ID   A0A424S9H7_9PROT        Unreviewed;       438 AA.
AC   A0A424S9H7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   05-JUN-2019, entry version 2.
DE   RecName: Full=Proline--tRNA ligase {ECO:0000256|SAAS:SAAS00682368};
DE            EC=6.1.1.15 {ECO:0000256|SAAS:SAAS00682368};
GN   ORFNames=CBD13_003125 {ECO:0000313|EMBL:RPH00430.1};
OS   Candidatus Pelagibacter sp. TMED153.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Pelagibacterales;
OC   Pelagibacteraceae; Candidatus Pelagibacter.
OX   NCBI_TaxID=1986803 {ECO:0000313|EMBL:RPH00430.1};
RN   [1] {ECO:0000313|EMBL:RPH00430.1}
RP   NUCLEOTIDE SEQUENCE.
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
RT   resource for marine microbiology.";
RL   PeerJ 5:e3558-e3558(2017).
RN   [2] {ECO:0000313|EMBL:RPH00430.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TMED153 {ECO:0000313|EMBL:RPH00430.1};
RA   Graham E.D., Tully B.J.;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a
CC       two-step reaction: proline is first activated by ATP to form Pro-
CC       AMP and then transferred to the acceptor end of tRNA(Pro).
CC       {ECO:0000256|SAAS:SAAS01079608}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-
CC         prolyl-tRNA(Pro); Xref=Rhea:RHEA:14305, Rhea:RHEA-COMP:9700,
CC         Rhea:RHEA-COMP:9702, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:60039, ChEBI:CHEBI:78442, ChEBI:CHEBI:78532,
CC         ChEBI:CHEBI:456215; EC=6.1.1.15;
CC         Evidence={ECO:0000256|SAAS:SAAS01124670};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|SAAS:SAAS01079617}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS01079619}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. ProS type 2 subfamily. {ECO:0000256|SAAS:SAAS01000298}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:RPH00430.1}.
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DR   EMBL; NHHC02000046; RPH00430.1; -; Genomic_DNA.
DR   CDD; cd00779; ProRS_core_prok; 1.
DR   Gene3D; 3.40.50.800; -; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
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; IPR033730; ProRS_core_prok.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PRINTS; PR01046; TRNASYNTHPRO.
DR   TIGRFAMs; TIGR00409; proS_fam_II; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|SAAS:SAAS00682373};
KW   ATP-binding {ECO:0000256|SAAS:SAAS00682365};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS01079612};
KW   Ligase {ECO:0000256|SAAS:SAAS00682366, ECO:0000313|EMBL:RPH00430.1};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00682360};
KW   Protein biosynthesis {ECO:0000256|SAAS:SAAS00682364}.
FT   DOMAIN       38    339       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
FT   COILED      354    381       {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
//