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Database: UniProt
Entry: Q4WT07_ASPFU
LinkDB: Q4WT07_ASPFU
Original site: Q4WT07_ASPFU 
ID   Q4WT07_ASPFU            Unreviewed;       486 AA.
AC   Q4WT07;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   28-JAN-2026, entry version 91.
DE   SubName: Full=Sphingosine kinase (SphK), putative {ECO:0000313|EMBL:EAL90425.1};
GN   ORFNames=AFUA_1G10980 {ECO:0000313|EMBL:EAL90425.1};
OS   Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS   Af293) (Neosartorya fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL90425.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL90425.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Af293 {ECO:0000313|EMBL:EAL90425.1,
RC   ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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:EAL90425.1}.
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DR   EMBL; AAHF01000004; EAL90425.1; -; Genomic_DNA.
DR   RefSeq; XP_752463.1; XM_747370.1.
DR   AlphaFoldDB; Q4WT07; -.
DR   FunCoup; Q4WT07; 599.
DR   STRING; 330879.Q4WT07; -.
DR   GeneID; 3510483; -.
DR   KEGG; afm:AFUA_1G10980; -.
DR   eggNOG; KOG1116; Eukaryota.
DR   HOGENOM; CLU_013399_0_1_1; -.
DR   InParanoid; Q4WT07; -.
DR   OMA; TMGNFYA; -.
DR   OrthoDB; 3853857at2759; -.
DR   Proteomes; UP000002530; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046512; P:sphingosine biosynthetic process; IBA:GO_Central.
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   InterPro; IPR045540; YegS/DAGK_C.
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   Pfam; PF19279; YegS_C; 1.
DR   SMART; SM00046; DAGKc; 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:EAL90425.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          117..256
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   486 AA;  52540 MW;  B6643F27E762D7D3 CRC64;
     MASSDGATRP SFNADQPDSQ SQLLQPESTL TVGQSVTLTL GNDALVIVET KETQSIALYN
     ILHAEVSSAG LTITYADPVT KHDVTVGALQ YTIADEDKAK AETFAARLLD LAYGNAKRYR
     RFKVLINPFG GKGIASRLYH QYAAPILAAA HCVVEVEETT HGGHATEIAE QIDIDAYDAI
     VCCSGDGLPY EVFNGLAKKP NAREALSKLA VAMIPGGSGN AMAWNLCGTG SVSVAALAIV
     KGVRTPIDLV SVTQGKTRTL SFLSQSFGIV AESDLGTDNI RWMGAHRFTY GFLVRLMQRT
     VWPCDLAIKV EIDDKKAIKE HYRKYAAGEP PRRPSEDTVA GSGGLPDLKY GTVLDELPQD
     WEVVPGESMG NFYAGNMAIM SADTNFFPAS LPNDGLIDVV TIDGTISRLT SLKMMTEIPE
     GGFFDMPDVR IRKASAYRLT PREKEGYISV DGERIPFEPF QVEVHRGLGT VLSKSGHLYE
     AEGPRP
//
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