ID A0A1E3PEN8_9ASCO Unreviewed; 451 AA.
AC A0A1E3PEN8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=ThrRS/AlaRS common domain-containing protein {ECO:0000313|EMBL:ODQ63402.1};
GN ORFNames=NADFUDRAFT_84523 {ECO:0000313|EMBL:ODQ63402.1};
OS Nadsonia fulvescens var. elongata DSM 6958.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Nadsonia.
OX NCBI_TaxID=857566 {ECO:0000313|EMBL:ODQ63402.1, ECO:0000313|Proteomes:UP000095009};
RN [1] {ECO:0000313|EMBL:ODQ63402.1, ECO:0000313|Proteomes:UP000095009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6958 {ECO:0000313|EMBL:ODQ63402.1,
RC ECO:0000313|Proteomes:UP000095009};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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}.
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DR EMBL; KV454415; ODQ63402.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3PEN8; -.
DR STRING; 857566.A0A1E3PEN8; -.
DR OrthoDB; 5490212at2759; -.
DR Proteomes; UP000095009; 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; 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.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000095009}.
FT DOMAIN 1..295
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
SQ SEQUENCE 451 AA; 49028 MW; 793700B082D69C64 CRC64;
MSKVYASAIV GALACQKDSY LKTLTTKVVS CVALTVPKPS KSKSKVIPPV ETPRYEVEFE
DTILFPEGGG QPSDTGVLHV IESDVTIPVF SVRRDGLVAR HAVPEPLTPG ATVTMNLTWG
RRMDHMQQHT GQHLLSAVLD NYELATLSWS MGAGVQAGGD AILNYLDIPR KLTNDEIKSV
QHEVNEHIQA ALPIRVVVPE SLEDGNTKTH KLPGDYDASK GVIRVIEIGG EEDDTSSKEL
KSKSTRLDHN TCCGTHLSST SQIGSLVLLH QIPHKATQSR LYFIAGDRVP IYMQQCHTKL
RSVNAALSCQ MADIEANLTR ISLQVRDLTS REKFWMSQAA LHEATVLREK LSKSKVAILY
LPEASLDFFN LVIKELGEEP LKQATVVLAG GAGKDGGAIV VAGVNVPDIV NEVLKFAPKA
RGGGKGRWQG KVNEWESGAV ELLVEHITNL A
//
