ID B9W9I2_CANDC Unreviewed; 1232 AA.
AC B9W9I2;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Vigilin-like protein, putative {ECO:0000313|EMBL:CAX45465.1};
GN OrderedLocusNames=Cd36_11110 {ECO:0000313|CGD:CAL0000164210};
GN ORFNames=CD36_11110 {ECO:0000313|EMBL:CAX45465.1};
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX45465.1, ECO:0000313|Proteomes:UP000002605};
RN [1] {ECO:0000313|EMBL:CAX45465.1, ECO:0000313|Proteomes:UP000002605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC {ECO:0000313|Proteomes:UP000002605};
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(2009).
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DR EMBL; FM992688; CAX45465.1; -; Genomic_DNA.
DR RefSeq; XP_002417752.1; XM_002417707.1.
DR AlphaFoldDB; B9W9I2; -.
DR GeneID; 8045301; -.
DR KEGG; cdu:CD36_11110; -.
DR CGD; CAL0000164210; Cd36_11110.
DR VEuPathDB; FungiDB:CD36_11110; -.
DR eggNOG; KOG2208; Eukaryota.
DR HOGENOM; CLU_003293_1_0_1; -.
DR OrthoDB; 5489311at2759; -.
DR Proteomes; UP000002605; Chromosome 1.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 8.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR PANTHER; PTHR10627:SF31; DODECA-SATELLITE-BINDING PROTEIN 1, ISOFORM A; 1.
DR PANTHER; PTHR10627; SCP160; 1.
DR Pfam; PF00013; KH_1; 5.
DR SMART; SM00322; KH; 8.
DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 7.
DR PROSITE; PS50084; KH_TYPE_1; 7.
PE 4: Predicted;
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117}.
FT DOMAIN 185..283
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 584..653
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 660..735
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 739..815
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 820..891
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 895..973
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 977..1045
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 1149..1232
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..36
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..253
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1232 AA; 136920 MW; 13CA5C00DA4CC3A9 CRC64;
MPTPAEIIAA RLNRADTTQD GYEQEQEQEE EEELVTSTET TSSTNAKPSI TDETAFPTLG
GKKSASPVIS NTGSASTWGP SMKTPVRSST ASPVPTPVQH ATPKTTNGIK SKVSTIQEAF
SLDVEDQLNV ARPEFIKILT FVKQETKTNI ECTTSQHTKK RTFLITGRPD EVKLAKRLVI
KKLTKPVKIS FNIPAKLRSR VIGQGGKTLK PIIQANEVKI EIGDQIEGED TGDDETQEEE
KEEKEEEKEE EEEDIFSKTV QVTIDGDVEG SKRAKNAILA IVKEETKNLS AKVPVNETIK
PFAIKELKSI VDKFPTLEFA IPDYKSNRHT IVIVGERELV LEAKPEVKAA LEKLSNKVVI
EEVPIPKIKQ QFLPIEQVFN EHNVLIQLPK DGEGKVKFIG DKKKIPGAQA SAKKTTSQYK
VEILDMSKAH KGNLKHVKAV ASVLTKTGVF DEIAKTNDVT IHVPSNKDLV TSATIPIEIV
SKNDDEHIKI AKKAIVNQVN KITPDLTKNI EDIDEFLLNK VDETIKDISK QQSVEYVILG
KIITLFNFQQ SNEDAEDFDD VSDPDSAFKK VDEALNKLRE LATNLTNVTL SITSKEQDQI
SGPRGTTLKS ILASVEPNTV KIELHHPTSD ELYIHGIKSS VATIKKEIEN VLTDAKEFGN
EYTTTIQVPS QVLSRLIGKN GANLNQIRNE FGTRIDVPLE KDESKDKSST KTEVTIIGVK
RNVEETKTKV ATLAKKWADE TLVRLRIESQ YHRRMIGPRA VYINRLQDKY NVKIRFPSEN
SINFADAPNS KDEVTIKGPS KGVAKAEEEL KELYAFEKEN GFKQIIQIPL KAIARVIGKS
GETINDIADG TGIEYTFNRE SEESKGYSEV ELTGSKSALK EAISKIQEII DEVENFVSRS
IKVEPIYHRD LIGPGGSIMK EIISKAGGDE VPRNRQYKLL NIPNEGSGSD EVTSQGDKKI
VDKIIDAIEK IIEEKRASIT QEIDLPKEKH RLIIGPNGTI RHSLQSEFGV TIEIPRPNDE
STVIKIIGLP EKIENAKIKI EELTKDDWNE SIDVPVIYHA LVSERGAIFK KLKNDFNVEI
VHGNFTRLAN KLSTASIPTP PESAYPQKDG ELFKFTIVDA NDSATTATSE EIIPWRLKGS
EEATAKAAKF INERLDLAKN SKSIGWFYAS QPSVFSKVIG PQGSKVNQIR KKSNTFITVP
RATTDKNAAN FIYLVGDEDN LNIAKKEIEN LL
//
