ID A8N786_COPC7 Unreviewed; 1078 AA.
AC A8N786;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 2.
DT 24-JAN-2024, entry version 86.
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=CC1G_03229 {ECO:0000313|EMBL:EAU91061.2};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU91061.2, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU91061.2, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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}.
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:EAU91061.2}.
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DR EMBL; AACS02000003; EAU91061.2; -; Genomic_DNA.
DR RefSeq; XP_001830692.2; XM_001830640.2.
DR AlphaFoldDB; A8N786; -.
DR SMR; A8N786; -.
DR STRING; 240176.A8N786; -.
DR GeneID; 6007136; -.
DR KEGG; cci:CC1G_03229; -.
DR VEuPathDB; FungiDB:CC1G_03229; -.
DR eggNOG; KOG0434; Eukaryota.
DR HOGENOM; CLU_001493_1_1_1; -.
DR InParanoid; A8N786; -.
DR OMA; EIIVIHK; -.
DR OrthoDB; 656at2759; -.
DR Proteomes; UP000001861; 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 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:UP000001861}.
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; 124289 MW; CD4CA671541DF44A CRC64;
MAFPAHDIGA QFDFPKEEEK VLQFWRDIDA FQTSLKLSEG RPEYSFYDGP PFATGLPHYG
HLLAGTIKDI VTRHAHVSGY HVTRRFGWDT HGLPVEHEID KRLGITGKED VMKMGIDKYN
AECRSIVMRY SSEWRRTVER MGRWIDFDND YKTLNLSFME SVWWAFSELH KKGMVYRGLR
VMPYSTGCTT PLSNFEAGQA YKDVSDPAIT VAFPLVDDPS TSLLAWTTTP WTLPSNLGLC
VHPDYTYIKI HDAERDQNFI IHENLLRTLY KDPKKAKYKK LAQFQGADMK DWRYVPLFDY
FTEQFEDKAF RVLVDTYVTD ADGTGIVHQA PAFGEDDHRV AIAHEVLRPD EMPPCPIDDK
GHFTKEVRDF EGLHVKAADS PIQKALKAKG RLIVQSTLKH SYPFCWRSGT PLIYRAIPVW
FVKVSPIVEQ LVANNEETRW VPSFVGEHRF GNWLANARDW NVSRNRYWGT PIPLWVSDDF
EEIVCVGSVE ELERLSGVKG ITDLHRDKID HITIPSQKGK GVLRRVEEVF DCWFESGSMP
YAQLHYPFEN KELFEKTFPA DFVSEGIDQT RGWFYTLLVL STHLFGRAPW KNLIVTGLVL
AADGKKMSKS LKNYPDPNLI IDKYGADATR MFLVNSPIVR GDNLRFREEG VRDVISRVLL
PWLNSFRFFL GHAALYKKAF KEDFVYNAHA PLPNNVMDRW VLARCQSLIK LVTQEMAAYR
LYTIIPRLLE LIDELTNWYI RFNRKRLKGE DGKEDTYAAL NTLFETLFTL CRTMSSYTPF
LTENLYQTLK QYIPKDPKAG DVRSVHFLLF PTVKEEYFDE TIERQVKRMQ AVIELTRNIR
ERNNISLKVP LKELLVFHPD PVYIADIQSL ERYIKSELNV RDVVFTSDES SSGVRYKAVA
DWGVLGKKLR KDLGRVRNAL PNVSSDAVKS YVETGKISVD GIELVEGDLQ VQRFLELPAG
LETQFATQTD NDVVVRLDIQ IHKDLQSEWL SRELTNRIQK LRKKAGLQAV DEVDYFYQFK
DDDGADILAA IEENKEAILK TVHGLPRDVK EKNPAKEVIA EEEQEIADVK FVLTLSKP
//
