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Database: UniProt
Entry: A0A2S5BIK3_9BASI
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ID   A0A2S5BIK3_9BASI        Unreviewed;      1182 AA.
AC   A0A2S5BIK3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Cyclin-dependent protein kinase inhibitor {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BMF94_0198 {ECO:0000313|EMBL:POY76608.1};
OS   Rhodotorula taiwanensis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=741276 {ECO:0000313|EMBL:POY76608.1, ECO:0000313|Proteomes:UP000237144};
RN   [1] {ECO:0000313|EMBL:POY76608.1, ECO:0000313|Proteomes:UP000237144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD1149 {ECO:0000313|EMBL:POY76608.1,
RC   ECO:0000313|Proteomes:UP000237144};
RX   PubMed=29375494;
RA   Tkavc R., Matrosova V.Y., Grichenko O.E., Gostincar C., Volpe R.P.,
RA   Klimenkova P., Gaidamakova E.K., Zhou C.E., Stewart B.J., Lyman M.G.,
RA   Malfatti S.A., Rubinfeld B., Courtot M., Singh J., Dalgard C.L.,
RA   Hamilton T., Frey K.G., Gunde-Cimerman N., Dugan L., Daly M.J.;
RT   "Prospects for Fungal Bioremediation of Acidic Radioactive Waste Sites:
RT   Characterization and Genome Sequence of Rhodotorula taiwanensis MD1149.";
RL   Front. Microbiol. 8:2528-2528(2018).
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:POY76608.1}.
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DR   EMBL; PJQD01000002; POY76608.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S5BIK3; -.
DR   STRING; 741276.A0A2S5BIK3; -.
DR   OrthoDB; 4907at2759; -.
DR   Proteomes; UP000237144; Unassembled WGS sequence.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   CDD; cd14483; SPX_PHO81_NUC-2_like; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR030395; GP_PDE_dom.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR004331; SPX_dom.
DR   PANTHER; PTHR24189; MYOTROPHIN; 1.
DR   PANTHER; PTHR24189:SF50; MYOTROPHIN-RELATED; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF03105; SPX; 2.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 8.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 4.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
DR   PROSITE; PS51704; GP_PDE; 1.
DR   PROSITE; PS51382; SPX; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Reference proteome {ECO:0000313|Proteomes:UP000237144};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1..220
FT                   /note="SPX"
FT                   /evidence="ECO:0000259|PROSITE:PS51382"
FT   REPEAT          423..455
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          456..488
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          525..552
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          595..627
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          870..1182
FT                   /note="GP-PDE"
FT                   /evidence="ECO:0000259|PROSITE:PS51704"
FT   REGION          377..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..396
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1182 AA;  126348 MW;  AA87216C085DDFDA CRC64;
     MKFGKTLQQQ IFAQNGFPGW SSYFCDYKGL KKIINSLAKG RPADAALLAA GVRPPRPAAE
     DSMPVEATTT EAQLFAHAST ANGGVVGEGP TTLLQAHKAA FFFKLERELE KINDFYYQRE
     SALKVRLRTL IDKRKLLTAS LSDPDGKVKA LSRDSSSFGA LYEGFRNFER DLGRLQARRP
     FLSLIETSQT YIELNATAFR KICKKWDKAC RRQADRFGET KPQQGQPDGQ LYLARQVEVQ
     PVFNREFIAQ LADGAAGPTL TMGAAETDTA LNAAVASANL ISLENLVASD GARGSADGSS
     IDGTGGAAPH LPTLFDRADR AEALEDLETA LVSAVKAGDR AIVDEVLGLL LPKKGDTAEH
     GSPVARILWR AALEKPSSGA TTPVSSAPTT NGLEPTMNGV EKRPEPVTIS QDLLDFAFVD
     DINGRTALHE AASAGRLPLV VACLDKGVSS AQADVYGRQP LHYAAMNGHA DVCRKLIEAG
     ASPSTPDLDG YSPIIYSITN GWTAVVETFL AAGVTFETPT IGGADQLNAL SLACQYGHEA
     IARLLLERGA QILPDPAGYW PQHLAAREGH DGVLRLLVEA FKGDSAPIDA QDKYSQSTPL
     AHAASEGHTE SVKVLLAAGA DVHALDEFKR PAIHYAAWQG HVDCVNLLID SGATQPSAAA
     RSDAADRDAA LATASTSTMD MDPLALDLDA DMIPDLSLPP PIIPFHIYGH AYLGDAKCLV
     HVTLGHPNTT LPPFPAPVRL YDQPSHGHPP SLKLVITPRP DSSGTSIPHS VILPLADERE
     VFSFQVDSLA DFSLEFDLFP TFGSKMIGKA VAVSSTFSDL KHQGSYVVPI VDPHLKVIGD
     IPFEINVVKP FARAQLQIGG QFETYWKSTA TLNAGNPSAG GGAADQGPSV VTASSLSGEH
     VRIVVQVTSD GHPVAWPQWK LPIEGLDVFV GDVTLDQLQS LAKRLGKSVD VSRVANAVDP
     SVWYKAIADS LVSLEELLRI LPASLGVNLE IRYPTRSDIR RLGLARTIEV NDFVDSVLST
     VYTSIQASAS GNGTSGDSSP SHRRIVLSSF NPVVCTALNW KQPNFSVFFA SYCGLSRTGN
     AGGGLQYNQA GRLIPANRIE EDRRCTSIRE AVKFAKANNL LGVMLDATML VQIPSLIQSA
     REHGLLITTF GTASRVLLAD AHMSDGVLSY ASSDFLKQTA AS
//
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