ID A0A0M0J5U1_9EUKA Unreviewed; 992 AA.
AC A0A0M0J5U1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Protein kinase domain containing protein {ECO:0000313|EMBL:KOO21707.1};
GN ORFNames=Ctob_001726 {ECO:0000313|EMBL:KOO21707.1};
OS Chrysochromulina tobinii.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC Chrysochromulinaceae; Chrysochromulina.
OX NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO21707.1, ECO:0000313|Proteomes:UP000037460};
RN [1] {ECO:0000313|Proteomes:UP000037460}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460};
RX PubMed=26397803; DOI=10.1371/journal.pgen.1005469;
RA Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., Jha R.K.,
RA Patterson J., Monnat R.J. Jr., Barlow S.B., Starkenburg S.R.,
RA Cattolico R.A.;
RT "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin:
RT Metabolic Tools for Enhanced Algal Fitness in the Prominent Order
RT Prymnesiales (Haptophyceae).";
RL PLoS Genet. 11:e1005469-e1005469(2015).
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:KOO21707.1}.
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DR EMBL; JWZX01003341; KOO21707.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0J5U1; -.
DR OrthoDB; 10768at2759; -.
DR Proteomes; UP000037460; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 2.
DR CDD; cd05123; STKc_AGC; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
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; IPR004182; GRAM.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045270; STKc_AGC.
DR PANTHER; PTHR24353:SF37; CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT PRKX; 1.
DR PANTHER; PTHR24353; CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASE; 1.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF02893; GRAM; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00615; RGS; 1.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00315; RGS; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50132; RGS; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; cGMP {ECO:0000256|ARBA:ARBA00022535};
KW cGMP-binding {ECO:0000256|ARBA:ARBA00022992};
KW Kinase {ECO:0000313|EMBL:KOO21707.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000037460};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 48..111
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 351..456
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 501..639
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 654..911
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 683
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 992 AA; 110981 MW; E53CFF2D44713BA1 CRC64;
MGCAGSKAGG AEGSAKGHAH GRSMSSHFQP EKDAEAFREA LFRDVGLPKT YKDGEAIITE
GQASDSAIFI RKGTATILKG TKEVAKRSKG DLIGEMTLLL GDLPGSSVIA AGTVEAYVVQ
HSRLAEHIAS DPEKCGRVFR MLASTLSDRI SEASSKMRAE VVAKNAKNTI TAKKPQGDTT
LNVAKYRQLF ALDKDEPLVL RTTCSMRKEA NALKDANVSF GDMYLFEKHL CFDWKVFGFH
KQQTVDLTDV VALLKSTELA NTVEVQCKGY SLELTLPESC EETWVQMEQC RRQATAAALQ
AASAELGPTK AQVYEEVDKT IMDALELGKS GGHTARESPR ASSGSSQTHG LSMDLTEMDW
SLFLSGAKQM RFKKGDSVLR EGMPTRALYQ ILQGSLRVEL QLKDQPTAVV VGHRGPGEMF
GETSLLKSGC ATASIVTDSE EAILVCVDGA YLESLFTSHP KLPGRFFAFL ASYQARRLRN
LTEAFSNEKR QVAGQHLANV SIHEILQNPA YMGIFRKFIS KACEDRADER EAYTMSLAMF
EFWMDVQDFR SEPEPPQLLD MGTRIYEHFI KSDGVMRLSC FTETQRAAIK TELGKLTVGS
LDIKEARKLF DEAQKIAVSA IEDQCMSPFL SSEHFAYILE LKAKEGRVPG LPDFRLIRVL
GQGGFGQVLE VVKRDCGKHY AMKVMHKEMM RRSLGSSWRR KIHLEKDLMA CLHHPFLVNL
SYAFQNTEFL VLVMDLVPAG DLSEFVLTKK RLTAEQVRFI MMEVVCVIGY CHQQNVLYRD
MKPENLLIDE EGHVRMIDMG LAARVSKKQP KRRSRVGTDC YMAPEVRWAK DRREPYGMSC
DWYTVGVLMY EFSAGTVPYA HPEDENPQYR PHDFKDSAAE SLVMGLLHQD HNVRLGCDSR
GIAGILDHPY WRGIDWDLVP LKKFDSPCVN LKAPAKRKKD KENLAVQIAN DISEAEREAP
DQEYEVAEWD FVSPTAVVDE YMENMYQCVS SI
//
