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Database: UniProt
Entry: M9LJB3_PSEA3
LinkDB: M9LJB3_PSEA3
Original site: M9LJB3_PSEA3 
ID   M9LJB3_PSEA3            Unreviewed;      1104 AA.
AC   M9LJB3;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Choline kinase {ECO:0000313|EMBL:GAC71396.1};
GN   ORFNames=PANT_3c00011 {ECO:0000313|EMBL:GAC71396.1};
OS   Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX   NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC71396.1, ECO:0000313|Proteomes:UP000011976};
RN   [1] {ECO:0000313|Proteomes:UP000011976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX   PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA   Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA   Machida M., Kitamoto D.;
RT   "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT   producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL   Genome Announc. 1:E0006413-E0006413(2013).
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- PATHWAY: Phospholipid metabolism. {ECO:0000256|ARBA:ARBA00025707}.
CC   -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC       {ECO:0000256|ARBA:ARBA00038211}.
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DR   EMBL; DF196769; GAC71396.1; -; Genomic_DNA.
DR   AlphaFoldDB; M9LJB3; -.
DR   STRING; 1151754.M9LJB3; -.
DR   OrthoDB; 144299at2759; -.
DR   Proteomes; UP000011976; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1200.10; -; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   PANTHER; PTHR22603; CHOLINE/ETHANOALAMINE KINASE; 1.
DR   PANTHER; PTHR22603:SF93; RE24176P; 1.
DR   Pfam; PF01633; Choline_kinase; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:GAC71396.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011976};
KW   Transferase {ECO:0000313|EMBL:GAC71396.1}.
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          153..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          424..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          505..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          737..761
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          864..986
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..192
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..537
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..752
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        902..925
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        941..977
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1104 AA;  118777 MW;  FBE617E33E87FD0E CRC64;
     MQSQHQLRST AAHAQRDAST MDSPLMDGFP PSSPSPSPSP ALSACSYSST SSAGDYSDYD
     PDLNALSLEA IDEPQYPLVD AGLTLPRNHT HPPGLADSSD IDPRQSALAS GAATPVASQS
     SRSLRNMDTP NASSPSSVGA ALSAFSSLYL SQSHSHANPG SAAPSTSTST YHTADTDHSA
     PDSDDDRADR DAATDGFDAL DVDEEDMHAE GIPAARGWRL DARQADTRHF RSKVIELFSH
     QLQLQGWSQD TVHSSLWPLQ PDHLNLKRIS GAFTNAVFFA SYQPADSSHT APVAPPTVLL
     RVYGASSEAL LSRRAELLIL HTLSSLYEIG PHILGTFANG RVEEFYDCDP IQKEGMRDFG
     DREAYMLPGG SLVVKGREGR AHWVARRMNE LHSVPLEVMR TVLEQGNLHG PSQKGFGRGI
     ENHIMASSHR PRRKHRSRHT PAPLEKDAPS PNVYGLDTRG VMRASPAPMA PGEPSPAASI
     DIRAGSAYAH RNSSTVSLDS LATSYNSQSS FSSDSPSLTD VTSPTLSASS VSGTPNPYFP
     PIANGPMSPL ALVPQGRTSQ KPKSSRGPYP GVWRRLKRWS LEAAKVIELV DRFAKSDSGA
     KAIAMCFSGH PSIRQELQAD PNALSTATIG PTPGNLRNSL RAIRAIDLPS LYHQVEEFKR
     FVRKWERKEG PSRRVFAHND AQYGNLLAIK HYNASTAPPT IQSGNGSRDA KAIPAETPSI
     PAGMPRLLSN GVRRDSIASA AGSQSPESVR SKSRSRANLR KPAPLHHRIV VIDFEYASPN
     PRGYDIANHF QEWRADYHHP TLSWSLTHHA SYPDQEQRRK WLRAYVEQGR LLRMGGRASK
     GGPAAMDVPG DMVLPPAVAS LQYPPSNSAI HGPITTERPS APVTPGTGAA QVAALEKSLG
     DRSRLTPSQR TPNESGVSAK SGSGSLAGAL QREVDGQASR VIGRRSSNDS ISSSSWQAPP
     SGPLRATNIS APSTPAGSLG PMSPLLDGSA SPQVMALASL DASIEREIDR LEREVAIWSP
     ATHAVWGLWG IVFAKEELEA VLTKAAAEAR GEPVKETVLS ETSTLSVPSA ACSETFDNLR
     YALGRIELFR QEWQRLKEMG IDSI
//
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