ID A0A3B5BM20_9TELE Unreviewed; 730 AA.
AC A0A3B5BM20;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-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};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000029722.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000029722.1}
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 AlphaFoldDB; A0A3B5BM20; -.
DR Ensembl; ENSSPAT00000030205.1; ENSSPAP00000029722.1; ENSSPAG00000022346.1.
DR GeneTree; ENSGT00940000157839; -.
DR Proteomes; UP000261400; 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 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 136..346
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 730 AA; 82221 MW; BAF6371376C53271 CRC64;
MEDDLMFSME EDGSAKRPPE QRSVLQLRAS SLSDANASDD DDEDFICPIL DDSAREVCHY
LKNLVYSRQL SNSPRNNLVY KSDETDTAAE HRTYKVLSET ARAAWLHAIA KAKAMPDPWA
QFHLEEIATE PCIRYRYNAV TGEWAQDQVH IKMAAQPFGK GAMRECFRTK KLSNFSHSSN
WKSASNYVSK RYMETVDRNV YFEDVRLQME AKLWGEEYNR HKPPKQVDIM QMCVMEMTER
PGKPLFHLEH YIEGQYIKYN SNSGFVRDDN IRLTPQAFSH FSFERSGHQL IVVDIQGVGD
LYTDPQIHTE KGDDFGDGNL GVRGMALFFH SHLCNKICKS MGLTPFDLSS PEKSQLDCTN
KLLKSAQTVL RGSEEPCGSP RVRTFSASRA PPLLSRLSET SSADESMSDV DSAPCSPLIL
PCSPLAAVAS MGKSPTGLSF AGMSEHERLH NNNNNTGEHK DPDSGGDSGY PSERRSEGDP
NDHVDGLTEE KWSFYHSSRA HVHRPSCVAT EVERLNTLLQ KKIGQSILGK VHLAMVRYHE
AGRFCEKDEQ WDQDSAMFHL ERAALCGELE AIVALGQCCL QLPHHILPDI ELEDNAGNRM
KGFKYLLLAA EAGDRSSMII VAKAFDTGIN LSAERKQDWE EAVHWYDSAL NMTDYDEGGE
FDGTQDEPRY LLLAREAEMF QEGGHNLKAD PQRAGDLFTE AAEAAMEAMK GRLANQYYMK
AEEAWALMEE
//
