ID A0A0K1W2H6_9MOLU Unreviewed; 474 AA.
AC A0A0K1W2H6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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:AKX34535.1};
GN ORFNames=SLITO_v1c09240 {ECO:0000313|EMBL:AKX34535.1};
OS Spiroplasma litorale.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=216942 {ECO:0000313|EMBL:AKX34535.1, ECO:0000313|Proteomes:UP000067476};
RN [1] {ECO:0000313|EMBL:AKX34535.1, ECO:0000313|Proteomes:UP000067476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN-1 {ECO:0000313|EMBL:AKX34535.1,
RC ECO:0000313|Proteomes:UP000067476};
RX PubMed=26430038;
RA Lo W.S., Lai Y.C., Lien Y.W., Wang T.H., Kuo C.H.;
RT "Complete Genome Sequence of Spiroplasma litorale TN-1T (DSM 21781), a
RT Bacterium Isolated from a Green-Eyed Horsefly (Tabanus nigrovittatus).";
RL Genome Announc. 3:e01116-15(2015).
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|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; CP012357; AKX34535.1; -; Genomic_DNA.
DR RefSeq; WP_075058623.1; NZ_CP012357.1.
DR AlphaFoldDB; A0A0K1W2H6; -.
DR STRING; 216942.SLITO_v1c09240; -.
DR KEGG; sll:SLITO_v1c09240; -.
DR PATRIC; fig|216942.3.peg.940; -.
DR OrthoDB; 9809052at2; -.
DR Proteomes; UP000067476; 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; 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};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_01571}; Reference proteome {ECO:0000313|Proteomes:UP000067476}.
FT DOMAIN 36..283
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 474 AA; 54390 MW; 43A3896FDA406BB8 CRC64;
MAQKLEKITS RDIDFTRWYT DVVKNAKLMD YGQVKGTMIL KPNGYAIWEK IQENLDKKFK
SLGVKNVYFP LLIPESLFNK EKKHVEGFAP ELATVTMVGD KDLGEKLFIR PTSEVLIADF
LEKEIKSYRD LPIKYNQWVN VLRWEKTTRP FLRSSEFLWQ EGHTFHDSAE EAKKMTLDIL
EVYKSFVKEI LLIPVIDGQK TEHEKFAGAK ETYTIESIMY DGQALQSGTS HFFGDNFSKA
FNIKFQNKNQ KEENAYSTSW GVSTRLIGAL IMTHGDDNGL ILPSKIAPTQ ISIIAVNNSE
QIIDTCKELK SQLEDMYRVE IDNTDKSFGF KMAESEIQGI PLRIEVGPKD LADNNVTISD
RLHNNKVKVK LSEVKNNVIS IIDKYDLELK NRAIKNLESK IFKATTFEKY INIINSTPGF
VSVPFCGEIE CENNIKQESS TVSRCIKDFD VNDGELCFKC NKNAKMHTYF ARSY
//
