ID A0A437AQS2_9MICR Unreviewed; 501 AA.
AC A0A437AQS2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=proline--tRNA ligase {ECO:0000256|ARBA:ARBA00012831};
DE EC=6.1.1.15 {ECO:0000256|ARBA:ARBA00012831};
DE AltName: Full=Prolyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029731};
GN ORFNames=TUBRATIS_001070 {ECO:0000313|EMBL:RVD93367.1};
OS Tubulinosema ratisbonensis.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Tubulinosematoidea;
OC Tubulinosematidae; Tubulinosema.
OX NCBI_TaxID=291195 {ECO:0000313|EMBL:RVD93367.1, ECO:0000313|Proteomes:UP000282876};
RN [1] {ECO:0000313|EMBL:RVD93367.1, ECO:0000313|Proteomes:UP000282876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Franzen {ECO:0000313|EMBL:RVD93367.1,
RC ECO:0000313|Proteomes:UP000282876};
RA Polonais V., Peyretaillade E., Niehus S., Wawrzyniak I., Franchet A.,
RA Gaspin C., Reichstadt M., Belser C., Labadie K., Delbac F., Ferrandon D.;
RT "Draft genome sequence of the microsporidian Tubulinosema ratisbonensis.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:RVD93367.1}.
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DR EMBL; RCSS01000034; RVD93367.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A437AQS2; -.
DR STRING; 291195.A0A437AQS2; -.
DR VEuPathDB; MicrosporidiaDB:TUBRATIS_001070; -.
DR Proteomes; UP000282876; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00862; ProRS_anticodon_zinc; 1.
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:0000313|EMBL:RVD93367.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000282876}.
FT DOMAIN 50..291
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 501 AA; 57958 MW; 04A2BBF0D3B8CE2B CRC64;
MHATDQKFGI TVKKETNFSE WYSQILLQGN MMDYYDVSGC YIMKPSSMFI WNKIKEFFNE
KICELGVQEC YFPMLLTKDS LEKEKGHLEN FSPELAWITK CGEENIDVPV AVRPTSEAIM
YPYFAKWIRS HRDLPLKLNQ WCSVLRWEVK STLPFIRGRE FLWQEGHTVH LTKEESDKEV
KIILDFYTEI YTELLAVPVI QGIKSENEKF GGASYTRTIE TFISDTGKGI QAATSHSLGT
NFSKMFEISV QANTEGKIER TFVYQNSWGI TTRSIGIALM IHSDNKGCVL PPKICKEQIV
IVPCGISDKI DLNQKNAFEI YVNEIINELK SEGLRVHYDN RENYSPGYKF NYWEIQGVPI
RLEIGLRDFN KNEVVLVRRL DGKKRPVKNE NLGKLLQSEI NLIHQEMYNK AKENLENKLV
EVKNIKEFNK FLNKKMIPKA LWCGLIECEE NIKKFSTERN KDGSVSISGA KSLCIMNEVE
DGKCFLCENL AKFLAIFGRT Y
//
