ID K2QUA5_MACPH Unreviewed; 301 AA.
AC K2QUA5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Alanyl-transfer RNA synthetases family profile domain-containing protein {ECO:0000259|PROSITE:PS50860};
GN ORFNames=MPH_09638 {ECO:0000313|EMBL:EKG13356.1};
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:EKG13356.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG13356.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG13356.1,
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:EKG13356.1}.
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DR EMBL; AHHD01000414; EKG13356.1; -; Genomic_DNA.
DR AlphaFoldDB; K2QUA5; -.
DR STRING; 1126212.K2QUA5; -.
DR VEuPathDB; FungiDB:MPH_09638; -.
DR eggNOG; ENOG502S23F; Eukaryota.
DR HOGENOM; CLU_004485_3_0_1; -.
DR InParanoid; K2QUA5; -.
DR OrthoDB; 5490212at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 2.40.30.130; -; 1.
DR InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
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:SF2; THREONYL AND ALANYL TRNA SYNTHETASE SECOND ADDITIONAL DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01411; tRNA-synt_2c; 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.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007129}.
FT DOMAIN 39..284
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 301 AA; 32427 MW; C17F6E411F68DD3C CRC64;
MFGEGNKNLR QDGEPTNTPN IVTSPIIANA PGEKAPGSSS TKLVYQHDDS LREYTTKIVS
VEPISSLAEP DRALVKNASD NDHVVETEET IFYVQGGGQL TDTGSMTADG SGDGSFEVLA
ARKCSDGRVL HFGRFSGSAF TPGQAVKQII DGEKRDLYSR IHDAGHIVGL AVRQVAEEAP
ELNLAEGKAQ HWPGAAHVEF GGHIDGKYKE AIQKKVDGML EKDLPVKVHW WTEKELREKC
VYVAPEMTAP DGELLRAVDI VGAGAYPCGG THVASTKLCG KITVRKISRK SGVSRVSYEA
K
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