ID A0A246JNI1_9SPHN Unreviewed; 508 AA.
AC A0A246JNI1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=CDQ92_18730 {ECO:0000313|EMBL:OWQ94053.1};
OS Sphingopyxis bauzanensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=651663 {ECO:0000313|EMBL:OWQ94053.1, ECO:0000313|Proteomes:UP000197361};
RN [1] {ECO:0000313|EMBL:OWQ94053.1, ECO:0000313|Proteomes:UP000197361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22271 {ECO:0000313|EMBL:OWQ94053.1,
RC ECO:0000313|Proteomes:UP000197361};
RX PubMed=20023054; DOI=10.1099/ijs.0.018218-0;
RA Zhang D.C., Liu H.C., Xin Y.H., Zhou Y.G., Schinner F., Margesin R.;
RT "Sphingopyxis bauzanensis sp. nov., a psychrophilic bacterium isolated from
RT soil.";
RL Int. J. Syst. Evol. Microbiol. 60:2618-2622(2010).
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:OWQ94053.1}.
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DR EMBL; NISK01000005; OWQ94053.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A246JNI1; -.
DR OrthoDB; 9809052at2; -.
DR Proteomes; UP000197361; 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 PANTHER; PTHR43382:SF2; BIFUNCTIONAL GLUTAMATE_PROLINE--TRNA LIGASE; 1.
DR PANTHER; PTHR43382; PROLYL-TRNA SYNTHETASE; 1.
DR Pfam; PF03129; HGTP_anticodon; 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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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:UP000197361}.
FT DOMAIN 4..295
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 508 AA; 56442 MW; DA592D2EA7243ACD CRC64;
MVKHALSVTR QADFAAWYQD VIAEADLAEE SGVRGCMVIK PWGYGIWERI QTVMDAAIKD
AGVQNCYFPL FIPLSFFEKE ADHVDGFAKE MAVVTHHRLI QDGKGKLIPD PEAKLEEPLI
VRPTSETVIG AAMSRWVQSW RDLPLKVNQW ANVVRWEMRT RMFLRTSEFL WQEGHTAHAD
KADAMAETLR ALEMYRAFAE DVLAMPVVAG EKPENERFPG AVATYSIEAM MQDGKALQAG
TSHYLGTGFA EAAGIRYQDK DGGHSLCHTT SWGTSTRMIG GVIMTHGDDD GLRCPPRIAP
HQIVIVPMLR DNEEDQAILD YCAALQAELK TLDAFREPLR VHLDAGANKA QTKRWGWVKK
GAPVILEIGP RDVAGGNVAV IRRDRLYKDD GKLNSAFIAK GDFVGQAVAT LEDIQTSLHA
EAKQRLDANI RRDVTDLAAH FKGDDKFVGW AEVQWSRPTG AALDKIVEQL KAFKLTMRNT
PLDAAPADGK CFFTGEPAIE RVLVGRTY
//
