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 Q2JMD7

Entry ID Method Resolution Chain Position Source
AF-Q2JMD7-F1 Predicted AlphaFoldDB

No variants for Q2JMD7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2JMD7

No associated diseases with Q2JMD7

6 regional properties for Q2JMD7

Type Name Position InterPro Accession
domain Translational (tr)-type GTP-binding domain 545 - 718 IPR000795
domain Small GTP-binding protein domain 547 - 708 IPR005225
domain Translation initiation factor IF-2, N-terminal 2 - 53 IPR006847-1
domain Translation initiation factor IF-2, N-terminal 471 - 519 IPR006847-2
domain Translation initiation factor IF- 2, domain 3 832 - 941 IPR023115
domain Translation initiation factor IF-2, domain II 724 - 819 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
MTDKVRIYDI AREMGRDSRD VLEVCEQLGI PFKTHSSTIS PEQAELVRSK LGAPHIVKPP
70 80 90 100 110 120
RPRPKPPSES LPPEPPAEAK VGERPQQKVP GTASAIVGIR RPAPAQQPAP VGEAKTAETL
130 140 150 160 170 180
PAAKPSLSRP ERVSPEKGSA GGAQLIGPPR RQVTPLVRSS EATQKPETVS QPATPPTPSE
190 200 210 220 230 240
SAAAKASGSE PSPVAKRPIV LSPPQRATSG TKPPAERPEP PQKAPEPSRP SPSEAPSPSH
250 260 270 280 290 300
ARVPQPAEEK APSPPPAQRP RPQLVSAPVR PGTRSPATKE DSVSSGKAGE APRPQRRMEL
310 320 330 340 350 360
VGPPTRPVAK PAPPEPDAAS PLPERIPGER PSPVLVEAPV RPTPPKVKRK TEEEEDDELQ
370 380 390 400 410 420
ALSRRAARVQ AKRKRSRRRG EGDGDGLDLD PMTIISAVKQ AELNALKPLA RPTAKPPSYR
430 440 450 460 470 480
PPAATAAPPA RPRPAARLQQ QPTSAEAGAA DRASGTEPLP EEKVLLLDGS LTVQELAHRL
490 500 510 520 530 540
RVAETEIIKT LFFKGVMVTI NQVLDESLAE SVAKELGYEI RRPKAEPEAK KTEMLDVEDI
550 560 570 580 590 600
DHLVSRPPVV TIMGHVDHGK TTLLDAIRDT KVAQGEAGGI TQRIGAYHVD VNFEGQKRRI
610 620 630 640 650 660
VFLDTPGHQA FTAMRARGAR VTDIAVLVVA ADDGVQPQTL EAISHARAAQ VPIIVAINKI
670 680 690 700 710 720
DKPGSQPERI KQQLAEHGLL PEEWGGDTPM VEVSALTRRN LDALLEMILL VADVAELQAN
730 740 750 760 770 780
PNRPARGTVI EAHLDKARGP VATLLVQNGT LRVGDTLVAG AVLGRVKAMM DDRGQRLQEA
790 800 810 820 830 840
GPSSAVQLLG LDEVPAAGDE FQVYTDEKEA RRIAQERAEV LRQTRLQQAL LSRRVSLGSV
850 860 870 880 890 900
SAKAQEGQLK ELNLIIKTDV QGSAEAIQTA LRDLPQEEVQ LRVLLAAPGE ITETDVDLAA
910 920 930 940 950 960
ASDAIILGFN TTLAPGARQA ADDKGVDVRE YDIIYNLLDD LRAAMEGLLE PEEVEEPLGQ
970 980 990 1000 1010 1020
AEVRLVIPIG RGAVAGSYVL SGKVQRNALV RVRRRGEVVY EGRLDSLKRF KDDVREVAAG
1030 1040 1050
FECGIGIDKF QSWQEGDIIE VYQMVTKRRT LASV