ID V5EHX7_KALBG Unreviewed; 734 AA.
AC V5EHX7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, 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=PSEUBRA_SCAF1g00634 {ECO:0000313|EMBL:EST10206.1};
OS Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST10206.1, ECO:0000313|Proteomes:UP000019377};
RN [1] {ECO:0000313|Proteomes:UP000019377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA Goldman G.H.;
RT "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT high producer of endo-1,4-xylanase isolated from an insect pest of
RT sugarcane.";
RL Genome Announc. 1:E0092013-E0092013(2013).
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; KI545851; EST10206.1; -; Genomic_DNA.
DR RefSeq; XP_016295195.1; XM_016436196.1.
DR AlphaFoldDB; V5EHX7; -.
DR STRING; 1365824.V5EHX7; -.
DR GeneID; 27418825; -.
DR eggNOG; KOG4163; Eukaryota.
DR HOGENOM; CLU_001882_4_1_1; -.
DR OMA; EVYWVTH; -.
DR OrthoDB; 2733051at2759; -.
DR Proteomes; UP000019377; 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 ECO:0000313|EMBL:EST10206.1}; 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:UP000019377}.
FT DOMAIN 266..513
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 186..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 734 AA; 81090 MW; EC406452CD1B21EE CRC64;
MEAISSALSA LSIQTEKVVK HAAANSPESW RSAVSDVAST LGFPTSNYTK TVVFKPKTAK
TATPTPVVLI AKDDSEYNTG AVAKHIGQKE MRLAAPEVLK EFLNATKDDV SALSITKDNA
SQLIAVLDAS LATSTEHFAV HAASSEETLF MSGAEITKYL QSTGVKLEVV DFAKLKAEAA
TPVAKASAPS SSSASAPGST QGPIPASSKA KAAEAAKIPD AEQIGITVRK AGDFSEWYSQ
VLRKGDMLDY YDVSGCYILK PWSYFVWQSI QNFFDAEIKK IGVENCYFPM FVSADVLERE
KDHIEGFAPE VAWVTKAGNS DLERPVAIRP TSETVMYPYY AKWIQSHRDL PLKLNQWNSV
VRWEFKHPQP FLRTREFLWQ EGHTAHMTLE QADEEVMHIL DLYRQVYEKL LAVPVVPGVK
SEKEKFAGGY YTTTVEGFVP TTGRGIQGGT SHCLGQNFSK MFNITVEDPK AAEEHRGKDE
GKLHVWQNSW GLSTRTIGVM VMVHGDDDGL VMPPRVAQVQ VVIIPCGIGV KTTPAEKEAI
MDACDQTAKD LKAAGIRAKA DLRDNYSPGF KFNDWEMRGV PIRLEIGPKD LEKKSVVSVR
RDNKAKAPLS VEGLSESIAK LLDTIHDDMF AKADAEYRSR RKVCEQWDDF TSILNDKCHV
VIPWCEVEAC EDEIKKRSAR QATAGEAEDE KAPSMGAKSL CIPFDQKQFG EVKGKKCPQC
GKDAKRWTMF GRSY
//
