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Database: UniProt
Entry: H3DDW5_TETNG
LinkDB: H3DDW5_TETNG
Original site: H3DDW5_TETNG 
ID   H3DDW5_TETNG            Unreviewed;      1441 AA.
AC   H3DDW5;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
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:ENSTNIP00000018708.1, 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:ENSTNIP00000018708.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   STRING; 99883.ENSTNIP00000018708; -.
DR   Ensembl; ENSTNIT00000018935.1; ENSTNIP00000018708.1; ENSTNIG00000015634.1.
DR   GeneTree; ENSGT00940000153424; -.
DR   HOGENOM; CLU_002849_2_0_1; -.
DR   InParanoid; H3DDW5; -.
DR   OMA; RSMHDFQ; -.
DR   TreeFam; TF314166; -.
DR   Proteomes; UP000007303; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0070887; P:cellular response to chemical stimulus; IEA:UniProt.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0048583; P:regulation of response to stimulus; IEA:UniProt.
DR   GO; GO:0010033; P:response to organic substance; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd08782; Death_DAPK1; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 4.
DR   Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.5.460; Single helix bin; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR000488; Death_domain.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR020859; ROC_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24342:SF17; DEATH-ASSOCIATED PROTEIN KINASE 1; 1.
DR   PANTHER; PTHR24342; SERINE/THREONINE-PROTEIN KINASE 17; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00248; ANK; 9.
DR   SMART; SM00005; DEATH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF47986; DEATH domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 7.
DR   PROSITE; PS50088; ANK_REPEAT; 8.
DR   PROSITE; PS50017; DEATH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS51424; ROC; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          13..273
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REPEAT          376..408
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          412..444
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          445..477
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          478..510
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          511..543
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          544..576
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          577..609
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          610..642
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          681..952
FT                   /note="Roc"
FT                   /evidence="ECO:0000259|PROSITE:PS51424"
FT   DOMAIN          1326..1405
FT                   /note="Death"
FT                   /evidence="ECO:0000259|PROSITE:PS50017"
FT   BINDING         46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1441 AA;  160967 MW;  F25AE865D58F60A2 CRC64;
     MTIFNQENVE EFYEIGNELG SGQFAVVRRC RHRSTGVEYA AKFIKKRRSK SSRRGVSRED
     IEREVNILKE IQHANIITLH EVFENKAEVI LILELVAGGE LFDFLAEKES LSEDTQFLKQ
     ILDGVFYLHS KQIAHFDLKP ENIMLLNRSV PHPRIKIIDF GLAHKIDFGN DFKNIFGTPE
     FVAPEVVNYE PLGLEADMWS VGVITYILLS GASPFLGDNK QETLANVSAV DYTFDEEFFS
     NTSILAKDFI ARLLVKDPKK RMAIQDSLQH PWIKPKDTQQ ALSRKESAVN MEKFKKFAAR
     RKWKQSVRLI SLCNRLSRSF LSRSNISVAR SDDTLDEEDS FVMKAIIHAI NDDNVPGLTH
     LLGSLNSYDV NQPNKHGIPP LLIAAGCGNI QIIEVLMRKG AEIQAGDKNH QSGANAIYYA
     ARHGHVDTLK FLHEKNCPLD IQDKSGETAL HVAARYGNVD VVGYLCSIRA NPDLADREQE
     TPLHCAAWHG YSTVARALCQ AGCRVDAKNR EGESPLLTAS ARGFVDIVEC LVEHRANLET
     CDKDGHTALH LAVRRCQVEV VRCLLRHHCH LDQQDRHGNT ALHIACKDGN LPIVIALCNA
     KANLDLPNKY GRTPLHLAAS NGSLEVVRHL CLAGVNIDAV TNDGKTAEEL ANADHHEQIV
     SLLVRLKKDN HKLSYIQQLR PTQTIQPRKL KLFGHPGAGK STLLESLKCG ILRSFFRRRR
     TRMTNTARQP NSPVNSKPPV SVSISNLYPG CENVSVRSRS MMFEPSLTKG VLEVFSPVHS
     TLSTADEQAT KAIDIQHANI HSVGDFSVWE FSGNPVYYCS YDYFAANDNT AIHLVLFSLE
     EPYETQLSHV TYWLNLLKAL TLPQDNIGFG GRIQQPLLVV LVATHADLAD IPRAFSGEFT
     YDKEKVLLKE VRNRFGLDLQ ISEKLFVMDA GASNSKDLKL LRSHLLELRS SIISKCSPMT
     QLTERLLNTL PAWRKLSGPN QLTSWQQFVS DVQEHINPLV SQDHLRALTM QLHSMGEINI
     MQSETVQDVV LLEPRWLCSS ILGKLLSVET PKAIHHYRGR YRLEEVQALV PESDVEELLQ
     ILDAMDICAR DTTNPFMVDV PTLIKTSGLH RSWTEEDEED EALIYGGVRL VPAEHLTPFP
     CGLFHKLQVN LCRWSHQQKS EEEGGDDFDG DIHLWTNGAK VSQTGVEALV LLVNHGQGVE
     IQVRGHDSER AKCYTLLDTI CSITENLLTS TLPGLLTAKY YLSPQQLRER HTPIMIYQPK
     DFFRAQAQRE TSLTNTMGGY RESFSSILSF GCAEVYQQGT LGTDVHISDV PLLARRKLCR
     MLDPPDAMGK DWCLLAMNLG LTELVAKHSN GTSNGAAEPD SPQPSPTAAL LQEWSGRADS
     TVGVLMGKLR ELGRRDAADF LLKASPVFRV NVEAIGRAAN GYPPICNGGT SYNSISSVIS
     R
//
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