ID A0A167IZ08_CALVF Unreviewed; 1077 AA.
AC A0A167IZ08;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=CALVIDRAFT_540348 {ECO:0000313|EMBL:KZO93095.1};
OS Calocera viscosa (strain TUFC12733).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1330018 {ECO:0000313|EMBL:KZO93095.1, ECO:0000313|Proteomes:UP000076738};
RN [1] {ECO:0000313|EMBL:KZO93095.1, ECO:0000313|Proteomes:UP000076738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUFC12733 {ECO:0000313|EMBL:KZO93095.1,
RC ECO:0000313|Proteomes:UP000076738};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-
CC isoleucyl-tRNA(Ile); Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666,
CC Rhea:RHEA-COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58045, ChEBI:CHEBI:78442, ChEBI:CHEBI:78528,
CC ChEBI:CHEBI:456215; EC=6.1.1.5;
CC Evidence={ECO:0000256|ARBA:ARBA00000114};
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; KV417304; KZO93095.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167IZ08; -.
DR STRING; 1330018.A0A167IZ08; -.
DR OrthoDB; 656at2759; -.
DR Proteomes; UP000076738; 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; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR CDD; cd00818; IleRS_core; 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_02003; Ile_tRNA_synth_type2; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033709; Anticodon_Ile_ABEc.
DR InterPro; IPR002301; Ile-tRNA-ligase.
DR InterPro; IPR023586; Ile-tRNA-ligase_type2.
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; PTHR42780:SF1; ISOLEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR42780; SOLEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF19302; DUF5915; 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:UP000076738}.
FT DOMAIN 21..644
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 698..854
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1077 AA; 123931 MW; 6C14188E4D577D99 CRC64;
MSFQAHDVSA KFDFAQEEEK VLAFWREIDA FRTSVKLSEG RPEFSFYDGP PFATGLPHYG
HILAGTIKDI ITRHAHSSGF HVERRFGWDT HGLPVEHEID KKLGIRGKED VLAMGIDKYN
AECRAIVMRY AGEWRTMVER IGRWIDFDND YKTLYPTFME SVWWVFGQLY EKGMVYRGLR
VMPYSTGCTT PLSNFEAGQD YRDVSDPAVT VAFTLVDDPK TSLLAWTTTP WTLPSNLALC
VHPDFIYIKI HDEERDENYI LCEGMLKTLY KDPKKAKFKK LGQFKGSDMK GWRYVPLFDY
FTKQYGDRAF RVLNDTYVTA EDGTGIVHQA PAFGDEDHRI AMANGLLRPD EMPPCPLDDA
GCFTSEVPDF EGQYVKDADK AIQRVLKQRG KLIVQSTLIH SYPHCWRSGT PLIQRAIPAW
FIRVQPIVDK LVKNNRATRW VPQSVGELRF GNWLANARDW NVSRNRYWGT PIPLWASDDY
EEVVAISSIQ QLKDLSGRDD ITDLHRENID DIIIPSKQGK GDLHRVPEVF DCWFESGSMP
YAQNHYPFEN KAKFESTFPA QFICEGLDQT RGWFYTLLVL STHLFDTAPW ENLIVTGLVL
AENGKKMSKS KKNYPDPNIL VNKYGADALR MFLVNSPITR GENLRFREDG VREVISRVLL
PWLNSFRFFL AQVTLLKKTT NVDFMWDPHA KRSPNIMDRW ILARCQSLIK LVQEEMAAYR
LYTIIPRLLD LVDELTNWYI RFNRRRLKGG DSATDCVFAL NTLFEALFTL CRTMSSYTPF
LTENLYQGLR QFIPESYFGN DDSRSIHFIC FPEVNEEYLD PVIERQVQRM QTVIVLSRGL
REKHNISLKR PLKTLTIFHP SKEYLDDVQS LLPYIESELN VREVVLTSEE HEIGVGYRAT
ADWPTLGKKL RKDLVKVKNA LPNLTTDQVK AYVATGKVEV AGIPLVHGDL QVSRFVELEA
DGGHDTATDN DVVVILDVRN HPELEGEGMA RELINRVQRL RKAAGLQPTD DVEVYYKFEE
GEGEDLVTII EQYADMINKA VRSVPVDDSK RPQHLKVFVE ETQQIGDTFF VLSFVKA
//
