ID A1C7T2_ASPCL Unreviewed; 441 AA.
AC A1C7T2;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Cofactor for methionyl-and glutamyl-tRNA synthetases, putative {ECO:0000313|EMBL:EAW14453.1};
GN ORFNames=ACLA_074910 {ECO:0000313|EMBL:EAW14453.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW14453.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW14453.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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DR EMBL; DS027045; EAW14453.1; -; Genomic_DNA.
DR RefSeq; XP_001275879.1; XM_001275878.1.
DR AlphaFoldDB; A1C7T2; -.
DR STRING; 344612.A1C7T2; -.
DR EnsemblFungi; EAW14453; EAW14453; ACLA_074910.
DR GeneID; 4707500; -.
DR KEGG; act:ACLA_074910; -.
DR VEuPathDB; FungiDB:ACLA_074910; -.
DR eggNOG; KOG2241; Eukaryota.
DR HOGENOM; CLU_009710_6_6_1; -.
DR OMA; EYEGQVC; -.
DR OrthoDB; 1341752at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd10304; GST_C_Arc1p_N_like; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR002547; tRNA-bd_dom.
DR PANTHER; PTHR11586; TRNA-AMINOACYLATION COFACTOR ARC1 FAMILY MEMBER; 1.
DR PANTHER; PTHR11586:SF33; TYROSINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR Pfam; PF01588; tRNA_bind; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50886; TRBD; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00209};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|PROSITE-
KW ProRule:PRU00209}.
FT DOMAIN 241..365
FT /note="TRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS50886"
FT REGION 165..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 441 AA; 47019 MW; DE0C40CB5FAC542B CRC64;
MAVPSAPESS LLSLLYRSYP TAVSPDATEL DLLHASSKIF PETTLSVEDQ AAIKQWLATN
AGLQTALSKD EKSVVDSILA QLNTHLATRT TLLGTKPSVA DVAVYAQLGP LVEKWTPEER
TGEKGYHHIV RHVDFVQNSR LFSLQIPEEE KVKIDVTDVR FVPKPVDPKE EKERKKREKA
AAQNPEAGKP LVVGQGKPEK AAKGPEEAGA AGAPPKTNKK EKKEKKEKAP KPAPAPAAPP
SPSLIDLRVG HILRAINHPN ADSLYVSTID CGDAPGTDNT SLDEATGKTV RTVCSGLNGL
IPLEEMQNRK IVAVCNLKPV TMRGIKSCAM VLAASPRVAE GEDSHAGPVE LVNPPADAPA
GTRIGFEGWL EGEPEKVLNP KKKVWETFQP GFTTTDDLEV AFEASAVPAV QGQEGKPALG
KLVALTGGVC TVKSLKGATV R
//