ID A0A2I1FX79_9GLOM Unreviewed; 565 AA.
AC A0A2I1FX79;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=asparagine--tRNA ligase {ECO:0000256|ARBA:ARBA00012816};
DE EC=6.1.1.22 {ECO:0000256|ARBA:ARBA00012816};
DE AltName: Full=Asparaginyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029886};
GN ORFNames=RhiirA4_392786 {ECO:0000313|EMBL:PKY38991.1};
OS Rhizophagus irregularis.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=588596 {ECO:0000313|EMBL:PKY38991.1, ECO:0000313|Proteomes:UP000234323};
RN [1] {ECO:0000313|EMBL:PKY38991.1, ECO:0000313|Proteomes:UP000234323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4 {ECO:0000313|EMBL:PKY38991.1,
RC ECO:0000313|Proteomes:UP000234323};
RA Ropars J., Sedzielewska K., Noel J., Charron P., Farinelli L., Marton T.,
RA Kruger M., Pelin A., Brachmann A., Corradi N.;
RT "Genome analyses suggest a sexual origin of heterokaryosis in a supposedly
RT ancient asexual fungus.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-
CC asparaginyl-tRNA(Asn); Xref=Rhea:RHEA:11180, Rhea:RHEA-COMP:9659,
CC Rhea:RHEA-COMP:9674, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78515, ChEBI:CHEBI:456215; EC=6.1.1.22;
CC Evidence={ECO:0000256|ARBA:ARBA00000422};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
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:PKY38991.1}.
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DR EMBL; LLXI01000047; PKY38991.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I1FX79; -.
DR VEuPathDB; FungiDB:FUN_005631; -.
DR VEuPathDB; FungiDB:GLOIN_2v1536882; -.
DR VEuPathDB; FungiDB:RhiirA1_427839; -.
DR OrthoDB; 347413at2759; -.
DR Proteomes; UP000234323; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd04323; AsnRS_cyto_like_N; 1.
DR CDD; cd00776; AsxRS_core; 1.
DR Gene3D; 3.30.1910.20; asparaginyl-tRNA synthetase, N-terminal domain; 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; IPR048952; AsnRS_N.
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:SF16; ASPARAGINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF20917; AsnRS_N; 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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:PKY38991.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000234323}.
FT DOMAIN 265..557
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 67..120
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 565 AA; 64311 MW; 860D8B8F040D36A9 CRC64;
MAETLQKPSV KSSETVYIDE VNGSDETSTG TQNAPYKTAV RALQVKGDNI SILVRKTPEE
GYKDISGTAL KKAKKRVEEL AKKAKKEDEK KKAEAEKVKL QREEEERKLE EAKKIVLKQD
PNLPLAIKIK IRQSVASRGK RVKVSGWVHR LRTQGKDMKF IVLRDGSGYL QCLLTGELCH
TYDALILSLE STVTIYGVIS ELPAGKTAPD NHELLADYWE VTHHAPGGDD AFTNKLNADA
DPSILYEQRH LVIRGETASA VLKARSAIMK AFRDHFDSKG FTEVNPPCMV QTQVEGGSTL
FEMNYYGEKA YLTQTSQLYL ETCLPSLGDV YCISESYRAE KSHTRRHLSE YSHLEAEMAF
ITFDDLLDTL EDLICDTIDR VLANETTRKL VYQLHPDFVP PQRPFLRMDY KDAIQYLKDH
NIKKENGSFY EFGEDIPEFP ERTMTDQINK PIFLCRFPAE IKAFYMKRCA EDNRVTESVD
VLIPGVGEVV GGSMRISDMN ELLAGYKREG INPTPYYWYT DQRKYGTTEH GGFGLGVERF
LAWLLHRDNV KECCLYPRFM GRCLP
//
