| Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Isoleucine--tRNA ligase |
Protein Synonyms/Alias | IleRS |
Gene Name | ileS |
Gene Synonyms/Alias | SSO0722; ORFNames=C10_008 |
Created Date | 3-June-2014 |
Organism | Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) |
NCBI Taxa ID | 273057 |
Phosphorylation | Position | Peptide | Code | Type | References | | 638 | MLKKVNESMKDYKVH | S | HTP | [1] | | 9 | IKDCILRYQRVLGKR | Y | HTP | [1] | | 642 | VNESMKDYKVHEMTN | Y | HTP | [1] | |
Reference | [1]Change of carbon source causes dramatic effects in the phospho-proteome of the archaeon Sulfolobus solfataricus. Esser D,Pham TK,Reimann J,Albers SV,Siebers B,Wright PC J. Proteome Res. 2012, Oct, 5;11(10):4823-33. [ PMID:22639831] |
Functional Description From UniProt | FUNCTION: 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) |
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| Aminoacyl-tRNAsynthetase; ATP-binding; Completeproteome; Cytoplasm; Ligase; Metal-binding; Nucleotide-binding; Proteinbiosynthesis; Referenceproteome; Zinc |
Protein Sequence | MIKDCILRYQ RVLGKRVHDQ PGYDTHGLPI EVATEKLLGI SNKQEIIDKI GVETFINKCK 60
EFALSNADKM TQNFKNVGVF MDWERPYYTL DPSYISSSWS VIKKAYEKGM LDKGTAVLHW 120
CPRCETTLSD YEVSEYRDLE DPSIYVKFKI KGEKNRYLLI WTTTPWTIPS NVFVMINKDY 180
DYADVEVNGE ILVIAKDRVE AVMKEASITN YKILRTYKGS ELIGIKYEHP LREFVSAQTK 240
LDDFHQVVDA GNIVTLTDGT GLVHSATGHG EEDFTVGQKY GFPVVMFVND RGEFTEEGGK 300
YKGLKVRDAS KAIISDLKSK NTLFFEGKIV HRYPVCWRCK TPLILRAIDQ WFIRVTKIKD 360
KMLNEIEKVN WIPDWGKSRI SNMVKELRDW VISRQRFWGT PLPIWICERC NNVMVVGSKE 420
ELESIAIDPV PNDLHRPWID NVRVKCNKCG GVAKRIPDVA DVWFDSGVAF FASLGKDWQE 480
KWKELGPVDL VLEGHDQLRG WFFSLLRSGL ILLDRAPYTS VLVHGFMLDE QGREMHKSLG 540
NYVEPSVVVE KYGRDILRLW LLRNTTWEDA KFSWKALELT KRDLQIIWNT FVFASMYMNL 600
DNFEPDKYTL DDIIKYAKIE DLWILSRFNS MLKKVNESMK DYKVHEMTNY LINFLIEDVS 660
RFYIRLIRKR AWIEANTQDK IAMYYILYYI LKQWIILAST IIPFISEKIY KSFVVNAKES 720
VSMESSINYD ERFIDNELER AFEVAREINE ASLNARAKAG IKLRWPLAKV YIFIENEDTL 780
AKVGRIKDVL ISMLNAKDIE ISKIEGFKSF SKYKVEPNRS IIGKEYKSMS PKIVEYIENN 840
RDIIAMDILN KKQHVAKIDN FDIILNASYV IISEETVEGF ISSKFSKGIV VISKEISESE 900
EEEGLIRDII RRIQFMRKQL KLNVLDYIEI SMKVPEERVK TIQKWEEFIK SETRASNIIL 960
GEAKGDITMD WDIEGESYII GIKKST 986 |
| GO:0005737 C:cytoplasm IEA:UniProtKB-SubCell GO:0002161 F:aminoacyl-tRNA editing activity IEA:InterPro GO:0005524 F:ATP binding IEA:UniProtKB-KW GO:0004822 F:isoleucine-tRNA ligase activity IEA:UniProtKB-EC GO:0046872 F:metal ion binding IEA:UniProtKB-KW GO:0006428 P:isoleucyl-tRNA aminoacylation IEA:InterPro |
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