SYP_METMP
ID SYP_METMP Reviewed; 460 AA.
AC Q6LZD3; Q9HHB1;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=MMP0696;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Stathopoulos C., Li T., Longman R., Vothknecht U.C., Becker H.D., Ibba M.,
RA Soell D.;
RT "A single class II synthetase specifies two amino acids in archaeal
RT translation.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
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; AF197899; AAG28517.1; -; Genomic_DNA.
DR EMBL; BX950229; CAF30252.1; -; Genomic_DNA.
DR RefSeq; WP_011170640.1; NC_005791.1.
DR AlphaFoldDB; Q6LZD3; -.
DR SMR; Q6LZD3; -.
DR STRING; 267377.MMP0696; -.
DR EnsemblBacteria; CAF30252; CAF30252; MMP0696.
DR GeneID; 41279165; -.
DR KEGG; mmp:MMP0696; -.
DR PATRIC; fig|267377.15.peg.713; -.
DR eggNOG; arCOG00402; Archaea.
DR HOGENOM; CLU_001882_4_2_2; -.
DR OMA; EVYWVTH; -.
DR OrthoDB; 14454at2157; -.
DR BioCyc; MMAR267377:MMP_RS03645-MON; -.
DR BRENDA; 6.1.1.15; 3262.
DR Proteomes; UP000000590; 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; Reference proteome.
FT CHAIN 1..460
FT /note="Proline--tRNA ligase"
FT /id="PRO_0000249158"
FT CONFLICT 304
FT /note="N -> K (in Ref. 1; AAG28517)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="E -> D (in Ref. 1; AAG28517)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="L -> I (in Ref. 1; AAG28517)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="V -> I (in Ref. 1; AAG28517)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="L -> V (in Ref. 1; AAG28517)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="N -> S (in Ref. 1; AAG28517)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="S -> A (in Ref. 1; AAG28517)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="K -> E (in Ref. 1; AAG28517)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="N -> E (in Ref. 1; AAG28517)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 460 AA; 53319 MW; DFD7C169F00980F7 CRC64;
MEFSEWYSDI LEKAGIYDLR YPIKGCGVYL PYGFKIRRYS FEILRKLLDE TGHDETLFPM
LIPENLLAKE GEHIKGFEDE VFWVTHGGKT PLEVKLALRP TSETTMYYMM KQWIKVHTDL
PLKLYQVVNT FRYETKHTRP LIRLREIMSF KEAHTAHATK KECDAQIEEA LTLYKAFFDE
IGVPYVISKR PEWDKFPGAD YTMAFDTIYP DGKTMQIGTV HNLGQNFAKT FELEFETPDG
EKDFVYQTCY GISDRAIASL ISVHGDEKGL VIPVDVAPIQ IVLIPLLFKG KEEIVMDKIK
ELNNTLKSEF RVHLDDRDIR PGRKYNDWEL KGVPLRIELG PRDIENGHAL IVRRDTGEKI
TVEYSNILEE VEKIVSMYKE NLKLKAEEKV KSFITVLDFE NDVNSLSEKV KAKLLENKGI
ILIPFNESIY NEEFEELIDA SVLGLTTYEG KEYISVARTY
