ID A0A2T4GZ25_FUSCU Unreviewed; 534 AA.
AC A0A2T4GZ25;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=asparagine--tRNA ligase {ECO:0000256|ARBA:ARBA00012816};
DE EC=6.1.1.22 {ECO:0000256|ARBA:ARBA00012816};
GN ORFNames=FCULG_00010751 {ECO:0000313|EMBL:PTD08816.1}, HYE67_004691
GN {ECO:0000313|EMBL:QPC62460.1};
OS Fusarium culmorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5516 {ECO:0000313|EMBL:PTD08816.1, ECO:0000313|Proteomes:UP000241587};
RN [1] {ECO:0000313|EMBL:PTD08816.1, ECO:0000313|Proteomes:UP000241587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV {ECO:0000313|EMBL:PTD08816.1,
RC ECO:0000313|Proteomes:UP000241587};
RA Schmidt R.;
RT "Fusarium culmorum secondary metabolites in fungal-bacterial-plant
RT interactions.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QPC62460.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Class2-1B {ECO:0000313|EMBL:QPC62460.1};
RA Yuan Z.;
RT "The chromosome-scale genome resource for two endophytic Fusarium species:
RT F. culmorum and F. pseudograminearum.";
RL Submitted (NOV-2020) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; PVEM01000004; PTD08816.1; -; Genomic_DNA.
DR EMBL; CP064748; QPC62460.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4GZ25; -.
DR OMA; DNMDLAE; -.
DR Proteomes; UP000241587; Unassembled WGS sequence.
DR Proteomes; UP000663297; Chromosome 2.
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, ECO:0000313|EMBL:PTD08816.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000241587}.
FT DOMAIN 184..524
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 114..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 534 AA; 60287 MW; 63F050DC944FDD1A CRC64;
MRSFRASRVP KTVRQWPQRR SYAVRVPGEC QKDIKTVAEL KAWGPSSPVP DVEVSGWVRS
VRKSSGVRFI DITDGSSMRP VQVVVDKSLA ADMRPGAAVR LKGTWVDESG KKTLASSSAH
LPDTKGECET STSPEQPELK VSEVEILGGS DPMTYPIQNK YQSPESLRTI SHLRSRTPLN
STMLRLRSDA TAMLTQFFFR ERFQQTHPPI ITSSDCEGAG EAFVVKASSP DEFFRAPKYL
TVSSQLHLEA LAQSLGNVWT LSPTFRAEQS DTSRHLSEFY MLEAEMSFVD DMNEVMNLAQ
RMLNSLTSGL KELNAAKELE KNRVDSKEPS ERLAFKDLVE QKQLDRRWRG MLTTKTWPRI
TYSEAIEILK PIADQFEHRP QWGAGLQSEH EKYLAEKIGY DEATDAYVPV FITQYPRDIK
AFYMRQSSSS PSSGLTVDCF DLLVPNMGEL AGGSMREHRL PQLKENMRAL GLEVPRKHSA
GGKEMAWYLD LRRWGCPPHG GFGLGFDRLL SYLSGVPNVR DVVPFPRHYH RCDC
//
