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 P0AG26

Entry ID Method Resolution Chain Position Source
AF-P0AG26-F1 Predicted AlphaFoldDB

No variants for P0AG26

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P0AG26

No associated diseases with P0AG26

7 regional properties for P0AG26

Type Name Position InterPro Accession
domain ACT domain 622 - 702 IPR002912
domain HD/PDEase domain 41 - 166 IPR003607
domain TGS 386 - 447 IPR004095
domain HD domain 45 - 144 IPR006674
domain RelA/SpoT 214 - 345 IPR007685
domain RelA/SpoT, TGS domain 389 - 447 IPR033655
domain RelA/SpoT, AH and RIS domains 459 - 541 IPR045600

Functions

Description
EC Number 3.1.7.2 Diphosphoric monoester hydrolases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

1 GO annotations of molecular function

Name Definition
guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity Catalysis of the reaction: guanosine 3',5'-bis(diphosphate) + H2O = guanosine 5'-diphosphate + diphosphate.

1 GO annotations of biological process

Name Definition
guanosine tetraphosphate biosynthetic process The chemical reactions and pathways resulting in the formation of guanine tetraphosphate (5'-ppGpp-3'), a derivative of guanine riboside with four phosphates.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MYLFESLNQL IQTYLPEDQI KRLRQAYLVA RDAHEGQTRS SGEPYITHPV AVACILAEMK
70 80 90 100 110 120
LDYETLMAAL LHDVIEDTPA TYQDMEQLFG KSVAELVEGV SKLDKLKFRD KKEAQAENFR
130 140 150 160 170 180
KMIMAMVQDI RVILIKLADR THNMRTLGSL RPDKRRRIAR ETLEIYSPLA HRLGIHHIKT
190 200 210 220 230 240
ELEELGFEAL YPNRYRVIKE VVKAARGNRK EMIQKILSEI EGRLQEAGIP CRVSGREKHL
250 260 270 280 290 300
YSIYCKMVLK EQRFHSIMDI YAFRVIVNDS DTCYRVLGQM HSLYKPRPGR VKDYIAIPKA
310 320 330 340 350 360
NGYQSLHTSM IGPHGVPVEV QIRTEDMDQM AEMGVAAHWA YKEHGETSTT AQIRAQRWMQ
370 380 390 400 410 420
SLLELQQSAG SSFEFIESVK SDLFPDEIYV FTPEGRIVEL PAGATPVDFA YAVHTDIGHA
430 440 450 460 470 480
CVGARVDRQP YPLSQPLTSG QTVEIITAPG ARPNAAWLNF VVSSKARAKI RQLLKNLKRD
490 500 510 520 530 540
DSVSLGRRLL NHALGGSRKL NEIPQENIQR ELDRMKLATL DDLLAEIGLG NAMSVVVAKN
550 560 570 580 590 600
LQHGDASIPP ATQSHGHLPI KGADGVLITF AKCCRPIPGD PIIAHVSPGK GLVIHHESCR
610 620 630 640 650 660
NIRGYQKEPE KFMAVEWDKE TAQEFITEIK VEMFNHQGAL ANLTAAINTT TSNIQSLNTE
670 680 690 700
EKDGRVYSAF IRLTARDRVH LANIMRKIRV MPDVIKVTRN RN