ID L5L7Q9_9MOLU Unreviewed; 474 AA.
AC L5L7Q9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Proline--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_01571};
DE EC=6.1.1.15 {ECO:0000256|HAMAP-Rule:MF_01571};
DE AltName: Full=Prolyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01571};
DE Short=ProRS {ECO:0000256|HAMAP-Rule:MF_01571};
GN Name=proS {ECO:0000256|HAMAP-Rule:MF_01571,
GN ECO:0000313|EMBL:ELK19677.1};
GN ORFNames=D500_0864 {ECO:0000313|EMBL:ELK19677.1};
OS Mycoplasma feriruminatoris.
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=1179777 {ECO:0000313|EMBL:ELK19677.1};
RN [1] {ECO:0000313|EMBL:ELK19677.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G5847 {ECO:0000313|EMBL:ELK19677.1};
RX PubMed=23469346;
RA Fischer A., Santana-Cruz I., Giglio M., Nadendla S., Drabek E., Vilei E.M.,
RA Frey J., Jores J.;
RT "Genome Sequence of Mycoplasma feriruminatoris sp. nov., a Fast-Growing
RT Mycoplasma Species.";
RL Genome Announc. 1:E00216-12(2013).
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:0000256|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:0000256|ARBA:ARBA00000857,
CC ECO:0000256|HAMAP-Rule:MF_01571};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01571}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_01571}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC ProS type 3 subfamily. {ECO:0000256|HAMAP-Rule:MF_01571}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELK19677.1}.
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DR EMBL; ANFU01000081; ELK19677.1; -; Genomic_DNA.
DR RefSeq; WP_008364468.1; NZ_KB199642.1.
DR AlphaFoldDB; L5L7Q9; -.
DR STRING; 1179777.D500_0864; -.
DR PATRIC; fig|1179777.3.peg.780; -.
DR eggNOG; COG0441; Bacteria.
DR HOGENOM; CLU_001882_4_2_14; -.
DR OrthoDB; 9809052at2; -.
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; 3.40.50.800; Anticodon-binding domain; 1.
DR Gene3D; 3.30.110.30; C-terminal domain of ProRS; 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 NCBIfam; TIGR00408; proS_fam_I; 1.
DR PANTHER; PTHR43382:SF2; BIFUNCTIONAL GLUTAMATE_PROLINE--TRNA LIGASE; 1.
DR PANTHER; PTHR43382; PROLYL-TRNA SYNTHETASE; 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; SSF64586; C-terminal domain of ProRS; 1.
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 {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_01571};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01571}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01571};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01571};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01571};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_01571}.
FT DOMAIN 33..283
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 474 AA; 55332 MW; 197400369433F4F6 CRC64;
MKKQLDKITP RNIDFSQWYT DIVINTKLAS YGAVKGTMIF RPYGYRIWEL IQKYLDEEFK
KLNVDNVYFP LLIPESLFNK EKEHIDGFSP EIATVTKVGD KKLEENLFIR PTSEVLMMDY
FSNEVNSYRD LPLIYNQWCN VMRWEKTTRP FLRTSEFLWQ EGHTVHSSYN EAEDFCLKIL
NVYEKFAKEV LLLPVICGKK TEKEKFAGAQ DTYTIESLMF DGQALQCGTS HFFGNNFTKV
YDIKFQNKEN KLEHAYSTSW GVSTRLIGAI IMTHSDDNGL VLPSKIAPIQ IQIIQIKNTE
QIDQVVDVIK DQLSDYRINV DNSDKTFGFK ISEAEIKGIP IRIEIGPRDL ENNQITISRR
DQQENKIKIN YNDVKKVVDQ MIKEYDQTLY NNALENRKNR TFKANSIEEY IEILKQNQGF
VLVPFCGRIE CEEDIKTKTA TNSRCIPFDQ KQVQGKCFNC KKDTCLQVLF ARAY
//
