ID A0A3Q1BP40_AMPOC Unreviewed; 706 AA.
AC A0A3Q1BP40;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Eukaryotic elongation factor 2 kinase {ECO:0000256|PIRNR:PIRNR038139};
DE EC=2.7.11.20 {ECO:0000256|PIRNR:PIRNR038139};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000016065.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000016065.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 AlphaFoldDB; A0A3Q1BP40; -.
DR Ensembl; ENSAOCT00000024898.1; ENSAOCP00000016065.1; ENSAOCG00000021033.1.
DR GeneTree; ENSGT00940000157839; -.
DR Proteomes; UP000257160; 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 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:UP000257160};
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 106..316
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 706 AA; 79726 MW; 9BD322382EF4A15F CRC64;
MEEDGSAKRA PVQRSVQQLR TSSLSDANTS DDDDDDHFIS PILDDSARDV CHYLKNLVYS
RHTDSEYSFG WQAAWLHAIE KAKAMPDPWA QFHLEEIATE PCIRYRYNAV TGEWAQDQVH
IKMAAQPFGK GAMRECFRTK KLSNFSHSSN WKSASNYVAK RYMETVDRNV YFEDVRLQME
AKLWGEEYNR HKPPKQVDIM QMCVMEMAVR PGKPLFHLEH YIEGKYIKYN SNSGFVRDDN
IRLTPQAFSH FSFERSGHQL IVVDIQGVGD LYTDPQIHTE KGDDFGDGNL GVRGMALFFH
SHMCNKICKS MGLTPFDLAP AEKSQLDGTN KLLKSAQTVL RGCEEPCGSP RVRTFSTGRA
PPLLSRLSET SSADESMSDV DSAPCSPLIL PCSPLAAVGS MDSDFKHSHF LNSCLQESDS
GGDSGYPSER RSEGDPNDHV DGKVTFSLFF HLLVFMLLVS LQLTEEKWSF YHSSRAHVHR
PSCVATEVER LNSLLQKKIG QSILGKVHLA MVRYHEAGRF CEKDEPWDQN SAMFHLDRAA
LCGELEAIVA LGQCYLQLPH HILPDMELED NAGNRMKGFK YLLQAAEAGD RSSMIIMARA
FDTGINLSAD RSQDWEEAIH WYDSVLNMTD YDEGGEFDGT QDEPRYLLLA REAEMFQEGG
HNLTADPQRA GDLFTEAAEA AMAAMKGRLA NQYYMKAEEA WALMEE
//
