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Database: UniProt
Entry: A0A117LH50_9CHLR
LinkDB: A0A117LH50_9CHLR
Original site: A0A117LH50_9CHLR 
ID   A0A117LH50_9CHLR        Unreviewed;       477 AA.
AC   A0A117LH50;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   13-SEP-2023, entry version 28.
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=XD73_0160 {ECO:0000313|EMBL:KUK46963.1};
OS   Anaerolinea thermophila.
OC   Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC   Anaerolinea.
OX   NCBI_TaxID=167964 {ECO:0000313|EMBL:KUK46963.1, ECO:0000313|Proteomes:UP000064249};
RN   [1] {ECO:0000313|EMBL:KUK46963.1, ECO:0000313|Proteomes:UP000064249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=46_16 {ECO:0000313|EMBL:KUK46963.1};
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
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:KUK46963.1}.
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DR   EMBL; LGFU01000003; KUK46963.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A117LH50; -.
DR   PATRIC; fig|167964.4.peg.510; -.
DR   Proteomes; UP000064249; 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:0006433; P:prolyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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: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..281
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   477 AA;  54312 MW;  EB265456E31474F1 CRC64;
     MSNDSLTAQN ENFSEWYNQI IQKAELADYA PVRGCMVVRP YGWALWENIQ KALDARFKAT
     GHQNAAFPLF IPMSFLEKEK EHVEGFSPEL AVVTHGGGQE LEEPLVVRPT SETIIGYMYS
     KWIKSYRDLP VLINQWANVV RWEMRTRLFL RTLEFYWQEG HTAHATAAEA EEETLRMLHI
     YEDFAVNEAA IPVITGMKSE TEKFAGAVHS YTIEAMMGDT KALQSGTSHN LGQNFAKAFD
     IQYLDTQNQL QYCWTTSWGL STRFVGAIIM THGDDQGLIL PPRLAPIQVV IVPIFRNEDE
     QQKVMEYAEK VKNALSAFRI TLDDRFEQTP GYKFNDWEMR GVPLRIEIGP RDVANDKVVI
     ARRDIPGKAG KSFVEFNALP QTVQQLLDEL HLSMLQKATD FRDEHIINAA SYDELKEAVQ
     NGWAYSHWCE SKACEAKIKE DTKATIRCIP LSQEHTKGTC VVCGKATNTK AYFAKAY
//
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