ID   SYP2_RHOJR              Reviewed;         479 AA.
AC   Q0SAY4;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Proline--tRNA ligase 2 {ECO:0000255|HAMAP-Rule:MF_01571};
DE            EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01571};
DE   AltName: Full=Prolyl-tRNA synthetase 2 {ECO:0000255|HAMAP-Rule:MF_01571};
DE            Short=ProRS 2 {ECO:0000255|HAMAP-Rule:MF_01571};
GN   Name=proS2 {ECO:0000255|HAMAP-Rule:MF_01571};
GN   OrderedLocusNames=RHA1_ro03499;
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1;
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABG95302.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000431; ABG95302.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_050787323.1; NC_008268.1.
DR   AlphaFoldDB; Q0SAY4; -.
DR   SMR; Q0SAY4; -.
DR   STRING; 101510.RHA1_ro03499; -.
DR   EnsemblBacteria; ABG95302; ABG95302; RHA1_ro03499.
DR   KEGG; rha:RHA1_ro03499; -.
DR   PATRIC; fig|101510.16.peg.3532; -.
DR   eggNOG; COG0442; Bacteria.
DR   HOGENOM; CLU_001882_4_2_11; -.
DR   OMA; EVYWVTH; -.
DR   Proteomes; UP000008710; 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..479
FT                   /note="Proline--tRNA ligase 2"
FT                   /id="PRO_0000288413"
SQ   SEQUENCE   479 AA;  52973 MW;  1D058198BB29ADE4 CRC64;
     MARDERGVTA QSEDFAAWYN EVVFKAGLVD RGPAKGTMVI RPYGYRLWEL LQSELDRRIK
     DTGHENAYFP LLIPESYLGR EAEHVEGFSP ELAVVTHVGG KVLEEPLVVR PTSETIIGEM
     MAKWISSHRD LPLLLNQWAN VVRWELRPRM FLRTTEFLWQ EGHTAHVDEA SARRETMLAL
     DIYHEVAREL AAIPVVPGEK TPGERFAGAV ATYTIEGMMR DGRALQSGTS HYMGIKFASA
     FDIRFTSETG REELCHTTSW GMSTRMIGGI VMTHGDDKGL VFPPRLAPHQ VVIVPITRGG
     NVAVEGAADE LAHRLRSVGV RTHVDARPHL TPGFKYNEWE MRGVPVRLEL GPRDLEDGTV
     MMVKRLGDDG KQAVPIDSLP EAMPGVLDDF QAFLLARATA FRDGHARTVD NWTDFADAVS
     TGWALALHCG IAACEEEIKS LTAATPRCVP LGGEPETGVC VRCGAASAYG KRVIFGRAY