ID A0AA39XYR0_9PEZI Unreviewed; 537 AA.
AC A0AA39XYR0;
DT 24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2024, sequence version 1.
DT 28-JAN-2026, entry version 10.
DE SubName: Full=ATP-NAD kinase-like domain-containing protein {ECO:0000313|EMBL:KAK0641996.1};
GN ORFNames=B0T16DRAFT_462020 {ECO:0000313|EMBL:KAK0641996.1};
OS Cercophora newfieldiana.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Lasiosphaeriaceae; Cercophora.
OX NCBI_TaxID=92897 {ECO:0000313|EMBL:KAK0641996.1, ECO:0000313|Proteomes:UP001174936};
RN [1] {ECO:0000313|EMBL:KAK0641996.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SMH2532-1 {ECO:0000313|EMBL:KAK0641996.1};
RG Lawrence Berkeley National Laboratory;
RA Hensen N., Bonometti L., Westerberg I., Brannstrom I.O., Guillou S.,
RA Cros-Aarteil S., Calhoun S., Haridas S., Kuo A., Mondo S., Pangilinan J.,
RA Riley R., Labutti K., Andreopoulos B., Lipzen A., Chen C., Yanf M.,
RA Daum C., Ng V., Clum A., Steindorff A., Ohm R., Martin F., Silar P.,
RA Natvig D., Lalanne C., Gautier V., Ament-Velasquez S.L., Kruys A.,
RA Hutchinson M.I., Powell A.J., Barry K., Miller A.N., Grigoriev I.V.,
RA Debuchy R., Gladieux P., Thoren M.H., Johannesson H.;
RT "Genome-scale phylogeny and comparative genomics of the fungal order
RT Sordariales.";
RL Submitted (JUN-2023) 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:KAK0641996.1}.
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DR EMBL; JAULSV010000006; KAK0641996.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AA39XYR0; -.
DR Proteomes; UP001174936; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0016020; C:membrane; IEA:TreeGrafter.
DR GO; GO:0001727; F:lipid kinase activity; IEA:TreeGrafter.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:UniProtKB-ARBA.
DR GO; GO:0046512; P:sphingosine biosynthetic process; IEA:TreeGrafter.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.40.50.10330; Probable inorganic polyphosphate/atp-NAD kinase, domain 1; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR055916; DUF7493.
DR InterPro; IPR050187; Lipid_Phosphate_FormReg.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR PANTHER; PTHR12358:SF31; ACYLGLYCEROL KINASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12358; SPHINGOSINE KINASE; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF24321; DUF7493; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KAK0641996.1};
KW Reference proteome {ECO:0000313|Proteomes:UP001174936};
KW Transferase {ECO:0000313|EMBL:KAK0641996.1}.
FT DOMAIN 139..278
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 537 AA; 58040 MW; 6A183FA5DEC47FB7 CRC64;
MSAEATAASA PDSDARQRSE PTTAHAVAND VLELSPKFIL TLEGNGVLLP SLPDRKAHRT
CGLPVSAPNG SPISVPYYNV LWAELSEDGK SLSIDYAEQK AHALEVRTAN FAISQGSASP
EEVTQWVEHL LDRSYGGAAR RKRAWVLVNP HAGPGGADKV WHKQVKPIFQ AARMPLTVVR
TSYSGEAVEL AKEVNIDDFD IAVPCSGDGL PHEVFNGFGK RADARRALSK IAVCHIPCGS
GNAMSCNLYG THRPSLAALA IVKGLPTPFD LVSITQGDRR TLSFLSQALG MVADLDITTE
PLRWMGAARF TFGFLVLALQ RRVYPCDIAV KVEIEHKEAV KQHYGQKVGQ SSKSGNESDG
TTDIQAPSPT ASSPVGSDED QGLPPLKYGT AIDKLPEGWE LVPHEKLGNF YCGNMAYMAP
DLNFFSAALA NDGMMDLVTV DGDVSPLKAI ALQLSVESGE FFDSPLVSYR KVSAYRIIPR
ENSPKGYISI DGESFPWEPF QAEIHQGLGL TLSKKRGYEA PGPLNWDTVT TSERLHA
//