PXR1_CHAGB
ID PXR1_CHAGB Reviewed; 368 AA.
AC Q2HFA6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Protein PXR1;
DE AltName: Full=PinX1-related protein 1;
GN Name=PXR1; ORFNames=CHGG_01098;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAQ92863.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH408029; EAQ92863.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001220319.1; XM_001220318.1.
DR AlphaFoldDB; Q2HFA6; -.
DR STRING; 38033.XP_001220319.1; -.
DR PRIDE; Q2HFA6; -.
DR EnsemblFungi; EAQ92863; EAQ92863; CHGG_01098.
DR GeneID; 4387049; -.
DR eggNOG; KOG2809; Eukaryota.
DR HOGENOM; CLU_052839_0_0_1; -.
DR InParanoid; Q2HFA6; -.
DR OrthoDB; 1577610at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR000467; G_patch_dom.
DR Pfam; PF01585; G-patch; 1.
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..368
FT /note="Protein PXR1"
FT /id="PRO_0000324886"
FT DOMAIN 25..79
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 368 AA; 40618 MW; 1F0492C562C4685A CRC64;
MGLAGAKNKR KLGNDPNNTK WSRNTDTFGQ KILRAQGWQP GEYLGAKDAA HAEWHTEANT
THIRVTLKDD TLGLGAKRNN GDECTGLDAF QHLLGRLNGK SDEALEAEQK VRNDVKLSLY
IQKKFGMMRF VKGGWLVGDQ VKQTPDEEAE EIPDSTETSE APEPAAVESK KRKADRRSDK
EDDKLGKKEK KSKKRKAGSE GDVGGEGGQK EKDKKSKRRK TESDECEEPA VTPKTAESLD
EASGASEAGN TKNEKKDKKR DKKEKKERRD KKEKKEKRRI EKAAAESGAE TGDSISEEKK
RKKKEATSEP SSAPTPTDSN SSTPTGSGYS TPIPTGSSRY LARSRFIAQK KMAFADSAAL
NQIFMIKS