A0DB19

PR
Gene name
GSPATT00015130001
Protein name
Lissencephaly-1 homolog 1
Names
Species
Paramecium tetraurelia
KEGG Pathway
ptm:GSPATT00015130001
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

38-119 (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 A0DB19

Entry ID Method Resolution Chain Position Source
AF-A0DB19-F1 Predicted AlphaFoldDB

No variants for A0DB19

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A0DB19

No associated diseases with A0DB19

9 regional properties for A0DB19

Type Name Position InterPro Accession
repeat WD40 repeat 94 - 318 IPR001680-1
repeat WD40 repeat 321 - 401 IPR001680-2
domain LIS1 homology motif 7 - 38 IPR006594
conserved_site WD40 repeat, conserved site 162 - 176 IPR019775-1
conserved_site WD40 repeat, conserved site 204 - 218 IPR019775-2
conserved_site WD40 repeat, conserved site 347 - 361 IPR019775-3
repeat G-protein beta WD-40 repeat 120 - 134 IPR020472-1
repeat G-protein beta WD-40 repeat 204 - 218 IPR020472-2
repeat G-protein beta WD-40 repeat 347 - 361 IPR020472-3

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, cytoskeleton
  • Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
  • Localizes to the plus end of microtubules and to the centrosome
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
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 associated complex Any multimeric complex connected to a microtubule.
microtubule organizing center An intracellular structure that can catalyze gamma-tubulin-dependent microtubule nucleation and that can anchor microtubules by interacting with their minus ends, plus ends or sides.

1 GO annotations of molecular function

Name Definition
dynein complex binding Binding to a dynein complex, a protein complex that contains two or three dynein heavy chains and several light chains, and has microtubule motor activity.

3 GO annotations of biological process

Name Definition
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.
establishment of mitotic spindle orientation A cell cycle process that sets the alignment of mitotic spindle relative to other cellular structures.
microtubule sliding The movement of one microtubule along another microtubule.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MVLTARQRDE LNQAIHQYLL ISYQQSAQLF KTEAAVKDGQ IEADLLEKKW NSIVRLSKRV
70 80 90 100 110 120
ITLEQQVEQL NEQLAQAQAG KIQFNKSDDE QRLTPIEKFK LEGHRAGVNC VAFHPQYQIL
130 140 150 160 170 180
GSASDDGSIK LWDYESGHFE KTLKGHTSNV NCLAFDPTGK YICSASSDLS IKIWELKNHT
190 200 210 220 230 240
CVKTLIGHEH SVSTVQFSDH GDFILSASRD KNIKLWEVAT GFCKKTFSEH QEWVRCAVFS
250 260 270 280 290 300
NDEKQIASCS QDQMIYIWVI DSGQVLHQLS GHEHVVEQVK YIPEHGAKQI LTQQQQQNIQ
310 320 330 340 350 360
TINLLVSVSR DKEIKIWNTI LGTNLFTLSG HDNWVNGVSF HPDGVHMLSV SDDKTIRVWN
370 380 390 400
LKEQKQKKKI ENAHDKFILK CEINKFIFAT CSVDQTIKLW LLS