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 Q9VQN8

Entry ID Method Resolution Chain Position Source
AF-Q9VQN8-F1 Predicted AlphaFoldDB

No variants for Q9VQN8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9VQN8

No associated diseases with Q9VQN8

4 regional properties for Q9VQN8

Type Name Position InterPro Accession
domain AAA+ ATPase domain 282 - 418 IPR003593
domain ATPase, AAA-type, core 286 - 415 IPR003959
conserved_site ATPase, AAA-type, conserved site 388 - 407 IPR003960
domain AAA ATPase, AAA+ lid domain 444 - 494 IPR041569

Functions

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

2 GO annotations of cellular component

Name Definition
centrosome A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle.
chromosome A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information.

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.
hydrolase activity Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
magnesium ion binding Binding to a magnesium (Mg) ion.
microtubule severing ATPase activity Catalysis of the reaction: ATP + H2O = ADP + phosphate. Catalysis of the severing of a microtubule at a specific spot along its length, coupled to the hydrolysis of ATP.

5 GO annotations of biological process

Name Definition
ATP metabolic process The chemical reactions and pathways involving ATP, adenosine triphosphate, a universally important coenzyme and enzyme regulator.
microtubule severing The process in which a microtubule is broken down into smaller segments. Severing enzymes remove dimers from the middle of the filament to create new ends, unlike depolymerizing kinesins that use ATP to uncap microtubules at their ends.
mitotic sister chromatid segregation The cell cycle process in which replicated homologous chromosomes are organized and then physically separated and apportioned to two sets during the mitotic cell cycle. Each replicated chromosome, composed of two sister chromatids, aligns at the cell equator, paired with its homologous partner. One homolog of each morphologic type goes into each of the resulting chromosome sets.
regulation of microtubule depolymerization Any process that modulates the frequency, rate or extent of microtubule depolymerization.
response to wounding 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 stimulus indicating damage to the organism.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9UBP0 SPAST Spastin Homo sapiens (Human) PR
A6NCM1 IQCA1L IQ and AAA domain-containing protein 1-like Homo sapiens (Human) PR
Q6PIW4 FIGNL1 Fidgetin-like protein 1 Homo sapiens (Human) PR
A6H690 Iqca1l IQ and AAA domain-containing protein 1-like Mus musculus (Mouse) PR
Q6AXQ7 Iqca1l IQ and AAA domain-containing protein 1-like Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MSDEQSSWRS KLLLICQQTR SSSESIHFAA LKDHHARLQA CESMEKAMKE RCQKKITMSR
70 80 90 100 110 120
RTKRGITHAG YLFEMPHNSV FEPECRGFYE SCQQTEMASS DLQAPALEVS STYPVQQAVK
130 140 150 160 170 180
SRPEGQFPES RNNSTKKIDA QQYSSESSSQ SGFGFRTARE QLIMDELKKK NRQATSEVDA
190 200 210 220 230 240
VPTGMMNFRK KTLGGKRTVS SNFVSPVAQN DNSTSSRSSS IPPALAHLDS KMVDHILGES
250 260 270 280 290 300
MHDFKPVAWE DIAGLESAKS TFLEAIIMPL RRPDLFTGVR CPPRGVLLFG PPGTGKTLIA
310 320 330 340 350 360
KSIASQAKAK FFSINPSSLT SKWVGDAEKL VKTLFAVAAA HQPAIIFIDE VDSLLSKRSA
370 380 390 400 410 420
NENESTLRLK NEFLIHLDGA ASNEEIRVLV IGATNRPQEL DEAVRRRFVR RLYVPLPTRE
430 440 450 460 470 480
ARQKIIEKLI HQVKHNLDVR QVIELAELTD GYSGADVDTL CRYASMAPLR SLTPDQMEVI
490 500 510 520
ETHQLPAVTM DDFKQALRVI SKSVSSEDCK QFEAWNEIYG VRH