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 Q8K224

Entry ID Method Resolution Chain Position Source
AF-Q8K224-F1 Predicted AlphaFoldDB

46 variants for Q8K224

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388570881 4 K>N No EVA
rs3388575079 7 D>G No EVA
rs3388562935 45 S>P No EVA
rs3388577812 77 Q>* No EVA
rs3388576814 91 D>E No EVA
rs3388568341 95 L>P No EVA
rs3388569422 107 Y>C No EVA
rs3388575064 120 M>I No EVA
rs3388575065 136 R>S No EVA
rs3388568329 158 K>N No EVA
rs3388573012 161 Y>C No EVA
rs3388572560 164 T>S No EVA
rs3388577827 290 K>N No EVA
rs3388575268 364 H>Y No EVA
rs3388571238 375 D>G No EVA
rs3388575319 423 L>V No EVA
rs3391838795 435 S>C No EVA
rs3391931558 435 S>W No EVA
rs3391978788 437 Q>L No EVA
rs3391978213 439 Q>L No EVA
rs3388572566 447 K>M No EVA
rs259849008 483 D>G No EVA
rs235032797 496 V>L No EVA
rs3388573075 603 D>N No EVA
rs3388570860 607 W>C No EVA
rs3388576084 641 G>D No EVA
rs3391978133 678 V>D No EVA
rs3392003182 684 V>A No EVA
rs3391849000 688 R>W No EVA
rs3391978803 708 Y>C No EVA
rs3391978232 713 Y>H No EVA
rs3391902151 714 G>R No EVA
rs262035785 718 R>K No EVA
rs3391848981 719 L>F No EVA
rs248745056 754 D>N No EVA
rs3388575298 763 W>C No EVA
rs250358437 772 R>Q No EVA
rs3388573040 855 G>* No EVA
rs3391838794 874 H>Q No EVA
rs3391982161 877 V>E No EVA
rs245810496 919 V>A No EVA
rs3392041730 963 Y>S No EVA
rs3391704858 972 W>G No EVA
rs3388568338 975 V>A No EVA
rs3388572548 1007 K>N No EVA
rs3388573098 1015 R>G No EVA

No associated diseases with Q8K224

4 regional properties for Q8K224

Type Name Position InterPro Accession
domain GNAT domain 528 - 753 IPR000182
domain Helicase domain 282 - 488 IPR007807
domain tRNA(Met) cytidine acetyltransferase TmcA, N-terminal 9 - 201 IPR013562
domain Possible tRNA binding domain 763 - 975 IPR027992

Functions

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

3 GO annotations of cellular component

Name Definition
midbody A thin cytoplasmic bridge formed between daughter cells at the end of cytokinesis. The midbody forms where the contractile ring constricts, and may persist for some time before finally breaking to complete cytokinesis.
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.
telomerase holoenzyme complex Telomerase is a ribonucleoprotein enzyme complex, with a minimal catalytic core composed of a catalytic reverse transcriptase subunit and an RNA subunit that provides the template for telomeric DNA addition. In vivo, the holoenzyme complex often contains additional subunits.

6 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
DNA polymerase binding Binding to a DNA polymerase.
mRNA N-acetyltransferase activity Catalysis of the reaction: a cytidine in mRNA + acetyl-CoA + ATP + H2O = ADP + an N(4)-acetylcytidine in mRNA + CoA + H(+) + phosphate.
N-acetyltransferase activity Catalysis of the transfer of an acetyl group to a nitrogen atom on the acceptor molecule.
rRNA cytidine N-acetyltransferase activity Catalysis of the reaction: acetyl-CoA + cytidine = CoA + N4-acetylcytidine. The cytidine is within the polynucleotide chain of an rRNA.
tRNA binding Binding to a transfer RNA.

