RN [1] {ECO:0000313|EMBL:OGN13544.1, ECO:0000313|Proteomes:UP000178197}
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:OGN13544.1}.
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DR EMBL; MGJT01000005; OGN13544.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8FKA3; -.
DR Proteomes; UP000178197; 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..316
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 410 AA; 46714 MW; BA6CEE6DB224032A CRC64;
MKLSQLFSRT ERQAPKDETS ANAQFLERGG FVYKNNAGIY TFLPLGWRVM GKIAQIIREE
MNAIGGQEIF MPALVDKRYM DATGRWDVEV AFEVKGKKEK EARFTLGWTH EEIITEIASK
YINSFKDLPF SAYQIQTKFR DEPRAKSGLL RGREFMMKDL YSFHASEGDM MNFYSEVRAA
YNKIFERCGL KAFYTLAAGG VFTASTTNEF QVVSSVGEDT IFVCTQCEYS ENKEISSLKD
ESLCLKCGGR VKEEKSIEVG NIFPLGTKYT EALHLQYVSE RGEKNFVVMG SYGIGLGRLM
GTVVEVHHDD KGIIWPESIS PFRVHLIVLD NEWEKGNQLY KKLLDKGVEI LYDDREDKTA
GEKFADADLI GTPIRLVISA KTLKAKSVEM KRRGQEKAEL VKLSNMERYF
//
