ID A0A0C9LS83_9FUNG Unreviewed; 739 AA.
AC A0A0C9LS83;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=MAM1_0025c02054 {ECO:0000313|EMBL:GAN02610.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN02610.1};
RN [1] {ECO:0000313|EMBL:GAN02610.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN02610.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; DF836314; GAN02610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9LS83; -.
DR STRING; 91626.A0A0C9LS83; -.
DR OrthoDB; 2733051at2759; -.
DR Proteomes; UP000053815; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; 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 Gene3D; 3.90.960.10; YbaK/aminoacyl-tRNA synthetase-associated domain; 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 InterPro; IPR036754; YbaK/aa-tRNA-synt-asso_dom_sf.
DR InterPro; IPR007214; YbaK/aa-tRNA-synth-assoc-dom.
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 Pfam; PF04073; tRNA_edit; 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 SUPFAM; SSF55826; YbaK/ProRS associated domain; 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, ECO:0000313|EMBL:GAN02610.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053815}.
FT DOMAIN 269..516
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 203..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 739 AA; 83092 MW; 533792F5CC88C9B4 CRC64;
MTPYSNKKLV INEDQHQKQL KHKQWQQSQH YKLSISPKTV SHDAVNDSKT WTEALSSNTN
EQYQVTKTLI LKPKTAKTAP ATPVVVIALE STETNATALG KKLSLKDCRF ANEDLLKGTF
GVDKDSVSPF ALSNVQDLSL VHLVVDNAIL ALDAATLLAF HPSAADKTVF VTVDQLKSYF
ASINKEFIDV DFKALAAAKP PATDAKKPAK APKAKKEAAA PSEEANQMGL GCKKEEDFPK
WYQQVLTKSE MLEYYDVSGC YILRPLAYNV WKEITNFFDA EITEMGVEDT YFPMFVSNRV
LEREKDHIEG FAPEVAWVTK AGNSDLEEPI AIRPTSETVM YPYFSKWIRS HRDLPFRINQ
WCSVVRWEFK NPQPFLRTRE FLWQEGHTAH LTLESADVEV KQILDLYEQV YTDLLALPVV
KGVKSEKERF AGGYYTTTVE GFIPTTGRAI QGGTSHCLGQ NFSKMFNITV EDPSAPANAT
EEAKKLHVWQ NSWGLSTRTI GVMVMTHGDD KGLVMPPRVA LIQTVIVPCG LTVKTTKAES
DKIFDACQDV ANRLKKAGLK SKADLRENYT PGFKFNHWEI RGVPLRLEVG PKDLEKNQVT
AVRRDTGAKF AVSLDNLEAG IKEALDTIQR EMYEKAAKKM QESIVRVSKW EDFVPTLNKK
KLLLVPWCDR TECEDDIKER SAKVANEGEE EDDRAPSMGA KSLCNPFNQP TEDPIVPGVT
KCIACEHDAK HFMLFGRSY
//
