| Tag | Content |
|---|
| CPLM ID | CPLM-013200 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Isoleucine--tRNA ligase |
Protein Synonyms/Alias | Isoleucyl-tRNA synthetase; IleRS |
Gene Name | ileS |
Gene Synonyms/Alias | BSU15430 |
Created Date | July 27, 2013 |
Organism | Bacillus subtilis (strain 168) |
NCBI Taxa ID | 224308 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 497 | GSNIWFEKEAKDLLP | acetylation | [1] |
|
Reference | [1] The acetylproteome of Gram-positive model bacterium Bacillus subtilis. Kim D, Yu BJ, Kim JA, Lee YJ, Choi SG, Kang S, Pan JG. Proteomics. 2013 May;13(10-11):1726-36. [ PMID: 23468065] |
Functional Description | Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile) (By similarity). |
Sequence Annotation | MOTIF 57 67 "HIGH" region.
MOTIF 594 598 "KMSKS" region.
BINDING 553 553 Aminoacyl-adenylate (By similarity).
BINDING 597 597 ATP (By similarity). |
Keyword | Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 921 AA |
Protein Sequence | MDFKDTLLMP KTDFPMRGNL PNREPDIQKK WEEEDIYRLV QERTKDRPKF VLHDGPPYAN 60
GDIHMGHALN KILKDFIVRY KSMSGYNAPY VPGWDTHGLP IETALTKNKK VNRKEMSVAE 120
FRKLCEEYAW KQIEGQREQF KRLGVRGDWE NPYVTLKPEY EAQQIRVFGE MAKRGYIYKG 180
LKPVNWSPSS ESALAEAEIE YQDKRSASIY VAFGVKDGKG VLENGERIII WTTTPWTIPA 240
NLGISVHPDL EYSVIAVGED RFVVASALVE NVASACGFDQ YEVTRTVKGK DLENIIAEHP 300
LYGRDSLVML GEHVTTDAGT GCVHTAPGHG EDDFIIGQKY GLDVLCPVDE KGVMTSEAPG 360
FEGMFYDDAN KAITQQLDEK GALVKLEFIT HSYPHDWRTK KPTIFRATAQ WFASIKDFRS 420
DLLDAIKETK WVPEWGEQRL HNMVRDRGDW CISRQRAWGV PIPVFYAENG EPVITDETIE 480
HVSELFRQHG SNIWFEKEAK DLLPEGFTHP GSPNGTFTKE QDIMDVWFDS GSSHQAVLEE 540
RDDLVRPADL YLEGSDQYRG WFNSSLSTAV AVTGKAPYKG VLSHGFALDG EGRKMSKSIG 600
NVVVPAKVMK QLGADILRLW VSSVDYQADV RVSDAILKQV AEVYRKIRNT FRFLHGNLFD 660
FDPKTNAVAV EDLREVDQYM LIKLNKLIDK VKKAYDEYEF AVVYHSIHNF CTIELSSFYL 720
DFAKDIVYIE HADHPDRRSM QTVFYETLLA LVKLSAPILP HTADELWSHL TFVEEQSVQL 780
TDMPETITVP NSEATEEKFD RFMALRDDVL KALETARNEK IIGKSLEANL KLYPNKENKE 840
LLASIKENLS QLFIVSELTI SEENEAPNDA QSFATGKIAV EKAEGEMCER SRVISKDVGA 900
NPKYPTLSLR NAEIVEKYYQ K 921 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. GO:0005524; F:ATP binding; IEA:HAMAP. GO:0004822; F:isoleucine-tRNA ligase activity; IEA:HAMAP. GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:HAMAP. GO:0006450; P:regulation of translational fidelity; IEA:GOC. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |