ID C4YNR0_CANAW Unreviewed; 572 AA.
AC C4YNR0;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Choline kinase N-terminal domain-containing protein {ECO:0000259|Pfam:PF04428};
GN ORFNames=CAWG_02843 {ECO:0000313|EMBL:EEQ44569.1};
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748 {ECO:0000313|EMBL:EEQ44569.1, ECO:0000313|Proteomes:UP000001429};
RN [1] {ECO:0000313|EMBL:EEQ44569.1, ECO:0000313|Proteomes:UP000001429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1 {ECO:0000313|EMBL:EEQ44569.1,
RC ECO:0000313|Proteomes:UP000001429};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC {ECO:0000256|ARBA:ARBA00038211}.
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DR EMBL; CM000310; EEQ44569.1; -; Genomic_DNA.
DR AlphaFoldDB; C4YNR0; -.
DR PaxDb; 5476-C4YNR0; -.
DR VEuPathDB; FungiDB:CAWG_02843; -.
DR HOGENOM; CLU_012712_4_2_1; -.
DR OMA; CEQVINW; -.
DR Proteomes; UP000001429; Chromosome 3.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR CDD; cd05157; ETNK_euk; 1.
DR Gene3D; 3.90.1200.10; -; 1.
DR InterPro; IPR007521; Choline_kin_N.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR22603; CHOLINE/ETHANOALAMINE KINASE; 1.
DR PANTHER; PTHR22603:SF99; RE24176P; 1.
DR Pfam; PF04428; Choline_kin_N; 1.
DR Pfam; PF01633; Choline_kinase; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
FT DOMAIN 62..109
FT /note="Choline kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04428"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 572 AA; 66464 MW; AFE5B60C97132846 CRC64;
MMEISPANIK EQSRSRSRSR TRNSTANSRS TSATRRPSLS STHRRSLSSS SLNKLTITTT
QVDQERSVPS VQVYLDNSLP LDFFKQDIIA LTKTLKISKW HKRQLTINNL SINRISGALT
NAIYKIEYHD ESQNIHLPTL LLRVYGKNVD ELIDRDNELA ILIKLSQKRI GPRLLGIFSN
GRFEQFLDGF ITLNKEQIRD EILSQMLGRR MKDLHYKIEL DAKDYESKQP TCWNLIDKWL
KIFEQELLPG YLEVNYNLQD IFIVPFDQFK QIITKYKQWL FNKYDDKHFT NNYKFCHNDT
QYGNLLLHES FNPKDIVVST SDTTNSSNNI IDGEVTIKST SNKKDTNLVV IDFEYSGANF
PAYDIVNHFS EWMSDYHDPE KSYFIHQENY PNQLEQINLI KSYIEYDFQY PSSNLKTGKT
PEDLINNTTN PISIIQYEIE KLYNECIYWR ATVQIFWCLW GLIQNGPLKK PLNSNALSEQ
GINSTYNITV GGIENLDISD HTQDEIAGSN NDALIEEIIT SSDDDFDYLK YANQKVALIF
GDLIQFGIID EKEVDEKYLS IIKYIDTKTF DI
//