ID A0A024V054_PLAFA Unreviewed; 1336 AA.
AC A0A024V054;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=diacylglycerol kinase (ATP) {ECO:0000256|ARBA:ARBA00012133};
DE EC=2.7.1.107 {ECO:0000256|ARBA:ARBA00012133};
GN ORFNames=PFFVO_02615 {ECO:0000313|EMBL:ETW18719.1}, PFFVO_05487
GN {ECO:0000313|EMBL:ETW15600.1};
OS Plasmodium falciparum Vietnam Oak-Knoll (FVO).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=1036723 {ECO:0000313|EMBL:ETW15600.1, ECO:0000313|Proteomes:UP000030690};
RN [1] {ECO:0000313|EMBL:ETW15600.1, ECO:0000313|Proteomes:UP000030690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vietnam Oak-Knoll {ECO:0000313|EMBL:ETW15600.1}, and Vietnam
RC Oak-Knoll (FVO) {ECO:0000313|Proteomes:UP000030690};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Hoffman S., Volkman S., Rosenthal P., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Annotation of Plasmodium falciparum Vietnam Oak-Knoll (FVO).";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETW15600.1, ECO:0000313|Proteomes:UP000030690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vietnam Oak-Knoll {ECO:0000313|EMBL:ETW15600.1}, and Vietnam
RC Oak-Knoll (FVO) {ECO:0000313|Proteomes:UP000030690};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium falciparum Vietnam Oak-Knoll (FVO).";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000256|ARBA:ARBA00009280}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KI925173; ETW15600.1; -; Genomic_DNA.
DR EMBL; KI925078; ETW18719.1; -; Genomic_DNA.
DR EnsemblProtists; ETW15600; ETW15600; PFFVO_05487.
DR EnsemblProtists; ETW18719; ETW18719; PFFVO_02615.
DR Proteomes; UP000030690; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR CDD; cd00029; C1; 1.
DR CDD; cd20805; C1_DGK_rpt2; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR037607; DGK.
DR InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF54; DIACYLGLYCEROL KINASE THETA; 1.
DR Pfam; PF00609; DAGK_acc; 2.
DR Pfam; PF00781; DAGK_cat; 1.
DR SMART; SM00045; DAGKa; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 2.
DR PROSITE; PS50146; DAGK; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 26..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 118..172
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 181..238
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 384..463
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT DOMAIN 923..993
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 473..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..599
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1146
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1336 AA; 157587 MW; 72D1DDCC0CE9522D CRC64;
MEDFAYIDKN VYINILLVFI KKIKDYIVGI GILKILFCVC IILLSIFIAK RKNKKKKKIH
VYLQLNRKKN NSTKVSNSSK KSTISNEDEI SQKNLSKISD NGKLEEISNG YYHLTYTSHI
FNLKTINRIE LCNVCEENIY SFFFHKKNIF ECIMCRNKCH IECAPNSNLM SCKTSVFFKN
KHKFIKLRNC SWNDKCDICD QKFYFFSLYT LLKRHIYKCI WCNKYFHLRC LIKNSYKKKK
IIKEDENVVD TQKMKNLCTY GNNEYILYPY QLTIKENVLI DFLISAYNKV QENDIKLDDI
FLSYTLNDFY NLEKKFKKDM IEPIEHFPSY KFRSVNDLLY FDYVNHFKSF RNIKKKKKKK
IIQIHLNFLL NFFPVHLPIY HIKSNKTFLL IFVNVKSGGQ TGKNLYQELL MYFNPIQIIN
IKNEKNVLNA LNMFKQMFYL KKIILLICGG DGTISIFIDT LIKFFLKQNS NNENKEQVQK
NEQVNKEPIL DNKNKTTSSN KTTFLNKTLT NITEKIRYNK DLLKKKWGGG TPTSQANNNT
NNHMNTQGGK LSSKFFLIKR KMKENKKNND NNDNDKYSTS EEDTSDFSDT DDEDGDEEEK
FSSIKEQLFK TKVNEDTLNV TENYEHIYRQ IKNFQNKDIH EKDDAYEDIT EENKNKIEQN
HKKKEKKKDN NKNNSSIMND HGSDINEDCY FSATGFEGES IYHNVYYDHN NKNSNDLHMT
TNISDNLCGY YGDTKKKKLK YIVKGDNNNG DSTMVSVPSN NKKKNNNNNN NNKTTITTTT
TTTITNNNDN NNDNNNDNNH NDNHNNNHNN NHNNNNNTNS SHNNSSIIIN NEDLHNMTDK
KNEGLNKINN IEEFNKGEMC MFEKQCNILE NINKDYKLLN TGYDEKSHID DETFFDSCDK
SKDDIQCTHS NLILKELSEE TNLEKDNEED NKYSLESCIS TTPISILPLG TGNDLSISLG
WGSEYNNDIF FYLNKLKHCK NELVDVWNMK GYDSNNNLIL NNSFINYFDI GIIARLALHF
DNIRKKYPHF FNSRIGNKIL YGEVGFRDFC FNTYKYKLNK NIKIYCDGKK VNIEENLESV
CIINIPYFLG GIKIWKDDEL EKNYYSDFEK ENNKMNDSEY ISDHEKADHH HHNNKKKKKK
KKKTKCKIKN NDSIINKDEK YNTDNINDNS FESYSSGTNI YNRYDNMYKK LYTDQDKQNI
MNNISLKKDL LINQTNINSP EIKNIEKFIN RNENASDYAN NIYKSYRLDS YKQKKRQHKY
RKQKINDKVI EVIGFRNIFH LFQVQIGMSK AIKLCQGSEI VVKINKKFIK NKNKIYFQYD
GEPGYLNIHK LHFTHK
//