6 GO annotations of biological process

Name Definition
negative regulation of telomere maintenance via telomerase Any process that stops, prevents, or reduces the frequency, rate or extent of the addition of telomeric repeats by telomerase.
positive regulation of translation Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA.
protein acetylation The addition of an acetyl group to a protein amino acid. An acetyl group is CH3CO-, derived from acetic
regulation of centrosome duplication Any process that modulates the frequency, rate or extent of centrosome duplication. Centrosome duplication is the replication of a centrosome, a structure comprised of a pair of centrioles and peri-centriolar material from which a microtubule spindle apparatus is organized.
rRNA acetylation involved in maturation of SSU-rRNA Any rRNA acetylation that is involved in maturation of SSU-rRNA.
tRNA acetylation The modification of tRNA structure by addition of an acetyl group to tRNA. An acetyl group is CH3CO-, derived from acetic

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P53914 KRE33 RNA cytidine acetyltransferase Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q9H0A0 NAT10 RNA cytidine acetyltransferase Homo sapiens (Human) PR
O01757 nath-10 RNA cytidine acetyltransferase Caenorhabditis elegans PR
Q9XIK4 At1g10490 RNA cytidine acetyltransferase 1 Arabidopsis thaliana (Mouse-ear cress) PR
Q9M2Q4 At3g57940 RNA cytidine acetyltransferase 2 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MNRKKVDNRI RILIENGVAE RQRSLFVVVG DRGKDQVVIL HHMLSKATVK ARPSVLWCYK
70 80 90 100 110 120
KELGFSSHRK KRMRQLQKKI KSGTLNLKQD DPFELFVAAT NIRYCYYNET HKILGNTFGM
130 140 150 160 170 180
CVLQDFEALT PNLLARTVET VEGGGLVVIL LRTMNSLKQL YTMTMDVHSR YRTEAHQDVV
190 200 210 220 230 240
GRFNERFILS LASCKKCLVI DDQLDILPIS SHVASIEALP PQAPDENLSP AALELLELKE
250 260 270 280 290 300
SLQDTQPVGV LVDCCKTLDQ AKAVLKFIEG ISEKTLRSTV ALTAARGRGK SAALGLAIAG
310 320 330 340 350 360
AVAFGYSNIF VTSPSPDNLH TLFEFVFKGF DALQYQEHLD YEIVQSLNPE FNKAVIRVNV
370 380 390 400 410 420
FREHRQTIQY IHPADAVKLG QAELVVIDEA AAIPLPLVKS LLGPYLVFMA STINGYEGTG
430 440 450 460 470 480
RSLSLKLIQQ LRQQSAQSQV STTAENKTTT TARLASARTL HEVSLQESIR YAPGDAVEKW
490 500 510 520 530 540
LNDLLCLDCL NITRIVSGCP LPEACELYYV NRDTLFCYHK ASEVFLQRLM ALYVASHYKN
550 560 570 580 590 600
SPNDLQMLSD APAHHLFCLL PPVPPTQNAL PEVLAVVQVC LEGEISRQSI LNSLSRGKKA
610 620 630 640 650 660
SGDLIPWTVS EQFQDPDFGG LSGGRVVRIA VHPDYQGMGY GSRALQLLQM YYEGKFPCLE
670 680 690 700 710 720
EKVLETPQEI RTVSSEAVSL LEEVITPRKD LPPLLLKLNE RPAERLDYLG VSYGLTPRLL
730 740 750 760 770 780
KFWKRAGFVP VYLRQTPNDL TGEHSCIMLK TLADEDEAEQ GAWLAAFWKD FRRRFLALLS
790 800 810 820 830 840
YQFSTFSPAL SLNIIQNRNV AKSALPALGR EHLEALFLPY DLKRLEMYSR NMVDYHLIMD
850 860 870 880 890 900
LIPAISRLYF LNQLGDLSLS AAQSALLLGI GLQHKSVDQL EKEIELPSGQ LMGLFNRIIR
910 920 930 940 950 960
KVVKLFNDVQ EKAIEEQMVA VKDVVMEPTM KTLSDDLDEA AKEFQEKHKK EVGKLKDMDL
970 980 990 1000 1010 1020
SQYVIRGDDE EWNEVLSKAG QNASIVSLKS DKKRKLETKQ EPKQSKKLKK RDNNRKDMKL
KRKK