SYP_AMOA5
ID SYP_AMOA5 Reviewed; 491 AA.
AC B3ER64;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=Aasi_0277;
OS Amoebophilus asiaticus (strain 5a2).
OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Amoebophilaceae;
OC Candidatus Amoebophilus.
OX NCBI_TaxID=452471;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5a2;
RX PubMed=20023027; DOI=10.1128/jb.01379-09;
RA Schmitz-Esser S., Tischler P., Arnold R., Montanaro J., Wagner M.,
RA Rattei T., Horn M.;
RT "The genome of the amoeba symbiont 'Candidatus Amoebophilus asiaticus'
RT reveals common mechanisms for host cell interaction among amoeba-associated
RT bacteria.";
RL J. Bacteriol. 192:1045-1057(2010).
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; CP001102; ACE05716.1; -; Genomic_DNA.
DR RefSeq; WP_012472478.1; NC_010830.1.
DR AlphaFoldDB; B3ER64; -.
DR SMR; B3ER64; -.
DR STRING; 452471.Aasi_0277; -.
DR EnsemblBacteria; ACE05716; ACE05716; Aasi_0277.
DR KEGG; aas:Aasi_0277; -.
DR eggNOG; COG0442; Bacteria.
DR HOGENOM; CLU_001882_4_2_10; -.
DR OMA; EVYWVTH; -.
DR OrthoDB; 665824at2; -.
DR Proteomes; UP000001227; 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; 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 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..491
FT /note="Proline--tRNA ligase"
FT /id="PRO_1000215544"
SQ SEQUENCE 491 AA; 56331 MW; 7F11E0309FB5CE4D CRC64;
MHKKLPTRAE NFSEWYNEII KRAELAENAA VRGCMTIRPY GFAIWEKMQA ILDKAFKATG
HENAYFPIFI PKSYLNREAA HVEGFAKECA VVTHYRLKAT EDGQQVVVDP SAKLEEELIV
RPTSETIIWN SYKNWIQSYR DLPLLINQWC NVVRWEMRTR LFLRTAEFLW QEGHTAHATQ
AEAEQEALQM LNIYADFGKD YLAIPFLKGI KTEHERFAGA EETYTIEALM QDGKALQAGT
SHFLGQRFAK AFEVTFTNQA GQLDYVWGTS WGLTTRLIGA LVMTHSDDKG LVLPPRVAPI
QIVIIPIYRT QEEKEAIQQQ AQHIQQQLIA HNISAKLDGR DEHKPGWKFA EYELKGVPIR
MAIGPNDLAN NTVELTRRDT SEKTTVPTDN IIVVVKSMLD SIHDNLYQRA YEFREQNTYQ
VNSYEEFKTA ISQKRGFILA HWDGTKETER QIHAETKATI RCIPLEVNTE PGVCIYTGKP
SKQRVVFGQA Y