ID Q4SA00_TETNG Unreviewed; 1438 AA.
AC Q4SA00;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE SubName: Full=(spotted green pufferfish) hypothetical protein {ECO:0000313|EMBL:CAG02532.1};
GN ORFNames=GSTENG00021667001 {ECO:0000313|EMBL:CAG02532.1};
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:CAG02532.1};
RN [1] {ECO:0000313|EMBL:CAG02532.1, 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|EMBL:CAG02532.1}
RP NUCLEOTIDE SEQUENCE.
RG Genoscope;
RG Whitehead Institute Centre for Genome Research;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSTNIP00000014439.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the Ntn-hydrolase family.
CC {ECO:0000256|ARBA:ARBA00010872}.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005232}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00464}.
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DR EMBL; CAAE01014693; CAG02532.1; -; Genomic_DNA.
DR STRING; 99883.ENSTNIP00000014439; -.
DR Ensembl; ENSTNIT00000014638.1; ENSTNIP00000014439.1; ENSTNIG00000011492.1.
DR KEGG; tng:GSTEN00021667G001; -.
DR GeneTree; ENSGT00970000196672; -.
DR HOGENOM; CLU_245376_0_0_1; -.
DR OMA; PRMKGMK; -.
DR TreeFam; TF333567; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR CDD; cd04701; Asparaginase_2; 1.
DR Gene3D; 3.60.20.30; (Glycosyl)asparaginase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 2.
DR Gene3D; 3.30.428.10; HIT-like; 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; IPR000542; Carn_acyl_trans.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR039551; Cho/carn_acyl_trans.
DR InterPro; IPR042231; Cho/carn_acyl_trans_2.
DR InterPro; IPR011146; HIT-like.
DR InterPro; IPR036265; HIT-like_sf.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000246; Peptidase_T2.
DR PANTHER; PTHR10188; L-ASPARAGINASE; 1.
DR PANTHER; PTHR10188:SF42; SI:CH211-256M1.8; 1.
DR Pfam; PF01112; Asparaginase_2; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR Pfam; PF01230; HIT; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF54197; HIT-like; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS00440; ACYLTRANSF_C_2; 1.
DR PROSITE; PS51084; HIT_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 950..1054
FT /note="HIT"
FT /evidence="ECO:0000259|PROSITE:PS51084"
FT DOMAIN 1119..1429
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 570..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 264
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
FT ACT_SITE 769
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600246-1"
SQ SEQUENCE 1438 AA; 159111 MW; E2766517E1655152 CRC64;
MALLNFPIPE LDVTLQEVSR VLQLVLSPDL YSEFKSSVED QREILQDAQQ QFAIVAADQE
NWDTEIFKRN LLSCDDPLPT STALPFVLLP SQAEQCTQLW RAAALLWAAA RLHGEPSLLE
GSTSLECTQQ SELFAATRVP GRSQDEIKDI YTQLVHVKNQ PRAAKDNDPA VICSLSGLDR
KAWAASREEI LERGGDTAAS LGLMEGALLA LCLDDNDAPS EMAAILNALK LGVGGRQSPC
LRYYDKVLNV VVFKDGTAGM LFEHSAVDGM VACLVAHCVY TLSETSELNL VHTNAENANG
PSRKTSDNSA FPAPMRFPLN NLDMPKPSPE AEVTQSLLSF DLTSYPDVFS ALRGQRGLFD
AWINFSLQLS LRETLGESAA NRLLIITPTH MRHYKHGRCD PTYSVTVYSR QLVDALASYI
GSENTLQYTT ELLHMFHVAF VEHKRLIKNT KQGQGVGPHI ATLRQSLPSD NPLRKYLDHF
RCPPVYITGT DVMEPVECLV GNVYAPNQLA VGYLWRREKV CIVLNGSGMF SLSLAKLQKS
LKKNLELVMG LAVQYAIAHQ MGALESIFKQ RQTDKQDDEA NQRQGNSNHD NGCDGSSDCN
SDYTLVIHGG AGEDMMLNSK EIKLIEFALG AALAVGSQML QNGGSSLDAV QRSVEALENC
FLFNAGKGSV LNKDGKHEME ATIVDGSERK SGSVACLQSV KNPIKAARCV MEQSPHSLIV
GEGAEEFLSG LEEKQEFVAP EYFHTDIRHK ELLAKLRHIN PLKNNHPQTV GAVALDRFQN
LAAASSTGGL VGKLKGRVGD TAVAGAGIYA DDKVALTCSG DGDIFLRHTV AQKIASLYHH
KGIFLRQACR EVMAEDLNGT CAGIIAVDAK GEPAHIRILP LHGLEPKWQP HLSPEEEFHT
YNPGYCTSKS GPRWEDEALA EVQAQIRNGL PNPAAELCFD FYGDASCDDL FSRIVRGEQQ
QWRVWEDDQH VAFLTPYPNS PGFTVVVPRK PLSSDIFKLS EDDYKGLILA VYKVAKLLEN
TMKTQNVALI FEGFEIDYAH AKLIPLLPSL DGSVPAQLQS EFHQRYPGYV SSLDGPAVDA
GDIAKLHSKV ALCHPPRSWE DPESHSMLAI SDQWYRNMFQ IQNTLFHSTV EYFHSSCQYS
YALTPITSDT ISSPMGLGSD SEPVSVNLLG QDVYLADSMQ FVLEYFLRFQ ENLPGVYYIS
PSFRGEDPDA THLNQFYHVE CELVGGIEKA MSIAERYVAH LTKSMLKNHS DVILNTAGTL
AHVTALLSQL DGKTPLPKVP LDEAIAMMPS ADCVEWVQDG QPQYGRKLTR KGERFLIKKY
GSVVWLTEMD HLGVPFYQAY VEGTEQTKAK AADLLLGLGE TVGLGERHFS PETVEAALRQ
HAVQDASYRW YINMRRVKPL RTSGWGMGSE RYLCWLLQHD DIRDVVIIPR MKGVKYMP
//
