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RRP8_ARATH
ID   RRP8_ARATH              Reviewed;         287 AA.
AC   Q84JC0; Q9FM44;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Ribosomal RNA-processing protein 8;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=At5g40530; ORFNames=MNF13.4;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
CC   -!- FUNCTION: Probable methyltransferase required to silence rDNA.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q84JC0-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RRP8 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB08523.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB009052; BAB08523.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED94560.1; -; Genomic_DNA.
DR   EMBL; BT002940; AAO22753.1; -; mRNA.
DR   EMBL; BT004445; AAO42439.1; -; mRNA.
DR   RefSeq; NP_001330531.1; NM_001344336.1.
DR   RefSeq; NP_198869.2; NM_123417.4. [Q84JC0-1]
DR   AlphaFoldDB; Q84JC0; -.
DR   SMR; Q84JC0; -.
DR   STRING; 3702.AT5G40530.2; -.
DR   PRIDE; Q84JC0; -.
DR   EnsemblPlants; AT5G40530.1; AT5G40530.1; AT5G40530. [Q84JC0-1]
DR   GeneID; 834051; -.
DR   Gramene; AT5G40530.1; AT5G40530.1; AT5G40530. [Q84JC0-1]
DR   KEGG; ath:AT5G40530; -.
DR   Araport; AT5G40530; -.
DR   eggNOG; KOG3045; Eukaryota.
DR   HOGENOM; CLU_027694_1_2_1; -.
DR   InParanoid; Q84JC0; -.
DR   OMA; KWPTNPL; -.
DR   OrthoDB; 962356at2759; -.
DR   PhylomeDB; Q84JC0; -.
DR   PRO; PR:Q84JC0; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q84JC0; baseline and differential.
DR   Genevisible; Q84JC0; AT.
DR   GO; GO:0005677; C:chromatin silencing complex; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0033553; C:rDNA heterochromatin; ISS:UniProtKB.
DR   GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0000183; P:rDNA heterochromatin assembly; ISS:UniProtKB.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.2150; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR007823; RRP8.
DR   InterPro; IPR042036; RRP8_N.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR12787; PTHR12787; 1.
DR   Pfam; PF05148; Methyltransf_8; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Chromatin regulator; Methyltransferase; Nucleus;
KW   Reference proteome; Repressor; rRNA processing; S-adenosyl-L-methionine;
KW   Transcription; Transcription regulation; Transferase.
FT   CHAIN           1..287
FT                   /note="Ribosomal RNA-processing protein 8"
FT                   /id="PRO_0000390459"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         107
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O43159"
FT   BINDING         142
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O43159"
FT   BINDING         160
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O43159"
FT   BINDING         172
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O43159"
FT   BINDING         173
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O43159"
FT   BINDING         189
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O43159"
SQ   SEQUENCE   287 AA;  32760 MW;  D108B51393E964DE CRC64;
     MTTEENKTSR NRKRKRQRNP KPSKEEPIET TPKNQNEKKN QRDTKNQQHG GSSAPSKRPK
     PSNFLDALRE RLSGGQFRML NEKLYTCSGK EALDYFKEDP QMFDMYHTGY QQQMSNWPEL
     PVNSIINWLL SNSSSLVVAD FGCGDARIAK SVKNKVFSFD LVSKNPSVIA CDMSNTSLES
     SSVDVAVFCL SLMGTNYSSY IKEAHRVLRP SGMLLIAEVK SRFDPNNGGA DPKDFVKAVC
     DLGFTSVLKD FSNKMFILFH FKKKEQMNSN QKIIKWPELK ACLYKRR
 
 
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