ID A0A0V1MLL1_9BILA Unreviewed; 2019 AA.
AC A0A0V1MLL1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Diacylglycerol kinase {ECO:0000256|RuleBase:RU361128};
DE Short=DAG kinase {ECO:0000256|RuleBase:RU361128};
DE EC=2.7.1.107 {ECO:0000256|RuleBase:RU361128};
DE Flags: Fragment;
GN Name=Dgkb {ECO:0000313|EMBL:KRZ72737.1};
GN ORFNames=T10_970 {ECO:0000313|EMBL:KRZ72737.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ72737.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ72737.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ72737.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-
CC phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608,
CC ChEBI:CHEBI:456216; EC=2.7.1.107;
CC Evidence={ECO:0000256|ARBA:ARBA00001383,
CC ECO:0000256|RuleBase:RU361128};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000256|ARBA:ARBA00009280, ECO:0000256|RuleBase:RU361128}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000256|ARBA:ARBA00010044}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC family. {ECO:0000256|ARBA:ARBA00010550}.
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:KRZ72737.1}.
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DR EMBL; JYDO01000074; KRZ72737.1; -; Genomic_DNA.
DR Proteomes; UP000054843; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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 GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd20799; C1_DGK_typeI_rpt1; 1.
DR CDD; cd00051; EFh; 1.
DR CDD; cd19501; RecA-like_FtsH; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 3.40.1690.20; -; 1.
DR Gene3D; 1.10.238.110; Diacylglycerol kinase alpha; 2.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.760; Peptidase M41; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR029477; DAG_kinase_typeI_N.
DR InterPro; IPR038199; DGK_typeI_N_sf.
DR InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR43655; ATP-DEPENDENT PROTEASE; 1.
DR PANTHER; PTHR43655:SF8; PARAPLEGIN; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF14513; DAG_kinase_N; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF01434; Peptidase_M41; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF47473; EF-hand; 2.
DR SUPFAM; SSF140990; FtsH protease domain-like; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU361128};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Kinase {ECO:0000256|RuleBase:RU361128, ECO:0000313|EMBL:KRZ72737.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU361128};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|RuleBase:RU361128};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..2019
FT /note="Diacylglycerol kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012384740"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 580..598
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 66..106
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1376..1411
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1472..1523
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1538..1584
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1641..1780
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 180..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ72737.1"
SQ SEQUENCE 2019 AA; 228659 MW; 8BF0B13A0FE017D9 CRC64;
LLFFLFPFSI MSTISDDSEK NSKTTNSTGK VWQMTAYERQ RVRHDPITDD SVLSLSPRSL
SSELMCPICL DMLKNTMTTK ECLHRFCQDC ITTALRSGNK ECPTCRCKLV SKRSLRPDPN
FDGIITKIYP SREEYDAMEA EAFDKMKKHH STISLQRSIQ EGMKFQSQLR RLNRFACMMD
ERERRRKRKE SEITAANPKQ KSSSENSSES PRASSSTSDR QFGFLIKPHP NMIFSKSFPS
FLTEPRYLTS NVLVSIDHVI DYLAMRIRFD YEGSKNCTIV DQKLLDFLDR LANFDETKGC
PVPCQLFIMS ENSEMIRVDN EHSSIEMLSR KHCAENKPIE LYFSYPELFS EDKPSSSSAE
TSVMQMLMVF TEFHLTYMRK PSMSSIISFR QHSFQKSVIR LLRRFYVPYL LHPVGHHRCL
SLQFFTRFAA VRCFHKSAKF YQRNQSENPN DSNEKPKPPE NNVSNFIVAL LYAFTLAVCI
SYWSNSNIED TYLIPWNMFV YEMLAKGEVE EVIVVPDSDI VTIRLYANAV IRNHVAPRRI
YHMRVSEIHN FEENLRKAEE SLGITAESAV SVVYHRNSTW PIILFATVFF FLLLRAFFRL
GSRGGKATKF PVVNFYDSFR KARFRIVRPF VSSTVPRIHF SDVVGLSEAK VEVKEFVDYL
KRPAAYTRLG AKLPKGALLL GPPGCGKTLL AKAVSTEASV PFLAINGTEF VEIIGGLGAA
RVRDLFKEAK RQMPCIIYID EIDAIGRARR GDANYPSAFQ SSEEEQTLNQ LLVEMDGMDT
TKGIIILAST NRPDILDKAL LRRGRFDRHI LIDLPTAKER AEIFEYYLKK IKLSTKINFE
NYLSDRTPGF SGADIKNVCN EAAIRAATLG KTGVELCDIE YALERAVIGS EKKSSVMTLK
EKERIAYHES GHALVGWLLK YTKALLKLSI IPRTKNVTGM GFSQHAQSEK HLLTRDELMD
RMCMALGGRA AENIVFGQVS SGAEDDLKKV TRTAYAMIKV FGMHEKIGPI SFGRVSDERE
GDFMRKPYSK KLQAMMDEEV ALLVGQINKK AETILRNNRE KLDLIAKKLL RCETIVYDDL
VELIGEPPYG PKGGTLNEIQ LPDNVMIETE SDKNNFGNKI SQMKYVECSV LVMWIMKVTD
DNDYVCQSAL MMTADPVFAF QLCLVESAKS FGKIVQFSMT SSACGRSIFC GKHVKWRKLT
PAEFEKLHDR TKELKQVMVA FQDGGALAKY RRPNETVDFE GFKALLDLYL ETDIPFDLCL
HLFRSFIKDR TKDEEVAFQT TTQSNCKTNR GSLAASTISN TACTPSSRRS SFTLSENKLN
IHDYIQRKCR NQEQHDSRLF FLGLTNDQSE TSTCQCSAVV RLKDIDCYFS LLENGTPEEK
LEYTFHLYDA DGNGYLDSNE IECIIEQMMS VAEHLAWDTV ELKPILRDML LEIDYDADGT
VSLEEWKRGG LTTIPLLVLL GIDSQALRED GTHMWRLKHF NKPTYCNLCM KRLVSFSGKQ
GLCCTLCKYT VHERCAGGAA NNCISTYAKS KRETSIMIHH WVDSNCSERC VRCKKHIKAL
EGKRCRWCKG EIHQRCLNDW DVKCNLGKLA HHILPPTSLV PLVLTERRRS SSKSFKMGQN
SSTNNGSLSS AMPSFEIDIS PDTKPLLVLL NPKSGGKQGT KLYRKLQYLL NPRQVFLLDN
NGPLEGLKMF QNISNMNILC CGGDGTVKWV LDAMDQINYG DNRPPVAVLP LGTGNDLSRC
LNWGGGFAGK TGNDLIAFLK SIEKSRVVTL DRWETNLIEN DDSEKGDAMP NNIITNYFSV
GVDASIAHRF HTMREKYPEK FSSRMKNKLW YFEFATSESL QATCKNLHEY VEIHCDGSPL
NLDSGPPLEG IAFLNIPSIY GGSNLWGRNA SAAKSKRFWG IGSLGLRPNS ESLTNSCNLL
GNNQDMGDKK IEVVGIQSVI SMGQVKAGLR TSAKRLAQCS SAIIKTKKRF PMQIDGEPWV
QQPCTISIAH KNQVPMLQAN KKAHLHKSFG CINQACSES
//
