ID A0A0A0AKA7_CHAVO Unreviewed; 725 AA.
AC A0A0A0AKA7;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Eukaryotic elongation factor 2 kinase {ECO:0000256|PIRNR:PIRNR038139};
DE EC=2.7.11.20 {ECO:0000256|PIRNR:PIRNR038139};
GN ORFNames=N301_14968 {ECO:0000313|EMBL:KGL94476.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL94476.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL94476.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL94476.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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; KL872063; KGL94476.1; -; Genomic_DNA.
DR RefSeq; XP_009884759.1; XM_009886457.1.
DR AlphaFoldDB; A0A0A0AKA7; -.
DR STRING; 50402.A0A0A0AKA7; -.
DR GeneID; 104287727; -.
DR KEGG; cvf:104287727; -.
DR CTD; 29904; -.
DR OrthoDB; 317178at2759; -.
DR Proteomes; UP000053858; Unassembled WGS sequence.
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 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 Elongation factor {ECO:0000313|EMBL:KGL94476.1};
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:KGL94476.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053858};
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 357..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 725 AA; 82468 MW; DE791FD00141CF16 CRC64;
MADEDLIFRM EGIDNARSTT ANSGNYLDAD SDDEDNYFIC PITDDPVSNK SASIKVDNYY
SSLAKTEQYG SSSSPRNSFS FKETWKHAIQ KAKHMPDPWA EFHLEDIETE QATRYRYNAV
TGDWVEDEVL IKMASQPFGR GAMRECFRTK KLSNFLHTQN WKGAYNYVAK QYIESVGRDV
YFEDVQLQME AKLWGEEYNR HKPPKQVDIV QTCIIEMKNR PGKPLFHLEH YIEGTYIKYN
SNSGFVRDDN IRLTPQAFSH FTFERSGHQL IIVDIQGVGD LYTDPQIHTE NGTDFGDGNL
GVRGMALFFH SHSCNKICKS MGLAPFDLSS KEKDALDCNK KLLESAQTIL RGTEEKCGSS
RVRTVSGSRP PLLSRLSENS GDESMSDVAF DSLPCSPSSA TPHSQKMDML NWPVFNEVDN
LVHKDCDQLD NQRDFENGGD SGYPSEKRSE LEDLDHRERG HSNNNRRHES DEDSLGSSAR
VSVEKWSLYN ASRVHIHRPS CVAQEIQRLN ALELEKKIGK SVLGKVHLAM VRYHEAGRFC
EKDKEWDRES ALFHLEHAAD CGELEAIVGL GLMCSQLPHH ILSEVNLEDT KENRNKGFDY
LLRAAEAGDR PSMILVARAY DTGVNLGSDR VQDWKEALYW YNAALNMTDY DEGGEYDGTQ
DEPRYLLLAR EAEMLMTGGF HLNKDPQRSG ELYTEAAEAA MEAMKGRLAN QYYQKAEEAW
AMMEE
//
