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 B6YR69

Entry ID Method Resolution Chain Position Source
AF-B6YR69-F1 Predicted AlphaFoldDB

No variants for B6YR69

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B6YR69

No associated diseases with B6YR69

No regional properties for B6YR69

Type Name Position InterPro Accession
No domain, repeats, and functional sites for B6YR69

Functions

Description
EC Number 2.4.99.17 Transferring other glycosyl groups
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
S-adenosylmethionine:tRNA ribosyltransferase-isomerase activity Catalysis of the reaction: S-adenosylmethionine + 7-(aminomethyl)-7-deazaguanosine-tRNA = adenine + methionine + epoxyqueuosine-tRNA. 7-(aminomethyl)-7-deazaguanosine-tRNA is also known as preQ1-tRNA, and epoxyqueuosine-tRNA as oQ-tRNA.

1 GO annotations of biological process

Name Definition
queuosine biosynthetic process The chemical reactions and pathways resulting in the formation of queuosines, a series of nucleosides found in tRNA and having an additional pentenyl ring added via an NH group to the methyl group of 7-methylguanosine. The pentenyl ring may carry other substituents.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MRLSKFKFHL PQELIALFPS VDRDESRLMV VYHKTGRVEH VIFKDIIQYF NEKDTFIFND
70 80 90 100 110 120
TSVIPARLNG NKEKTGARVE VFLLRELDPI QRIWDVLVDP ARKIRIGNKL YFENEDSDTI
130 140 150 160 170 180
VAEIIDNTTS RGRIIRFLYD GPYESFKKIL YNLGNMPIPD YLDRKVTKED RERYQTIYAK
190 200 210 220 230 240
NEGAVVAPAA GLHFSHELMK RLELKGCELT FITVHSGMGN FRAIDVEDLF KYKSESERIV
250 260 270 280 290 300
INTETATKIN QAKQNRKQIC AVGTSVLRTI EDRENVVTSQ GYLNPFTGWT NKFIFPPYNF
310 320 330 340 350
ITSTSLITGF HLPLSSMLLQ VAAFGGFDLI MDVYKQAIEA KYRFGVYGDA MLII