ID F2UBS1_SALR5 Unreviewed; 1193 AA.
AC F2UBS1;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
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=PTSG_12343 {ECO:0000313|EMBL:EGD73937.1};
OS Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN [1] {ECO:0000313|Proteomes:UP000007799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Salpingoeca rosetta.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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; GL832967; EGD73937.1; -; Genomic_DNA.
DR RefSeq; XP_004993500.1; XM_004993443.1.
DR AlphaFoldDB; F2UBS1; -.
DR STRING; 946362.F2UBS1; -.
DR EnsemblProtists; EGD73937; EGD73937; PTSG_12343.
DR GeneID; 16074077; -.
DR KEGG; sre:PTSG_12343; -.
DR eggNOG; KOG0434; Eukaryota.
DR InParanoid; F2UBS1; -.
DR OMA; LLTYWNT; -.
DR OrthoDB; 656at2759; -.
DR Proteomes; UP000007799; 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:UP000007799}.
FT DOMAIN 124..750
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 805..967
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 39..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1193 AA; 135571 MW; CEA5734D5F440297 CRC64;
MDNMDTLKAE IDEQAKVLKE LDEKRQAALQ KLQALEQKYQ DATGEPAPSK AARDTTDKDK
GGKKGKKGKD KKAAAAGAAG KDQPKKDAQG KGKKGKAAGK GKKGSESEGT GKEMFSFPGE
EENILKFWNE KDAFQLSMKF SASKPNVEKF VFFDGPPFAT GLPHYGHLLA GTIKDVVTRY
AHMRGYHVPR RFGWDCHGLP VEYEIDKEYG IKGPDDVMKM GIATYNDACR AIVMRYSEEW
RRTVSRLGRW IDFDNDYKTM YPWFMESVWY VFKQIFDKNL VYRGYKVMPF STALSTPLSN
FEASQDMRDV DDPAVTIAFK QVDGDASFLA WTTTPWTLPS NLALCVHPEF EYVKFRDEKR
GENFIALKGR LFGPGGLYTE EQKEDVTILE SYKGADLKDM RYEPLFPYFA DRKDKAFRVL
VDTYVTDDSG TGIVHNAPGH GEDDFRVCTA AGVVTTEDLV CPVDHTGKYT KDVPEMEGMY
VKDADKVIIK RMKEEGKLFA SARIRHAYPH CWRSGTPLLY LTLPSWFIRV TELNEKLLKN
NKSTYWVPNN IRDGRFHKWL ENARDWAISR NRYWGTPLPL WVSDDGEEVV CVGSIEELQE
LSGRDDITDL HRQYVDEVTI PSKQGKGVLR RVSEVFDCWF ESGSMPYAQQ HYPFEHKEDF
EQNFPADFIA EGIDQTRGWF YTLLVIGTCL FDKAPWKNLI VNGLVLASDG RKMSKRLKNY
PDPNLVLHED GADALRLYLI TSPAVRAENL RFERKGVQGL IREVFLPWLN AFRFFEQQAD
RLKASSGQPF LFDDTAKCNT DNPTDRWILA FVQELLEFIH AEMQAYRLYT VVPRLLKFVD
NLTNWYVRLN RKRLKGAEGD EDAAIALWAL GEVLMTMAKF MAPFTPFFAE WMYQHMKPYI
KVSPEAEAQL RTIDGVREDE SVHFNLVPDP KPFYEDHSVV RAFEVLKRTI DGGRVLRERN
KMPVKYPAME LVVVSTTENV LEDLQSLQTY VTSELNIRKL TLSSDESAYK VKLKAQPDFK
TLGSRLKSDI KKVAAAVRQL THDQLTEYQS TQTIELCGHT LTGTDLVLSY EYAGDDNKYA
AQADGDILVL LDVLEYPELV DEGIAREVVS RVQKMRQAAG LSPTDPITVT HKLQGGKKTD
DLERVLGSHQ SYIAEALSCT FQPASDEADA SAVIATEALK IKGASLQVTI FKA
//
