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 A8FDD1

Entry ID Method Resolution Chain Position Source
AF-A8FDD1-F1 Predicted AlphaFoldDB

No variants for A8FDD1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A8FDD1

No associated diseases with A8FDD1

6 regional properties for A8FDD1

Type Name Position InterPro Accession
domain Translational (tr)-type GTP-binding domain 207 - 376 IPR000795
domain Small GTP-binding protein domain 210 - 366 IPR005225
domain Translation initiation factor IF-2, N-terminal 1 - 50 IPR006847-1
domain Translation initiation factor IF-2, N-terminal 131 - 180 IPR006847-2
domain Translation initiation factor IF- 2, domain 3 482 - 597 IPR023115
domain Translation initiation factor IF-2, domain II 383 - 476 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
MAKVRVYEYA KAIDVSSKDI IAALKDMNVE VNNHMATLED DTVKKLDAIY KKAKAKETAN
70 80 90 100 110 120
EKPAEQKKQS SNKINDRKKN DVQNNQFNKN KKNNNQNKNK NKRGGNNKSQ HQQARPVKPK
130 140 150 160 170 180
KELPEKIEFT NSMTVGQLAE ELGKETAEII KKLMMLGVMA TINQELDKDT VELIASEYGV
190 200 210 220 230 240
PVEEVIILEE TELEKYEVED KEEDMQVRPP VVTIMGHVDH GKTTLLDSIR KTKVVEGEAG
250 260 270 280 290 300
GITQHIGAYQ IEENGKKITF LDTPGHAAFT TMRARGAEVT DTTILVVAAD DGVMPQTVEA
310 320 330 340 350 360
INHAKAAEVP IIVAVNKIDK PTANPDRVMQ ELTEHGLVPE AWGGETIFVP LSAKTGEGID
370 380 390 400 410 420
ELIEMILLVS EVGELKANPN RAAKGTVIEA ELDKGRGSVA TLLVQTGTLH VGDPIVVGNT
430 440 450 460 470 480
FGRVRAMVND IGRRVKTAGP STPVEITGLN DVPNAGDQFL VFKDEKTARQ VGEARASKQL
490 500 510 520 530 540
DEQRSDKAKL SLDDLFEQIK QGEVKDINLI VKADVQGSAE ALTAALQKIE VEGVKVKIIH
550 560 570 580 590 600
TGVGAITESD IILASASNAI VIGFNVRPDG NAKSTAETEN VDIRLHRIIY KVIDEIEAAM
610 620 630 640 650 660
KGMLDPEYEE KVIGQVEVRQ TFKVSKIGTI AGGYVTEGTI TRDSGIRLIR DGVVIFEGEV
670 680 690 700
DVLKRFKDDV KEVSQGYECG ITIKKYNDIR EGDVMESFVM QEIERK