ID A0A424S9H7_9PROT Unreviewed; 438 AA. AC A0A424S9H7; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 13-SEP-2023, entry version 14. 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=CBD13_003125 {ECO:0000313|EMBL:RPH00430.1}; OS Candidatus Pelagibacter sp. TMED153. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales; OC Pelagibacteraceae; Candidatus Pelagibacter. OX NCBI_TaxID=1986803 {ECO:0000313|EMBL:RPH00430.1}; RN [1] {ECO:0000313|EMBL:RPH00430.1, ECO:0000313|Proteomes:UP000195484} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TMED153 {ECO:0000313|EMBL:RPH00430.1}; RX PubMed=28713657; DOI=10.7717/peerj.3558; RA Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.; RT "290 metagenome-assembled genomes from the Mediterranean Sea: a resource RT for marine microbiology."; RL PeerJ 5:e3558-e3558(2017). 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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}. 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:RPH00430.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; NHHC02000046; RPH00430.1; -; Genomic_DNA. DR AlphaFoldDB; A0A424S9H7; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. 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; IPR004500; Pro-tRNA-synth_IIa_bac-type. DR InterPro; IPR044140; ProRS_anticodon_short. DR InterPro; IPR033730; ProRS_core_prok. DR NCBIfam; TIGR00409; proS_fam_II; 1. DR PANTHER; PTHR42753; MITOCHONDRIAL RIBOSOME PROTEIN L39/PROLYL-TRNA LIGASE FAMILY MEMBER; 1. DR PANTHER; PTHR42753:SF2; PROLYL-TRNA SYNTHETASE; 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 Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:RPH00430.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}. FT DOMAIN 38..339 FT /note="Aminoacyl-transfer RNA synthetases class-II family FT profile" FT /evidence="ECO:0000259|PROSITE:PS50862" FT COILED 354..381 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 438 AA; 50890 MW; AAABF1D782CBDA9A CRC64; MYLSKLFIPI TKDLPAEAKI KSHQLMLRAG MIKQSSAGIY SWLPLGFKVM KKIEQIVREE QNLIGAQEML MPTIQSSEIW KESGRYKDYG EEMLRIKDRQ GREMLYGPTN EELVTDIFRS SIKSYKSLPQ ILYHIQWKFR DEIRPRFGVM RCREFYMKDA YSFDLSDEDA KKSYNKMFYS YIRTFSRLGL KAIPMSADTG PIGGDLSHEF IILAETGESQ IYADKKIFEI DLNKYDFSDK SLQKMREDFS SIYAVTDDKY KETDFNKKVK KENQIKTKGI EVGHIFYFSD KYSKPLSCLI DTQGGKKIAV KMGSYGIGIS RLVGATIEAN YNKNVMKWPK SISPFDVVII PSISKNNNEN MEKAEKIYKE LKKQNIDVLL DDVDESMSNK FKKHDLIGIP YQIIIGSKSE QDKFEFKELN SKNEMLNLEN IKSQLKKK //