ID I0JXM2_METFB Unreviewed; 507 AA.
AC I0JXM2;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
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:CCG91991.1};
GN ORFNames=MFUM_280011 {ECO:0000313|EMBL:CCG91991.1};
OS Methylacidiphilum fumariolicum (strain SolV).
OC Bacteria; Verrucomicrobiota; Methylacidiphilae; Methylacidiphilales;
OC Methylacidiphilaceae; Methylacidiphilum (ex Ratnadevi et al. 2023).
OX NCBI_TaxID=1156937 {ECO:0000313|EMBL:CCG91991.1, ECO:0000313|Proteomes:UP000004837};
RN [1] {ECO:0000313|EMBL:CCG91991.1, ECO:0000313|Proteomes:UP000004837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SolV {ECO:0000313|EMBL:CCG91991.1,
RC ECO:0000313|Proteomes:UP000004837};
RX PubMed=22740660; DOI=10.1128/JB.00501-12;
RA Khadem A.F., Wieczorek A.S., Pol A., Vuilleumier S., Harhangi H.R.,
RA Dunfield P.F., Kalyuzhnaya M.G., Murrell J.C., Francoijs K.-J.,
RA Stunnenberg H.G., Stein L.Y., DiSpirito A.A., Semrau J.D., Lajus A.,
RA Medigue C., Klotz M.G., Jetten M.S.M., Op den Camp H.J.M.;
RT "Draft Genome Sequence of the Volcano-Inhabiting Thermoacidophilic
RT Methanotroph Methylacidiphilum fumariolicum Strain SolV.";
RL J. Bacteriol. 194:3729-3730(2012).
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:CCG91991.1}.
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DR EMBL; CAHT01000031; CCG91991.1; -; Genomic_DNA.
DR RefSeq; WP_009059361.1; NZ_CAHT01000031.1.
DR AlphaFoldDB; I0JXM2; -.
DR STRING; 1156937.GCA_000953475_00769; -.
DR eggNOG; COG0442; Bacteria.
DR InParanoid; I0JXM2; -.
DR OrthoDB; 9809052at2; -.
DR Proteomes; UP000004837; 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; 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:UP000004837}.
FT DOMAIN 46..296
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 507 AA; 58069 MW; 982757E57E342F9C CRC64;
MNLRKEFAIS PTRNEDFPEW YQQVVSAADL AENSEVRGCM IIKPWGYALW ERIQKELDQR
IKATGHKNVY FPLFIPLEYL QREAEHVEGF AKECAVVTHH RLEKGPDGKL HPASPLAEPL
VIRPTSETII GAAFSRWIQS YRDLPLLINQ WANVVRWEMR PRLFLRTTEF LWQEGHTAHA
TREEAKEEAL FILKLYEEFM RAYLALPVIT GEKPESERFP GADNTFTLEA LVQDRKAVQV
GTSHFLGQNF SKANNIRFLD SQGKMEFAWT SSWGVSTRLI GTLIMAHGDD NGLVLPPTVS
PIQVVILPLF KKEEEKTKVL DVVNFLAEEI KKLSFAAEPI RVEIDKREIG GGVKSWEWIK
KGVPLRIEIG SQEVSSGLIT LKRRDKGVKE KEQLPAHVFL EKLPQLLSEI QEAIYSRAEN
FLKQNTRLID TKEEFYEFFA SKDSKGNELS GGFAYAHWDG SRETEEKLKE DLKITIRCIP
WDPQNTPGIC PFSGRPSKGR VLFAKAY
//
