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 D5HA94

Entry ID Method Resolution Chain Position Source
AF-D5HA94-F1 Predicted AlphaFoldDB

No variants for D5HA94

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for D5HA94

No associated diseases with D5HA94

3 regional properties for D5HA94

Type Name Position InterPro Accession
domain Cell division protein FtsQ/DivIB, C-terminal 196 - 309 IPR005548
domain POTRA domain, FtsQ-type 124 - 192 IPR013685
domain POTRA domain 124 - 192 IPR034746

Functions

Description
EC Number
Subcellular Localization
  • Cell inner membrane ; Multi-pass membrane protein ; Cytoplasmic side
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

5 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
ATP-dependent peptidase activity Catalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis.
metalloendopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
zinc ion binding Binding to a zinc ion (Zn).

2 GO annotations of biological process

Name Definition
protein catabolic process The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MADQTSQNDN QNGSGLPGGG PSGTGRGRLI IWVIAGTLLA LWAYSYWGMG ASGGERISYS
70 80 90 100 110 120
EFRTQLQQEN VERVEVKGNA INGSLKSQAT RSEQGNTIEY QNFVTYLPSF GDEQLMDLLE
130 140 150 160 170 180
SQGVNVVTKP ESSFPWGLVI MGLLPVLLLF GVGYIFLRRM QSQGQGLFSV RQSKAELYDK
190 200 210 220 230 240
DEEDTTFDDV AGADSAKEEL REIIKFLKNP KRFEGLGGKV PKGVLLVGPP GTGKTLLARA
250 260 270 280 290 300
VAGEANAPFF SVSGSDFMEM FVGVGASRVR DMFSEAKETS PAIIFIDELD SIGRKRGAGL
310 320 330 340 350 360
GGGNDEREQT LNQLLSELDG FEENEGVIVM AATNRPDILD SALTRPGRFD RQITVDLPTK
370 380 390 400 410 420
QSRHEILKIH AREKPLSDDV DLEEIARSTP GFSGADLENL LNEAALLAGR HGHDAIQYSD
430 440 450 460 470 480
IEQARDKVMM GLKRDGMVLD DEEKKLLAYH EAGHAIVGAV LPNADPVHKV TIVPRGKAMG
490 500 510 520 530 540
VTQQLPEKDQ YLYRHDYILD RLAVIMGGRA AEELIFDTAT SGAENDLKQV RKMARKMVLD
550 560 570 580 590 600
WGMGDQFKHI SLGEDQGNVF LGDEIAKGRE YSDDTAREVD EEIRRISEDA FQRAVDTLNE
610 620 630 640 650 660
HHEAFDQLAD MLIEQEEVSG KDVLNLVNGD TDEIGHMPTT NGAAASEENG SADDHEPDEA
670 680
TVIEEDGESG EGRASGSADA SGS