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 B6YUR8

Entry ID Method Resolution Chain Position Source
AF-B6YUR8-F1 Predicted AlphaFoldDB

No variants for B6YUR8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B6YUR8

No associated diseases with B6YUR8

5 regional properties for B6YUR8

Type Name Position InterPro Accession
domain PUA domain 505 - 579 IPR002478
domain tRNA-guanine(15) transglycosylase-like 6 - 337 IPR002616
domain Uncharacterised domain CHP00451 485 - 575 IPR004521
domain tRNA-guanine transglycosylase, patch-forming domain C2 435 - 503 IPR029402
domain tRNA-guanine(15) transglycosylase, C1 domain 357 - 426 IPR032729

Functions

Description
EC Number 2.4.2.48 Pentosyltransferases
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

3 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
pentosyltransferase activity Catalysis of the transfer of a pentosyl group from one compound (donor) to another (acceptor).
RNA binding Binding to an RNA molecule or a portion thereof.

1 GO annotations of biological process

Name Definition
tRNA modification The covalent alteration of one or more nucleotides within a tRNA molecule to produce a tRNA molecule with a sequence that differs from that coded genetically.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MVEFKFEVKA RDAAGRIGKL EVNGKKIETP AIMPVINPKQ LTVTPKELKE MGFGIIITNS
70 80 90 100 110 120
YIIYKTPELR EKALEVGIHR LLDYDGIIEV DSGSFQLMRY GGVDVTNREI VEFQERIGVD
130 140 150 160 170 180
IGTFLDIPTP PDAPREKAEE DLRITLERAK EAEEIKGIAM NAAVQGSTYP DLRTYAARKL
190 200 210 220 230 240
SEMNFEIHPI GAVVPLMESY RYRDLVDVVI ASKQGLRSDR PVHLFGAGHP MIFALAVAMG
250 260 270 280 290 300
IDLFDSASYA LYAKDDRYLT PEGTKHLSEL EYFPCSCPVC SRYTPRELRE MPKEERTRLL
310 320 330 340 350 360
ALHNLWVIRE ELNRVKQAIK EGELWRLVDE RARSHPKLYA AYKRLLEYQD YLEKNEPITK
370 380 390 400 410 420
ASAFFKVSEE SLKWPIVQRA KARAERVKAK FPETINHPIF GEIPKYLSLS YPFAQSEGEE
430 440 450 460 470 480
DFTIEKPGKR EVRNYVMAVA EYQFGEGTRE AFKDAFVELS RKTGMPRQIK AKGKHLATFR
490 500 510 520 530 540
AEDGLLTLGI EGAKRLHEIL PFPRMRVVVD EDAEPFARKG KNVFAKFVID ADENIRPYDE
550 560 570
VLIVNRNDEL LATGQTLLNG RELKLFQSGL AVKVRRGVEK