ID A3GH32_PICST Unreviewed; 1302 AA.
AC A3GH32;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 2.
DT 24-JAN-2024, entry version 91.
DE SubName: Full=Positive regulatory protein of phosphate pathway {ECO:0000313|EMBL:EAZ62748.2};
GN Name=PHO81 {ECO:0000313|EMBL:EAZ62748.2};
GN ORFNames=PICST_81069 {ECO:0000313|EMBL:EAZ62748.2};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:EAZ62748.2, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:EAZ62748.2, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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:EAZ62748.2}.
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DR EMBL; AAVQ01000002; EAZ62748.2; -; Genomic_DNA.
DR RefSeq; XP_001386771.2; XM_001386734.1.
DR STRING; 322104.A3GH32; -.
DR GeneID; 4851581; -.
DR KEGG; pic:PICST_81069; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG1161; Eukaryota.
DR eggNOG; KOG2421; Eukaryota.
DR HOGENOM; CLU_002842_1_0_1; -.
DR InParanoid; A3GH32; -.
DR OMA; LCTALNW; -.
DR OrthoDB; 4907at2759; -.
DR Proteomes; UP000002258; Chromosome 1.
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; 2.
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:SF165; ANK_REP_REGION DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24198; ANKYRIN REPEAT AND PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF03105; SPX; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 7.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 3.
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:UP000002258};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..190
FT /note="SPX"
FT /evidence="ECO:0000259|PROSITE:PS51382"
FT REPEAT 503..535
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 578..610
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 612..644
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 953..1302
FT /note="GP-PDE"
FT /evidence="ECO:0000259|PROSITE:PS51704"
FT REGION 255..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1183..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1302 AA; 146180 MW; 1A51E0112FB54018 CRC64;
MKFGKYLASR QLELPEYSGH FIDYKALKKL IKQLAIPTTT STNDESNRPL TQAEIQQTLK
ENKASFFFRV ERELDKVNSF YLEKQANLAI NLDLLVMKKN ELLTKSAYFI NQQNNSSNGG
GPTSNPSANS INANFRNSIS YLNLYQNFKK IHQDLIRLQQ FIELNETGFS KVVKKWDKRS
KSHTKELFIS TAVSVQPVFH KNEINELSDL VTQSLFDLES IMDGDYSTLN NYSSSSLAAT
SPPILKVLSR TNSTSNINIP SDPSDSASER HQSISSLPIP GNFPASRNSS IINLQNNEID
ELYSSFVNVA TIKDPDLSIL SRWVDKVKSS SKSGRNESSA SISSSSSGKP QFNSIAKFKL
SKIFLLSVAN LKISDSFLES FLDLIHYEID FAFINDEFNN NKNILHECCS IPPDSTHERS
HHVIINNGVK VINSTDSINH SRTFIIQHIM NNLDQQQRAN LLICKDFNGR TCLHYASQNN
RLDLLEILTT YFPKEHIDDL DNDSMSPLLL AIKHGNLNVI KKLVQSGSNC FPQNDESKLQ
YLPINYACKF GEYKTLEYLL SYSKPTNNNE QLNQQDVEGL PPLHVIARSG HYKLIKLLIQ
YGAEINRVDG FNKWTPIFYA ASEGHVKTTQ ELVKLGAKLN IVDEDGYNVL YYCVVEGHIN
VLNELLNHYN TIQSNQKREN INTINTIISE EIIASKQQQN SSTDSNNSMS ILVENDDDSE
DSGSIDKNNV DSIPDLQLPP PILPLRRYGH NFLEQKVLIE LIFPSDAEFI NFFNSTTDLK
PGRITLTSNN SDIVPRNILL PIADDTKAIN NCVFQTEVDS LNEFRIDFEI FPKFGTRLIA
KTTALSFSQI DTSSPEINSI QLPLFDLRLR NIGELKFNYQ VIFPFSGTLL ETSKFDTYWK
SSTSFVKNRQ TLKLNAAGGL SPNNFLSPSS INSMIGSSST ASKSNASGNG NSNLINNPLT
STNELVSGST PSSIVTATSL SGEYLRIKIC LLNDGTPVVC PHWSIPITEN IDLYLPNLSL
EQLSSITNDL FDYGKVIHDL SGMTIKDIVL IKKLLRIIYL PLDVLLEILN VEINLNLELV
FPSLYELENL PFIGNIQSNL NNFIDFTLND VFNHIRSSKL SHGSSGRSII FLSSNSLICK
ILNWKQPNFP VFLIMNGIAY NGNKRKFESR TANGLLIEDI QKSKAASGHQ PITPDSKPPN
KSSRDKIVSN HQEVTIRSIK EAVNFTINNN LIGLITSIHL LDLVPKLVPL IRSRGLVLVA
SSDVGDEENE ESLQKELDSY TRTEINGLRF DDVLSFKEDI TM
//