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Database: UniProt
Entry: H2THE9_TAKRU
LinkDB: H2THE9_TAKRU
Original site: H2THE9_TAKRU 
ID   H2THE9_TAKRU            Unreviewed;       635 AA.
AC   H2THE9;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 3.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000024099.3, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000024099.3, ECO:0000313|Proteomes:UP000005226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA   Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu facilitates
RT   insights into distinct features of genome evolution in teleosts and
RT   mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000024099.3}
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};
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DR   AlphaFoldDB; H2THE9; -.
DR   Ensembl; ENSTRUT00000024198.3; ENSTRUP00000024099.3; ENSTRUG00000009590.3.
DR   eggNOG; KOG0584; Eukaryota.
DR   GeneTree; ENSGT00940000157161; -.
DR   HOGENOM; CLU_000550_3_2_1; -.
DR   InParanoid; H2THE9; -.
DR   OMA; ICHRWED; -.
DR   TreeFam; TF315363; -.
DR   Proteomes; UP000005226; Chromosome 3.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd13983; STKc_WNK; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR024678; Kinase_OSR1/WNK_CCT.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR13902; SERINE/THREONINE-PROTEIN KINASE WNK WITH NO LYSINE -RELATED; 1.
DR   PANTHER; PTHR13902:SF10; SERINE_THREONINE-PROTEIN KINASE WNK2; 1.
DR   Pfam; PF12202; OSR1_C; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          158..416
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          83..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..121
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   635 AA;  70492 MW;  AA2B00C0658B5D67 CRC64;
     MLEPTGDGSH LDSVVRGGSD PAAYPSSSYR RIVHQRFIRR SLWFSDADEQ ALETPECDAA
     AVSGSGGTVL NVHLRTIVDR TRGTSCGIQE DSSTESQGGQ KDSATESASA DEEKEKCGNA
     LKPTGSEDAK ATVKAASEEN EEEAEMKAVS TSPGGRFLKF DIELGRGSFK TVYKGLDTET
     WVEVAWCELQ DRKLSKVERQ RFKEEAEMLK GLQHPNIVRF YDFWESPLKG KKCIVLVTEL
     MTSGTLKTYL KRFKVMKPKV LRSWCRQILK GLHFLHTRTP PIIHRDLKCD NIFITGPTGS
     VKIGDLGLAT LKAASFAKSV IGTPEFMAPE MYEEHYDEAV DVYAFGMCML EMATSEYPYS
     ECQNAAQIYR KVTSGVKPAS YNKVKDPEIK EIIGECICQK KEERYSIKDL LNHAFFAEDT
     GVRVELAEED DGKKASIALK LWVEDHKKLK GKYKESGAIE FTFDLEKEVP EVVAQEMVES
     GFFHESDSKT VGKSIRDRVA LIKWRRARTV SAAAALDQGD GAHPMQMPSH GISAGPTLIG
     QPLLEPEDSE ADQFNRLQNL PASATSVTYS TLDSGMGSTV YSDSHSSQQS VLYQSQLDPI
     TMTTQQVCIR SIYSQVDYVN VDLFKSLQAN IAEMV
//
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