GenomeNet

Database: UniProt
Entry: A0A0P7Z520_SCLFO
LinkDB: A0A0P7Z520_SCLFO
Original site: A0A0P7Z520_SCLFO 
ID   A0A0P7Z520_SCLFO        Unreviewed;       904 AA.
AC   A0A0P7Z520;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=protein kinase C {ECO:0000256|ARBA:ARBA00012429};
DE            EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429};
GN   ORFNames=Z043_105035 {ECO:0000313|EMBL:KPP75696.1};
OS   Scleropages formosus (Asian bonytongue) (Osteoglossum formosum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Osteoglossidae; Scleropages.
OX   NCBI_TaxID=113540 {ECO:0000313|EMBL:KPP75696.1, ECO:0000313|Proteomes:UP000034805};
RN   [1] {ECO:0000313|EMBL:KPP75696.1, ECO:0000313|Proteomes:UP000034805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Aro1 {ECO:0000313|EMBL:KPP75696.1};
RA   Tan M.H., Gan H.M., Croft L.J., Austin C.M.;
RT   "The genome of the Asian arowana (Scleropages formosus).";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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=2.7.11.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00000946};
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=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000569};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. PKC subfamily. {ECO:0000256|ARBA:ARBA00005490}.
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:KPP75696.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JARO02001360; KPP75696.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7Z520; -.
DR   STRING; 113540.ENSSFOP00015012814; -.
DR   Proteomes; UP000034805; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd11630; HR1_PKN1_2; 1.
DR   CDD; cd11622; HR1_PKN_1; 1.
DR   CDD; cd05589; STKc_PKN; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.10.287.160; HR1 repeat; 3.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011072; HR1_rho-bd.
DR   InterPro; IPR036274; HR1_rpt_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR037317; PKN1_HR1_2.
DR   InterPro; IPR037313; PKN_HR1_1.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24351:SF242; PROTEIN KINASE C; 1.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF02185; HR1; 3.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00742; Hr1; 3.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF46585; HR1 repeat; 3.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS51860; REM_1; 3.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01207};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KPP75696.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034805};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          43..119
FT                   /note="REM-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51860"
FT   DOMAIN          129..217
FT                   /note="REM-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51860"
FT   DOMAIN          219..300
FT                   /note="REM-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51860"
FT   DOMAIN          541..836
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          837..904
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          77..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          122..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          869..890
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   904 AA;  101989 MW;  BEED6C3B42171A3F CRC64;
     MASDGSMLES LGEKAEDGAH PDPESASDPG GLSVLEQLGL DQNSDFSDSS VQQRLDEQRE
     RIRREIRKEL KIKEGAENLR RATTDKRNAQ QVENQLRSSN RRLDALHTQL QELDAHIVVK
     GSDDTRDDAP QSPGAVSHTS TNQDRIAALE RQLNIELKVK QGAENMIPIY ANGPTKVLSV
     LHDKKLLQTA QQMLQDSKTK IDIIRMQIRK AVQASEQHTE DMQGKPDLCG VELRIEELRH
     HYRVEHAVAE GAKNVLRLLG ASKVQDRKAM SEAQCRLSES TQRLDLLRDS LEQRLADLPE
     DHPKACLIKE ELVLASSPAF SSRHGAPYLH NQYSTLSKPS PLTGTLQVQL LGCVGLLEVV
     PGRSRGTPVL LPCYSPGEGR SFMRSGKGLY SRSGSMSGKV PSKSDELSSE VSAVLKLENT
     VVGQTAWRTV GEQAWNQTFT LELERSREME IAVYWKDYRS LCALKYLKLE DFLDNQKHQV
     QLELEPQGLL LAEVTFFNPI IDRVPRLRRQ KKIFSKQQGK AFLRSRPVNV DIATWVRLLK
     NAIPTVNNSG TYSPSAHAHN AGEISVEKLS LDSESPQRSE PRRDLDAHTP VLLSEYKKTG
     TMYAIKALKK GDIIARDEVE SLMCEKRIFE TVNISRHPFL VNLFACFQTP EHVCFVMEYT
     AGGDLMMHIH ADVFTEPRAM FYAACVVLGL HFLHDHKIVY RDLKLDNLLL DTEGYVKIAD
     FGLCKEGMGY GDRTSTFCGT PEFLAPEVLT DTSYTRAVDW WGLGVLVYEM LVGESPFPGD
     DEEEVFDSIV NDEVRYPRFL STEAIGLMRR LLRRNPDRRL GSSEKDAEDV KKQPFFRGMD
     WEALLQKKLP PPFIPSIVGK EDVSNFDEEF TAELPTLTPP REPRTLSRKD QDSFRDFDYV
     SDLC
//
DBGET integrated database retrieval system