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 P75386

Entry ID Method Resolution Chain Position Source
AF-P75386-F1 Predicted AlphaFoldDB

No variants for P75386

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P75386

No associated diseases with P75386

3 regional properties for P75386

Type Name Position InterPro Accession
domain HD/PDEase domain 58 - 187 IPR003607
domain HD domain 62 - 167 IPR006674
domain RelA/SpoT 238 - 367 IPR007685

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
MFYNWLKLYK FSKMATLVEI ERDFLQKTAQ KFAPEVVALI TKALDYSKKW HGEQKRLSGE
70 80 90 100 110 120
PFFIHPLRTA LRLVEWNMDS NTVCAGLLHD IIEDTQVTEA DLTAIFGKEI TDLVVKVTKI
130 140 150 160 170 180
TSESKKQRQL NRKKEDLNLK SLVNIAMSSQ QEVNALVLKL ADRLDNISSI EFLAVEKQKI
190 200 210 220 230 240
IAKETLELYA KIAGRIGMYP VKTQLADLSF KVLDPKNFNN TLSKINQQKV FYDNEWGNFK
250 260 270 280 290 300
KQLEEMLEQN QIEYRLESRI KGIYSTYQKL TFHEQNIAKI HDLFAIRLIV KSELDCYHLL
310 320 330 340 350 360
GLIHLNFTVL MKHFKDYIAS PKQNFYQSIH TTVRLKGLNV EIQIRTQRMD HVSKYGFASH
370 380 390 400 410 420
WIYKEKKEGL LASALQVNYL NSKQMHSRDF FKRIFGTDII KVNVSSDNEP NIVKKLNVES
430 440 450 460 470 480
NSKLLDIAYE LYPKQFNKLE KIKLDGVEVM SFDVTAENEM VIEFCFGKTN NLKRRWLRYM
490 500 510 520 530 540
NNHVFRERVK KDLNKLKKAV KYSELPLYEK ALEELHLKLA DETQIKQRLN ALGIKKLTEF
550 560 570 580 590 600
LELIEYPHFP KNEHLYFLAS NNQKWRELIK PIKFALSQAV FQNSYFEQIE GIYITKIVIE
610 620 630 640 650 660
TCCTKIPDMP EQVIGILMKN ILRVHLHDCR ELANQKQPKI IPLYWNAHQL KMRPRKFRCQ
670 680 690 700 710 720
INIRGVWSET TVNKIVQTII EGDSYLERII PKIDKQKDEF ELNITMFIDN YHQLITIMEQ
730
ITTKNISYVW KYL