ID   A3LRD3_PICST            Unreviewed;       854 AA.
AC   A3LRD3;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 2.
DT   27-MAR-2024, entry version 99.
DE   SubName: Full=Regulatory protein {ECO:0000313|EMBL:ABN65716.2};
GN   ORFNames=PICST_65402 {ECO:0000313|EMBL:ABN65716.2};
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:ABN65716.2, ECO:0000313|Proteomes:UP000002258};
RN   [1] {ECO:0000313|EMBL:ABN65716.2, 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).
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DR   EMBL; CP000497; ABN65716.2; -; Genomic_DNA.
DR   RefSeq; XP_001383745.2; XM_001383708.1.
DR   AlphaFoldDB; A3LRD3; -.
DR   STRING; 322104.A3LRD3; -.
DR   GeneID; 4838004; -.
DR   KEGG; pic:PICST_65402; -.
DR   eggNOG; ENOG502QUTG; Eukaryota.
DR   HOGENOM; CLU_009666_2_0_1; -.
DR   InParanoid; A3LRD3; -.
DR   OMA; LHYLCQF; -.
DR   OrthoDB; 3019647at2759; -.
DR   Proteomes; UP000002258; Chromosome 3.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:UniProt.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:UniProt.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 3.10.260.10; Transcription regulator HTH, APSES-type DNA-binding domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR036887; HTH_APSES_sf.
DR   InterPro; IPR018004; KilA/APSES_HTH.
DR   InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type.
DR   PANTHER; PTHR43828; ASPARAGINASE; 1.
DR   PANTHER; PTHR43828:SF7; REGULATORY PROTEIN SWI4; 1.
DR   Pfam; PF00023; Ank; 2.
DR   Pfam; PF04383; KilA-N; 1.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM01252; KilA-N; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF54616; DNA-binding domain of Mlu1-box binding protein MBP1; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 2.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS51299; HTH_APSES; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002258};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1..93
FT                   /note="HTH APSES-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51299"
FT   REPEAT          330..362
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          457..482
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          93..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          182..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          667..741
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        101..126
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..168
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   854 AA;  97007 MW;  FFC7DC9D704023FF CRC64;
     MNDSPIMRRC KDDWVNATQI LKCCNFPKAK RTKILEKGVQ QGLHEKVQGG FGRFQGTWIP
     LPDAQRLATM YGVTADAAPV LFLNLEDPNL VIPQKVKPQP KEPSSSKRKY TKKAKKPEDN
     KKLKTDENAP QMSTFTQQPP QPPQQDYIHI NGNVSGNGMS NIPNFTPHNQ AVQNEFQNYQ
     MQFQRMQQQQ QQQQQQQQQH QQHQVKFYPN QPNPNGANGY SQTPLAAQMM GNFQHSSKPS
     SNENWSQDEL GNTQKDSDTS VSTNEDPKHI QNGMNDSMTA DITQSPKSSQ EENTYSAQLL
     KFFSEDNAQI PYFIHNPPYN FNINEAIDDE GHTPLHWAAS IGNYQMIHLL LSKGASPLVV
     NSFGLNPLSK LISFNNCSEL KNFPKVLDDL ELCLINTDIN GRTPLHYLCQ YSKVKSKYES
     LRYYMNIILN KLTAMSNYNP SKQIDLLKNV LDHQDVNGDT CLHLAVRFSS AKLAKLLLQI
     SALPTQYPAA GLNYSAPAVK HESEGQYQVL ATPMQTVANG IETPDTQRTM IQDDDMDEDD
     TTTERVDKNH IEHLIKGEDN KENIFVDGKG YNAVSTPISK PHQNASASTH QPLAVISERT
     VESTPIHDKK FQLSTIHQTY KPQPPRLDEN GKIVEEKVKN KLEENVDMKL SMLDLSSMIT
     GMINSLSDSY NHEFQQYEGK INELEEQLKS KQNANDESTQ YFTKMLNRVG IEQFSNVEEG
     KQKLTDAIDL HEEEIRTKEQ SLIRVLERNQ AYQLATLVEK QEIDLMVNQD KGESVEDELE
     LIDQNKIDYA VELTKMQIKR NKLVSKLTQG IKTFGIDSKM YKYRKLISLS CGLKVEDIDS
     LIDGIEESLV ENMS
//