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 Q877A8

Entry ID Method Resolution Chain Position Source
AF-Q877A8-F1 Predicted AlphaFoldDB

No variants for Q877A8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q877A8

No associated diseases with Q877A8

No regional properties for Q877A8

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q877A8

Functions

Description
EC Number 1.11.1.6 Peroxidases
Subcellular Localization
  • Secreted
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
extracellular region The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.

3 GO annotations of molecular function

Name Definition
catalase activity Catalysis of the reaction: 2 hydrogen peroxide = O2 + 2 H2O.
heme binding Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
metal ion binding Binding to a metal ion.

2 GO annotations of biological process

Name Definition
cellular response to hydrogen peroxide Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hydrogen peroxide (H2O2) stimulus.
hydrogen peroxide catabolic process The chemical reactions and pathways resulting in the breakdown of hydrogen peroxide (H2O2).

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MRALSLASLI GIASAACPYM TGELERRDTG TDDATAATEE FLSQYYMADN DTFLTSDVGG
70 80 90 100 110 120
PIEDQNSLQV GDRGPTLLED FIFRQKIQRF DHERVPERAV HARGVGAHGV FTSYGDYSNI
130 140 150 160 170 180
TAASFLGAEG KETPVFVRFS TVAGSRGSSD LARDVHGFAT RFYTDEGNFD IVGNNIPVFF
190 200 210 220 230 240
IQDAILFPDL IHAVKPRGDN EIPQAATAHD SAWDFFSQQP SSLHTLLWAM SGHGIPRSLR
250 260 270 280 290 300
HVDGFGIHTF RFVTDNGDSK LVKFHWKSLQ GKASMVWEEA QQVSGKNPDF MRQDLFEAIE
310 320 330 340 350 360
AGRYPEWELG VQIMDEEDQL KFGFDLFDPT KIVPEEYVPI TKLGKMTLNR NPRNYFAETE
370 380 390 400 410 420
QVMFQPGHIV RGVDFTEDPL LQGRLFSYLD TQLNRHGGPN FEQLPINQPR VPVHNNNRDG
430 440 450 460 470 480
AGQMFIPLNP NAYSPNTLNK GSPKQANQTV GKGFFTAPGR ESTGRFTRAV SPSFEDVWSQ
490 500 510 520 530 540
PRLFYNSLTP AEQQFVVDAI RFENSNVKSS VVRNNVIIQL NRVSNDLARR VARAIGVEEP
550 560 570 580 590 600
EADPTYYHNN KTTDVGTFGQ KLKKLDGLKV GFLASVETPA SIEAASELSK QLSEDGVDVV
610 620 630 640 650 660
VVAERLSDGV DQTYSGSDAI QFDAVIVAPG AEGLFSTFSF TAPSNATSSS TLFPAGRPLQ
670 680 690 700 710 720
IVIDGFRFGK PVGAVGSAAT ALKNAGIQTS RDGVYVDKSV TSGFVDGIKD GLRTFKFLDR
FKLDH