ID F7A4C9_CALJA Unreviewed; 723 AA.
AC F7A4C9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=Eukaryotic elongation factor 2 kinase {ECO:0000256|PIRNR:PIRNR038139};
DE EC=2.7.11.20 {ECO:0000256|PIRNR:PIRNR038139};
GN Name=EEF2K {ECO:0000313|EMBL:JAB27925.1};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|EMBL:JAB27925.1};
RN [1] {ECO:0000313|EMBL:JAB27925.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Bladder {ECO:0000313|EMBL:JAB05366.1}, Cerebellum
RC {ECO:0000313|EMBL:JAB52012.1}, Cerebral cortex
RC {ECO:0000313|EMBL:JAB27925.1}, Hippocampus
RC {ECO:0000313|EMBL:JAB13212.1}, and Skeletal muscle
RC {ECO:0000313|EMBL:JAB34604.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[translation elongation factor 2] + ATP = [translation
CC elongation factor 2]-phosphate + ADP + H(+); Xref=Rhea:RHEA:21436,
CC Rhea:RHEA-COMP:11268, Rhea:RHEA-COMP:11269, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
CC ChEBI:CHEBI:456216; EC=2.7.11.20;
CC Evidence={ECO:0000256|PIRNR:PIRNR038139};
CC -!- ACTIVITY REGULATION: Undergoes calcium/calmodulin-dependent
CC intramolecular autophosphorylation, and this results in it becoming
CC partially calcium/calmodulin-independent.
CC {ECO:0000256|PIRNR:PIRNR038139}.
CC -!- SUBUNIT: Monomer or homodimer. {ECO:0000256|PIRNR:PIRNR038139}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Alpha-type
CC protein kinase family. {ECO:0000256|PIRNR:PIRNR038139}.
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DR EMBL; GAMT01006495; JAB05366.1; -; mRNA.
DR EMBL; GAMT01006494; JAB05367.1; -; mRNA.
DR EMBL; GAMS01009924; JAB13212.1; -; mRNA.
DR EMBL; GAMS01009923; JAB13213.1; -; mRNA.
DR EMBL; GAMR01006007; JAB27925.1; -; mRNA.
DR EMBL; GAMQ01007247; JAB34604.1; -; mRNA.
DR EMBL; GAMP01000743; JAB52012.1; -; mRNA.
DR EMBL; GAMP01000742; JAB52013.1; -; mRNA.
DR RefSeq; XP_002756013.1; XM_002755967.3.
DR AlphaFoldDB; F7A4C9; -.
DR STRING; 9483.ENSCJAP00000016581; -.
DR eggNOG; ENOG502QVA3; Eukaryota.
DR HOGENOM; CLU_382143_0_0_1; -.
DR InParanoid; F7A4C9; -.
DR OrthoDB; 317178at2759; -.
DR TreeFam; TF316085; -.
DR Bgee; ENSCJAG00000009038; Expressed in cerebellum and 6 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004686; F:elongation factor-2 kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd16967; Alpha_kinase_eEF2K; 1.
DR Gene3D; 3.20.200.10; MHCK/EF2 kinase; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR004166; a-kinase_dom.
DR InterPro; IPR017400; eEF-2K.
DR InterPro; IPR047588; eEF2K_a_kinase_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR45992:SF2; EUKARYOTIC ELONGATION FACTOR 2 KINASE; 1.
DR PANTHER; PTHR45992; EUKARYOTIC ELONGATION FACTOR 2 KINASE-RELATED; 1.
DR Pfam; PF02816; Alpha_kinase; 1.
DR PIRSF; PIRSF038139; Elongation_factor_2_kinase; 1.
DR SMART; SM00811; Alpha_kinase; 1.
DR SUPFAM; SSF81901; HCP-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51158; ALPHA_KINASE; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR038139};
KW Calcium {ECO:0000256|PIRNR:PIRNR038139};
KW Calmodulin-binding {ECO:0000256|PIRNR:PIRNR038139};
KW Elongation factor {ECO:0000313|EMBL:JAB27925.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR038139};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR038139};
KW Protein biosynthesis {ECO:0000313|EMBL:JAB27925.1};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR038139};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR038139}.
FT DOMAIN 114..324
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 11..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 723 AA; 81762 MW; C5B5CFB2DB4DC9A3 CRC64;
MADEDLIFRL EGVDGGPRAG HDGGSDGDSD DEEGYFICPI TDDPRSNQNV NSKVNKYCSN
LMKSERYGSS GSPANSFHVK EAWKHAIEKA KHMPDPWAEF HLEDIATERA TRHRYNAVTG
EWVNDEVLIK MASQPFGRGA MRECFRTKKL SNFLHAQQWK GASNYVAKRY IEPVDRDVYF
EDVRLQMEAK LWGEEYNRHK PPKQVDIMQM CILELKDRPG QPLFHLEHYI EGKYIKYNSN
SGFVRDDNIR LTPQAFSHFT FERSGHQLIV VDIQGVGDLY TDPQIHTEMG TDFGDGNLGV
RGMALFFYSH ACNRICESMG LAPFDLSPRE RDAVNQNTKL LQSAKTILRG TEEKCGSPRI
RTLSGSRPPL LRPLSENSGD ENMSDMTFDS LPSSPSSATP HSQKLDHLHW PVFTDLDNMA
SRDHDHLDNH RDSENSGDSG YPSEKRGDLD DPEPREHGHS NGNRKYESDE DSLGSSGRVC
VEKWNLLNSS RLHLPRASAV ALEVQRLNAL DLEKKIGKSI LGKVHLAMVR YHEGGRFCKK
GEEWDQESAV FHLEHAADLG ELEAIVGLGL MYSQLPHHIL ANVSLKETQE NKTKGFDYLL
KAAEAGDRQS MILVARAFDA GQNLSPDRCQ DWLEALHWYN TALEMTDCDE GGEYDGMQDE
PRYTLLAREA EMLFTGGYGL KKDPQRSGDL YTQAAEAAME AMKGRLANQY YQKAEEAWAQ
MEE
//
