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Database: UniProt
Entry: A0A1L8SQ97_9ENTE
LinkDB: A0A1L8SQ97_9ENTE
Original site: A0A1L8SQ97_9ENTE 
ID   A0A1L8SQ97_9ENTE        Unreviewed;       479 AA.
AC   A0A1L8SQ97;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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   ORFNames=RV00_GL000821 {ECO:0000313|EMBL:OJG34289.1};
OS   Enterococcus devriesei.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=319970 {ECO:0000313|EMBL:OJG34289.1, ECO:0000313|Proteomes:UP000183700};
RN   [1] {ECO:0000313|EMBL:OJG34289.1, ECO:0000313|Proteomes:UP000183700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22802 {ECO:0000313|EMBL:OJG34289.1,
RC   ECO:0000313|Proteomes:UP000183700};
RA   Zhong Z., Sun Z., Liu W., Zhang W., Zhang H.;
RT   "Draft genome sequences of 29 type strains of Enterococci.";
RL   Submitted (DEC-2014) 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: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:OJG34289.1}.
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DR   EMBL; JXKM01000014; OJG34289.1; -; Genomic_DNA.
DR   RefSeq; WP_071863171.1; NZ_JXKM01000014.1.
DR   AlphaFoldDB; A0A1L8SQ97; -.
DR   STRING; 319970.RV00_GL000821; -.
DR   OrthoDB; 9809052at2; -.
DR   Proteomes; UP000183700; Unassembled WGS sequence.
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:0016740; F:transferase activity; IEA:UniProt.
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};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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          37..277
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   479 AA;  55115 MW;  6C46DD41EE9133B2 CRC64;
     MTNLQKEDFS KWYLQTIQKA DLMDYSPVRG CIIFKADGWE LWEHIQEDFN KYLKTQDIRN
     VYFPMLIPKH FLEKEEEHVE GFAPELPWLT KVGDEPLEEP YALRPTSETL IGDAFSNWIN
     SYRDLPYEIN QWANVFRWEK KTMPFLRTSE FLWQEGHTAH ESEESARERT MAILEAYATL
     IEDTLAIPVY RGQKTPSERF AGAVDTYSVE AMMRDGKAVQ AGTSHYLGQN FAEAFDIKFL
     NRNNEHEHVY TTSWGISTRL IGSLIMVHGD EQGLVLPPKV APTQVILVPV GPWQKNPEIL
     DRLKELKASL AQKDLRVRID TTDNTPGFKF NEWELKGAAL RVEFGPRDLE NNQAVIKMRD
     LNDKESVSLD GIEDYIVEQL DVMQKRLFDS AVKRYEANEH TDIDTLDELK AHIEKSKAAG
     EVPGFVLIGW DGTEETEAKI KEETGFTTRN IPFNPPVEKT VDIVSGKPAK HTVWIARAY
//
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