URC2_LACKL
ID URC2_LACKL Reviewed; 726 AA.
AC Q6YFE6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Uracil catabolism protein 2;
GN Name=URC2;
OS Lachancea kluyveri (Yeast) (Saccharomyces kluyveri).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=4934;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=18550080; DOI=10.1016/j.jmb.2008.05.029;
RA Andersen G., Bjoernberg O., Polakova S., Pynyaha Y., Rasmussen A.,
RA Moeller K., Hofer A., Moritz T., Sandrini M.P., Merico A.M., Compagno C.,
RA Aekerlund H.E., Gojkovic Z., Piskur J.;
RT "A second pathway to degrade pyrimidine nucleic acid precursors in
RT eukaryotes.";
RL J. Mol. Biol. 380:656-666(2008).
RN [2]
RP SEQUENCE REVISION TO 280 AND 436.
RA Rasmussen A., Piskur J.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable transcriptional activator involved in uracil
CC catabolism. {ECO:0000269|PubMed:18550080}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the URC2 family. {ECO:0000305}.
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DR EMBL; AY154653; AAO06875.2; -; Genomic_DNA.
DR AlphaFoldDB; Q6YFE6; -.
DR SMR; Q6YFE6; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
PE 3: Inferred from homology;
KW Activator; DNA-binding; Metal-binding; Nucleotide metabolism; Nucleus;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..726
FT /note="Uracil catabolism protein 2"
FT /id="PRO_0000367586"
FT DNA_BIND 24..53
FT /note="Zn(2)-C6 fungal-type"
FT REGION 152..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 726 AA; 82079 MW; 698812063449BCAD CRC64;
MASDNSQTQT RTKKPRKKRK TYSCGVCRKF KTRCDFEPLV GKCHRCNVLR LECSLTKERE
EEILAAVEST SKSTLAPASL VSGQLPALAA ANPVVANDAV VVAPVAATLS SRLNKLESSV
GSLNSKLDLA LMLLQGSNSA ISNLKNLTSS KAGMGDRNAT YDDDDDGDDD GHDHSDSDNF
VNGIKLQEPP LKLISDIDER LFPTKAQSQQ DILAKTQRPF VVARFNFLKY FNQHEQLCLD
LSRDFLVKSH FWIIPGGIKE INRTYVEKHL FITSVFTIIA MGFDENNKYE KEQEQLYPLV
ERFLTNTLTM FEKLTDHDIE AILYCSMFNI SRKSKRHRQL KFNSLVLCNF AVNSVLNIVD
FHKIKERVLI NEEYSALDLY HLRILNSLTA CRLQYSIGSG NFTIQDDMLK EFNNLTAKFP
QANFGDDIKI SEINLGDIVN GIFLNFKAYF KGFSKRFRAE TRGHADRNRD CLVIPELEYW
LKNWDELLSK DGGGVLLFAY DFYYSMICRS FLTEFFEEEF QNDVVYFKCA LKTMKRYCFS
LLDGFLKLPP SLIKGAPTIT LHQLVYACLT LCDFLHCFDV AERQQVLNLC TKIYWHLNTI
GEKLNEATDN VGKIIKSLID TSKRKAQVSG RLAVPRNTKR GSPSMTPGFQ QSVQSSSALQ
GSKAGSPQSA RSVNSQGSGA DSLAAASFNM PDVAQFNSFE DFFQDFFDNL KPTTQSMFST
LQQQQQ