ID A0A0F9ZMG6_9BACT Unreviewed; 403 AA.
AC A0A0F9ZMG6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=UR35_C0002G0137 {ECO:0000313|EMBL:KKP45304.1};
OS Candidatus Woesebacteria bacterium GW2011_GWB1_33_22.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1618566 {ECO:0000313|EMBL:KKP45304.1, ECO:0000313|Proteomes:UP000034778};
RN [1] {ECO:0000313|EMBL:KKP45304.1, ECO:0000313|Proteomes:UP000034778}
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:KKP45304.1}.
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DR EMBL; LBOW01000002; KKP45304.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F9ZMG6; -.
DR STRING; 1618566.UR35_C0002G0137; -.
DR PATRIC; fig|1618566.3.peg.318; -.
DR Proteomes; UP000034778; 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 ECO:0000313|EMBL:KKP45304.1}; 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..313
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 403 AA; 46390 MW; 1A5CD576AFE29A68 CRC64;
MKQSSLFPKT RKEAPKDAES INHKLLVRAG FMDQLMAGSW TLLPMGWKVV TKINQIIREE
MNAIGAQEML MPLLHPKEIW NETGRWDKAN DIMYKLSDPR QKEYALSFTH EEIVMDLLRK
NITSYKDLPV SVYHFSTKFR NELRAKSGIL RGREFMMKDL YSAHTTEENL MEYYEKVKDA
YSKIFRRLGF NFKVTKASGG VFTDKFTHEF QVLSDAGEDT IYWRDGDPEA INEEVLKGDK
KDYKSSKAIE VGNIFPLGTW YAERMRAYFT DEDGKKKPIW FGSYGIGPTR VMGTWVEVSH
DNKGIIWNKE ISPFQVHLIG LSGKGEDIYE KLKNAGIDVL FDDRDVPAGQ KFNDADLIGI
PVRLVVSDKT GDLSAQAGEI EYKERTSDKT ELLDFEEVIK KIK
//
