ID A0A3Q2EHX4_CYPVA Unreviewed; 691 AA.
AC A0A3Q2EHX4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Eukaryotic elongation factor 2 kinase {ECO:0000313|Ensembl:ENSCVAP00000032001.1};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000032001.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000032001.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3Q2EHX4; -.
DR Ensembl; ENSCVAT00000027382.1; ENSCVAP00000032001.1; ENSCVAG00000021788.1.
DR GeneTree; ENSGT00940000157839; -.
DR Proteomes; UP000265020; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR004166; 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 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000265020};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 94..327
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 691 AA; 77996 MW; 003E199B0BD27BBF CRC64;
IMDDELMFSM EEEGSAQRPS SQRNGFKQRA SSLSDANASE DDDDEENFIS PILGESAKES
GNYLKDFAYN RQLSNSLPKT NFLYRAAWIK AIEKARAMPD PWAQFHLEEI ETEPCIRYRY
SAVTGEWAQD QIHIKMAAQK LSNFSHSSNW KSASNYVAKR YMETVDREVY FEDVRLQMEA
KLWGEEYNRH RPPKQVDIMQ MCVVEMTNRP GKPVFHLEHY IEGKYIKYNS NSGFVRDDNI
RLTPQPSIIS PFPPSGLQSL HGPSDPHREG NRFRRWESRY VSSLYSLMAT EIPQSDDIGV
PGVRGMALFF HSHLCNKICK SMGLTPFDLS EPESSQLDCT NKLLKSAKTV LRGCEEVCGS
PRVRTWSASR VPPLLSRLSD PSSADESASD VDSIPCSPLT LPFSPVVAPG SMGRSPSGTF
LKLYYSESES GGDSGYPSER RSEGDPNDHI DGMTDEKWTF FHSSRAHVHR SSCVATEVER
LNALMQKKIG QSILGKVHLA MVRYHEAGRF CEKDEQWDQD SAFFHLERAA LCGELEAIVA
LGKCYLQLPH HVLPDMEVEV KPGFKYLLQA AEAGDRSSMI IVARAFDTGF NLSADRSQDW
AEAIHWYDSA LNMMDYDEGG EFDGTQDEPR YLLLAREAEM YQEGGFNLTA DPQKAGDLFT
EAAEAAIAAM KGRLANQYYM KAEEAWALVE E
//