Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q9DBE9

Entry ID Method Resolution Chain Position Source
AF-Q9DBE9-F1 Predicted AlphaFoldDB

45 variants for Q9DBE9

Variant ID(s) Position Change Description Diseaes Association Provenance
rs13471824 31 K>E No EVA
rs3389204353 117 D>G No EVA
rs3389211205 121 N>Y No EVA
rs3389211210 153 C>* No EVA
rs3389171832 179 Q>R No EVA
rs3389211198 186 S>T No EVA
rs3389220451 195 V>L No EVA
rs3389185519 212 D>E No EVA
rs3389593561 243 E>G No EVA
rs3389211184 285 A>T No EVA
rs3389213177 312 R>I No EVA
rs218259651 333 S>N No EVA
rs3389210845 389 L>R No EVA
rs3402747620 430 L>* No EVA
rs3389208462 478 V>L No EVA
rs3389226482 485 K>N No EVA
rs27010762 489 Y>C No EVA
rs220234408 493 T>A No EVA
rs248436209 494 Q>K No EVA
rs230849596 502 E>G No EVA
rs3389198429 514 K>R No EVA
rs3389221998 525 W>* No EVA
rs3389224438 537 D>E No EVA
rs27010763 555 Q>R No EVA
rs3402635108 556 K>T No EVA
rs3389220446 591 L>S No EVA
rs3389171826 613 S>N No EVA
rs3389146793 653 I>T No EVA
rs3389181259 656 P>R No EVA
rs3389211220 666 A>T No EVA
rs3413143545 684 A>V No EVA
rs3389204349 701 K>R No EVA
rs3389185486 735 E>D No EVA
rs3389211209 735 E>Q No EVA
rs250446423 744 V>M No EVA
rs3389146780 770 V>M No EVA
rs3402729344 775 S>R No EVA
rs3402350168 777 Y>* No EVA
rs3389211271 784 K>E No EVA
rs3389198447 795 K>Q No EVA
rs3389204344 796 K>N No EVA
rs27010765 809 K>R No EVA
rs3389185490 810 G>D No EVA
rs3389206599 823 Q>H No EVA
rs3389213166 833 K>I No EVA

No associated diseases with Q9DBE9

3 regional properties for Q9DBE9

Type Name Position InterPro Accession
domain Ribosomal RNA methyltransferase, FtsJ domain 24 - 200 IPR002877
domain Ribosomal RNA methyltransferase, SPB1-like, C-terminal 617 - 830 IPR012920
domain Ribosomal RNA methyltransferase Spb1, domain of unknown function DUF3381 232 - 398 IPR024576

Functions

Description
EC Number
Subcellular Localization
  • Nucleus, nucleolus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
chromosome A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information.
nucleolus A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
preribosome, large subunit precursor A preribosomal complex consisting of 27SA, 27SB, and/or 7S pre-rRNA, 5S rRNA, ribosomal proteins including late-associating large subunit proteins, and associated proteins; a precursor of the eukaryotic cytoplasmic large ribosomal subunit.
preribosome, small subunit precursor A preribosomal complex consisting of 20S pre-rRNA, ribosomal proteins including late-associating small subunit proteins, and associated proteins; a precursor of the eukaryotic cytoplasmic small ribosomal subunit.

4 GO annotations of molecular function

Name Definition
RNA 2'-O-methyltransferase activity Catalysis of the reaction: S-adenosyl-L-methionine + RNA = S-adenosyl-L-homocysteine + RNA containing 2'-O-methylribonucleotide.
RNA methyltransferase activity Catalysis of the transfer of a methyl group from a donor to a nucleoside residue in an RNA molecule.
rRNA (guanine) methyltransferase activity Catalysis of the reaction: S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA containing methylguanine.
rRNA (uridine-2'-O-)-methyltransferase activity Catalysis of the reaction: S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA containing 2'-O-methyluridine.

