PXR1_LODEL
ID PXR1_LODEL Reviewed; 345 AA.
AC A5E4P1;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Protein PXR1;
DE AltName: Full=PinX1-related protein 1;
GN Name=PXR1; ORFNames=LELG_04580;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: Involved in rRNA-processing at A0, A1 and A2 sites and
CC regulates negatively telomerase. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PINX1 family. {ECO:0000305}.
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DR EMBL; CH981529; EDK46399.1; -; Genomic_DNA.
DR RefSeq; XP_001524608.1; XM_001524558.1.
DR AlphaFoldDB; A5E4P1; -.
DR STRING; 379508.A5E4P1; -.
DR EnsemblFungi; EDK46399; EDK46399; LELG_04580.
DR GeneID; 5231354; -.
DR KEGG; lel:LELG_04580; -.
DR VEuPathDB; FungiDB:LELG_04580; -.
DR eggNOG; KOG2809; Eukaryota.
DR HOGENOM; CLU_052839_0_0_1; -.
DR InParanoid; A5E4P1; -.
DR OMA; WDQSSEA; -.
DR OrthoDB; 1577610at2759; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR005819; H1/H5.
DR Pfam; PF01585; G-patch; 1.
DR PRINTS; PR00624; HISTONEH5.
DR SMART; SM00443; G_patch; 1.
DR PROSITE; PS50174; G_PATCH; 1.
PE 3: Inferred from homology;
KW Nucleus; Reference proteome; Ribosome biogenesis; rRNA processing.
FT CHAIN 1..345
FT /note="Protein PXR1"
FT /id="PRO_0000324890"
FT DOMAIN 25..71
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 345 AA; 40308 MW; 8AD20372DFEA2B49 CRC64;
MGLAGTKVKQ RFGLDPRNTN WSNNNNQFGH QYLTKMGWTP GKGIGLVPDS ITTHLKINIK
TDNAGLGAKL QKRNKDANEL DECSGVDAFQ RILGRLNGKE DAVNKVMDMK RDDMIINGKM
GIRFVKGEVL SSTWDKEKKA LISYANGKNE DKKDKDEVSL LRKRKVEDEE KREVKKSRKD
IKEKKEKKEK KEKKEKKEKK EKKEKKEKKE KKEKKEKKEK KEKKEKKEKK EKSDKKEKKE
KKDKKEKKEK KEKKEKKEKK EKKEKKEKKE KKEKKEKKEK KDKLDKESSN AANVESTKSL
VSDSSRESTP TPIASRLSVR SKWIKQKRAS VMDAKALNEI FMISN