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 B0SBH8

Entry ID Method Resolution Chain Position Source
AF-B0SBH8-F1 Predicted AlphaFoldDB

No variants for B0SBH8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B0SBH8

No associated diseases with B0SBH8

No regional properties for B0SBH8

Type Name Position InterPro Accession
No domain, repeats, and functional sites for B0SBH8

Functions

Description
EC Number 2.5.1.75 Transferring alkyl or aryl groups, other than methyl groups
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
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
tRNA dimethylallyltransferase activity Catalysis of the reaction: dimethylallyl diphosphate + tRNA = diphosphate + tRNA containing 6-dimethylallyladenosine.

1 GO annotations of biological process

Name Definition
tRNA processing The process in which a pre-tRNA molecule is converted to a mature tRNA, ready for addition of an aminoacyl group.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MILPILGGPT GSGKTSLTQV LDPKRFEIVS FDSRQVYRDL PVGTTAPTPE ECSTIRHWLI
70 80 90 100 110 120
GFLNANESIN ANQFSLLARN AIADIQSRGK IPFLLGGTGF YLRAFLLGMY PVPTVPKETK
130 140 150 160 170 180
DYVFTLPLEE ARSQLLAKDP KAMESLSDQD GYRIKRALEV VLTGVLWSDV SKETVGGFWK
190 200 210 220 230 240
DNPEVKIVGH WLDWPREILY QRINTRVETI IRGMLEETKE VLSKYGPDCP GLRTLGYNFA
250 260 270 280 290
LAFLNGMIDS NTFIEQLAQS HRNYAKRQIT WFKKESFLSP ISYDAAVQLY TNIEQR