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 Q6PFX8

Entry ID Method Resolution Chain Position Source
AF-Q6PFX8-F1 Predicted AlphaFoldDB

12 variants for Q6PFX8

Variant ID(s) Position Change Description Diseaes Association Provenance
rs213607553 36 G>S No EVA
rs242558211 39 A>T No EVA
rs3388696580 63 L>P No EVA
rs13477942 65 T>S No EVA
rs3388708146 134 H>L No EVA
rs3388707549 146 P>H No EVA
rs3394675967 158 G>W No EVA
rs3388709996 161 G>R No EVA
rs3388700588 281 L>V No EVA
rs265102301 338 S>N No EVA
rs27505935 375 Q>R No EVA
rs3388708597 377 W>L No EVA

No associated diseases with Q6PFX8

1 regional properties for Q6PFX8

Type Name Position InterPro Accession
domain Regulator of MON1-CCZ1 complex, C-terminal 476 - 630 IPR009755

Functions

Description
EC Number 6.3.2.41 Acid--amino-acid ligases (peptide synthases)
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.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ligase activity, forming carbon-nitrogen bonds Catalysis of the joining of two molecules, or two groups within a single molecule, via a carbon-nitrogen bond, with the concomitant hydrolysis of the diphosphate bond in ATP or a similar triphosphate.
metal ion binding Binding to a metal ion.
N-acetyl-L-aspartate-L-glutamate ligase activity Catalysis of the reaction: ATP + N-acetyl-L-aspartate + L-glutamate = ADP + phosphate + N-acetylaspartyl-glutamate.

1 GO annotations of biological process

Name Definition
protein modification process The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications). Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification).

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q0VCE9 RIMKLB Beta-citrylglutamate synthase B Bos taurus (Bovine) PR
Q9ULI2 RIMKLB Beta-citrylglutamate synthase B Homo sapiens (Human) PR
Q8IXN7 RIMKLA N-acetylaspartylglutamate synthase A Homo sapiens (Human) PR
Q80WS1 Rimklb Beta-citrylglutamate synthase B Mus musculus (Mouse) PR
10 20 30 40 50 60
MCAQVWLLTD RLIREDYPQV QILRALRQRC SEQDVGFRAV FLDQIAVTVV GGHLGLQLSQ
70 80 90 100 110 120
KPLTTFPDVV VVRVSTPSVQ SDSEITILRH LEKLGCRLVN RPQSILNCIN KFWTFQELAG
130 140 150 160 170 180
HGVPMPDTFS YGGHEDFSKM IDEAEPLGYP VVVKSTRGHR GKAVFLARDK HHLSDICHLV
190 200 210 220 230 240
RHDVPYLFQK YVKESHGKDI RVVVVGGQVI GSMLRCSTDG RMQSNCFLGG VGVKCPLTEQ
250 260 270 280 290 300
GKQLAIQVSN ILGMDFCGID LLIMDDGSFT VCEANANVGF LAFDQACNLD VGAIIADYAM
310 320 330 340 350 360
SLLPNRQTGK MAILPGLASP REKNEPNGCV SAQGVAESVY AITNGSTSSE SEPELGEARD
370
SSVKTMGAPP AHVAQAWLQH