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Database: UniProt
Entry: D8QNT8_SELML
LinkDB: D8QNT8_SELML
Original site: D8QNT8_SELML 
ID   D8QNT8_SELML            Unreviewed;      1707 AA.
AC   D8QNT8;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 71.
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=SELMODRAFT_437676 {ECO:0000313|EMBL:EFJ38164.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ38164.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA   Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA   Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA   Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA   Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA   Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA   Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA   Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA   Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA   Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA   Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA   Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA   Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(2011).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594}.
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DR   EMBL; GL377565; EFJ38164.1; -; Genomic_DNA.
DR   RefSeq; XP_002960625.1; XM_002960579.1.
DR   STRING; 88036.D8QNT8; -.
DR   EnsemblPlants; EFJ38164; EFJ38164; SELMODRAFT_437676.
DR   Gramene; EFJ38164; EFJ38164; SELMODRAFT_437676.
DR   KEGG; smo:SELMODRAFT_437676; -.
DR   eggNOG; KOG0433; Eukaryota.
DR   HOGENOM; CLU_240710_0_0_1; -.
DR   InParanoid; D8QNT8; -.
DR   Proteomes; UP000001514; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IBA:GO_Central.
DR   GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR   GO; GO:0009791; P:post-embryonic development; IEA:UniProt.
DR   GO; GO:0048608; P:reproductive structure development; IEA:UniProt.
DR   CDD; cd00010; AAI_LTSS; 1.
DR   CDD; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR   CDD; cd00818; IleRS_core; 1.
DR   Gene3D; 1.10.730.20; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 1.10.10.830; Ile-tRNA synthetase CP2 domain-like; 1.
DR   Gene3D; 1.10.110.10; Plant lipid-transfer and hydrophobic proteins; 1.
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; IPR036312; Bifun_inhib/LTP/seed_sf.
DR   InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
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; IPR006458; Ovate_C.
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   InterPro; IPR010663; Znf_FPG/IleRS.
DR   NCBIfam; TIGR01568; A_thal_3678; 1.
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; PF14368; LTP_2; 1.
DR   Pfam; PF04844; Ovate; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF06827; zf-FPG_IleRS; 1.
DR   PRINTS; PR00984; TRNASYNTHILE.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF47699; Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   PROSITE; PS51754; OVATE; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1707
FT                   /note="isoleucine--tRNA ligase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003121015"
FT   DOMAIN          1636..1695
FT                   /note="OVATE"
FT                   /evidence="ECO:0000259|PROSITE:PS51754"
FT   REGION          1232..1279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1395..1428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1472..1537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1249..1263
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1482..1503
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1504..1527
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1707 AA;  188967 MW;  7251293DA9E3F904 CRC64;
     MLSRIFVTGG IMLLAIAIAT DGAAVDSPPP PSSCDTARAI EALQDCRAAV DAKTGTGKPS
     AACCEELKKV GKICLCAIIK EPPRGVEIEK MRKGFVLSVS CEAVGVPAFF FSRGLRERSS
     GAMLGLHSFP RSPVLAAAKN AGKQPDSRYK GTIELPQTKF SLKANSVTRE PEIQRFWEQK
     QLLETITQKN QGEPFTLHDG PPYANGDLHM GHALNKILKD FINRYQLLQG RKIFYVPGWD
     CHGLPIELKV LQSIDAEARM KLSPIELRKK AAEFALKTVD QQRSSFQRYG VWGSWNSPYL
     TLQPAYEAAQ IGVFCQMVLN GYIYRGRKPV HWSPSSGTAL AEAELEYPEG HTSRSMYAVF
     KMTFASDKFP KELEYLLSSL GVAIWTTTPW TIPGNTGVAV NDKLMYSVVE VVFNNDDSSL
     GGKKSTKAGR KYGNGLLKPV VSHLIVAADL VSSLEDKWNV QLVVKGSCTG SALEFCRYKH
     PLENREGVIV IGGDYITTDS GTGLVHTAPG HGQEDFVTGQ KYGLPMLSPV DDNGNFTDEA
     NEFAGMSVLS DGNEAVIKAL DANSSLLMEE AYGKNNLQMF PRIDSRIVHK YPYDWRTKKP
     TIFRATEQWF ASVEGFMPLA LAAIKNVDWI PSQGENRITS MVSGRKEWCI SRQRAWGVPI
     PVFYHVDTGE PLLNEQTISH VQAIIAQQGS DAWWSLTTED LLPDTYKAKA SNYRKGTDTM
     DVWFDSGTSW ASVLGTKRWP ADVYLEGSDQ HRGWFQSSLL TSVATKGVAP YRQVLTHGFV
     LDEKNVKMSK SLGNVVDPRS VIEGGKNQKE QPAYGADVLR LWVASVDYTG DVAIGPQILK
     QTADVYRKLR GTLRYLLSNL HDWKPELEIE YDDLPGIDKY TLFQLASVMD SLKDSLDKYQ
     FGKFFQSVQR YAVLDLSNFY LDISKDRLYV GGTDSFTRRS CQAVLASLLL YLARGISPVV
     PHLAEDAWQH LPFSYILPDG SKAESVFEAG WPEVDPRWRT ISDRDKKLWS LLLELRVEVN
     KVLESARMGK LIGANLDAKV CLHLGGEDDA LLHSTLQAMA GSEDGTVDKL HVIFLTSQVE
     VVDCEDADCA YTGSCKLEGS GGRAWIGVKR AEGQKCERCW KYSPAVGSFT LHSTLCERCY
     KIRRGRGEED EQLGAKGNEE QGRGVESSID ACVWTFVGSP NLEWHCRRVD CAPHFTGDGS
     RAMGRRRLRF KFTNVISRVF LLRAHRVKPV APSSVVAPAA SKKSSSSFTS DSNREEEPEE
     ERSLIAPAPA APAPAKAKKK NRKPVFGYSC CSREEAIVRE NCQYKRVKGL SKKPVGAASS
     RAAPMVVASR QEEEMWEREG LWSVIAAVDS GKVVKKKVVL KKRKKSQSSP RLLRAPANSE
     ISAMEEQVLI VGQAARVTSD PSSSERERKG SSTHTFRLST SSGDASLGPE ALAWDKEHSL
     FASDDSSAPG SSKLVHRATT LEDEQRHEAI EEVGLKNHAG QTPRPKKSSS SSSASTSGSS
     GGGTRGHHHR HHLHHHHHHH HHNSSFHLSR NHASGNKMTG ALSEFDELGL LLSSSSKMPP
     PPPRCDGKRI SSASSLESSA KFWEDGREVA SKVLPEFPRH KVGAESAPAL DDHARTKKKK
     KPKDLVRGKV RESVPVMLVS SNPYEDFRQS MVQMIFEKRL NKAADLEELL ECYLYLNPPG
     FHEVIVQVFT DLWLQALSTE NQQQQNI
//
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