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 O94423

Entry ID Method Resolution Chain Position Source
AF-O94423-F1 Predicted AlphaFoldDB

No variants for O94423

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O94423

No associated diseases with O94423

5 regional properties for O94423

Type Name Position InterPro Accession
repeat WD40 repeat 154 - 234 IPR001680-1
repeat WD40 repeat 238 - 322 IPR001680-2
repeat WD40 repeat 325 - 365 IPR001680-3
repeat WD40 repeat 368 - 416 IPR001680-4
domain Anaphase-promoting complex subunit 4-like, WD40 domain 156 - 219 IPR024977

Functions

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

1 GO annotations of cellular component

Name Definition
anaphase-promoting complex A ubiquitin ligase complex that degrades mitotic cyclins and anaphase inhibitory protein, thereby triggering sister chromatid separation and exit from mitosis. Substrate recognition by APC occurs through degradation signals, the most common of which is termed the Dbox degradation motif, originally discovered in cyclin B.

2 GO annotations of molecular function

Name Definition
anaphase-promoting complex binding Binding to an anaphase-promoting complex. A ubiquitin ligase complex that degrades mitotic cyclins and anaphase inhibitory protein, thereby triggering sister chromatid separation and exit from mitosis.
ubiquitin ligase activator activity Binds to and increases the activity of a ubiquitin ligase.

7 GO annotations of biological process

Name Definition
anaphase-promoting complex-dependent catabolic process The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, with ubiquitin-protein ligation catalyzed by the anaphase-promoting complex, and mediated by the proteasome.
meiotic cell cycle Progression through the phases of the meiotic cell cycle, in which canonically a cell replicates to produce four offspring with half the chromosomal content of the progenitor cell via two nuclear divisions.
positive regulation of anaphase-promoting complex-dependent catabolic process Any process that activates or increases the frequency, rate or extent of anaphase-promoting complex-dependent catabolic process.
positive regulation of ascospore formation Any process that activates, maintains or increases the frequency, rate or extent of ascospore formation, a process in which a sexual spore, named ascospore, from Ascomycete fungi was produced inside an ascus.
positive regulation of meiotic cell cycle Any process that activates or increases the frequency, rate or extent of progression through the meiotic cell cycle.
positive regulation of metaphase/anaphase transition of meiosis II Any process that activates or increases the frequency, rate or extent of metaphase/anaphase transition of meiosis II.
sporulation resulting in formation of a cellular spore The process in which a relatively unspecialized cell acquires the specialized features of a cellular spore, a cell form that can be used for dissemination, for survival of adverse conditions because of its heat and dessication resistance, and/or for reproduction.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGDRFIPIRN VSNEFNFSFQ SFKECVLSHG SNLRRKTSGT IQRQFMELLS MELFGSQASR
70 80 90 100 110 120
SRAFYYGEDK RKIEKKMLDT PDRKSYSLSP ISPQSQDMLR QPQKPKRAFP KTPYKILDAP
130 140 150 160 170 180
YLKNDFYLNL LDWGQSNVLA VGLASSIYLW SAASGKVVQL HDFGATNHVT SVLWTGKGTQ
190 200 210 220 230 240
LAVGTDSGVI YIWDIESTKS VRSLKGHSER VAALAWNDNT LTSGGKDEVI LHHDLRAPGC
250 260 270 280 290 300
CAEMMKVHEQ EICGLQWDRS LGQLASGGND NNLFVWDYRS SRPLHKFEEH TAAVKAIGWS
310 320 330 340 350 360
PHQRGILASG GGTIDRCLTI HNTLTGRLQN KLDTGSQVCN MAWSKTSNEI VTTHGFAKNQ
370 380 390 400 410 420
VSLWKYPSLK NIANLTAHTN RVLYLSMSPD GQSIVTGAGD ETLRFWKLFN KKPKEESTLI
R