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

9 structures for P0A705

Entry ID Method Resolution Chain Position Source
1ND9 NMR - A 2-50 PDB
1ZO1 EM 1380 A I 388-888 PDB
3JCJ EM 370 A f 1-890 PDB
3JCN EM 460 A b 1-890 PDB
5ME0 EM 1350 A W 1-890 PDB
5ME1 EM 1350 A W 1-890 PDB
6O7K EM 420 A f 382-890 PDB
6O9K EM 400 A z 382-890 PDB
AF-P0A705-F1 Predicted AlphaFoldDB

5 variants for P0A705

Variant ID(s) Position Change Description Diseaes Association Provenance
409 D>E strain: IQ489 [UniProt] No
423 G>GG strain: IQ490 [UniProt] No
432 H>Q strain: ECOAU9326 [UniProt] No
490 Q>G strain: ECOAU9302, ECOAU9306, ECOAU9307 and ECOAU9309 [UniProt] No
684 G>A strain: ECOAU9306 [UniProt] No

No associated diseases with P0A705

7 regional properties for P0A705

Type Name Position InterPro Accession
domain Translational (tr)-type GTP-binding domain 389 - 558 IPR000795
domain Small GTP-binding protein domain 393 - 548 IPR005225
domain Translation initiation factor IF-2, N-terminal 1 - 52 IPR006847-1
domain Translation initiation factor IF-2, N-terminal 314 - 364 IPR006847-2
domain Initiation factor 2 associated domain, bacterial 56 - 94 IPR013575
domain Translation initiation factor IF- 2, domain 3 665 - 779 IPR023115
domain Translation initiation factor IF-2, domain II 565 - 658 IPR044145

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

5 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.
guanosine tetraphosphate binding Binding to guanosine tetraphosphate (5'-ppGpp-3'), a guanosine bisphosphate having diphosphate groups at both the 3' and 5'-positions.
ribosomal small subunit binding Binding to a small ribosomal subunit.
translation initiation factor activity Functions in the initiation of ribosome-mediated translation of mRNA into a polypeptide.

3 GO annotations of biological process

Name Definition
chaperone-mediated protein folding The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone.
response to cold Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cold stimulus, a temperature stimulus below the optimal temperature for that organism.
translational initiation The process preceding formation of the peptide bond between the first two amino acids of a protein. This includes the formation of a complex of the ribosome, mRNA or circRNA, and an initiation complex that contains the first aminoacyl-tRNA.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P46199 MTIF2 Translation initiation factor IF-2, mitochondrial Homo sapiens (Human) PR
Q91YJ5 Mtif2 Translation initiation factor IF-2, mitochondrial Mus musculus (Mouse) PR
10 20 30 40 50 60
MTDVTIKTLA AERQTSVERL VQQFADAGIR KSADDSVSAQ EKQTLIDHLN QKNSGPDKLT
70 80 90 100 110 120
LQRKTRSTLN IPGTGGKSKS VQIEVRKKRT FVKRDPQEAE RLAAEEQAQR EAEEQARREA
130 140 150 160 170 180
EESAKREAQQ KAEREAAEQA KREAAEQAKR EAAEKDKVSN QQDDMTKNAQ AEKARREQEA
190 200 210 220 230 240
AELKRKAEEE ARRKLEEEAR RVAEEARRMA EENKWTDNAE PTEDSSDYHV TTSQHARQAE
250 260 270 280 290 300
DESDREVEGG RGRGRNAKAA RPKKGNKHAE SKADREEARA AVRGGKGGKR KGSSLQQGFQ
310 320 330 340 350 360
KPAQAVNRDV VIGETITVGE LANKMAVKGS QVIKAMMKLG AMATINQVID QETAQLVAEE
370 380 390 400 410 420
MGHKVILRRE NELEEAVMSD RDTGAAAEPR APVVTIMGHV DHGKTSLLDY IRSTKVASGE
430 440 450 460 470 480
AGGITQHIGA YHVETENGMI TFLDTPGHAA FTSMRARGAQ ATDIVVLVVA ADDGVMPQTI
490 500 510 520 530 540
EAIQHAKAAQ VPVVVAVNKI DKPEADPDRV KNELSQYGIL PEEWGGESQF VHVSAKAGTG
550 560 570 580 590 600
IDELLDAILL QAEVLELKAV RKGMASGAVI ESFLDKGRGP VATVLVREGT LHKGDIVLCG
610 620 630 640 650 660
FEYGRVRAMR NELGQEVLEA GPSIPVEILG LSGVPAAGDE VTVVRDEKKA REVALYRQGK
670 680 690 700 710 720
FREVKLARQQ KSKLENMFAN MTEGEVHEVN IVLKADVQGS VEAISDSLLK LSTDEVKVKI
730 740 750 760 770 780
IGSGVGGITE TDATLAAASN AILVGFNVRA DASARKVIEA ESLDLRYYSV IYNLIDEVKA
790 800 810 820 830 840
AMSGMLSPEL KQQIIGLAEV RDVFKSPKFG AIAGCMVTEG VVKRHNPIRV LRDNVVIYEG
850 860 870 880
ELESLRRFKD DVNEVRNGME CGIGVKNYND VRTGDVIEVF EIIEIQRTIA