ID R4XGV7_TAPDE Unreviewed; 427 AA.
AC R4XGV7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Threonyl/alanyl tRNA synthetase SAD domain-containing protein {ECO:0000259|SMART:SM00863};
GN ORFNames=TAPDE_004050 {ECO:0000313|EMBL:CCG83733.1};
OS Taphrina deformans (strain PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563
OS / JCM 9778 / NBRC 8474) (Peach leaf curl fungus) (Lalaria deformans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Taphrinomycetes;
OC Taphrinales; Taphrinaceae; Taphrina.
OX NCBI_TaxID=1097556 {ECO:0000313|EMBL:CCG83733.1, ECO:0000313|Proteomes:UP000013776};
RN [1] {ECO:0000313|EMBL:CCG83733.1, ECO:0000313|Proteomes:UP000013776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563 / JCM 9778 /
RC NBRC 8474 {ECO:0000313|Proteomes:UP000013776};
RX PubMed=23631913; DOI=10.1128/mBio.00055-13;
RA Cisse O.H., Almeida J.M.G.C.F., Fonseca A., Kumar A.A., Salojaervi J.,
RA Overmyer K., Hauser P.M., Pagni M.;
RT "Genome sequencing of the plant pathogen Taphrina deformans, the causal
RT agent of peach leaf curl.";
RL MBio 4:e00055-e00013(2013).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Alax-L subfamily. {ECO:0000256|ARBA:ARBA00008429}.
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:CCG83733.1}.
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DR EMBL; CAHR02000173; CCG83733.1; -; Genomic_DNA.
DR AlphaFoldDB; R4XGV7; -.
DR STRING; 1097556.R4XGV7; -.
DR VEuPathDB; FungiDB:TAPDE_004050; -.
DR eggNOG; KOG2105; Eukaryota.
DR Proteomes; UP000013776; Unassembled WGS sequence.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:UniProt.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0043039; P:tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 2.40.30.130; -; 1.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR012947; tRNA_SAD.
DR PANTHER; PTHR43462; ALANYL-TRNA EDITING PROTEIN; 1.
DR PANTHER; PTHR43462:SF1; ALANYL-TRNA EDITING PROTEIN AARSD1; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000013776}.
FT DOMAIN 215..261
FT /note="Threonyl/alanyl tRNA synthetase SAD"
FT /evidence="ECO:0000259|SMART:SM00863"
FT COILED 297..324
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 427 AA; 46993 MW; D0F4A95CE0195E49 CRC64;
MGLGLKKRTF CPHGVLNGTN EAKRVVGNLA CQHDTYLQRL STTVCDCQKN SLKKPSKDEA
YEVQFLDTIL FPEGGGQPWD HGSVVAMKDG QPTEIPVRKV LRRKLEAIHY VPTPIEVGTQ
VELKLDFDRR FDQAQQHSGQ HLLSAVLDTL DIPTLAWSMG PELVYIEVPR LPEDLKAVER
QCNKHIADNL TITVTETRER PKNLPADYDA SAGVIRVVSI GGIDANPCCG THVRSTAELN
SLTILYTNPI KGANRNNHRI YFVVGGRCQK LLSEVHGNAR TMGANLSCQI SDLPEKITVM
QNQLKELMKR EKNLKSDLVQ FDSQVVRAKL EKTGKAYLHK PTGDIEYLNA LLAALPNPIP
GICVLVAGER DGGPIVITGE ETQVKELSAR VKQALPAMKG GGRPQKFQGK VAAYAAKDLV
FLGNLLD
//
