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Database: UniProt
Entry: Q4SB54_TETNG
LinkDB: Q4SB54_TETNG
Original site: Q4SB54_TETNG 
ID   Q4SB54_TETNG            Unreviewed;      1019 AA.
AC   Q4SB54;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   SubName: Full=Chromosome undetermined SCAF14677, whole genome shotgun sequence {ECO:0000313|EMBL:CAG02128.1};
GN   ORFNames=GSTENG00021126001 {ECO:0000313|EMBL:CAG02128.1};
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:CAG02128.1};
RN   [1] {ECO:0000313|EMBL:CAG02128.1}
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:CAG02128.1}
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 osteocalcin/matrix Gla protein family.
CC       {ECO:0000256|ARBA:ARBA00008850}.
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DR   EMBL; CAAE01014677; CAG02128.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4SB54; -.
DR   KEGG; tng:GSTEN00021126G001; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0048468; P:cell development; IEA:UniProt.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd09575; SAM_DGK-delta; 1.
DR   Gene3D; 3.30.60.20; -; 3.
DR   Gene3D; 4.10.740.10; Coagulation Factor IX; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR   InterPro; IPR037607; DGK.
DR   InterPro; IPR037606; DGK-delta_SAM.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR035972; GLA-like_dom_SF.
DR   InterPro; IPR000294; GLA_domain.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR   PANTHER; PTHR11255:SF30; DIACYLGLYCEROL KINASE DELTA; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   Pfam; PF00594; Gla; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   PRINTS; PR00001; GLABLOOD.
DR   SMART; SM00109; C1; 3.
DR   SMART; SM00046; DAGKc; 1.
DR   SMART; SM00069; GLA; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 3.
DR   SUPFAM; SSF57630; GLA-domain; 1.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   PROSITE; PS50146; DAGK; 1.
DR   PROSITE; PS00011; GLA_1; 1.
DR   PROSITE; PS50998; GLA_2; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1019
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004243844"
FT   DOMAIN          43..89
FT                   /note="Gla"
FT                   /evidence="ECO:0000259|PROSITE:PS50998"
FT   DOMAIN          152..202
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          263..410
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   DOMAIN          754..854
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   REGION          503..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          853..905
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        532..547
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1019 AA;  112810 MW;  BF800762A0FD8874 CRC64;
     MRPTAAVRLL ALLFLSTLAR CTVFLDPSSA ARVLRPSTRG RRANAFALEE LLPGDLEREC
     YEETCSQEEA AEIFHTKEKT LEFWFRYVEV TECRHRNGGC WQYCADVPGG VECGAPTDNR
     KEMEEWMAAL RSVQNRQNYE STQYSMDHFS GMHNWYACSH ARPTYCNVCR EALSGVTSHG
     LSCEVCKFKA HKRCAVRATN NCKWTTLASI GKDIIEDEDG VSMPHQWLEG NLPVSAKCHV
     CDKTCGSVLR LQDWRCLWCK AMSGDNQGVK FLRRFKQLLN PAQVFDLMNG GPHLGLRLFQ
     KFDTFRILVC GGDGSVGWVL SEIDALTLHK QVRLCRRSRR AAAPARRGAD RQLCVQCQLG
     VLPLGTGNDL ARVLGWGSAC DDDTQLPQIL EKLERASTKM LDRWSIMVYE TKFPRQHSVS
     TVQQILTYED SVAAHLSKIL TSDQHSVVIS SAKVLCETVK DFVARVGKAY EKNTESSEES
     EAMAKKCGVL KEKLDSLLKT LNEESQASSV PHLAPPPTIA EEQEETEGNT SPPPLPHHPP
     PPPLPHSCSS RSGASPAAAA IFKPREQLML RANSLKKAIR QIIEHTEKVG KTPCEKLMGK
     GSREGTPLLS TKILYPGISV LTSQLRRRNN FWGGLKKTII REVAQCHHSL EQELAHAVNA
     SSKAMDLVYA NSKGSGVNQA AGPALGCVCW LFGCRSAFPS ARPPSRPQTL GCGLVLQMVV
     NVKVLLRETE LLLAGKMSMG PLTDFSKRSR IHQWGTEEVG AWLDFLCLTE YKDIFTGHDV
     RGAELLHLER RDLKVPTPRL LPQWNLHFLS LEPGPSRRLG GAGLTVSLLL QDLGVTKVGH
     MKRILQGIRE LNRSSSASNS ARPGDGPVQE GPSSQKAPQW PAVTPGVPNI AKTRQPAASR
     RAPRQRPKPC TVCKFKAHKR CAVRATNNCK WTTLASIGKD IIEDEDGVSM PHQWLEGNLP
     VSAKCHVCDK TCGSVLRLQD WRCLWCKAMV RPVATVTDAA SVSSCLILTA AKEKQRHSP
//
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