ID K2RC45_MACPH Unreviewed; 563 AA.
AC K2RC45;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=proline--tRNA ligase {ECO:0000256|ARBA:ARBA00012831};
DE EC=6.1.1.15 {ECO:0000256|ARBA:ARBA00012831};
DE AltName: Full=Prolyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029731};
GN ORFNames=MPH_10763 {ECO:0000313|EMBL:EKG12133.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG12133.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG12133.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG12133.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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 -!- 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:EKG12133.1}.
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DR EMBL; AHHD01000458; EKG12133.1; -; Genomic_DNA.
DR AlphaFoldDB; K2RC45; -.
DR STRING; 1126212.K2RC45; -.
DR VEuPathDB; FungiDB:MPH_10763; -.
DR eggNOG; KOG4163; Eukaryota.
DR HOGENOM; CLU_001882_4_1_1; -.
DR InParanoid; K2RC45; -.
DR OrthoDB; 2733051at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:InterPro.
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; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129}.
FT DOMAIN 81..338
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 563 AA; 63589 MW; 621884E534D9F784 CRC64;
MASEQPATTA LPEHKKDGGK RKEKKDPQQK KEKPQQKPQQ KKKVEGAALI GIDVAKEDDL
GEWYQQVLTK GGMLAYYDVA GCYILKPSSY AIWESIQAWF NERIKKMGVK NCYFPIFISA
DNLQREKDHV EGFAAEVAWV TKGGKSDLEK PVAVRPTSET AMYPYFANEI RSHRDLPLKL
NQWNNVVRWE FKHPMPFIRS REFLWQEGHT AHLTKEQAGE EVLQILDYYA GVYQELLACP
VVKGVKTENE KFPGAEYTTT IEGYIPATGR GIQAATSHCL GQHFSKMFDI TVEDPSPVKE
GESKKPPINV WQNSWGLTTR SIGVMVLTHS DNKGLVIPPR VADIQVVVIP VGITAKTTAE
DREALYKETE AIAEVLRSVN IRVEVDMREG YSPGWKFNDW ELKGVPLRIE FGPKDREKHS
VMYSRRDREG KGPILISELD NAIPTLLETI QNDMFQKAKA DFDNARKQIT NWDDFVPALD
NKSVCLIPHC LGGECEDEIK ELSARKNETP GEAQDARAPS MGAKSLCIPY EQPKESLAEG
ETKCLNPNCQ AKAQKWVLFG RSY
//
