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Database: UniProt
Entry: Q4T924_TETNG
LinkDB: Q4T924_TETNG
Original site: Q4T924_TETNG 
ID   Q4T924_TETNG            Unreviewed;       664 AA.
AC   Q4T924;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   SubName: Full=(spotted green pufferfish) hypothetical protein {ECO:0000313|EMBL:CAF90608.1};
DE   Flags: Fragment;
GN   ORFNames=GSTENG00004952001 {ECO:0000313|EMBL:CAF90608.1};
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|EMBL:CAF90608.1};
RN   [1] {ECO:0000313|EMBL:CAF90608.1}
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|EMBL:CAF90608.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Genoscope;
RG   Whitehead Institute Centre for Genome Research;
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type 1 subfamily. {ECO:0000256|ARBA:ARBA00006303}.
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:CAF90608.1}.
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DR   EMBL; CAAE01007648; CAF90608.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4T924; -.
DR   KEGG; tng:GSTEN00004952G001; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR   Gene3D; 3.30.1360.30; GAD-like domain; 1.
DR   InterPro; IPR004364; Aa-tRNA-synt_II.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR004115; GAD-like_sf.
DR   InterPro; IPR029351; GAD_dom.
DR   PANTHER; PTHR22594:SF5; ASPARTATE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF02938; GAD; 1.
DR   Pfam; PF00152; tRNA-synt_2; 2.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 2.
DR   SUPFAM; SSF55261; GAD domain-like; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 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}.
FT   DOMAIN          204..367
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          496..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..556
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..609
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         664
FT                   /evidence="ECO:0000313|EMBL:CAF90608.1"
SQ   SEQUENCE   664 AA;  74171 MW;  EE622EDED868A4A3 CRC64;
     SMLGHLRLKC AELLESCGAL VRDPSVFHFL WVLDFPLFLA SEEEAEKLES AHHPFTAPLP
     EDAHLLYTEP QKVRGQHYDL VLNGCEVGGG SIRIHKASEQ HHVLKNILKV SSKEVNHFLE
     SVSGPRRSNM LLQEDPRLLS HLLEALDSGD IAVWFRIKLF SQNTTLVKKG LFQLFMSARA
     GQFYSLPQSP QQFKQLLMVA GIDRYFQIAR CYRDEGSKPD RQPEFTQVDI EMSFVEQTGI
     MSLVEALLQH SWPDQLGPLQ LPFQTMTFEE AMRDYGVDKP DTRFAMKLVE LRDVFLSTDV
     QFVRAALSQP GGSVQAIRVP GGMKHLTGRH LNTLRETAAT QFGQELSLVQ LREDGTLISP
     LKKLLSPETT EELLQRTGSG PGDLLLIAAG SLDTVRSMLG HLRLKCAELL ESCGALVRDP
     SVFHFLWVLD FPLFLASEEE VEKLESAHHP FTAPLPEDAH LLYTEPQKVV PRALLLLCEG
     HMPLAFCRVG PGPTLRPGAE RLRGRRRVHS NPQGVRAASR PEEHPKGQFK GGEPFPGVSQ
     WSQAFKHASP GGSQTSVPPA GGPGLGRTTS WRHSFGSGQT ALHHGRISKY PRRDRLPQVR
     PRPRPDELRP RFAIGGGAEA LSHLCQVARG VRKLRRRHLQ GEDAFGCLRK VKSNQRQGDF
     LNVK
//
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