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 Q02190

Entry ID Method Resolution Chain Position Source
AF-Q02190-F1 Predicted AlphaFoldDB

No variants for Q02190

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q02190

No associated diseases with Q02190

5 regional properties for Q02190

Type Name Position InterPro Accession
domain AAA+ ATPase domain 167 - 306 IPR003593
domain ATPase, AAA-type, core 171 - 304 IPR003959
conserved_site ATPase, AAA-type, conserved site 274 - 292 IPR003960
domain Proteasomal ATPase OB C-terminal domain 61 - 113 IPR032501
domain AAA ATPase, AAA+ lid domain 329 - 368 IPR041569

Functions

Description
EC Number 1.3.7.3 With an iron-sulfur protein as acceptor
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

2 GO annotations of molecular function

Name Definition
cobalt ion binding Binding to a cobalt ion (Co).
phycoerythrobilin:ferredoxin oxidoreductase activity Catalysis of the reaction: (3Z)-phycoerythrobilin + oxidized ferredoxin = 15,16-dihydrobiliverdin + reduced ferredoxin.

1 GO annotations of biological process

Name Definition
phytochromobilin biosynthetic process The chemical reactions and pathways resulting in the formation of phytochromobilin, which involves the oxidative cleavage of heme by a heme oxygenase(HO) to form biliverdin IX alpha.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTNQRFKSTD PVNIEGWSWQ PFLEDAIKRL EGLNVEPYPV PDRFLQREDQ TGSKSKSIPV
70 80 90 100 110 120
TTATWACKTE KFRQVRAACV SAGSAASVLN FVINPKSTYD LPFFGGDLVT LPAGHLLALD
130 140 150 160 170 180
LQPAIKTDEV HTTHVWDRLI PIFERWRDQL PYGGPIPEEA QPFFSPGFLW TRLPLGEEGD
190 200 210 220 230 240
ELIQSIVRPA FNDYLDLYLE LAASAERVTD ERSEVLLQGQ RKYTDYRAEK DPARGMLTRF
250
HGSEWTEAYI HTVLFDL