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 O16686

Entry ID Method Resolution Chain Position Source
AF-O16686-F1 Predicted AlphaFoldDB

No variants for O16686

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O16686

No associated diseases with O16686

2 regional properties for O16686

Type Name Position InterPro Accession
domain Pseudouridine synthase, RsuA/RluA-like 156 - 302 IPR006145
conserved_site Pseudouridine synthase, RluA-like, conserved site 195 - 209 IPR006224

Functions

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

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

2 GO annotations of molecular function

Name Definition
pseudouridine synthase activity Catalysis of the reaction: RNA uridine = RNA pseudouridine. Conversion of uridine in an RNA molecule to pseudouridine by rotation of the C1'-N-1 glycosidic bond of uridine in RNA to a C1'-C5.
RNA binding Binding to an RNA molecule or a portion thereof.

1 GO annotations of biological process

Name Definition
enzyme-directed rRNA pseudouridine synthesis The intramolecular conversion of uridine to pseudouridine during ribosome biogenesis where the enzyme specifies the site that becomes pseudouridylated without using a guide RNA.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P53294 PUS6 tRNA pseudouridine(31) synthase Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
10 20 30 40 50 60
MSDTTDVPEN QKSPKPSGKA DKRKIEEKPE NSSLKRKKFE DPNKKVDPLE ELPMKVPFKI
70 80 90 100 110 120
VDGVRHLAPY WACYRTRTKG RWIGRKMVEV FSGEFLSTNR NYAKIACKMG RIYVNGEQMT
130 140 150 160 170 180
DVDYVMRNGD RVEHWAHRHE HPIRDLPIRV ISETDDLFVV EKPPSLPVHT CGQYAIHTVL
190 200 210 220 230 240
GQLRVNEGRT GLRVLHRLDR ATSGVLLFAK NYETDLEFKT TLKQGEWSKE YICKVDGVFP
250 260 270 280 290 300
DEEQVCEQPI GPLVISMGIQ CVRPDGKDAK SRFRKLWSDG TQSVVQVHIE TGRTHQIRVH
310 320 330 340 350 360
SQFLGHPIAG DQIYNSAVWG PTKGKNADYQ KSFDELCEDV RNTHKCENWH EKPNPEFEQR
370 380 390 400 410 420
MEHLAADTTP ITPEAPSLTL EQRPEFDEIC QKCNVESKKV PENHFQLYLH CLKYETKKWS
430
FKTEMPDWAV QK