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

22 structures for P07677

Entry ID Method Resolution Chain Position Source
1SKY X-ray 320 A E 1-473 PDB
7L1Q EM 340 A D/E/F 1-473 PDB
7L1R EM 310 A D/E/F 1-473 PDB
7L1S EM 360 A D/E/F 1-473 PDB
7XKH EM 310 A D/E/F 1-473 PDB
7XKO EM 340 A D/E/F 1-473 PDB
7XKP EM 300 A D/E/F 1-473 PDB
7XKQ EM 330 A D/E/F 1-473 PDB
7XKR EM 260 A D/E/F 1-473 PDB
8HH1 EM 290 A D/E/F 1-473 PDB
8HH2 EM 300 A D/E/F 1-473 PDB
8HH3 EM 430 A D/E/F 1-473 PDB
8HH4 EM 310 A D/E/F 1-473 PDB
8HH5 EM 290 A D/E/F 1-473 PDB
8HH6 EM 290 A D/E/F 1-473 PDB
8HH7 EM 250 A D/E/F 1-473 PDB
8HH8 EM 280 A D/E/F 1-473 PDB
8HH9 EM 360 A D/E/F 1-473 PDB
8HHA EM 340 A D/E/F 1-473 PDB
8HHB EM 350 A D/E/F 1-473 PDB
8HHC EM 330 A D/E/F 1-473 PDB
AF-P07677-F1 Predicted AlphaFoldDB

No variants for P07677

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P07677

No associated diseases with P07677

4 regional properties for P07677

Type Name Position InterPro Accession
domain ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain 138 - 351 IPR000194
domain AAA+ ATPase domain 150 - 335 IPR003593
domain ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain 6 - 80 IPR004100
active_site ATPase, alpha/beta subunit, nucleotide-binding domain, active site 342 - 351 IPR020003

Functions

Description
EC Number 7.1.2.2 Hydron translocation linked to the hydrolysis of a nucleoside triphosphate
Subcellular Localization
  • Cell membrane ; Peripheral membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
proton-transporting ATP synthase complex, catalytic core F(1) The sector of a hydrogen-transporting ATP synthase complex in which the catalytic activity resides; it comprises the catalytic core and central stalk, and is peripherally associated with a membrane, such as the plasma membrane or the mitochondrial inner membrane, when the entire ATP synthase is assembled.

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
proton-transporting ATP synthase activity, rotational mechanism Enables the synthesis of ATP from ADP and phosphate by the transfer of protons from one side of a membrane to the other by a rotational mechanism driven by a gradient according to the reaction: ADP + H2O + phosphate + H+(in) -> ATP + H+(out).
proton-transporting ATPase activity, rotational mechanism Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) = ADP + phosphate + H+(out), by a rotational mechanism.

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
MTRGRVIQVM GPVVDVKFEN GHLPAIYNAL KIQHKARNEN EVDIDLTLEV ALHLGDDTVR
70 80 90 100 110 120
TIAMASTDGL IRGMEVIDTG APISVPVGQV TLGRVFNVLG EPIDLEGDIP ADARRDPIHR
130 140 150 160 170 180
PAPKFEELAT EVEILETGIK VVDLLAPYIK GGKIGLFGGA GVGKTVLIQE LIHNIAQEHG
190 200 210 220 230 240
GISVFAGVGE RTREGNDLYH EMKDSGVISK TAMVFGQMNE PPGARMRVAL TGLTMAEYFR
250 260 270 280 290 300
DEQGQDGLLF IDNIFRFTQA GSEVSALLGR MPSAIGYQPT LATEMGQLQE RITSTAKGSI
310 320 330 340 350 360
TSIQAIYVPA DDYTDPAPAT TFSHLDATTN LERKLAEMGI YPAVDPLVST SRALAPEIVG
370 380 390 400 410 420
EEHYQVARKV QQTLERYKEL QDIIAILGMD ELSDEDKLVV HRARRIQFFL SQNFHVAEQF
430 440 450 460 470
TGQPGSYVPV KETVRGFKEI LEGKYDHLPE DRFRLVGRIE EVVEKAKAMG VEV