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Database: UniProt
Entry: A0A8H4R0I0_9AGAR
LinkDB: A0A8H4R0I0_9AGAR
Original site: A0A8H4R0I0_9AGAR 
ID   A0A8H4R0I0_9AGAR        Unreviewed;      1078 AA.
AC   A0A8H4R0I0;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 11.
DE   RecName: Full=Isoleucine--tRNA ligase, cytoplasmic {ECO:0000256|ARBA:ARBA00069879};
DE            EC=6.1.1.5 {ECO:0000256|ARBA:ARBA00013165};
DE   AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00032665};
GN   ORFNames=D9613_000448 {ECO:0000313|EMBL:KAF4621094.1};
OS   Agrocybe pediades.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Agrocybe.
OX   NCBI_TaxID=84607 {ECO:0000313|EMBL:KAF4621094.1, ECO:0000313|Proteomes:UP000521872};
RN   [1] {ECO:0000313|EMBL:KAF4621094.1, ECO:0000313|Proteomes:UP000521872}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 102.39 {ECO:0000313|EMBL:KAF4621094.1,
RC   ECO:0000313|Proteomes:UP000521872};
RA   Floudas D., Bentzer J., Ahren D., Johansson T., Persson P., Tunlid A.;
RL   Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Ile) + L-isoleucine + ATP = L-isoleucyl-tRNA(Ile) + AMP +
CC         diphosphate; Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666, Rhea:RHEA-
CC         COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58045,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78528, ChEBI:CHEBI:456215; EC=6.1.1.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00048359};
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:KAF4621094.1}.
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DR   EMBL; JAACJL010000015; KAF4621094.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A8H4R0I0; -.
DR   Proteomes; UP000521872; Unassembled WGS sequence.
DR   GO; GO:0002161; F:aminoacyl-tRNA deacylase 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   FunFam; 3.90.740.10:FF:000044; Isoleucine--tRNA ligase; 1.
DR   FunFam; 3.40.50.620:FF:000176; Isoleucine-tRNA ligase, putative; 1.
DR   FunFam; 1.10.730.10:FF:000004; Isoleucyl-tRNA synthetase, cytoplasmic; 1.
DR   FunFam; 3.40.50.620:FF:000023; Isoleucyl-tRNA synthetase,cytoplasmic; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 1.
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:UP000521872}.
FT   DOMAIN          21..642
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          698..853
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   1078 AA;  123737 MW;  A4C69FDE98125EAE CRC64;
     MSFPPHDLST PFDFAKEEEK VIAFWREIDA FQTSLKLSEG RPEYTFYDGP PFATGLPHYG
     HLLAGTIKDI VTRHAHVTGH HVSRRFGWDT HGLPVEHEID KRLNITGKDD VLAMGIDKYN
     EECRKIVMRY SSEWRQTVER MGRWIDFDND YKTLNLPFME SVWWAFSELF KKGMVYRGLR
     VMPYSTGCTT PLSNFEAGQA YKDVNDPAVT VAFPLVDDPS TSLLAWTTTP WTLPSNLALC
     VHPDYTYIKI HDTEKDQNFI IHENLLRTLY KDPKKAKFKK VAQFQGSDMK GWRYVPLFEY
     FTDQFEDKAF RVLVDTYVTD ADGTGIVHQA PAFGEDDHRI AIAHGVLRPD EMPPCPIDDK
     GHFTKEVPDF EGLHVKAADS PIQKYLKAKN RLIVQSTLNH SYPFCWRSGT PLIYRAIPVW
     FVKVTPIIDQ LVANNEGTRW VPQNVGDNRF GNWLANARDW NVSRNRYWGT PMPLWVSDDM
     EEIVCVGSVE ELEQLSGVKG ITDLHRDKID HITIPSKQGK GVLKRVEEVF DCWFESGSMP
     YAQQHYPFEN KELFERTHPA DFVSEGIDQT RGWFYTLLVL STHLFGKAPW KNLIVTGLVL
     AADGKKMSKS LKNYPDPNLI IDKYGADATR MFLVNSPIVR GDNLRFREEG VREVISRVLL
     PWLNSFRFFM GHVALLKKTT GFDFKYNAHA PLPNNVMDRW ILARCQSLIK LVREEMAAYR
     LYTVIPRLLD LVDELTNWYI RFNRKRLKGE DGKEDTVSAL NTLFEALFTL CRIMSSYTPF
     ITENLYQSLR TFIPEDPAAG DTRSVHFLSF PEVKEEYFDA EIERKVQRMQ AVIDLGRNVR
     ERNNISLKVP LKELLVFHTD PAYLDDVKPL QRYIESELNV RDIVFSSDEA QSGIRYKAVA
     DWAVLGRKLR KDLGRVRNAL PAVSSEEIKA YIDTGKIKVD GIELVEGDLT VQRYLELPPS
     SEGQFATNTD NDVVIRLDIQ VHAELQGEWL ARELTNRVQK LRKKAGLQAT DDVNVFYRFE
     EGTGSDILAA IKDNMDIITK TVGSLPADVK EKAAGSVVII EEEQEIDDVK FLLYLARS
//
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