ID   SYP_SPHEL               Reviewed;         510 AA.
AC   Q7X2P1;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 80.
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};
OS   Sphingomonas elodea.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=179878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31461 / PS-60;
RX   PubMed=14767675; DOI=10.1007/s10295-004-0118-9;
RA   Harding N.E., Patel Y.N., Coleman R.J.;
RT   "Organization of genes required for gellan polysaccharide biosynthesis in
RT   Sphingomonas elodea ATCC 31461.";
RL   J. Ind. Microbiol. Biotechnol. 31:70-82(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; AY220099; AAP46176.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7X2P1; -.
DR   SMR; Q7X2P1; -.
DR   STRING; 1081640.AGFU01000034_gene2871; -.
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; PF00587; tRNA-synt_2b; 1.
DR   SMART; SM00946; ProRS-C_1; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   SUPFAM; SSF64586; SSF64586; 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..510
FT                   /note="Proline--tRNA ligase"
FT                   /id="PRO_0000249150"
SQ   SEQUENCE   510 AA;  56995 MW;  09575549C5AFBE02 CRC64;
     MIKHALSVTR DGDFAQWYQT VISEADMAED SGVRGCMVIR PWGYGIWERI QRLLDDRIKA
     TGHENCYFPL FIPLSYFEKE AEHVDGFAKE MAVVTHHRLI QKDGRLVPDP EAKLEEPLVV
     RPTSETVIGA AMSRWVQSWR DLPVLINQWA NVVRWEMRTR MFLRTAEFLW QEGHTAHATV
     EEAQEETRKM LEVYRDFAET CLAMPVVAGE KPENERFPGA VSTFSIEAMM QDGKALQAGT
     SHFLGTTFSS AQDIKFQNSE GQFELAQTTS WGVSTRMIGG LIMVHGDDDG LRVPPMVAPW
     QIVIVPMLRD QPEDAATIDY CKSLQAELAK LTALGEPVRA LLDLKAVKAQ TKRWGWVKKG
     APIVIEVGGR DVAGGNVSVI QRNKLYREDG KLDSRIMPRG DFVAEAAAIL ESIQQGLYLD
     ARERLDSNIR RDVTDFDGLA AMFADSVKFP GWAEVSWAKP TGAELDAVVE RLKALKLTFR
     NVPGTAAPAE GTCLFTGKPA VERILVARAY