ID C5A5P1_THEGJ Unreviewed; 483 AA. AC C5A5P1; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAR-2024, entry version 85. 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 ECO:0000313|EMBL:ACS33553.1}; GN OrderedLocusNames=TGAM_1051 {ECO:0000313|EMBL:ACS33553.1}; OS Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=593117 {ECO:0000313|EMBL:ACS33553.1, ECO:0000313|Proteomes:UP000001488}; RN [1] {ECO:0000313|EMBL:ACS33553.1, ECO:0000313|Proteomes:UP000001488} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15229 / JCM 11827 / EJ3 RC {ECO:0000313|Proteomes:UP000001488}; RX PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70; RA Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M., RA Anthouard V., Forterre P., Wincker P., Confalonieri F.; RT "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, RT the most radioresistant organism known amongst the Archaea."; RL Genome Biol. 10:R70.1-R70.23(2007). 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|ARBA:ARBA00004496, CC 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001398; ACS33553.1; -; Genomic_DNA. DR RefSeq; WP_015858667.1; NC_012804.1. DR AlphaFoldDB; C5A5P1; -. DR STRING; 593117.TGAM_1051; -. DR PaxDb; 593117-TGAM_1051; -. DR GeneID; 7986925; -. DR KEGG; tga:TGAM_1051; -. DR PATRIC; fig|593117.10.peg.1048; -. DR eggNOG; arCOG00402; Archaea. DR HOGENOM; CLU_001882_4_2_2; -. DR OrthoDB; 7375at2157; -. DR Proteomes; UP000001488; Chromosome. 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}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_01571}. FT DOMAIN 41..283 FT /note="Aminoacyl-transfer RNA synthetases class-II family FT profile" FT /evidence="ECO:0000259|PROSITE:PS50862" SQ SEQUENCE 483 AA; 56181 MW; 89A3DA57FD926675 CRC64; MAKVKREKWS NEFSEWYNEL LETAGIIDKR YPVKGMNVWL PYGLKIMRNI EKFIHSEMAR TGHEEVLFPA LIPETEFQKE AEHIKGFEDE VYWVTHAGLD PLDVRLILRP TSETAMYSMF SLWIRSHADL PFKVYQIVNV YRYETKHTRP LIRVREISRF FEAHTAHVDF EDAERQIKED LEIFDRLAKF LALPYVISRR PDWDKFPGAF YSLGAEIMMP DGRTLQIGTM HNYKQNFAKA YNIQYETETG DHEYVHQTTF GMSERLLAAV IAVHGDDSGM VLPPTIAPIQ VVIVPIPKKD ANVDVFAYAR EIAEELGKAG FRVHVDERDI RPGRKYYDWE LKGVPLRIEV GPRDVEGRKA VLARRDTFEK VTVERDAIVE EVKKTLDAIH ENLYQRAKEF LESHIKRVDT IEEAKAVFED RRGIVEIPWC GDEECGLKME EELDAKMLGT PYPEEKAREG IEGKKCPVCG REAKFIARFA RTY //