| Tag | Content |
|---|
| CPLM ID | CPLM-009061 |
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 | TTHA1067 |
Created Date | July 27, 2013 |
Organism | Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) |
NCBI Taxa ID | 300852 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 878 | YRVLPNLKLLGRKYG | acetylation | [1] |
|
Reference | [1] Acetylome with structural mapping reveals the significance of lysine acetylation in Thermus thermophilus. Okanishi H, Kim K, Masui R, Kuramitsu S. J Proteome Res. 2013 Aug 1;. [ PMID: 23901841] |
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 47 57 "HIGH" region.
MOTIF 591 595 "KMSKS" region.
METAL 181 181 Zinc 1.
METAL 184 184 Zinc 1.
METAL 389 389 Zinc 1.
METAL 392 392 Zinc 1.
METAL 461 461 Zinc 2.
METAL 464 464 Zinc 2.
METAL 502 502 Zinc 2.
METAL 504 504 Zinc 2.
BINDING 57 57 Aminoacyl-adenylate.
BINDING 319 319 Valine.
BINDING 328 328 Valine.
BINDING 550 550 Aminoacyl-adenylate.
BINDING 553 553 Aminoacyl-adenylate.
BINDING 554 554 Aminoacyl-adenylate.
BINDING 581 581 Aminoacyl-adenylate.
BINDING 594 594 ATP (By similarity). |
Keyword | 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1043 AA |
Protein Sequence | MFKEVGEPNF PKLEEEVLAF WKREKIFQKS VENRKGGPRY TVYEGPPTAN GLPHVGHAQA 60
RSYKDLFPRY KTMRGYYAPR RAGWDTHGLP VELEVEKKLG LKSKREIEAY GIERFNQACR 120
ESVFTYEKEW EAFTERIAYW VDLENAYATL EPTYIESIWW SLKNLFDRGL LYRDHKVVPY 180
CPRCGTPLSS HEVALGYKEI QDPSVYVRFP LKEPKKLGLE KASLLIWTTT PWTLPGNVAA 240
AVHPEYTYAA FQVGDEALIL EEGLGRKLLG EGTPVLKTFP GKALEGLPYT PPYPQALEKG 300
YFVVLADYVS QEDGTGIVHQ APAFGAEDLE TARVYGLPLL KTVDEEGKLL VEPFKGLYFR 360
EANRAILRDL RGRGLLFKEE SYLHSYPHCW RCSTPLMYYA TESWFIKNTL FKDELIRKNQ 420
EIHWVPPHIK EGRYGEWLKN LVDWALSRNR YWGTPLPIWV CQACGKEEAI GSFQELKARA 480
TKPLPEPFDP HRPYVDQVEL ACACGGTMRR VPYVIDVWYD SGAMPFASLH YPFEHEEVFR 540
ESFPADFIAE GIDQTRGWFN SLHQLGVMLF GSIAFKNVIC HGLILDEKGQ KMSKSKGNVV 600
DPWDIIREFG ADALRWYIYV SAPPEADRRF GPNLVRETVR DYFLTLWNVY SFFVTYANLD 660
RPDLKNPPPP EKRPEMDRWL LARMQDLIQR VTEALEAYDP TTSARALRDF VVEDLSQWYV 720
RRNRRRFWKN EDALDREAAY ATLYEALVLV ATLAAPFTPF LAEVLWQNLV RSVRPEAKES 780
VHLADWPEAD PALADEALVA QMRAVLKVVD LARAARAKSG VKTRTPLPLL LVTAPTALER 840
EGLKRFAHEI AEELNVKEVR VLEPGEEILS YRVLPNLKLL GRKYGKLVPK IREALQRERE 900
RAAALALKGE AIPLEVEGEA LTLLPEEVLL EAEAPKGYQA LEKDGYVAAL KVEVTEALRM 960
EGLARDLIRL LQQARKDMGL KVSDRIRVGY EAEGPYLEAL KRHGPWIAEE VLATAFGEGL 1020
FGGFEARVED EEGKAVFHLA RAE 1043 |
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:0008270; F:zinc ion binding; IEA:HAMAP. GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:HAMAP. GO:0006450; P:regulation of translational fidelity; IEA:GOC. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |