B0XTS1

PR
Gene name
sconB (AFUB_029730)
Protein name
Probable E3 ubiquitin ligase complex SCF subunit sconB
Names
Sulfur controller B, Sulfur metabolite repression control protein B
Species
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
KEGG Pathway
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-169 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for B0XTS1

Entry ID Method Resolution Chain Position Source
AF-B0XTS1-F1 Predicted AlphaFoldDB

No variants for B0XTS1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B0XTS1

No associated diseases with B0XTS1

9 regional properties for B0XTS1

Type Name Position InterPro Accession
repeat WD40 repeat 356 - 475 IPR001680-1
repeat WD40 repeat 475 - 696 IPR001680-2
domain F-box domain 193 - 240 IPR001810
conserved_site WD40 repeat, conserved site 380 - 394 IPR019775-1
conserved_site WD40 repeat, conserved site 460 - 474 IPR019775-2
conserved_site WD40 repeat, conserved site 501 - 515 IPR019775-3
repeat G-protein beta WD-40 repeat 380 - 394 IPR020472-1
repeat G-protein beta WD-40 repeat 460 - 474 IPR020472-2
repeat G-protein beta WD-40 repeat 640 - 654 IPR020472-3

Functions

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

1 GO annotations of cellular component

Name Definition
nuclear SCF ubiquitin ligase complex A ubiquitin ligase complex, located in the nucleus, in which a cullin from the Cul1 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by a Skp1 adaptor and an F-box protein. SCF complexes are involved in targeting proteins for degradation by the proteasome. The best characterized complexes are those from yeast and mammals (with core subunits named Cdc53/Cul1, Rbx1/Hrt1/Roc1).

3 GO annotations of molecular function

Name Definition
identical protein binding Binding to an identical protein or proteins.
ubiquitin binding Binding to ubiquitin, a protein that when covalently bound to other cellular proteins marks them for proteolytic degradation.
ubiquitin ligase-substrate adaptor activity The binding activity of a molecule that brings together a ubiquitin ligase and its substrate. Usually mediated by F-box BTB/POZ domain proteins.

5 GO annotations of biological process

Name Definition
protein polyubiquitination Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain.
regulation of transcription involved in G1/S transition of mitotic cell cycle Any process that regulates transcription such that the target genes are involved in the transition between G1 and S phase of the mitotic cell cycle.
response to arsenic-containing substance Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an arsenic stimulus from compounds containing arsenic, including arsenates, arsenites, and arsenides.
response to cadmium ion Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cadmium (Cd) ion stimulus.
SCF-dependent proteasomal ubiquitin-dependent protein 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 an SCF (Skp1/Cul1/F-box protein) complex, and mediated by the proteasome.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MDAHELSFRD GHGSSTSTMK DGCASAEKPH YLPGDSSFTS VFGPSETVED VETEPGSTQD
70 80 90 100 110 120
KPHSFNTQKP IRENLAGKNV APFLARHIPE QYAPLGSQGG QPVEISSANS KYCYRHRPDL
130 140 150 160 170 180
KCRRQADEPT MDKLQRELET LPQSDQQGIA HAWSIFSAAP AKHRKLILQG IMAQCCFPQL
190 200 210 220 230 240
SFISATVRDL IRIDFLTALP PEISFKILCY LDTTSLCKAA QVSRRWRALA DDDVVWHRMC
250 260 270 280 290 300
EQHIHRKCKK CGWGLPLLDR KRLRESKREI ERRAATWDVS KQPAGIEGSS ATIETAAAGS
310 320 330 340 350 360
KRKPESGKED TAMVKRQCTS IVSQSEQNED YFKTRYRPWK EVYKDRFKVG TNWKYGRCST
370 380 390 400 410 420
RVFKGHSNGI MCLQFEDNIL ATGSYDATIK IWDTETGEEL RTLKGHQSGI RCLQFDDTKL
430 440 450 460 470 480
ISGSMDHTLK VWNWRTGECI STYSGHRGGV VGLHFDATIL ASGSVDKTVK IWNFEDKSTC
490 500 510 520 530 540
LLRGHTDWVN AVRVDSASRT VFSASDDCTV KLWDLDTKSC IRTFHGHVGQ VQQVVPLPRE
550 560 570 580 590 600
FEFEDHDVEC ENDNVSVTSG DSPAASPQAL PGFDGQTSDT PSSAFGPAFD DGRPSPPRYI
610 620 630 640 650 660
VTSALDSTIR LWETSSGRCL RTFFGHLEGV WALAADTLRI VSGAEDRMVK IWDPRTGKCE
670 680 690
RTFTGHSGPV TCIGLGDSRF ATGSEDCEVR MYSFQT