ID A0A0J0XGW6_9TREE Unreviewed; 1385 AA.
AC A0A0J0XGW6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Cyclin-dependent protein kinase inhibitor {ECO:0008006|Google:ProtNLM};
GN ORFNames=CC85DRAFT_293342 {ECO:0000313|EMBL:KLT40272.1};
OS Cutaneotrichosporon oleaginosum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT40272.1, ECO:0000313|Proteomes:UP000053611};
RN [1] {ECO:0000313|EMBL:KLT40272.1, ECO:0000313|Proteomes:UP000053611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBC0246 {ECO:0000313|EMBL:KLT40272.1,
RC ECO:0000313|Proteomes:UP000053611};
RG DOE Joint Genome Institute;
RA Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT T. oleaginosus allow insights into substrate utilization and the diverse
RT evolutionary trajectories of mating systems in fungi.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KQ087238; KLT40272.1; -; Genomic_DNA.
DR RefSeq; XP_018276763.1; XM_018424863.1.
DR SMR; A0A0J0XGW6; -.
DR STRING; 879819.A0A0J0XGW6; -.
DR GeneID; 28985466; -.
DR OrthoDB; 4907at2759; -.
DR Proteomes; UP000053611; 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; PTHR24198; ANKYRIN REPEAT AND PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24198:SF165; IPT_TIG DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF03009; GDPD; 1.
DR Pfam; PF03105; SPX; 2.
DR SMART; SM00248; ANK; 7.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 5.
DR PROSITE; PS50088; ANK_REPEAT; 6.
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:UP000053611};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..260
FT /note="SPX"
FT /evidence="ECO:0000259|PROSITE:PS51382"
FT REPEAT 438..470
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 471..503
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 505..537
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 537..561
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 573..608
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 609..641
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 879..1177
FT /note="GP-PDE"
FT /evidence="ECO:0000259|PROSITE:PS51704"
FT REGION 102..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1210..1309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1326..1352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1366..1385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1250..1264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1385 AA; 150122 MW; F334F2EC1A9B8939 CRC64;
MKFGKSIVAS QVAGWSEYYL NYKALKKIIN SLAAGRPASE VAILATGGRL KKHSADLASP
ATSAIETPTF PALDSTLSLG APAAPDVEAD GVVDTPSIAV TADPEGDSLD LEPLPAEAQP
PAPGGTHSMI SASHRNGSAR EGSFKAHRDA FFFLLQRELE KINQFYLIKE RELRLRLLTL
LSNRKRLLRS QRELGSDGAD VGEGEKRSAE WSSLEEGWRL FERDLGKLQG FIEINATGFR
KILKKWDKRS KSNTKELYLE RQVEVQPCFN REFIARLSDI VAANLVDMGN GIDLVSASLL
TADLPEPIAE DALTFDREDY ESDPGEALAT DALLDLEVNL PKVVEGGRES LTHWLKQAKR
LLAKDKTGSR AMRIVWRAAL TVPDDYLDLV FMLPLDFHYV DKINDRGPLH LACINGSLKL
VEKCIDKAPE LIEREDAYAR RPIHYAAMHG HPSLVSLLLN AGAKVSPTDK DGYTPLMHAI
TQGHLEVVRI FVSGEADVEP TALSTDLIPL SLACQYGHVE VAELLLKRGA KIRPNSEGMY
PMHVAAKAGH EAICRLLVDQ GKGGGKDKPD KYNLWTPMHH AAVGGRPEHL ACIRVLVAAG
CDVNALDEYG KSPGWYAAWF GQVGILNFLV ESGARLNTRD TEIRGMENLG LSADPQMDGM
SPGSDVELEP PAMEDFELIP SLSLPPPMVP LRVYGHEFLA KRCLVQLSLG HPFSKGDEKT
PPVKIYSRSS GSDSLHMWSS LKLVMTSKSD TTINPHSIIL PLADSREVFS FQVQSLEKFT
LEVSLYPTFG SKVIGRALIH PSTFTNIQDH KGFTAFLVDH HLKTIGEVAF EVSCIQPFEG
AQLEIGGRVE TYWKSTVAPS NAAQDHAHQF QSHRPIGVST LNPSARPTVA APQQDEPALV
TASSLSGDYM RLQVQVTRDG VPVVYPDAKL PVPDFDVGVS NLTFAQFEAL AQAHGRTLPK
SGRADSLAGW HALVAGQYAS LKDVLDLVPP EVGINLCLRY TRAFDAARLG IARSIEVNAF
VDAVLQVVYD AGRSTPGRRF LFSSFDPTVC TALNWKQPNY AVMFASYCGL DRRQVGGARL
VPVAPGSEPD NRCLSVREAV NFAKQTNLLG VILEATTLAA VPSLVASVKD AGLLLAAFGN
DQDIAGLRQG SGDGRTVDAY CTNGIMTLVI YSTSAVAHVR RRARNSIYPQ GHRIASLPRL
LHSTTFTMAS TTSETTAAPP SSSSSPSSSV PIPRTHSHAH SQHNAAHPPH AHAANDHDHA
HAPAHPSPAM DASKLNHTPA PLPLSEGEPG SPPLRDASTM FSNPFGGGET AYLDNEPQHP
TVAETGVLST SPRQGPGPRM GQLKRRESEP MPQRRIIRLA SFGGEGLAAK PARPCPGEVE
EEAIV
//
