ID A0A2K6UGH0_SAIBB Unreviewed; 725 AA.
AC A0A2K6UGH0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
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|Ensembl:ENSSBOP00000031009.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000031009.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000031009.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 RefSeq; XP_010339071.1; XM_010340769.1.
DR AlphaFoldDB; A0A2K6UGH0; -.
DR STRING; 39432.ENSSBOP00000031009; -.
DR Ensembl; ENSSBOT00000047897.1; ENSSBOP00000031009.1; ENSSBOG00000031730.1.
DR GeneID; 101029579; -.
DR KEGG; sbq:101029579; -.
DR CTD; 29904; -.
DR GeneTree; ENSGT00940000157839; -.
DR OrthoDB; 317178at2759; -.
DR Proteomes; UP000233220; Unplaced.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0031952; P:regulation of protein autophosphorylation; IEA:Ensembl.
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 3: Inferred from homology;
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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR038139};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR038139};
KW Reference proteome {ECO:0000313|Proteomes:UP000233220};
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 116..326
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 725 AA; 82175 MW; 3E990EC623DF91B2 CRC64;
MADEDLIFRL EGVDGGQSPR AGHDGDSDGD SDDEEGYFIC PITDDPRSNQ NVNSKVNKYC
SNLTKSERYG SSGSPANSFH VKEAWKHAIE KAKHMPDPWA EFHLEDIATE RATRHRYNAV
TGEWVDDEVL IKMASQPFGR GAMRECFRTK KLSNFLHAQQ WKGASNYVAK RYIEPVDRDV
YFEDVRLQME AKLWGEEYNR HKPPKQVDIM QMCILELKDR PGQPLFHLEH YIEGKYIKYN
SNSGFVRDDN IRLTPQAFSH FTFERSGHQL IVVDIQGVGD LYTDPQIHTE TGTDFGDGNL
GVRGMALFFY SHACNRICES MGLAPFDLSP RERDAVNQNT KLLQSAKTIL RGTEEKCGSP
RVRTFSGSRP PLLRPLSENS GDENMSDMTF DSLPSSPSSA TPHSQKLEHL HWPVFSDLDN
MVSRDPDHLD NHRDSENSGD SGYPSEKRGD LDDPEPREHG HSNGNRKYES DEDSLGSSGR
VCVEKWNLLN SSRLHLPRAS AVALEVQRLN ALDLEKKIGK SILGKVHLAM VRYHEGGRFC
KKGEEWDQES AVFHLEHAAD LGELEAIVGL GLMYSQLPHH ILADVSLKET EENKTKGFDY
LLKAAEAGDR QSMILVARAF DTGQNLSPDR CQDWLEALHW YNTALEMTDC DEGGEYDGMQ
DEPRYMLLAR EAEMLFMGGY RLKKDPQRSG DLYTQAAEAA MEAMKGRLAN QYYQKAEEAW
AQMEE
//
