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Database: UniProt
Entry: K0T7D7_THAOC
LinkDB: K0T7D7_THAOC
Original site: K0T7D7_THAOC 
ID   K0T7D7_THAOC            Unreviewed;       854 AA.
AC   K0T7D7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EJK73550.1};
GN   ORFNames=THAOC_04819 {ECO:0000313|EMBL:EJK73550.1};
OS   Thalassiosira oceanica (Marine diatom).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC   Thalassiosiraceae; Thalassiosira.
OX   NCBI_TaxID=159749 {ECO:0000313|EMBL:EJK73550.1, ECO:0000313|Proteomes:UP000266841};
RN   [1] {ECO:0000313|EMBL:EJK73550.1, ECO:0000313|Proteomes:UP000266841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1005 {ECO:0000313|EMBL:EJK73550.1,
RC   ECO:0000313|Proteomes:UP000266841};
RX   PubMed=22835381; DOI=10.1186/gb-2012-13-7-r66;
RA   Lommer M., Specht M., Roy A.S., Kraemer L., Andreson R., Gutowska M.A.,
RA   Wolf J., Bergner S.V., Schilhabel M.B., Klostermeier U.C., Beiko R.G.,
RA   Rosenstiel P., Hippler M., Laroche J.;
RT   "Genome and low-iron response of an oceanic diatom adapted to chronic iron
RT   limitation.";
RL   Genome Biol. 13:R66-R66(2012).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. CDPK subfamily. {ECO:0000256|ARBA:ARBA00024334}.
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:EJK73550.1}.
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DR   EMBL; AGNL01004410; EJK73550.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0T7D7; -.
DR   EnsemblProtists; EJK73550; EJK73550; THAOC_04819.
DR   eggNOG; KOG0032; Eukaryota.
DR   OMA; VHARCAN; -.
DR   Proteomes; UP000266841; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00038; CAP_ED; 2.
DR   CDD; cd00051; EFh; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR24349:SF507; -; 1.
DR   PANTHER; PTHR24349; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00100; cNMP; 2.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266841}.
FT   DOMAIN          137..431
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          545..632
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          648..765
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          785..814
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          815..850
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   BINDING         171
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   854 AA;  95135 MW;  3D89D79255E577EA CRC64;
     MSPRLSTLAR TWTSKNAAWG TVAAAAAAAA ALAAWHPREV GDGDSGDAGD ALTCNLLVDE
     RGKVTSPDRG PSHDSLLLRI LGASQTSTNR HACHCESSGL KNEDKEIKRA NIQRSRTIRI
     LSSKATQNRK LSDVYDVNFD TPLGEGAFGK VLLVSHKQTG ERVAMKRIPK KLASREDFQR
     EMEALLRIQK WGGHPHICAL HEHFDEGGYY YLILDLVEGG EMFDHLVNHG AYSEADAARL
     VREVASALDF LHGIGVEEQV HNDVKPENLM LSSTAQRCGS IQLVDFGCAE VEGEDDDDDD
     HLDLDDIFSR KRGAKGSNKH VGQGGFTPAY SSPEAFEDRN AAPLPPSDMW ALGVIVYIML
     TGVHPFDIQG RATDEDIERE VRNCDAPLPL GPKHPFTRHL SPSARDLIAS LMERDPKKRL
     SAFEMLHHPW VTGETASTNI MIGSDQKLNR FRKFKTRLQT QFFADAVGWS DEAIAEETRR
     RTSLIERSFH AFDGSDLKMR KLLSNRKHGL LASELGLGLD NEPRNEVQEV DNRAEMTMSD
     YQDLLSENMK QKYFPKGHVI YNEGDTGRSM YFINSGTVIV STSDGIKNKR HSGDFFGEGA
     LLHPKGKHSA TITCKTPVHV IEISREYFEQ YMAEDTGVVL SLREKQKIRK RNRAKALLKL
     QSGMKTKKAA FGEVIYSEGD EGDSLYLVEK GKIDLTSGGH NVLVATEGNF CGEHSLLTGR
     LRNTTATCIN EEGCILERMS GYDFRKLMEA SPLVRESLVD LMNRRDFKKA MVLKLGESFP
     YGNPRKAFDA VDVGKKGYLD YQDIATLMRL LDKKYTDDEC SNVFETIDLS KDGKVTYNEF
     AKVFIGDIRA TASM
//
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