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SYIC_NOSCE
ID   SYIC_NOSCE              Reviewed;        1046 AA.
AC   C4V8Q1;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Probable isoleucine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.5;
DE   AltName: Full=Isoleucyl-tRNA synthetase;
DE            Short=IleRS;
GN   ORFNames=NCER_100885;
OS   Nosema ceranae (strain BRL01) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae; Nosema.
OX   NCBI_TaxID=578460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRL01;
RX   PubMed=19503607; DOI=10.1371/journal.ppat.1000466;
RA   Cornman R.S., Chen Y.P., Schatz M.C., Street C., Zhao Y., Desany B.,
RA   Egholm M., Hutchison S., Pettis J.S., Lipkin W.I., Evans J.D.;
RT   "Genomic analyses of the microsporidian Nosema ceranae, an emergent
RT   pathogen of honey bees.";
RL   PLoS Pathog. 5:E1000466-E1000466(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-
CC         isoleucyl-tRNA(Ile); Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666,
CC         Rhea:RHEA-COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58045, ChEBI:CHEBI:78442, ChEBI:CHEBI:78528,
CC         ChEBI:CHEBI:456215; EC=6.1.1.5;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; ACOL01000062; EEQ82400.1; -; Genomic_DNA.
DR   RefSeq; XP_002996071.1; XM_002996025.1.
DR   AlphaFoldDB; C4V8Q1; -.
DR   SMR; C4V8Q1; -.
DR   STRING; 578460.C4V8Q1; -.
DR   PRIDE; C4V8Q1; -.
DR   EnsemblFungi; EEQ82400; EEQ82400; NCER_100885.
DR   KEGG; nce:NCER_100885; -.
DR   VEuPathDB; MicrosporidiaDB:NCER_100885; -.
DR   HOGENOM; CLU_001493_1_1_1; -.
DR   InParanoid; C4V8Q1; -.
DR   OMA; WIDFKDD; -.
DR   Proteomes; UP000009082; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 3.40.50.620; -; 2.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR002301; Ile-tRNA-ligase.
DR   InterPro; IPR023586; Ile-tRNA-ligase_type2.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   PANTHER; PTHR42780; PTHR42780; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00984; TRNASYNTHILE.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00392; ileS; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..1046
FT                   /note="Probable isoleucine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000388380"
FT   MOTIF           46..56
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000250"
FT   MOTIF           615..619
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000250"
FT   BINDING         618
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1046 AA;  122145 MW;  B2FCC7669CD0CEF7 CRC64;
     MKFDSNLSIN DIETKILKFW KDTKCFKKSN ELSKNKKKYT FYDGPPFATG LPHFGHILAG
     TVKDVITRYQ YQHNKRVDRR FGWDCHGLPV EFEIDKNLGI SVKQEILEMG IDKYNAECKS
     IVMKHSSEWK DTVEKMGRWV DFDNSYKTMD LSFMTSVWYV FSQLYKKGYV YRGYRVMPFS
     TGCMTTLSSS EAKSNYKMVN DLSVVVEFPL KSKLFDKKVS ILAWTTTPWT LPSNCGLVVN
     KDFDYQIFEI DHKFYCMLPN RIQDFNKKEV ILHELFKGEL LIGLEYEQPF NYFEEYRRCG
     FFKIIGGSFV SSTDGTGIVH AAPAFGEDDY NCFVENNLIK QNDLVPCPVD ENGKFTAEVF
     DYKGIYVKDA DKLIIKHLKE KIFCVKQISH NYPFCWRSEK PLIYRLVSSW FIKVSDSVDK
     LIKNNEIINW VPKDIKHKKF GKWLSNAKDW AFSRSRFWGT PIPLWVSDDY SEILCVESAE
     ELEKLSGKKI TDLHMEFIDD IILTKNGKTL RRIPEVFDCW FESGCMPYAQ HSWPFRKVDN
     LNCEEIRHHF HDSDNTLVYE NKILENFPAD FIGEGIDQTR GWFYTLHVIS TLLFDKPAFK
     NVIVNGIVLA ENGKKMSKKD KNYPDPNIVM KTFGADSLRM YLISSPVVEA DNLLFKEDGV
     KDVSKLLIIP WMNVLKFYTT SLQKRNDCEK LELDNWINYT FNEFLSSVSN YMNNYQLSKV
     CGLAYKFLDN LSNWYLRIHR EEIRSGNTKI LFNILKKFSV IMSPFAPFFS EYSFQCLLSS
     QQNEKSNSIN SVHFQMYPEA QDSGDNSFEN AKDIIDAIRY LRDKHTISLK TPLKEVKIIS
     DELFMKDAAK FSNTIIRECH VFNLIFVKES EVPELKIEYK AKPCFEYLKK DLKTMNDKIK
     IINKLTQSEI RDLAFLDLSE EKYNVKRENI LIEKKATFPT GLCFASNKFV ILVDNTIDDN
     VLEKKLAREF NSFIQKLRKS CGLKMNDTVN VEVDSEKIKQ ITKKFYPINF STEGQIVSPI
     DSDAQIDVFS YEGQELKVIL RLNKFL
 
 
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