ID A5DAK1_PICGU Unreviewed; 642 AA.
AC A5DAK1;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 2.
DT 27-MAR-2024, entry version 91.
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=PGUG_00306 {ECO:0000313|EMBL:EDK36208.2};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK36208.2, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK36208.2, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|RuleBase:RU363035}.
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DR EMBL; CH408155; EDK36208.2; -; Genomic_DNA.
DR RefSeq; XP_001486929.1; XM_001486879.1.
DR AlphaFoldDB; A5DAK1; -.
DR STRING; 294746.A5DAK1; -.
DR GeneID; 5128973; -.
DR KEGG; pgu:PGUG_00306; -.
DR VEuPathDB; FungiDB:PGUG_00306; -.
DR eggNOG; KOG0433; Eukaryota.
DR HOGENOM; CLU_001493_4_3_1; -.
DR InParanoid; A5DAK1; -.
DR OMA; DCWWNMS; -.
DR OrthoDB; 656at2759; -.
DR Proteomes; UP000001997; 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:0006428; P:isoleucyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 3.40.50.620; HUPs; 2.
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; 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; 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:UP000001997}.
FT DOMAIN 42..633
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
SQ SEQUENCE 642 AA; 73457 MW; 6E241AA9CF051AC9 CRC64;
MSIRSSIRHK SYSSTLHLPK TRFGPKIPDS DNLNRLIKSS SDDVYQQQAQ LLDRKKFVLH
DGPPYANGDL HMGHALNKIL KDIINRFELI RNNRRIIYRP GWDCHGLPIE QKALAEARKE
DETRNLSSTE IRQLCRNLAE TMIDRQRQQF RQFAIMTDFS APYITMSREY EARQLQVFQK
LVKNKLLSRQ SKPVWWSCES QTALAEAELE YRDHRSVAVY VKFPVKNAEY LKDKIKIGDD
LKLLIWTSTP WTIPGNKAIC VHEGLLYTIL QGMGERLIVA KDRAEELLKL NSDYEETDIL
ISGKDLIGMS YFVPGSQDSF PVLHGSHVTA TAGSGLVHTA PAHGMEDYLI GRSNNLKIAS
VVDGRGQFIT ENCPEQYASV RGLAANKPEG IWKVIGLLEQ WGMIFHIDKK YQHSYPYDWR
SKAPVIQRAT PQWFVNVEKV KQAAEDSLKN VTFVPENGIN RLSSFIRNRN EWCISRQRAW
GVPLPIVYSQ NGEALDNPEV VEYIVKRIEE FGTDEWFAEE SNIQRWIPEK YDGNLYKKGT
DTMDVWFDSG TSWTDLGNEI ADVYLEGSDQ HRGWFQSSLL NKVIASGKDE IFEPQAPFRK
VITHGFTLDG KNDKMSKSKG NVIVPSHVMN GGGKPMLSQN WC
//
