ID SYP_JANSC Reviewed; 452 AA.
AC Q28TI5;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Proline--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01570};
DE EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01570};
DE AltName: Full=Prolyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01570};
DE Short=ProRS {ECO:0000255|HAMAP-Rule:MF_01570};
GN Name=proS {ECO:0000255|HAMAP-Rule:MF_01570}; OrderedLocusNames=Jann_1060;
OS Jannaschia sp. (strain CCS1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=290400;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCS1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W.,
RA Buchan A., Gonzalez J.M., Schell M.A., Richardson P.;
RT "Complete sequence of chromosome of Jannaschia sp. CCS1.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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_01570}.
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_01570};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01570}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01570}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC ProS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_01570}.
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DR EMBL; CP000264; ABD53977.1; -; Genomic_DNA.
DR RefSeq; WP_011454184.1; NC_007802.1.
DR AlphaFoldDB; Q28TI5; -.
DR SMR; Q28TI5; -.
DR STRING; 290400.Jann_1060; -.
DR KEGG; jan:Jann_1060; -.
DR eggNOG; COG0442; Bacteria.
DR HOGENOM; CLU_016739_4_2_5; -.
DR OrthoDB; 9809052at2; -.
DR Proteomes; UP000008326; 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; cd00861; ProRS_anticodon_short; 1.
DR CDD; cd00779; ProRS_core_prok; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR HAMAP; MF_01570; Pro_tRNA_synth_type2; 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; IPR004500; Pro-tRNA-synth_IIa_bac-type.
DR InterPro; IPR023716; Prolyl-tRNA_ligase_IIa_type2.
DR InterPro; IPR044140; ProRS_anticodon_short.
DR InterPro; IPR033730; ProRS_core_prok.
DR NCBIfam; TIGR00409; proS_fam_II; 1.
DR PANTHER; PTHR42753; MITOCHONDRIAL RIBOSOME PROTEIN L39/PROLYL-TRNA LIGASE FAMILY MEMBER; 1.
DR PANTHER; PTHR42753:SF2; PROLINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01046; TRNASYNTHPRO.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 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..452
FT /note="Proline--tRNA ligase"
FT /id="PRO_0000248902"
SQ SEQUENCE 452 AA; 50845 MW; 4C5C17CE7C0583C7 CRC64;
MRLSRYFLPV LKETPAEAQI VSHRLMLRAG MIKQASAGIY SWLPLGYKVL KRIERIVHEE
QIRAGHIPML MPTLQSADLW QKSGRFDAYG PEMLRLKDRH DRDMLYGPTN EEMITDMVGT
FVTSYKSLPL TLYHIQWKFR DEVRPRFGVM RGREFLMKDG YNFDLTKEAA LHAYNRHLVS
YLRTYERMGL QAIPMRADSG PIGGDYTHEF LVLADTGESE VFYDAEITDL KFGDREIDYD
DVAQCDAVLQ EFTSRYARTD ETHDEAEFAA IPGDRQRSAR GIEVGQIFYF GTEYSEKLGA
HVQNDEGERV PLHMGSHGIG VSRLLGAIIE ASHDDKGIIW PEGVTPFHCG IVNLKQGDAE
ADAACEALET ALENAGLEPL YDDRNERAGG KFATMDLIGL PWRITVGPRG LKNGVVELTS
RRTGESEELT PDAAVARVAE VYAAHKPVNA AV
//
