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Database: UniProt
Entry: F2SQV4_TRIRC
LinkDB: F2SQV4_TRIRC
Original site: F2SQV4_TRIRC 
ID   F2SQV4_TRIRC            Unreviewed;       580 AA.
AC   F2SQV4;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
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=TERG_04967 {ECO:0000313|EMBL:EGD88722.1};
OS   Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD88722.1, ECO:0000313|Proteomes:UP000008864};
RN   [1] {ECO:0000313|Proteomes:UP000008864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226}.
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DR   EMBL; GG700652; EGD88722.1; -; Genomic_DNA.
DR   RefSeq; XP_003234375.1; XM_003234327.1.
DR   AlphaFoldDB; F2SQV4; -.
DR   STRING; 559305.F2SQV4; -.
DR   GeneID; 10372929; -.
DR   VEuPathDB; FungiDB:TERG_04967; -.
DR   eggNOG; KOG0555; Eukaryota.
DR   HOGENOM; CLU_004553_2_10_1; -.
DR   InParanoid; F2SQV4; -.
DR   OMA; DCCLYPR; -.
DR   OrthoDB; 347413at2759; -.
DR   Proteomes; UP000008864; 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; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EGD88722.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008864}.
FT   DOMAIN          277..572
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          76..110
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   580 AA;  65467 MW;  ED7ADF574046D6E2 CRC64;
     MASATKDVFI DEDVGQDDDS ATGTETAAYK TLVYAMLLHP ATAEAPVQYM TRKSETGPVA
     EGEEASVRLQ WKPATKSALK KAANLVEQRK KKALKEKELA IREKEEADKR RLVLEEAKKV
     VVKEDDSLPK PVKIRLNEKD PAVVRPRAEG DKQPGTRVRV VGRVHRLRVQ KDMIFLTLTD
     GYGLLQCVFT GDLTKTYDAM TLTLETSMAI HGEMRAVPVK QHAPDNRELH ADFFQVIGRA
     AGDKEAITTR VAADADPQTL LDNRHLVLRG ETSSSVLKVR AAVVRAFRKT FEQKQMLEVT
     PPAMVQTQVE GGSTLFEFDY YGEKAYLTQS SQLYLETCLA SLGDVFCICP SFRAEKSLTR
     RHLSEYTHIE SELDFITFND LLDHIEEIIC SVIDISLADP QIAAFVKQLN PNFTPPARPF
     RRMRYSEAIE WLNEHGINNE EDKPHSFGDD IAEAAERKMT DIINKPILLT HFPAEIKAFY
     MKKDAEDPRV TESVDVLMPG VGEIVGGSMR MDDWDELMGA YKKEGMDPTP YYWYTDQRKY
     GTSPHGGYGL GLERFLAWMC GRYTVRECSL YPRFTGRCTP
//
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