ID L5LDJ3_MYODS Unreviewed; 691 AA.
AC L5LDJ3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Diacylglycerol kinase theta {ECO:0000313|EMBL:ELK24414.1};
GN ORFNames=MDA_GLEAN10003923 {ECO:0000313|EMBL:ELK24414.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK24414.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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DR EMBL; KB112961; ELK24414.1; -; Genomic_DNA.
DR eggNOG; KOG1169; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR CDD; cd17111; RA1_DAGK-theta; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR InterPro; IPR037607; DGK.
DR InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF54; DIACYLGLYCEROL KINASE THETA; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00788; RA; 1.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50200; RA; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ELK24414.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 166..265
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT REGION 124..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 691 AA; 76074 MW; C22D120C1E8ECF91 CRC64;
MALGVPLAEA PRLHAQLESL DSWAAQGLTP GFVPTVCNFM SHEKCLRQVK TPCTSLAPSL
VRVHKQTLKI FDGSDAVHRN RFRVVSVPRL ARSEEVLEAA LRAYYITEDP RGFELQALPW
PLQAGDPRAG GKAWGGRTSE EEEGGRGPRS REVSPEAWII RTLPRTQDVL KIYPAWLKVG
VAYVSICVTP ESTARTVVLE VLPLLGRQAE GPESFQLEEV FMSSRQVQRT VLADEESLLN
RLRDIRQTSL RQMSQTRFYV AESKAVAPRV SLFVGGLPPG LSPQEYGSLL DEAVATKAGL
VTLSHVYPAQ GAVVLDVACF AEAERLYMLV RDTAVHGQLL TALVLPDVLH TKLPPDCCPL
LVFVNPKSGG LKGRDLGCSX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXCSR GAGPGGLPRP WRVVCPQIVQ MSNYCGIGID
AELSLDFHQA REEEPSKFTS RFHNKGVYVR VGLQKMSQAR SLHKEIRLQV EQQEVELPSI
EGLIFINIPS WGSGADLWGS DSDSRFEKPR MDDGLLEVDG EPWVQAPGHM IISAVGPKVH
MLRKAKQKPK KAGTPKDARA DEVPTPEGGL K
//
