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SPB1_RAT
ID   SPB1_RAT                Reviewed;         829 AA.
AC   Q5RJT2;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=pre-rRNA 2'-O-ribose RNA methyltransferase FTSJ3 {ECO:0000255|HAMAP-Rule:MF_03163};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03163};
DE   AltName: Full=Protein ftsJ homolog 3 {ECO:0000255|HAMAP-Rule:MF_03163};
DE   AltName: Full=Putative rRNA methyltransferase 3 {ECO:0000255|HAMAP-Rule:MF_03163};
GN   Name=Ftsj3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335; SER-336; SER-345;
RP   SER-353 AND SER-531, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: RNA 2'-O-methyltransferase involved in the processing of the
CC       34S pre-rRNA to 18S rRNA and in 40S ribosomal subunit formation.
CC       {ECO:0000255|HAMAP-Rule:MF_03163}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleotide in rRNA + S-adenosyl-L-methionine = a 2'-O-
CC         methylribonucleotide in rRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:48628, Rhea:RHEA-COMP:12164, Rhea:RHEA-COMP:12165,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:90675, ChEBI:CHEBI:90676; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03163};
CC   -!- SUBUNIT: Interacts with NIP7. {ECO:0000255|HAMAP-Rule:MF_03163}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC       Rule:MF_03163}.
CC   -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q9DBE9}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA methyltransferase RlmE family. SPB1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03163}.
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DR   EMBL; BC086512; AAH86512.1; -; mRNA.
DR   RefSeq; NP_001012014.1; NM_001012014.1.
DR   AlphaFoldDB; Q5RJT2; -.
DR   SMR; Q5RJT2; -.
DR   STRING; 10116.ENSRNOP00000013295; -.
DR   iPTMnet; Q5RJT2; -.
DR   PhosphoSitePlus; Q5RJT2; -.
DR   PaxDb; Q5RJT2; -.
DR   PRIDE; Q5RJT2; -.
DR   Ensembl; ENSRNOT00000013295; ENSRNOP00000013295; ENSRNOG00000009857.
DR   GeneID; 303608; -.
DR   KEGG; rno:303608; -.
DR   UCSC; RGD:1307110; rat.
DR   CTD; 117246; -.
DR   RGD; 1307110; Ftsj3.
DR   eggNOG; KOG1098; Eukaryota.
DR   GeneTree; ENSGT00550000075004; -.
DR   HOGENOM; CLU_009422_8_1_1; -.
DR   InParanoid; Q5RJT2; -.
DR   OMA; LMWVFQQ; -.
DR   OrthoDB; 1362679at2759; -.
DR   PhylomeDB; Q5RJT2; -.
DR   TreeFam; TF106102; -.
DR   Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   PRO; PR:Q5RJT2; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000009857; Expressed in spleen and 20 other tissues.
DR   Genevisible; Q5RJT2; RN.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR   GO; GO:0030688; C:preribosome, small subunit precursor; IEA:UniProtKB-UniRule.
DR   GO; GO:0062105; F:RNA 2'-O-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016435; F:rRNA (guanine) methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0000453; P:enzyme-directed rRNA 2'-O-methylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0001510; P:RNA methylation; ISS:UniProtKB.
DR   GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_01547; RNA_methyltr_E; 1.
DR   HAMAP; MF_03163; RNA_methyltr_E_SPB1; 1.
DR   InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR015507; rRNA-MeTfrase_E.
DR   InterPro; IPR012920; rRNA_MeTfrase_SPB1-like_C.
DR   InterPro; IPR024576; rRNA_MeTfrase_Spb1_DUF3381.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR028589; SPB1-like.
DR   Pfam; PF11861; DUF3381; 1.
DR   Pfam; PF01728; FtsJ; 1.
DR   Pfam; PF07780; Spb1_C; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   Citrullination; Coiled coil; Isopeptide bond; Methyltransferase; Nucleus;
KW   Phosphoprotein; Reference proteome; Ribosome biogenesis; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase; Ubl conjugation.
FT   CHAIN           1..829
FT                   /note="pre-rRNA 2'-O-ribose RNA methyltransferase FTSJ3"
FT                   /id="PRO_0000155580"
FT   REGION          332..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          443..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          528..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          794..829
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          722..760
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT   COMPBIAS        336..362
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..469
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..507
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        570..586
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..634
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        801..818
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        157
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT   BINDING         56
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT   BINDING         58
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT   BINDING         76
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT   BINDING         92
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT   BINDING         117
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT   MOD_RES         333
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IY81"
FT   MOD_RES         335
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         336
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         345
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         353
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         389
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DBE9"
FT   MOD_RES         531
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         544
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IY81"
FT   MOD_RES         575
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IY81"
FT   MOD_RES         659
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IY81"
FT   MOD_RES         671
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IY81"
FT   MOD_RES         766
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DBE9"
FT   CROSSLNK        570
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IY81"
FT   CROSSLNK        626
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IY81"
FT   CROSSLNK        642
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IY81"
FT   CROSSLNK        661
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IY81"
FT   CROSSLNK        693
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IY81"
SQ   SEQUENCE   829 AA;  94767 MW;  00CF7A6D13B1B40F CRC64;
     MGKKGKVGKS RRDKFYHLAK ETGYRSRSAF KLIQLNRRFQ FLQKARALLD LCAAPGGWLQ
     VAAKFMPVSS LIVGVDLVPI KPLPNVVTLQ EDITTERCRQ ALRKELKTWK VDVVLNDGAP
     NVGASWVHDA YSQAHLTLMA LRLACDFLAR GGCFITKVFR SRDYQPLLWI FQQLFHRVQA
     TKPQASRHES AEIFVVCQGF LAPDKVDAKF FDPKFAFKEV EVQAKTVTEL VTKKKPKAEG
     YAEGDLTLYH RTSVTDFLRA ANPVDFLSKA SEISIDDKEL AQHPATTEDI RACCQDIKVL
     GRKELRSLLN WRTKLRRYVA KKLKEQAKAL DISLSSEEEG DEEESAAETK QASEEEEERE
     EEEQLNRTLA EMKAQEVAEL KRKKKKLLRE QRKQRERVEL KMDLPGVSIA DEGETGMFSL
     RTIRGQQLLE EVTQGDMNAA DTFLSDLPRD DIYVSDAEDD DDTSLESDLD PEELAGVRTH
     SDQKEQKSLQ FAQVDDSKEE EGENPLLVPL EEKAVLQEEQ ASLWFSKDGF SGIDDDADEA
     LEISQAQLLY KSRQKEQQPT DPPPPPTNLK TEKKSSQCQN EVPKETEAIT DTGGEDRDSS
     DSDSSSSEDE DDWKVSRGKK RSRGSKADED GFEVVPIEDP VKYRILDPEG LALGAVIASS
     KKAKRDLIDN SFNRYAFNEE EEELPEWFVQ EEKQHRIRQL PLDKKEVEHY RKRWREINAR
     PIKKVAEAKA RKKRRMLKKL EQTKKKAEAV VNTVDISERE KVAQLRSLYK KAGLGKEKRQ
     VTYVVAKKGV GRKVRRPAGV RGHFKVVDSR MKKDQRAQRK EQKRNHRRK
 
 
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