ID A0A197SJW5_9ACTN Unreviewed; 543 AA.
AC A0A197SJW5;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN ORFNames=A8W25_27105 {ECO:0000313|EMBL:OAR23174.1};
OS Streptomyces sp. ERV7.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1322334 {ECO:0000313|EMBL:OAR23174.1, ECO:0000313|Proteomes:UP000078470};
RN [1] {ECO:0000313|EMBL:OAR23174.1, ECO:0000313|Proteomes:UP000078470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERV7 {ECO:0000313|EMBL:OAR23174.1,
RC ECO:0000313|Proteomes:UP000078470};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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:OAR23174.1}.
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DR EMBL; LYOY01000051; OAR23174.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A197SJW5; -.
DR STRING; 1322334.A8W25_27105; -.
DR Proteomes; UP000078470; 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:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.200.40; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR007168; Phageshock_PspC_N.
DR InterPro; IPR045540; YegS/DAGK_C.
DR PANTHER; PTHR12358:SF54; SPHINGOID LONG-CHAIN BASES KINASE 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12358; SPHINGOSINE KINASE; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF04024; PspC; 1.
DR Pfam; PF19279; YegS_C; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000078470};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 282..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 330..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 354..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..96
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 230..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..253
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 543 AA; 56333 MW; AD15BA14F8FF868B CRC64;
MTERPGHAQQ LARTAGGPGG PAVLVCVGGD GTAHEIMTGL LAGREERRAA LLVLPGGRGN
SFYRELWSDR PWPAALEAAL SAPRVRHVDL ARIAETGELA LLGASSGLAA QALTSVRDAL
GTGRRRYQTA VARTMLAFRP YRGRVSVDGV VVQSGETVSV LVGGGRRRGG QFMPLPRSVL
DDGLLDICVA GAELPLREMV RLARDGSHVG HEGVVYTWGR VPHPPTARHH GVMTQPTETP
VAPPDPDPGP VPAAPQLRRS GHNKVIGGVC GGLGRYCDID PVIFRVALGV LTVTGGLGLV
FYGFGWLLLP LDDEDENEAR RLLSGRVEGP ALAAVLMALA GCGIFLSMLN NGSVMSFAGL
LTVAVAGIGV WSQRRSVMPP DAPPDAVTAQ TVGGTPSPRR SPSTTVRRSA AERALPLRSP
LARPSTVLAA RSAPTAAAAT DPRARTAIPP SAAQSIFEGW AWVVWRVKTT AAVPHSTAAT
AGSTAVRSSW GRMRPSVDGG CPLGGRPAGA GALAGAAGGC GRCAVRPCRP PSRRSDRAAG
ARR
//
