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 P40173

Entry ID Method Resolution Chain Position Source
AF-P40173-F1 Predicted AlphaFoldDB

No variants for P40173

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P40173

No associated diseases with P40173

9 regional properties for P40173

Type Name Position InterPro Accession
domain Elongation factor EFG, domain V-like 614 - 701 IPR000640
domain Translational (tr)-type GTP-binding domain 9 - 295 IPR000795
domain Translation elongation factor EFTu-like, domain 2 336 - 402 IPR004161
domain Small GTP-binding protein domain 11 - 185 IPR005225
domain Translation elongation factor EFG/EF2, domain IV 491 - 612 IPR005517
domain Elongation factor G, domain III 417 - 492 IPR009022
conserved_site Tr-type G domain, conserved site 52 - 67 IPR031157
domain EFG, domain V 617 - 694 IPR035649
domain Elongation Factor G, domain II 416 - 490 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
MATTSLDLAK VRNIGIMAHI DAGKTTTTER ILFYTGVSYK IGEVHDGAAT MDWMEQEQER
70 80 90 100 110 120
GITITSAATT CHWPLEDNDY TINIIDTPGH VDFTVEVERS LRVLDGAVTV FDGVAGVEPQ
130 140 150 160 170 180
SETVWRQADR YGVPRICFVN KLDRTGAEFH RCVDMISDRL GAQPLVMQLP IGAEADFQGV
190 200 210 220 230 240
VDLVRMKALV WSADAAKGEM YDVVDIPATH TEAAEEWRGK LVEAVAENDE EVMELFLEGQ
250 260 270 280 290 300
EPTEEQLYAA IRRVTIASGK SSDTTVTPVF CGTAFKNKGV QPLLDAVVRY LPTPLDVEAI
310 320 330 340 350 360
EGHDVKDPEV VVKRKPSEDE PLAALAFKIM SDPHLGKLTF VRVYSGRLVS GTAVLNSVKG
370 380 390 400 410 420
RKERIGKIYR MHANKREEIE SVGAGDIVAV MGLKQTTTGE TLSDDKSPVI LESMDFPAPV
430 440 450 460 470 480
IQVAIEPKSK GDQEKLGVAI QRLAEEDPSF QVHTNEETGQ TIIGGMGELH LEVLVDRMRR
490 500 510 520 530 540
EFKVEANVGK PQVAYRETIR KTVERVDYTH KKQTGGTGQF AKVQIAIEPI EGGDASYEFV
550 560 570 580 590 600
NKVTGGRIPK EYIPSVDAGA QEAMQFGILA GYEMTGVRVT LIDGGYHEVD SSELAFKIAG
610 620 630 640 650 660
SQAFKEAARK ASPVLLEPMM AVEVTTPEDY MGDVIGDINS RRGQIQAMEE RMGARVVKGL
670 680 690 700
VPLSEMFGYV GDLRSKTSGR ASYSMQFDSY AEVPRNVAEE IIAKAKGE