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 O61577

Entry ID Method Resolution Chain Position Source
AF-O61577-F1 Predicted AlphaFoldDB

No variants for O61577

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O61577

No associated diseases with O61577

5 regional properties for O61577

Type Name Position InterPro Accession
domain AAA+ ATPase domain 266 - 408 IPR003593
domain ATPase, AAA-type, core 270 - 406 IPR003959
conserved_site ATPase, AAA-type, conserved site 378 - 397 IPR003960
domain Spastin/Vps4, C-terminal 471 - 514 IPR015415
domain AAA ATPase, AAA+ lid domain 428 - 464 IPR041569

Functions

Description
EC Number 5.6.1.1 Enzymes altering polypeptide conformation or assembly
Subcellular Localization
  • Cytoplasm
  • Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
  • Cytoplasm, cytoskeleton, spindle pole
  • Predominantly cytoplasmic (By similarity)
  • Also localized to the interphase centrosome and the mitotic spindle poles (PubMed:8907702)
  • Enhanced recruitment to the mitotic spindle poles requires microtubules and interaction with KATNB1 (By similarity)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

8 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.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
microtubule Any of the long, generally straight, hollow tubes of internal diameter 12-15 nm and external diameter 24 nm found in a wide variety of eukaryotic cells; each consists (usually) of 13 protofilaments of polymeric tubulin, staggered in such a manner that the tubulin monomers are arranged in a helical pattern on the microtubular surface, and with the alpha/beta axes of the tubulin subunits parallel to the long axis of the tubule; exist in equilibrium with pool of tubulin monomers and can be rapidly assembled or disassembled in response to physiological stimuli; concerned with force generation, e.g. in the spindle.
microtubule cytoskeleton The part of the cytoskeleton (the internal framework of a cell) composed of microtubules and associated proteins.
midbody A thin cytoplasmic bridge formed between daughter cells at the end of cytokinesis. The midbody forms where the contractile ring constricts, and may persist for some time before finally breaking to complete cytokinesis.
mitotic spindle pole Either of the ends of a mitotic spindle, a spindle that forms as part of mitosis, where spindle microtubules are organized; usually contains a microtubule organizing center and accessory molecules, spindle microtubules and astral microtubules.
spindle The array of microtubules and associated molecules that forms between opposite poles of a eukaryotic cell during mitosis or meiosis and serves to move the duplicated chromosomes apart.
spindle pole Either of the ends of a spindle, where spindle microtubules are organized; usually contains a microtubule organizing center and accessory molecules, spindle microtubules and astral microtubules.

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.
isomerase activity Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5.
microtubule binding Binding to a microtubule, a filament composed of tubulin monomers.
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.

3 GO annotations of biological process

Name Definition
cell cycle The progression of biochemical and morphological phases and events that occur in a cell during successive cell replication or nuclear replication events. Canonically, the cell cycle comprises the replication and segregation of genetic material followed by the division of the cell, but in endocycles or syncytial cells nuclear replication or nuclear division may not be followed by cell division.
cell division The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSVDEICENT KMGREYALLG NYETSLVYYQ GVLQQIQKLL TSVHEPQRKH QWQTIRQELS
70 80 90 100 110 120
QEYEHVKNIT KTLNGFKSEP AAPEPAPNHR AAPFSHHQHA AKPAAAEPAR DPDVWPPPTP
130 140 150 160 170 180
VDHRPSPPYQ RAARKDPPRR SEPSKPANRA PGNDRGGRGP SDRRGDARSG GGGRGGARGS
190 200 210 220 230 240
DKDKNRGGKS DKDKKAPSGE EGDEKKFDPA GYDKDLVENL ERDIVQRNPN VHWADIAGLT
250 260 270 280 290 300
EAKRLLEEAV VLPLWMPDYF KGIRRPWKGV LMVGPPGTGK TMLAKAVATE CGTTFFNVSS
310 320 330 340 350 360
ASLTSKYHGE SEKLVRLLFE MARFYAPSTI FIDEIDSICS KRGTGSEHEA SRRVKSELLI
370 380 390 400 410 420
QMDGVSGPSA GEESSKMVMV LAATNFPWDI DEALRRRLEK RIYIPLPEID GREQLLRINL
430 440 450 460 470 480
KEVPLADDID LKSIAEKMDG YSGADITNVC RDASMMAMRR RIQGLRPEEI RHIPKEELNQ
490 500 510
PSTPADFLLA LQKVSKSVGK EDLVKYMAWM EEFGSV