5 GO annotations of biological process

Name Definition
enzyme-directed rRNA 2'-O-methylation The addition of methyl groups to the 2'-oxygen atom of nucleotide residues in an rRNA molecule during ribosome biogenesis where the methylase specifies the site that becomes methylated without using a guide RNA.
maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Any process involved in the maturation of an rRNA molecule originally produced as part of a tricistronic rRNA transcript that contained the Small SubUnit (SSU) rRNA, the 5.8S rRNA, and the Large SubUnit (LSU) rRNA, in that order, from 5' to 3' along the primary transcript.
maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Any process involved in the maturation of a precursor Large SubUnit (LSU) ribosomal RNA (rRNA) molecule into a mature LSU-rRNA molecule from the pre-rRNA molecule originally produced as a tricistronic rRNA transcript that contains the Small Subunit (SSU) rRNA, 5.8S rRNA, and Large Subunit (LSU) in that order from 5' to 3' along the primary transcript.
RNA methylation Posttranscriptional addition of a methyl group to either a nucleotide or 2'-O ribose in a polyribonucleotide. Usually uses S-adenosylmethionine as a cofactor.
rRNA methylation The posttranscriptional addition of methyl groups to specific residues in an rRNA molecule.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q5ZKM1 FTSJ3 pre-rRNA 2'-O-ribose RNA methyltransferase FTSJ3 Gallus gallus (Chicken) PR
Q8IY81 FTSJ3 pre-rRNA 2'-O-ribose RNA methyltransferase FTSJ3 Homo sapiens (Human) PR
10 20 30 40 50 60
MGKKGKVGKS RRDKFYHLAK ETGYRSRSAF KLIQLNRRFQ FLQKARALLD LCAAPGGWLQ
70 80 90 100 110 120
VAAKFMPVSS LIVGVDLVPI KPLPNVVTLQ EDITTERCRQ ALRKELKTWK VDVVLNDGAP
130 140 150 160 170 180
NVGASWVHDA YSQAHLTLMA LRLACDFLAR GGCFITKVFR SRDYQPLLWI FQQLFHRVQA
190 200 210 220 230 240
TKPQASRHES AEIFVVCQGF LAPDKVDAKF FDPKFAFKEV EVQAKTVTEL VTKKKPKAEG
250 260 270 280 290 300
YAEGDLTLYH RTSVTDFLRA ANPVDFLSKA SEISIDDEEL AQHPATTEDI RVCCQDIKVL
310 320 330 340 350 360
GRKELRSLLN WRTKLRRYVA KKLKEQAKAL DISLSSEEEE EGDEEEAVAE TKQAPEEEEE
370 380 390 400 410 420
REEEQLNRTL AEMKAQEVAE LKRKKKKLLR EQRKQRERVE LKMDLPGVSI ADEGETGMFS
430 440 450 460 470 480
LRTIRGQQLL EEVTQGDMNA ADTFLSDLPR DDIYVSDAED DDDTSLESDL DPEELAGVRT
490 500 510 520 530 540
HSDLKEQKYL RFTQVDDNKE EEGENPLLVP LEEKAVLQEE QASLWFSKDG FSGIEDDADE
550 560 570 580 590 600
ALEISQAQLL YKSRQKEQQP TDPPPPPTNL KTEKKSPQGQ NEVPKETEAI LGTEAVTDPG
610 620 630 640 650 660
GEERGNSSDS DSSSSEDEDS WKVSRGVKRG RGSKADEDGF EVVPIQDPVK YRILDPEGLA
670 680 690 700 710 720
LGAVIASSKK AKRDLIDNSF NRYAFNEEEG ELPEWFAQEE KQHRIRQLPV DKKEVEHYRK
730 740 750 760 770 780
RWREINARPI KKVAEAKARK KRRVLKKLEQ TKKKAEAVVN TVDISEREKV AQLRSLYKKA
790 800 810 820 830
GLGKEKRQVT YVVAKKGVGR KVRRPAGVKG HFKVVDSRMK KDQRAQQRKE QKKKHKRK