ID A0A218V7B4_9PASE Unreviewed; 747 AA.
AC A0A218V7B4;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, 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|EMBL:OWK61884.1};
GN ORFNames=RLOC_00007215 {ECO:0000313|EMBL:OWK61884.1};
OS Lonchura striata domestica (Bengalese finch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Lonchura.
OX NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK61884.1, ECO:0000313|Proteomes:UP000197619};
RN [1] {ECO:0000313|EMBL:OWK61884.1, ECO:0000313|Proteomes:UP000197619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=White83orange57 {ECO:0000313|EMBL:OWK61884.1};
RA Colquitt B.M., Brainard M.S.;
RT "Genome of assembly of the Bengalese finch, Lonchura striata domestica.";
RL Submitted (MAY-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWK61884.1}.
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DR EMBL; MUZQ01000034; OWK61884.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218V7B4; -.
DR STRING; 299123.ENSLSDP00000005835; -.
DR Proteomes; UP000197619; 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:OWK61884.1};
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:OWK61884.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000197619};
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 132..342
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 70..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 747 AA; 85141 MW; 0448F6071415FB59 CRC64;
MADEDLIFRM EGIDNARTTP VDSGNYLDAD SDDEDNYFIC PITDDPVSNK SANAKVDNYY
SSLAKTEQYS SSSSPRSFSF KNDTQHRSKH GSVVDHGRET WKHAIEKAKH MPDPWAEFHL
EDIETEHATR YRYNAVTGDW VEDEVLIKMA SQPFGRGAMR ECFRTKKLSN FLHTQNWKGA
YNYVAKQYIE SVSRDVYFED VRLQMEAKLW GEEYNRHKPP KQVDIVQTCI IEMQNRPGKP
LFHLEHYIEG KYIKYNSNSG FVRDDSIRLT PQAFSHFTFE RSGHQLIVVD IQGVGDLYTD
PQIHTESGKD FGDGNLGVRG MALFFHSHFC NNICKSMGLA PFDLSSKEKD ALDYNKKLLE
SAQTILRGTE EKCGSSRVRT VSGSRPPLLF RLSENSGDES MSDVAFDSLP CSPSSATPHS
HKVDMLNWPV FSEVDNLDHL DNKRDFENGG DSGYPSEKRS ETEDLDHRER GHSNNNRKQE
SDEDSLGSSA RISVEKWNLY NSSRVHIHRP SCVAQEIQRL NALELEKKIG KSVLGKVHLA
MVRYHEAGRF CEKDKEWDQE SALFHLEHAA DCGELEAIVG LGLMCSQLPH HIISEVTLED
TKENRNKGFN YLLRAAEAGD RPSMILVARA YDTGVNLGAD REPSSEIIFD FRAQDWKEAL
HWYNAALNMT DYDEGGEYDG TQDEPRYLLL AREAEMLMMG GFNLDKDPQR SGELYTEAAE
AAMEAMKGRL ANQYYQKAEE AWAMMEE
//
