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 P47388

Entry ID Method Resolution Chain Position Source
AF-P47388-F1 Predicted AlphaFoldDB

No variants for P47388

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P47388

No associated diseases with P47388

4 regional properties for P47388

Type Name Position InterPro Accession
domain Translational (tr)-type GTP-binding domain 120 - 289 IPR000795
domain Small GTP-binding protein domain 125 - 280 IPR005225
domain Translation initiation factor IF- 2, domain 3 394 - 508 IPR023115
domain Translation initiation factor IF-2, domain II 298 - 391 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.

1 GO annotations of biological process

Name Definition
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKKNRAFNQV KKTKFDGRIK TSAKHQLRNV KTGVKDGVFI YKGPLTVSEF ASKTNIAVAN
70 80 90 100 110 120
IIKHFFLNGL ALTVNSVLTN EQLADACVNF GFDFKMETEV THENIVANIQ FEDSDDLLQP
130 140 150 160 170 180
RPPIVTIMGH VDHGKTSLLD TIRKTNVTAK EFGGITQKIG AYQVKNHQNK TITFIDTPGH
190 200 210 220 230 240
EAFTLMRARG AKVTDIVVLV VAADDGIKKQ TEEAISHAKS ANTPIIVFIN KMDKPTANPD
250 260 270 280 290 300
LVIQQLNKFD LVPEAWGGKT IFVMGSALTG QGINELLDNI LLLGEVEGYQ ANYNAHSSGY
310 320 330 340 350 360
AIEVQTSKGL GPIANVIVKR GTLKLGDIVV LGPAYGRVRT MHDENGNSLK QATPSKPVQI
370 380 390 400 410 420
SGFDIMPVAG EKFIVFDDEK DAKLIANKFK EQQKQKANNL TVNQTLKEQI KNKEIKILNL
430 440 450 460 470 480
IFKADSDGSL QAIKQAVENI NVAKISLSII HAAVGQISES DIMLAKASGA LLFSLNLGLS
490 500 510 520 530 540
QTVKNIASLQ GVKLEVHYHI PKLAEEIENI LKGQLDPVYE EIEIGKAEVL QLWFHSKIGN
550 560 570 580 590 600
IAGTIVKSGK IKRGNLCKLF RDKEIIFEGR IDSLKNEKTP VNLIETGKNC GIVINGCNDI
610
KIGDIIVAYE KQIVKDGKL