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Database: UniProt
Entry: A0A0V0QAS5_PSEPJ
LinkDB: A0A0V0QAS5_PSEPJ
Original site: A0A0V0QAS5_PSEPJ 
ID   A0A0V0QAS5_PSEPJ        Unreviewed;       351 AA.
AC   A0A0V0QAS5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=ATP-NAD kinase-like domain {ECO:0000313|EMBL:KRW99175.1};
GN   ORFNames=PPERSA_07418 {ECO:0000313|EMBL:KRW99175.1};
OS   Pseudocohnilembus persalinus (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC   Pseudocohnilembus.
OX   NCBI_TaxID=266149 {ECO:0000313|EMBL:KRW99175.1, ECO:0000313|Proteomes:UP000054937};
RN   [1] {ECO:0000313|EMBL:KRW99175.1, ECO:0000313|Proteomes:UP000054937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=36N120E {ECO:0000313|EMBL:KRW99175.1};
RX   PubMed=26486372; DOI=10.1038/srep15470;
RA   Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA   Miao W.;
RT   "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT   persalinus provides insight into its virulence through horizontal gene
RT   transfer.";
RL   Sci. Rep. 5:15470-15470(2015).
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:KRW99175.1}.
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DR   EMBL; LDAU01000220; KRW99175.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0QAS5; -.
DR   EnsemblProtists; KRW99175; KRW99175; PPERSA_07418.
DR   InParanoid; A0A0V0QAS5; -.
DR   OMA; FAQNTRC; -.
DR   OrthoDB; 374620at2759; -.
DR   Proteomes; UP000054937; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0017050; F:D-erythro-sphingosine kinase activity; IEA:UniProt.
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; 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; 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, ECO:0000313|EMBL:KRW99175.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054937};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          63..185
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   351 AA;  39899 MW;  25E25C1142E2AC18 CRC64;
     MGCCSAKLPT IDEKDYFQYL PDEVINQRIP KEFEKTCCSK KPVPIPEDPF KEKKRNGRSL
     KNHKKVIELF EKQGVKIVKT IQTPGNNQIQ KILEDEPLIK EVDCVVAMGG DGTLREVVEG
     VYLKSKKENL QQQIPCALIA GGTGNALTAT IYKIENRYNY EYVVNQIVNG KLRKCDMMEV
     DYFNNKLKQR EKQIALSMIT WGVGVTCTFT AEKLRWCGPP RYNIGIAYRV LKDGLQDVTL
     EIDGRKDKVV DIKSNCLMIM NGQHAGDGLR FNPFGKLDDE LFEVAFLGQG RCKTFDLFSQ
     VKDKARHIFD NSVQLGMCKS IKIDTNKPSL IHIDGECTKY QETPLIQVKV M
//
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