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Database: UniProt
Entry: A0A1E7QK65_WOLPI
LinkDB: A0A1E7QK65_WOLPI
Original site: A0A1E7QK65_WOLPI 
ID   A0A1E7QK65_WOLPI        Unreviewed;       383 AA.
AC   A0A1E7QK65;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Proline--tRNA ligase {ECO:0000256|ARBA:ARBA00019110};
DE            EC=6.1.1.15 {ECO:0000256|ARBA:ARBA00012831};
DE   AltName: Full=Prolyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029731};
DE   Flags: Fragment;
GN   ORFNames=BIY23_04745 {ECO:0000313|EMBL:OEY86858.1};
OS   Wolbachia pipientis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia.
OX   NCBI_TaxID=955 {ECO:0000313|EMBL:OEY86858.1, ECO:0000313|Proteomes:UP000175679};
RN   [1] {ECO:0000313|EMBL:OEY86858.1, ECO:0000313|Proteomes:UP000175679}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=wPpe {ECO:0000313|Proteomes:UP000175679};
RA   Brown A.M., Wasala S.K., Howe D.K., Peetz A.B., Zasada I.A., Denver D.R.;
RT   "Genomic evidence for plant-parasitic nematodes as the earliest Wolbachia
RT   hosts.";
RL   Submitted (SEP-2016) 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:OEY86858.1}.
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DR   EMBL; MJMG01000003; OEY86858.1; -; Genomic_DNA.
DR   RefSeq; WP_070064911.1; NZ_MJMG01000003.1.
DR   AlphaFoldDB; A0A1E7QK65; -.
DR   OrthoDB; 9809052at2; -.
DR   Proteomes; UP000175679; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; cd00779; ProRS_core_prok; 1.
DR   Gene3D; 3.40.50.800; Anticodon-binding domain; 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; IPR002316; Pro-tRNA-ligase_IIa.
DR   InterPro; IPR004500; Pro-tRNA-synth_IIa_bac-type.
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; 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   4: Predicted;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:OEY86858.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000175679}.
FT   DOMAIN          33..327
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   NON_TER         383
FT                   /evidence="ECO:0000313|EMBL:OEY86858.1"
SQ   SEQUENCE   383 AA;  43878 MW;  1AE21D29B5907CC2 CRC64;
     MYLSKYYLPT LKEAPSDAGI ISHKYSLRAG LIKQVVSGIY TWLPLGLKVL QNIEYIIREE
     MEKSGAIEIL MPCIQPASLW QESGRYNDYG EEMLRINDRG QRNMLFGPTH EEVAIDLIRN
     VVKSYKSLPL YLYQIQWKFR DELRPRFGVM RGREFLMKDA YSFDIDYENA INSYNLMYKT
     YIKIFKRIGL TPIGVRADTG PIGGNLSHEF HILANTGEST LYYDNEFVKL LEDEEIESLR
     HIYAVADDMY NIESCPISQE RLKISKGIEV GHIFYFGDKY SQPMKANITL KSGENVNIHM
     GSYGVGVSRL VGAIIEVFHD SKGIIWPEAV APFKIGLINL HHRTEKCTKI ANELYKAFGG
     NTVLYDDLEE STGIKFARMD LIG
//
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