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Database: UniProt
Entry: A0A0G4EG48_VITBC
LinkDB: A0A0G4EG48_VITBC
Original site: A0A0G4EG48_VITBC 
ID   A0A0G4EG48_VITBC        Unreviewed;      1155 AA.
AC   A0A0G4EG48;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=isoleucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013165};
DE            EC=6.1.1.5 {ECO:0000256|ARBA:ARBA00013165};
DE   AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00032665};
GN   ORFNames=Vbra_11931 {ECO:0000313|EMBL:CEL95501.1};
OS   Vitrella brassicaformis (strain CCMP3155).
OC   Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX   NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEL95501.1, ECO:0000313|Proteomes:UP000041254};
RN   [1] {ECO:0000313|EMBL:CEL95501.1, ECO:0000313|Proteomes:UP000041254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhu J., Qi W., Song R.;
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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DR   EMBL; CDMY01000228; CEL95501.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4EG48; -.
DR   STRING; 1169540.A0A0G4EG48; -.
DR   VEuPathDB; CryptoDB:Vbra_11931; -.
DR   InParanoid; A0A0G4EG48; -.
DR   OMA; HCWRCKT; -.
DR   OrthoDB; 227382at2759; -.
DR   PhylomeDB; A0A0G4EG48; -.
DR   Proteomes; UP000041254; Unassembled WGS sequence.
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:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR   Gene3D; 1.10.730.20; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR   HAMAP; MF_02002; Ile_tRNA_synth_type1; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR033708; Anticodon_Ile_BEm.
DR   InterPro; IPR002301; Ile-tRNA-ligase.
DR   InterPro; IPR023585; Ile-tRNA-ligase_type1.
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   NCBIfam; TIGR00392; ileS; 1.
DR   PANTHER; PTHR42765:SF1; ISOLEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42765; SOLEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00984; TRNASYNTHILE.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|RuleBase:RU363035};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363035};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363035};
KW   Reference proteome {ECO:0000313|Proteomes:UP000041254};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1155
FT                   /note="isoleucine--tRNA ligase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005187074"
FT   DOMAIN          168..806
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          853..1011
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   REGION          51..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1155 AA;  128070 MW;  EEF083CC7E185B84 CRC64;
     MQQWTAAVLP GLFCSVLISL IFSADIGKAD VTERDGCSRR STEGLQHRTI RRIQSPKRSA
     DEPPCFIAPA ATRPPPVALR RRVPSRHMLS TAPPPPPAAA AASAAVAEKA PEQTAPTSSE
     QKTATAGKKG GRGKGKGKEE ENPFSDSINL PQTTFTQRAN AVTREPELQA FWAEQRVYER
     QAESNPGEVF VLHDGPPYAN GELHMGHALN KILKDFINRY QSLRGRKVRY VPGWDCHGLP
     IELAVLKSMK SSERQQLTPL DLRRKAASFA LSQVDKQRDS FKRYGVMGEW EKPYLTLDPE
     YEAAQIDILG KMLLKGHVYK GKKPVHWSPS SQTALAEAEL EYPDGHVSKS IYASFKVTSP
     SDGLARLLPD GGGGGGSGGG DVGVAVWTTT PWTIPGNMAV AVNPELQYAL VRRPDSDAVL
     IVAKDLVKEV SKALGALDEL TGEGLEVLAT IKGEDLVDTQ YEHPLYGRVS RVVAGGDYIT
     TDTGTGLVHT APGHGQEDFE TGQKYGLEPL SPVDNYGRFT AEAGERFEGL SVLKEGNEAI
     IQALDECGSL LKAEDYPHRY PYDWRTKKPT IFRATEQWFI SVDAFREAAL AAIDEVRWIP
     EMGKTRIASM TSSRSDWCIS RQRSWGVPIP VFYQAHTNEP LINNSTITHI KEVFRQHGTD
     AWWTMDTQQL LPEPYRSEWS LWVRGNDTID VWFDSGSSWA GVVNTRDNLR HDNPVELYLE
     GSDQHRGWFQ SSLLTSVAVR GAPPYQTVLT HGFVLDEKGY KMSKSLGNVL SPLTIIEGGS
     DKKKQPAYGA DVLRLWVATV DYSSDVLVGG TIIKQVFDAY RKLRNTARFL IGNIHDFDKE
     QDGVAYEDLP EVDKWVLGKT ASLIRRVREA YESYQFYRVT QELLAFSNQL LSNFYLDVSK
     DRLYISTPND RRRRACQSVI RVVTEAFALL LAPLLPHMAE DIWQNLPHDG EGVRRSGSVF
     EAGWPSGAEA SPPFREDKWD LVMTLRDDVN KVIESARTAK LVGANSEAAV HIHCPDPQTT
     SWLRELLPDQ SPLLATTTTT TDGRISAVDD LRFLFLTSQV HLADSPGAVE GSCPEFRLSA
     EQTGSGCTVG VSKAVGTKCE RCWMWGEDVS EWQGSPRSQD DPPSRHSLCP RCRAAVEQFL
     DRRRARAEGG RTNQP
//
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