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 Q8CHZ9

Entry ID Method Resolution Chain Position Source
AF-Q8CHZ9-F1 Predicted AlphaFoldDB

19 variants for Q8CHZ9

Variant ID(s) Position Change Description Diseaes Association Provenance
rs31192806 19 D>G No EVA
rs586543897 26 A>T No EVA
rs3388738999 33 I>N No EVA
rs3388742087 34 S>L No EVA
rs31192809 40 A>V No EVA
rs3388744498 73 R>K No EVA
rs3388734580 93 L>H No EVA
rs3388737889 102 V>E No EVA
rs3388741807 103 I>S No EVA
rs3388741193 123 K>Q No EVA
rs3388741223 136 L>P No EVA
rs3388742205 201 Q>L No EVA
rs3388741758 223 N>H No EVA
rs3388738995 223 N>S No EVA
rs583858258 250 R>Q No EVA
rs3388741738 268 N>I No EVA
rs587493289 320 E>G No EVA
rs583957628 322 I>V No EVA
rs579577912 355 L>F No EVA

No associated diseases with Q8CHZ9

No regional properties for Q8CHZ9

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q8CHZ9

Functions

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

3 GO annotations of cellular component

Name Definition
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
mitochondrial nucleoid The region of a mitochondrion to which the DNA is confined.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

2 GO annotations of molecular function

Name Definition
double-stranded DNA binding Binding to double-stranded DNA.
nucleic acid binding Binding to a nucleic acid.

4 GO annotations of biological process

Name Definition
DNA geometric change The process in which a transformation is induced in the geometry of a DNA double helix, resulting in a change in twist, writhe, or both, but with no change in linking number. Includes the unwinding of double-stranded DNA by helicases.
DNA-templated transcription termination The completion of transcription: the RNA polymerase pauses, the RNA-DNA hybrid dissociates, followed by the release of the RNA polymerase from its DNA template.
regulation of DNA-templated transcription Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
termination of mitochondrial transcription A transcription termination process that completes the production of a primary mitochondrial transcript.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q5ZJC8 MTERF3 Transcription termination factor 3, mitochondrial Gallus gallus (Chicken) PR
Q96E29 MTERF3 Transcription termination factor 3, mitochondrial Homo sapiens (Human) PR
Q99551 MTERF1 Transcription termination factor 1, mitochondrial Homo sapiens (Human) PR
Q8R3J4 Mterf3 Transcription termination factor 3, mitochondrial Mus musculus (Mouse) PR
B9EJ57 Mterf1b Transcription termination factor 1b, mitochondrial Mus musculus (Mouse) PR
10 20 30 40 50 60
MASRNIWCVR RNFLFDLRDW MLQYSAEVFL KSISFRPFSA ECDSKDKESL EEEREDLLSN
70 80 90 100 110 120
LVTMGVDIDM ARRRQPGVFN KAVTNEQELK LFLLSKGASD KVIGSIISRY PRAITRTPES
130 140 150 160 170 180
LSKRWDLWRK IMASDLEIVN ILERSPESFF RSNNNLNLEN NIKFLCSVGL THKCLCRLLT
190 200 210 220 230 240
NAPRTFSNSL NLNKQMVEFL QETGMSLGHN DPRDFVRKII SKNPSILIQS TKRVKTNIEF
250 260 270 280 290 300
LQSTFNLNKR DLLLLICGPG ARILDLSNDC TKKNYTNIRE RLLSLGCSEE EVQRFVLSYL
310 320 330 340 350 360
NMVFLSEKKF NDKIDCLIEE KISASQIIEN PRILDSSINT LKTRIRELSH AGYDLSTSSI
370
ALLSWSQRRY EAKLKRLCG