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 A6VNE0

Entry ID Method Resolution Chain Position Source
AF-A6VNE0-F1 Predicted AlphaFoldDB

No variants for A6VNE0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A6VNE0

No associated diseases with A6VNE0

6 regional properties for A6VNE0

Type Name Position InterPro Accession
domain Translational (tr)-type GTP-binding domain 337 - 506 IPR000795
domain Small GTP-binding protein domain 340 - 496 IPR005225
domain Translation initiation factor IF-2, N-terminal 262 - 312 IPR006847
domain Initiation factor 2 associated domain, bacterial 12 - 46 IPR013575
domain Translation initiation factor IF- 2, domain 3 613 - 727 IPR023115
domain Translation initiation factor IF-2, domain II 513 - 606 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
MTEKEQNAEN APKKLSLKRR EKTTVSATTA GGKAKAVQVE VRKSRKIDTE AAIKAAEAAK
70 80 90 100 110 120
LKAQEEAEAK AKAEAEKAEQ EKATAAKVRE KAAKPTKAEA KPENSTVAKA ADPEKEKRKA
130 140 150 160 170 180
EEAELRRKAD ELARQKAEEQ ARKAAEDAKR YAEAAKDTVE HHNDSDDFSD YHLTSSYARE
190 200 210 220 230 240
AEDEDNRRRE NHIRTGKNKV TKAKKGGRDD NGSKDERSAD RRNQKDMRGK GKQSKQGKRG
250 260 270 280 290 300
STLQQAFTKP AQVTKSDVVI GETITVAELA NKMAIKATEI IKTMMKMGEM VTINQVLDQE
310 320 330 340 350 360
TAQLVAEELG HKVILRKENE LEESVLEDRD VNAEKVQRAP VVTIMGHVDH GKTSLLDYIR
370 380 390 400 410 420
KAKVAAGEAG GITQHIGAYH VETKGKIITF LDTPGHAAFT SMRARGAKAT DIVVLVVAAD
430 440 450 460 470 480
DGVMPQTIEA IQHARAAGVP IVVAVNKIDK PEANPERVEQ ELLQYDVVAE KFGGDVQFVY
490 500 510 520 530 540
VSAKKGSGVD DLLDAILLQS EVLELTAVKD GMASGVVIES YLDKGRGPVA TILVQSGTLK
550 560 570 580 590 600
RGDIVLCGFE FGRVRAMRDE DGKDINEAGP SIPVEVLGLS GVPAAGDEAT VVRDEKKARE
610 620 630 640 650 660
VALYRQGKFR EVKLARQQKA KLENMFSNMS EGDVAELNVI VKADVQGSVE AIVQSLQELS
670 680 690 700 710 720
TEEVKVKVVG SGVGGITETD ATLAAASNAI MVGFNVRADA SARRVIENEN IDLRYYSIIY
730 740 750 760 770 780
ELLNEIKAAM SGMLQPEFKQ EIIGLAEVRD IFRHPKFGAI AGCMVTEGIV KRNNPIRVLR
790 800 810 820 830
DNVVIFEGEL ESLRRFKDDV NEVRNGMECG IGVKNYNDVK VGDQIEVFEV VEVKRSI