ID   A3LRL8_PICST            Unreviewed;       852 AA.
AC   A3LRL8;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   02-SEP-2026, entry version 110.
DE   SubName: Full=Beta-1,6-N-acetylglucosaminyltransferase, contains WSC domain {ECO:0000313|EMBL:ABN65407.1};
DE   Flags: Fragment;
GN   Name=CTF1 {ECO:0000313|EMBL:ABN65407.1};
GN   ORFNames=PICST_57681 {ECO:0000313|EMBL:ABN65407.1};
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC   Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN65407.1, ECO:0000313|Proteomes:UP000002258};
RN   [1] {ECO:0000313|EMBL:ABN65407.1, 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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00227}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00227}.
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DR   EMBL; CP000497; ABN65407.1; -; Genomic_DNA.
DR   RefSeq; XP_001383436.1; XM_001383399.1.
DR   AlphaFoldDB; A3LRL8; -.
DR   STRING; 322104.A3LRL8; -.
DR   GeneID; 4837996; -.
DR   KEGG; pic:PICST_57681; -.
DR   eggNOG; ENOG502QV53; Eukaryota.
DR   HOGENOM; CLU_006329_0_0_1; -.
DR   InParanoid; A3LRL8; -.
DR   OMA; VYWEMPR; -.
DR   OrthoDB; 5121955at2759; -.
DR   Proteomes; UP000002258; Chromosome 3.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   CDD; cd12148; fungal_TF_MHR; 1.
DR   CDD; cd00067; GAL4; 1.
DR   Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 1.
DR   InterPro; IPR052073; Amide_Lactam_Regulators.
DR   InterPro; IPR007219; XnlR_reg_dom.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   InterPro; IPR001138; Zn2Cys6_DnaBD.
DR   PANTHER; PTHR47171; FARA-RELATED; 1.
DR   PANTHER; PTHR47171:SF3; FARA-RELATED; 1.
DR   Pfam; PF04082; Fungal_trans; 1.
DR   Pfam; PF00172; Zn_clus; 1.
DR   SMART; SM00906; Fungal_trans; 1.
DR   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR   PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU00227}; Glycosyltransferase {ECO:0000313|EMBL:ABN65407.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00227};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00227}; Reference proteome {ECO:0000313|Proteomes:UP000002258};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|PROSITE-
KW   ProRule:PRU00227};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|PROSITE-ProRule:PRU00227};
KW   Transferase {ECO:0000313|EMBL:ABN65407.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00227}.
FT   DOMAIN          18..49
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50048"
FT   REGION          54..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          711..734
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..120
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        711..723
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        724..734
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABN65407.1"
SQ   SEQUENCE   852 AA;  95555 MW;  B22C79DF24D01FA9 CRC64;
     EKPKAFTIKY KRPRGSRACT VCRSRKVRCD AEIHIPCTNC ITFGCDCVLP EVKKRGNSSQ
     DSKPKRRQTV SISSKDKITV NDEHDHSSAS DINNGSNSQP SASLEKPSDT SSSATSGASS
     NEPILNISSV SIPPSLTSTY KTRPSIHKRE LVSSNNRAAL TFLGSSSVGV VVQRVGENHV
     QLTSDIYDFT DNSMDAVELE ILKLRGAFLL PSFELQLDLI NSYFEHVHPL MPVLNRTQFM
     YKFNDPNDNP SLMLLQAVLL CGCRVSRNPL LFDSKGSSDL AALTFFRRAK SLYEANYESD
     PVSVVQTLIL IGSYWEGPED VTKNSFYWTR VAVGLAQGFG FQRDVNNSKN LTTSEKKIWR
     RIWWCLFEKD RNVAIAFGRP SVIDLNDCDV PMLTLDDFNE DDPELEIKSP YPVNETEALY
     FIHLVKLAEI TGIIIRHQYS VKSEQLKRKN KFSIIQHCDM LMGIWFTNLP PQLVFSLTDQ
     STQNFYSCLL NAQYYNRLYL IHRSNLIRMA KSSSTDPNNY KYPSWGISFQ SARMISIISK
     ILLDGDQIKY CPVMYVYIAF SALVMLIYHV DSSNSVIAST ASDSLFVSRA VLRELAGYWP
     VAGVLMKFFD KYANDKIKRA KVIENGTRIA EFQELHANQN DQKNGKGYFE HVSNNNAAIK
     KEGPYLTGNS PSGVSATSGV SPGGEIYNDY QKAQYKNPNI DELVQQYKQK DTSAQKLQKD
     KTVDTSPASS TQSFPNISLV TEKLPANHNF FENFEPTQLF PDIRYSYPPT RVHSPSAEAS
     AEPIGSNVYA NVRHRPTNDG SDVVDEAYPS TTPGASSYTN FIDSSFINMN LQSGIENSSL
     TDDIASLFNL KY
//