ID H3CK65_TETNG Unreviewed; 1073 AA.
AC H3CK65;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=valine--tRNA ligase {ECO:0000256|ARBA:ARBA00013169};
DE EC=6.1.1.9 {ECO:0000256|ARBA:ARBA00013169};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029936};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000008644.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000008644.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; H3CK65; -.
DR Ensembl; ENSTNIT00000008812.1; ENSTNIP00000008644.1; ENSTNIG00000005916.1.
DR GeneTree; ENSGT00940000159890; -.
DR HOGENOM; CLU_001493_0_2_1; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR CDD; cd00817; ValRS_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 HAMAP; MF_02004; Val_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033705; Anticodon_Ia_Val.
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 InterPro; IPR002303; Valyl-tRNA_ligase.
DR NCBIfam; TIGR00422; valS; 1.
DR PANTHER; PTHR11946:SF116; VALINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000007303}.
FT DOMAIN 108..732
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 778..929
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 20..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1038..1065
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 40..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1073 AA; 120934 MW; FA03BA6FF9C3AE5B CRC64;
RPHPPVLSLA PPLKWVSSHR CFRGKAAKPS SSSSQSDPQR PKAEKQRRRR EREEAVLTRQ
RNTSEDAVLK WSQKQKIAYS AHSSAGAKKD TSLPFPPSYS PEYVEPRWYE WWEKEGFFTP
EQHDRSAHAV DQTFCLCIPP PNVTGTLHVG HALTVAVEDA LVRWRRMQGQ RVLWVPGCDH
AGIATQTVVE RKLRRETGKR RQDFSRQEFL QEVWKWKEEK GEQIYQQLRS LGASLDWSRA
CFTLDPGFSG AVTEAFVRLC DAGLIYRAES LVNWSCALES AISDIEVDSR ELPGPTLISV
PGYETQVEFG RMFTFAYPLE GCAWSDGEVA VSTTRPETML GDVAVAVHPD DPRYQAVHGK
LCRHPFTHRL LPIITDTLVD MQLGTGAVKV TPAHDHTDFL LSQRHSLPRL TVIGGDGTMT
AACGPWLQAV KRFQARQLVV EALVEKKLFR GHRGHSMSLP VCSRSGDVVE PLLRKQWFVR
CQQMAQRAVQ AVEEQQLRIS PPFHTKTWRR WLSGASDWCI SRQLWWGHRI PAYRVKLPDW
SEEQEELWVC GRSQEEARRR AADRCGVRPD AVTLTQDPDV LDTWFSSALF PFAMLGWPEQ
SADLQRFYPN SLLETGSDLI FFWVARMVML GTQLTGQLPF RQVLLHPLVR DQHGRKMSKS
LGNVIDPLDV IHGASLEVLQ QKVKEGNVDP REQLVAMEAV RKDFPAGIPA CGADALRLSL
CSHRLQGEDI RLSISQVLAC RTFCNKMWQT LRFTLRVLAE GPTPLRTLEE TAPVSSMDQW
ICSRLYSTLL QCEQAFPAWD LHLVTAGLQA FWVHSLCDVY LEYIKPLLAH QRCSSGQMLR
SVLFHCVSTS LALLSPFMPF ITEELWQRLR PFQPGAATQT SLCLQPYPST SQLAHWHFPA
VEQDFELVQD LVRVARSLRA QCGMTQERPA AWAVCSPGQA QVLHRFGPAV RTLGRISSLH
VCCPDGAGAP AAPPPAGSLV GVVDHTCRVH LAAQAGASPE ARTQQLSLRR DKLLPKLQKV
LLTVQCPDYR SKAPAHAREK MEAKMLRLQQ ELRSLEEQMK SLKEPPGALG GEL
//
