ID A0A0Q5URE1_9FLAO Unreviewed; 492 AA.
AC A0A0Q5URE1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=ASG38_08390 {ECO:0000313|EMBL:KQS47457.1};
OS Flavobacterium sp. Leaf359.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1736351 {ECO:0000313|EMBL:KQS47457.1, ECO:0000313|Proteomes:UP000051024};
RN [1] {ECO:0000313|Proteomes:UP000051024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf359 {ECO:0000313|Proteomes:UP000051024};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf359 {ECO:0000313|Proteomes:UP000051024};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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|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:KQS47457.1}.
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DR EMBL; LMPW01000012; KQS47457.1; -; Genomic_DNA.
DR RefSeq; WP_056069973.1; NZ_LMPW01000012.1.
DR AlphaFoldDB; A0A0Q5URE1; -.
DR STRING; 1736351.ASG38_08390; -.
DR OrthoDB; 9809052at2; -.
DR Proteomes; UP000051024; 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; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000051024}.
FT DOMAIN 27..295
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 492 AA; 55705 MW; E2FAE1FDEF209631 CRC64;
MSKNLTKRSE DYSKWYNELV VKADLAENSG VRGCMVIKPY GYAIWEKMQA ELDRMFKETG
HQNAYFPLFV PKSMFEAEEK NAEGFAKECA IVTHYRLKND PDKPGKLMVD PNARLEEELI
VRPTSEAIIW STYKGWVQSY RDLPLLINQW ANVVRWEMRT RLFLRTAEFL WQEGHTAHAT
QSEAIAESEQ MMNVYADFVQ NFMAIPVIKG VKTETERFAG AVETYCIEAL MQDGKALQAG
TSHFLGQNFA KAFDVKFANA EGKQEHVWGT SWGVSTRLMG ALVMTHSDDN GLVLPPNLAP
IQVVIVPIYK TDEEFAAITE AANTLVSQLR KLRISVKFDD RTTQKPGFKF AEWELKGVPV
RVAVGPKDLE NGTFEVARRD TLSKEVVLKD NIVNHINGLL EEIQDSLFSK ALDYRDTHIT
EVNSFDEFKD VLENKGGFIA AHWDGTPETE EKIKDLTKAT IRCIALDRVE ESGSCVFTGK
PSVGRVLFAK AY
//
