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Database: UniProt
Entry: A0A091E2C6_FUKDA
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ID   A0A091E2C6_FUKDA        Unreviewed;       470 AA.
AC   A0A091E2C6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Calcium/calmodulin-dependent protein kinase type II subunit delta {ECO:0000256|ARBA:ARBA00039734};
DE            EC=2.7.11.17 {ECO:0000256|ARBA:ARBA00012434};
GN   ORFNames=H920_09426 {ECO:0000313|EMBL:KFO29186.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO29186.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO29186.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO29186.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) 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=2.7.11.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00000902};
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=2.7.11.17; Evidence={ECO:0000256|ARBA:ARBA00000517};
CC   -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC       {ECO:0000256|ARBA:ARBA00004278}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004278}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004278}. Sarcoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00037846}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00037846}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00037846}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. CaMK subfamily. {ECO:0000256|ARBA:ARBA00005354}.
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DR   EMBL; KN122621; KFO29186.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091E2C6; -.
DR   STRING; 885580.ENSFDAP00000006172; -.
DR   eggNOG; KOG0033; Eukaryota.
DR   Proteomes; UP000028990; Unassembled WGS sequence.
DR   GO; GO:0043226; C:organelle; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.450.50; -; 1.
DR   Gene3D; 6.10.140.620; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR013543; Ca/CaM-dep_prot_kinase-assoc.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR032710; NTF2-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24347:SF365; CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II SUBUNIT DELTA; 1.
DR   PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   Pfam; PF08332; CaMKII_AD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF54427; NTF2-like; 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   3: Inferred from homology;
KW   Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   Kinase {ECO:0000313|EMBL:KFO29186.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW   Sarcoplasmic reticulum {ECO:0000256|ARBA:ARBA00022951};
KW   Transferase {ECO:0000313|EMBL:KFO29186.1}.
FT   DOMAIN          1..231
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          308..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..325
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   470 AA;  52737 MW;  DDBDC4C8507D10CD CRC64;
     MKVSIGLTKS LQLTDNTADY LLSELIFLGQ GHFIASVGAP RRSGIMLAIS RVTGGELFED
     IVAREYYSEA DASHCIQQIL ESVNHCHLNG IVHRDLKPEN LLLASKSKGA AVKLADFGLA
     IEVQGDQQAW FGFAGTPGYL SPEVLRKDPY GKPVDMWACG VILYILLVGY PPFWDEDQHR
     LYQQIKAGAY DFPSPEWDTV TPEAKDLINK MLTINPAKRI TASEALKHPW IFQRSTVASM
     MHRQETVDCL KKFNARRKLK GAILTTMLAT RNFSGMCFFL FSAYPQINNK ANVITSPKEN
     IPTPALEPQT TVIHNPDGNK ESTESSNTTI EDEDVKARKQ EIIKVTEQLI EAINNRDFEA
     YTKICDPGLT AFEPEALGNL VEGMDFHRFY FENALSKSSK PIHTIILNPH VHLVGDDAAC
     IAYIRLTQYM DGSGMPKTMQ SEETRVWHRR DGKWQNVHFH RSGSPTVPIK
//
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