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 Q8MM62

Entry ID Method Resolution Chain Position Source
AF-Q8MM62-F1 Predicted AlphaFoldDB

No variants for Q8MM62

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8MM62

No associated diseases with Q8MM62

3 regional properties for Q8MM62

Type Name Position InterPro Accession
domain PAS domain 109 - 233 IPR000014
domain GGDEF domain 226 - 397 IPR000160
domain EAL domain 405 - 658 IPR001633

Functions

Description
EC Number 3.1.4.35 Phosphoric diester hydrolases
Subcellular Localization
  • Cytoplasm, cytosol
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cAMP-dependent protein kinase complex An enzyme complex, composed of regulatory and catalytic subunits, that catalyzes protein phosphorylation. Inactive forms of the enzyme have two regulatory chains and two catalytic chains; activation by cAMP produces two active catalytic monomers and a regulatory dimer.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

7 GO annotations of molecular function

Name Definition
3',5'-cyclic-AMP phosphodiesterase activity Catalysis of the reaction: 3',5'-cyclic AMP + H2O = AMP + H+.
3',5'-cyclic-GMP phosphodiesterase activity Catalysis of the reaction: 3',5'-cyclic GMP + H2O = GMP + H+.
cAMP binding Binding to cAMP, the nucleotide cyclic AMP (adenosine 3',5'-cyclophosphate).
cAMP-dependent protein kinase inhibitor activity Binds to and stops, prevents or reduces the activity of a cAMP-dependent protein kinase.
cGMP binding Binding to cGMP, the nucleotide cyclic GMP (guanosine 3',5'-cyclophosphate).
metal ion binding Binding to a metal ion.
protein kinase A catalytic subunit binding Binding to one or both of the catalytic subunits of protein kinase A.

6 GO annotations of biological process

Name Definition
adenylate cyclase-activating G protein-coupled cAMP receptor signaling pathway An adenylate cyclase-activating G protein-coupled receptor signaling pathway initiated by extracellular cAMP binding to its receptor on the surface of the target cell, and ending with the regulation of a downstream cellular process.
cAMP catabolic process The chemical reactions and pathways resulting in the breakdown of the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
cGMP-mediated signaling Any intracellular signal transduction in which the signal is passed on within the cell via cyclic GMP (cGMP). Includes production of cGMP, and downstream effectors that further transmit the signal within the cell.
negative regulation of cAMP-dependent protein kinase activity Any process that stops, prevents or reduces the frequency, rate or extent of cAMP-dependent protein kinase activity.
protein localization to cell cortex A process in which a protein is transported to, or maintained in, the cell cortex.
regulation of positive chemotaxis to cAMP by DIF-1 Any process that modulates the rate, frequency, or extent of directed movement of a motile cell or organism up a concentration gradient of 3',5'-cAMP by the action of DIF-1. DIF-1 is a chlorinated alkylphenone.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MNSKYGDNII DFLRYLEKFV KSLTKDNKIE EFKTFDIKSL LYPRNKDYFG NLSKFLLAVI
70 80 90 100 110 120
SARIGSNFIN EDDIFEISEL LKEFLGQELE HLPYLSYEEL YVEIVEQVGE INGTVSEIIE
130 140 150 160 170 180
AITVTIDFLD TFEKVSQTID RSNEKQKLLA YLSAPVNQLD NSVSGVFNEN DYTDIQRFFT
190 200 210 220 230 240
ELTNENNQSP DSNISILIND FQSLLNILES QQASSSSSKM IINDSPRTQQ RNGTTEQQKK
250 260 270 280 290 300
QQQQQYLQKN KEPFYSKDKI MQVSGPSYVF TPSDCNVSIQ VGIPPDTLKR DQSICHFIVP
310 320 330 340 350 360
HFLISKDVSL SEVEFPIFYN KFVQKGKTKV VIICTVEQKQ RIETILCESI FGPAPEHIYT
370 380 390 400 410 420
DEEITIPDYK IDLLTERLAI DPRANDEKLD SYVIFKTFDT FGVVDIDLPS ASDPTKLINL
430 440 450 460 470 480
RIRNTKGLIS FHEDYHVVQK QLHLKLQEQQ QDQQDKSSSS TTDKQMINTS GNRIILKNNT
490 500 510 520 530 540
VSVIDSTIES QYVPVLPFGN DHEQVKKFKA PILGVTFLGV SHGLDFTHCS HTTGFIIWIN
550 560 570 580 590 600
GSGVVVDPPV GNTTYLQTNG IYGKTVEHII LTHCHADHDS GILQKIIERN KVTLYTTKTI
610 620 630 640 650 660
NESYMRKLKA LTGLPEQSLK NYYTWVPVTI GNKIKILGAE FEFDYSFHVI PTIRFKLEIY
670 680 690 700 710 720
NKKISYSADT FYDLQKFKQL KDQGVLSKKR IERLKSFVFD ADMIIHESGV APIHTPMANL
730 740 750 760 770 780
LELPSEIRKK IRVVHCSSSV DTKGEIIRPK EGLENTEIIK VDRKYKGVAE CIQIQTALNH
790 800 810 820 830 840
CSVFSKLSPA EVQRVFFLCK KIWVKRNDVI IKKGSPSDMF YIILSGKVLV YENEYEPIKS
850 860 870 880 890 900
TTSVGTVVTD TTTITTTVKT DAIKIPTIKL CAGETLGESA LQLDKNIDAS ATVIAETDVC
910 920 930 940 950 960
LLVWKTMDLR TEFHSNLNTF ISKVHMDLSH INSCRDAIIR AFQHNITQHI NKEEVDSIAN
970 980 990 1000 1010 1020
GSKDVSFAHH QVIFNEGDTS DSMYIIKQGR VRIHSKKNKN IIRYLNVGDF FGETAYRRSN
1030 1040 1050 1060 1070 1080
EDSNFLPTRS FTATAIDPTI LLKLDIESIV NPRIQNIIEQ KAKKNAEDNI RYHAYSPKIR
1090
TPRTPRKVYP IEGLSI