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PXR1_ASPTN
ID   PXR1_ASPTN              Reviewed;         298 AA.
AC   Q0CU52;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Protein pxr1;
DE   AltName: Full=PinX1-related protein 1;
GN   Name=pxr1; ORFNames=ATEG_02782;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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=EAU36056.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH476597; EAU36056.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001211960.1; XM_001211960.1.
DR   AlphaFoldDB; Q0CU52; -.
DR   EnsemblFungi; EAU36056; EAU36056; ATEG_02782.
DR   GeneID; 4317344; -.
DR   OrthoDB; 1577610at2759; -.
DR   Proteomes; UP000007963; 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   PROSITE; PS50174; G_PATCH; 1.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome; Ribosome biogenesis; rRNA processing.
FT   CHAIN           1..298
FT                   /note="Protein pxr1"
FT                   /id="PRO_0000324882"
FT   DOMAIN          25..79
FT                   /note="G-patch"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          145..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..168
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..232
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   298 AA;  32943 MW;  0B15FFFE76D2039C CRC64;
     MGLAAPRKRT KISHDPNNTN WARSTSGFGH KILSSQGWTP GSFLGARDAA HADMFTAASA
     GHIRVVVKDD TLGLGARAGR DPNEPTGLDA FKGLLGRLNG KSDAELAADQ RKADDIKLAR
     YAAFKWQAVR FVSGGLLAQE KLERLPERES VQQSRAAVET SDSNRNSEND ASKVSKKKKK
     KTSSDSSSDE QSSRSEKRRE KKEKKDKKEK KEKKDKKDKK RKRAEEDNDA SQKSASETPA
     PEKESTGLES DSTSVSVVKA SRERRPLGRQ IVRGRHIAQK KRALMDDKSL NEIFMVKA
 
 
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