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Database: UniProt
Entry: F9FHM8_FUSOF
LinkDB: F9FHM8_FUSOF
Original site: F9FHM8_FUSOF 
ID   F9FHM8_FUSOF            Unreviewed;       506 AA.
AC   F9FHM8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=asparagine--tRNA ligase {ECO:0000256|ARBA:ARBA00012816};
DE            EC=6.1.1.22 {ECO:0000256|ARBA:ARBA00012816};
GN   ORFNames=FOXB_05907 {ECO:0000313|EMBL:EGU83497.1};
OS   Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU83497.1};
RN   [1] {ECO:0000313|EMBL:EGU83497.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU83497.1};
RX   PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA   Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT   "A highly conserved effector in Fusarium oxysporum is required for full
RT   virulence on Arabidopsis.";
RL   Mol. Plant Microbe Interact. 25:180-190(2012).
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:EGU83497.1}.
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DR   EMBL; AFQF01001831; EGU83497.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9FHM8; -.
DR   STRING; 660025.F9FHM8; -.
DR   PaxDb; 5507-FOXG_12729P0; -.
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   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}.
FT   DOMAIN          166..496
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          85..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   506 AA;  57314 MW;  712904CB2321B64B CRC64;
     MAPNKTKDIK TVAELKAWGP TSHVPDVEVC GWVRSVRKSS GVRFIDITDG SSMRPVQVVV
     DKNLATDMRP GAAVRLKGTW VDESRKQSDI EEISQASSED ETSTGSEQPE LKVSEVEVLG
     GSDPMTYPIQ NKYQTPESLR TISHLRPRTP LNSTMLRFRS DSTAMLTQFF FRERFQQTHP
     PIITSSDCEG AGEAFAVKAS SPDEFFRDPK YLTVSSQLHL EALAQALGNV WTLSPTFRAE
     QSDTSRHLSE FYMLEAEMSF VDNMEEVMNL AQRMLNSMAS GLKELNAAKE LEQNRFDSKE
     PSERLAFNDL IDQKQLDRRW RGMLTTKTWP RITYSEALEI LKPIADQFEH KPTWGSGLQS
     EHEKYLAEKI GYDKATDAYV PIFITQYPRD IKAFYMRQSS SSPASGLTVD CFDLLVPHLG
     ELAGGSMREH RLPQLEENMR ALGLEVPSKR SDKGKELAWY LDLRRWGCPP HGGFGLGFDR
     LLSYLTGVPN VRDVVPFPRH YHRCDC
//
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