ID V4JYC9_9CREN Unreviewed; 485 AA.
AC V4JYC9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=MGAcid_03640 {ECO:0000313|EMBL:ESQ23594.1};
OS uncultured Acidilobus sp. MG.
OC Archaea; Thermoproteota; Thermoprotei; Acidilobales; Acidilobaceae;
OC Acidilobus; environmental samples.
OX NCBI_TaxID=1410573 {ECO:0000313|EMBL:ESQ23594.1, ECO:0000313|Proteomes:UP000017902};
RN [1] {ECO:0000313|EMBL:ESQ23594.1, ECO:0000313|Proteomes:UP000017902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jay Z.J., Rusch D.B., Tringe S.G., Bailey C., Jennings R.M., Inskeep W.P.;
RT "Predominant Acidilobus-like populations from geothermal environments of
RT Yellowstone National Park exhibit similar metabolic potential in different
RT hypoxic microbial communities.";
RL Submitted (OCT-2013) 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:ESQ23594.1}.
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DR EMBL; AYMA01000001; ESQ23594.1; -; Genomic_DNA.
DR AlphaFoldDB; V4JYC9; -.
DR STRING; 1410573.MGAcid_03640; -.
DR PATRIC; fig|1410573.3.peg.342; -.
DR Proteomes; UP000017902; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_01571}.
FT DOMAIN 45..287
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT COILED 372..402
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 485 AA; 56193 MW; F98F349C73871066 CRC64;
MKRVPGPQRK RWQESFSEWF DWVLERAEVY DYGRYPVKGM GVWMPYGFQI RKRVLELIRN
LLDSRGHEEV LFPLLIPDWM LAKESEHIRG FEDEVYWVTH GGLEPLDVKL ALRPTSETPI
TYYESLWIQS YKQLPRRFYQ IVSVFRYETK ATRPMIRLRE VTSFKEAHTV HETFEDAERQ
VLDAIDIYKK FFDSLYIPYL VSKRPDWDKF AGALYTIAFD TIMPDGRTLQ IGTVHNLGQN
FTKAFGFRIQ RSDETFDYPW QTSYGVSDRV VATIIATHGD DLGLVLPSTV APYQVVIVPI
PPSDKDKLDT VLDYARQVLE VTKGVGLRAL LDDRGDLTPG EKYYLWDAKG VPIRIEVGLR
EASSKTVTLV RRVDLSKRVV KLEDLVNELQ KTLRDLDNTL YERAWRFLRE RVLRASSVEE
AKRALDERGG VVELPWCGLE DCAVKAAEQL NAKALGTPWP SEPAEGNCPI CGRPAMTYMR
YARQY
//
