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 A6VU29

Entry ID Method Resolution Chain Position Source
AF-A6VU29-F1 Predicted AlphaFoldDB

No variants for A6VU29

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A6VU29

No associated diseases with A6VU29

6 regional properties for A6VU29

Type Name Position InterPro Accession
domain Translational (tr)-type GTP-binding domain 354 - 523 IPR000795
domain Small GTP-binding protein domain 357 - 513 IPR005225
domain Translation initiation factor IF-2, N-terminal 279 - 328 IPR006847
domain Initiation factor 2 associated domain, bacterial 62 - 95 IPR013575
domain Translation initiation factor IF- 2, domain 3 631 - 744 IPR023115
domain Translation initiation factor IF-2, domain II 529 - 623 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
MTVQTVKILS ELVSTPVDKL LAQMKDAGLP QTSASQEVSE VEKQVLLSYL KRQHGEEGDN
70 80 90 100 110 120
SQRITLQRKT TSTLSRDGGK AVNVAVKKKR TYVKRDDEEA QKQEELAKRL AEEQERLAQE
130 140 150 160 170 180
KARLELERKQ EEEKAAKAKA EAEEKARQEA AVKNVVADAG AVNETEQYVS DTGAAEPVES
190 200 210 220 230 240
PKQPKASKKV SQPAMDSKKS TVAPKGKKGP VRHDNDKDKD KPRGRVNPDN KRTSRVNVND
250 260 270 280 290 300
EDEFTRRGKL GRKNKKPSKQ EHGFQKPTAK MIHEVALPES ITVADLAEKM AVKGAEVIKI
310 320 330 340 350 360
MFKMGAMATI NQTIDRDTAT LVVEEMGHTV KFIDENAVEN DMIEAIDYQG EAIKRAPVVT
370 380 390 400 410 420
VMGHVDHGKT SLLDYIRTTR VAAGESGGIT QHIGAYHVET PHGMISFLDT PGHAAFTSMR
430 440 450 460 470 480
ARGAKATDIV ILVCAADDGV MPQTIEAIQH ARAAGVPMVV AMTKIDKEGA DIDRVKNELV
490 500 510 520 530 540
AQEVVPEEWG GDIQFVGVSA KSGEGIEALL EAVLLQAEVL ELTAVPSAPA KGVVVEARLD
550 560 570 580 590 600
RGRGSVATLL VQNGTLKKGD IVLAGLQMGR VRALLDETGK AIDSAGPSIP VEILGLDGTP
610 620 630 640 650 660
EAGEEFIVVA DERKAREVAN FRQGKYREVR FARQHSAKLE NLFSEMGKDE VRTLNVVLKA
670 680 690 700 710 720
DVRGSLEALI KSLTDMNTDE VKVNVVSSGV GGITETDATL ALASDAVIFG FNVRADNSAK
730 740 750 760 770 780
QFIERESIDL RYYSVIYNII DDVKSALSGM LSPDLREDIK GTAEVRDVFR SPKFGLIAGC
790 800 810 820 830 840
MVIEGTVYRN KQIRVLRDDV VIYEGELESL RRFKDAVNEV SRGMECGIGV KNYNDVKVGD
850
KIEVFETVEV ARTL