ID A0A0N0DH03_FUSLA Unreviewed; 534 AA.
AC A0A0N0DH03;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=asparagine--tRNA ligase {ECO:0000256|ARBA:ARBA00012816};
DE EC=6.1.1.22 {ECO:0000256|ARBA:ARBA00012816};
GN ORFNames=FLAG1_02339 {ECO:0000313|EMBL:KPA44751.1};
OS Fusarium langsethiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=179993 {ECO:0000313|EMBL:KPA44751.1, ECO:0000313|Proteomes:UP000037904};
RN [1] {ECO:0000313|EMBL:KPA44751.1, ECO:0000313|Proteomes:UP000037904}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fl201059 {ECO:0000313|EMBL:KPA44751.1,
RC ECO:0000313|Proteomes:UP000037904};
RA Lysoe E., Divon H.H., Terzi V., Orru L., Lamontanara A., Kolseth A.-K.,
RA Frandsen R.J., Nielsen K., Thrane U.;
RT "The draft genome sequence of Fusarium langsethiae, a T-2/HT-2 mycotoxin
RT producer.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KPA44751.1}.
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DR EMBL; JXCE01000022; KPA44751.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0DH03; -.
DR OrthoDB; 2786597at2759; -.
DR Proteomes; UP000037904; Unassembled WGS sequence.
DR GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00776; AsxRS_core; 1.
DR CDD; cd04318; EcAsnRS_like_N; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004522; Asn-tRNA-ligase.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR NCBIfam; TIGR00457; asnS; 1.
DR PANTHER; PTHR22594:SF34; ASPARAGINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:KPA44751.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000037904}.
FT DOMAIN 184..524
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 107..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 534 AA; 60323 MW; 335219534CCA1A44 CRC64;
MRSFRAYRVP KTVRQWPQRR SYAVRVPGEC QKDIKTVAEL KAWGPSSPVP DVEVSGWVRS
VRKSSGVRFI DITDGSSMRP VQVVVDKSLA ADMRPGAAVR LKGTWVDESG GETPIDGSAQ
TPDTKNECET STSPEQPELK VSEVEILGGS DPMTYPIQNK YQSPESLRTI SHLRPRTPLN
STMLRLRSDA TAMLTQFFFR ERFQQTHPPI ITSSDCEGAG EAFAVKASSP DEFFREPKYL
TVSSQLHLEA LAQALGNVWT LSPTFRAEQS DTSRHLSEFY MLEAEISFVD DMNEVMNLAQ
RMLNSLTSGL KELNAAKELE QNRVDSKEPS ERLAFKDLVE QEQLDRRWRG MLTTKTWPRI
TYSEAIEMLE PIADQFEHKP QWGAGLQSEH EKYLAEKIGY DETTDAYVPV FITQYPRDIK
AFYMRQSSSS PSPGLTVDCF DLLVPNMGEL AGGSMREHRL PQLEENMRAL GLEVPSKRSA
GGKELAWYLD LRRWGCPPHG GFGLGFDRLL SYLSGVPNVR DVVPFPRHYH RCDC
//
