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Database: UniProt
Entry: I4YGS2_WALMC
LinkDB: I4YGS2_WALMC
Original site: I4YGS2_WALMC 
ID   I4YGS2_WALMC            Unreviewed;       429 AA.
AC   I4YGS2;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, 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};
DE   Flags: Fragment;
GN   ORFNames=WALSEDRAFT_59473 {ECO:0000313|EMBL:EIM23164.1};
OS   Wallemia mellicola (strain ATCC MYA-4683 / CBS 633.66) (Wallemia sebi (CBS
OS   633.66)).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC   Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX   NCBI_TaxID=671144 {ECO:0000313|EMBL:EIM23164.1, ECO:0000313|Proteomes:UP000005242};
RN   [1] {ECO:0000313|EMBL:EIM23164.1, ECO:0000313|Proteomes:UP000005242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4683 / CBS 633.66 {ECO:0000313|Proteomes:UP000005242};
RX   PubMed=22326418; DOI=10.1016/j.fgb.2012.01.007;
RA   Padamsee M., Kumar T.K.A., Riley R., Binder M., Boyd A., Calvo A.M.,
RA   Furukawa K., Hesse C., Hohmann S., James T.Y., LaButti K., Lapidus A.,
RA   Lindquist E., Lucas S., Miller K., Shantappa S., Grigoriev I.V.,
RA   Hibbett D.S., McLaughlin D.J., Spatafora J.W., Aime M.C.;
RT   "The genome of the xerotolerant mold Wallemia sebi reveals adaptations to
RT   osmotic stress and suggests cryptic sexual reproduction.";
RL   Fungal Genet. Biol. 49:217-226(2012).
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DR   EMBL; JH668225; EIM23164.1; -; Genomic_DNA.
DR   RefSeq; XP_006956560.1; XM_006956498.1.
DR   AlphaFoldDB; I4YGS2; -.
DR   STRING; 671144.I4YGS2; -.
DR   GeneID; 18473372; -.
DR   KEGG; wse:WALSEDRAFT_59473; -.
DR   eggNOG; KOG0554; Eukaryota.
DR   HOGENOM; CLU_004553_2_0_1; -.
DR   InParanoid; I4YGS2; -.
DR   OMA; VPHAGWG; -.
DR   OrthoDB; 347413at2759; -.
DR   Proteomes; UP000005242; 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:EIM23164.1}; 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:UP000005242}.
FT   DOMAIN          126..421
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EIM23164.1"
SQ   SEQUENCE   429 AA;  48570 MW;  4BE909435B609B17 CRC64;
     MKLPLTIKEI EKLSAKSTVT LNGWIRSVRH QKKLSFANVS DGTADIQVLL PPDSHRGLTT
     GASISVDGTV CQHPRNQSLE IKAESLKLWG ECPGENYPMQ KKDHGSEHLR DNAHLRVRSR
     QIASVIRLRD QLSYNFASWF KDFGFMNVQP PIITSSDCEG AGEVFEVRHP TKSEKFFGRD
     AYLSVSTQLH LEAISSGFSR VYTLSPTFRA EGSQTNRHLA EFWMLEAELS FVEDLETVMQ
     VVENSIKSSV KNLTEHSEGI PSMSVDSDWP RLTYTEAIEI LKKRHEDAPF QYIPEWGASL
     QSEHERYLAD TYYGRPLFVT DYPENIKPFY MRVNDDGKTV SCFDLLAPGI GELAGGSLRE
     ERLQVLEDKM STAGLDRETY EWYVDLRRFG SVPHGGFGIG YERLISALSG VSNLRDVVLF
     PRWAGRCTF
//
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