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Database: UniProt
Entry: Q4SZM3_TETNG
LinkDB: Q4SZM3_TETNG
Original site: Q4SZM3_TETNG 
ID   Q4SZM3_TETNG            Unreviewed;       933 AA.
AC   Q4SZM3;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 97.
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};
DE   Flags: Fragment;
GN   ORFNames=GSTENG00009778001 {ECO:0000313|EMBL:CAF93909.1};
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|EMBL:CAF93909.1};
RN   [1] {ECO:0000313|EMBL:CAF93909.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|EMBL:CAF93909.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Genoscope;
RG   Whitehead Institute Centre for Genome Research;
RL   Submitted (FEB-2004) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CAF93909.1}.
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DR   EMBL; CAAE01011581; CAF93909.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4SZM3; -.
DR   KEGG; tng:GSTEN00009778G001; -.
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; 1.10.730.20; -; 2.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 1.10.10.830; Ile-tRNA synthetase CP2 domain-like; 1.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR002301; Ile-tRNA-ligase.
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; 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}.
FT   DOMAIN          38..648
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAF93909.1"
FT   NON_TER         933
FT                   /evidence="ECO:0000313|EMBL:CAF93909.1"
SQ   SEQUENCE   933 AA;  103793 MW;  AD3647AF2A0F8F99 CRC64;
     YRDTVLVPRT DFPMKVTGQK LLDQEVAIQK KCGFADLYAW QRSRKAKKEF CVHDGPPYAN
     GDPHVGHALN KILKDIRNRF EMLKGRRVHY IPGWDCHGLP IELKALGELT PSSLTPLQIR
     QKARAFAEEA ITRQKAAFQR WGVMADWDHC YYTHHGVYEA AQLKVFQEMH GKGFIYQDHK
     PVFWSPSSRT ALAEAELEYN PDHVSRAIYA TFPLTTVPAN IASEVGLDNV SVLVWTTQPW
     TIPANQAVCY MPKAQYSVVK RTDSSQMLLI AAERTASLAS LLGTELETVG TFTGSQLEGG
     ICKHPVIPDK FVQLLPANHV TMAKGTGLVH TAPAHGMDDY SVASHFNLPV ECMVDEDGKF
     TELAGPELHN LAVMTEGTDK VISMLKDCGA LVNEERCVHS YPYDWRTKQP VIIRPSRQWF
     IDTASLKDKA KEALKKVHIL PESARGSLLA MLDRRTYWCI SRQRSWGVPI PVFYHRETGE
     PLLNKYTMSH ITSLFKEKGS DCWWELPLET LLPEEVLEKS KAGPAIDYVR GEDVLDIWFD
     SGTSWAAVLE ETGCMADAYL EGKDQIGGWF QSSLLTSVAV RNKAPYRSLV VHGFVVGEKG
     EKMSKSVGNV VDPDEVINGG KDTATTAYGA DVLRWWVAES NVFSEVQIGA NVLNSARDDI
     NKVPRSSSAY CLVNDVFIGL GSCWRHMTDH FLQLRNSLRF LLGNLQGFDP QVQATEPADM
     HYIDQYMLHL LHKYSIKVTD AYSEFGILAG SSVSFKPSSP VTFPVFISAS SKIGHKETQT
     LFKSGWIQST SVWLRPGVEE MVEGACAIRD SFLSSIPGKN PAKYDLTIAI KPGLLFELME
     CLQGEATSTS SQLAELMMVA RVDLTSELPV DLPPDALLSH GTFLINLEGG VIRENSAYAI
     AAVPTSGSRC PRCRRHTAET ADALCPRCRT VLQ
//
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