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Database: UniProt
Entry: A0A3B4CA84_PYGNA
LinkDB: A0A3B4CA84_PYGNA
Original site: A0A3B4CA84_PYGNA 
ID   A0A3B4CA84_PYGNA        Unreviewed;       757 AA.
AC   A0A3B4CA84;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Eukaryotic elongation factor 2 kinase {ECO:0000256|PIRNR:PIRNR038139};
DE            EC=2.7.11.20 {ECO:0000256|PIRNR:PIRNR038139};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000008852.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000008852.1}
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_017539725.1; XM_017684236.1.
DR   RefSeq; XP_017539726.1; XM_017684237.1.
DR   AlphaFoldDB; A0A3B4CA84; -.
DR   STRING; 42514.ENSPNAP00000008852; -.
DR   Ensembl; ENSPNAT00000035080.1; ENSPNAP00000008852.1; ENSPNAG00000014517.1.
DR   GeneID; 108412273; -.
DR   CTD; 29904; -.
DR   GeneTree; ENSGT00940000157839; -.
DR   OrthoDB; 317178at2759; -.
DR   Proteomes; UP000261440; 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:0061300; P:cerebellum vasculature development; IEA:Ensembl.
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          138..348
FT                   /note="Alpha-type protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS51158"
FT   REGION          440..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..476
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   757 AA;  85703 MW;  47F466441EF710C4 CRC64;
     MMADDELMFS MEEVGSLKRS SGVRTVHFGN SSSVDDDEDD FYICPITDDP ASPAKEVCNY
     LKNIANSRPL SNSLPRNSFT YKNKNETEPE VQSVRFGSLT EKGRATWKHA IEKARAMPDP
     WAEFHLEDVE TEPCIRYRYN AITGGWAQDQ VFIKMSSQPF GKGAMRECYR AKKLSNFSHS
     SNWKSASNYV AKQYMETVGR DVYFEDVRLQ MEAKLWGEEY NRHRPPKQVD IMQMCVVEMT
     SRPGKPVYHL EHYIEGQYIK YNSNSGFVRD DNIRLTPQAF SHFTFERSGH QLIVVDIQGV
     GDLYTDPQIH TEKGTDFGDG NLGVRGMALF FHSHLCNKIC KSMGLTPFDM SPAESTQLDC
     TNKLLLSAKT MLRGCEEQCG SPRVRTTSLS RMPPILSQLS ETSSADENIS DVDSIPCSPL
     SLGLSADRSP KVWSFLNDMS ETDMDQKSSE NGGDSGYPSE RRSEGDLGEH NDRFRPVYSR
     HYSESDEDSV RRKAVVNASK LSVTVNSPDC HTLTEEKWSF FHSSRAHIHR PSCVAVEVER
     LNSLFLERKI GQSVLGKVHL AMVRYHEAGR FCEKDAPWDQ DSAMYHLERA AMCGELEAIV
     ALGQCYLQLP HHVLPEIKLE DSMENRKKGF NLLLQAAEAG DRPSMTLVAR AFDTGNSLPP
     DSTQDWKEAV RWYDCVLNMT DYDEGGEFDG MHDEPRYLLL AREAEMYQQG GFNLDADPQR
     AGDLFTEAAD AAMEAMKGRL ANQYYMKAEE AWSAMEE
//
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