ID   SYP_MAGSA               Reviewed;         500 AA.
AC   Q2W136;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   25-MAY-2022, entry version 95.
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=amb3636;
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=342108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA   Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT   "Complete genome sequence of the facultative anaerobic magnetotactic
RT   bacterium Magnetospirillum sp. strain AMB-1.";
RL   DNA Res. 12:157-166(2005).
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAE52439.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AP007255; BAE52439.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011385993.1; NC_007626.1.
DR   AlphaFoldDB; Q2W136; -.
DR   SMR; Q2W136; -.
DR   STRING; 342108.amb3636; -.
DR   PRIDE; Q2W136; -.
DR   EnsemblBacteria; BAE52439; BAE52439; amb3636.
DR   KEGG; mag:amb3636; -.
DR   HOGENOM; CLU_001882_4_2_5; -.
DR   OMA; EVYWVTH; -.
DR   OrthoDB; 665824at2; -.
DR   Proteomes; UP000007058; 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; 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; 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..500
FT                   /note="Proline--tRNA ligase"
FT                   /id="PRO_0000249130"
SQ   SEQUENCE   500 AA;  56165 MW;  AB89A85D0A8D21E4 CRC64;
     MSKAKKTAVT PTREENFPEW YQQVIKASDM AENSPVRGCM VIKPWGYGIW EAIQRDLDRR
     IKETGHENCY FPLFIPLSFL EKEAAHVEGF AKEMAVVTHH RLVAEDGKLV PSGKLEEPLV
     VRPTSETIIG DAFARWIQSY RDLPMLVNQW ANVVRWEMRP RIFLRTAEFL WQEGHTAHAT
     AEEAMDETLK MLEVYRVMAE EVLAMPVIVG EKPAHERFPG ADKTYSIEAM MQDGKALQAG
     TSHFLGQHFS KAQNIRYQTA QGGEEFCYTT SWGVSTRLIG GVIMSHADDN GLRVPPRIAP
     KQIVFVPITR ADGDEALIED FLAPIVKDLS AQSFGGERLR VHVDRRPLAP PEKRWEWVKK
     GAPIICEVGP RDVAGGSVAM IRRDGELKGQ ITPKDELVSR AAAILEDIQK TLFTQAATAL
     KERTVTVRTL DDFLAVFADD TTFGRKFVRA RWCGDSDTLA KLDEYSITIR NVPFDQDGEA
     GTCVLSGRPA TQEVIFAKSY