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 Q89J81

Entry ID Method Resolution Chain Position Source
AF-Q89J81-F1 Predicted AlphaFoldDB

No variants for Q89J81

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q89J81

No associated diseases with Q89J81

9 regional properties for Q89J81

Type Name Position InterPro Accession
domain Elongation factor EFG, domain V-like 598 - 685 IPR000640
domain Translational (tr)-type GTP-binding domain 8 - 283 IPR000795
domain Translation elongation factor EFTu-like, domain 2 322 - 389 IPR004161
domain Small GTP-binding protein domain 10 - 180 IPR005225
domain Translation elongation factor EFG/EF2, domain IV 477 - 596 IPR005517
domain Elongation factor G, domain III 403 - 478 IPR009022
conserved_site Tr-type G domain, conserved site 51 - 66 IPR031157
domain EFG, domain V 601 - 678 IPR035649
domain Elongation Factor G, domain II 402 - 475 IPR041095

Functions

Description
EC Number
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
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

3 GO annotations of molecular function

Name Definition
GTP binding Binding to GTP, guanosine triphosphate.
GTPase activity Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate.
translation elongation factor activity Functions in chain elongation during polypeptide synthesis at the ribosome.

1 GO annotations of biological process

Name Definition
ribosome disassembly The disaggregation of a ribosome into its constituent components; includes the dissociation of ribosomal subunits.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPRQHAIEDY RNFGIMAHID AGKTTTTERI LYYTGKSHKI GEVHEGAATM DWMEQEQERG
70 80 90 100 110 120
ITITSAATTA FWAGKRLNII DTPGHVDFTI EVERSLRVLD GAVCVLDSNQ GVEPQTETVW
130 140 150 160 170 180
RQGDKYKVPR IVFANKMDKT GADFFKCLAD IVDRLGAKPI AIQLPIGAEN NFKGLVDLVK
190 200 210 220 230 240
MKGIVWNDES LGAKFDYVDI PEDLVEQAKE YREKMVEAAV ELDDDALAAF LDGNEPDEAT
250 260 270 280 290 300
LKRLIRKAVL TGAFYPVLCG SAFKNKGVQP LLDAVVDYLP SPIDVPAIKG TDDRGNEVVR
310 320 330 340 350 360
KADDKEPLAL LAFKIMDDPF VGTITFCRIY SGVLQSGTGV VNSTREKKER IGRMLLMHAN
370 380 390 400 410 420
NREDIKEAYA GDIVALAGLK EARTGDTLCD PDKQVILEKM EFPEPVIEIA IEPKSKADQE
430 440 450 460 470 480
KLGVALAKLA AEDPSFRVST DQESGQTILK GMGELHLDIK VDILKRTYKV DANIGAPQVA
490 500 510 520 530 540
FRERVTKKAE VKYTHKKQTG GTGQFAEVSI VVEPNEPGKG YEFESKIVGG AVPKEYIPGV
550 560 570 580 590 600
EKGLNSVMSS GVVAGFPVVD VKVQLVDGKY HDVDSSALAF EIASRAAFRE ALQKGKSVLL
610 620 630 640 650 660
EPIMKVEVVT PEDYTGSVIG DLNSRRGQIQ GQDMRGNANV INAMVPLMNM FGYVNNLRSM
670 680
SQGRATFTMQ FDHYAEAPAN VSAEVQKKFA