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 A4VXH3

Entry ID Method Resolution Chain Position Source
AF-A4VXH3-F1 Predicted AlphaFoldDB

No variants for A4VXH3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A4VXH3

No associated diseases with A4VXH3

6 regional properties for A4VXH3

Type Name Position InterPro Accession
domain Translational (tr)-type GTP-binding domain 442 - 609 IPR000795
domain Small GTP-binding protein domain 444 - 601 IPR005225
domain Translation initiation factor IF-2, N-terminal 1 - 51 IPR006847-1
domain Translation initiation factor IF-2, N-terminal 362 - 413 IPR006847-2
domain Translation initiation factor IF- 2, domain 3 717 - 832 IPR023115
domain Translation initiation factor IF-2, domain II 617 - 712 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
MSKKRLNEIA RELGVSSKEV VAKAQELGFE VKSHASSVDE ASAKRLAESF GGQKSEATKV
70 80 90 100 110 120
AAKVSKPEKV DETPKVETAK VEKAKETQPV VKEEVAASAV QSASHRPQSR NFKAEREARA
130 140 150 160 170 180
KEQAAKRAQN QGKGGQAKSD QDRRDNRQLG QGRSNNERND RRDNRRDQRP EERKDNRFGD
190 200 210 220 230 240
RRDNRDNRRQ DNRSGRLARF EQREAAKPAG PKIDFKARAA ALKAEQNAEY ARTSEERFRQ
250 260 270 280 290 300
AQEAKKQPKK PKEIKFEEPV VESKPFVKPA LVASVPEQVA ETTVDTRRKK QARPDKKRDF
310 320 330 340 350 360
NSDEEDGPRK QQRNRNSQNQ VRNQRTSNWN NNKKNKKGKA NQPAKPVTER KFHELPTEFE
370 380 390 400 410 420
YTAGMTVAEI AKRIKREPAE IVKKLFLMGV MATQNQSLDG DTIELLMVDY GIEAKEKVEV
430 440 450 460 470 480
DNADIERFFV EEGYLNEEEM TERPPVVTIM GHVDHGKTTL LDTLRNSRVA TGEAGGITQH
490 500 510 520 530 540
IGAYQIEEAG KKITFLDTPG HAAFTSMRAR GASVTDLTIL VVAADDGVMP QTIEAINHSK
550 560 570 580 590 600
AANVPIIVAI NKIDKPGANP ERVIGELAEH GVISTAWGGE SEFVEISAKF NQNIDELLET
610 620 630 640 650 660
VLLVAEIQEL KADPTVRAIG TVIEAHLDKG KGAVATLLVQ QGTLNVQDPI VVGNTFGRVR
670 680 690 700 710 720
AMTNDLGRRV KTAGPSTPVS ITGLNETPMA GDHFAVYEDE KSARAAGEER AKRALLKQRQ
730 740 750 760 770 780
ATQRVSLENL FDTLKAGEVK SVNVIIKADV QGSVEALASS LQKIEVEGVR VNIVHSAVGA
790 800 810 820 830 840
INESDITLAE ASNALVIGFN VRPTAEARSQ AEADDVEVRL HSIIYKVIEE MEDAMKGMLD
850 860 870 880 890 900
PEYEEKIIGE AIIRETFKVS KVGTIGGFMV VRGKVTRDSS VRVIRDGVVV FDGKLASLKR
910 920 930
YKDDVKEVGN AQEGGLMIEN YNDLKVDDTI EAYIMEEIKK