ID H2B2D9_KAZAF Unreviewed; 1072 AA.
AC H2B2D9;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 13-SEP-2023, entry version 54.
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 Name=KAFR0L01790 {ECO:0000313|EMBL:CCF60789.1};
GN ORFNames=KAFR_0L01790 {ECO:0000313|EMBL:CCF60789.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF60789.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF60789.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE650832; CCF60789.1; -; Genomic_DNA.
DR RefSeq; XP_003959924.1; XM_003959875.1.
DR AlphaFoldDB; H2B2D9; -.
DR STRING; 1071382.H2B2D9; -.
DR GeneID; 13886997; -.
DR KEGG; kaf:KAFR_0L01790; -.
DR eggNOG; KOG0434; Eukaryota.
DR HOGENOM; CLU_001493_1_1_1; -.
DR InParanoid; H2B2D9; -.
DR OrthoDB; 656at2759; -.
DR Proteomes; UP000005220; Chromosome 12.
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:UP000005220}.
FT DOMAIN 17..640
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 693..851
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1072 AA; 123395 MW; 63CEB87F93995E38 CRC64;
MSESPAHFSF PKEEEKVLAL WEEIDAFHRS LELTKDKPEF SFFDGPPFAT GTPHYGHILA
STIKDIVPRY ATMTGHHVER RFGWDTHGVP IEHIIDKKLN IKNKDDVYKL GIDKYNDECR
AIVMTYAAEW RKTLGRLGRW IDFDNDYKTM YPSFMESVWW AFKELYKKDQ VYRGFRVMPY
STGLTTPLSN FEAQQNYKDV LDPAVTIGFN VIGQEKTQLV AWTTTPWTLP ANMALCVNED
FEYVKIHDEK KDCYYIMLES LIKNLYRKPK DEKFKIVERL KGSDLVGLKY EPLFPYFVEQ
FKDTAFRVVS DSYVTAESGT GIVHNAATYG EEDYKVCLNA GIISEDTILP DALDDLGVFT
EVATDLAGLY VKDADKKIIK LLTEKGNLLL NSQIRHSYPF CWRSDTPLLY RTVPGWFVRV
KEIVPKILDS VQKSNWVPNT IKEKRFSNWI ANARDWNVSR NRYWGTPIPL WVSDDYEEVV
CVGSVAELEE LTGVTGIKDL HRDTIDGLTI PSKQGKGELK RIEEVFDCWF ESGSMPYASQ
HYPFENTEKF DQKVPANFIS EGLDQTRGWF YTLSVLGTHL FGEVPYKNVI VSGIVLASDG
RKMSKSLKNY PDPNIVLEKY GSDALRLYLI NSPVLKAESL KFKEEGVKEV VSKVLLPWWN
SYKFLEGQIA LLQKTSDITF EYDPSVRSEN VMDRWILASL QSLVQYIHKE MGDYRLYTVV
PRLLNFIDEL TNWYIRFNRR RLKGENGVED CIKALNTLFE ALFTFVRAMA PFTPFLSDGI
YLRLKEFIPA DVLAKFTKDD RSVHFLSYPV VREELFDEDI EKAVARMQSV IDLGRNIREK
KTISLKTPLK TLVILHSDKD YLKDIEALQN YIVEELNVRD IVITTDEEKY GVEYKAVADW
PVLGKKLKKD AKKVKDALPS CSSDEVRAYL ETGKLEVAGI ELVKGDLNVI RGLPESQAQS
GNETRTDQEV LIIMDTNIYP ELKSEGLARE LVNRIQKLRK KCGLNATDDV LVQYELVKDT
IEFESIVNEH NEMLSKTCRS EISQFDGSRS DGIADEEQTI NDTAFKLKIF RL
//
