ID A0A401S5A0_CHIPU Unreviewed; 1141 AA.
AC A0A401S5A0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 14.
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=chiPu_0003983 {ECO:0000313|EMBL:GCC25572.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC25572.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC25572.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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}.
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:GCC25572.1}.
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DR EMBL; BEZZ01000090; GCC25572.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401S5A0; -.
DR STRING; 137246.A0A401S5A0; -.
DR OMA; EIIVIHK; -.
DR Proteomes; UP000287033; 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 Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000287033}.
FT DOMAIN 32..511
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 566..722
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1141 AA; 130160 MW; 64CBF49870ED9F70 CRC64;
MFFLLCIECR RYQWASSNYG SQLWAQQDID PLRWVFKQLY DKGLVYRGVK VMPFSTACNT
PLSNFESHQN YKDVQDPSVI VTFPLEEDES VSLVAWTTTP WTLPSNLAVC VSPEYQYVKI
KDNTTGNVYI IMEARLEALF KSDSEYAVLD RFKGAALKGK KYRPLFDYFS KCKETGAFTV
LVDNYVKEEE GTGVVHQAPY FGADDFRVCV DYGIIQKDST PVCPVDASGC FTAEVKDFAG
LYVKDADKHI LKYLKDKGRV VHSGTYKHNY PFCWRSDTPL IYKAVPSWFV RVEHMVDKLL
ENNDKCYWVP EFVREKRFGN WLKDARDWAI SRNRYWGTPI PLWVSEDFEE VVCVGSVAEL
EELSGIKVED LHRESVDNIT IPSHCGKGVL KRVSEVFDCW FESGSMPYAQ VHYPFENRRE
FEDTFPADFI AEGIDQTRGW FYTLLVLSTA LFGKPPFRNV IVNGLVLASD GQKMSKRKKN
YPDPMHIVNS YGADALRLYL INSPVVRAEN LRFKEEGVRD VLKDVFLPWY NAYRFLVQNV
QRLHKEEGIQ FLFNESTIED SDNIMDKWIL SFTQSLIRFL KAEMEAYRLY TVVPRLVKFV
DLLTNWYVRM NRRRLKGENG VEDCRKTLET LFSVLFCMCR LMAPFTPFIT ELMYQNLRHL
VDLSSVPDKD THSIHYLMLP QVRESVIDQR IEGAVAQMQL VIELGRVIRD RKTLPVKYPL
KEVVVIHQDS EALNDIRALE KYILEELNVR QLTLSTDKGK YGIQLRAEPD HMVLGKRLKG
AFKSVTAAIK ALQSTQLEEF QKTGTIVVEG HELHEEDLRL MHKFDPNTGI SAQYEAHSDA
QVLVLLDVTP DQPMVDEGVA REVINRIQKL RKKAHLVPSD EITVYYSSEP KGEYLDNVIQ
GHIDFILGTI KASLKPYPVP ITAGIIIQEK TQLKGSNLDL TLVKGASTID APVLGPACAY
INLKVCVDGQ KQDGVVLLEN PKGDNVLDFV KLKNVIINIF RLQTTKIAIY HDKSELTNGT
DLMTLNGKTL HVTSGVTPAE TVMQTDTLLF QYVNLQLVNA KPQECLNGTV GALLLENPAG
QNGLTYADLY HEAAKVFGLR SKKLRLCLGD TKAEEITDDS SMKMLNMKTI YIHVLPTTAE
A
//
