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 B3EFB1

Entry ID Method Resolution Chain Position Source
AF-B3EFB1-F1 Predicted AlphaFoldDB

No variants for B3EFB1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B3EFB1

No associated diseases with B3EFB1

6 regional properties for B3EFB1

Type Name Position InterPro Accession
domain Translational (tr)-type GTP-binding domain 449 - 619 IPR000795
domain Small GTP-binding protein domain 452 - 609 IPR005225
domain Translation initiation factor IF-2, N-terminal 8 - 57 IPR006847-1
domain Translation initiation factor IF-2, N-terminal 377 - 425 IPR006847-2
domain Translation initiation factor IF- 2, domain 3 728 - 842 IPR023115
domain Translation initiation factor IF-2, domain II 628 - 721 IPR044145

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
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

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 initiation factor activity Functions in the initiation of ribosome-mediated translation of mRNA into a polypeptide.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAIEEMEKKY RISDIARELQ VSPQEVLQFV KLEGGKVAST SSMVDQGMRE LIFGHFSNEK
70 80 90 100 110 120
KMVDETMKIR QEKQRRLSRL EEQSRKTYEK ERQLKETLHS ASVAPAVHEE KKEPVVPEVR
130 140 150 160 170 180
LVVSVPDELV SSEKVEEIEQ IEQPVQLEQP VMAAQADQTD QTDQTDQADQ ADRTDQVIQT
190 200 210 220 230 240
DQPVQEEPLE EVPAPKEMPV KEEPSVNEQL VSFETPKNIG GLTVIGTLDM HSPFDRSSEA
250 260 270 280 290 300
ERKKKNRKKN FKEQADALKS EFDTTVKEEV AADEKGAVKK KPAKPPGETN AATPAGTAST
310 320 330 340 350 360
AGAQPLKKGK KKKKPDVNDK VISANIRTTI SGMDDSGGTG SRQKFRKLRK IERERESEAA
370 380 390 400 410 420
EAFRESQQMI VRVTEYASPH ELADLMGVTA KDIIQKCFSL GKFVTINQRL DKESIELIAL
430 440 450 460 470 480
EFGFEAEFIS EVEATAVLIE ADEPEDMQIR PPVITIMGHV DHGKTSLLDY IRNSNVVAGE
490 500 510 520 530 540
SGGITQHIGA YEVTVESDRK ITFLDTPGHE AFTAMRARGA QVTDIVILVV AADDSVMPQT
550 560 570 580 590 600
IEAINHAKAA GVPIVVAINK VDKPEANPEK IKTQLSEAGV LVEEWGGEYQ CQEISAKKGI
610 620 630 640 650 660
GIAELMEKVL AEAEIRELKG NFSREINANG IIVESELDKG KGVISTVLVQ RGFLKIGDPF
670 680 690 700 710 720
VAGNTMGKIR ALMDERGKRI LFAGPSQPVR VLGFEELPQS GDVLTVMSSD RDARDLAQKR
730 740 750 760 770 780
QVIRREHEFR RSTRVKLDSI ARQIKEGLMK ELSMIIKADT DGSIQALADG LMKIQNEEVK
790 800 810 820 830 840
VQIIHQGVGQ ITETDVLLAA ASDAIIIGFR VRPNVNAKKL AEKEDLDVRF YSVIYHVLED
850 860 870 880 890 900
VEKALEGMLS PELHEESLGS LEVRQVFRVP KVGNVGGCYM LEGKVFRDSK VRLLREGVQI
910 920 930 940 950
YDGQLDALRR FKDDVKEVDA GYECGISLKN YDDIKVGDIV EAYRIVEKKR KL