ID   SYP_METM5               Reviewed;         460 AA.
AC   A4FYA4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Proline--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01571};
DE            EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01571};
DE   AltName: Full=Prolyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01571};
DE            Short=ProRS {ECO:0000255|HAMAP-Rule:MF_01571};
GN   Name=proS {ECO:0000255|HAMAP-Rule:MF_01571}; OrderedLocusNames=MmarC5_0880;
OS   Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=402880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC BAA-1333;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a two-
CC       step reaction: proline is first activated by ATP to form Pro-AMP and
CC       then transferred to the acceptor end of tRNA(Pro). {ECO:0000255|HAMAP-
CC       Rule:MF_01571}.
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:0000255|HAMAP-Rule:MF_01571};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01571}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01571}.
CC   -!- DOMAIN: Consists of three domains: the N-terminal catalytic domain, the
CC       anticodon-binding domain and the C-terminal extension.
CC       {ECO:0000255|HAMAP-Rule:MF_01571}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       ProS type 3 subfamily. {ECO:0000255|HAMAP-Rule:MF_01571}.
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; CP000609; ABO35188.1; -; Genomic_DNA.
DR   RefSeq; WP_011868642.1; NC_009135.1.
DR   AlphaFoldDB; A4FYA4; -.
DR   SMR; A4FYA4; -.
DR   STRING; 402880.MmarC5_0880; -.
DR   EnsemblBacteria; ABO35188; ABO35188; MmarC5_0880.
DR   GeneID; 4929300; -.
DR   KEGG; mmq:MmarC5_0880; -.
DR   eggNOG; arCOG00402; Archaea.
DR   HOGENOM; CLU_001882_4_2_2; -.
DR   OMA; EVYWVTH; -.
DR   OrthoDB; 14454at2157; -.
DR   Proteomes; UP000000253; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00778; ProRS_core_arch_euk; 1.
DR   Gene3D; 3.30.110.30; -; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   Gene3D; 3.40.50.800; -; 1.
DR   HAMAP; MF_01571; Pro_tRNA_synth_type3; 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; IPR004499; Pro-tRNA-ligase_IIa_arc-type.
DR   InterPro; IPR017449; Pro-tRNA_synth_II.
DR   InterPro; IPR015264; Pro-tRNA_synth_II_arc.
DR   InterPro; IPR033721; ProRS_core_arch_euk.
DR   PANTHER; PTHR43382; PTHR43382; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF09181; ProRS-C_2; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PRINTS; PR01046; TRNASYNTHPRO.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   SUPFAM; SSF64586; SSF64586; 1.
DR   TIGRFAMs; TIGR00408; proS_fam_I; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..460
FT                   /note="Proline--tRNA ligase"
FT                   /id="PRO_0000318776"
SQ   SEQUENCE   460 AA;  53274 MW;  AE2476417C72B13D CRC64;
     MEFSEWYSDI LEKAGIYDLR YPIKGCGVYL PYGFKIRRYS FEILRKLLDE TNHDETLFPM
     LIPENLLAKE GEHIKGFEDE VFWVTHGGKT PLEVKLALRP TSETTMYYMM KQWIKVHTDL
     PMKLYQVVNT FRYETKHTRP LIRLREIMSF KEAHTAHATK EDCDAQITEA LNLYGEFFDE
     ICVPYIISKR PEWDKFPGAD YTMAFDTIYP DGKTMQIGTV HNLGQNFAKT FELEFETPDG
     EKDFVYQTCY GISDRAIASL ISVHGDEKGL VIPVDVAPIQ IVLIPLLFKG KEEIVMDKIK
     ELNNTLKSEF RVHLDDRDIR PGRKYNDWEI KGVPLRIELG PRDIENGQAL IVRRDTGEKI
     TVEYSNILEE VEKIVSMYKE NLKIKADEKI KNFLTVVNFE SDVNALSEKV KAALLENKGI
     ILIPFDESVY NEEFEELIDA SVLGQTAYEG KDYISVARTY