ID A0A0A7LKA5_9BACT Unreviewed; 491 AA.
AC A0A0A7LKA5;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, 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=PK28_02565 {ECO:0000313|EMBL:AIZ62843.1};
OS Hymenobacter sp. DG25B.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1385664 {ECO:0000313|EMBL:AIZ62843.1, ECO:0000313|Proteomes:UP000030789};
RN [1] {ECO:0000313|EMBL:AIZ62843.1, ECO:0000313|Proteomes:UP000030789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG25B {ECO:0000313|EMBL:AIZ62843.1,
RC ECO:0000313|Proteomes:UP000030789};
RA Jung H.-Y., Kim M.K., Srinivasan S., Lim S.;
RT "Hymenobacter radioresistens genome sequence.";
RL Submitted (NOV-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|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}.
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DR EMBL; CP010054; AIZ62843.1; -; Genomic_DNA.
DR RefSeq; WP_044511095.1; NZ_CP010054.1.
DR AlphaFoldDB; A0A0A7LKA5; -.
DR STRING; 1385664.PK28_02565; -.
DR KEGG; hyd:PK28_02565; -.
DR HOGENOM; CLU_001882_4_2_10; -.
DR OrthoDB; 9809052at2; -.
DR Proteomes; UP000030789; 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; 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:UP000030789}.
FT DOMAIN 27..295
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 491 AA; 55864 MW; 512A9AC87EF776D8 CRC64;
MSKSLPKRSE DYSLWYNELV KRAGLAENSA VRGCMVIKPY GYAIWEKMQR TLDDMFKRTG
HQNAYFPLFV PKSLFEAEEK NAEGFAKECA VVTHYRLQTD PDNPGKLRVD PNAKLEEELI
VRPTSEAIIW STYKGWIQSY RDLPLLINQW ANVVRWEMRT RLFLRTAEFL WQEGHTAHAT
AEEALAETRQ MLDVYAEFAE EHLALPVIKG VKTENERFAG ALETYCIEGM MQDGKALQAG
TSHFLGQNFA KAFDVQFANK QGQLEHVWGT SWGVSTRLMG ALVMAHSDDE GLVLPPKLAP
IQVVIVPIYK TGQLDELLER IRPIQMGLIA RGISVKIDDR DTERPGFKFA EWELKGVPVR
MAVGMRDLDA GTVEIARRDT KEKMNLPLAD IVASIDQLLQ DIQQNIYRKA LAFRDTLTTR
VDTYEEFKQV LEGKGGFVVA HYDGTSETEE RIKEETKATI RCLALNEPDE EGICILTGKP
SQRRAYFAKA Y
//
