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 Q59NX9

Entry ID Method Resolution Chain Position Source
AF-Q59NX9-F1 Predicted AlphaFoldDB

No variants for Q59NX9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q59NX9

No associated diseases with Q59NX9

No regional properties for Q59NX9

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q59NX9

Functions

Description
EC Number 2.1.1.314 Methyltransferases
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.

1 GO annotations of molecular function

Name Definition
diphthine synthase activity Catalysis of the reaction: S-adenosyl-L-methionine + 2-(3-carboxy-3-aminopropyl)-L-histidine = S-adenosyl-L-homocysteine + 2-(3-carboxy-3-(methylammonio)propyl)-L-histidine.

2 GO annotations of biological process

Name Definition
methylation The process in which a methyl group is covalently attached to a molecule.
peptidyl-diphthamide biosynthetic process from peptidyl-histidine The modification of peptidyl-histidine to 2'-(3-carboxamido-3-(trimethylammonio)propyl)-L-histidine, known as diphthamide, found in translation elongation factor EF-2. The process occurs in eukaryotes and archaea but not eubacteria.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLYLIGLGLS YESDITVRGL ETVKKCKRVY LEAYTSILMA ANQESLEKFY GREIILADRE
70 80 90 100 110 120
LVETGSDDIL KDADKEDVAF LVVGDPFGAT THTDLVIRAR ELGIKVETIH NASVMNAVGA
130 140 150 160 170 180
CGLQLYQFGQ TVSLVFFTDS WKPDSFYGKI MENRKIGLHT LLLLDIKVKE QSIENMARGR
190 200 210 220 230 240
LIYEPPRYMD IATAAQQLLE IESIRQEQAY TPNTPCVAIS RLGSPTQTFK AGTLQELSEY
250 260 270 280 290
DSGEPLHSLV MLGRQVHELE LEYLYQFVDD KEKFKKFVEQ DQEFFKPAPY VPPEDVDSE