ID   SYP_METAR               Reviewed;         474 AA.
AC   Q0W0C9;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=UNCMA_01030;
GN   ORFNames=RRC469;
OS   Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=351160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22066 / NBRC 105507 / MRE50;
RX   PubMed=16857943; DOI=10.1126/science.1127062;
RA   Erkel C., Kube M., Reinhardt R., Liesack W.;
RT   "Genome of rice cluster I archaea -- the key methane producers in the rice
RT   rhizosphere.";
RL   Science 313:370-372(2006).
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}.
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DR   EMBL; AM114193; CAJ38164.1; -; Genomic_DNA.
DR   RefSeq; WP_012034428.1; NC_009464.1.
DR   AlphaFoldDB; Q0W0C9; -.
DR   SMR; Q0W0C9; -.
DR   STRING; 351160.RRC469; -.
DR   EnsemblBacteria; CAJ38164; CAJ38164; RRC469.
DR   GeneID; 5144523; -.
DR   KEGG; rci:RRC469; -.
DR   PATRIC; fig|351160.9.peg.107; -.
DR   eggNOG; arCOG00402; Archaea.
DR   OMA; EVYWVTH; -.
DR   OrthoDB; 14454at2157; -.
DR   Proteomes; UP000000663; 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; IPR016061; Pro-tRNA_ligase_II_C.
DR   InterPro; IPR017449; Pro-tRNA_synth_II.
DR   InterPro; IPR033721; ProRS_core_arch_euk.
DR   PANTHER; PTHR43382; PTHR43382; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF09180; ProRS-C_1; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PRINTS; PR01046; TRNASYNTHPRO.
DR   SMART; SM00946; ProRS-C_1; 1.
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; Reference proteome.
FT   CHAIN           1..474
FT                   /note="Proline--tRNA ligase"
FT                   /id="PRO_0000288425"
SQ   SEQUENCE   474 AA;  54354 MW;  32D028EF4072D174 CRC64;
     MEEESKSLPS KDNFSEWYNE LLMTAQIMDV RYPIKGVYVW YPFGFSIRKK VYNMLRNLLD
     VDHQETYFPM LIPKPELLKE SEHIKGFEDE VYWVTHGGLS ELEVPLALRP TSETAIYPMY
     KLWIRSHADL PLKLYQIVNT FRYETKHTRP LIRLREITSF KEAHTAHATW DDAEKQVHEA
     MDLYSEFFTK LAVPFIVHKR PEWDKFPGAD YTMAFDTMMP DGKSLQVGTV HHLGTKFAKT
     YDITYEDEKG ERQYVNQTCY GISERCIAAV IGIHGDNKGL VLPPNASQTQ VVIIPIIFKK
     DDGGVKEACQ KVKELLRAND IVAVIDDADE RPGAKYYKWE MKGTPFRIEI GPRDIKNNSV
     MLVRRDGKKE SIPMDGLPET VRNKLFEFQT DLLNAARDSM LARVKACETL DEAKQQIENG
     WATMPWCGEK ACGLEMENAV NCKLLGEAHT IKGAGKCPIC GKATDRIITM ARSY