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 Q9UZ78

Entry ID Method Resolution Chain Position Source
AF-Q9UZ78-F1 Predicted AlphaFoldDB

No variants for Q9UZ78

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9UZ78

No associated diseases with Q9UZ78

3 regional properties for Q9UZ78

Type Name Position InterPro Accession
domain GNAT domain 469 - 664 IPR000182
domain Helicase domain 283 - 457 IPR007807
domain tRNA(Met) cytidine acetyltransferase TmcA, N-terminal 28 - 219 IPR013562

Functions

Description
EC Number 2.3.1.193 Transferring groups other than amino-acyl groups
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
tRNA binding Binding to a transfer RNA.
tRNA N-acetyltransferase activity Catalysis of the reaction: acetyl-CoA + cytidine = CoA + N4-acetylcytidine. The cytidine is within the polynucleotide chain of a tRNA.

2 GO annotations of biological process

Name Definition
tRNA acetylation The modification of tRNA structure by addition of an acetyl group to tRNA. An acetyl group is CH3CO-, derived from acetic
tRNA wobble cytosine modification The process in which a cytosine in position 34 of a tRNA is post-transcriptionally modified.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTIKIRFPKD VREYARKEKV KESIIKLTET SLAEAITNFH RRMIILQGDT LEKAKLAGIL
70 80 90 100 110 120
AGGVARILSE YIPEFLDRKL RDEDKIEVLY ATDALGEDTY GRKRFEEFRK HFSVLAPNAE
130 140 150 160 170 180
LTSVTFKYSR DILGRTFDIL VLDLSYDYSP NDLGRIIETV RGGGLIFILT NPFEKWKDMW
190 200 210 220 230 240
TGFHKSLVTP PYTIDDVKKR FNRRLIRKFT EHKGIYIVDA DKKKIERRPR KNKSQAKLPE
250 260 270 280 290 300
REKVEIPRDI KFPRELYELC LTRGQVEVLK ALEDLIENPG MVVLTADRGR GKSVSVGIAS
310 320 330 340 350 360
IGLAITSKKK NFRIVVTAPE LENVQSLLKF AERSLKVLGY KTKTVKESGL IKEVYAKGIG
370 380 390 400 410 420
IRYYPPTKGY RQKADLYIVD EAAGIHVPIL HRYLEKERVV FSSTIHGYEG AGRGFSVKFL
430 440 450 460 470 480
KKAKEKREYK EIHLSVPIRY AEGDPIERWL FDVLLLDAEP VELTEEDYEL IRKMEVYLEE
490 500 510 520 530 540
PDLDDWFEND REDLRHFVGI YVLAHYRNRP SDVALLADAP HHEARVLRLK NGKIVTAIQI
550 560 570 580 590 600
AKEGGIPKAV IDKMAKGYKP PGNIIPDMMV KHHYAKEFAK LRGYRIVRIA THPDAMDLGL
610 620 630 640 650 660
GSKALELLVK EAQEKGLDWV GSGFGASEEL IRFWVRNGFA VVHLSPTRNP VSGEYTAIVI
670 680 690 700 710 720
KPISERAKEI VKKANDEFRL RLTEWLGDTH RDLEPEIARW LFETPFGEAV NYPIHLTKVQ
730 740 750 760 770 780
RKRLEMFIKR VLTYDTVVDA VKPLVKLYFL DGWMRPYLDD RQIALLIHRV LQAHDWKETA
790 800 810
KLLNRTELYT MIELRDIVRG LWYYYKHMLK DEEKDIS